HEADER    VIRAL PROTEIN                           20-FEB-20   XXXX
TITLE     CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE FROM SARS COV-2.
KEYWDS    SARS CORONA VIRUS, ENDONUCLEASE, STRUCTURAL GENOMICS, CENTER FOR
KEYWDS   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, VIRAL PROTEIN
EXPDTA    X-RAY DIFFRACTION
AUTHOR    Y.KIM,R.JEDRZEJCZAK,N.MALTSEVA,M.ENDRES,A.GODZIK,K.MICHALSKA,
AUTHOR   2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR   3 (CSGID)
JRNL        AUTH   Y.KIM,R.JEDRZEJCZAK,N.I.MALTSEVA,M.WILAMOWSKI,M.ENDRES,
JRNL        AUTH 2 A.GODZIK,K.MICHALSKA,A.JOACHIMIAK
JRNL        TITL   CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE NENDOU FROM
JRNL        TITL 2 SARS-COV-2.
JRNL        REF    PROTEIN SCI.                               2020
JRNL        REFN                   ESSN 1469-896X
JRNL        PMID   32304108
JRNL        DOI    10.1002/PRO.3873
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   Y.KIM,R.JEDRZEJCZAK,N.I.MALTSEVA,M.ENDRES,A.GODZIK,
REMARK   1  AUTH 2 K.MICHALSKA,A.JOACHIMIAK
REMARK   1  TITL   CRYSTAL STRUCTURE OF NSP15 ENDORIBONUCLEASE FROM SARS COV-2.
REMARK   1  REF    BIORXIV                                    2020
REMARK   1  REFN
REMARK   1  DOI    10.1101/2020.03.02.968388
SEQRES   1 A  371  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 A  371  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES   3 A  371  LEU GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS
SEQRES   4 A  371  PHE ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE
SEQRES   5 A  371  ASN ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL
SEQRES   6 A  371  GLU LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL
SEQRES   7 A  371  ALA PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL
SEQRES   8 A  371  PRO GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE
SEQRES   9 A  371  ALA ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA
SEQRES  10 A  371  PRO ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR
SEQRES  11 A  371  ASP ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO
SEQRES  12 A  371  LEU THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL
SEQRES  13 A  371  ASP LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR
SEQRES  14 A  371  GLU GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO
SEQRES  15 A  371  LYS GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU
SEQRES  16 A  371  ALA VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP
SEQRES  17 A  371  GLY VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN
SEQRES  18 A  371  SER ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET
SEQRES  19 A  371  GLU ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE
SEQRES  20 A  371  GLU ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE
SEQRES  21 A  371  VAL TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU
SEQRES  22 A  371  HIS LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER
SEQRES  23 A  371  PRO PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR
SEQRES  24 A  371  VAL LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER
SEQRES  25 A  371  SER LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP
SEQRES  26 A  371  ASP PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL
SEQRES  27 A  371  VAL SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU
SEQRES  28 A  371  ILE SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU
SEQRES  29 A  371  THR PHE TYR PRO LYS LEU GLN
SEQRES   1 B  371  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES   2 B  371  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES   3 B  371  LEU GLU ASN VAL ALA PHE ASN VAL VAL ASN LYS GLY HIS
SEQRES   4 B  371  PHE ASP GLY GLN GLN GLY GLU VAL PRO VAL SER ILE ILE
SEQRES   5 B  371  ASN ASN THR VAL TYR THR LYS VAL ASP GLY VAL ASP VAL
SEQRES   6 B  371  GLU LEU PHE GLU ASN LYS THR THR LEU PRO VAL ASN VAL
SEQRES   7 B  371  ALA PHE GLU LEU TRP ALA LYS ARG ASN ILE LYS PRO VAL
SEQRES   8 B  371  PRO GLU VAL LYS ILE LEU ASN ASN LEU GLY VAL ASP ILE
SEQRES   9 B  371  ALA ALA ASN THR VAL ILE TRP ASP TYR LYS ARG ASP ALA
SEQRES  10 B  371  PRO ALA HIS ILE SER THR ILE GLY VAL CYS SER MET THR
SEQRES  11 B  371  ASP ILE ALA LYS LYS PRO THR GLU THR ILE CYS ALA PRO
SEQRES  12 B  371  LEU THR VAL PHE PHE ASP GLY ARG VAL ASP GLY GLN VAL
SEQRES  13 B  371  ASP LEU PHE ARG ASN ALA ARG ASN GLY VAL LEU ILE THR
SEQRES  14 B  371  GLU GLY SER VAL LYS GLY LEU GLN PRO SER VAL GLY PRO
SEQRES  15 B  371  LYS GLN ALA SER LEU ASN GLY VAL THR LEU ILE GLY GLU
SEQRES  16 B  371  ALA VAL LYS THR GLN PHE ASN TYR TYR LYS LYS VAL ASP
SEQRES  17 B  371  GLY VAL VAL GLN GLN LEU PRO GLU THR TYR PHE THR GLN
SEQRES  18 B  371  SER ARG ASN LEU GLN GLU PHE LYS PRO ARG SER GLN MET
SEQRES  19 B  371  GLU ILE ASP PHE LEU GLU LEU ALA MET ASP GLU PHE ILE
SEQRES  20 B  371  GLU ARG TYR LYS LEU GLU GLY TYR ALA PHE GLU HIS ILE
SEQRES  21 B  371  VAL TYR GLY ASP PHE SER HIS SER GLN LEU GLY GLY LEU
SEQRES  22 B  371  HIS LEU LEU ILE GLY LEU ALA LYS ARG PHE LYS GLU SER
SEQRES  23 B  371  PRO PHE GLU LEU GLU ASP PHE ILE PRO MET ASP SER THR
SEQRES  24 B  371  VAL LYS ASN TYR PHE ILE THR ASP ALA GLN THR GLY SER
SEQRES  25 B  371  SER LYS CYS VAL CYS SER VAL ILE ASP LEU LEU LEU ASP
SEQRES  26 B  371  ASP PHE VAL GLU ILE ILE LYS SER GLN ASP LEU SER VAL
SEQRES  27 B  371  VAL SER LYS VAL VAL LYS VAL THR ILE ASP TYR THR GLU
SEQRES  28 B  371  ILE SER PHE MET LEU TRP CYS LYS ASP GLY HIS VAL GLU
SEQRES  29 B  371  THR PHE TYR PRO LYS LEU GLN
HETNAM     GOL GLYCEROL
HETNAM      MG MAGNESIUM ION
HETNAM     ACY ACETIC ACID
HETNAM      CL CHLORIDE ION
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL   3  GOL    9(C3 H8 O3)
FORMUL   5   MG    MG 2+
FORMUL   8  ACY    3(C2 H4 O2)
FORMUL  12   CL    CL 1-
FORMUL  17  HOH   *346(H2 O)
HELIX    1 AA1 SER A    2  GLY A   14  1                                  13
HELIX    2 AA2 PRO A   51  LYS A   61  1                                  11
HELIX    3 AA3 GLU A   69  LEU A   76  1                                   8
HELIX    4 AA4 GLU A  114  ALA A  118  5                                   5
HELIX    5 AA5 GLY A  130  ASN A  137  1                                   8
HELIX    6 AA6 SER A  208  LEU A  217  1                                  10
HELIX    7 AA7 ALA A  218  TYR A  226  1                                   9
HELIX    8 AA8 ALA A  232  VAL A  237  1                                   6
HELIX    9 AA9 LEU A  251  SER A  262  1                                  12
HELIX   10 AB1 LEU A  299  LYS A  308  1                                  10
HELIX   11 AB2 SER B    2  GLY B   14  1                                  13
HELIX   12 AB3 PRO B   51  LYS B   61  1                                  11
HELIX   13 AB4 GLU B   69  LEU B   76  1                                   8
HELIX   14 AB5 GLU B  114  ALA B  118  5                                   5
HELIX   15 AB6 GLY B  130  ALA B  138  1                                   9
HELIX   16 AB7 SER B  208  LEU B  217  1                                  10
HELIX   17 AB8 ALA B  218  TYR B  226  1                                   9
HELIX   18 AB9 ALA B  232  VAL B  237  1                                   6
HELIX   19 AC1 LEU B  251  SER B  262  1                                  12
HELIX   20 AC2 LEU B  299  LYS B  308  1                                  10
SHEET    1 AA1 3 VAL A  25  ILE A  28  0
SHEET    2 AA1 3 THR A  31  VAL A  36 -1  O  TYR A  33   N  SER A  26
SHEET    3 AA1 3 VAL A  39  GLU A  45 -1  O  VAL A  39   N  VAL A  36
SHEET    1 AA2 5 ILE A  80  ALA A  81  0
SHEET    2 AA2 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80
SHEET    3 AA2 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124
SHEET    4 AA2 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145
SHEET    5 AA2 5 SER A 155  VAL A 156 -1  N  SER A 155   O  TYR A 179
SHEET    1 AA3 5 ILE A  80  ALA A  81  0
SHEET    2 AA3 5 VAL A 122  ASP A 125  1  O  PHE A 123   N  ILE A  80
SHEET    3 AA3 5 GLY A 141  THR A 145  1  O  VAL A 142   N  PHE A 124
SHEET    4 AA3 5 ASN A 178  VAL A 183 -1  O  ASN A 178   N  THR A 145
SHEET    5 AA3 5 VAL A 186  GLN A 188 -1  O  GLN A 188   N  LYS A 181
SHEET    1 AA4 2 TRP A  87  ASP A  88  0
SHEET    2 AA4 2 ALA A  93  PRO A  94 -1  O  ALA A  93   N  ASP A  88
SHEET    1 AA5 2 THR A  99  ILE A 100  0
SHEET    2 AA5 2 ASP A 107  ALA A 109  1  O  ILE A 108   N  THR A  99
SHEET    1 AA6 2 ALA A 161  LEU A 163  0
SHEET    2 AA6 2 VAL A 166  LEU A 168 -1  O  VAL A 166   N  LEU A 163
SHEET    1 AA7 3 PHE A 264  GLU A 267  0
SHEET    2 AA7 3 LYS A 277  ASP A 283 -1  O  THR A 282   N  GLU A 265
SHEET    3 AA7 3 SER A 289  VAL A 295 -1  O  VAL A 295   N  LYS A 277
SHEET    1 AA8 3 SER A 316  ILE A 323  0
SHEET    2 AA8 3 THR A 326  LYS A 335 -1  O  PHE A 330   N  VAL A 319
SHEET    3 AA8 3 HIS A 338  PRO A 344 -1  O  GLU A 340   N  TRP A 333
SHEET    1 AA9 3 VAL B  25  ILE B  28  0
SHEET    2 AA9 3 THR B  31  VAL B  36 -1  O  TYR B  33   N  SER B  26
SHEET    3 AA9 3 VAL B  39  GLU B  45 -1  O  LEU B  43   N  VAL B  32
SHEET    1 AB1 5 ILE B  80  ALA B  81  0
SHEET    2 AB1 5 THR B 121  ASP B 125  1  O  PHE B 123   N  ILE B  80
SHEET    3 AB1 5 ASN B 140  THR B 145  1  O  VAL B 142   N  PHE B 124
SHEET    4 AB1 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145
SHEET    5 AB1 5 SER B 155  VAL B 156 -1  N  SER B 155   O  TYR B 179
SHEET    1 AB2 5 ILE B  80  ALA B  81  0
SHEET    2 AB2 5 THR B 121  ASP B 125  1  O  PHE B 123   N  ILE B  80
SHEET    3 AB2 5 ASN B 140  THR B 145  1  O  VAL B 142   N  PHE B 124
SHEET    4 AB2 5 ASN B 178  VAL B 183 -1  O  ASN B 178   N  THR B 145
SHEET    5 AB2 5 VAL B 186  GLN B 188 -1  O  GLN B 188   N  LYS B 181
SHEET    1 AB3 2 TRP B  87  ASP B  88  0
SHEET    2 AB3 2 ALA B  93  PRO B  94 -1  O  ALA B  93   N  ASP B  88
SHEET    1 AB4 2 THR B  99  ILE B 100  0
SHEET    2 AB4 2 ASP B 107  ALA B 109  1  O  ILE B 108   N  THR B  99
SHEET    1 AB5 2 ALA B 161  LEU B 163  0
SHEET    2 AB5 2 VAL B 166  LEU B 168 -1  O  VAL B 166   N  LEU B 163
SHEET    1 AB6 3 PHE B 264  GLU B 267  0
SHEET    2 AB6 3 LYS B 277  ASP B 283 -1  O  THR B 282   N  GLU B 265
SHEET    3 AB6 3 SER B 289  VAL B 295 -1  O  VAL B 295   N  LYS B 277
SHEET    1 AB7 3 SER B 316  ILE B 323  0
SHEET    2 AB7 3 THR B 326  LYS B 335 -1  O  ILE B 328   N  VAL B 321
SHEET    3 AB7 3 HIS B 338  PRO B 344 -1  O  GLU B 340   N  TRP B 333
LINK         OG  SER A 262                MG    MG A 403     1555   1555  2.08
LINK         O   PRO A 263                MG    MG A 403     1555   1555  2.28
LINK         OD1 ASP A 283                MG    MG A 403     1555   1555  2.61
SITE     1 AC1  5 LEU A  43  PHE A  44  GLU A  45  GLU A 267
SITE     2 AC1  5 HOH A 623
SITE     1 AC2  5 GLY A 126  ARG A 127  THR A 145  GLU A 146
SITE     2 AC2  5 GLY A 147
SITE     1 AC3  5 SER A 262  PRO A 263  ASP A 283  ALA A 284
SITE     2 AC3  5 GLN A 285
SITE     1 AC4  4 GLY A  77  ASP A  79  PRO A 119  HOH A 518
SITE     1 AC5  8 GLU A  69  LYS A  90  THR A 167  SER A 198
SITE     2 AC5  8 ASN A 200  HOH A 542  HOH A 547  HOH A 555
SITE     1 AC6  3 ASN A 200  LEU A 201  TYR A 279
SITE     1 AC7  5 ASN B  75  SER B 274  THR B 275  VAL B 276
SITE     2 AC7  5 HOH B 530
SITE     1 AC8  6 LYS B  90  THR B 167  SER B 198  ARG B 199
SITE     2 AC8  6 ASN B 200  HOH B 501
SITE     1 AC9  5 GLY B  77  ASP B  79  PRO B 119  THR B 121
SITE     2 AC9  5 HOH B 509
SITE     1 AD1  3 THR A 322  VAL B 149  GLY B 151
SITE     1 AD2  5 LEU B  43  PHE B  44  GLU B  45  TRP B  59
SITE     2 AD2  5 HOH B 513
SITE     1 AD3  4 GLU B 192  LYS B 320  THR B 322  GLU B 327
SITE     1 AD4  5 GLU B 146  LYS B 174  GLN B 176  PHE B 177
SITE     2 AD4  5 ASN B 178
SITE     1 AD5  8 LEU B 312  SER B 313  VAL B 314  VAL B 315
SITE     2 AD5  8 CYS B 334  LYS B 335  ASP B 336  GLY B 337
CRYST1  150.539  150.539  111.310  90.00  90.00 120.00 P 63         12
ORIGX1      1.000000  0.000000  0.000000        0.00000
ORIGX2      0.000000  1.000000  0.000000        0.00000
ORIGX3      0.000000  0.000000  1.000000        0.00000
SCALE1      0.006643  0.003835  0.000000        0.00000
SCALE2      0.000000  0.007670  0.000000        0.00000
SCALE3      0.000000  0.000000  0.008984        0.00000
MODEL        1
ATOM      1  N   ALA A   0     -47.374  30.865  -0.250  1.00 84.12           N
ANISOU    1  N   ALA A   0     8694  10754  12515   1463  -1341   1365       N
ATOM      2  CA  ALA A   0     -47.137  31.596  -1.490  1.00 81.50           C
ANISOU    2  CA  ALA A   0     8258  10390  12318   1359  -1177   1154       C
ATOM      3  C   ALA A   0     -48.453  32.022  -2.131  1.00 74.88           C
ANISOU    3  C   ALA A   0     7619   9375  11458   1204  -1039   1038       C
ATOM      4  O   ALA A   0     -48.485  32.933  -2.957  1.00 72.79           O
ANISOU    4  O   ALA A   0     7302   9114  11240   1065   -950    871       O
ATOM      5  CB  ALA A   0     -46.322  30.749  -2.460  1.00 83.08           C
ANISOU    5  CB  ALA A   0     8369  10457  12741   1531   -997   1138       C
ATOM      6  N  AMET A   1     -49.531  31.339  -1.747  0.57 71.75           N
ANISOU    6  N  AMET A   1     7448   8820  10992   1231  -1018   1135       N
ATOM      7  N  BMET A   1     -49.547  31.373  -1.748  0.43 71.64           N
ANISOU    7  N  BMET A   1     7434   8809  10975   1225  -1020   1131       N
ATOM      8  CA AMET A   1     -50.859  31.680  -2.237  0.57 67.18           C
ANISOU    8  CA AMET A   1     7045   8092  10387   1096   -911   1033       C
ATOM      9  CA BMET A   1     -50.841  31.691  -2.334  0.43 67.02           C
ANISOU    9  CA BMET A   1     7022   8065  10378   1095   -898   1022       C
ATOM     10  C  AMET A   1     -51.331  32.972  -1.584  0.57 62.96           C
ANISOU   10  C  AMET A   1     6486   7726   9709    911  -1070    970       C
ATOM     11  C  BMET A   1     -51.478  32.870  -1.611  0.43 62.70           C
ANISOU   11  C  BMET A   1     6482   7665   9678    916  -1055    976       C
ATOM     12  O  AMET A   1     -51.149  33.170  -0.377  0.57 64.38           O
ANISOU   12  O  AMET A   1     6635   8088   9737    884  -1271   1070       O
ATOM     13  O  BMET A   1     -51.581  32.875  -0.379  0.43 63.70           O
ANISOU   13  O  BMET A   1     6646   7926   9631    893  -1225   1087       O
ATOM     14  CB AMET A   1     -51.842  30.544  -1.947  0.57 67.02           C
ANISOU   14  CB AMET A   1     7261   7862  10342   1163   -836   1150       C
ATOM     15  CB BMET A   1     -51.762  30.475  -2.285  0.43 66.82           C
ANISOU   15  CB BMET A   1     7228   7802  10359   1172   -784   1117       C
ATOM     16  CG AMET A   1     -51.693  29.914  -0.560  0.57 68.96           C
ANISOU   16  CG AMET A   1     7559   8181  10461   1259  -1003   1383       C
ATOM     17  CG BMET A   1     -51.708  29.621  -3.533  0.43 65.28           C
ANISOU   17  CG BMET A   1     7090   7386  10327   1240   -538   1032       C
ATOM     18  SD AMET A   1     -52.653  30.703   0.754  0.57 64.50           S
ANISOU   18  SD AMET A   1     7104   7780   9622   1078  -1195   1439       S
ATOM     19  SD BMET A   1     -51.878  30.593  -5.042  0.43 58.41           S
ANISOU   19  SD BMET A   1     6162   6504   9527   1091   -393    787       S
ATOM     20  CE AMET A   1     -54.199  29.802   0.651  0.57 60.65           C
ANISOU   20  CE AMET A   1     6946   7016   9082   1023   -980   1440       C
ATOM     21  CE BMET A   1     -53.432  31.429  -4.741  0.43 54.39           C
ANISOU   21  CE BMET A   1     5805   6003   8857    907   -451    723       C
ATOM     22  N   SER A   2     -51.917  33.861  -2.384  1.00 52.97           N
ANISOU   22  N   SER A   2     5276   6416   8436    758   -956    779       N
ATOM     23  CA  SER A   2     -52.445  35.103  -1.839  1.00 42.55           C
ANISOU   23  CA  SER A   2     4011   5218   6938    558  -1026    660       C
ATOM     24  C   SER A   2     -53.357  35.760  -2.859  1.00 34.48           C
ANISOU   24  C   SER A   2     3104   4069   5928    449   -862    500       C
ATOM     25  O   SER A   2     -53.204  35.569  -4.067  1.00 32.94           O
ANISOU   25  O   SER A   2     2886   3765   5865    489   -728    456       O
ATOM     26  CB  SER A   2     -51.323  36.067  -1.444  1.00 44.73           C
ANISOU   26  CB  SER A   2     4069   5715   7212    476  -1165    610       C
ATOM     27  OG  SER A   2     -51.045  36.994  -2.480  1.00 39.74           O
ANISOU   27  OG  SER A   2     3364   5048   6686    379  -1050    455       O
ATOM     28  N   LEU A   3     -54.304  36.548  -2.348  1.00 30.26           N
ANISOU   28  N   LEU A   3     2691   3558   5249    314   -874    416       N
ATOM     29  CA  LEU A   3     -55.209  37.284  -3.222  1.00 29.43           C
ANISOU   29  CA  LEU A   3     2674   3351   5157    230   -749    290       C
ATOM     30  C   LEU A   3     -54.455  38.311  -4.056  1.00 28.78           C
ANISOU   30  C   LEU A   3     2481   3284   5170    169   -711    205       C
ATOM     31  O   LEU A   3     -54.689  38.432  -5.264  1.00 28.45           O
ANISOU   31  O   LEU A   3     2470   3143   5196    172   -595    170       O
ATOM     32  CB  LEU A   3     -56.296  37.962  -2.389  1.00 35.11           C
ANISOU   32  CB  LEU A   3     3513   4092   5735    121   -761    219       C
ATOM     33  CG  LEU A   3     -57.146  39.019  -3.092  1.00 33.17           C
ANISOU   33  CG  LEU A   3     3320   3764   5518     49   -664    102       C
ATOM     34  CD1 LEU A   3     -58.016  38.393  -4.167  1.00 34.73           C
ANISOU   34  CD1 LEU A   3     3585   3849   5763    106   -566    118       C
ATOM     35  CD2 LEU A   3     -57.993  39.783  -2.087  1.00 27.98           C
ANISOU   35  CD2 LEU A   3     2742   3136   4755    -46   -665     14       C
ATOM     36  N   GLU A   4     -53.544  39.057  -3.429  1.00 27.95           N
ANISOU   36  N   GLU A   4     2252   3311   5055     92   -806    169       N
ATOM     37  CA  GLU A   4     -52.803  40.085  -4.151  1.00 25.41           C
ANISOU   37  CA  GLU A   4     1832   2995   4829     -1   -749     80       C
ATOM     38  C   GLU A   4     -51.873  39.481  -5.195  1.00 24.88           C
ANISOU   38  C   GLU A   4     1634   2908   4911     88   -673    122       C
ATOM     39  O   GLU A   4     -51.602  40.113  -6.222  1.00 28.97           O
ANISOU   39  O   GLU A   4     2137   3369   5501     24   -554     64       O
ATOM     40  CB  GLU A   4     -52.012  40.951  -3.169  1.00 31.88           C
ANISOU   40  CB  GLU A   4     2535   3976   5602   -139   -864      7       C
ATOM     41  CG  GLU A   4     -52.865  41.871  -2.296  1.00 39.35           C
ANISOU   41  CG  GLU A   4     3622   4916   6415   -275   -877    -99       C
ATOM     42  CD  GLU A   4     -53.629  41.132  -1.206  1.00 48.87           C
ANISOU   42  CD  GLU A   4     4932   6177   7459   -229   -961    -38       C
ATOM     43  OE1 GLU A   4     -53.430  39.908  -1.052  1.00 50.66           O
ANISOU   43  OE1 GLU A   4     5127   6444   7676    -92  -1028    106       O
ATOM     44  OE2 GLU A   4     -54.431  41.780  -0.500  1.00 50.35           O
ANISOU   44  OE2 GLU A   4     5243   6352   7537   -331   -938   -136       O
ATOM     45  N   ASN A   5     -51.376  38.267  -4.954  1.00 27.17           N
ANISOU   45  N   ASN A   5     1837   3234   5253    238   -721    228       N
ATOM     46  CA  ASN A   5     -50.534  37.612  -5.948  1.00 29.85           C
ANISOU   46  CA  ASN A   5     2052   3531   5759    341   -610    249       C
ATOM     47  C   ASN A   5     -51.358  37.132  -7.135  1.00 29.00           C
ANISOU   47  C   ASN A   5     2115   3247   5657    369   -435    223       C
ATOM     48  O   ASN A   5     -50.904  37.206  -8.282  1.00 36.57           O
ANISOU   48  O   ASN A   5     3034   4161   6698    353   -288    169       O
ATOM     49  CB  ASN A   5     -49.773  36.450  -5.311  1.00 35.87           C
ANISOU   49  CB  ASN A   5     2673   4355   6602    521   -702    380       C
ATOM     50  CG  ASN A   5     -49.063  35.588  -6.332  1.00 42.39           C
ANISOU   50  CG  ASN A   5     3442   5094   7571    645   -529    383       C
ATOM     51  OD1 ASN A   5     -49.445  34.441  -6.565  1.00 47.47           O
ANISOU   51  OD1 ASN A   5     4196   5594   8246    773   -446    441       O
ATOM     52  ND2 ASN A   5     -48.028  36.139  -6.956  1.00 40.36           N
ANISOU   52  ND2 ASN A   5     3014   4914   7407    589   -455    304       N
ATOM     53  N   VAL A   6     -52.570  36.637  -6.879  1.00 26.57           N
ANISOU   53  N   VAL A   6     1993   2854   5247    391   -444    252       N
ATOM     54  CA  VAL A   6     -53.445  36.224  -7.973  1.00 24.01           C
ANISOU   54  CA  VAL A   6     1822   2400   4900    382   -302    209       C
ATOM     55  C   VAL A   6     -53.774  37.415  -8.861  1.00 25.80           C
ANISOU   55  C   VAL A   6     2101   2628   5075    253   -244    133       C
ATOM     56  O   VAL A   6     -53.766  37.312 -10.095  1.00 31.46           O
ANISOU   56  O   VAL A   6     2860   3296   5799    228   -115     94       O
ATOM     57  CB  VAL A   6     -54.719  35.563  -7.417  1.00 26.04           C
ANISOU   57  CB  VAL A   6     2240   2594   5059    396   -331    242       C
ATOM     58  CG1 VAL A   6     -55.725  35.330  -8.533  1.00 27.19           C
ANISOU   58  CG1 VAL A   6     2521   2654   5157    341   -215    174       C
ATOM     59  CG2 VAL A   6     -54.380  34.253  -6.723  1.00 23.40           C
ANISOU   59  CG2 VAL A   6     1895   2211   4786    532   -351    347       C
ATOM     60  N   ALA A   7     -54.060  38.565  -8.250  1.00 22.11           N
ANISOU   60  N   ALA A   7     1645   2207   4550    166   -328    114       N
ATOM     61  CA  ALA A   7     -54.362  39.758  -9.030  1.00 22.85           C
ANISOU   61  CA  ALA A   7     1800   2267   4616     65   -271     75       C
ATOM     62  C   ALA A   7     -53.143  40.247  -9.800  1.00 29.32           C
ANISOU   62  C   ALA A   7     2516   3106   5519      7   -179     50       C
ATOM     63  O   ALA A   7     -53.287  40.787 -10.903  1.00 30.49           O
ANISOU   63  O   ALA A   7     2742   3204   5640    -55    -78     47       O
ATOM     64  CB  ALA A   7     -54.899  40.858  -8.116  1.00 24.32           C
ANISOU   64  CB  ALA A   7     2026   2458   4758     -4   -350     47       C
ATOM     65  N   PHE A   8     -51.944  40.066  -9.242  1.00 30.37           N
ANISOU   65  N   PHE A   8     2466   3326   5748     21   -214     40       N
ATOM     66  CA  PHE A   8     -50.729  40.415  -9.969  1.00 28.94           C
ANISOU   66  CA  PHE A   8     2147   3180   5670    -40   -103      2       C
ATOM     67  C   PHE A   8     -50.625  39.619 -11.263  1.00 27.85           C
ANISOU   67  C   PHE A   8     2046   2982   5552     10     65     -2       C
ATOM     68  O   PHE A   8     -50.315  40.171 -12.325  1.00 27.71           O
ANISOU   68  O   PHE A   8     2061   2942   5526    -88    208    -32       O
ATOM     69  CB  PHE A   8     -49.502  40.174  -9.087  1.00 26.57           C
ANISOU   69  CB  PHE A   8     1595   3020   5482     -9   -194     -2       C
ATOM     70  CG  PHE A   8     -48.191  40.399  -9.794  1.00 37.77           C
ANISOU   70  CG  PHE A   8     2817   4496   7039    -66    -67    -54       C
ATOM     71  CD1 PHE A   8     -47.573  41.637  -9.760  1.00 39.06           C
ANISOU   71  CD1 PHE A   8     2900   4712   7229   -252    -44   -126       C
ATOM     72  CD2 PHE A   8     -47.574  39.370 -10.489  1.00 40.93           C
ANISOU   72  CD2 PHE A   8     3110   4886   7555     55     58    -48       C
ATOM     73  CE1 PHE A   8     -46.369  41.846 -10.408  1.00 38.02           C
ANISOU   73  CE1 PHE A   8     2573   4642   7230   -328     94   -183       C
ATOM     74  CE2 PHE A   8     -46.375  39.575 -11.143  1.00 41.01           C
ANISOU   74  CE2 PHE A   8     2921   4958   7705     -1    203   -112       C
ATOM     75  CZ  PHE A   8     -45.770  40.813 -11.099  1.00 40.28           C
ANISOU   75  CZ  PHE A   8     2735   4938   7630   -198    218   -176       C
ATOM     76  N   ASN A   9     -50.877  38.311 -11.189  1.00 29.15           N
ANISOU   76  N   ASN A   9     2228   3113   5737    146     69     22       N
ATOM     77  CA  ASN A   9     -50.766  37.468 -12.374  1.00 31.72           C
ANISOU   77  CA  ASN A   9     2599   3371   6082    178    253    -20       C
ATOM     78  C   ASN A   9     -51.801  37.849 -13.422  1.00 27.90           C
ANISOU   78  C   ASN A   9     2335   2842   5426     73    319    -39       C
ATOM     79  O   ASN A   9     -51.516  37.818 -14.624  1.00 33.74           O
ANISOU   79  O   ASN A   9     3119   3572   6128      6    486    -89       O
ATOM     80  CB  ASN A   9     -50.916  35.997 -11.986  1.00 31.80           C
ANISOU   80  CB  ASN A   9     2610   3312   6161    338    254      5       C
ATOM     81  CG  ASN A   9     -49.676  35.439 -11.317  1.00 31.70           C
ANISOU   81  CG  ASN A   9     2356   3343   6346    481    230     46       C
ATOM     82  OD1 ASN A   9     -48.846  34.800 -11.962  1.00 34.08           O
ANISOU   82  OD1 ASN A   9     2549   3607   6794    555    396      2       O
ATOM     83  ND2 ASN A   9     -49.544  35.677 -10.017  1.00 34.15           N
ANISOU   83  ND2 ASN A   9     2572   3743   6658    521     25    130       N
ATOM     84  N   VAL A  10     -53.006  38.216 -12.987  1.00 23.18           N
ANISOU   84  N   VAL A  10     1863   2230   4713     56    189      3       N
ATOM     85  CA  VAL A  10     -54.061  38.549 -13.937  1.00 27.76           C
ANISOU   85  CA  VAL A  10     2618   2796   5132    -21    212     10       C
ATOM     86  C   VAL A  10     -53.708  39.813 -14.709  1.00 30.23           C
ANISOU   86  C   VAL A  10     2965   3122   5400   -132    272     38       C
ATOM     87  O   VAL A  10     -53.871  39.875 -15.933  1.00 34.51           O
ANISOU   87  O   VAL A  10     3615   3675   5822   -205    371     40       O
ATOM     88  CB  VAL A  10     -55.411  38.682 -13.209  1.00 28.33           C
ANISOU   88  CB  VAL A  10     2771   2861   5133      5     62     48       C
ATOM     89  CG1 VAL A  10     -56.479  39.189 -14.163  1.00 30.18           C
ANISOU   89  CG1 VAL A  10     3138   3112   5217    -58     50     79       C
ATOM     90  CG2 VAL A  10     -55.822  37.345 -12.612  1.00 26.78           C
ANISOU   90  CG2 VAL A  10     2580   2636   4960     84     42     26       C
ATOM     91  N   VAL A  11     -53.202  40.834 -14.015  1.00 32.63           N
ANISOU   91  N   VAL A  11     3190   3422   5785   -165    222     58       N
ATOM     92  CA  VAL A  11     -52.936  42.104 -14.681  1.00 35.02           C
ANISOU   92  CA  VAL A  11     3554   3694   6058   -282    294     98       C
ATOM     93  C   VAL A  11     -51.682  42.026 -15.544  1.00 41.84           C
ANISOU   93  C   VAL A  11     4345   4588   6966   -364    482     52       C
ATOM     94  O   VAL A  11     -51.552  42.777 -16.517  1.00 45.71           O
ANISOU   94  O   VAL A  11     4939   5053   7375   -476    594     96       O
ATOM     95  CB  VAL A  11     -52.838  43.246 -13.654  1.00 36.03           C
ANISOU   95  CB  VAL A  11     3640   3780   6268   -322    212    104       C
ATOM     96  CG1 VAL A  11     -54.114  43.338 -12.836  1.00 36.54           C
ANISOU   96  CG1 VAL A  11     3779   3814   6292   -244     66    130       C
ATOM     97  CG2 VAL A  11     -51.639  43.054 -12.747  1.00 42.72           C
ANISOU   97  CG2 VAL A  11     4276   4701   7254   -336    195     25       C
ATOM     98  N   ASN A  12     -50.749  41.131 -15.223  1.00 26.45           N
ANISOU   98  N   ASN A  12     2214   2689   5145   -306    530    -24       N
ATOM     99  CA  ASN A  12     -49.502  41.035 -15.971  1.00 35.54           C
ANISOU   99  CA  ASN A  12     3249   3877   6376   -374    730    -89       C
ATOM    100  C   ASN A  12     -49.480  39.890 -16.972  1.00 36.46           C
ANISOU  100  C   ASN A  12     3418   3993   6443   -338    892   -150       C
ATOM    101  O   ASN A  12     -48.842  40.017 -18.022  1.00 39.47           O
ANISOU  101  O   ASN A  12     3812   4391   6792   -443   1102   -198       O
ATOM    102  CB  ASN A  12     -48.314  40.880 -15.015  1.00 42.27           C
ANISOU  102  CB  ASN A  12     3814   4803   7443   -330    697   -140       C
ATOM    103  CG  ASN A  12     -48.072  42.120 -14.179  1.00 48.37           C
ANISOU  103  CG  ASN A  12     4524   5596   8257   -437    590   -130       C
ATOM    104  OD1 ASN A  12     -47.522  43.111 -14.660  1.00 52.49           O
ANISOU  104  OD1 ASN A  12     5044   6105   8793   -601    708   -148       O
ATOM    105  ND2 ASN A  12     -48.471  42.066 -12.915  1.00 50.76           N
ANISOU  105  ND2 ASN A  12     4789   5926   8573   -364    384   -112       N
ATOM    106  N   LYS A  13     -50.153  38.778 -16.678  1.00 34.55           N
ANISOU  106  N   LYS A  13     3217   3721   6189   -213    825   -165       N
ATOM    107  CA  LYS A  13     -50.122  37.605 -17.540  1.00 33.39           C
ANISOU  107  CA  LYS A  13     3125   3545   6016   -189    999   -259       C
ATOM    108  C   LYS A  13     -51.481  37.238 -18.118  1.00 32.36           C
ANISOU  108  C   LYS A  13     3231   3400   5663   -232    956   -257       C
ATOM    109  O   LYS A  13     -51.581  36.232 -18.830  1.00 36.03           O
ANISOU  109  O   LYS A  13     3770   3837   6081   -244   1102   -362       O
ATOM    110  CB  LYS A  13     -49.555  36.400 -16.775  1.00 31.68           C
ANISOU  110  CB  LYS A  13     2737   3281   6021     -7   1010   -299       C
ATOM    111  CG  LYS A  13     -48.105  36.558 -16.349  1.00 38.11           C
ANISOU  111  CG  LYS A  13     3264   4147   7069     50   1064   -312       C
ATOM    112  CD  LYS A  13     -47.174  36.573 -17.550  1.00 44.29           C
ANISOU  112  CD  LYS A  13     3992   4949   7887    -42   1353   -423       C
ATOM    113  CE  LYS A  13     -45.715  36.631 -17.123  1.00 50.29           C
ANISOU  113  CE  LYS A  13     4413   5781   8916     24   1414   -450       C
ATOM    114  NZ  LYS A  13     -44.790  36.557 -18.288  1.00 51.04           N
ANISOU  114  NZ  LYS A  13     4434   5892   9067    -64   1738   -579       N
ATOM    115  N   GLY A  14     -52.525  38.019 -17.848  1.00 33.40           N
ANISOU  115  N   GLY A  14     3470   3553   5667   -262    770   -156       N
ATOM    116  CA  GLY A  14     -53.857  37.696 -18.312  1.00 30.51           C
ANISOU  116  CA  GLY A  14     3278   3211   5106   -299    696   -149       C
ATOM    117  C   GLY A  14     -54.537  36.567 -17.576  1.00 31.15           C
ANISOU  117  C   GLY A  14     3352   3242   5242   -205    623   -195       C
ATOM    118  O   GLY A  14     -55.743  36.367 -17.764  1.00 27.14           O
ANISOU  118  O   GLY A  14     2953   2768   4591   -245    532   -192       O
ATOM    119  N   HIS A  15     -53.811  35.826 -16.748  1.00 32.39           N
ANISOU  119  N   HIS A  15     3378   3324   5603    -84    658   -225       N
ATOM    120  CA  HIS A  15     -54.345  34.731 -15.945  1.00 30.53           C
ANISOU  120  CA  HIS A  15     3151   3010   5439     12    606   -239       C
ATOM    121  C   HIS A  15     -53.276  34.379 -14.919  1.00 30.80           C
ANISOU  121  C   HIS A  15     3007   2992   5703    165    599   -198       C
ATOM    122  O   HIS A  15     -52.193  34.972 -14.899  1.00 34.54           O
ANISOU  122  O   HIS A  15     3336   3514   6275    179    629   -183       O
ATOM    123  CB  HIS A  15     -54.712  33.522 -16.806  1.00 30.97           C
ANISOU  123  CB  HIS A  15     3330   3003   5435    -41    770   -371       C
ATOM    124  CG  HIS A  15     -53.525  32.760 -17.307  1.00 32.88           C
ANISOU  124  CG  HIS A  15     3509   3159   5825      8   1008   -471       C
ATOM    125  ND1 HIS A  15     -52.481  33.364 -17.975  1.00 33.27           N
ANISOU  125  ND1 HIS A  15     3477   3266   5898    -30   1134   -496       N
ATOM    126  CD2 HIS A  15     -53.215  31.445 -17.234  1.00 29.40           C
ANISOU  126  CD2 HIS A  15     3070   2563   5539     99   1166   -555       C
ATOM    127  CE1 HIS A  15     -51.580  32.452 -18.293  1.00 35.39           C
ANISOU  127  CE1 HIS A  15     3676   3436   6333     41   1361   -603       C
ATOM    128  NE2 HIS A  15     -52.001  31.280 -17.855  1.00 35.91           N
ANISOU  128  NE2 HIS A  15     3796   3359   6489    132   1384   -636       N
ATOM    129  N   PHE A  16     -53.578  33.405 -14.068  1.00 30.88           N
ANISOU  129  N   PHE A  16     3024   2915   5796    274    555   -170       N
ATOM    130  CA  PHE A  16     -52.586  32.947 -13.105  1.00 33.38           C
ANISOU  130  CA  PHE A  16     3173   3195   6317    442    526    -96       C
ATOM    131  C   PHE A  16     -51.508  32.147 -13.825  1.00 40.24           C
ANISOU  131  C   PHE A  16     3952   3980   7356    523    751   -173       C
ATOM    132  O   PHE A  16     -51.801  31.129 -14.461  1.00 47.25           O
ANISOU  132  O   PHE A  16     4960   4734   8258    522    924   -268       O
ATOM    133  CB  PHE A  16     -53.235  32.108 -12.009  1.00 29.40           C
ANISOU  133  CB  PHE A  16     2731   2606   5834    536    426    -12       C
ATOM    134  CG  PHE A  16     -52.286  31.723 -10.909  1.00 29.87           C
ANISOU  134  CG  PHE A  16     2625   2660   6064    718    342    114       C
ATOM    135  CD1 PHE A  16     -52.006  32.608  -9.879  1.00 27.72           C
ANISOU  135  CD1 PHE A  16     2237   2537   5759    720    135    206       C
ATOM    136  CD2 PHE A  16     -51.662  30.486 -10.911  1.00 32.94           C
ANISOU  136  CD2 PHE A  16     2972   2898   6645    886    468    140       C
ATOM    137  CE1 PHE A  16     -51.128  32.263  -8.867  1.00 32.02           C
ANISOU  137  CE1 PHE A  16     2625   3130   6412    868     23    331       C
ATOM    138  CE2 PHE A  16     -50.782  30.134  -9.902  1.00 36.71           C
ANISOU  138  CE2 PHE A  16     3333   3441   7176   1024    348    284       C
ATOM    139  CZ  PHE A  16     -50.516  31.024  -8.878  1.00 39.33           C
ANISOU  139  CZ  PHE A  16     3548   3960   7434   1012    117    380       C
ATOM    140  N   ASP A  17     -50.262  32.610 -13.728  1.00 35.96           N
ANISOU  140  N   ASP A  17     3191   3516   6956    580    765   -153       N
ATOM    141  CA  ASP A  17     -49.132  31.954 -14.371  1.00 33.43           C
ANISOU  141  CA  ASP A  17     2732   3133   6836    672    994   -232       C
ATOM    142  C   ASP A  17     -48.066  31.531 -13.368  1.00 37.00           C
ANISOU  142  C   ASP A  17     2952   3610   7496    873    898   -114       C
ATOM    143  O   ASP A  17     -46.978  31.107 -13.776  1.00 40.64           O
ANISOU  143  O   ASP A  17     3289   4069   8082    939   1037   -155       O
ATOM    144  CB  ASP A  17     -48.523  32.873 -15.435  1.00 43.04           C
ANISOU  144  CB  ASP A  17     3897   4458   7998    515   1137   -332       C
ATOM    145  CG  ASP A  17     -47.732  32.113 -16.481  1.00 56.60           C
ANISOU  145  CG  ASP A  17     5566   6092   9849    544   1456   -479       C
ATOM    146  OD1 ASP A  17     -47.980  30.901 -16.651  1.00 63.42           O
ANISOU  146  OD1 ASP A  17     6522   6785  10790    639   1591   -539       O
ATOM    147  OD2 ASP A  17     -46.854  32.726 -17.127  1.00 61.43           O
ANISOU  147  OD2 ASP A  17     6050   6794  10496    462   1596   -546       O
ATOM    148  N   GLY A  18     -48.345  31.638 -12.072  1.00 35.84           N
ANISOU  148  N   GLY A  18     2802   3528   7287    928    637     37       N
ATOM    149  CA  GLY A  18     -47.377  31.252 -11.064  1.00 34.96           C
ANISOU  149  CA  GLY A  18     2542   3505   7238   1073    494    167       C
ATOM    150  C   GLY A  18     -46.244  32.231 -10.862  1.00 35.96           C
ANISOU  150  C   GLY A  18     2418   3845   7401   1031    408    163       C
ATOM    151  O   GLY A  18     -45.160  31.830 -10.428  1.00 46.31           O
ANISOU  151  O   GLY A  18     3552   5239   8805   1160    362    223       O
ATOM    152  N   GLN A  19     -46.463  33.507 -11.160  1.00 37.43           N
ANISOU  152  N   GLN A  19     2580   4121   7519    850    388     92       N
ATOM    153  CA  GLN A  19     -45.425  34.520 -11.046  1.00 39.71           C
ANISOU  153  CA  GLN A  19     2651   4600   7838    758    337     61       C
ATOM    154  C   GLN A  19     -45.480  35.199  -9.683  1.00 42.17           C
ANISOU  154  C   GLN A  19     2911   5075   8038    718     55    147       C
ATOM    155  O   GLN A  19     -46.539  35.300  -9.057  1.00 46.46           O
ANISOU  155  O   GLN A  19     3614   5580   8460    695    -73    200       O
ATOM    156  CB  GLN A  19     -45.573  35.567 -12.152  1.00 41.04           C
ANISOU  156  CB  GLN A  19     2837   4761   7995    554    506    -66       C
ATOM    157  CG  GLN A  19     -45.697  34.987 -13.553  1.00 46.18           C
ANISOU  157  CG  GLN A  19     3576   5270   8699    551    807   -175       C
ATOM    158  CD  GLN A  19     -44.431  34.293 -14.018  1.00 52.43           C
ANISOU  158  CD  GLN A  19     4214   6069   9637    645    974   -228       C
ATOM    159  OE1 GLN A  19     -43.328  34.632 -13.589  1.00 56.41           O
ANISOU  159  OE1 GLN A  19     4498   6724  10210    657    900   -209       O
ATOM    160  NE2 GLN A  19     -44.585  33.313 -14.902  1.00 55.19           N
ANISOU  160  NE2 GLN A  19     4675   6263  10033    704   1208   -311       N
ATOM    161  N   GLN A  20     -44.320  35.665  -9.228  1.00 44.50           N
ANISOU  161  N   GLN A  20     2974   5568   8367    695    -31    144       N
ATOM    162  CA  GLN A  20     -44.233  36.403  -7.976  1.00 46.28           C
ANISOU  162  CA  GLN A  20     3128   5983   8472    616   -279    186       C
ATOM    163  C   GLN A  20     -44.596  37.866  -8.189  1.00 43.02           C
ANISOU  163  C   GLN A  20     2761   5592   7994    361   -268     78       C
ATOM    164  O   GLN A  20     -44.313  38.453  -9.237  1.00 46.09           O
ANISOU  164  O   GLN A  20     3125   5933   8453    240    -81    -22       O
ATOM    165  CB  GLN A  20     -42.825  36.309  -7.388  1.00 54.62           C
ANISOU  165  CB  GLN A  20     3895   7276   9582    680   -382    214       C
ATOM    166  CG  GLN A  20     -42.476  34.966  -6.779  1.00 70.11           C
ANISOU  166  CG  GLN A  20     5804   9249  11584    948   -467    359       C
ATOM    167  CD  GLN A  20     -41.079  34.951  -6.189  1.00 89.11           C
ANISOU  167  CD  GLN A  20     7888  11928  14040   1019   -592    386       C
ATOM    168  OE1 GLN A  20     -40.211  35.721  -6.603  1.00 92.82           O
ANISOU  168  OE1 GLN A  20     8153  12544  14571    886   -531    276       O
ATOM    169  NE2 GLN A  20     -40.857  34.080  -5.212  1.00 98.18           N
ANISOU  169  NE2 GLN A  20     8989  13155  15160   1225   -770    537       N
ATOM    170  N   GLY A  21     -45.214  38.455  -7.181  1.00 36.47           N
ANISOU  170  N   GLY A  21     2007   4823   7026    274   -452     96       N
ATOM    171  CA  GLY A  21     -45.601  39.853  -7.211  1.00 33.55           C
ANISOU  171  CA  GLY A  21     1701   4447   6598     36   -448     -8       C
ATOM    172  C   GLY A  21     -46.955  40.057  -6.562  1.00 40.06           C
ANISOU  172  C   GLY A  21     2734   5188   7301     10   -556     17       C
ATOM    173  O   GLY A  21     -47.761  39.137  -6.426  1.00 41.41           O
ANISOU  173  O   GLY A  21     3030   5266   7440    158   -583    107       O
ATOM    174  N   GLU A  22     -47.208  41.296  -6.146  1.00 39.34           N
ANISOU  174  N   GLU A  22     2684   5119   7145   -193   -600    -75       N
ATOM    175  CA  GLU A  22     -48.466  41.661  -5.511  1.00 39.83           C
ANISOU  175  CA  GLU A  22     2975   5101   7056   -236   -667    -82       C
ATOM    176  C   GLU A  22     -48.904  43.034  -5.996  1.00 42.20           C
ANISOU  176  C   GLU A  22     3426   5273   7336   -422   -542   -189       C
ATOM    177  O   GLU A  22     -48.076  43.932  -6.170  1.00 44.84           O
ANISOU  177  O   GLU A  22     3649   5648   7742   -590   -487   -281       O
ATOM    178  CB  GLU A  22     -48.350  41.672  -3.979  1.00 46.88           C
ANISOU  178  CB  GLU A  22     3804   6180   7829   -275   -888    -79       C
ATOM    179  CG  GLU A  22     -48.295  40.297  -3.331  1.00 58.49           C
ANISOU  179  CG  GLU A  22     5217   7736   9272    -67  -1030     82       C
ATOM    180  CD  GLU A  22     -46.898  39.710  -3.309  1.00 70.41           C
ANISOU  180  CD  GLU A  22     6501   9416  10835     34  -1065    142       C
ATOM    181  OE1 GLU A  22     -45.938  40.440  -3.634  1.00 74.79           O
ANISOU  181  OE1 GLU A  22     6896  10072  11448    -92  -1016     42       O
ATOM    182  OE2 GLU A  22     -46.760  38.517  -2.965  1.00 75.02           O
ANISOU  182  OE2 GLU A  22     7068  10024  11411    238  -1130    289       O
ATOM    183  N   VAL A  23     -50.207  43.187  -6.213  1.00 41.19           N
ANISOU  183  N   VAL A  23     3542   4985   7125   -389   -492   -169       N
ATOM    184  CA  VAL A  23     -50.799  44.483  -6.536  1.00 40.99           C
ANISOU  184  CA  VAL A  23     3678   4809   7088   -520   -390   -236       C
ATOM    185  C   VAL A  23     -51.872  44.779  -5.495  1.00 34.45           C
ANISOU  185  C   VAL A  23     2989   3951   6149   -528   -466   -273       C
ATOM    186  O   VAL A  23     -52.469  43.843  -4.944  1.00 31.70           O
ANISOU  186  O   VAL A  23     2674   3653   5719   -410   -555   -213       O
ATOM    187  CB  VAL A  23     -51.370  44.505  -7.964  1.00 25.43           C
ANISOU  187  CB  VAL A  23     1848   2678   5137   -463   -241   -166       C
ATOM    188  CG1 VAL A  23     -50.279  44.205  -8.981  1.00 26.40           C
ANISOU  188  CG1 VAL A  23     1843   2838   5349   -478   -130   -152       C
ATOM    189  CG2 VAL A  23     -52.508  43.518  -8.100  1.00 23.75           C
ANISOU  189  CG2 VAL A  23     1751   2429   4846   -301   -277    -85       C
ATOM    190  N   PRO A  24     -52.138  46.046  -5.176  1.00 34.92           N
ANISOU  190  N   PRO A  24     3139   3916   6212   -671   -409   -378       N
ATOM    191  CA  PRO A  24     -53.154  46.345  -4.158  1.00 30.62           C
ANISOU  191  CA  PRO A  24     2720   3338   5574   -682   -445   -442       C
ATOM    192  C   PRO A  24     -54.554  46.029  -4.659  1.00 32.21           C
ANISOU  192  C   PRO A  24     3072   3405   5762   -526   -396   -355       C
ATOM    193  O   PRO A  24     -54.910  46.326  -5.803  1.00 26.60           O
ANISOU  193  O   PRO A  24     2430   2557   5121   -473   -301   -285       O
ATOM    194  CB  PRO A  24     -52.971  47.846  -3.902  1.00 33.62           C
ANISOU  194  CB  PRO A  24     3159   3605   6011   -878   -345   -593       C
ATOM    195  CG  PRO A  24     -52.341  48.366  -5.151  1.00 36.51           C
ANISOU  195  CG  PRO A  24     3509   3859   6507   -921   -220   -549       C
ATOM    196  CD  PRO A  24     -51.464  47.262  -5.663  1.00 32.88           C
ANISOU  196  CD  PRO A  24     2873   3565   6055   -845   -286   -457       C
ATOM    197  N   VAL A  25     -55.356  45.429  -3.782  1.00 31.92           N
ANISOU  197  N   VAL A  25     3080   3426   5622   -466   -464   -357       N
ATOM    198  CA  VAL A  25     -56.681  44.934  -4.130  1.00 27.47           C
ANISOU  198  CA  VAL A  25     2614   2784   5041   -331   -434   -286       C
ATOM    199  C   VAL A  25     -57.693  45.450  -3.117  1.00 28.15           C
ANISOU  199  C   VAL A  25     2788   2832   5076   -364   -403   -387       C
ATOM    200  O   VAL A  25     -57.427  45.466  -1.910  1.00 29.96           O
ANISOU  200  O   VAL A  25     3011   3170   5202   -461   -454   -478       O
ATOM    201  CB  VAL A  25     -56.709  43.391  -4.182  1.00 29.34           C
ANISOU  201  CB  VAL A  25     2811   3122   5216   -220   -510   -181       C
ATOM    202  CG1 VAL A  25     -58.122  42.884  -4.409  1.00 30.15           C
ANISOU  202  CG1 VAL A  25     3002   3163   5290   -128   -476   -142       C
ATOM    203  CG2 VAL A  25     -55.780  42.883  -5.268  1.00 25.68           C
ANISOU  203  CG2 VAL A  25     2263   2669   4824   -176   -496   -106       C
ATOM    204  N   SER A  26     -58.852  45.878  -3.611  1.00 29.62           N
ANISOU  204  N   SER A  26     3047   2878   5329   -283   -318   -372       N
ATOM    205  CA  SER A  26     -59.999  46.200  -2.776  1.00 30.37           C
ANISOU  205  CA  SER A  26     3202   2930   5405   -275   -259   -462       C
ATOM    206  C   SER A  26     -61.192  45.372  -3.233  1.00 31.62           C
ANISOU  206  C   SER A  26     3357   3099   5559   -141   -264   -372       C
ATOM    207  O   SER A  26     -61.442  45.236  -4.435  1.00 33.24           O
ANISOU  207  O   SER A  26     3547   3259   5826    -51   -270   -263       O
ATOM    208  CB  SER A  26     -60.338  47.692  -2.835  1.00 34.36           C
ANISOU  208  CB  SER A  26     3770   3239   6046   -301   -127   -553       C
ATOM    209  OG  SER A  26     -60.726  48.077  -4.141  1.00 44.33           O
ANISOU  209  OG  SER A  26     5043   4365   7435   -182    -91   -424       O
ATOM    210  N   ILE A  27     -61.920  44.809  -2.275  1.00 27.57           N
ANISOU  210  N   ILE A  27     2860   2660   4954   -152   -257   -425       N
ATOM    211  CA  ILE A  27     -63.066  43.955  -2.556  1.00 25.53           C
ANISOU  211  CA  ILE A  27     2584   2430   4686    -66   -250   -368       C
ATOM    212  C   ILE A  27     -64.313  44.638  -2.018  1.00 30.84           C
ANISOU  212  C   ILE A  27     3257   3041   5420    -45   -136   -472       C
ATOM    213  O   ILE A  27     -64.397  44.937  -0.820  1.00 37.01           O
ANISOU  213  O   ILE A  27     4084   3844   6133   -135    -71   -601       O
ATOM    214  CB  ILE A  27     -62.902  42.555  -1.948  1.00 27.57           C
ANISOU  214  CB  ILE A  27     2859   2815   4800    -98   -310   -323       C
ATOM    215  CG1 ILE A  27     -61.824  41.775  -2.703  1.00 22.55           C
ANISOU  215  CG1 ILE A  27     2197   2211   4161    -68   -397   -208       C
ATOM    216  CG2 ILE A  27     -64.228  41.809  -1.964  1.00 24.70           C
ANISOU  216  CG2 ILE A  27     2489   2470   4427    -64   -259   -315       C
ATOM    217  CD1 ILE A  27     -61.669  40.349  -2.238  1.00 27.68           C
ANISOU  217  CD1 ILE A  27     2872   2935   4711    -63   -441   -133       C
ATOM    218  N  AILE A  28     -65.289  44.848  -2.897  0.52 31.75           N
ANISOU  218  N  AILE A  28     3311   3098   5655     71   -112   -418       N
ATOM    219  N  BILE A  28     -65.265  44.920  -2.902  0.48 31.95           N
ANISOU  219  N  BILE A  28     3338   3116   5686     72   -109   -420       N
ATOM    220  CA AILE A  28     -66.564  45.452  -2.532  0.52 34.28           C
ANISOU  220  CA AILE A  28     3581   3361   6082    133      0   -500       C
ATOM    221  CA BILE A  28     -66.509  45.562  -2.500  0.48 34.33           C
ANISOU  221  CA BILE A  28     3594   3357   6095    131      6   -507       C
ATOM    222  C  AILE A  28     -67.587  45.062  -3.592  0.52 34.71           C
ANISOU  222  C  AILE A  28     3523   3455   6210    254    -48   -393       C
ATOM    223  C  BILE A  28     -67.617  45.031  -3.395  0.48 34.81           C
ANISOU  223  C  BILE A  28     3540   3472   6213    241    -34   -414       C
ATOM    224  O  AILE A  28     -67.264  44.963  -4.779  0.52 34.83           O
ANISOU  224  O  AILE A  28     3528   3473   6233    305   -144   -262       O
ATOM    225  O  BILE A  28     -67.390  44.697  -4.561  0.48 33.58           O
ANISOU  225  O  BILE A  28     3363   3344   6050    286   -138   -283       O
ATOM    226  CB AILE A  28     -66.430  46.989  -2.387  0.52 36.24           C
ANISOU  226  CB AILE A  28     3866   3425   6480    160    104   -578       C
ATOM    227  CB BILE A  28     -66.401  47.106  -2.548  0.48 36.20           C
ANISOU  227  CB BILE A  28     3860   3400   6495    175    101   -562       C
ATOM    228  CG1AILE A  28     -67.750  47.615  -1.934  0.52 36.66           C
ANISOU  228  CG1AILE A  28     3852   3398   6677    249    251   -677       C
ATOM    229  CG1BILE A  28     -67.632  47.757  -1.915  0.48 36.80           C
ANISOU  229  CG1BILE A  28     3884   3396   6702    244    258   -684       C
ATOM    230  CG2AILE A  28     -65.949  47.616  -3.687  0.52 36.41           C
ANISOU  230  CG2AILE A  28     3894   3334   6607    245     48   -432       C
ATOM    231  CG2BILE A  28     -66.199  47.598  -3.967  0.48 36.80           C
ANISOU  231  CG2BILE A  28     3919   3381   6680    287     37   -396       C
ATOM    232  CD1AILE A  28     -67.680  49.116  -1.752  0.52 39.24           C
ANISOU  232  CD1AILE A  28     4232   3493   7184    288    393   -766       C
ATOM    233  CD1BILE A  28     -67.553  49.264  -1.843  0.48 39.25           C
ANISOU  233  CD1BILE A  28     4245   3467   7200    290    393   -758       C
ATOM    234  N  AASN A  29     -68.820  44.805  -3.145  0.52 37.36           N
ANISOU  234  N  AASN A  29     3768   3847   6581    277     22   -460       N
ATOM    235  N  BASN A  29     -68.816  44.943  -2.830  0.48 38.03           N
ANISOU  235  N  BASN A  29     3866   3917   6666    262     55   -498       N
ATOM    236  CA AASN A  29     -69.957  44.547  -4.035  0.52 40.71           C
ANISOU  236  CA AASN A  29     4039   4341   7089    380    -25   -387       C
ATOM    237  CA BASN A  29     -69.939  44.215  -3.436  0.48 39.75           C
ANISOU  237  CA BASN A  29     3945   4246   6911    315     16   -447       C
ATOM    238  C  AASN A  29     -69.752  43.290  -4.882  0.52 37.52           C
ANISOU  238  C  AASN A  29     3635   4065   6556    323   -150   -293       C
ATOM    239  C  BASN A  29     -69.447  42.782  -3.664  0.48 37.64           C
ANISOU  239  C  BASN A  29     3736   4092   6472    207    -71   -392       C
ATOM    240  O  AASN A  29     -70.062  43.274  -6.075  0.52 32.27           O
ANISOU  240  O  AASN A  29     2896   3448   5916    391   -249   -188       O
ATOM    241  O  BASN A  29     -68.804  42.202  -2.776  0.48 35.29           O
ANISOU  241  O  BASN A  29     3549   3814   6047     99    -45   -432       O
ATOM    242  CB AASN A  29     -70.244  45.753  -4.936  0.52 43.88           C
ANISOU  242  CB AASN A  29     4374   4629   7668    552    -51   -288       C
ATOM    243  CB BASN A  29     -70.432  44.939  -4.677  0.48 42.49           C
ANISOU  243  CB BASN A  29     4182   4554   7407    478    -57   -326       C
ATOM    244  CG AASN A  29     -70.363  47.050  -4.161  0.52 47.27           C
ANISOU  244  CG AASN A  29     4828   4872   8260    614    105   -390       C
ATOM    245  CG BASN A  29     -70.506  46.443  -4.484  0.48 45.73           C
ANISOU  245  CG BASN A  29     4597   4774   8005    598     39   -348       C
ATOM    246  OD1AASN A  29     -69.750  48.058  -4.519  0.52 47.98           O
ANISOU  246  OD1AASN A  29     4999   4791   8439    669    120   -336       O
ATOM    247  OD1BASN A  29     -69.866  47.205  -5.209  0.48 47.37           O
ANISOU  247  OD1BASN A  29     4872   4861   8266    662     -6   -239       O
ATOM    248  ND2AASN A  29     -71.155  47.034  -3.096  0.52 48.16           N
ANISOU  248  ND2AASN A  29     4882   5003   8414    590    249   -552       N
ATOM    249  ND2BASN A  29     -71.288  46.877  -3.502  0.48 47.79           N
ANISOU  249  ND2BASN A  29     4798   4990   8372    620    198   -496       N
ATOM    250  N  AASN A  30     -69.235  42.227  -4.261  0.52 34.88           N
ANISOU  250  N  AASN A  30     3393   3783   6078    195   -138   -330       N
ATOM    251  N  BASN A  30     -69.723  42.187  -4.821  0.48 34.58           N
ANISOU  251  N  BASN A  30     3284   3778   6076    233   -169   -300       N
ATOM    252  CA AASN A  30     -68.977  40.951  -4.938  0.52 31.35           C
ANISOU  252  CA AASN A  30     2972   3412   5527    132   -211   -267       C
ATOM    253  CA BASN A  30     -69.138  40.908  -5.214  0.48 31.93           C
ANISOU  253  CA BASN A  30     3022   3500   5608    142   -227   -255       C
ATOM    254  C  AASN A  30     -68.100  41.135  -6.177  0.52 26.23           C
ANISOU  254  C  AASN A  30     2359   2737   4868    175   -310   -160       C
ATOM    255  C  BASN A  30     -68.059  41.103  -6.267  0.48 26.49           C
ANISOU  255  C  BASN A  30     2394   2771   4898    175   -316   -154       C
ATOM    256  O  AASN A  30     -68.212  40.389  -7.153  0.52 25.30           O
ANISOU  256  O  AASN A  30     2228   2688   4699    150   -366   -117       O
ATOM    257  O  BASN A  30     -67.975  40.332  -7.227  0.48 25.51           O
ANISOU  257  O  BASN A  30     2274   2705   4714    145   -371   -107       O
ATOM    258  CB AASN A  30     -70.286  40.239  -5.300  0.52 34.68           C
ANISOU  258  CB AASN A  30     3268   3947   5961    102   -205   -296       C
ATOM    259  CB BASN A  30     -70.221  39.965  -5.731  0.48 34.57           C
ANISOU  259  CB BASN A  30     3255   3955   5927     92   -240   -271       C
ATOM    260  CG AASN A  30     -70.236  38.748  -5.022  0.52 35.76           C
ANISOU  260  CG AASN A  30     3479   4122   5984    -34   -170   -320       C
ATOM    261  CG BASN A  30     -70.334  38.691  -4.915  0.48 35.84           C
ANISOU  261  CG BASN A  30     3487   4137   5994    -44   -158   -330       C
ATOM    262  OD1AASN A  30     -69.390  38.273  -4.264  0.52 35.06           O
ANISOU  262  OD1AASN A  30     3528   3976   5815    -83   -137   -309       O
ATOM    263  OD1BASN A  30     -69.391  38.286  -4.234  0.48 35.08           O
ANISOU  263  OD1BASN A  30     3532   3978   5818    -83   -135   -310       O
ATOM    264  ND2AASN A  30     -71.149  38.002  -5.632  0.52 37.61           N
ANISOU  264  ND2AASN A  30     3620   4453   6216    -99   -177   -348       N
ATOM    265  ND2BASN A  30     -71.492  38.046  -4.988  0.48 37.92           N
ANISOU  265  ND2BASN A  30     3645   4494   6269   -118   -116   -391       N
ATOM    266  N   THR A  31     -67.225  42.135  -6.132  1.00 27.41           N
ANISOU  266  N   THR A  31     2564   2789   5061    216   -311   -135       N
ATOM    267  CA  THR A  31     -66.319  42.498  -7.211  1.00 30.22           C
ANISOU  267  CA  THR A  31     2964   3106   5414    241   -368    -39       C
ATOM    268  C   THR A  31     -64.916  42.698  -6.661  1.00 25.92           C
ANISOU  268  C   THR A  31     2502   2500   4847    187   -349    -59       C
ATOM    269  O   THR A  31     -64.742  43.177  -5.537  1.00 26.73           O
ANISOU  269  O   THR A  31     2626   2565   4965    154   -302   -141       O
ATOM    270  CB  THR A  31     -66.800  43.780  -7.919  1.00 32.35           C
ANISOU  270  CB  THR A  31     3193   3307   5793    351   -383     37       C
ATOM    271  OG1 THR A  31     -68.182  43.643  -8.271  1.00 35.43           O
ANISOU  271  OG1 THR A  31     3458   3787   6218    417   -420     56       O
ATOM    272  CG2 THR A  31     -65.991  44.047  -9.181  1.00 30.14           C
ANISOU  272  CG2 THR A  31     2974   3006   5474    357   -434    158       C
ATOM    273  N   VAL A  32     -63.920  42.320  -7.455  1.00 24.15           N
ANISOU  273  N   VAL A  32     2310   2284   4581    164   -381      1       N
ATOM    274  CA  VAL A  32     -62.517  42.517  -7.116  1.00 18.83           C
ANISOU  274  CA  VAL A  32     1668   1581   3907    115   -374    -10       C
ATOM    275  C   VAL A  32     -61.997  43.709  -7.905  1.00 25.50           C
ANISOU  275  C   VAL A  32     2534   2337   4820    122   -352     38       C
ATOM    276  O   VAL A  32     -62.174  43.779  -9.128  1.00 23.88           O
ANISOU  276  O   VAL A  32     2342   2130   4602    154   -362    127       O
ATOM    277  CB  VAL A  32     -61.690  41.256  -7.414  1.00 27.04           C
ANISOU  277  CB  VAL A  32     2710   2678   4888     94   -392     18       C
ATOM    278  CG1 VAL A  32     -60.240  41.467  -7.013  1.00 28.82           C
ANISOU  278  CG1 VAL A  32     2913   2903   5134     56   -400     10       C
ATOM    279  CG2 VAL A  32     -62.278  40.054  -6.695  1.00 25.71           C
ANISOU  279  CG2 VAL A  32     2551   2555   4661     87   -395     -4       C
ATOM    280  N   TYR A  33     -61.363  44.649  -7.208  1.00 21.30           N
ANISOU  280  N   TYR A  33     2017   1733   4344     71   -314    -21       N
ATOM    281  CA  TYR A  33     -60.786  45.831  -7.826  1.00 25.58           C
ANISOU  281  CA  TYR A  33     2598   2155   4965     48   -261     15       C
ATOM    282  C   TYR A  33     -59.294  45.894  -7.538  1.00 23.30           C
ANISOU  282  C   TYR A  33     2285   1893   4674    -68   -250    -38       C
ATOM    283  O   TYR A  33     -58.811  45.343  -6.545  1.00 26.41           O
ANISOU  283  O   TYR A  33     2631   2386   5020   -118   -295   -113       O
ATOM    284  CB  TYR A  33     -61.449  47.117  -7.316  1.00 28.39           C
ANISOU  284  CB  TYR A  33     2994   2361   5433     74   -190    -33       C
ATOM    285  CG  TYR A  33     -62.913  47.256  -7.653  1.00 29.04           C
ANISOU  285  CG  TYR A  33     3057   2413   5563    213   -198     31       C
ATOM    286  CD1 TYR A  33     -63.887  46.698  -6.838  1.00 22.21           C
ANISOU  286  CD1 TYR A  33     2135   1625   4679    246   -207    -47       C
ATOM    287  CD2 TYR A  33     -63.323  47.962  -8.776  1.00 26.45           C
ANISOU  287  CD2 TYR A  33     2758   1993   5300    310   -198    180       C
ATOM    288  CE1 TYR A  33     -65.225  46.827  -7.138  1.00 25.23           C
ANISOU  288  CE1 TYR A  33     2454   2006   5127    371   -213      0       C
ATOM    289  CE2 TYR A  33     -64.662  48.097  -9.083  1.00 28.27           C
ANISOU  289  CE2 TYR A  33     2930   2227   5584    454   -233    254       C
ATOM    290  CZ  TYR A  33     -65.609  47.528  -8.260  1.00 31.79           C
ANISOU  290  CZ  TYR A  33     3283   2764   6033    484   -239    152       C
ATOM    291  OH  TYR A  33     -66.946  47.659  -8.558  1.00 36.42           O
ANISOU  291  OH  TYR A  33     3766   3379   6693    624   -273    215       O
ATOM    292  N   THR A  34     -58.567  46.579  -8.416  1.00 25.21           N
ANISOU  292  N   THR A  34     2555   2059   4966   -113   -192     14       N
ATOM    293  CA  THR A  34     -57.162  46.881  -8.198  1.00 29.19           C
ANISOU  293  CA  THR A  34     3008   2582   5501   -245   -160    -50       C
ATOM    294  C   THR A  34     -56.920  48.354  -8.494  1.00 30.50           C
ANISOU  294  C   THR A  34     3254   2564   5769   -325    -48    -55       C
ATOM    295  O   THR A  34     -57.570  48.944  -9.362  1.00 32.80           O
ANISOU  295  O   THR A  34     3644   2723   6095   -254      2     61       O
ATOM    296  CB  THR A  34     -56.240  46.007  -9.066  1.00 31.12           C
ANISOU  296  CB  THR A  34     3185   2928   5712   -252   -160      6       C
ATOM    297  OG1 THR A  34     -54.874  46.269  -8.726  1.00 28.26           O
ANISOU  297  OG1 THR A  34     2722   2616   5401   -377   -136    -70       O
ATOM    298  CG2 THR A  34     -56.452  46.293 -10.549  1.00 29.53           C
ANISOU  298  CG2 THR A  34     3072   2654   5494   -229    -88    126       C
ATOM    299  N   LYS A  35     -55.993  48.949  -7.751  1.00 33.12           N
ANISOU  299  N   LYS A  35     3547   2890   6148   -480    -12   -184       N
ATOM    300  CA  LYS A  35     -55.664  50.358  -7.914  1.00 37.85           C
ANISOU  300  CA  LYS A  35     4233   3286   6860   -598    124   -220       C
ATOM    301  C   LYS A  35     -54.619  50.499  -9.014  1.00 36.49           C
ANISOU  301  C   LYS A  35     4046   3108   6712   -688    202   -145       C
ATOM    302  O   LYS A  35     -53.520  49.945  -8.907  1.00 32.38           O
ANISOU  302  O   LYS A  35     3380   2754   6170   -781    172   -205       O
ATOM    303  CB  LYS A  35     -55.154  50.956  -6.603  1.00 44.08           C
ANISOU  303  CB  LYS A  35     4990   4084   7675   -772    142   -431       C
ATOM    304  CG  LYS A  35     -54.979  52.468  -6.638  1.00 47.28           C
ANISOU  304  CG  LYS A  35     5517   4229   8219   -908    315   -505       C
ATOM    305  CD  LYS A  35     -54.082  52.951  -5.506  1.00 54.48           C
ANISOU  305  CD  LYS A  35     6366   5209   9125  -1157    331   -744       C
ATOM    306  CE  LYS A  35     -54.767  52.852  -4.152  1.00 58.23           C
ANISOU  306  CE  LYS A  35     6855   5746   9524  -1159    278   -901       C
ATOM    307  NZ  LYS A  35     -55.267  54.174  -3.682  1.00 62.02           N
ANISOU  307  NZ  LYS A  35     7506   6011  10047  -1202    446  -1016       N
ATOM    308  N   VAL A  36     -54.966  51.230 -10.070  1.00 36.82           N
ANISOU  308  N   VAL A  36     4230   2963   6796   -653    304     -3       N
ATOM    309  CA  VAL A  36     -54.078  51.474 -11.201  1.00 36.77           C
ANISOU  309  CA  VAL A  36     4250   2927   6791   -754    414     85       C
ATOM    310  C   VAL A  36     -53.876  52.978 -11.302  1.00 45.31           C
ANISOU  310  C   VAL A  36     5477   3735   8004   -881    584     87       C
ATOM    311  O   VAL A  36     -54.782  53.703 -11.733  1.00 49.78           O
ANISOU  311  O   VAL A  36     6212   4088   8616   -769    631    228       O
ATOM    312  CB  VAL A  36     -54.639  50.905 -12.510  1.00 34.40           C
ANISOU  312  CB  VAL A  36     4025   2669   6377   -618    390    284       C
ATOM    313  CG1 VAL A  36     -53.741  51.279 -13.678  1.00 38.46           C
ANISOU  313  CG1 VAL A  36     4602   3141   6871   -748    539    373       C
ATOM    314  CG2 VAL A  36     -54.790  49.397 -12.411  1.00 27.19           C
ANISOU  314  CG2 VAL A  36     2984   1991   5354   -521    259    254       C
ATOM    315  N   ASP A  37     -52.692  53.447 -10.905  1.00 50.20           N
ANISOU  315  N   ASP A  37     6023   4360   8690  -1111    675    -66       N
ATOM    316  CA  ASP A  37     -52.357  54.872 -10.928  1.00 52.30           C
ANISOU  316  CA  ASP A  37     6441   4445   8988  -1234    829    -97       C
ATOM    317  C   ASP A  37     -53.359  55.692 -10.119  1.00 44.47           C
ANISOU  317  C   ASP A  37     5577   3279   8043  -1142    837   -150       C
ATOM    318  O   ASP A  37     -53.770  56.781 -10.522  1.00 45.43           O
ANISOU  318  O   ASP A  37     5886   3168   8209  -1100    950    -54       O
ATOM    319  CB  ASP A  37     -52.252  55.394 -12.363  1.00 68.87           C
ANISOU  319  CB  ASP A  37     8703   6399  11066  -1234    960    118       C
ATOM    320  CG  ASP A  37     -50.898  55.114 -12.984  1.00 87.72           C
ANISOU  320  CG  ASP A  37    10981   8926  13421  -1425   1047     88       C
ATOM    321  OD1 ASP A  37     -49.876  55.529 -12.396  1.00 94.59           O
ANISOU  321  OD1 ASP A  37    11752   9868  14322  -1618   1095    -93       O
ATOM    322  OD2 ASP A  37     -50.852  54.469 -14.053  1.00 93.48           O
ANISOU  322  OD2 ASP A  37    11717   9711  14089  -1386   1072    236       O
ATOM    323  N   GLY A  38     -53.759  55.160  -8.967  1.00 38.70           N
ANISOU  323  N   GLY A  38     4743   2662   7300  -1108    724   -299       N
ATOM    324  CA  GLY A  38     -54.604  55.884  -8.045  1.00 45.81           C
ANISOU  324  CA  GLY A  38     5738   3430   8238  -1054    760   -402       C
ATOM    325  C   GLY A  38     -56.094  55.694  -8.225  1.00 49.99           C
ANISOU  325  C   GLY A  38     6330   3866   8799   -786    715   -265       C
ATOM    326  O   GLY A  38     -56.867  56.252  -7.436  1.00 55.35           O
ANISOU  326  O   GLY A  38     7065   4445   9522   -724    762   -360       O
ATOM    327  N   VAL A  39     -56.528  54.936  -9.229  1.00 46.14           N
ANISOU  327  N   VAL A  39     5821   3424   8285   -631    630    -54       N
ATOM    328  CA  VAL A  39     -57.948  54.693  -9.447  1.00 42.26           C
ANISOU  328  CA  VAL A  39     5350   2899   7806   -377    556     82       C
ATOM    329  C   VAL A  39     -58.198  53.192  -9.462  1.00 34.68           C
ANISOU  329  C   VAL A  39     4247   2175   6756   -305    386    104       C
ATOM    330  O   VAL A  39     -57.336  52.399  -9.854  1.00 36.94           O
ANISOU  330  O   VAL A  39     4456   2650   6930   -389    330    111       O
ATOM    331  CB  VAL A  39     -58.465  55.348 -10.748  1.00 41.34           C
ANISOU  331  CB  VAL A  39     5372   2637   7698   -233    592    351       C
ATOM    332  CG1 VAL A  39     -58.257  56.852 -10.703  1.00 42.72           C
ANISOU  332  CG1 VAL A  39     5707   2571   7955   -291    760    336       C
ATOM    333  CG2 VAL A  39     -57.788  54.743 -11.968  1.00 40.17           C
ANISOU  333  CG2 VAL A  39     5226   2574   7461   -289    561    515       C
ATOM    334  N   ASP A  40     -59.395  52.807  -9.026  1.00 34.71           N
ANISOU  334  N   ASP A  40     4209   2224   6755   -138    310    102       N
ATOM    335  CA  ASP A  40     -59.763  51.401  -8.947  1.00 38.02           C
ANISOU  335  CA  ASP A  40     4508   2913   7023    -69    154    107       C
ATOM    336  C   ASP A  40     -60.287  50.914 -10.292  1.00 33.31           C
ANISOU  336  C   ASP A  40     3921   2388   6347     61     73    326       C
ATOM    337  O   ASP A  40     -61.100  51.586 -10.935  1.00 36.09           O
ANISOU  337  O   ASP A  40     4337   2610   6767    196     84    483       O
ATOM    338  CB  ASP A  40     -60.814  51.188  -7.860  1.00 41.79           C
ANISOU  338  CB  ASP A  40     4936   3421   7522     14    132     -9       C
ATOM    339  CG  ASP A  40     -60.344  51.655  -6.497  1.00 52.40           C
ANISOU  339  CG  ASP A  40     6290   4722   8897   -139    212   -243       C
ATOM    340  OD1 ASP A  40     -59.142  51.492  -6.195  1.00 55.69           O
ANISOU  340  OD1 ASP A  40     6679   5233   9249   -315    197   -332       O
ATOM    341  OD2 ASP A  40     -61.173  52.189  -5.731  1.00 58.50           O
ANISOU  341  OD2 ASP A  40     7087   5383   9756    -91    293   -347       O
ATOM    342  N   VAL A  41     -59.818  49.743 -10.713  1.00 27.72           N
ANISOU  342  N   VAL A  41     3149   1891   5493     21     -7    336       N
ATOM    343  CA  VAL A  41     -60.233  49.119 -11.962  1.00 31.48           C
ANISOU  343  CA  VAL A  41     3637   2477   5848     95    -81    496       C
ATOM    344  C   VAL A  41     -60.799  47.744 -11.639  1.00 27.29           C
ANISOU  344  C   VAL A  41     3004   2146   5218    138   -188    430       C
ATOM    345  O   VAL A  41     -60.149  46.946 -10.954  1.00 31.30           O
ANISOU  345  O   VAL A  41     3450   2748   5696     66   -195    307       O
ATOM    346  CB  VAL A  41     -59.065  49.011 -12.960  1.00 31.62           C
ANISOU  346  CB  VAL A  41     3701   2526   5785    -23    -20    554       C
ATOM    347  CG1 VAL A  41     -59.505  48.277 -14.217  1.00 34.18           C
ANISOU  347  CG1 VAL A  41     4052   2993   5941     23    -88    685       C
ATOM    348  CG2 VAL A  41     -58.534  50.396 -13.303  1.00 33.08           C
ANISOU  348  CG2 VAL A  41     4007   2493   6070    -90    110    630       C
ATOM    349  N   GLU A  42     -62.009  47.476 -12.123  1.00 24.85           N
ANISOU  349  N   GLU A  42     2675   1903   4865    252   -272    519       N
ATOM    350  CA  GLU A  42     -62.647  46.191 -11.876  1.00 25.06           C
ANISOU  350  CA  GLU A  42     2614   2102   4804    268   -352    451       C
ATOM    351  C   GLU A  42     -61.889  45.076 -12.584  1.00 30.14           C
ANISOU  351  C   GLU A  42     3269   2872   5312    180   -356    437       C
ATOM    352  O   GLU A  42     -61.593  45.172 -13.778  1.00 31.52           O
ANISOU  352  O   GLU A  42     3507   3072   5397    151   -347    536       O
ATOM    353  CB  GLU A  42     -64.100  46.217 -12.347  1.00 23.46           C
ANISOU  353  CB  GLU A  42     2360   1965   4590    386   -443    542       C
ATOM    354  CG  GLU A  42     -64.717  44.837 -12.475  1.00 45.31           C
ANISOU  354  CG  GLU A  42     5052   4924   7239    356   -517    482       C
ATOM    355  CD  GLU A  42     -66.121  44.872 -13.034  1.00 45.73           C
ANISOU  355  CD  GLU A  42     5016   5087   7272    447   -625    567       C
ATOM    356  OE1 GLU A  42     -66.846  45.851 -12.764  1.00 49.09           O
ANISOU  356  OE1 GLU A  42     5389   5428   7834    576   -634    631       O
ATOM    357  OE2 GLU A  42     -66.497  43.920 -13.750  1.00 47.31           O
ANISOU  357  OE2 GLU A  42     5187   5461   7328    387   -697    562       O
ATOM    358  N   LEU A  43     -61.574  44.016 -11.843  1.00 30.83           N
ANISOU  358  N   LEU A  43     3304   3026   5383    140   -354    319       N
ATOM    359  CA  LEU A  43     -60.918  42.845 -12.404  1.00 29.59           C
ANISOU  359  CA  LEU A  43     3149   2956   5137     82   -332    288       C
ATOM    360  C   LEU A  43     -61.838  41.648 -12.565  1.00 27.68           C
ANISOU  360  C   LEU A  43     2887   2816   4812     87   -377    251       C
ATOM    361  O   LEU A  43     -61.624  40.842 -13.472  1.00 28.38           O
ANISOU  361  O   LEU A  43     3008   2968   4806     35   -349    238       O
ATOM    362  CB  LEU A  43     -59.728  42.425 -11.533  1.00 27.83           C
ANISOU  362  CB  LEU A  43     2880   2718   4976     44   -289    206       C
ATOM    363  CG  LEU A  43     -58.516  43.356 -11.491  1.00 27.13           C
ANISOU  363  CG  LEU A  43     2782   2565   4960    -14   -229    206       C
ATOM    364  CD1 LEU A  43     -57.396  42.714 -10.688  1.00 21.65           C
ANISOU  364  CD1 LEU A  43     1994   1918   4313    -40   -224    132       C
ATOM    365  CD2 LEU A  43     -58.052  43.696 -12.898  1.00 30.38           C
ANISOU  365  CD2 LEU A  43     3256   2967   5322    -61   -155    280       C
ATOM    366  N   PHE A  44     -62.859  41.517 -11.721  1.00 26.57           N
ANISOU  366  N   PHE A  44     2698   2692   4706    126   -423    214       N
ATOM    367  CA  PHE A  44     -63.665  40.305 -11.697  1.00 26.21           C
ANISOU  367  CA  PHE A  44     2629   2732   4599     96   -441    154       C
ATOM    368  C   PHE A  44     -64.957  40.582 -10.948  1.00 25.37           C
ANISOU  368  C   PHE A  44     2449   2650   4541    139   -482    134       C
ATOM    369  O   PHE A  44     -64.924  41.045  -9.804  1.00 22.17           O
ANISOU  369  O   PHE A  44     2029   2180   4215    168   -455     99       O
ATOM    370  CB  PHE A  44     -62.888  39.162 -11.032  1.00 27.91           C
ANISOU  370  CB  PHE A  44     2865   2915   4826     63   -380     85       C
ATOM    371  CG  PHE A  44     -63.673  37.890 -10.883  1.00 26.12           C
ANISOU  371  CG  PHE A  44     2642   2726   4556     16   -363     21       C
ATOM    372  CD1 PHE A  44     -63.801  37.012 -11.945  1.00 20.58           C
ANISOU  372  CD1 PHE A  44     1978   2066   3774    -55   -330    -19       C
ATOM    373  CD2 PHE A  44     -64.261  37.561  -9.673  1.00 23.72           C
ANISOU  373  CD2 PHE A  44     2320   2408   4283     17   -359    -13       C
ATOM    374  CE1 PHE A  44     -64.514  35.836 -11.809  1.00 24.81           C
ANISOU  374  CE1 PHE A  44     2530   2614   4283   -129   -291    -98       C
ATOM    375  CE2 PHE A  44     -64.975  36.386  -9.530  1.00 24.50           C
ANISOU  375  CE2 PHE A  44     2437   2522   4351    -50   -318    -70       C
ATOM    376  CZ  PHE A  44     -65.102  35.522 -10.600  1.00 24.82           C
ANISOU  376  CZ  PHE A  44     2512   2587   4334   -125   -283   -116       C
ATOM    377  N   GLU A  45     -66.086  40.303 -11.593  1.00 28.14           N
ANISOU  377  N   GLU A  45     2742   3111   4839    130   -540    141       N
ATOM    378  CA  GLU A  45     -67.394  40.381 -10.958  1.00 25.69           C
ANISOU  378  CA  GLU A  45     2320   2853   4586    161   -564    103       C
ATOM    379  C   GLU A  45     -67.867  38.964 -10.660  1.00 25.07           C
ANISOU  379  C   GLU A  45     2232   2841   4453     50   -526     -4       C
ATOM    380  O   GLU A  45     -68.087  38.173 -11.583  1.00 29.06           O
ANISOU  380  O   GLU A  45     2744   3438   4860    -38   -549    -29       O
ATOM    381  CB  GLU A  45     -68.402  41.108 -11.847  1.00 25.97           C
ANISOU  381  CB  GLU A  45     2254   2989   4624    234   -669    195       C
ATOM    382  CG  GLU A  45     -69.788  41.215 -11.228  1.00 40.16           C
ANISOU  382  CG  GLU A  45     3886   4857   6515    281   -685    148       C
ATOM    383  CD  GLU A  45     -70.833  41.717 -12.205  1.00 51.96           C
ANISOU  383  CD  GLU A  45     5235   6499   8006    360   -822    253       C
ATOM    384  OE1 GLU A  45     -70.484  41.955 -13.380  1.00 57.41           O
ANISOU  384  OE1 GLU A  45     5985   7244   8586    364   -913    373       O
ATOM    385  OE2 GLU A  45     -72.004  41.871 -11.798  1.00 56.31           O
ANISOU  385  OE2 GLU A  45     5606   7129   8662    417   -840    222       O
ATOM    386  N   ASN A  46     -68.019  38.650  -9.377  1.00 21.52           N
ANISOU  386  N   ASN A  46     1784   2339   4054     35   -454    -70       N
ATOM    387  CA  ASN A  46     -68.388  37.302  -8.956  1.00 24.26           C
ANISOU  387  CA  ASN A  46     2155   2704   4359    -78   -388   -152       C
ATOM    388  C   ASN A  46     -69.837  37.021  -9.335  1.00 29.19           C
ANISOU  388  C   ASN A  46     2644   3470   4978   -142   -415   -211       C
ATOM    389  O   ASN A  46     -70.762  37.633  -8.791  1.00 31.15           O
ANISOU  389  O   ASN A  46     2766   3766   5303    -96   -415   -230       O
ATOM    390  CB  ASN A  46     -68.174  37.146  -7.453  1.00 22.65           C
ANISOU  390  CB  ASN A  46     2004   2420   4182    -81   -308   -178       C
ATOM    391  CG  ASN A  46     -68.506  35.755  -6.958  1.00 24.05           C
ANISOU  391  CG  ASN A  46     2242   2580   4317   -195   -221   -230       C
ATOM    392  OD1 ASN A  46     -68.500  34.794  -7.724  1.00 29.64           O
ANISOU  392  OD1 ASN A  46     2988   3285   4989   -271   -201   -255       O
ATOM    393  ND2 ASN A  46     -68.798  35.641  -5.668  1.00 29.78           N
ANISOU  393  ND2 ASN A  46     2994   3282   5038   -223   -150   -251       N
ATOM    394  N   LYS A  47     -70.037  36.093 -10.270  1.00 22.01           N
ANISOU  394  N   LYS A  47     1747   2633   3981   -258   -427   -257       N
ATOM    395  CA  LYS A  47     -71.364  35.635 -10.652  1.00 24.50           C
ANISOU  395  CA  LYS A  47     1921   3113   4273   -369   -457   -340       C
ATOM    396  C   LYS A  47     -71.676  34.245 -10.114  1.00 31.35           C
ANISOU  396  C   LYS A  47     2851   3933   5127   -542   -322   -459       C
ATOM    397  O   LYS A  47     -72.645  33.622 -10.560  1.00 31.56           O
ANISOU  397  O   LYS A  47     2782   4091   5118   -693   -326   -561       O
ATOM    398  CB  LYS A  47     -71.513  35.650 -12.176  1.00 33.94           C
ANISOU  398  CB  LYS A  47     3080   4464   5350   -419   -578   -325       C
ATOM    399  CG  LYS A  47     -71.362  37.026 -12.808  1.00 45.54           C
ANISOU  399  CG  LYS A  47     4495   5985   6822   -254   -714   -173       C
ATOM    400  CD  LYS A  47     -72.340  38.024 -12.202  1.00 57.39           C
ANISOU  400  CD  LYS A  47     5805   7534   8466   -116   -766   -124       C
ATOM    401  CE  LYS A  47     -73.781  37.728 -12.601  1.00 71.32           C
ANISOU  401  CE  LYS A  47     7341   9539  10220   -190   -858   -180       C
ATOM    402  NZ  LYS A  47     -74.082  38.148 -13.999  1.00 79.79           N
ANISOU  402  NZ  LYS A  47     8334  10811  11171   -167  -1054    -71       N
ATOM    403  N   THR A  48     -70.880  33.748  -9.170  1.00 30.83           N
ANISOU  403  N   THR A  48     2942   3685   5085   -530   -208   -442       N
ATOM    404  CA  THR A  48     -71.037  32.409  -8.629  1.00 27.72           C
ANISOU  404  CA  THR A  48     2655   3193   4684   -675    -62   -513       C
ATOM    405  C   THR A  48     -71.659  32.470  -7.236  1.00 26.56           C
ANISOU  405  C   THR A  48     2482   3028   4582   -690     23   -519       C
ATOM    406  O   THR A  48     -71.891  33.541  -6.669  1.00 28.75           O
ANISOU  406  O   THR A  48     2664   3360   4900   -584    -19   -489       O
ATOM    407  CB  THR A  48     -69.688  31.687  -8.581  1.00 30.63           C
ANISOU  407  CB  THR A  48     3226   3365   5047   -638      8   -458       C
ATOM    408  OG1 THR A  48     -68.989  32.060  -7.386  1.00 30.37           O
ANISOU  408  OG1 THR A  48     3257   3238   5044   -517     18   -353       O
ATOM    409  CG2 THR A  48     -68.840  32.062  -9.786  1.00 26.49           C
ANISOU  409  CG2 THR A  48     2716   2862   4488   -573    -68   -434       C
ATOM    410  N   THR A  49     -71.930  31.293  -6.679  1.00 31.92           N
ANISOU  410  N   THR A  49     3266   3614   5250   -836    168   -566       N
ATOM    411  CA  THR A  49     -72.424  31.162  -5.316  1.00 30.76           C
ANISOU  411  CA  THR A  49     3146   3434   5108   -884    285   -562       C
ATOM    412  C   THR A  49     -71.300  31.024  -4.299  1.00 33.50           C
ANISOU  412  C   THR A  49     3691   3622   5416   -788    317   -428       C
ATOM    413  O   THR A  49     -71.577  30.801  -3.116  1.00 25.19           O
ANISOU  413  O   THR A  49     2713   2537   4323   -842    418   -403       O
ATOM    414  CB  THR A  49     -73.363  29.958  -5.208  1.00 33.67           C
ANISOU  414  CB  THR A  49     3536   3782   5476  -1117    442   -668       C
ATOM    415  OG1 THR A  49     -72.664  28.768  -5.595  1.00 35.08           O
ANISOU  415  OG1 THR A  49     3916   3771   5641  -1181    519   -650       O
ATOM    416  CG2 THR A  49     -74.572  30.145  -6.112  1.00 31.77           C
ANISOU  416  CG2 THR A  49     3048   3758   5266  -1232    387   -813       C
ATOM    417  N   LEU A  50     -70.051  31.144  -4.732  1.00 23.39           N
ANISOU  417  N   LEU A  50     2488   2264   4136   -657    232   -339       N
ATOM    418  CA  LEU A  50     -68.872  31.054  -3.889  1.00 24.88           C
ANISOU  418  CA  LEU A  50     2820   2341   4294   -549    219   -200       C
ATOM    419  C   LEU A  50     -68.465  32.435  -3.398  1.00 23.32           C
ANISOU  419  C   LEU A  50     2547   2236   4079   -432    111   -170       C
ATOM    420  O   LEU A  50     -68.890  33.453  -3.953  1.00 23.16           O
ANISOU  420  O   LEU A  50     2384   2317   4100   -396     46   -235       O
ATOM    421  CB  LEU A  50     -67.724  30.417  -4.670  1.00 30.46           C
ANISOU  421  CB  LEU A  50     3611   2921   5041   -473    203   -141       C
ATOM    422  CG  LEU A  50     -67.935  28.980  -5.147  1.00 39.06           C
ANISOU  422  CG  LEU A  50     4815   3860   6166   -585    344   -182       C
ATOM    423  CD1 LEU A  50     -66.773  28.528  -6.015  1.00 38.88           C
ANISOU  423  CD1 LEU A  50     4851   3715   6207   -489    347   -153       C
ATOM    424  CD2 LEU A  50     -68.113  28.046  -3.960  1.00 44.01           C
ANISOU  424  CD2 LEU A  50     5602   4350   6770   -643    468    -93       C
ATOM    425  N   PRO A  51     -67.655  32.508  -2.340  1.00 22.84           N
ANISOU  425  N   PRO A  51     2584   2142   3954   -376     89    -70       N
ATOM    426  CA  PRO A  51     -67.113  33.806  -1.924  1.00 21.43           C
ANISOU  426  CA  PRO A  51     2347   2039   3756   -294     -7    -67       C
ATOM    427  C   PRO A  51     -66.333  34.459  -3.055  1.00 26.35           C
ANISOU  427  C   PRO A  51     2890   2662   4459   -193   -108    -62       C
ATOM    428  O   PRO A  51     -65.764  33.787  -3.918  1.00 27.57           O
ANISOU  428  O   PRO A  51     3068   2752   4654   -164   -115    -25       O
ATOM    429  CB  PRO A  51     -66.205  33.450  -0.743  1.00 22.18           C
ANISOU  429  CB  PRO A  51     2570   2114   3743   -274    -35     55       C
ATOM    430  CG  PRO A  51     -66.799  32.203  -0.189  1.00 23.50           C
ANISOU  430  CG  PRO A  51     2866   2210   3853   -368     84    105       C
ATOM    431  CD  PRO A  51     -67.330  31.442  -1.375  1.00 24.43           C
ANISOU  431  CD  PRO A  51     2956   2245   4081   -408    156     46       C
ATOM    432  N   VAL A  52     -66.315  35.793  -3.039  1.00 28.56           N
ANISOU  432  N   VAL A  52     3087   3000   4764   -150   -160   -107       N
ATOM    433  CA  VAL A  52     -65.775  36.549  -4.168  1.00 28.65           C
ANISOU  433  CA  VAL A  52     3029   3010   4849    -77   -232   -101       C
ATOM    434  C   VAL A  52     -64.298  36.228  -4.376  1.00 29.74           C
ANISOU  434  C   VAL A  52     3209   3101   4988    -24   -283    -19       C
ATOM    435  O   VAL A  52     -63.855  35.969  -5.502  1.00 32.36           O
ANISOU  435  O   VAL A  52     3528   3405   5363      4   -289     -3       O
ATOM    436  CB  VAL A  52     -66.014  38.057  -3.963  1.00 25.95           C
ANISOU  436  CB  VAL A  52     2618   2692   4551    -41   -251   -152       C
ATOM    437  CG1 VAL A  52     -65.603  38.486  -2.560  1.00 23.38           C
ANISOU  437  CG1 VAL A  52     2346   2378   4160    -73   -238   -179       C
ATOM    438  CG2 VAL A  52     -65.274  38.866  -5.017  1.00 18.60           C
ANISOU  438  CG2 VAL A  52     1651   1732   3683     25   -314   -114       C
ATOM    439  N   ASN A  53     -63.516  36.221  -3.293  1.00 27.00           N
ANISOU  439  N   ASN A  53     2904   2767   4589    -14   -318     29       N
ATOM    440  CA  ASN A  53     -62.083  35.979  -3.422  1.00 23.61           C
ANISOU  440  CA  ASN A  53     2463   2322   4184     51   -380    110       C
ATOM    441  C   ASN A  53     -61.790  34.541  -3.823  1.00 29.69           C
ANISOU  441  C   ASN A  53     3287   3005   4989     92   -334    184       C
ATOM    442  O   ASN A  53     -60.787  34.277  -4.496  1.00 32.13           O
ANISOU  442  O   ASN A  53     3556   3277   5375    163   -341    220       O
ATOM    443  CB  ASN A  53     -61.373  36.319  -2.113  1.00 23.32           C
ANISOU  443  CB  ASN A  53     2435   2363   4063     40   -458    148       C
ATOM    444  CG  ASN A  53     -61.772  35.398  -0.980  1.00 25.64           C
ANISOU  444  CG  ASN A  53     2835   2667   4240      9   -442    218       C
ATOM    445  OD1 ASN A  53     -62.900  35.453  -0.487  1.00 27.53           O
ANISOU  445  OD1 ASN A  53     3129   2917   4415    -71   -366    156       O
ATOM    446  ND2 ASN A  53     -60.846  34.548  -0.555  1.00 28.52           N
ANISOU  446  ND2 ASN A  53     3226   3028   4583     76   -505    360       N
ATOM    447  N   VAL A  54     -62.646  33.604  -3.421  1.00 29.38           N
ANISOU  447  N   VAL A  54     3339   2916   4910     43   -259    195       N
ATOM    448  CA  VAL A  54     -62.458  32.212  -3.810  1.00 27.65           C
ANISOU  448  CA  VAL A  54     3197   2565   4745     70   -178    250       C
ATOM    449  C   VAL A  54     -62.745  32.034  -5.294  1.00 29.52           C
ANISOU  449  C   VAL A  54     3406   2760   5049     39   -110    149       C
ATOM    450  O   VAL A  54     -61.944  31.448  -6.033  1.00 28.78           O
ANISOU  450  O   VAL A  54     3320   2580   5034     98    -65    162       O
ATOM    451  CB  VAL A  54     -63.344  31.296  -2.949  1.00 26.05           C
ANISOU  451  CB  VAL A  54     3119   2301   4476     -8    -93    285       C
ATOM    452  CG1 VAL A  54     -63.216  29.861  -3.409  1.00 23.34           C
ANISOU  452  CG1 VAL A  54     2880   1773   4214      7     25    328       C
ATOM    453  CG2 VAL A  54     -62.969  31.433  -1.483  1.00 23.65           C
ANISOU  453  CG2 VAL A  54     2868   2060   4058     13   -166    404       C
ATOM    454  N   ALA A  55     -63.893  32.539  -5.753  1.00 27.04           N
ANISOU  454  N   ALA A  55     3053   2523   4701    -56   -101     44       N
ATOM    455  CA  ALA A  55     -64.243  32.423  -7.166  1.00 25.02           C
ANISOU  455  CA  ALA A  55     2769   2278   4459   -108    -67    -48       C
ATOM    456  C   ALA A  55     -63.236  33.153  -8.044  1.00 24.28           C
ANISOU  456  C   ALA A  55     2620   2213   4394    -36   -116    -34       C
ATOM    457  O   ALA A  55     -62.907  32.690  -9.142  1.00 22.80           O
ANISOU  457  O   ALA A  55     2454   1991   4216    -56    -56    -80       O
ATOM    458  CB  ALA A  55     -65.653  32.963  -7.403  1.00 23.53           C
ANISOU  458  CB  ALA A  55     2506   2208   4226   -201    -90   -132       C
ATOM    459  N   PHE A  56     -62.739  34.298  -7.572  1.00 27.03           N
ANISOU  459  N   PHE A  56     2905   2618   4748     25   -203     12       N
ATOM    460  CA  PHE A  56     -61.724  35.035  -8.316  1.00 23.57           C
ANISOU  460  CA  PHE A  56     2416   2197   4343     72   -230     28       C
ATOM    461  C   PHE A  56     -60.480  34.185  -8.534  1.00 27.63           C
ANISOU  461  C   PHE A  56     2939   2632   4927    134   -170     60       C
ATOM    462  O   PHE A  56     -59.899  34.184  -9.626  1.00 28.29           O
ANISOU  462  O   PHE A  56     3009   2705   5033    133   -113     28       O
ATOM    463  CB  PHE A  56     -61.378  36.322  -7.567  1.00 24.83           C
ANISOU  463  CB  PHE A  56     2518   2405   4509    100   -311     56       C
ATOM    464  CG  PHE A  56     -60.200  37.060  -8.131  1.00 26.63           C
ANISOU  464  CG  PHE A  56     2694   2639   4784    125   -322     74       C
ATOM    465  CD1 PHE A  56     -60.238  37.572  -9.416  1.00 26.62           C
ANISOU  465  CD1 PHE A  56     2694   2646   4774    100   -294     62       C
ATOM    466  CD2 PHE A  56     -59.065  37.265  -7.366  1.00 29.28           C
ANISOU  466  CD2 PHE A  56     2972   2990   5161    157   -362    106       C
ATOM    467  CE1 PHE A  56     -59.158  38.260  -9.935  1.00 20.61           C
ANISOU  467  CE1 PHE A  56     1895   1883   4052    100   -274     78       C
ATOM    468  CE2 PHE A  56     -57.983  37.955  -7.877  1.00 24.77           C
ANISOU  468  CE2 PHE A  56     2331   2434   4646    153   -356    106       C
ATOM    469  CZ  PHE A  56     -58.029  38.453  -9.164  1.00 21.07           C
ANISOU  469  CZ  PHE A  56     1880   1948   4177    121   -296     90       C
ATOM    470  N   GLU A  57     -60.066  33.444  -7.506  1.00 24.89           N
ANISOU  470  N   GLU A  57     2613   2229   4616    195   -174    130       N
ATOM    471  CA  GLU A  57     -58.881  32.604  -7.625  1.00 25.23           C
ANISOU  471  CA  GLU A  57     2637   2185   4764    297   -120    184       C
ATOM    472  C   GLU A  57     -59.114  31.454  -8.597  1.00 27.52           C
ANISOU  472  C   GLU A  57     3013   2347   5098    273     37    114       C
ATOM    473  O   GLU A  57     -58.240  31.136  -9.412  1.00 29.36           O
ANISOU  473  O   GLU A  57     3214   2524   5417    321    129     82       O
ATOM    474  CB  GLU A  57     -58.481  32.080  -6.247  1.00 32.31           C
ANISOU  474  CB  GLU A  57     3542   3061   5673    383   -185    315       C
ATOM    475  CG  GLU A  57     -57.262  31.180  -6.242  1.00 41.64           C
ANISOU  475  CG  GLU A  57     4676   4150   6995    534   -148    409       C
ATOM    476  CD  GLU A  57     -56.836  30.795  -4.839  1.00 51.82           C
ANISOU  476  CD  GLU A  57     5962   5461   8268    631   -261    582       C
ATOM    477  OE1 GLU A  57     -57.168  31.538  -3.892  1.00 56.95           O
ANISOU  477  OE1 GLU A  57     6612   6246   8780    564   -386    604       O
ATOM    478  OE2 GLU A  57     -56.174  29.747  -4.683  1.00 56.91           O
ANISOU  478  OE2 GLU A  57     6608   5983   9031    776   -220    700       O
ATOM    479  N   LEU A  58     -60.291  30.828  -8.533  1.00 24.91           N
ANISOU  479  N   LEU A  58     2786   1968   4710    177     89     66       N
ATOM    480  CA  LEU A  58     -60.581  29.705  -9.418  1.00 24.89           C
ANISOU  480  CA  LEU A  58     2881   1837   4739    112    252    -35       C
ATOM    481  C   LEU A  58     -60.658  30.150 -10.873  1.00 23.61           C
ANISOU  481  C   LEU A  58     2698   1760   4511     18    288   -165       C
ATOM    482  O   LEU A  58     -60.141  29.468 -11.766  1.00 24.40           O
ANISOU  482  O   LEU A  58     2843   1769   4660      8    434   -249       O
ATOM    483  CB  LEU A  58     -61.883  29.028  -8.992  1.00 23.23           C
ANISOU  483  CB  LEU A  58     2772   1582   4474    -12    297    -74       C
ATOM    484  CG  LEU A  58     -61.883  28.440  -7.581  1.00 28.12           C
ANISOU  484  CG  LEU A  58     3460   2101   5125     53    293     66       C
ATOM    485  CD1 LEU A  58     -63.266  27.936  -7.202  1.00 31.38           C
ANISOU  485  CD1 LEU A  58     3960   2493   5470   -109    355      9       C
ATOM    486  CD2 LEU A  58     -60.858  27.325  -7.473  1.00 29.14           C
ANISOU  486  CD2 LEU A  58     3656   2013   5404    193    402    156       C
ATOM    487  N   TRP A  59     -61.299  31.292 -11.130  1.00 23.68           N
ANISOU  487  N   TRP A  59     2648   1940   4408    -47    168   -177       N
ATOM    488  CA  TRP A  59     -61.381  31.796 -12.496  1.00 24.08           C
ANISOU  488  CA  TRP A  59     2692   2094   4363   -131    176   -256       C
ATOM    489  C   TRP A  59     -60.002  32.144 -13.038  1.00 30.96           C
ANISOU  489  C   TRP A  59     3524   2947   5292    -56    231   -236       C
ATOM    490  O   TRP A  59     -59.705  31.889 -14.210  1.00 33.28           O
ANISOU  490  O   TRP A  59     3862   3246   5537   -124    342   -327       O
ATOM    491  CB  TRP A  59     -62.299  33.013 -12.555  1.00 24.62           C
ANISOU  491  CB  TRP A  59     2697   2327   4329   -170     25   -223       C
ATOM    492  CG  TRP A  59     -62.241  33.729 -13.866  1.00 25.73           C
ANISOU  492  CG  TRP A  59     2836   2582   4359   -226      2   -239       C
ATOM    493  CD1 TRP A  59     -62.831  33.349 -15.037  1.00 26.62           C
ANISOU  493  CD1 TRP A  59     2998   2784   4331   -362     28   -332       C
ATOM    494  CD2 TRP A  59     -61.554  34.953 -14.140  1.00 23.38           C
ANISOU  494  CD2 TRP A  59     2498   2327   4060   -168    -49   -152       C
ATOM    495  NE1 TRP A  59     -62.552  34.263 -16.025  1.00 24.25           N
ANISOU  495  NE1 TRP A  59     2700   2590   3922   -379    -14   -284       N
ATOM    496  CE2 TRP A  59     -61.770  35.258 -15.499  1.00 25.55           C
ANISOU  496  CE2 TRP A  59     2816   2709   4183   -260    -49   -170       C
ATOM    497  CE3 TRP A  59     -60.777  35.821 -13.369  1.00 24.08           C
ANISOU  497  CE3 TRP A  59     2525   2376   4247    -71    -90    -66       C
ATOM    498  CZ2 TRP A  59     -61.237  36.393 -16.102  1.00 35.18           C
ANISOU  498  CZ2 TRP A  59     4036   3972   5358   -244    -74    -82       C
ATOM    499  CZ3 TRP A  59     -60.250  36.947 -13.968  1.00 32.27           C
ANISOU  499  CZ3 TRP A  59     3551   3449   5260    -70   -106     -8       C
ATOM    500  CH2 TRP A  59     -60.482  37.224 -15.321  1.00 36.28           C
ANISOU  500  CH2 TRP A  59     4119   4039   5627   -150    -91     -4       C
ATOM    501  N   ALA A  60     -59.145  32.730 -12.199  1.00 29.04           N
ANISOU  501  N   ALA A  60     3193   2699   5143     64    164   -132       N
ATOM    502  CA  ALA A  60     -57.788  33.036 -12.635  1.00 25.76           C
ANISOU  502  CA  ALA A  60     2703   2277   4808    125    226   -121       C
ATOM    503  C   ALA A  60     -57.013  31.770 -12.971  1.00 27.17           C
ANISOU  503  C   ALA A  60     2899   2316   5110    185    403   -176       C
ATOM    504  O   ALA A  60     -56.175  31.778 -13.880  1.00 27.27           O
ANISOU  504  O   ALA A  60     2882   2324   5157    180    531   -239       O
ATOM    505  CB  ALA A  60     -57.059  33.838 -11.558  1.00 26.48           C
ANISOU  505  CB  ALA A  60     2674   2411   4976    216    106    -16       C
ATOM    506  N   LYS A  61     -57.283  30.677 -12.259  1.00 31.83           N
ANISOU  506  N   LYS A  61     3177   3435   5481   -794     73   -317       N
ATOM    507  CA  LYS A  61     -56.614  29.406 -12.487  1.00 32.74           C
ANISOU  507  CA  LYS A  61     3110   3555   5776   -704    -34   -377       C
ATOM    508  C   LYS A  61     -57.392  28.486 -13.422  1.00 30.06           C
ANISOU  508  C   LYS A  61     2774   3157   5488   -611     -3   -360       C
ATOM    509  O   LYS A  61     -57.124  27.280 -13.451  1.00 30.50           O
ANISOU  509  O   LYS A  61     2721   3185   5684   -516   -111   -377       O
ATOM    510  CB  LYS A  61     -56.359  28.700 -11.155  1.00 28.23           C
ANISOU  510  CB  LYS A  61     2507   2966   5253   -647   -240   -307       C
ATOM    511  CG  LYS A  61     -55.486  29.485 -10.192  1.00 29.21           C
ANISOU  511  CG  LYS A  61     2608   3154   5336   -731   -304   -338       C
ATOM    512  CD  LYS A  61     -55.299  28.736  -8.884  1.00 30.07           C
ANISOU  512  CD  LYS A  61     2716   3237   5473   -662   -526   -258       C
ATOM    513  CE  LYS A  61     -54.358  29.481  -7.952  1.00 31.28           C
ANISOU  513  CE  LYS A  61     2833   3462   5589   -743   -611   -306       C
ATOM    514  NZ  LYS A  61     -54.128  28.735  -6.686  1.00 32.36           N
ANISOU  514  NZ  LYS A  61     2986   3572   5739   -667   -848   -228       N
ATOM    515  N   ARG A  62     -58.346  29.025 -14.179  1.00 25.73           N
ANISOU  515  N   ARG A  62     2356   2587   4833   -631    130   -332       N
ATOM    516  CA  ARG A  62     -59.120  28.213 -15.106  1.00 27.04           C
ANISOU  516  CA  ARG A  62     2528   2705   5039   -552    155   -327       C
ATOM    517  C   ARG A  62     -58.217  27.618 -16.183  1.00 28.05           C
ANISOU  517  C   ARG A  62     2505   2857   5296   -527    192   -468       C
ATOM    518  O   ARG A  62     -57.124  28.116 -16.466  1.00 31.70           O
ANISOU  518  O   ARG A  62     2877   3382   5786   -593    255   -580       O
ATOM    519  CB  ARG A  62     -60.221  29.048 -15.758  1.00 28.86           C
ANISOU  519  CB  ARG A  62     2922   2920   5122   -576    280   -288       C
ATOM    520  CG  ARG A  62     -59.701  30.061 -16.765  1.00 27.48           C
ANISOU  520  CG  ARG A  62     2785   2782   4874   -654    435   -384       C
ATOM    521  CD  ARG A  62     -60.747  31.110 -17.099  1.00 24.50           C
ANISOU  521  CD  ARG A  62     2606   2378   4326   -673    530   -325       C
ATOM    522  NE  ARG A  62     -60.214  32.140 -17.985  1.00 28.20           N
ANISOU  522  NE  ARG A  62     3150   2861   4702   -760    678   -405       N
ATOM    523  CZ  ARG A  62     -59.492  33.178 -17.575  1.00 30.97           C
ANISOU  523  CZ  ARG A  62     3543   3234   4989   -871    740   -432       C
ATOM    524  NH1 ARG A  62     -59.208  33.327 -16.288  1.00 30.90           N
ANISOU  524  NH1 ARG A  62     3500   3244   4998   -900    655   -390       N
ATOM    525  NH2 ARG A  62     -59.050  34.067 -18.453  1.00 35.06           N
ANISOU  525  NH2 ARG A  62     4150   3751   5419   -962    888   -504       N
ATOM    526  N   ASN A  63     -58.690  26.532 -16.788  1.00 31.37           N
ANISOU  526  N   ASN A  63     2895   3227   5796   -439    161   -473       N
ATOM    527  CA  ASN A  63     -57.950  25.897 -17.868  1.00 30.49           C
ANISOU  527  CA  ASN A  63     2653   3130   5802   -405    206   -612       C
ATOM    528  C   ASN A  63     -58.049  26.745 -19.131  1.00 29.41           C
ANISOU  528  C   ASN A  63     2593   3025   5556   -475    390   -686       C
ATOM    529  O   ASN A  63     -59.150  27.068 -19.589  1.00 31.71           O
ANISOU  529  O   ASN A  63     3034   3284   5730   -472    441   -623       O
ATOM    530  CB  ASN A  63     -58.492  24.491 -18.124  1.00 30.42           C
ANISOU  530  CB  ASN A  63     2616   3043   5900   -294    118   -594       C
ATOM    531  CG  ASN A  63     -57.503  23.610 -18.859  1.00 35.74           C
ANISOU  531  CG  ASN A  63     3122   3722   6736   -234    116   -741       C
ATOM    532  OD1 ASN A  63     -57.238  23.808 -20.045  1.00 38.48           O
ANISOU  532  OD1 ASN A  63     3448   4101   7070   -262    250   -855       O
ATOM    533  ND2 ASN A  63     -56.957  22.625 -18.157  1.00 37.48           N
ANISOU  533  ND2 ASN A  63     3233   3904   7105   -147    -37   -741       N
ATOM    534  N   ILE A  64     -56.900  27.109 -19.692  1.00 27.53           N
ANISOU  534  N   ILE A  64     2257   2850   5355   -539    490   -823       N
ATOM    535  CA  ILE A  64     -56.846  27.968 -20.868  1.00 27.64           C
ANISOU  535  CA  ILE A  64     2365   2888   5250   -626    679   -897       C
ATOM    536  C   ILE A  64     -56.477  27.175 -22.121  1.00 35.88           C
ANISOU  536  C   ILE A  64     3326   3933   6374   -588    752  -1029       C
ATOM    537  O   ILE A  64     -56.081  27.756 -23.130  1.00 35.15           O
ANISOU  537  O   ILE A  64     3278   3871   6206   -672    919  -1126       O
ATOM    538  CB  ILE A  64     -55.888  29.150 -20.653  1.00 30.80           C
ANISOU  538  CB  ILE A  64     2753   3353   5595   -767    783   -959       C
ATOM    539  CG1 ILE A  64     -54.461  28.647 -20.433  1.00 33.30           C
ANISOU  539  CG1 ILE A  64     2817   3741   6095   -776    754  -1100       C
ATOM    540  CG2 ILE A  64     -56.350  30.002 -19.477  1.00 29.55           C
ANISOU  540  CG2 ILE A  64     2710   3183   5334   -807    721   -831       C
ATOM    541  CD1 ILE A  64     -53.422  29.743 -20.429  1.00 34.70           C
ANISOU  541  CD1 ILE A  64     2952   3994   6237   -937    883  -1200       C
ATOM    542  N   LYS A  65     -56.595  25.857 -22.066  1.00 35.07           N
ANISOU  542  N   LYS A  65     3119   3791   6415   -470    634  -1037       N
ATOM    543  CA  LYS A  65     -56.391  24.980 -23.205  1.00 31.64           C
ANISOU  543  CA  LYS A  65     2620   3342   6059   -416    687  -1157       C
ATOM    544  C   LYS A  65     -57.734  24.467 -23.711  1.00 31.38           C
ANISOU  544  C   LYS A  65     2726   3235   5961   -350    649  -1080       C
ATOM    545  O   LYS A  65     -58.744  24.552 -23.004  1.00 32.06           O
ANISOU  545  O   LYS A  65     2909   3281   5990   -326    556   -937       O
ATOM    546  CB  LYS A  65     -55.489  23.801 -22.813  1.00 35.96           C
ANISOU  546  CB  LYS A  65     2944   3887   6832   -320    576  -1242       C
ATOM    547  CG  LYS A  65     -54.052  24.200 -22.520  1.00 44.99           C
ANISOU  547  CG  LYS A  65     3904   5122   8068   -377    616  -1365       C
ATOM    548  CD  LYS A  65     -53.325  23.131 -21.720  1.00 57.59           C
ANISOU  548  CD  LYS A  65     5297   6705   9878   -255    437  -1402       C
ATOM    549  CE  LYS A  65     -53.916  22.991 -20.325  1.00 62.78           C
ANISOU  549  CE  LYS A  65     6025   7308  10521   -206    242  -1222       C
ATOM    550  NZ  LYS A  65     -53.152  22.027 -19.484  1.00 64.93           N
ANISOU  550  NZ  LYS A  65     6129   7559  10984    -84     50  -1248       N
ATOM    551  N   PRO A  66     -57.794  23.956 -24.943  1.00 32.77           N
ANISOU  551  N   PRO A  66     2914   3397   6140   -326    725  -1180       N
ATOM    552  CA  PRO A  66     -59.051  23.363 -25.427  1.00 28.08           C
ANISOU  552  CA  PRO A  66     2431   2736   5501   -261    670  -1124       C
ATOM    553  C   PRO A  66     -59.492  22.224 -24.522  1.00 28.41           C
ANISOU  553  C   PRO A  66     2403   2708   5685   -167    492  -1045       C
ATOM    554  O   PRO A  66     -58.748  21.270 -24.284  1.00 32.82           O
ANISOU  554  O   PRO A  66     2816   3241   6414   -104    427  -1110       O
ATOM    555  CB  PRO A  66     -58.690  22.870 -26.833  1.00 29.11           C
ANISOU  555  CB  PRO A  66     2550   2868   5642   -253    777  -1279       C
ATOM    556  CG  PRO A  66     -57.558  23.733 -27.251  1.00 30.34           C
ANISOU  556  CG  PRO A  66     2674   3101   5753   -353    944  -1387       C
ATOM    557  CD  PRO A  66     -56.770  24.010 -26.002  1.00 31.61           C
ANISOU  557  CD  PRO A  66     2696   3300   6013   -374    883  -1357       C
ATOM    558  N   VAL A  67     -60.710  22.339 -24.003  1.00 30.32           N
ANISOU  558  N   VAL A  67     2752   2914   5853   -159    417   -907       N
ATOM    559  CA  VAL A  67     -61.243  21.354 -23.065  1.00 31.36           C
ANISOU  559  CA  VAL A  67     2851   2972   6091    -97    265   -815       C
ATOM    560  C   VAL A  67     -62.604  20.895 -23.566  1.00 30.67           C
ANISOU  560  C   VAL A  67     2857   2836   5959    -76    237   -777       C
ATOM    561  O   VAL A  67     -63.260  21.591 -24.357  1.00 31.24           O
ANISOU  561  O   VAL A  67     3033   2943   5893   -104    310   -786       O
ATOM    562  CB  VAL A  67     -61.340  21.926 -21.631  1.00 30.71           C
ANISOU  562  CB  VAL A  67     2789   2901   5977   -127    198   -682       C
ATOM    563  CG1 VAL A  67     -59.954  22.158 -21.058  1.00 31.46           C
ANISOU  563  CG1 VAL A  67     2767   3040   6147   -139    188   -731       C
ATOM    564  CG2 VAL A  67     -62.141  23.214 -21.630  1.00 24.84           C
ANISOU  564  CG2 VAL A  67     2184   2203   5050   -191    270   -609       C
ATOM    565  N   PRO A  68     -63.050  19.711 -23.141  1.00 32.75           N
ANISOU  565  N   PRO A  68     3091   3015   6338    -27    127   -740       N
ATOM    566  CA  PRO A  68     -64.404  19.270 -23.490  1.00 32.19           C
ANISOU  566  CA  PRO A  68     3092   2904   6235    -25     95   -706       C
ATOM    567  C   PRO A  68     -65.451  20.243 -22.973  1.00 33.60           C
ANISOU  567  C   PRO A  68     3360   3127   6279    -70    104   -592       C
ATOM    568  O   PRO A  68     -65.271  20.898 -21.944  1.00 33.07           O
ANISOU  568  O   PRO A  68     3304   3086   6176    -98     96   -504       O
ATOM    569  CB  PRO A  68     -64.522  17.907 -22.800  1.00 27.98           C
ANISOU  569  CB  PRO A  68     2516   2261   5855     14    -21   -668       C
ATOM    570  CG  PRO A  68     -63.121  17.431 -22.673  1.00 28.09           C
ANISOU  570  CG  PRO A  68     2428   2252   5994     67    -43   -741       C
ATOM    571  CD  PRO A  68     -62.292  18.658 -22.441  1.00 27.72           C
ANISOU  571  CD  PRO A  68     2354   2307   5870     31     27   -746       C
ATOM    572  N   GLU A  69     -66.555  20.338 -23.707  1.00 31.29           N
ANISOU  572  N   GLU A  69     3131   2847   5912    -71    115   -605       N
ATOM    573  CA  GLU A  69     -67.664  21.166 -23.262  1.00 28.67           C
ANISOU  573  CA  GLU A  69     2867   2556   5470    -94    114   -513       C
ATOM    574  C   GLU A  69     -68.305  20.560 -22.019  1.00 28.33           C
ANISOU  574  C   GLU A  69     2798   2466   5502   -114     40   -409       C
ATOM    575  O   GLU A  69     -68.335  19.340 -21.841  1.00 28.92           O
ANISOU  575  O   GLU A  69     2828   2461   5699   -108    -22   -415       O
ATOM    576  CB  GLU A  69     -68.691  21.329 -24.381  1.00 31.19           C
ANISOU  576  CB  GLU A  69     3243   2902   5706    -74    121   -567       C
ATOM    577  CG  GLU A  69     -68.225  22.264 -25.489  1.00 35.31           C
ANISOU  577  CG  GLU A  69     3849   3474   6094    -66    205   -639       C
ATOM    578  CD  GLU A  69     -69.249  22.432 -26.593  1.00 41.81           C
ANISOU  578  CD  GLU A  69     4748   4320   6818    -34    188   -688       C
ATOM    579  OE1 GLU A  69     -69.514  21.450 -27.318  1.00 48.02           O
ANISOU  579  OE1 GLU A  69     5504   5076   7666    -17    146   -767       O
ATOM    580  OE2 GLU A  69     -69.793  23.548 -26.734  1.00 45.40           O
ANISOU  580  OE2 GLU A  69     5300   4818   7132    -19    205   -651       O
ATOM    581  N   VAL A  70     -68.814  21.437 -21.151  1.00 31.46           N
ANISOU  581  N   VAL A  70     3237   2903   5814   -141     55   -315       N
ATOM    582  CA  VAL A  70     -69.283  21.013 -19.833  1.00 31.45           C
ANISOU  582  CA  VAL A  70     3230   2862   5859   -176      8   -210       C
ATOM    583  C   VAL A  70     -70.375  19.959 -19.959  1.00 32.01           C
ANISOU  583  C   VAL A  70     3274   2882   6005   -192    -34   -214       C
ATOM    584  O   VAL A  70     -70.433  19.008 -19.169  1.00 39.74           O
ANISOU  584  O   VAL A  70     4246   3782   7073   -223    -82   -160       O
ATOM    585  CB  VAL A  70     -69.758  22.232 -19.021  1.00 31.65           C
ANISOU  585  CB  VAL A  70     3312   2948   5763   -203     51   -127       C
ATOM    586  CG1 VAL A  70     -70.308  21.798 -17.673  1.00 35.27           C
ANISOU  586  CG1 VAL A  70     3779   3369   6252   -251     20    -24       C
ATOM    587  CG2 VAL A  70     -68.616  23.219 -18.837  1.00 26.71           C
ANISOU  587  CG2 VAL A  70     2717   2360   5071   -206     92   -127       C
ATOM    588  N   LYS A  71     -71.251  20.102 -20.958  1.00 27.98           N
ANISOU  588  N   LYS A  71     2759   2413   5457   -176    -22   -282       N
ATOM    589  CA  LYS A  71     -72.309  19.117 -21.160  1.00 27.96           C
ANISOU  589  CA  LYS A  71     2718   2374   5532   -204    -62   -308       C
ATOM    590  C   LYS A  71     -71.731  17.723 -21.374  1.00 31.93           C
ANISOU  590  C   LYS A  71     3196   2768   6169   -206   -111   -350       C
ATOM    591  O   LYS A  71     -72.292  16.731 -20.895  1.00 32.62           O
ANISOU  591  O   LYS A  71     3272   2778   6344   -258   -146   -322       O
ATOM    592  CB  LYS A  71     -73.191  19.526 -22.342  1.00 27.81           C
ANISOU  592  CB  LYS A  71     2694   2425   5448   -171    -61   -395       C
ATOM    593  CG  LYS A  71     -72.444  19.696 -23.655  1.00 26.78           C
ANISOU  593  CG  LYS A  71     2596   2307   5273   -116    -50   -495       C
ATOM    594  CD  LYS A  71     -73.383  20.088 -24.782  1.00 26.18           C
ANISOU  594  CD  LYS A  71     2540   2294   5113    -78    -71   -572       C
ATOM    595  CE  LYS A  71     -72.622  20.308 -26.080  1.00 27.54           C
ANISOU  595  CE  LYS A  71     2777   2474   5213    -34    -46   -666       C
ATOM    596  NZ  LYS A  71     -73.512  20.788 -27.173  1.00 30.94           N
ANISOU  596  NZ  LYS A  71     3260   2964   5533     13    -82   -733       N
ATOM    597  N   ILE A  72     -70.600  17.631 -22.076  1.00 30.45           N
ANISOU  597  N   ILE A  72     3004   2565   6000   -154   -106   -421       N
ATOM    598  CA  ILE A  72     -69.946  16.340 -22.268  1.00 31.69           C
ANISOU  598  CA  ILE A  72     3136   2612   6292   -135   -153   -471       C
ATOM    599  C   ILE A  72     -69.475  15.785 -20.930  1.00 32.40           C
ANISOU  599  C   ILE A  72     3237   2615   6458   -151   -202   -368       C
ATOM    600  O   ILE A  72     -69.717  14.618 -20.600  1.00 34.83           O
ANISOU  600  O   ILE A  72     3559   2807   6868   -172   -257   -349       O
ATOM    601  CB  ILE A  72     -68.779  16.473 -23.263  1.00 30.32           C
ANISOU  601  CB  ILE A  72     2944   2457   6119    -73   -120   -582       C
ATOM    602  CG1 ILE A  72     -69.295  16.891 -24.640  1.00 27.72           C
ANISOU  602  CG1 ILE A  72     2638   2195   5698    -63    -79   -684       C
ATOM    603  CG2 ILE A  72     -68.007  15.169 -23.353  1.00 27.03           C
ANISOU  603  CG2 ILE A  72     2492   1923   5854    -34   -170   -639       C
ATOM    604  CD1 ILE A  72     -70.127  15.832 -25.322  1.00 27.64           C
ANISOU  604  CD1 ILE A  72     2621   2128   5753    -74   -127   -756       C
ATOM    605  N   LEU A  73     -68.800  16.620 -20.137  1.00 33.23           N
ANISOU  605  N   LEU A  73     3352   2766   6506   -143   -189   -298       N
ATOM    606  CA  LEU A  73     -68.308  16.173 -18.838  1.00 29.28           C
ANISOU  606  CA  LEU A  73     2879   2189   6058   -151   -253   -196       C
ATOM    607  C   LEU A  73     -69.458  15.799 -17.913  1.00 27.05           C
ANISOU  607  C   LEU A  73     2656   1858   5763   -232   -263    -91       C
ATOM    608  O   LEU A  73     -69.351  14.846 -17.133  1.00 33.68           O
ANISOU  608  O   LEU A  73     3545   2578   6673   -248   -327    -25       O
ATOM    609  CB  LEU A  73     -67.441  17.261 -18.205  1.00 30.41           C
ANISOU  609  CB  LEU A  73     3021   2409   6126   -138   -237   -153       C
ATOM    610  CG  LEU A  73     -66.247  17.740 -19.035  1.00 31.76           C
ANISOU  610  CG  LEU A  73     3125   2638   6303    -83   -204   -262       C
ATOM    611  CD1 LEU A  73     -65.477  18.820 -18.295  1.00 32.41           C
ANISOU  611  CD1 LEU A  73     3207   2794   6313    -96   -188   -218       C
ATOM    612  CD2 LEU A  73     -65.335  16.577 -19.388  1.00 34.46           C
ANISOU  612  CD2 LEU A  73     3407   2891   6796    -12   -268   -341       C
ATOM    613  N   ASN A  74     -70.567  16.535 -17.986  1.00 29.06           N
ANISOU  613  N   ASN A  74     2912   2201   5928   -283   -198    -78       N
ATOM    614  CA  ASN A  74     -71.726  16.208 -17.163  1.00 28.69           C
ANISOU  614  CA  ASN A  74     2901   2124   5875   -373   -184      1       C
ATOM    615  C   ASN A  74     -72.332  14.875 -17.578  1.00 27.01           C
ANISOU  615  C   ASN A  74     2682   1809   5773   -414   -214    -43       C
ATOM    616  O   ASN A  74     -72.656  14.037 -16.728  1.00 29.05           O
ANISOU  616  O   ASN A  74     3001   1960   6075   -485   -232     32       O
ATOM    617  CB  ASN A  74     -72.768  17.322 -17.253  1.00 32.07           C
ANISOU  617  CB  ASN A  74     3305   2681   6198   -399   -109     -3       C
ATOM    618  CG  ASN A  74     -72.257  18.641 -16.715  1.00 36.24           C
ANISOU  618  CG  ASN A  74     3865   3293   6612   -373    -73     48       C
ATOM    619  OD1 ASN A  74     -71.292  18.681 -15.953  1.00 40.72           O
ANISOU  619  OD1 ASN A  74     4474   3825   7173   -365   -103    109       O
ATOM    620  ND2 ASN A  74     -72.907  19.731 -17.106  1.00 39.66           N
ANISOU  620  ND2 ASN A  74     4283   3833   6953   -356    -16     19       N
ATOM    621  N   ASN A  75     -72.490  14.661 -18.886  1.00 29.85           N
ANISOU  621  N   ASN A  75     2984   2190   6168   -378   -216   -166       N
ATOM    622  CA  ASN A  75     -73.090  13.422 -19.367  1.00 28.09           C
ANISOU  622  CA  ASN A  75     2754   1870   6048   -425   -244   -225       C
ATOM    623  C   ASN A  75     -72.262  12.207 -18.980  1.00 31.44           C
ANISOU  623  C   ASN A  75     3242   2123   6582   -408   -311   -197       C
ATOM    624  O   ASN A  75     -72.808  11.110 -18.815  1.00 40.15           O
ANISOU  624  O   ASN A  75     4386   3105   7765   -479   -332   -191       O
ATOM    625  CB  ASN A  75     -73.264  13.479 -20.882  1.00 30.24           C
ANISOU  625  CB  ASN A  75     2968   2201   6322   -378   -245   -370       C
ATOM    626  CG  ASN A  75     -74.224  14.564 -21.316  1.00 27.34           C
ANISOU  626  CG  ASN A  75     2553   1985   5851   -384   -204   -400       C
ATOM    627  OD1 ASN A  75     -75.065  15.013 -20.539  1.00 29.24           O
ANISOU  627  OD1 ASN A  75     2782   2277   6052   -442   -170   -333       O
ATOM    628  ND2 ASN A  75     -74.102  14.995 -22.564  1.00 27.09           N
ANISOU  628  ND2 ASN A  75     2501   2022   5770   -317   -206   -505       N
ATOM    629  N   LEU A  76     -70.952  12.377 -18.832  1.00 32.01           N
ANISOU  629  N   LEU A  76     3321   2178   6664   -314   -349   -186       N
ATOM    630  CA  LEU A  76     -70.076  11.305 -18.384  1.00 32.27           C
ANISOU  630  CA  LEU A  76     3410   2049   6800   -268   -432   -159       C
ATOM    631  C   LEU A  76     -70.013  11.191 -16.868  1.00 35.57           C
ANISOU  631  C   LEU A  76     3928   2395   7190   -310   -470     -2       C
ATOM    632  O   LEU A  76     -69.319  10.308 -16.356  1.00 38.17           O
ANISOU  632  O   LEU A  76     4330   2585   7589   -264   -557     40       O
ATOM    633  CB  LEU A  76     -68.669  11.507 -18.950  1.00 35.75           C
ANISOU  633  CB  LEU A  76     3790   2514   7280   -140   -462   -240       C
ATOM    634  CG  LEU A  76     -68.569  11.368 -20.469  1.00 38.64           C
ANISOU  634  CG  LEU A  76     4086   2915   7681    -95   -427   -403       C
ATOM    635  CD1 LEU A  76     -67.203  11.800 -20.970  1.00 40.53           C
ANISOU  635  CD1 LEU A  76     4253   3210   7935     10   -420   -487       C
ATOM    636  CD2 LEU A  76     -68.862   9.935 -20.882  1.00 41.06           C
ANISOU  636  CD2 LEU A  76     4431   3063   8108   -101   -473   -461       C
ATOM    637  N   GLY A  77     -70.717  12.057 -16.143  1.00 37.06           N
ANISOU  637  N   GLY A  77     4134   2679   7267   -390   -408     81       N
ATOM    638  CA  GLY A  77     -70.738  11.980 -14.697  1.00 37.49           C
ANISOU  638  CA  GLY A  77     4304   2671   7271   -445   -430    228       C
ATOM    639  C   GLY A  77     -69.491  12.481 -14.011  1.00 34.66           C
ANISOU  639  C   GLY A  77     3967   2327   6876   -358   -500    284       C
ATOM    640  O   GLY A  77     -69.205  12.053 -12.889  1.00 36.11           O
ANISOU  640  O   GLY A  77     4268   2408   7042   -372   -568    397       O
ATOM    641  N   VAL A  78     -68.736  13.375 -14.648  1.00 35.39           N
ANISOU  641  N   VAL A  78     3955   2542   6950   -277   -488    204       N
ATOM    642  CA  VAL A  78     -67.523  13.906 -14.041  1.00 35.39           C
ANISOU  642  CA  VAL A  78     3950   2573   6924   -206   -553    236       C
ATOM    643  C   VAL A  78     -67.891  14.764 -12.839  1.00 38.82           C
ANISOU  643  C   VAL A  78     4462   3067   7220   -281   -523    356       C
ATOM    644  O   VAL A  78     -68.774  15.629 -12.919  1.00 40.74           O
ANISOU  644  O   VAL A  78     4692   3417   7372   -348   -416    358       O
ATOM    645  CB  VAL A  78     -66.710  14.707 -15.068  1.00 38.20           C
ANISOU  645  CB  VAL A  78     4175   3052   7288   -132   -516    110       C
ATOM    646  CG1 VAL A  78     -65.527  15.384 -14.398  1.00 34.19           C
ANISOU  646  CG1 VAL A  78     3644   2598   6751    -84   -570    132       C
ATOM    647  CG2 VAL A  78     -66.241  13.800 -16.196  1.00 28.96           C
ANISOU  647  CG2 VAL A  78     2936   1816   6252    -54   -543    -16       C
ATOM    648  N   ASP A  79     -67.217  14.523 -11.715  1.00 38.04           N
ANISOU  648  N   ASP A  79     4452   2897   7104   -261   -623    450       N
ATOM    649  CA  ASP A  79     -67.470  15.257 -10.483  1.00 39.46           C
ANISOU  649  CA  ASP A  79     4729   3120   7143   -332   -605    565       C
ATOM    650  C   ASP A  79     -66.405  16.291 -10.157  1.00 38.11           C
ANISOU  650  C   ASP A  79     4512   3052   6915   -280   -644    552       C
ATOM    651  O   ASP A  79     -66.710  17.278  -9.483  1.00 40.11           O
ANISOU  651  O   ASP A  79     4811   3390   7038   -343   -587    605       O
ATOM    652  CB  ASP A  79     -67.585  14.289  -9.298  1.00 43.08           C
ANISOU  652  CB  ASP A  79     5363   3420   7584   -370   -691    697       C
ATOM    653  CG  ASP A  79     -68.659  13.240  -9.501  1.00 46.80           C
ANISOU  653  CG  ASP A  79     5900   3775   8107   -451   -641    716       C
ATOM    654  OD1 ASP A  79     -69.742  13.582 -10.023  1.00 50.23           O
ANISOU  654  OD1 ASP A  79     6274   4288   8523   -531   -510    672       O
ATOM    655  OD2 ASP A  79     -68.416  12.070  -9.137  1.00 51.85           O
ANISOU  655  OD2 ASP A  79     6653   4240   8806   -433   -739    770       O
ATOM    656  N   ILE A  80     -65.172  16.095 -10.623  1.00 32.73           N
ANISOU  656  N   ILE A  80     3734   2369   6332   -172   -735    470       N
ATOM    657  CA  ILE A  80     -64.055  16.939 -10.218  1.00 31.94           C
ANISOU  657  CA  ILE A  80     3581   2357   6196   -132   -790    451       C
ATOM    658  C   ILE A  80     -62.936  16.762 -11.232  1.00 31.30           C
ANISOU  658  C   ILE A  80     3337   2304   6252    -27   -825    307       C
ATOM    659  O   ILE A  80     -62.840  15.727 -11.895  1.00 36.76           O
ANISOU  659  O   ILE A  80     3991   2905   7070     38   -861    251       O
ATOM    660  CB  ILE A  80     -63.599  16.584  -8.780  1.00 37.70           C
ANISOU  660  CB  ILE A  80     4440   3007   6879   -121   -937    571       C
ATOM    661  CG1 ILE A  80     -62.771  17.713  -8.165  1.00 43.80           C
ANISOU  661  CG1 ILE A  80     5181   3894   7566   -124   -971    565       C
ATOM    662  CG2 ILE A  80     -62.824  15.277  -8.768  1.00 39.03           C
ANISOU  662  CG2 ILE A  80     4609   3033   7188     -4  -1102    561       C
ATOM    663  CD1 ILE A  80     -62.554  17.545  -6.674  1.00 31.75           C
ANISOU  663  CD1 ILE A  80     3814   2304   5945   -137  -1103    694       C
ATOM    664  N   ALA A  81     -62.093  17.783 -11.364  1.00 32.63           N
ANISOU  664  N   ALA A  81     3407   2597   6393    -20   -804    237       N
ATOM    665  CA  ALA A  81     -60.970  17.757 -12.287  1.00 29.64           C
ANISOU  665  CA  ALA A  81     2860   2268   6136     59   -811     86       C
ATOM    666  C   ALA A  81     -59.664  17.605 -11.518  1.00 36.71           C
ANISOU  666  C   ALA A  81     3693   3161   7094    136   -972     72       C
ATOM    667  O   ALA A  81     -59.541  18.051 -10.373  1.00 33.60           O
ANISOU  667  O   ALA A  81     3378   2783   6607    102  -1045    163       O
ATOM    668  CB  ALA A  81     -60.929  19.024 -13.145  1.00 28.43           C
ANISOU  668  CB  ALA A  81     2632   2257   5913     -2   -652     -6       C
ATOM    669  N   ALA A  82     -58.687  16.974 -12.165  1.00 39.25           N
ANISOU  669  N   ALA A  82     3869   3468   7577    244  -1030    -54       N
ATOM    670  CA  ALA A  82     -57.395  16.690 -11.548  1.00 41.45           C
ANISOU  670  CA  ALA A  82     4054   3745   7952    346  -1203    -94       C
ATOM    671  C   ALA A  82     -56.447  17.859 -11.795  1.00 42.52           C
ANISOU  671  C   ALA A  82     4027   4050   8079    306  -1139   -214       C
ATOM    672  O   ALA A  82     -55.959  18.046 -12.915  1.00 43.09           O
ANISOU  672  O   ALA A  82     3947   4194   8230    314  -1028   -367       O
ATOM    673  CB  ALA A  82     -56.813  15.389 -12.093  1.00 40.58           C
ANISOU  673  CB  ALA A  82     3856   3529   8034    495  -1299   -184       C
ATOM    674  N   ASN A  83     -56.194  18.647 -10.747  1.00 42.19           N
ANISOU  674  N   ASN A  83     4028   4069   7933    250  -1201   -149       N
ATOM    675  CA  ASN A  83     -55.166  19.690 -10.757  1.00 45.39           C
ANISOU  675  CA  ASN A  83     4283   4624   8339    206  -1175   -261       C
ATOM    676  C   ASN A  83     -55.429  20.743 -11.832  1.00 46.49           C
ANISOU  676  C   ASN A  83     4383   4869   8414     91   -937   -345       C
ATOM    677  O   ASN A  83     -54.504  21.258 -12.463  1.00 48.03           O
ANISOU  677  O   ASN A  83     4410   5167   8672     70   -865   -497       O
ATOM    678  CB  ASN A  83     -53.772  19.081 -10.920  1.00 53.48           C
ANISOU  678  CB  ASN A  83     5091   5670   9560    336  -1308   -407       C
ATOM    679  CG  ASN A  83     -53.491  17.993  -9.901  1.00 61.67           C
ANISOU  679  CG  ASN A  83     6186   6584  10662    476  -1567   -323       C
ATOM    680  OD1 ASN A  83     -53.611  16.804 -10.196  1.00 68.69           O
ANISOU  680  OD1 ASN A  83     7092   7346  11662    593  -1636   -319       O
ATOM    681  ND2 ASN A  83     -53.123  18.396  -8.689  1.00 61.43           N
ANISOU  681  ND2 ASN A  83     6207   6582  10553    462  -1715   -253       N
ATOM    682  N   THR A  84     -56.702  21.073 -12.037  1.00 44.69           N
ANISOU  682  N   THR A  84     4313   4612   8054     15   -814   -250       N
ATOM    683  CA  THR A  84     -57.085  22.130 -12.963  1.00 40.39           C
ANISOU  683  CA  THR A  84     3778   4149   7417    -86   -606   -304       C
ATOM    684  C   THR A  84     -58.500  22.571 -12.621  1.00 37.07           C
ANISOU  684  C   THR A  84     3552   3697   6836   -156   -538   -164       C
ATOM    685  O   THR A  84     -59.189  21.946 -11.811  1.00 40.41           O
ANISOU  685  O   THR A  84     4086   4036   7234   -134   -627    -40       O
ATOM    686  CB  THR A  84     -56.991  21.671 -14.423  1.00 37.35           C
ANISOU  686  CB  THR A  84     3298   3763   7129    -48   -500   -431       C
ATOM    687  OG1 THR A  84     -57.184  22.794 -15.294  1.00 37.08           O
ANISOU  687  OG1 THR A  84     3287   3811   6991   -147   -310   -489       O
ATOM    688  CG2 THR A  84     -58.050  20.625 -14.722  1.00 33.23           C
ANISOU  688  CG2 THR A  84     2868   3126   6631      8   -519   -362       C
ATOM    689  N   VAL A  85     -58.925  23.663 -13.251  1.00 33.10           N
ANISOU  689  N   VAL A  85     3094   3260   6222   -240   -374   -190       N
ATOM    690  CA  VAL A  85     -60.266  24.209 -13.075  1.00 27.66           C
ANISOU  690  CA  VAL A  85     2565   2556   5389   -294   -294    -84       C
ATOM    691  C   VAL A  85     -60.914  24.328 -14.445  1.00 26.51           C
ANISOU  691  C   VAL A  85     2428   2417   5228   -294   -160   -143       C
ATOM    692  O   VAL A  85     -60.437  25.084 -15.301  1.00 27.41           O
ANISOU  692  O   VAL A  85     2508   2594   5314   -331    -50   -239       O
ATOM    693  CB  VAL A  85     -60.249  25.572 -12.366  1.00 29.18           C
ANISOU  693  CB  VAL A  85     2841   2811   5435   -385   -244    -46       C
ATOM    694  CG1 VAL A  85     -61.629  26.209 -12.420  1.00 24.36           C
ANISOU  694  CG1 VAL A  85     2376   2193   4688   -423   -140     32       C
ATOM    695  CG2 VAL A  85     -59.803  25.411 -10.929  1.00 33.59           C
ANISOU  695  CG2 VAL A  85     3424   3357   5982   -387   -390     28       C
ATOM    696  N   ILE A  86     -61.995  23.585 -14.652  1.00 25.89           N
ANISOU  696  N   ILE A  86     2402   2273   5161   -260   -168    -89       N
ATOM    697  CA  ILE A  86     -62.817  23.725 -15.847  1.00 27.96           C
ANISOU  697  CA  ILE A  86     2693   2543   5387   -259    -62   -131       C
ATOM    698  C   ILE A  86     -63.818  24.843 -15.578  1.00 30.31           C
ANISOU  698  C   ILE A  86     3114   2875   5528   -312     16    -60       C
ATOM    699  O   ILE A  86     -64.687  24.716 -14.711  1.00 30.94           O
ANISOU  699  O   ILE A  86     3261   2926   5567   -323    -16     40       O
ATOM    700  CB  ILE A  86     -63.528  22.415 -16.201  1.00 27.81           C
ANISOU  700  CB  ILE A  86     2664   2443   5462   -205   -113   -121       C
ATOM    701  CG1 ILE A  86     -62.526  21.259 -16.242  1.00 30.27           C
ANISOU  701  CG1 ILE A  86     2869   2698   5934   -137   -211   -180       C
ATOM    702  CG2 ILE A  86     -64.250  22.549 -17.532  1.00 31.08           C
ANISOU  702  CG2 ILE A  86     3093   2874   5840   -199    -20   -188       C
ATOM    703  CD1 ILE A  86     -61.413  21.449 -17.248  1.00 25.82           C
ANISOU  703  CD1 ILE A  86     2193   2188   5429   -117   -152   -328       C
ATOM    704  N   TRP A  87     -63.693  25.943 -16.312  1.00 28.20           N
ANISOU  704  N   TRP A  87     2883   2663   5168   -343    124   -116       N
ATOM    705  CA  TRP A  87     -64.566  27.091 -16.119  1.00 30.61           C
ANISOU  705  CA  TRP A  87     3312   2994   5325   -375    196    -61       C
ATOM    706  C   TRP A  87     -65.794  26.953 -17.010  1.00 29.36           C
ANISOU  706  C   TRP A  87     3194   2824   5136   -332    232    -67       C
ATOM    707  O   TRP A  87     -65.669  26.791 -18.228  1.00 30.55           O
ANISOU  707  O   TRP A  87     3327   2978   5302   -307    269   -149       O
ATOM    708  CB  TRP A  87     -63.834  28.396 -16.422  1.00 30.37           C
ANISOU  708  CB  TRP A  87     3331   3010   5198   -433    290   -112       C
ATOM    709  CG  TRP A  87     -64.624  29.589 -16.015  1.00 27.26           C
ANISOU  709  CG  TRP A  87     3077   2625   4656   -458    348    -50       C
ATOM    710  CD1 TRP A  87     -65.357  30.405 -16.825  1.00 24.76           C
ANISOU  710  CD1 TRP A  87     2868   2308   4232   -440    429    -62       C
ATOM    711  CD2 TRP A  87     -64.790  30.088 -14.685  1.00 21.50           C
ANISOU  711  CD2 TRP A  87     2405   1897   3866   -494    322     30       C
ATOM    712  NE1 TRP A  87     -65.959  31.390 -16.082  1.00 26.04           N
ANISOU  712  NE1 TRP A  87     3142   2469   4281   -454    458      1       N
ATOM    713  CE2 TRP A  87     -65.626  31.217 -14.764  1.00 21.10           C
ANISOU  713  CE2 TRP A  87     2488   1848   3681   -494    401     56       C
ATOM    714  CE3 TRP A  87     -64.305  29.693 -13.435  1.00 21.87           C
ANISOU  714  CE3 TRP A  87     2417   1941   3953   -521    234     80       C
ATOM    715  CZ2 TRP A  87     -65.989  31.956 -13.642  1.00 26.53           C
ANISOU  715  CZ2 TRP A  87     3265   2535   4279   -524    410    121       C
ATOM    716  CZ3 TRP A  87     -64.667  30.426 -12.322  1.00 22.81           C
ANISOU  716  CZ3 TRP A  87     2635   2063   3968   -561    240    150       C
ATOM    717  CH2 TRP A  87     -65.501  31.545 -12.432  1.00 21.36           C
ANISOU  717  CH2 TRP A  87     2575   1883   3658   -564    335    167       C
ATOM    718  N   ASP A  88     -66.977  27.015 -16.401  1.00 27.42           N
ANISOU  718  N   ASP A  88     3001   2570   4847   -325    220     12       N
ATOM    719  CA  ASP A  88     -68.238  26.969 -17.136  1.00 27.21           C
ANISOU  719  CA  ASP A  88     2998   2547   4794   -281    241      1       C
ATOM    720  C   ASP A  88     -68.583  28.396 -17.539  1.00 26.67           C
ANISOU  720  C   ASP A  88     3040   2514   4581   -272    320     -9       C
ATOM    721  O   ASP A  88     -69.037  29.194 -16.717  1.00 24.20           O
ANISOU  721  O   ASP A  88     2794   2212   4188   -285    345     49       O
ATOM    722  CB  ASP A  88     -69.339  26.338 -16.290  1.00 29.56           C
ANISOU  722  CB  ASP A  88     3280   2825   5127   -285    202     73       C
ATOM    723  CG  ASP A  88     -70.598  26.040 -17.086  1.00 35.77           C
ANISOU  723  CG  ASP A  88     4045   3622   5925   -243    204     39       C
ATOM    724  OD1 ASP A  88     -70.793  26.636 -18.167  1.00 38.29           O
ANISOU  724  OD1 ASP A  88     4397   3968   6182   -198    234    -22       O
ATOM    725  OD2 ASP A  88     -71.402  25.204 -16.623  1.00 40.77           O
ANISOU  725  OD2 ASP A  88     4634   4234   6624   -260    173     71       O
ATOM    726  N   TYR A  89     -68.361  28.719 -18.814  1.00 29.36           N
ANISOU  726  N   TYR A  89     3414   2861   4879   -248    361    -83       N
ATOM    727  CA  TYR A  89     -68.655  30.061 -19.300  1.00 29.57           C
ANISOU  727  CA  TYR A  89     3578   2899   4757   -232    430    -90       C
ATOM    728  C   TYR A  89     -70.147  30.290 -19.496  1.00 34.78           C
ANISOU  728  C   TYR A  89     4276   3568   5369   -155    407    -70       C
ATOM    729  O   TYR A  89     -70.579  31.446 -19.559  1.00 36.58           O
ANISOU  729  O   TYR A  89     4624   3797   5477   -123    445    -55       O
ATOM    730  CB  TYR A  89     -67.905  30.319 -20.605  1.00 28.98           C
ANISOU  730  CB  TYR A  89     3554   2821   4637   -241    487   -174       C
ATOM    731  CG  TYR A  89     -66.418  30.533 -20.423  1.00 31.59           C
ANISOU  731  CG  TYR A  89     3860   3157   4986   -326    541   -210       C
ATOM    732  CD1 TYR A  89     -65.877  31.811 -20.443  1.00 32.09           C
ANISOU  732  CD1 TYR A  89     4046   3218   4929   -386    630   -214       C
ATOM    733  CD2 TYR A  89     -65.558  29.459 -20.226  1.00 29.81           C
ANISOU  733  CD2 TYR A  89     3486   2936   4905   -347    500   -247       C
ATOM    734  CE1 TYR A  89     -64.521  32.016 -20.278  1.00 30.91           C
ANISOU  734  CE1 TYR A  89     3853   3085   4806   -479    684   -264       C
ATOM    735  CE2 TYR A  89     -64.198  29.655 -20.061  1.00 30.25           C
ANISOU  735  CE2 TYR A  89     3490   3010   4993   -418    541   -297       C
ATOM    736  CZ  TYR A  89     -63.686  30.936 -20.087  1.00 33.19           C
ANISOU  736  CZ  TYR A  89     3967   3395   5249   -491    636   -309       C
ATOM    737  OH  TYR A  89     -62.336  31.144 -19.922  1.00 30.60           O
ANISOU  737  OH  TYR A  89     3569   3097   4962   -577    682   -375       O
ATOM    738  N   LYS A  90     -70.940  29.222 -19.598  1.00 36.27           N
ANISOU  738  N   LYS A  90     4364   3762   5655   -123    343    -78       N
ATOM    739  CA  LYS A  90     -72.388  29.386 -19.685  1.00 35.12           C
ANISOU  739  CA  LYS A  90     4216   3641   5486    -56    316    -73       C
ATOM    740  C   LYS A  90     -72.957  29.917 -18.376  1.00 32.68           C
ANISOU  740  C   LYS A  90     3917   3347   5152    -69    340     -3       C
ATOM    741  O   LYS A  90     -73.831  30.792 -18.381  1.00 35.14           O
ANISOU  741  O   LYS A  90     4284   3679   5386     -5    356     -1       O
ATOM    742  CB  LYS A  90     -73.043  28.058 -20.060  1.00 36.30           C
ANISOU  742  CB  LYS A  90     4242   3794   5757    -45    250   -109       C
ATOM    743  CG  LYS A  90     -72.605  27.520 -21.410  1.00 41.70           C
ANISOU  743  CG  LYS A  90     4924   4463   6456    -24    226   -191       C
ATOM    744  CD  LYS A  90     -73.125  28.390 -22.541  1.00 45.49           C
ANISOU  744  CD  LYS A  90     5511   4964   6810     55    224   -238       C
ATOM    745  CE  LYS A  90     -72.372  28.122 -23.832  1.00 51.80           C
ANISOU  745  CE  LYS A  90     6359   5744   7580     56    234   -314       C
ATOM    746  NZ  LYS A  90     -72.343  26.674 -24.168  1.00 54.36           N
ANISOU  746  NZ  LYS A  90     6561   6054   8039     36    183   -368       N
ATOM    747  N   ARG A  91     -72.473  29.405 -17.245  1.00 29.06           N
ANISOU  747  N   ARG A  91     3412   2874   4754   -144    340     52       N
ATOM    748  CA  ARG A  91     -72.899  29.874 -15.936  1.00 29.40           C
ANISOU  748  CA  ARG A  91     3482   2928   4759   -173    373    118       C
ATOM    749  C   ARG A  91     -71.957  30.907 -15.335  1.00 28.04           C
ANISOU  749  C   ARG A  91     3418   2745   4493   -214    418    149       C
ATOM    750  O   ARG A  91     -72.266  31.448 -14.267  1.00 29.68           O
ANISOU  750  O   ARG A  91     3672   2959   4647   -236    452    197       O
ATOM    751  CB  ARG A  91     -73.032  28.693 -14.964  1.00 29.64           C
ANISOU  751  CB  ARG A  91     3430   2942   4890   -238    342    168       C
ATOM    752  CG  ARG A  91     -73.975  27.598 -15.427  1.00 28.91           C
ANISOU  752  CG  ARG A  91     3232   2853   4901   -226    305    136       C
ATOM    753  CD  ARG A  91     -74.070  26.472 -14.401  1.00 30.47           C
ANISOU  753  CD  ARG A  91     3385   3012   5181   -308    287    195       C
ATOM    754  NE  ARG A  91     -72.759  25.947 -14.028  1.00 34.54           N
ANISOU  754  NE  ARG A  91     3922   3472   5731   -347    241    231       N
ATOM    755  CZ  ARG A  91     -72.212  26.078 -12.823  1.00 31.58           C
ANISOU  755  CZ  ARG A  91     3607   3076   5317   -400    240    306       C
ATOM    756  NH1 ARG A  91     -72.867  26.710 -11.859  1.00 30.90           N
ANISOU  756  NH1 ARG A  91     3575   3016   5149   -431    298    354       N
ATOM    757  NH2 ARG A  91     -71.012  25.569 -12.577  1.00 32.06           N
ANISOU  757  NH2 ARG A  91     3670   3091   5420   -416    175    325       N
ATOM    758  N   ASP A  92     -70.832  31.196 -15.991  1.00 25.78           N
ANISOU  758  N   ASP A  92     3169   2442   4183   -233    428    113       N
ATOM    759  CA  ASP A  92     -69.801  32.084 -15.452  1.00 27.88           C
ANISOU  759  CA  ASP A  92     3519   2700   4376   -295    470    127       C
ATOM    760  C   ASP A  92     -69.384  31.637 -14.053  1.00 26.81           C
ANISOU  760  C   ASP A  92     3344   2563   4280   -363    436    187       C
ATOM    761  O   ASP A  92     -69.283  32.431 -13.116  1.00 26.95           O
ANISOU  761  O   ASP A  92     3441   2582   4216   -402    466    224       O
ATOM    762  CB  ASP A  92     -70.270  33.541 -15.453  1.00 33.59           C
ANISOU  762  CB  ASP A  92     4388   3416   4959   -265    537    132       C
ATOM    763  CG  ASP A  92     -70.413  34.106 -16.853  1.00 44.79           C
ANISOU  763  CG  ASP A  92     5890   4817   6310   -203    563     78       C
ATOM    764  OD1 ASP A  92     -69.604  33.737 -17.731  1.00 48.05           O
ANISOU  764  OD1 ASP A  92     6281   5225   6750   -230    565     30       O
ATOM    765  OD2 ASP A  92     -71.335  34.919 -17.077  1.00 48.84           O
ANISOU  765  OD2 ASP A  92     6498   5321   6739   -123    580     80       O
ATOM    766  N   ALA A  93     -69.147  30.338 -13.920  1.00 23.81           N
ANISOU  766  N   ALA A  93     2856   2172   4018   -375    366    197       N
ATOM    767  CA  ALA A  93     -68.839  29.719 -12.641  1.00 22.04           C
ANISOU  767  CA  ALA A  93     2611   1933   3832   -426    311    262       C
ATOM    768  C   ALA A  93     -67.995  28.485 -12.901  1.00 21.80           C
ANISOU  768  C   ALA A  93     2479   1874   3931   -426    228    242       C
ATOM    769  O   ALA A  93     -67.980  27.967 -14.024  1.00 22.65           O
ANISOU  769  O   ALA A  93     2524   1976   4107   -386    224    180       O
ATOM    770  CB  ALA A  93     -70.120  29.346 -11.880  1.00 23.01           C
ANISOU  770  CB  ALA A  93     2742   2052   3950   -426    320    322       C
ATOM    771  N   PRO A  94     -67.266  27.995 -11.898  1.00 25.50           N
ANISOU  771  N   PRO A  94     2936   2321   4433   -463    154    287       N
ATOM    772  CA  PRO A  94     -66.532  26.740 -12.081  1.00 25.62           C
ANISOU  772  CA  PRO A  94     2858   2296   4582   -440     60    268       C
ATOM    773  C   PRO A  94     -67.491  25.582 -12.307  1.00 30.92           C
ANISOU  773  C   PRO A  94     3499   2917   5331   -414     36    292       C
ATOM    774  O   PRO A  94     -68.575  25.524 -11.723  1.00 32.52           O
ANISOU  774  O   PRO A  94     3752   3112   5493   -438     64    354       O
ATOM    775  CB  PRO A  94     -65.753  26.585 -10.770  1.00 25.21           C
ANISOU  775  CB  PRO A  94     2832   2227   4520   -475    -29    328       C
ATOM    776  CG  PRO A  94     -66.499  27.417  -9.784  1.00 27.44           C
ANISOU  776  CG  PRO A  94     3232   2528   4668   -525     24    400       C
ATOM    777  CD  PRO A  94     -67.027  28.579 -10.566  1.00 26.83           C
ANISOU  777  CD  PRO A  94     3186   2496   4511   -518    142    350       C
ATOM    778  N   ALA A  95     -67.081  24.653 -13.172  1.00 33.90           N
ANISOU  778  N   ALA A  95     3792   3263   5827   -372     -7    231       N
ATOM    779  CA  ALA A  95     -67.950  23.540 -13.530  1.00 22.57           C
ANISOU  779  CA  ALA A  95     2330   1774   4473   -355    -27    236       C
ATOM    780  C   ALA A  95     -68.124  22.542 -12.393  1.00 24.86           C
ANISOU  780  C   ALA A  95     2659   1984   4804   -385   -102    330       C
ATOM    781  O   ALA A  95     -69.098  21.782 -12.401  1.00 24.75           O
ANISOU  781  O   ALA A  95     2651   1924   4827   -406    -94    354       O
ATOM    782  CB  ALA A  95     -67.406  22.826 -14.769  1.00 22.76           C
ANISOU  782  CB  ALA A  95     2267   1776   4606   -302    -50    136       C
ATOM    783  N   HIS A  96     -67.219  22.524 -11.418  1.00 24.84           N
ANISOU  783  N   HIS A  96     2691   1959   4788   -394   -176    381       N
ATOM    784  CA  HIS A  96     -67.261  21.542 -10.346  1.00 25.05           C
ANISOU  784  CA  HIS A  96     2787   1892   4839   -415   -264    477       C
ATOM    785  C   HIS A  96     -67.103  22.228  -8.997  1.00 28.45           C
ANISOU  785  C   HIS A  96     3322   2344   5145   -467   -277    564       C
ATOM    786  O   HIS A  96     -66.445  23.264  -8.880  1.00 31.50           O
ANISOU  786  O   HIS A  96     3701   2803   5466   -468   -265    535       O
ATOM    787  CB  HIS A  96     -66.177  20.476 -10.529  1.00 27.94           C
ANISOU  787  CB  HIS A  96     3100   2179   5336   -346   -392    448       C
ATOM    788  CG  HIS A  96     -66.173  19.856 -11.891  1.00 26.08           C
ANISOU  788  CG  HIS A  96     2764   1927   5220   -292   -376    345       C
ATOM    789  ND1 HIS A  96     -65.170  20.082 -12.808  1.00 26.43           N
ANISOU  789  ND1 HIS A  96     2699   2016   5326   -233   -378    232       N
ATOM    790  CD2 HIS A  96     -67.060  19.034 -12.498  1.00 25.64           C
ANISOU  790  CD2 HIS A  96     2702   1814   5225   -299   -349    329       C
ATOM    791  CE1 HIS A  96     -65.434  19.417 -13.919  1.00 30.94           C
ANISOU  791  CE1 HIS A  96     3214   2558   5984   -198   -354    154       C
ATOM    792  NE2 HIS A  96     -66.577  18.774 -13.757  1.00 25.55           N
ANISOU  792  NE2 HIS A  96     2592   1813   5305   -236   -344    210       N
ATOM    793  N   ILE A  97     -67.712  21.627  -7.977  1.00 36.64           N
ANISOU  793  N   ILE A  97     4469   3312   6142   -520   -297    667       N
ATOM    794  CA  ILE A  97     -67.733  22.190  -6.631  1.00 41.90           C
ANISOU  794  CA  ILE A  97     5263   3989   6669   -581   -300    756       C
ATOM    795  C   ILE A  97     -66.319  22.270  -6.068  1.00 42.58           C
ANISOU  795  C   ILE A  97     5359   4068   6751   -542   -441    763       C
ATOM    796  O   ILE A  97     -65.782  23.362  -5.845  1.00 41.71           O
ANISOU  796  O   ILE A  97     5244   4040   6565   -553   -428    734       O
ATOM    797  CB  ILE A  97     -68.638  21.356  -5.706  1.00 47.84           C
ANISOU  797  CB  ILE A  97     6144   4652   7380   -655   -287    863       C
ATOM    798  CG1 ILE A  97     -69.995  21.101  -6.364  1.00 51.44           C
ANISOU  798  CG1 ILE A  97     6550   5117   7877   -695   -159    832       C
ATOM    799  CG2 ILE A  97     -68.807  22.043  -4.360  1.00 49.19           C
ANISOU  799  CG2 ILE A  97     6460   4845   7383   -729   -258    946       C
ATOM    800  CD1 ILE A  97     -70.873  20.139  -5.585  1.00 53.12           C
ANISOU  800  CD1 ILE A  97     6874   5234   8073   -788   -130    921       C
ATOM    801  N   SER A  98     -65.712  21.115  -5.826  1.00 41.14           N
ANISOU  801  N   SER A  98     5192   3785   6653   -493   -584    797       N
ATOM    802  CA  SER A  98     -64.416  21.049  -5.173  1.00 37.33           C
ANISOU  802  CA  SER A  98     4719   3290   6174   -443   -748    807       C
ATOM    803  C   SER A  98     -63.293  20.992  -6.204  1.00 35.03           C
ANISOU  803  C   SER A  98     4242   3037   6029   -349   -806    679       C
ATOM    804  O   SER A  98     -63.520  20.857  -7.408  1.00 34.07           O
ANISOU  804  O   SER A  98     4012   2933   6000   -323   -724    594       O
ATOM    805  CB  SER A  98     -64.355  19.839  -4.243  1.00 38.99           C
ANISOU  805  CB  SER A  98     5072   3358   6385   -428   -889    919       C
ATOM    806  OG  SER A  98     -65.402  19.879  -3.289  1.00 35.53           O
ANISOU  806  OG  SER A  98     4814   2884   5802   -534   -812   1033       O
ATOM    807  N   THR A  99     -62.064  21.101  -5.710  1.00 34.28           N
ANISOU  807  N   THR A  99     4110   2962   5952   -302   -949    656       N
ATOM    808  CA  THR A  99     -60.870  21.059  -6.538  1.00 36.34           C
ANISOU  808  CA  THR A  99     4181   3272   6356   -219  -1007    523       C
ATOM    809  C   THR A  99     -59.855  20.113  -5.911  1.00 37.66           C
ANISOU  809  C   THR A  99     4338   3362   6610   -116  -1232    538       C
ATOM    810  O   THR A  99     -60.003  19.670  -4.768  1.00 38.00           O
ANISOU  810  O   THR A  99     4544   3322   6573   -118  -1349    660       O
ATOM    811  CB  THR A  99     -60.257  22.456  -6.716  1.00 35.50           C
ANISOU  811  CB  THR A  99     3989   3306   6194   -271   -935    434       C
ATOM    812  OG1 THR A  99     -60.092  23.076  -5.434  1.00 38.24           O
ANISOU  812  OG1 THR A  99     4451   3677   6403   -327  -1002    507       O
ATOM    813  CG2 THR A  99     -61.152  23.326  -7.585  1.00 29.79           C
ANISOU  813  CG2 THR A  99     3267   2644   5410   -340   -725    400       C
ATOM    814  N   ILE A 100     -58.816  19.799  -6.681  1.00 36.70           N
ANISOU  814  N   ILE A 100     4028   3266   6650    -21  -1292    408       N
ATOM    815  CA  ILE A 100     -57.731  18.928  -6.242  1.00 37.55           C
ANISOU  815  CA  ILE A 100     4082   3312   6872    108  -1517    390       C
ATOM    816  C   ILE A 100     -56.424  19.645  -6.541  1.00 39.10           C
ANISOU  816  C   ILE A 100     4064   3646   7145    134  -1550    236       C
ATOM    817  O   ILE A 100     -56.067  19.829  -7.711  1.00 37.09           O
ANISOU  817  O   ILE A 100     3633   3460   6998    145  -1438     95       O
ATOM    818  CB  ILE A 100     -57.767  17.557  -6.929  1.00 42.39           C
ANISOU  818  CB  ILE A 100     4663   3797   7647    222  -1566    365       C
ATOM    819  CG1 ILE A 100     -59.042  16.800  -6.550  1.00 42.10           C
ANISOU  819  CG1 ILE A 100     4846   3615   7535    176  -1537    515       C
ATOM    820  CG2 ILE A 100     -56.535  16.746  -6.559  1.00 43.01           C
ANISOU  820  CG2 ILE A 100     4662   3820   7860    380  -1805    321       C
ATOM    821  CD1 ILE A 100     -59.222  15.493  -7.293  1.00 41.53           C
ANISOU  821  CD1 ILE A 100     4761   3406   7612    262  -1560    488       C
ATOM    822  N   GLY A 101     -55.713  20.050  -5.493  1.00 41.89           N
ANISOU  822  N   GLY A 101     4434   4044   7440    134  -1699    256       N
ATOM    823  CA  GLY A 101     -54.424  20.704  -5.665  1.00 44.45           C
ANISOU  823  CA  GLY A 101     4541   4504   7844    147  -1746    102       C
ATOM    824  C   GLY A 101     -54.482  21.990  -6.460  1.00 46.00           C
ANISOU  824  C   GLY A 101     4647   4835   7996     15  -1517      2       C
ATOM    825  O   GLY A 101     -53.602  22.242  -7.292  1.00 47.49           O
ANISOU  825  O   GLY A 101     4620   5116   8309     26  -1467   -163       O
ATOM    826  N   VAL A 102     -55.503  22.813  -6.224  1.00 44.48           N
ANISOU  826  N   VAL A 102     4623   4652   7625   -110  -1372     96       N
ATOM    827  CA  VAL A 102     -55.674  24.060  -6.961  1.00 41.64           C
ANISOU  827  CA  VAL A 102     4223   4396   7202   -230  -1157     20       C
ATOM    828  C   VAL A 102     -55.810  25.226  -5.991  1.00 38.89           C
ANISOU  828  C   VAL A 102     4000   4102   6674   -346  -1141     75       C
ATOM    829  O   VAL A 102     -54.953  26.116  -5.947  1.00 41.04           O
ANISOU  829  O   VAL A 102     4176   4476   6941   -412  -1131    -26       O
ATOM    830  CB  VAL A 102     -56.891  23.992  -7.901  1.00 42.22           C
ANISOU  830  CB  VAL A 102     4372   4425   7245   -254   -969     55       C
ATOM    831  CG1 VAL A 102     -57.142  25.350  -8.530  1.00 42.31           C
ANISOU  831  CG1 VAL A 102     4393   4525   7159   -369   -765     -1       C
ATOM    832  CG2 VAL A 102     -56.680  22.934  -8.973  1.00 44.20           C
ANISOU  832  CG2 VAL A 102     4494   4631   7671   -151   -969    -25       C
ATOM    833  N   CYS A 103     -56.889  25.231  -5.212  1.00 37.72           N
ANISOU  833  N   CYS A 103     4066   3887   6378   -381  -1128    226       N
ATOM    834  CA  CYS A 103     -57.194  26.318  -4.292  1.00 38.30           C
ANISOU  834  CA  CYS A 103     4286   4000   6266   -491  -1091    283       C
ATOM    835  C   CYS A 103     -57.403  25.750  -2.898  1.00 38.90           C
ANISOU  835  C   CYS A 103     4531   4003   6246   -469  -1259    418       C
ATOM    836  O   CYS A 103     -58.232  24.855  -2.710  1.00 43.73           O
ANISOU  836  O   CYS A 103     5257   4511   6846   -429  -1271    528       O
ATOM    837  CB  CYS A 103     -58.440  27.086  -4.741  1.00 40.15           C
ANISOU  837  CB  CYS A 103     4635   4234   6387   -569   -867    322       C
ATOM    838  SG  CYS A 103     -59.125  28.189  -3.489  1.00 44.80           S
ANISOU  838  SG  CYS A 103     5446   4835   6740   -681   -816    416       S
ATOM    839  N   SER A 104     -56.665  26.288  -1.923  1.00 37.57           N
ANISOU  839  N   SER A 104     4390   3885   6000   -506  -1384    409       N
ATOM    840  CA  SER A 104     -56.713  25.750  -0.566  1.00 46.93           C
ANISOU  840  CA  SER A 104     5751   5002   7080   -482  -1569    532       C
ATOM    841  C   SER A 104     -58.114  25.813   0.026  1.00 50.05           C
ANISOU  841  C   SER A 104     6392   5326   7299   -552  -1448    678       C
ATOM    842  O   SER A 104     -58.477  24.965   0.850  1.00 57.34           O
ANISOU  842  O   SER A 104     7479   6150   8159   -521  -1555    803       O
ATOM    843  CB  SER A 104     -55.731  26.504   0.331  1.00 57.72           C
ANISOU  843  CB  SER A 104     7110   6451   8371   -528  -1709    482       C
ATOM    844  OG  SER A 104     -54.410  26.414  -0.171  1.00 70.33           O
ANISOU  844  OG  SER A 104     8454   8126  10144   -467  -1824    331       O
ATOM    845  N   MET A 105     -58.915  26.799  -0.378  1.00 44.95           N
ANISOU  845  N   MET A 105     5780   4725   6574   -644  -1225    662       N
ATOM    846  CA  MET A 105     -60.256  26.927   0.177  1.00 46.70           C
ANISOU  846  CA  MET A 105     6207   4897   6641   -709  -1097    778       C
ATOM    847  C   MET A 105     -61.219  25.893  -0.396  1.00 40.99           C
ANISOU  847  C   MET A 105     5493   4086   5994   -664  -1026    839       C
ATOM    848  O   MET A 105     -62.145  25.466   0.301  1.00 41.18           O
ANISOU  848  O   MET A 105     5690   4039   5918   -700   -992    953       O
ATOM    849  CB  MET A 105     -60.790  28.341  -0.061  1.00 56.46           C
ANISOU  849  CB  MET A 105     7471   6206   7776   -802   -894    730       C
ATOM    850  CG  MET A 105     -62.111  28.624   0.634  1.00 66.54           C
ANISOU  850  CG  MET A 105     8946   7449   8887   -868   -761    828       C
ATOM    851  SD  MET A 105     -62.038  28.350   2.416  1.00 69.89           S
ANISOU  851  SD  MET A 105     9606   7825   9124   -916   -904    946       S
ATOM    852  CE  MET A 105     -61.162  29.811   2.954  1.00 62.19           C
ANISOU  852  CE  MET A 105     8648   6946   8035   -992   -933    859       C
ATOM    853  N   THR A 106     -61.019  25.473  -1.647  1.00 37.86           N
ANISOU  853  N   THR A 106     4919   3693   5771   -597   -995    759       N
ATOM    854  CA  THR A 106     -61.885  24.488  -2.278  1.00 34.82           C
ANISOU  854  CA  THR A 106     4532   3228   5470   -559   -934    799       C
ATOM    855  C   THR A 106     -61.241  23.119  -2.434  1.00 37.30           C
ANISOU  855  C   THR A 106     4788   3453   5932   -452  -1107    805       C
ATOM    856  O   THR A 106     -61.931  22.174  -2.833  1.00 35.73           O
ANISOU  856  O   THR A 106     4611   3166   5799   -426  -1075    846       O
ATOM    857  CB  THR A 106     -62.340  24.979  -3.660  1.00 33.21           C
ANISOU  857  CB  THR A 106     4199   3081   5340   -560   -756    704       C
ATOM    858  OG1 THR A 106     -61.194  25.231  -4.482  1.00 35.82           O
ANISOU  858  OG1 THR A 106     4350   3474   5786   -516   -794    577       O
ATOM    859  CG2 THR A 106     -63.155  26.252  -3.530  1.00 27.66           C
ANISOU  859  CG2 THR A 106     3576   2441   4493   -646   -585    707       C
ATOM    860  N   ASP A 107     -59.950  22.982  -2.137  1.00 41.21           N
ANISOU  860  N   ASP A 107     5206   3966   6486   -386  -1291    758       N
ATOM    861  CA  ASP A 107     -59.286  21.694  -2.280  1.00 37.88           C
ANISOU  861  CA  ASP A 107     4725   3454   6214   -259  -1470    754       C
ATOM    862  C   ASP A 107     -59.815  20.699  -1.258  1.00 38.94           C
ANISOU  862  C   ASP A 107     5088   3442   6267   -250  -1577    913       C
ATOM    863  O   ASP A 107     -59.850  20.982  -0.056  1.00 41.90           O
ANISOU  863  O   ASP A 107     5636   3806   6479   -301  -1648   1004       O
ATOM    864  CB  ASP A 107     -57.773  21.843  -2.116  1.00 37.58           C
ANISOU  864  CB  ASP A 107     4537   3482   6259   -184  -1655    655       C
ATOM    865  CG  ASP A 107     -57.079  22.219  -3.409  1.00 40.45           C
ANISOU  865  CG  ASP A 107     4642   3946   6782   -156  -1572    481       C
ATOM    866  OD1 ASP A 107     -57.758  22.284  -4.455  1.00 40.24           O
ANISOU  866  OD1 ASP A 107     4569   3923   6795   -182  -1389    446       O
ATOM    867  OD2 ASP A 107     -55.853  22.452  -3.375  1.00 43.78           O
ANISOU  867  OD2 ASP A 107     4906   4444   7284   -113  -1689    373       O
ATOM    868  N   ILE A 108     -60.240  19.530  -1.744  1.00 38.77           N
ANISOU  868  N   ILE A 108     5082   3300   6350   -194  -1582    944       N
ATOM    869  CA  ILE A 108     -60.471  18.388  -0.867  1.00 44.71           C
ANISOU  869  CA  ILE A 108     6046   3885   7058   -164  -1718   1083       C
ATOM    870  C   ILE A 108     -59.247  17.492  -0.780  1.00 46.72           C
ANISOU  870  C   ILE A 108     6242   4064   7445      1  -1977   1054       C
ATOM    871  O   ILE A 108     -59.171  16.645   0.123  1.00 44.41           O
ANISOU  871  O   ILE A 108     6148   3629   7096     46  -2145   1173       O
ATOM    872  CB  ILE A 108     -61.679  17.552  -1.334  1.00 46.41           C
ANISOU  872  CB  ILE A 108     6342   3987   7305   -210  -1582   1141       C
ATOM    873  CG1 ILE A 108     -61.460  17.050  -2.761  1.00 40.88           C
ANISOU  873  CG1 ILE A 108     5431   3284   6815   -123  -1547   1017       C
ATOM    874  CG2 ILE A 108     -62.961  18.364  -1.238  1.00 47.72           C
ANISOU  874  CG2 ILE A 108     6577   4222   7333   -365  -1347   1177       C
ATOM    875  CD1 ILE A 108     -62.559  16.147  -3.257  1.00 37.54           C
ANISOU  875  CD1 ILE A 108     5077   2747   6439   -164  -1438   1058       C
ATOM    876  N   ALA A 109     -58.284  17.657  -1.685  1.00 49.91           N
ANISOU  876  N   ALA A 109     6386   4556   8021     95  -2013    896       N
ATOM    877  CA  ALA A 109     -57.061  16.867  -1.693  1.00 50.86           C
ANISOU  877  CA  ALA A 109     6403   4626   8296    270  -2253    836       C
ATOM    878  C   ALA A 109     -56.022  17.607  -2.524  1.00 45.83           C
ANISOU  878  C   ALA A 109     5460   4158   7794    310  -2232    641       C
ATOM    879  O   ALA A 109     -56.337  18.551  -3.252  1.00 39.14           O
ANISOU  879  O   ALA A 109     4506   3433   6931    207  -2021    564       O
ATOM    880  CB  ALA A 109     -57.307  15.459  -2.244  1.00 41.51           C
ANISOU  880  CB  ALA A 109     5252   3269   7250    372  -2292    856       C
ATOM    881  N   LYS A 110     -54.771  17.165  -2.404  1.00 51.48           N
ANISOU  881  N   LYS A 110     6041   4876   8643    461  -2455    558       N
ATOM    882  CA  LYS A 110     -53.685  17.742  -3.186  1.00 56.34           C
ANISOU  882  CA  LYS A 110     6347   5650   9411    500  -2439    356       C
ATOM    883  C   LYS A 110     -53.413  16.956  -4.463  1.00 54.03           C
ANISOU  883  C   LYS A 110     5868   5323   9338    610  -2388    229       C
ATOM    884  O   LYS A 110     -53.131  17.553  -5.508  1.00 48.59           O
ANISOU  884  O   LYS A 110     4969   4759   8734    567  -2221     78       O
ATOM    885  CB  LYS A 110     -52.409  17.821  -2.344  1.00 68.23           C
ANISOU  885  CB  LYS A 110     7765   7211  10949    597  -2708    303       C
ATOM    886  CG  LYS A 110     -52.499  18.772  -1.161  1.00 78.01           C
ANISOU  886  CG  LYS A 110     9154   8516  11971    478  -2755    389       C
ATOM    887  CD  LYS A 110     -51.176  18.839  -0.412  1.00 89.95           C
ANISOU  887  CD  LYS A 110    10552  10095  13531    580  -3038    313       C
ATOM    888  CE  LYS A 110     -51.232  19.841   0.731  1.00 94.03           C
ANISOU  888  CE  LYS A 110    11216  10686  13825    451  -3082    382       C
ATOM    889  NZ  LYS A 110     -49.932  19.927   1.455  1.00 96.93           N
ANISOU  889  NZ  LYS A 110    11461  11130  14238    546  -3374    296       N
ATOM    890  N   LYS A 111     -53.492  15.631  -4.400  1.00 56.70           N
ANISOU  890  N   LYS A 111     6296   5486   9763    746  -2523    287       N
ATOM    891  CA  LYS A 111     -53.281  14.766  -5.548  1.00 55.91           C
ANISOU  891  CA  LYS A 111     6049   5327   9867    860  -2485    172       C
ATOM    892  C   LYS A 111     -54.453  13.810  -5.699  1.00 56.25           C
ANISOU  892  C   LYS A 111     6314   5182   9878    844  -2422    301       C
ATOM    893  O   LYS A 111     -55.116  13.472  -4.712  1.00 56.87           O
ANISOU  893  O   LYS A 111     6657   5137   9813    804  -2495    481       O
ATOM    894  CB  LYS A 111     -51.970  13.976  -5.412  1.00 57.74           C
ANISOU  894  CB  LYS A 111     6128   5522  10289   1080  -2744     69       C
ATOM    895  CG  LYS A 111     -50.759  14.718  -5.958  1.00 59.25           C
ANISOU  895  CG  LYS A 111     5982   5916  10614   1105  -2727   -152       C
ATOM    896  CD  LYS A 111     -49.464  13.972  -5.690  1.00 66.46           C
ANISOU  896  CD  LYS A 111     6781   6830  11642   1284  -2931   -265       C
ATOM    897  CE  LYS A 111     -49.073  14.051  -4.224  1.00 72.19           C
ANISOU  897  CE  LYS A 111     7643   7539  12245   1321  -3185   -158       C
ATOM    898  NZ  LYS A 111     -47.744  13.427  -3.971  1.00 76.32           N
ANISOU  898  NZ  LYS A 111     8047   8092  12858   1482  -3358   -287       N
ATOM    899  N   PRO A 112     -54.741  13.364  -6.927  1.00 56.93           N
ANISOU  899  N   PRO A 112     6303   5241  10086    861  -2278    208       N
ATOM    900  CA  PRO A 112     -55.930  12.522  -7.141  1.00 56.41           C
ANISOU  900  CA  PRO A 112     6435   5009   9990    818  -2197    315       C
ATOM    901  C   PRO A 112     -55.862  11.168  -6.456  1.00 62.10           C
ANISOU  901  C   PRO A 112     7344   5499  10753    946  -2412    421       C
ATOM    902  O   PRO A 112     -56.912  10.547  -6.251  1.00 66.07           O
ANISOU  902  O   PRO A 112     8070   5857  11176    871  -2358    550       O
ATOM    903  CB  PRO A 112     -55.982  12.363  -8.669  1.00 52.48           C
ANISOU  903  CB  PRO A 112     5756   4551   9633    832  -2028    154       C
ATOM    904  CG  PRO A 112     -55.142  13.480  -9.207  1.00 54.36           C
ANISOU  904  CG  PRO A 112     5745   5004   9905    810  -1945     -4       C
ATOM    905  CD  PRO A 112     -54.066  13.697  -8.192  1.00 55.89           C
ANISOU  905  CD  PRO A 112     5886   5241  10107    893  -2158     -4       C
ATOM    906  N   THR A 113     -54.673  10.692  -6.093  1.00 61.69           N
ANISOU  906  N   THR A 113     7219   5446  10773   1105  -2614    355       N
ATOM    907  CA  THR A 113     -54.526   9.377  -5.480  1.00 63.49           C
ANISOU  907  CA  THR A 113     7644   5518  10962   1196  -2762    425       C
ATOM    908  C   THR A 113     -54.961   9.339  -4.021  1.00 62.83           C
ANISOU  908  C   THR A 113     7856   5344  10670   1136  -2879    631       C
ATOM    909  O   THR A 113     -54.921   8.265  -3.412  1.00 68.98           O
ANISOU  909  O   THR A 113     8836   5983  11389   1199  -2994    708       O
ATOM    910  CB  THR A 113     -53.074   8.905  -5.586  1.00 67.34           C
ANISOU  910  CB  THR A 113     7952   6053  11580   1383  -2924    269       C
ATOM    911  OG1 THR A 113     -52.195   9.954  -5.158  1.00 67.10           O
ANISOU  911  OG1 THR A 113     7751   6188  11556   1400  -3014    205       O
ATOM    912  CG2 THR A 113     -52.743   8.519  -7.018  1.00 67.95           C
ANISOU  912  CG2 THR A 113     7809   6171  11837   1441  -2794     77       C
ATOM    913  N   GLU A 114     -55.372  10.467  -3.448  1.00 56.58           N
ANISOU  913  N   GLU A 114     7111   4627   9760   1015  -2845    720       N
ATOM    914  CA  GLU A 114     -55.767  10.485  -2.049  1.00 61.12           C
ANISOU  914  CA  GLU A 114     7978   5130  10114    943  -2938    907       C
ATOM    915  C   GLU A 114     -57.095   9.755  -1.849  1.00 63.18           C
ANISOU  915  C   GLU A 114     8516   5245  10246    813  -2795   1050       C
ATOM    916  O   GLU A 114     -57.849   9.501  -2.793  1.00 62.57           O
ANISOU  916  O   GLU A 114     8391   5143  10241    749  -2611   1012       O
ATOM    917  CB  GLU A 114     -55.854  11.923  -1.536  1.00 63.51           C
ANISOU  917  CB  GLU A 114     8255   5563  10314    837  -2921    953       C
ATOM    918  CG  GLU A 114     -54.511  12.479  -1.079  1.00 70.28           C
ANISOU  918  CG  GLU A 114     8946   6550  11206    948  -3131    861       C
ATOM    919  CD  GLU A 114     -54.549  13.969  -0.799  1.00 72.39           C
ANISOU  919  CD  GLU A 114     9138   7030  11335    790  -3008    832       C
ATOM    920  OE1 GLU A 114     -54.009  14.743  -1.618  1.00 71.36           O
ANISOU  920  OE1 GLU A 114     8724   7078  11312    778  -2906    662       O
ATOM    921  OE2 GLU A 114     -55.121  14.367   0.237  1.00 73.14           O
ANISOU  921  OE2 GLU A 114     9472   7110  11210    673  -3006    977       O
ATOM    922  N   THR A 115     -57.370   9.418  -0.587  1.00 64.39           N
ANISOU  922  N   THR A 115     8957   5310  10198    766  -2876   1204       N
ATOM    923  CA  THR A 115     -58.512   8.567  -0.263  1.00 63.57           C
ANISOU  923  CA  THR A 115     9122   5067   9965    649  -2749   1329       C
ATOM    924  C   THR A 115     -59.835   9.254  -0.576  1.00 63.57           C
ANISOU  924  C   THR A 115     9140   5119   9895    440  -2484   1372       C
ATOM    925  O   THR A 115     -60.775   8.610  -1.059  1.00 63.68           O
ANISOU  925  O   THR A 115     9214   5062   9918    355  -2320   1383       O
ATOM    926  CB  THR A 115     -58.453   8.164   1.211  1.00 65.96           C
ANISOU  926  CB  THR A 115     9727   5281  10054    640  -2882   1475       C
ATOM    927  OG1 THR A 115     -57.277   7.378   1.446  1.00 72.68           O
ANISOU  927  OG1 THR A 115    10567   6070  10979    844  -3128   1429       O
ATOM    928  CG2 THR A 115     -59.684   7.358   1.605  1.00 65.92           C
ANISOU  928  CG2 THR A 115     9997   5144   9906    494  -2720   1600       C
ATOM    929  N   ILE A 116     -59.926  10.561  -0.320  1.00 59.44           N
ANISOU  929  N   ILE A 116     8558   4722   9302    355  -2440   1389       N
ATOM    930  CA  ILE A 116     -61.186  11.275  -0.482  1.00 55.19           C
ANISOU  930  CA  ILE A 116     8049   4243   8677    156  -2189   1431       C
ATOM    931  C   ILE A 116     -61.658  11.276  -1.931  1.00 52.42           C
ANISOU  931  C   ILE A 116     7489   3925   8503    139  -2022   1314       C
ATOM    932  O   ILE A 116     -62.847  11.483  -2.194  1.00 51.83           O
ANISOU  932  O   ILE A 116     7444   3877   8373    -15  -1806   1335       O
ATOM    933  CB  ILE A 116     -61.047  12.715   0.061  1.00 52.90           C
ANISOU  933  CB  ILE A 116     7729   4092   8277     84  -2182   1455       C
ATOM    934  CG1 ILE A 116     -62.424  13.326   0.332  1.00 51.14           C
ANISOU  934  CG1 ILE A 116     7617   3923   7892   -129  -1928   1524       C
ATOM    935  CG2 ILE A 116     -60.254  13.581  -0.905  1.00 50.02           C
ANISOU  935  CG2 ILE A 116     7033   3925   8049    156  -2154   1271       C
ATOM    936  CD1 ILE A 116     -63.228  12.580   1.375  1.00 52.95           C
ANISOU  936  CD1 ILE A 116     8140   4050   7927   -230  -1872   1653       C
ATOM    937  N   CYS A 117     -60.758  11.030  -2.881  1.00 52.94           N
ANISOU  937  N   CYS A 117     7336   4000   8777    296  -2111   1179       N
ATOM    938  CA  CYS A 117     -61.103  11.039  -4.296  1.00 54.49           C
ANISOU  938  CA  CYS A 117     7333   4243   9129    288  -1956   1049       C
ATOM    939  C   CYS A 117     -61.623   9.699  -4.794  1.00 58.35           C
ANISOU  939  C   CYS A 117     7898   4605   9667    295  -1907   1035       C
ATOM    940  O   CYS A 117     -61.940   9.581  -5.982  1.00 58.94           O
ANISOU  940  O   CYS A 117     7826   4704   9863    290  -1789    926       O
ATOM    941  CB  CYS A 117     -59.888  11.452  -5.131  1.00 56.75           C
ANISOU  941  CB  CYS A 117     7331   4662   9569    430  -2014    870       C
ATOM    942  SG  CYS A 117     -59.128  13.004  -4.622  1.00 58.61           S
ANISOU  942  SG  CYS A 117     7437   5128   9703    404  -2029    827       S
ATOM    943  N   ALA A 118     -61.716   8.693  -3.925  1.00 59.65           N
ANISOU  943  N   ALA A 118     8295   4639   9730    302  -1989   1138       N
ATOM    944  CA  ALA A 118     -62.108   7.359  -4.377  1.00 55.22           C
ANISOU  944  CA  ALA A 118     7816   3945   9221    316  -1953   1121       C
ATOM    945  C   ALA A 118     -63.528   7.308  -4.930  1.00 52.15           C
ANISOU  945  C   ALA A 118     7448   3562   8803    140  -1718   1122       C
ATOM    946  O   ALA A 118     -63.705   6.810  -6.056  1.00 51.74           O
ANISOU  946  O   ALA A 118     7282   3493   8883    164  -1654   1014       O
ATOM    947  CB  ALA A 118     -61.902   6.352  -3.240  1.00 55.59           C
ANISOU  947  CB  ALA A 118     8130   3840   9152    356  -2086   1241       C
ATOM    948  N   PRO A 119     -64.567   7.786  -4.238  1.00 54.11           N
ANISOU  948  N   PRO A 119     7826   3844   8890    -36  -1581   1224       N
ATOM    949  CA  PRO A 119     -65.923   7.688  -4.793  1.00 58.12           C
ANISOU  949  CA  PRO A 119     8328   4369   9387   -196  -1363   1202       C
ATOM    950  C   PRO A 119     -66.219   8.681  -5.906  1.00 56.62           C
ANISOU  950  C   PRO A 119     7891   4333   9291   -225  -1247   1086       C
ATOM    951  O   PRO A 119     -67.340   8.680  -6.427  1.00 54.35           O
ANISOU  951  O   PRO A 119     7571   4081   8999   -348  -1079   1053       O
ATOM    952  CB  PRO A 119     -66.824   7.962  -3.572  1.00 62.79           C
ANISOU  952  CB  PRO A 119     9122   4963   9771   -363  -1255   1336       C
ATOM    953  CG  PRO A 119     -65.914   7.941  -2.375  1.00 63.64           C
ANISOU  953  CG  PRO A 119     9387   5021   9773   -281  -1434   1438       C
ATOM    954  CD  PRO A 119     -64.594   8.385  -2.892  1.00 57.23           C
ANISOU  954  CD  PRO A 119     8384   4264   9098   -101  -1612   1352       C
ATOM    955  N   LEU A 120     -65.259   9.519  -6.287  1.00 56.02           N
ANISOU  955  N   LEU A 120     7639   4348   9299   -116  -1330   1019       N
ATOM    956  CA  LEU A 120     -65.491  10.593  -7.242  1.00 48.81           C
ANISOU  956  CA  LEU A 120     6515   3578   8451   -146  -1213    920       C
ATOM    957  C   LEU A 120     -64.967  10.214  -8.619  1.00 41.42           C
ANISOU  957  C   LEU A 120     5395   2643   7700    -32  -1228    763       C
ATOM    958  O   LEU A 120     -63.943   9.535  -8.743  1.00 40.40           O
ANISOU  958  O   LEU A 120     5240   2444   7668    114  -1370    717       O
ATOM    959  CB  LEU A 120     -64.821  11.886  -6.775  1.00 45.33           C
ANISOU  959  CB  LEU A 120     6003   3277   7943   -123  -1246    927       C
ATOM    960  CG  LEU A 120     -65.275  12.441  -5.426  1.00 47.06           C
ANISOU  960  CG  LEU A 120     6400   3514   7968   -235  -1226   1069       C
ATOM    961  CD1 LEU A 120     -64.433  13.642  -5.042  1.00 46.52           C
ANISOU  961  CD1 LEU A 120     6247   3603   7825   -194  -1271   1043       C
ATOM    962  CD2 LEU A 120     -66.749  12.808  -5.467  1.00 47.41           C
ANISOU  962  CD2 LEU A 120     6477   3611   7925   -406  -1015   1095       C
ATOM    963  N   THR A 121     -65.676  10.662  -9.652  1.00 38.00           N
ANISOU  963  N   THR A 121     4835   2299   7306    -96  -1079    673       N
ATOM    964  CA  THR A 121     -65.245  10.487 -11.036  1.00 38.10           C
ANISOU  964  CA  THR A 121     4671   2345   7458     -5  -1061    510       C
ATOM    965  C   THR A 121     -64.349  11.667 -11.391  1.00 38.07           C
ANISOU  965  C   THR A 121     4497   2529   7439     60  -1046    421       C
ATOM    966  O   THR A 121     -64.831  12.758 -11.703  1.00 38.78           O
ANISOU  966  O   THR A 121     4521   2774   7440    -15   -918    394       O
ATOM    967  CB  THR A 121     -66.444  10.387 -11.972  1.00 38.12           C
ANISOU  967  CB  THR A 121     4636   2379   7470   -106   -912    448       C
ATOM    968  OG1 THR A 121     -67.254   9.266 -11.595  1.00 41.62           O
ANISOU  968  OG1 THR A 121     5231   2713   7870   -182   -900    511       O
ATOM    969  CG2 THR A 121     -65.984  10.211 -13.412  1.00 33.94           C
ANISOU  969  CG2 THR A 121     3948   1881   7066    -16   -894    277       C
ATOM    970  N   VAL A 122     -63.042  11.450 -11.335  1.00 38.06           N
ANISOU  970  N   VAL A 122     4426   2508   7527    199  -1179    370       N
ATOM    971  CA  VAL A 122     -62.054  12.496 -11.563  1.00 34.79           C
ANISOU  971  CA  VAL A 122     3849   2261   7109    250  -1174    280       C
ATOM    972  C   VAL A 122     -61.783  12.612 -13.055  1.00 35.91           C
ANISOU  972  C   VAL A 122     3817   2480   7346    291  -1074    105       C
ATOM    973  O   VAL A 122     -61.657  11.605 -13.758  1.00 38.78           O
ANISOU  973  O   VAL A 122     4156   2740   7839    364  -1102     29       O
ATOM    974  CB  VAL A 122     -60.759  12.197 -10.783  1.00 35.75           C
ANISOU  974  CB  VAL A 122     3955   2336   7291    379  -1369    291       C
ATOM    975  CG1 VAL A 122     -59.738  13.304 -10.988  1.00 35.21           C
ANISOU  975  CG1 VAL A 122     3704   2450   7223    409  -1354    186       C
ATOM    976  CG2 VAL A 122     -61.062  12.007  -9.305  1.00 36.54           C
ANISOU  976  CG2 VAL A 122     4267   2343   7274    338  -1476    472       C
ATOM    977  N   PHE A 123     -61.690  13.844 -13.547  1.00 35.32           N
ANISOU  977  N   PHE A 123     3640   2580   7200    241   -955     39       N
ATOM    978  CA  PHE A 123     -61.371  14.089 -14.947  1.00 36.31           C
ANISOU  978  CA  PHE A 123     3621   2789   7386    267   -850   -125       C
ATOM    979  C   PHE A 123     -59.861  14.213 -15.107  1.00 38.77           C
ANISOU  979  C   PHE A 123     3774   3156   7799    370   -909   -243       C
ATOM    980  O   PHE A 123     -59.227  15.037 -14.439  1.00 39.10           O
ANISOU  980  O   PHE A 123     3777   3291   7790    357   -940   -223       O
ATOM    981  CB  PHE A 123     -62.067  15.349 -15.452  1.00 35.57           C
ANISOU  981  CB  PHE A 123     3523   2840   7154    159   -687   -136       C
ATOM    982  CG  PHE A 123     -61.636  15.759 -16.827  1.00 37.84           C
ANISOU  982  CG  PHE A 123     3689   3218   7469    176   -576   -296       C
ATOM    983  CD1 PHE A 123     -62.045  15.040 -17.937  1.00 35.65           C
ANISOU  983  CD1 PHE A 123     3399   2890   7255    198   -530   -383       C
ATOM    984  CD2 PHE A 123     -60.823  16.863 -17.011  1.00 43.80           C
ANISOU  984  CD2 PHE A 123     4357   4106   8179    159   -512   -363       C
ATOM    985  CE1 PHE A 123     -61.650  15.414 -19.204  1.00 35.63           C
ANISOU  985  CE1 PHE A 123     3310   2969   7258    208   -422   -530       C
ATOM    986  CE2 PHE A 123     -60.425  17.243 -18.277  1.00 42.98           C
ANISOU  986  CE2 PHE A 123     4167   4080   8085    158   -393   -508       C
ATOM    987  CZ  PHE A 123     -60.840  16.517 -19.374  1.00 39.77           C
ANISOU  987  CZ  PHE A 123     3760   3623   7730    186   -348   -589       C
ATOM    988  N   PHE A 124     -59.292  13.402 -15.993  1.00 41.36           N
ANISOU  988  N   PHE A 124     4005   3434   8275    469   -921   -376       N
ATOM    989  CA  PHE A 124     -57.861  13.399 -16.260  1.00 37.77           C
ANISOU  989  CA  PHE A 124     3370   3035   7946    575   -965   -518       C
ATOM    990  C   PHE A 124     -57.598  13.863 -17.685  1.00 35.67           C
ANISOU  990  C   PHE A 124     2979   2880   7696    551   -791   -691       C
ATOM    991  O   PHE A 124     -58.370  13.561 -18.601  1.00 33.70           O
ANISOU  991  O   PHE A 124     2780   2596   7427    518   -696   -724       O
ATOM    992  CB  PHE A 124     -57.262  12.006 -16.047  1.00 39.45           C
ANISOU  992  CB  PHE A 124     3569   3088   8333    734  -1132   -548       C
ATOM    993  CG  PHE A 124     -57.414  11.486 -14.645  1.00 37.61           C
ANISOU  993  CG  PHE A 124     3486   2728   8077    768  -1317   -377       C
ATOM    994  CD1 PHE A 124     -56.456  11.760 -13.682  1.00 38.67           C
ANISOU  994  CD1 PHE A 124     3566   2900   8227    836  -1464   -354       C
ATOM    995  CD2 PHE A 124     -58.510  10.716 -14.293  1.00 41.82           C
ANISOU  995  CD2 PHE A 124     4221   3103   8566    724  -1343   -244       C
ATOM    996  CE1 PHE A 124     -56.591  11.280 -12.391  1.00 39.63           C
ANISOU  996  CE1 PHE A 124     3855   2897   8304    868  -1642   -193       C
ATOM    997  CE2 PHE A 124     -58.651  10.232 -13.006  1.00 38.51           C
ANISOU  997  CE2 PHE A 124     3970   2557   8107    742  -1499    -83       C
ATOM    998  CZ  PHE A 124     -57.692  10.514 -12.053  1.00 39.55           C
ANISOU  998  CZ  PHE A 124     4068   2721   8239    818  -1653    -52       C
ATOM    999  N   ASP A 125     -56.501  14.595 -17.865  1.00 38.34           N
ANISOU  999  N   ASP A 125     3157   3349   8063    558   -749   -804       N
ATOM   1000  CA  ASP A 125     -56.110  15.153 -19.156  1.00 41.62           C
ANISOU 1000  CA  ASP A 125     3461   3877   8475    517   -568   -971       C
ATOM   1001  C   ASP A 125     -54.797  14.506 -19.574  1.00 41.58           C
ANISOU 1001  C   ASP A 125     3258   3877   8665    644   -604  -1153       C
ATOM   1002  O   ASP A 125     -53.744  14.803 -19.000  1.00 46.55           O
ANISOU 1002  O   ASP A 125     3747   4576   9365    684   -674  -1203       O
ATOM   1003  CB  ASP A 125     -55.977  16.675 -19.072  1.00 44.49           C
ANISOU 1003  CB  ASP A 125     3813   4396   8695    388   -452   -962       C
ATOM   1004  CG  ASP A 125     -55.739  17.324 -20.427  1.00 43.90           C
ANISOU 1004  CG  ASP A 125     3682   4424   8576    319   -245  -1111       C
ATOM   1005  OD1 ASP A 125     -55.591  16.597 -21.432  1.00 45.63           O
ANISOU 1005  OD1 ASP A 125     3851   4606   8880    376   -191  -1235       O
ATOM   1006  OD2 ASP A 125     -55.704  18.571 -20.484  1.00 41.88           O
ANISOU 1006  OD2 ASP A 125     3448   4276   8191    204   -133  -1104       O
ATOM   1007  N   GLY A 126     -54.859  13.634 -20.582  1.00 43.25           N
ANISOU 1007  N   GLY A 126     3450   4018   8966    709   -554  -1265       N
ATOM   1008  CA  GLY A 126     -53.670  12.941 -21.049  1.00 43.60           C
ANISOU 1008  CA  GLY A 126     3355   4079   9132    802   -570  -1431       C
ATOM   1009  C   GLY A 126     -52.586  13.857 -21.577  1.00 46.08           C
ANISOU 1009  C   GLY A 126     3498   4568   9442    745   -431  -1591       C
ATOM   1010  O   GLY A 126     -51.426  13.442 -21.667  1.00 50.33           O
ANISOU 1010  O   GLY A 126     3910   5146  10067    810   -464  -1716       O
ATOM   1011  N   ARG A 127     -52.936  15.095 -21.929  1.00 46.86           N
ANISOU 1011  N   ARG A 127     3597   4772   9437    617   -269  -1592       N
ATOM   1012  CA  ARG A 127     -51.951  16.061 -22.395  1.00 46.99           C
ANISOU 1012  CA  ARG A 127     3480   4951   9423    527   -117  -1732       C
ATOM   1013  C   ARG A 127     -51.024  16.540 -21.286  1.00 50.31           C
ANISOU 1013  C   ARG A 127     3790   5448   9876    528   -229  -1717       C
ATOM   1014  O   ARG A 127     -49.993  17.150 -21.586  1.00 54.28           O
ANISOU 1014  O   ARG A 127     4168   6077  10377    465   -128  -1851       O
ATOM   1015  CB  ARG A 127     -52.661  17.256 -23.031  1.00 46.90           C
ANISOU 1015  CB  ARG A 127     3569   5014   9236    368     81  -1706       C
ATOM   1016  CG  ARG A 127     -53.605  16.876 -24.160  1.00 48.97           C
ANISOU 1016  CG  ARG A 127     3977   5212   9416    353    183  -1716       C
ATOM   1017  CD  ARG A 127     -54.442  18.060 -24.609  1.00 45.51           C
ANISOU 1017  CD  ARG A 127     3714   4832   8744    200    326  -1637       C
ATOM   1018  NE  ARG A 127     -55.316  18.547 -23.546  1.00 42.21           N
ANISOU 1018  NE  ARG A 127     3430   4389   8220    161    221  -1431       N
ATOM   1019  CZ  ARG A 127     -56.222  19.506 -23.708  1.00 39.34           C
ANISOU 1019  CZ  ARG A 127     3233   4054   7662     57    300  -1333       C
ATOM   1020  NH1 ARG A 127     -56.376  20.080 -24.893  1.00 37.03           N
ANISOU 1020  NH1 ARG A 127     3013   3807   7249    -17    472  -1410       N
ATOM   1021  NH2 ARG A 127     -56.976  19.889 -22.687  1.00 40.89           N
ANISOU 1021  NH2 ARG A 127     3532   4228   7778     32    208  -1160       N
ATOM   1022  N   VAL A 128     -51.363  16.283 -20.027  1.00 48.09           N
ANISOU 1022  N   VAL A 128     3562   5092   9616    591   -433  -1560       N
ATOM   1023  CA  VAL A 128     -50.526  16.645 -18.889  1.00 48.41           C
ANISOU 1023  CA  VAL A 128     3515   5195   9682    607   -574  -1538       C
ATOM   1024  C   VAL A 128     -49.741  15.416 -18.457  1.00 52.93           C
ANISOU 1024  C   VAL A 128     4037   5692  10382    774   -766  -1577       C
ATOM   1025  O   VAL A 128     -50.274  14.299 -18.441  1.00 55.82           O
ANISOU 1025  O   VAL A 128     4508   5909  10791    875   -864  -1513       O
ATOM   1026  CB  VAL A 128     -51.378  17.202 -17.732  1.00 46.04           C
ANISOU 1026  CB  VAL A 128     3339   4865   9290    557   -680  -1333       C
ATOM   1027  CG1 VAL A 128     -50.490  17.698 -16.603  1.00 48.98           C
ANISOU 1027  CG1 VAL A 128     3608   5316   9685    560   -821  -1328       C
ATOM   1028  CG2 VAL A 128     -52.289  18.311 -18.232  1.00 45.42           C
ANISOU 1028  CG2 VAL A 128     3415   4841   9000    378   -479  -1266       C
ATOM   1029  N   ASP A 129     -48.470  15.620 -18.111  1.00 54.67           N
ANISOU 1029  N   ASP A 129     4101   6012  10657    799   -818  -1685       N
ATOM   1030  CA  ASP A 129     -47.594  14.508 -17.764  1.00 59.54           C
ANISOU 1030  CA  ASP A 129     4649   6575  11399    964   -994  -1746       C
ATOM   1031  C   ASP A 129     -48.125  13.750 -16.554  1.00 57.40           C
ANISOU 1031  C   ASP A 129     4525   6153  11132   1076  -1247  -1559       C
ATOM   1032  O   ASP A 129     -48.517  14.351 -15.550  1.00 53.40           O
ANISOU 1032  O   ASP A 129     4088   5651  10553   1032  -1342  -1419       O
ATOM   1033  CB  ASP A 129     -46.179  15.017 -17.481  1.00 70.18           C
ANISOU 1033  CB  ASP A 129     5797   8071  12798    962  -1014  -1888       C
ATOM   1034  CG  ASP A 129     -45.486  15.538 -18.724  1.00 79.00           C
ANISOU 1034  CG  ASP A 129     6773   9319  13925    864   -767  -2092       C
ATOM   1035  OD1 ASP A 129     -45.847  15.100 -19.836  1.00 81.89           O
ANISOU 1035  OD1 ASP A 129     7176   9642  14297    857   -626  -2154       O
ATOM   1036  OD2 ASP A 129     -44.574  16.382 -18.589  1.00 83.11           O
ANISOU 1036  OD2 ASP A 129     7153   9984  14442    786   -712  -2193       O
ATOM   1037  N   GLY A 130     -48.141  12.421 -16.660  1.00 60.54           N
ANISOU 1037  N   GLY A 130     4984   6413  11606   1212  -1352  -1557       N
ATOM   1038  CA  GLY A 130     -48.516  11.560 -15.559  1.00 57.21           C
ANISOU 1038  CA  GLY A 130     4722   5833  11183   1322  -1590  -1391       C
ATOM   1039  C   GLY A 130     -50.001  11.381 -15.338  1.00 51.23           C
ANISOU 1039  C   GLY A 130     4192   4936  10336   1268  -1589  -1198       C
ATOM   1040  O   GLY A 130     -50.387  10.545 -14.512  1.00 56.98           O
ANISOU 1040  O   GLY A 130     5089   5512  11051   1346  -1764  -1056       O
ATOM   1041  N   GLN A 131     -50.851  12.129 -16.042  1.00 45.13           N
ANISOU 1041  N   GLN A 131     3442   4209   9497   1136  -1394  -1186       N
ATOM   1042  CA  GLN A 131     -52.288  12.008 -15.821  1.00 42.69           C
ANISOU 1042  CA  GLN A 131     3339   3775   9108   1080  -1388  -1008       C
ATOM   1043  C   GLN A 131     -52.858  10.735 -16.430  1.00 49.19           C
ANISOU 1043  C   GLN A 131     4281   4446   9963   1131  -1381  -1005       C
ATOM   1044  O   GLN A 131     -53.876  10.227 -15.946  1.00 47.15           O
ANISOU 1044  O   GLN A 131     4220   4045   9651   1114  -1442   -846       O
ATOM   1045  CB  GLN A 131     -53.008  13.232 -16.380  1.00 41.59           C
ANISOU 1045  CB  GLN A 131     3180   3735   8888    933  -1188  -1004       C
ATOM   1046  CG  GLN A 131     -52.599  14.530 -15.712  1.00 48.84           C
ANISOU 1046  CG  GLN A 131     4022   4802   9732    845  -1183   -983       C
ATOM   1047  CD  GLN A 131     -53.751  15.213 -15.005  1.00 52.77           C
ANISOU 1047  CD  GLN A 131     4741   5292  10018    704  -1155   -781       C
ATOM   1048  OE1 GLN A 131     -54.846  15.337 -15.553  1.00 46.60           O
ANISOU 1048  OE1 GLN A 131     4089   4484   9134    615  -1021   -724       O
ATOM   1049  NE2 GLN A 131     -53.510  15.658 -13.778  1.00 58.16           N
ANISOU 1049  NE2 GLN A 131     5464   6000  10635    689  -1287   -682       N
ATOM   1050  N   VAL A 132     -52.231  10.211 -17.483  1.00 49.88           N
ANISOU 1050  N   VAL A 132     4259   4563  10130   1180  -1300  -1181       N
ATOM   1051  CA  VAL A 132     -52.645   8.920 -18.023  1.00 47.92           C
ANISOU 1051  CA  VAL A 132     4116   4173   9919   1238  -1313  -1189       C
ATOM   1052  C   VAL A 132     -52.388   7.817 -17.005  1.00 51.68           C
ANISOU 1052  C   VAL A 132     4702   4503  10430   1365  -1539  -1094       C
ATOM   1053  O   VAL A 132     -53.248   6.965 -16.755  1.00 56.10           O
ANISOU 1053  O   VAL A 132     5455   4903  10956   1367  -1595   -973       O
ATOM   1054  CB  VAL A 132     -51.926   8.636 -19.354  1.00 46.59           C
ANISOU 1054  CB  VAL A 132     3800   4075   9826   1268  -1180  -1407       C
ATOM   1055  CG1 VAL A 132     -52.268   7.242 -19.855  1.00 47.23           C
ANISOU 1055  CG1 VAL A 132     3986   4006   9952   1340  -1211  -1421       C
ATOM   1056  CG2 VAL A 132     -52.296   9.682 -20.390  1.00 44.30           C
ANISOU 1056  CG2 VAL A 132     3449   3910   9471   1133   -949  -1487       C
ATOM   1057  N   ASP A 133     -51.200   7.822 -16.395  1.00 49.58           N
ANISOU 1057  N   ASP A 133     4322   4291  10225   1467  -1670  -1148       N
ATOM   1058  CA  ASP A 133     -50.879   6.811 -15.395  1.00 56.39           C
ANISOU 1058  CA  ASP A 133     5299   5017  11110   1600  -1898  -1059       C
ATOM   1059  C   ASP A 133     -51.735   6.979 -14.146  1.00 53.71           C
ANISOU 1059  C   ASP A 133     5173   4584  10652   1548  -2014   -828       C
ATOM   1060  O   ASP A 133     -52.135   5.987 -13.524  1.00 55.05           O
ANISOU 1060  O   ASP A 133     5545   4583  10790   1600  -2139   -704       O
ATOM   1061  CB  ASP A 133     -49.393   6.873 -15.048  1.00 69.60           C
ANISOU 1061  CB  ASP A 133     6787   6787  12872   1721  -2014  -1183       C
ATOM   1062  CG  ASP A 133     -48.970   5.771 -14.098  1.00 84.43           C
ANISOU 1062  CG  ASP A 133     8781   8522  14777   1881  -2256  -1110       C
ATOM   1063  OD1 ASP A 133     -48.975   4.592 -14.512  1.00 89.63           O
ANISOU 1063  OD1 ASP A 133     9507   9054  15493   1975  -2282  -1141       O
ATOM   1064  OD2 ASP A 133     -48.633   6.084 -12.937  1.00 89.24           O
ANISOU 1064  OD2 ASP A 133     9424   9142  15342   1915  -2423  -1020       O
ATOM   1065  N   LEU A 134     -52.023   8.226 -13.760  1.00 56.09           N
ANISOU 1065  N   LEU A 134     5443   4990  10879   1438  -1964   -768       N
ATOM   1066  CA  LEU A 134     -52.931   8.462 -12.642  1.00 56.89           C
ANISOU 1066  CA  LEU A 134     5754   5005  10855   1368  -2046   -549       C
ATOM   1067  C   LEU A 134     -54.321   7.916 -12.930  1.00 54.91           C
ANISOU 1067  C   LEU A 134     5706   4616  10541   1279  -1955   -437       C
ATOM   1068  O   LEU A 134     -55.006   7.443 -12.015  1.00 54.15           O
ANISOU 1068  O   LEU A 134     5839   4385  10352   1253  -2045   -260       O
ATOM   1069  CB  LEU A 134     -53.007   9.958 -12.329  1.00 54.58           C
ANISOU 1069  CB  LEU A 134     5376   4859  10504   1263  -1986   -523       C
ATOM   1070  CG  LEU A 134     -51.821  10.587 -11.592  1.00 56.17           C
ANISOU 1070  CG  LEU A 134     5434   5184  10722   1318  -2116   -575       C
ATOM   1071  CD1 LEU A 134     -51.999  12.093 -11.492  1.00 52.70           C
ANISOU 1071  CD1 LEU A 134     4903   4897  10224   1190  -2017   -565       C
ATOM   1072  CD2 LEU A 134     -51.668   9.972 -10.213  1.00 58.66           C
ANISOU 1072  CD2 LEU A 134     5929   5382  10977   1401  -2362   -427       C
ATOM   1073  N   PHE A 135     -54.752   7.969 -14.192  1.00 50.60           N
ANISOU 1073  N   PHE A 135     5087   4108  10031   1221  -1770   -542       N
ATOM   1074  CA  PHE A 135     -56.055   7.426 -14.554  1.00 47.37           C
ANISOU 1074  CA  PHE A 135     4850   3583   9566   1131  -1681   -461       C
ATOM   1075  C   PHE A 135     -56.079   5.908 -14.440  1.00 48.54           C
ANISOU 1075  C   PHE A 135     5142   3560   9742   1215  -1781   -434       C
ATOM   1076  O   PHE A 135     -57.116   5.331 -14.093  1.00 53.06           O
ANISOU 1076  O   PHE A 135     5923   4001  10238   1141  -1778   -302       O
ATOM   1077  CB  PHE A 135     -56.427   7.869 -15.969  1.00 48.88           C
ANISOU 1077  CB  PHE A 135     4924   3866   9782   1059  -1473   -596       C
ATOM   1078  CG  PHE A 135     -57.654   7.196 -16.513  1.00 50.33           C
ANISOU 1078  CG  PHE A 135     5254   3944   9924    978  -1389   -553       C
ATOM   1079  CD1 PHE A 135     -58.914   7.562 -16.074  1.00 47.67           C
ANISOU 1079  CD1 PHE A 135     5062   3570   9480    843  -1340   -406       C
ATOM   1080  CD2 PHE A 135     -57.547   6.204 -17.473  1.00 51.53           C
ANISOU 1080  CD2 PHE A 135     5392   4042  10144   1029  -1354   -670       C
ATOM   1081  CE1 PHE A 135     -60.046   6.946 -16.577  1.00 47.69           C
ANISOU 1081  CE1 PHE A 135     5181   3495   9446    756  -1261   -383       C
ATOM   1082  CE2 PHE A 135     -58.674   5.585 -17.980  1.00 50.16           C
ANISOU 1082  CE2 PHE A 135     5346   3780   9933    948  -1283   -641       C
ATOM   1083  CZ  PHE A 135     -59.925   5.958 -17.533  1.00 48.25           C
ANISOU 1083  CZ  PHE A 135     5235   3512   9586    808  -1237   -500       C
ATOM   1084  N  AARG A 136     -54.957   5.246 -14.735  0.49 49.82           N
ANISOU 1084  N  AARG A 136     5198   3721  10012   1362  -1858   -563       N
ATOM   1085  N  BARG A 136     -54.953   5.247 -14.718  0.51 49.88           N
ANISOU 1085  N  BARG A 136     5206   3728  10019   1363  -1861   -562       N
ATOM   1086  CA AARG A 136     -54.907   3.793 -14.618  0.49 50.27           C
ANISOU 1086  CA AARG A 136     5396   3604  10101   1460  -1960   -541       C
ATOM   1087  CA BARG A 136     -54.909   3.792 -14.621  0.51 50.24           C
ANISOU 1087  CA BARG A 136     5393   3600  10098   1460  -1959   -542       C
ATOM   1088  C  AARG A 136     -55.083   3.341 -13.175  0.49 51.88           C
ANISOU 1088  C  AARG A 136     5822   3672  10216   1484  -2134   -349       C
ATOM   1089  C  BARG A 136     -55.035   3.318 -13.179  0.51 51.94           C
ANISOU 1089  C  BARG A 136     5826   3680  10228   1491  -2139   -354       C
ATOM   1090  O  AARG A 136     -55.646   2.270 -12.925  0.49 53.36           O
ANISOU 1090  O  AARG A 136     6221   3685  10368   1486  -2173   -259       O
ATOM   1091  O  BARG A 136     -55.518   2.207 -12.935  0.51 53.48           O
ANISOU 1091  O  BARG A 136     6226   3700  10395   1505  -2185   -271       O
ATOM   1092  CB AARG A 136     -53.584   3.261 -15.170  0.49 53.11           C
ANISOU 1092  CB AARG A 136     5584   3999  10597   1625  -2012   -724       C
ATOM   1093  CB BARG A 136     -53.617   3.260 -15.238  0.51 52.26           C
ANISOU 1093  CB BARG A 136     5473   3892  10490   1620  -2002   -729       C
ATOM   1094  CG AARG A 136     -53.324   3.570 -16.634  0.49 51.60           C
ANISOU 1094  CG AARG A 136     5192   3931  10482   1602  -1831   -925       C
ATOM   1095  CG BARG A 136     -53.365   3.727 -16.659  0.51 55.71           C
ANISOU 1095  CG BARG A 136     5702   4470  10997   1587  -1816   -925       C
ATOM   1096  CD AARG A 136     -52.050   2.878 -17.096  0.49 61.64           C
ANISOU 1096  CD AARG A 136     6320   5216  11886   1766  -1885  -1098       C
ATOM   1097  CD BARG A 136     -52.172   3.008 -17.261  0.51 61.20           C
ANISOU 1097  CD BARG A 136     6254   5177  11823   1741  -1849  -1106       C
ATOM   1098  NE AARG A 136     -51.656   3.260 -18.449  0.49 61.82           N
ANISOU 1098  NE AARG A 136     6145   5374  11970   1739  -1704  -1299       N
ATOM   1099  NE BARG A 136     -52.567   2.126 -18.353  0.51 62.56           N
ANISOU 1099  NE BARG A 136     6468   5268  12033   1745  -1749  -1190       N
ATOM   1100  CZ AARG A 136     -52.050   2.629 -19.550  0.49 62.63           C
ANISOU 1100  CZ AARG A 136     6273   5427  12096   1724  -1588  -1384       C
ATOM   1101  CZ BARG A 136     -52.339   2.380 -19.637  0.51 62.60           C
ANISOU 1101  CZ BARG A 136     6322   5380  12083   1715  -1582  -1365       C
ATOM   1102  NH1AARG A 136     -51.634   3.047 -20.738  0.49 62.54           N
ANISOU 1102  NH1AARG A 136     6093   5546  12123   1694  -1422  -1566       N
ATOM   1103  NH1BARG A 136     -52.737   1.520 -20.564  0.51 62.51           N
ANISOU 1103  NH1BARG A 136     6373   5283  12097   1720  -1508  -1433       N
ATOM   1104  NH2AARG A 136     -52.859   1.582 -19.466  0.49 62.38           N
ANISOU 1104  NH2AARG A 136     6446   5214  12042   1731  -1634  -1291       N
ATOM   1105  NH2BARG A 136     -51.703   3.488 -19.995  0.51 61.51           N
ANISOU 1105  NH2BARG A 136     5984   5431  11957   1674  -1485  -1475       N
ATOM   1106  N   ASN A 137     -54.612   4.137 -12.219  1.00 53.23           N
ANISOU 1106  N   ASN A 137     5964   3919  10341   1495  -2236   -286       N
ATOM   1107  CA  ASN A 137     -54.680   3.792 -10.807  1.00 60.73           C
ANISOU 1107  CA  ASN A 137     7132   4755  11187   1519  -2409   -108       C
ATOM   1108  C   ASN A 137     -55.893   4.387 -10.107  1.00 59.09           C
ANISOU 1108  C   ASN A 137     7106   4524  10821   1343  -2345     76       C
ATOM   1109  O   ASN A 137     -56.051   4.190  -8.899  1.00 61.56           O
ANISOU 1109  O   ASN A 137     7624   4749  11018   1334  -2465    234       O
ATOM   1110  CB  ASN A 137     -53.402   4.245 -10.095  1.00 69.18           C
ANISOU 1110  CB  ASN A 137     8077   5919  12288   1641  -2581   -151       C
ATOM   1111  CG  ASN A 137     -52.155   3.619 -10.686  1.00 74.71           C
ANISOU 1111  CG  ASN A 137     8596   6647  13145   1819  -2649   -337       C
ATOM   1112  OD1 ASN A 137     -51.749   2.526 -10.291  1.00 81.65           O
ANISOU 1112  OD1 ASN A 137     9586   7390  14045   1951  -2796   -315       O
ATOM   1113  ND2 ASN A 137     -51.540   4.309 -11.640  1.00 71.12           N
ANISOU 1113  ND2 ASN A 137     7865   6363  12792   1819  -2534   -523       N
ATOM   1114  N   ALA A 138     -56.744   5.108 -10.826  1.00 56.28           N
ANISOU 1114  N   ALA A 138     6687   4246  10451   1202  -2156     56       N
ATOM   1115  CA  ALA A 138     -57.930   5.711 -10.239  1.00 61.86           C
ANISOU 1115  CA  ALA A 138     7548   4944  11015   1028  -2073    214       C
ATOM   1116  C   ALA A 138     -59.100   4.737 -10.281  1.00 59.06           C
ANISOU 1116  C   ALA A 138     7410   4437  10594    930  -1996    303       C
ATOM   1117  O   ALA A 138     -59.244   3.947 -11.218  1.00 57.32           O
ANISOU 1117  O   ALA A 138     7163   4162  10455    956  -1936    209       O
ATOM   1118  CB  ALA A 138     -58.300   7.003 -10.970  1.00 68.09           C
ANISOU 1118  CB  ALA A 138     8164   5891  11817    926  -1907    147       C
ATOM   1119  N   ARG A 139     -59.939   4.801  -9.246  1.00 57.59           N
ANISOU 1119  N   ARG A 139     7442   4186  10252    809  -1990    480       N
ATOM   1120  CA  ARG A 139     -61.109   3.931  -9.184  1.00 55.77           C
ANISOU 1120  CA  ARG A 139     7421   3822   9947    688  -1897    564       C
ATOM   1121  C   ARG A 139     -62.159   4.358 -10.205  1.00 52.15           C
ANISOU 1121  C   ARG A 139     6868   3441   9507    547  -1694    500       C
ATOM   1122  O   ARG A 139     -62.567   3.570 -11.065  1.00 48.84           O
ANISOU 1122  O   ARG A 139     6449   2959   9150    535  -1625    425       O
ATOM   1123  CB  ARG A 139     -61.689   3.935  -7.767  1.00 61.16           C
ANISOU 1123  CB  ARG A 139     8359   4433  10448    584  -1922    759       C
ATOM   1124  CG  ARG A 139     -62.800   2.925  -7.552  1.00 71.13           C
ANISOU 1124  CG  ARG A 139     9854   5543  11630    459  -1827    846       C
ATOM   1125  CD  ARG A 139     -62.802   2.382  -6.132  1.00 80.65           C
ANISOU 1125  CD  ARG A 139    11339   6617  12686    448  -1921   1012       C
ATOM   1126  NE  ARG A 139     -63.469   3.271  -5.186  1.00 82.60           N
ANISOU 1126  NE  ARG A 139    11682   6936  12766    295  -1847   1134       N
ATOM   1127  CZ  ARG A 139     -63.510   3.063  -3.874  1.00 86.88           C
ANISOU 1127  CZ  ARG A 139    12462   7401  13149    262  -1909   1282       C
ATOM   1128  NH1 ARG A 139     -62.914   1.999  -3.351  1.00 88.64           N
ANISOU 1128  NH1 ARG A 139    12852   7464  13362    377  -2058   1331       N
ATOM   1129  NH2 ARG A 139     -64.142   3.919  -3.083  1.00 87.60           N
ANISOU 1129  NH2 ARG A 139    12627   7571  13085    116  -1819   1376       N
ATOM   1130  N   ASN A 140     -62.605   5.609 -10.125  1.00 50.83           N
ANISOU 1130  N   ASN A 140     6623   3409   9281    443  -1601    524       N
ATOM   1131  CA  ASN A 140     -63.543   6.182 -11.079  1.00 47.02           C
ANISOU 1131  CA  ASN A 140     6033   3023   8810    323  -1421    456       C
ATOM   1132  C   ASN A 140     -62.902   7.409 -11.710  1.00 47.72           C
ANISOU 1132  C   ASN A 140     5891   3273   8966    374  -1393    350       C
ATOM   1133  O   ASN A 140     -62.395   8.281 -10.997  1.00 49.82           O
ANISOU 1133  O   ASN A 140     6133   3603   9194    392  -1451    402       O
ATOM   1134  CB  ASN A 140     -64.861   6.560 -10.400  1.00 47.33           C
ANISOU 1134  CB  ASN A 140     6209   3074   8699    130  -1304    583       C
ATOM   1135  CG  ASN A 140     -65.357   5.485  -9.456  1.00 50.76           C
ANISOU 1135  CG  ASN A 140     6900   3348   9039     70  -1332    709       C
ATOM   1136  OD1 ASN A 140     -65.994   4.519  -9.875  1.00 54.95           O
ANISOU 1136  OD1 ASN A 140     7506   3781   9591     18  -1274    686       O
ATOM   1137  ND2 ASN A 140     -65.068   5.650  -8.170  1.00 50.72           N
ANISOU 1137  ND2 ASN A 140     7042   3310   8921     71  -1417    841       N
ATOM   1138  N   GLY A 141     -62.920   7.476 -13.036  1.00 38.62           N
ANISOU 1138  N   GLY A 141     4584   2183   7908    392  -1301    199       N
ATOM   1139  CA  GLY A 141     -62.282   8.586 -13.715  1.00 37.31           C
ANISOU 1139  CA  GLY A 141     4214   2161   7803    438  -1253     84       C
ATOM   1140  C   GLY A 141     -62.631   8.633 -15.184  1.00 40.18           C
ANISOU 1140  C   GLY A 141     4460   2585   8222    418  -1119    -66       C
ATOM   1141  O   GLY A 141     -63.104   7.651 -15.767  1.00 40.92           O
ANISOU 1141  O   GLY A 141     4603   2604   8339    406  -1096   -106       O
ATOM   1142  N   VAL A 142     -62.383   9.800 -15.776  1.00 36.75           N
ANISOU 1142  N   VAL A 142     3883   2302   7778    408  -1027   -148       N
ATOM   1143  CA  VAL A 142     -62.557  10.035 -17.204  1.00 38.75           C
ANISOU 1143  CA  VAL A 142     4028   2643   8051    394   -897   -300       C
ATOM   1144  C   VAL A 142     -61.267  10.637 -17.742  1.00 37.44           C
ANISOU 1144  C   VAL A 142     3688   2601   7935    485   -877   -436       C
ATOM   1145  O   VAL A 142     -60.726  11.581 -17.156  1.00 35.24           O
ANISOU 1145  O   VAL A 142     3359   2436   7594    475   -884   -403       O
ATOM   1146  CB  VAL A 142     -63.752  10.964 -17.492  1.00 41.45           C
ANISOU 1146  CB  VAL A 142     4396   3108   8246    250   -759   -264       C
ATOM   1147  CG1 VAL A 142     -63.790  11.344 -18.965  1.00 41.07           C
ANISOU 1147  CG1 VAL A 142     4248   3161   8195    250   -641   -420       C
ATOM   1148  CG2 VAL A 142     -65.054  10.295 -17.079  1.00 40.29           C
ANISOU 1148  CG2 VAL A 142     4388   2848   8072    151   -760   -162       C
ATOM   1149  N   LEU A 143     -60.775  10.092 -18.852  1.00 37.79           N
ANISOU 1149  N   LEU A 143     3641   2624   8092    563   -845   -598       N
ATOM   1150  CA  LEU A 143     -59.512  10.508 -19.442  1.00 38.60           C
ANISOU 1150  CA  LEU A 143     3567   2835   8263    645   -809   -753       C
ATOM   1151  C   LEU A 143     -59.725  10.950 -20.882  1.00 40.03           C
ANISOU 1151  C   LEU A 143     3690   3118   8400    594   -638   -894       C
ATOM   1152  O   LEU A 143     -60.507  10.341 -21.619  1.00 42.15           O
ANISOU 1152  O   LEU A 143     4026   3316   8672    569   -599   -929       O
ATOM   1153  CB  LEU A 143     -58.484   9.370 -19.393  1.00 40.75           C
ANISOU 1153  CB  LEU A 143     3789   3035   8659    781   -924   -826       C
ATOM   1154  CG  LEU A 143     -57.135   9.613 -20.074  1.00 44.33           C
ANISOU 1154  CG  LEU A 143     4047   3607   9189    857   -877  -1011       C
ATOM   1155  CD1 LEU A 143     -56.383  10.752 -19.402  1.00 45.51           C
ANISOU 1155  CD1 LEU A 143     4080   3878   9334    857   -892  -1002       C
ATOM   1156  CD2 LEU A 143     -56.298   8.343 -20.083  1.00 46.03           C
ANISOU 1156  CD2 LEU A 143     4241   3745   9505    983   -988  -1079       C
ATOM   1157  N   ILE A 144     -59.030  12.014 -21.279  1.00 42.12           N
ANISOU 1157  N   ILE A 144     3842   3546   8616    571   -537   -977       N
ATOM   1158  CA  ILE A 144     -59.004  12.472 -22.661  1.00 40.38           C
ANISOU 1158  CA  ILE A 144     3575   3422   8345    530   -372  -1122       C
ATOM   1159  C   ILE A 144     -57.558  12.500 -23.133  1.00 38.95           C
ANISOU 1159  C   ILE A 144     3216   3306   8278    610   -329  -1298       C
ATOM   1160  O   ILE A 144     -56.652  12.851 -22.369  1.00 37.12           O
ANISOU 1160  O   ILE A 144     2881   3126   8097    645   -388  -1292       O
ATOM   1161  CB  ILE A 144     -59.663  13.858 -22.833  1.00 36.97           C
ANISOU 1161  CB  ILE A 144     3205   3126   7716    397   -254  -1061       C
ATOM   1162  CG1 ILE A 144     -58.906  14.927 -22.041  1.00 38.79           C
ANISOU 1162  CG1 ILE A 144     3370   3466   7901    367   -250  -1020       C
ATOM   1163  CG2 ILE A 144     -61.121  13.811 -22.407  1.00 32.65           C
ANISOU 1163  CG2 ILE A 144     2806   2527   7073    326   -290   -910       C
ATOM   1164  CD1 ILE A 144     -59.212  16.340 -22.483  1.00 33.71           C
ANISOU 1164  CD1 ILE A 144     2771   2956   7079    252   -106  -1013       C
ATOM   1165  N   THR A 145     -57.341  12.106 -24.386  1.00 39.79           N
ANISOU 1165  N   THR A 145     3281   3413   8426    636   -226  -1464       N
ATOM   1166  CA  THR A 145     -56.017  12.130 -24.991  1.00 43.67           C
ANISOU 1166  CA  THR A 145     3619   4000   8974    670   -151  -1637       C
ATOM   1167  C   THR A 145     -56.134  12.575 -26.441  1.00 45.26           C
ANISOU 1167  C   THR A 145     3833   4278   9087    600     49  -1776       C
ATOM   1168  O   THR A 145     -57.216  12.563 -27.033  1.00 41.91           O
ANISOU 1168  O   THR A 145     3540   3812   8574    554     94  -1751       O
ATOM   1169  CB  THR A 145     -55.321  10.760 -24.940  1.00 46.65           C
ANISOU 1169  CB  THR A 145     3955   4296   9474    783   -266  -1693       C
ATOM   1170  OG1 THR A 145     -56.155   9.773 -25.558  1.00 52.55           O
ANISOU 1170  OG1 THR A 145     4823   4932  10210    791   -276  -1692       O
ATOM   1171  CG2 THR A 145     -55.016  10.346 -23.507  1.00 40.14           C
ANISOU 1171  CG2 THR A 145     3128   3399   8723    861   -468  -1568       C
ATOM   1172  N   GLU A 146     -54.995  12.968 -27.008  1.00 52.86           N
ANISOU 1172  N   GLU A 146     4665   5356  10063    586    167  -1928       N
ATOM   1173  CA  GLU A 146     -54.912  13.277 -28.428  1.00 54.13           C
ANISOU 1173  CA  GLU A 146     4846   5586  10134    520    364  -2076       C
ATOM   1174  C   GLU A 146     -54.542  12.067 -29.271  1.00 55.65           C
ANISOU 1174  C   GLU A 146     5023   5730  10391    584    365  -2200       C
ATOM   1175  O   GLU A 146     -54.849  12.043 -30.468  1.00 58.96           O
ANISOU 1175  O   GLU A 146     5518   6165  10720    538    494  -2293       O
ATOM   1176  CB  GLU A 146     -53.886  14.388 -28.673  1.00 56.56           C
ANISOU 1176  CB  GLU A 146     5038   6047  10404    439    524  -2181       C
ATOM   1177  CG  GLU A 146     -54.148  15.673 -27.907  1.00 59.69           C
ANISOU 1177  CG  GLU A 146     5450   6510  10718    358    544  -2068       C
ATOM   1178  CD  GLU A 146     -53.106  16.738 -28.197  1.00 67.36           C
ANISOU 1178  CD  GLU A 146     6312   7630  11652    256    718  -2183       C
ATOM   1179  OE1 GLU A 146     -52.234  16.499 -29.060  1.00 71.79           O
ANISOU 1179  OE1 GLU A 146     6805   8244  12230    237    828  -2345       O
ATOM   1180  OE2 GLU A 146     -53.155  17.812 -27.563  1.00 67.27           O
ANISOU 1180  OE2 GLU A 146     6336   7686  11535    159    725  -2078       O
ATOM   1181  N   GLY A 147     -53.893  11.068 -28.678  1.00 52.74           N
ANISOU 1181  N   GLY A 147     4572   5299  10168    694    221  -2204       N
ATOM   1182  CA  GLY A 147     -53.486   9.885 -29.407  1.00 54.86           C
ANISOU 1182  CA  GLY A 147     4820   5514  10509    769    216  -2324       C
ATOM   1183  C   GLY A 147     -53.850   8.593 -28.706  1.00 55.72           C
ANISOU 1183  C   GLY A 147     4991   5464  10715    878     16  -2228       C
ATOM   1184  O   GLY A 147     -54.715   8.576 -27.824  1.00 54.23           O
ANISOU 1184  O   GLY A 147     4901   5196  10508    871   -101  -2060       O
ATOM   1185  N   SER A 148     -53.187   7.504 -29.084  1.00 58.36           N
ANISOU 1185  N   SER A 148     5276   5749  11150    975    -16  -2336       N
ATOM   1186  CA  SER A 148     -53.532   6.189 -28.568  1.00 61.50           C
ANISOU 1186  CA  SER A 148     5759   5981  11628   1076   -187  -2259       C
ATOM   1187  C   SER A 148     -52.992   5.990 -27.159  1.00 63.30           C
ANISOU 1187  C   SER A 148     5939   6164  11948   1166   -371  -2157       C
ATOM   1188  O   SER A 148     -51.977   6.571 -26.767  1.00 67.21           O
ANISOU 1188  O   SER A 148     6287   6761  12489   1188   -373  -2207       O
ATOM   1189  CB  SER A 148     -52.989   5.093 -29.484  1.00 66.59           C
ANISOU 1189  CB  SER A 148     6376   6579  12344   1158   -153  -2416       C
ATOM   1190  OG  SER A 148     -53.667   5.086 -30.723  1.00 72.53           O
ANISOU 1190  OG  SER A 148     7217   7342  12998   1081    -14  -2490       O
ATOM   1191  N   VAL A 149     -53.686   5.151 -26.397  1.00 63.99           N
ANISOU 1191  N   VAL A 149     6163   6096  12053   1212   -527  -2014       N
ATOM   1192  CA  VAL A 149     -53.250   4.736 -25.072  1.00 66.27           C
ANISOU 1192  CA  VAL A 149     6455   6310  12416   1311   -720  -1907       C
ATOM   1193  C   VAL A 149     -53.132   3.220 -25.089  1.00 68.89           C
ANISOU 1193  C   VAL A 149     6864   6480  12832   1433   -828  -1923       C
ATOM   1194  O   VAL A 149     -54.114   2.518 -25.363  1.00 67.79           O
ANISOU 1194  O   VAL A 149     6881   6219  12656   1401   -831  -1868       O
ATOM   1195  CB  VAL A 149     -54.213   5.210 -23.973  1.00 65.42           C
ANISOU 1195  CB  VAL A 149     6472   6153  12230   1240   -806  -1695       C
ATOM   1196  CG1 VAL A 149     -53.779   4.676 -22.618  1.00 65.07           C
ANISOU 1196  CG1 VAL A 149     6465   6016  12243   1346  -1013  -1581       C
ATOM   1197  CG2 VAL A 149     -54.265   6.724 -23.948  1.00 67.88           C
ANISOU 1197  CG2 VAL A 149     6707   6620  12464   1133   -699  -1686       C
ATOM   1198  N   LYS A 150     -51.930   2.723 -24.811  1.00 73.04           N
ANISOU 1198  N   LYS A 150     7280   7003  13469   1572   -916  -2006       N
ATOM   1199  CA  LYS A 150     -51.661   1.294 -24.893  1.00 77.56           C
ANISOU 1199  CA  LYS A 150     7915   7424  14131   1709  -1011  -2044       C
ATOM   1200  C   LYS A 150     -52.528   0.515 -23.911  1.00 71.87           C
ANISOU 1200  C   LYS A 150     7414   6511  13380   1727  -1169  -1847       C
ATOM   1201  O   LYS A 150     -52.605   0.850 -22.726  1.00 69.22           O
ANISOU 1201  O   LYS A 150     7125   6158  13016   1727  -1290  -1699       O
ATOM   1202  CB  LYS A 150     -50.176   1.039 -24.629  1.00 89.40           C
ANISOU 1202  CB  LYS A 150     9244   8969  15757   1862  -1092  -2161       C
ATOM   1203  CG  LYS A 150     -49.851  -0.272 -23.933  1.00 97.70           C
ANISOU 1203  CG  LYS A 150    10387   9841  16893   2034  -1287  -2112       C
ATOM   1204  CD  LYS A 150     -48.351  -0.379 -23.692  1.00105.00           C
ANISOU 1204  CD  LYS A 150    11116  10837  17943   2186  -1366  -2243       C
ATOM   1205  CE  LYS A 150     -48.018  -1.399 -22.616  1.00110.90           C
ANISOU 1205  CE  LYS A 150    11966  11419  18754   2358  -1603  -2148       C
ATOM   1206  NZ  LYS A 150     -46.555  -1.434 -22.335  1.00113.44           N
ANISOU 1206  NZ  LYS A 150    12081  11821  19198   2512  -1695  -2279       N
ATOM   1207  N   GLY A 151     -53.190  -0.524 -24.414  1.00 69.59           N
ANISOU 1207  N   GLY A 151     7272   6078  13092   1732  -1158  -1847       N
ATOM   1208  CA  GLY A 151     -54.006  -1.382 -23.583  1.00 72.20           C
ANISOU 1208  CA  GLY A 151     7829   6212  13393   1737  -1285  -1675       C
ATOM   1209  C   GLY A 151     -55.392  -0.866 -23.279  1.00 73.27           C
ANISOU 1209  C   GLY A 151     8101   6333  13406   1566  -1245  -1521       C
ATOM   1210  O   GLY A 151     -56.051  -1.405 -22.383  1.00 78.27           O
ANISOU 1210  O   GLY A 151     8919   6818  14000   1547  -1346  -1359       O
ATOM   1211  N   LEU A 152     -55.860   0.157 -23.991  1.00 66.94           N
ANISOU 1211  N   LEU A 152     7221   5676  12537   1438  -1096  -1567       N
ATOM   1212  CA  LEU A 152     -57.176   0.732 -23.749  1.00 58.07           C
ANISOU 1212  CA  LEU A 152     6206   4555  11302   1278  -1052  -1434       C
ATOM   1213  C   LEU A 152     -57.839   1.062 -25.076  1.00 57.28           C
ANISOU 1213  C   LEU A 152     6083   4532  11146   1174   -888  -1542       C
ATOM   1214  O   LEU A 152     -57.243   1.734 -25.923  1.00 55.36           O
ANISOU 1214  O   LEU A 152     5696   4433  10906   1177   -776  -1683       O
ATOM   1215  CB  LEU A 152     -57.078   1.989 -22.877  1.00 55.38           C
ANISOU 1215  CB  LEU A 152     5800   4331  10912   1230  -1071  -1335       C
ATOM   1216  CG  LEU A 152     -56.686   1.763 -21.417  1.00 57.38           C
ANISOU 1216  CG  LEU A 152     6116   4503  11181   1305  -1246  -1192       C
ATOM   1217  CD1 LEU A 152     -56.551   3.090 -20.691  1.00 52.42           C
ANISOU 1217  CD1 LEU A 152     5411   4005  10502   1252  -1249  -1118       C
ATOM   1218  CD2 LEU A 152     -57.705   0.870 -20.726  1.00 59.92           C
ANISOU 1218  CD2 LEU A 152     6677   4638  11454   1259  -1323  -1031       C
ATOM   1219  N   GLN A 153     -59.068   0.591 -25.249  1.00 58.73           N
ANISOU 1219  N   GLN A 153     6420   4622  11275   1077   -873  -1480       N
ATOM   1220  CA  GLN A 153     -59.821   0.869 -26.465  1.00 56.68           C
ANISOU 1220  CA  GLN A 153     6159   4427  10948    976   -739  -1575       C
ATOM   1221  C   GLN A 153     -60.426   2.268 -26.387  1.00 50.27           C
ANISOU 1221  C   GLN A 153     5305   3758  10039    860   -666  -1517       C
ATOM   1222  O   GLN A 153     -61.077   2.600 -25.392  1.00 44.58           O
ANISOU 1222  O   GLN A 153     4652   3011   9277    795   -722  -1358       O
ATOM   1223  CB  GLN A 153     -60.918  -0.173 -26.663  1.00 65.11           C
ANISOU 1223  CB  GLN A 153     7396   5344  11998    910   -760  -1541       C
ATOM   1224  CG  GLN A 153     -61.461  -0.253 -28.079  1.00 74.28           C
ANISOU 1224  CG  GLN A 153     8562   6548  13114    846   -648  -1682       C
ATOM   1225  CD  GLN A 153     -60.524  -0.973 -29.030  1.00 84.59           C
ANISOU 1225  CD  GLN A 153     9819   7833  14487    957   -611  -1858       C
ATOM   1226  OE1 GLN A 153     -59.403  -1.337 -28.669  1.00 86.42           O
ANISOU 1226  OE1 GLN A 153     9988   8036  14810   1090   -664  -1887       O
ATOM   1227  NE2 GLN A 153     -60.984  -1.189 -30.256  1.00 89.44           N
ANISOU 1227  NE2 GLN A 153    10465   8464  15055    906   -524  -1982       N
ATOM   1228  N   PRO A 154     -60.229   3.108 -27.399  1.00 49.91           N
ANISOU 1228  N   PRO A 154     5163   3856   9945    829   -538  -1640       N
ATOM   1229  CA  PRO A 154     -60.659   4.504 -27.308  1.00 48.55           C
ANISOU 1229  CA  PRO A 154     4954   3814   9678    738   -468  -1590       C
ATOM   1230  C   PRO A 154     -62.073   4.736 -27.823  1.00 50.28           C
ANISOU 1230  C   PRO A 154     5269   4040   9794    614   -420  -1565       C
ATOM   1231  O   PRO A 154     -62.666   3.909 -28.518  1.00 53.51           O
ANISOU 1231  O   PRO A 154     5753   4380  10197    589   -416  -1622       O
ATOM   1232  CB  PRO A 154     -59.639   5.225 -28.199  1.00 48.43           C
ANISOU 1232  CB  PRO A 154     4804   3941   9655    770   -346  -1750       C
ATOM   1233  CG  PRO A 154     -59.337   4.221 -29.262  1.00 49.71           C
ANISOU 1233  CG  PRO A 154     4975   4056   9855    821   -309  -1899       C
ATOM   1234  CD  PRO A 154     -59.424   2.856 -28.607  1.00 52.77           C
ANISOU 1234  CD  PRO A 154     5445   4269  10335    889   -447  -1833       C
ATOM   1235  N   SER A 155     -62.602   5.902 -27.458  1.00 45.87           N
ANISOU 1235  N   SER A 155     4704   3567   9156    538   -388  -1483       N
ATOM   1236  CA  SER A 155     -63.870   6.400 -27.976  1.00 42.70           C
ANISOU 1236  CA  SER A 155     4368   3208   8649    427   -339  -1473       C
ATOM   1237  C   SER A 155     -63.634   7.798 -28.524  1.00 36.25           C
ANISOU 1237  C   SER A 155     3495   2538   7739    405   -229  -1531       C
ATOM   1238  O   SER A 155     -63.151   8.675 -27.802  1.00 40.78           O
ANISOU 1238  O   SER A 155     4014   3167   8312    415   -221  -1466       O
ATOM   1239  CB  SER A 155     -64.950   6.420 -26.891  1.00 42.30           C
ANISOU 1239  CB  SER A 155     4391   3100   8580    345   -412  -1302       C
ATOM   1240  OG  SER A 155     -66.160   6.964 -27.387  1.00 42.70           O
ANISOU 1240  OG  SER A 155     4480   3207   8537    243   -370  -1305       O
ATOM   1241  N   VAL A 156     -63.965   8.001 -29.794  1.00 36.29           N
ANISOU 1241  N   VAL A 156     3529   2600   7658    372   -146  -1653       N
ATOM   1242  CA  VAL A 156     -63.722   9.281 -30.450  1.00 45.88           C
ANISOU 1242  CA  VAL A 156     4726   3943   8761    349    -29  -1719       C
ATOM   1243  C   VAL A 156     -64.800  10.271 -30.030  1.00 46.39           C
ANISOU 1243  C   VAL A 156     4846   4054   8726    269    -43  -1606       C
ATOM   1244  O   VAL A 156     -65.998   9.970 -30.095  1.00 50.40           O
ANISOU 1244  O   VAL A 156     5419   4529   9201    211   -100  -1567       O
ATOM   1245  CB  VAL A 156     -63.683   9.110 -31.976  1.00 42.98           C
ANISOU 1245  CB  VAL A 156     4402   3616   8311    343     60  -1887       C
ATOM   1246  CG1 VAL A 156     -63.340  10.429 -32.648  1.00 39.72           C
ANISOU 1246  CG1 VAL A 156     4001   3329   7764    313    194  -1953       C
ATOM   1247  CG2 VAL A 156     -62.677   8.034 -32.359  1.00 43.60           C
ANISOU 1247  CG2 VAL A 156     4427   3648   8490    421     71  -1993       C
ATOM   1248  N   GLY A 157     -64.377  11.457 -29.599  1.00 45.05           N
ANISOU 1248  N   GLY A 157     4646   4001   8470    253     10  -1535       N
ATOM   1249  CA  GLY A 157     -65.291  12.469 -29.127  1.00 37.58           C
ANISOU 1249  CA  GLY A 157     3751   3140   7387    181      0  -1399       C
ATOM   1250  C   GLY A 157     -65.729  13.421 -30.221  1.00 38.41           C
ANISOU 1250  C   GLY A 157     3932   3358   7303    141     82  -1452       C
ATOM   1251  O   GLY A 157     -65.561  13.155 -31.415  1.00 43.05           O
ANISOU 1251  O   GLY A 157     4555   3948   7853    152    136  -1593       O
ATOM   1252  N   PRO A 158     -66.311  14.552 -29.830  1.00 36.17           N
ANISOU 1252  N   PRO A 158     3691   3164   6889     98     88  -1341       N
ATOM   1253  CA  PRO A 158     -66.750  15.538 -30.823  1.00 32.34           C
ANISOU 1253  CA  PRO A 158     3304   2774   6210     72    150  -1377       C
ATOM   1254  C   PRO A 158     -65.566  16.200 -31.508  1.00 32.76           C
ANISOU 1254  C   PRO A 158     3373   2886   6187     74    285  -1466       C
ATOM   1255  O   PRO A 158     -64.437  16.195 -31.012  1.00 33.91           O
ANISOU 1255  O   PRO A 158     3430   3030   6424     87    333  -1479       O
ATOM   1256  CB  PRO A 158     -67.546  16.555 -29.995  1.00 29.10           C
ANISOU 1256  CB  PRO A 158     2923   2425   5707     42    118  -1227       C
ATOM   1257  CG  PRO A 158     -67.814  15.880 -28.680  1.00 29.35           C
ANISOU 1257  CG  PRO A 158     2879   2388   5884     35     33  -1123       C
ATOM   1258  CD  PRO A 158     -66.665  14.953 -28.460  1.00 30.58           C
ANISOU 1258  CD  PRO A 158     2960   2462   6198     74     34  -1179       C
ATOM   1259  N   LYS A 159     -65.845  16.779 -32.677  1.00 32.89           N
ANISOU 1259  N   LYS A 159     3509   2956   6031     56    346  -1534       N
ATOM   1260  CA  LYS A 159     -64.816  17.535 -33.381  1.00 30.95           C
ANISOU 1260  CA  LYS A 159     3311   2768   5680     31    498  -1614       C
ATOM   1261  C   LYS A 159     -64.457  18.815 -32.641  1.00 37.38           C
ANISOU 1261  C   LYS A 159     4137   3647   6419     -8    552  -1507       C
ATOM   1262  O   LYS A 159     -63.313  19.275 -32.720  1.00 43.01           O
ANISOU 1262  O   LYS A 159     4820   4397   7127    -41    676  -1560       O
ATOM   1263  CB  LYS A 159     -65.275  17.869 -34.800  1.00 36.85           C
ANISOU 1263  CB  LYS A 159     4225   3545   6231     15    543  -1699       C
ATOM   1264  CG  LYS A 159     -65.218  16.711 -35.779  1.00 40.28           C
ANISOU 1264  CG  LYS A 159     4663   3926   6716     39    543  -1855       C
ATOM   1265  CD  LYS A 159     -65.516  17.189 -37.192  1.00 46.95           C
ANISOU 1265  CD  LYS A 159     5697   4809   7333     17    601  -1940       C
ATOM   1266  CE  LYS A 159     -65.308  16.083 -38.213  1.00 55.31           C
ANISOU 1266  CE  LYS A 159     6770   5818   8428     33    624  -2114       C
ATOM   1267  NZ  LYS A 159     -66.223  14.931 -37.982  1.00 59.73           N
ANISOU 1267  NZ  LYS A 159     7267   6305   9123     68    464  -2117       N
ATOM   1268  N   GLN A 160     -65.408  19.395 -31.917  1.00 32.52           N
ANISOU 1268  N   GLN A 160     3559   3047   5750    -11    469  -1367       N
ATOM   1269  CA  GLN A 160     -65.240  20.706 -31.311  1.00 34.20           C
ANISOU 1269  CA  GLN A 160     3818   3314   5861    -48    518  -1266       C
ATOM   1270  C   GLN A 160     -64.913  20.592 -29.826  1.00 33.68           C
ANISOU 1270  C   GLN A 160     3624   3235   5937    -49    466  -1168       C
ATOM   1271  O   GLN A 160     -65.235  19.604 -29.162  1.00 32.15           O
ANISOU 1271  O   GLN A 160     3340   2986   5891    -17    363  -1135       O
ATOM   1272  CB  GLN A 160     -66.502  21.554 -31.500  1.00 29.87           C
ANISOU 1272  CB  GLN A 160     3411   2794   5145    -40    464  -1184       C
ATOM   1273  CG  GLN A 160     -67.707  21.092 -30.688  1.00 33.57           C
ANISOU 1273  CG  GLN A 160     3818   3243   5695     -8    322  -1092       C
ATOM   1274  CD  GLN A 160     -68.440  19.922 -31.319  1.00 40.55           C
ANISOU 1274  CD  GLN A 160     4675   4087   6645     20    236  -1168       C
ATOM   1275  OE1 GLN A 160     -68.001  19.366 -32.325  1.00 47.82           O
ANISOU 1275  OE1 GLN A 160     5620   4988   7560     24    274  -1290       O
ATOM   1276  NE2 GLN A 160     -69.568  19.546 -30.728  1.00 42.63           N
ANISOU 1276  NE2 GLN A 160     4888   4340   6969     30    126  -1104       N
ATOM   1277  N   ALA A 161     -64.262  21.634 -29.313  1.00 33.13           N
ANISOU 1277  N   ALA A 161     3565   3212   5810    -93    538  -1121       N
ATOM   1278  CA  ALA A 161     -63.955  21.755 -27.897  1.00 30.42           C
ANISOU 1278  CA  ALA A 161     3129   2867   5560   -101    489  -1022       C
ATOM   1279  C   ALA A 161     -64.064  23.221 -27.507  1.00 31.36           C
ANISOU 1279  C   ALA A 161     3350   3038   5529   -152    543   -936       C
ATOM   1280  O   ALA A 161     -64.174  24.106 -28.360  1.00 34.43           O
ANISOU 1280  O   ALA A 161     3875   3453   5752   -180    629   -962       O
ATOM   1281  CB  ALA A 161     -62.563  21.205 -27.567  1.00 32.08           C
ANISOU 1281  CB  ALA A 161     3189   3073   5926    -97    516  -1098       C
ATOM   1282  N   SER A 162     -64.031  23.477 -26.203  1.00 34.15           N
ANISOU 1282  N   SER A 162     3653   3394   5930   -163    491   -834       N
ATOM   1283  CA  SER A 162     -64.166  24.825 -25.665  1.00 30.79           C
ANISOU 1283  CA  SER A 162     3321   3004   5372   -209    532   -749       C
ATOM   1284  C   SER A 162     -62.788  25.386 -25.340  1.00 29.73           C
ANISOU 1284  C   SER A 162     3134   2906   5256   -276    618   -790       C
ATOM   1285  O   SER A 162     -62.037  24.789 -24.562  1.00 33.79           O
ANISOU 1285  O   SER A 162     3506   3418   5916   -270    567   -799       O
ATOM   1286  CB  SER A 162     -65.050  24.829 -24.419  1.00 32.85           C
ANISOU 1286  CB  SER A 162     3573   3250   5656   -190    432   -617       C
ATOM   1287  OG  SER A 162     -65.064  26.112 -23.817  1.00 34.51           O
ANISOU 1287  OG  SER A 162     3870   3491   5752   -232    475   -546       O
ATOM   1288  N   LEU A 163     -62.463  26.531 -25.933  1.00 30.77           N
ANISOU 1288  N   LEU A 163     3385   3067   5239   -342    742   -819       N
ATOM   1289  CA  LEU A 163     -61.221  27.246 -25.658  1.00 29.77           C
ANISOU 1289  CA  LEU A 163     3220   2981   5110   -433    842   -865       C
ATOM   1290  C   LEU A 163     -61.577  28.641 -25.162  1.00 29.80           C
ANISOU 1290  C   LEU A 163     3376   2988   4959   -488    878   -771       C
ATOM   1291  O   LEU A 163     -62.008  29.491 -25.949  1.00 29.54           O
ANISOU 1291  O   LEU A 163     3529   2941   4755   -509    956   -765       O
ATOM   1292  CB  LEU A 163     -60.334  27.315 -26.900  1.00 30.78           C
ANISOU 1292  CB  LEU A 163     3358   3133   5205   -490    992  -1010       C
ATOM   1293  CG  LEU A 163     -59.046  28.121 -26.734  1.00 32.13           C
ANISOU 1293  CG  LEU A 163     3485   3354   5369   -610   1123  -1079       C
ATOM   1294  CD1 LEU A 163     -58.200  27.543 -25.613  1.00 32.80           C
ANISOU 1294  CD1 LEU A 163     3341   3471   5652   -596   1037  -1096       C
ATOM   1295  CD2 LEU A 163     -58.263  28.159 -28.034  1.00 30.92           C
ANISOU 1295  CD2 LEU A 163     3352   3224   5172   -678   1296  -1230       C
ATOM   1296  N   ASN A 164     -61.398  28.870 -23.860  1.00 29.46           N
ANISOU 1296  N   ASN A 164     3270   2957   4968   -505    817   -699       N
ATOM   1297  CA  ASN A 164     -61.715  30.153 -23.230  1.00 34.83           C
ANISOU 1297  CA  ASN A 164     4087   3632   5513   -554    844   -612       C
ATOM   1298  C   ASN A 164     -63.171  30.541 -23.471  1.00 36.52           C
ANISOU 1298  C   ASN A 164     4463   3810   5603   -484    808   -526       C
ATOM   1299  O   ASN A 164     -63.488  31.699 -23.747  1.00 38.68           O
ANISOU 1299  O   ASN A 164     4917   4064   5716   -509    876   -497       O
ATOM   1300  CB  ASN A 164     -60.772  31.257 -23.714  1.00 37.95           C
ANISOU 1300  CB  ASN A 164     4568   4046   5806   -676   1002   -681       C
ATOM   1301  CG  ASN A 164     -59.314  30.860 -23.617  1.00 36.05           C
ANISOU 1301  CG  ASN A 164     4137   3858   5701   -748   1048   -797       C
ATOM   1302  OD1 ASN A 164     -58.564  30.969 -24.588  1.00 36.51           O
ANISOU 1302  OD1 ASN A 164     4193   3937   5740   -816   1180   -912       O
ATOM   1303  ND2 ASN A 164     -58.905  30.392 -22.444  1.00 31.03           N
ANISOU 1303  ND2 ASN A 164     3341   3247   5201   -731    938   -773       N
ATOM   1304  N   GLY A 165     -64.065  29.561 -23.368  1.00 35.33           N
ANISOU 1304  N   GLY A 165     4248   3646   5532   -393    698   -492       N
ATOM   1305  CA  GLY A 165     -65.470  29.796 -23.624  1.00 32.10           C
ANISOU 1305  CA  GLY A 165     3948   3217   5032   -318    651   -433       C
ATOM   1306  C   GLY A 165     -65.846  29.890 -25.082  1.00 29.94           C
ANISOU 1306  C   GLY A 165     3788   2931   4656   -284    688   -493       C
ATOM   1307  O   GLY A 165     -66.995  30.228 -25.387  1.00 32.70           O
ANISOU 1307  O   GLY A 165     4239   3268   4916   -214    641   -454       O
ATOM   1308  N   VAL A 166     -64.919  29.609 -25.991  1.00 29.48           N
ANISOU 1308  N   VAL A 166     3718   2878   4606   -329    769   -594       N
ATOM   1309  CA  VAL A 166     -65.177  29.645 -27.424  1.00 30.85           C
ANISOU 1309  CA  VAL A 166     4018   3038   4667   -307    811   -660       C
ATOM   1310  C   VAL A 166     -65.161  28.209 -27.925  1.00 26.97           C
ANISOU 1310  C   VAL A 166     3388   2550   4311   -265    757   -738       C
ATOM   1311  O   VAL A 166     -64.111  27.554 -27.929  1.00 31.07           O
ANISOU 1311  O   VAL A 166     3776   3080   4948   -305    802   -816       O
ATOM   1312  CB  VAL A 166     -64.151  30.505 -28.172  1.00 32.66           C
ANISOU 1312  CB  VAL A 166     4374   3263   4771   -407    974   -726       C
ATOM   1313  CG1 VAL A 166     -64.488  30.558 -29.653  1.00 34.22           C
ANISOU 1313  CG1 VAL A 166     4740   3438   4823   -384   1014   -785       C
ATOM   1314  CG2 VAL A 166     -64.102  31.904 -27.580  1.00 31.16           C
ANISOU 1314  CG2 VAL A 166     4326   3056   4460   -461   1029   -650       C
ATOM   1315  N   THR A 167     -66.323  27.715 -28.336  1.00 30.34           N
ANISOU 1315  N   THR A 167     3837   2964   4726   -183    657   -727       N
ATOM   1316  CA  THR A 167     -66.420  26.377 -28.901  1.00 33.31           C
ANISOU 1316  CA  THR A 167     4110   3332   5216   -147    604   -806       C
ATOM   1317  C   THR A 167     -66.058  26.426 -30.380  1.00 37.74           C
ANISOU 1317  C   THR A 167     4789   3889   5661   -162    688   -915       C
ATOM   1318  O   THR A 167     -66.626  27.216 -31.140  1.00 38.31           O
ANISOU 1318  O   THR A 167     5050   3956   5549   -143    699   -904       O
ATOM   1319  CB  THR A 167     -67.828  25.814 -28.711  1.00 31.92           C
ANISOU 1319  CB  THR A 167     3900   3147   5079    -71    464   -761       C
ATOM   1320  OG1 THR A 167     -68.129  25.741 -27.312  1.00 33.69           O
ANISOU 1320  OG1 THR A 167     4025   3373   5404    -73    407   -663       O
ATOM   1321  CG2 THR A 167     -67.931  24.424 -29.317  1.00 25.67           C
ANISOU 1321  CG2 THR A 167     3016   2334   4402    -47    411   -850       C
ATOM   1322  N   LEU A 168     -65.111  25.585 -30.787  1.00 38.64           N
ANISOU 1322  N   LEU A 168     4802   4002   5877   -191    748  -1023       N
ATOM   1323  CA  LEU A 168     -64.598  25.640 -32.147  1.00 36.71           C
ANISOU 1323  CA  LEU A 168     4668   3758   5520   -224    861  -1140       C
ATOM   1324  C   LEU A 168     -63.971  24.303 -32.509  1.00 38.63           C
ANISOU 1324  C   LEU A 168     4760   3993   5926   -213    871  -1264       C
ATOM   1325  O   LEU A 168     -63.578  23.521 -31.638  1.00 41.40           O
ANISOU 1325  O   LEU A 168     4921   4335   6475   -194    819  -1260       O
ATOM   1326  CB  LEU A 168     -63.579  26.774 -32.309  1.00 39.04           C
ANISOU 1326  CB  LEU A 168     5062   4072   5699   -326   1031  -1158       C
ATOM   1327  CG  LEU A 168     -62.397  26.792 -31.330  1.00 41.10           C
ANISOU 1327  CG  LEU A 168     5145   4362   6109   -391   1094  -1170       C
ATOM   1328  CD1 LEU A 168     -61.202  26.009 -31.864  1.00 36.42           C
ANISOU 1328  CD1 LEU A 168     4416   3791   5631   -428   1199  -1327       C
ATOM   1329  CD2 LEU A 168     -61.993  28.219 -30.994  1.00 45.86           C
ANISOU 1329  CD2 LEU A 168     5869   4975   6582   -483   1197  -1115       C
ATOM   1330  N   ILE A 169     -63.882  24.057 -33.812  1.00 37.89           N
ANISOU 1330  N   ILE A 169     4767   3894   5737   -219    936  -1375       N
ATOM   1331  CA  ILE A 169     -63.139  22.922 -34.347  1.00 37.92           C
ANISOU 1331  CA  ILE A 169     4654   3887   5868   -215    985  -1520       C
ATOM   1332  C   ILE A 169     -61.735  23.418 -34.669  1.00 44.86           C
ANISOU 1332  C   ILE A 169     5519   4802   6722   -307   1185  -1617       C
ATOM   1333  O   ILE A 169     -61.542  24.215 -35.592  1.00 47.23           O
ANISOU 1333  O   ILE A 169     6005   5116   6823   -375   1317  -1657       O
ATOM   1334  CB  ILE A 169     -63.824  22.327 -35.582  1.00 35.12           C
ANISOU 1334  CB  ILE A 169     4413   3508   5422   -176    950  -1603       C
ATOM   1335  CG1 ILE A 169     -65.220  21.818 -35.215  1.00 36.58           C
ANISOU 1335  CG1 ILE A 169     4580   3666   5651    -99    752  -1522       C
ATOM   1336  CG2 ILE A 169     -62.982  21.202 -36.165  1.00 35.01           C
ANISOU 1336  CG2 ILE A 169     4291   3478   5534   -174   1021  -1768       C
ATOM   1337  CD1 ILE A 169     -65.968  21.191 -36.369  1.00 39.25           C
ANISOU 1337  CD1 ILE A 169     5017   3985   5911    -62    689  -1608       C
ATOM   1338  N   GLY A 170     -60.754  22.944 -33.907  1.00 45.64           N
ANISOU 1338  N   GLY A 170     5400   4917   7024   -312   1207  -1659       N
ATOM   1339  CA  GLY A 170     -59.427  23.528 -33.967  1.00 32.88           C
ANISOU 1339  CA  GLY A 170     3730   3353   5411   -409   1387  -1745       C
ATOM   1340  C   GLY A 170     -58.740  23.273 -35.298  1.00 39.15           C
ANISOU 1340  C   GLY A 170     4570   4162   6142   -457   1561  -1924       C
ATOM   1341  O   GLY A 170     -58.862  22.203 -35.896  1.00 40.52           O
ANISOU 1341  O   GLY A 170     4703   4307   6386   -392   1531  -2020       O
ATOM   1342  N   GLU A 171     -58.010  24.282 -35.761  1.00 40.65           N
ANISOU 1342  N   GLU A 171     4858   4394   6194   -583   1756  -1972       N
ATOM   1343  CA  GLU A 171     -57.156  24.190 -36.937  1.00 46.01           C
ANISOU 1343  CA  GLU A 171     5573   5100   6808   -663   1970  -2153       C
ATOM   1344  C   GLU A 171     -55.688  24.395 -36.608  1.00 47.13           C
ANISOU 1344  C   GLU A 171     5512   5314   7082   -758   2137  -2273       C
ATOM   1345  O   GLU A 171     -54.837  23.655 -37.110  1.00 53.03           O
ANISOU 1345  O   GLU A 171     6110   6092   7948   -757   2246  -2454       O
ATOM   1346  CB  GLU A 171     -57.595  25.215 -37.991  1.00 55.34           C
ANISOU 1346  CB  GLU A 171     7091   6263   7672   -753   2085  -2124       C
ATOM   1347  CG  GLU A 171     -59.042  25.060 -38.431  1.00 64.17           C
ANISOU 1347  CG  GLU A 171     8411   7322   8650   -654   1913  -2026       C
ATOM   1348  CD  GLU A 171     -59.482  26.147 -39.391  1.00 71.85           C
ANISOU 1348  CD  GLU A 171     9734   8267   9300   -724   1997  -1982       C
ATOM   1349  OE1 GLU A 171     -58.686  27.074 -39.651  1.00 75.29           O
ANISOU 1349  OE1 GLU A 171    10274   8717   9614   -863   2198  -2013       O
ATOM   1350  OE2 GLU A 171     -60.626  26.074 -39.887  1.00 73.41           O
ANISOU 1350  OE2 GLU A 171    10105   8423   9363   -641   1857  -1921       O
ATOM   1351  N   ALA A 172     -55.368  25.386 -35.780  1.00 43.95           N
ANISOU 1351  N   ALA A 172     5092   4942   6666   -838   2159  -2190       N
ATOM   1352  CA  ALA A 172     -54.031  25.555 -35.232  1.00 45.71           C
ANISOU 1352  CA  ALA A 172     5078   5242   7049   -920   2272  -2296       C
ATOM   1353  C   ALA A 172     -53.853  24.828 -33.906  1.00 46.22           C
ANISOU 1353  C   ALA A 172     4864   5316   7379   -802   2072  -2254       C
ATOM   1354  O   ALA A 172     -52.776  24.910 -33.307  1.00 47.53           O
ANISOU 1354  O   ALA A 172     4808   5551   7701   -846   2118  -2337       O
ATOM   1355  CB  ALA A 172     -53.714  27.042 -35.050  1.00 42.14           C
ANISOU 1355  CB  ALA A 172     4764   4814   6435  -1089   2408  -2240       C
ATOM   1356  N   VAL A 173     -54.888  24.129 -33.436  1.00 45.67           N
ANISOU 1356  N   VAL A 173     4811   5180   7361   -660   1850  -2132       N
ATOM   1357  CA  VAL A 173     -54.836  23.372 -32.193  1.00 45.06           C
ANISOU 1357  CA  VAL A 173     4518   5090   7512   -545   1651  -2075       C
ATOM   1358  C   VAL A 173     -55.769  22.178 -32.343  1.00 45.40           C
ANISOU 1358  C   VAL A 173     4581   5050   7619   -403   1490  -2039       C
ATOM   1359  O   VAL A 173     -56.659  22.163 -33.195  1.00 46.24           O
ANISOU 1359  O   VAL A 173     4882   5117   7572   -398   1498  -2016       O
ATOM   1360  CB  VAL A 173     -55.220  24.242 -30.970  1.00 43.84           C
ANISOU 1360  CB  VAL A 173     4402   4938   7317   -573   1545  -1896       C
ATOM   1361  CG1 VAL A 173     -56.727  24.444 -30.904  1.00 38.41           C
ANISOU 1361  CG1 VAL A 173     3930   4182   6481   -525   1423  -1723       C
ATOM   1362  CG2 VAL A 173     -54.681  23.637 -29.678  1.00 49.01           C
ANISOU 1362  CG2 VAL A 173     4812   5604   8204   -495   1391  -1879       C
ATOM   1363  N   LYS A 174     -55.553  21.161 -31.514  1.00 44.22           N
ANISOU 1363  N   LYS A 174     4237   4869   7694   -289   1337  -2038       N
ATOM   1364  CA  LYS A 174     -56.284  19.903 -31.608  1.00 43.44           C
ANISOU 1364  CA  LYS A 174     4138   4680   7688   -164   1192  -2024       C
ATOM   1365  C   LYS A 174     -57.441  19.916 -30.615  1.00 40.72           C
ANISOU 1365  C   LYS A 174     3870   4280   7323   -123   1003  -1819       C
ATOM   1366  O   LYS A 174     -57.229  20.108 -29.413  1.00 39.11           O
ANISOU 1366  O   LYS A 174     3578   4084   7198   -112    909  -1725       O
ATOM   1367  CB  LYS A 174     -55.351  18.722 -31.343  1.00 50.16           C
ANISOU 1367  CB  LYS A 174     4754   5509   8796    -59   1142  -2152       C
ATOM   1368  CG  LYS A 174     -55.762  17.434 -32.034  1.00 60.79           C
ANISOU 1368  CG  LYS A 174     6116   6764  10216     41   1092  -2230       C
ATOM   1369  CD  LYS A 174     -54.547  16.568 -32.327  1.00 66.56           C
ANISOU 1369  CD  LYS A 174     6639   7499  11151    117   1148  -2435       C
ATOM   1370  CE  LYS A 174     -53.547  17.310 -33.203  1.00 69.63           C
ANISOU 1370  CE  LYS A 174     6999   8006  11450     -2   1380  -2582       C
ATOM   1371  NZ  LYS A 174     -52.348  16.484 -33.517  1.00 71.44           N
ANISOU 1371  NZ  LYS A 174     7056   8268  11820     37   1394  -2725       N
ATOM   1372  N   THR A 175     -58.661  19.710 -31.120  1.00 37.00           N
ANISOU 1372  N   THR A 175     3558   3756   6743   -103    948  -1758       N
ATOM   1373  CA  THR A 175     -59.860  19.756 -30.296  1.00 35.14           C
ANISOU 1373  CA  THR A 175     3396   3479   6478    -77    793  -1580       C
ATOM   1374  C   THR A 175     -60.625  18.440 -30.230  1.00 34.58           C
ANISOU 1374  C   THR A 175     3306   3313   6520     10    652  -1567       C
ATOM   1375  O   THR A 175     -61.536  18.321 -29.402  1.00 32.66           O
ANISOU 1375  O   THR A 175     3090   3031   6288     26    525  -1429       O
ATOM   1376  CB  THR A 175     -60.814  20.856 -30.794  1.00 33.63           C
ANISOU 1376  CB  THR A 175     3413   3317   6049   -137    835  -1501       C
ATOM   1377  OG1 THR A 175     -61.054  20.690 -32.196  1.00 38.14           O
ANISOU 1377  OG1 THR A 175     4099   3883   6509   -144    912  -1607       O
ATOM   1378  CG2 THR A 175     -60.219  22.232 -30.546  1.00 33.92           C
ANISOU 1378  CG2 THR A 175     3494   3421   5971   -230    949  -1470       C
ATOM   1379  N   GLN A 176     -60.295  17.457 -31.063  1.00 34.35           N
ANISOU 1379  N   GLN A 176     3235   3242   6574     56    678  -1711       N
ATOM   1380  CA  GLN A 176     -60.959  16.159 -31.046  1.00 35.36           C
ANISOU 1380  CA  GLN A 176     3354   3265   6816    128    552  -1713       C
ATOM   1381  C   GLN A 176     -60.117  15.189 -30.227  1.00 39.38           C
ANISOU 1381  C   GLN A 176     3699   3707   7556    212    473  -1739       C
ATOM   1382  O   GLN A 176     -58.952  14.943 -30.557  1.00 47.62           O
ANISOU 1382  O   GLN A 176     4627   4770   8696    246    551  -1881       O
ATOM   1383  CB  GLN A 176     -61.171  15.635 -32.466  1.00 40.42           C
ANISOU 1383  CB  GLN A 176     4072   3885   7400    133    618  -1859       C
ATOM   1384  CG  GLN A 176     -62.081  14.419 -32.553  1.00 41.62           C
ANISOU 1384  CG  GLN A 176     4250   3927   7635    182    489  -1858       C
ATOM   1385  CD  GLN A 176     -62.515  14.117 -33.975  1.00 46.88           C
ANISOU 1385  CD  GLN A 176     5029   4588   8195    170    542  -1987       C
ATOM   1386  OE1 GLN A 176     -61.838  14.486 -34.935  1.00 52.22           O
ANISOU 1386  OE1 GLN A 176     5739   5319   8782    146    686  -2113       O
ATOM   1387  NE2 GLN A 176     -63.655  13.450 -34.117  1.00 47.91           N
ANISOU 1387  NE2 GLN A 176     5222   4652   8327    175    428  -1961       N
ATOM   1388  N   PHE A 177     -60.701  14.644 -29.165  1.00 36.71           N
ANISOU 1388  N   PHE A 177     3354   3289   7303    246    320  -1608       N
ATOM   1389  CA  PHE A 177     -59.978  13.817 -28.212  1.00 42.84           C
ANISOU 1389  CA  PHE A 177     4010   3989   8278    331    215  -1597       C
ATOM   1390  C   PHE A 177     -60.459  12.373 -28.263  1.00 44.34           C
ANISOU 1390  C   PHE A 177     4224   4028   8594    400    108  -1615       C
ATOM   1391  O   PHE A 177     -61.511  12.053 -28.823  1.00 43.35           O
ANISOU 1391  O   PHE A 177     4204   3862   8404    365     98  -1609       O
ATOM   1392  CB  PHE A 177     -60.137  14.360 -26.786  1.00 40.78           C
ANISOU 1392  CB  PHE A 177     3746   3742   8005    309    122  -1419       C
ATOM   1393  CG  PHE A 177     -59.974  15.848 -26.677  1.00 43.11           C
ANISOU 1393  CG  PHE A 177     4060   4170   8149    222    218  -1375       C
ATOM   1394  CD1 PHE A 177     -58.745  16.444 -26.909  1.00 46.32           C
ANISOU 1394  CD1 PHE A 177     4363   4667   8570    208    321  -1481       C
ATOM   1395  CD2 PHE A 177     -61.047  16.650 -26.326  1.00 43.19           C
ANISOU 1395  CD2 PHE A 177     4190   4211   8008    151    208  -1236       C
ATOM   1396  CE1 PHE A 177     -58.594  17.816 -26.805  1.00 46.21           C
ANISOU 1396  CE1 PHE A 177     4385   4760   8414    113    415  -1442       C
ATOM   1397  CE2 PHE A 177     -60.903  18.022 -26.219  1.00 39.82           C
ANISOU 1397  CE2 PHE A 177     3801   3889   7441     76    294  -1196       C
ATOM   1398  CZ  PHE A 177     -59.675  18.605 -26.458  1.00 41.19           C
ANISOU 1398  CZ  PHE A 177     3890   4138   7622     52    398  -1295       C
ATOM   1399  N   ASN A 178     -59.660  11.498 -27.659  1.00 35.25           N
ANISOU 1399  N   ASN A 178     2976   2789   7627    502     20  -1642       N
ATOM   1400  CA  ASN A 178     -60.066  10.135 -27.355  1.00 36.05           C
ANISOU 1400  CA  ASN A 178     3131   2760   7806    546   -112  -1590       C
ATOM   1401  C   ASN A 178     -60.558  10.087 -25.915  1.00 40.43           C
ANISOU 1401  C   ASN A 178     3732   3239   8390    540   -246  -1402       C
ATOM   1402  O   ASN A 178     -59.907  10.631 -25.017  1.00 35.20           O
ANISOU 1402  O   ASN A 178     3002   2610   7763    568   -283  -1346       O
ATOM   1403  CB  ASN A 178     -58.908   9.155 -27.551  1.00 40.31           C
ANISOU 1403  CB  ASN A 178     3579   3274   8464    645   -142  -1697       C
ATOM   1404  CG  ASN A 178     -58.489   9.031 -29.002  1.00 45.76           C
ANISOU 1404  CG  ASN A 178     4242   4025   9122    643     -6  -1883       C
ATOM   1405  OD1 ASN A 178     -59.292   9.237 -29.911  1.00 50.96           O
ANISOU 1405  OD1 ASN A 178     4992   4700   9671    577     73  -1921       O
ATOM   1406  ND2 ASN A 178     -57.227   8.688 -29.225  1.00 48.54           N
ANISOU 1406  ND2 ASN A 178     4471   4411   9561    714     19  -2003       N
ATOM   1407  N   TYR A 179     -61.698   9.441 -25.696  1.00 38.74           N
ANISOU 1407  N   TYR A 179     3634   2927   8156    496   -313  -1310       N
ATOM   1408  CA  TYR A 179     -62.334   9.404 -24.388  1.00 38.82           C
ANISOU 1408  CA  TYR A 179     3716   2866   8166    462   -415  -1128       C
ATOM   1409  C   TYR A 179     -62.207   8.021 -23.765  1.00 36.03           C
ANISOU 1409  C   TYR A 179     3417   2374   7898    517   -541  -1072       C
ATOM   1410  O   TYR A 179     -62.275   7.003 -24.462  1.00 44.99           O
ANISOU 1410  O   TYR A 179     4581   3445   9070    542   -546  -1153       O
ATOM   1411  CB  TYR A 179     -63.808   9.804 -24.485  1.00 38.35           C
ANISOU 1411  CB  TYR A 179     3752   2815   8003    345   -383  -1055       C
ATOM   1412  CG  TYR A 179     -64.024  11.298 -24.552  1.00 35.02           C
ANISOU 1412  CG  TYR A 179     3317   2572   7415    275   -294  -1014       C
ATOM   1413  CD1 TYR A 179     -64.349  12.023 -23.412  1.00 30.83           C
ANISOU 1413  CD1 TYR A 179     2816   2087   6812    224   -321   -858       C
ATOM   1414  CD2 TYR A 179     -63.893  11.986 -25.751  1.00 34.12           C
ANISOU 1414  CD2 TYR A 179     3182   2571   7209    261   -180  -1132       C
ATOM   1415  CE1 TYR A 179     -64.545  13.390 -23.467  1.00 33.00           C
ANISOU 1415  CE1 TYR A 179     3093   2509   6938    167   -240   -824       C
ATOM   1416  CE2 TYR A 179     -64.086  13.352 -25.815  1.00 34.42           C
ANISOU 1416  CE2 TYR A 179     3236   2750   7090    201   -102  -1089       C
ATOM   1417  CZ  TYR A 179     -64.411  14.049 -24.670  1.00 34.17           C
ANISOU 1417  CZ  TYR A 179     3227   2755   7000    158   -135   -938       C
ATOM   1418  OH  TYR A 179     -64.605  15.408 -24.732  1.00 35.69           O
ANISOU 1418  OH  TYR A 179     3448   3073   7039    106    -59   -900       O
ATOM   1419  N   TYR A 180     -62.017   7.998 -22.448  1.00 36.15           N
ANISOU 1419  N   TYR A 180     3464   2337   7934    535   -644   -934       N
ATOM   1420  CA  TYR A 180     -61.880   6.769 -21.683  1.00 41.60           C
ANISOU 1420  CA  TYR A 180     4239   2883   8682    588   -773   -859       C
ATOM   1421  C   TYR A 180     -62.561   6.965 -20.338  1.00 44.57           C
ANISOU 1421  C   TYR A 180     4731   3206   8999    518   -840   -664       C
ATOM   1422  O   TYR A 180     -62.536   8.066 -19.781  1.00 49.75           O
ANISOU 1422  O   TYR A 180     5354   3941   9606    484   -824   -600       O
ATOM   1423  CB  TYR A 180     -60.405   6.395 -21.476  1.00 39.24           C
ANISOU 1423  CB  TYR A 180     3847   2580   8482    732   -852   -927       C
ATOM   1424  CG  TYR A 180     -59.560   6.455 -22.731  1.00 45.13           C
ANISOU 1424  CG  TYR A 180     4453   3416   9278    791   -760  -1128       C
ATOM   1425  CD1 TYR A 180     -58.957   7.642 -23.131  1.00 46.37           C
ANISOU 1425  CD1 TYR A 180     4475   3728   9417    780   -660  -1213       C
ATOM   1426  CD2 TYR A 180     -59.355   5.323 -23.509  1.00 44.58           C
ANISOU 1426  CD2 TYR A 180     4398   3274   9268    850   -761  -1235       C
ATOM   1427  CE1 TYR A 180     -58.183   7.701 -24.275  1.00 44.95           C
ANISOU 1427  CE1 TYR A 180     4180   3633   9265    815   -555  -1398       C
ATOM   1428  CE2 TYR A 180     -58.579   5.373 -24.652  1.00 44.09           C
ANISOU 1428  CE2 TYR A 180     4216   3295   9239    895   -664  -1420       C
ATOM   1429  CZ  TYR A 180     -57.998   6.564 -25.031  1.00 49.12           C
ANISOU 1429  CZ  TYR A 180     4723   4092   9849    872   -557  -1500       C
ATOM   1430  OH  TYR A 180     -57.226   6.616 -26.170  1.00 55.04           O
ANISOU 1430  OH  TYR A 180     5367   4927  10619    899   -442  -1685       O
ATOM   1431  N   LYS A 181     -63.169   5.900 -19.816  1.00 46.02           N
ANISOU 1431  N   LYS A 181     5059   3251   9176    488   -906   -574       N
ATOM   1432  CA  LYS A 181     -63.893   5.983 -18.556  1.00 44.08           C
ANISOU 1432  CA  LYS A 181     4946   2949   8852    401   -949   -391       C
ATOM   1433  C   LYS A 181     -63.698   4.706 -17.754  1.00 43.80           C
ANISOU 1433  C   LYS A 181     5059   2744   8838    449  -1067   -308       C
ATOM   1434  O   LYS A 181     -63.698   3.605 -18.311  1.00 41.23           O
ANISOU 1434  O   LYS A 181     4779   2319   8566    485  -1080   -375       O
ATOM   1435  CB  LYS A 181     -65.391   6.231 -18.786  1.00 40.37           C
ANISOU 1435  CB  LYS A 181     4532   2506   8300    241   -848   -352       C
ATOM   1436  CG  LYS A 181     -66.175   6.504 -17.511  1.00 37.43           C
ANISOU 1436  CG  LYS A 181     4280   2111   7832    131   -856   -176       C
ATOM   1437  CD  LYS A 181     -67.635   6.808 -17.806  1.00 37.56           C
ANISOU 1437  CD  LYS A 181     4311   2182   7777    -24   -748   -165       C
ATOM   1438  CE  LYS A 181     -68.406   7.087 -16.525  1.00 42.44           C
ANISOU 1438  CE  LYS A 181     5039   2791   8293   -141   -733     -2       C
ATOM   1439  NZ  LYS A 181     -69.848   7.357 -16.785  1.00 47.74           N
ANISOU 1439  NZ  LYS A 181     5701   3530   8907   -289   -626     -6       N
ATOM   1440  N   LYS A 182     -63.532   4.865 -16.442  1.00 41.57           N
ANISOU 1440  N   LYS A 182     4870   2422   8504    448  -1152   -162       N
ATOM   1441  CA  LYS A 182     -63.414   3.753 -15.512  1.00 42.20           C
ANISOU 1441  CA  LYS A 182     5132   2333   8569    484  -1265    -57       C
ATOM   1442  C   LYS A 182     -64.443   3.914 -14.405  1.00 41.91           C
ANISOU 1442  C   LYS A 182     5268   2256   8402    335  -1240    118       C
ATOM   1443  O   LYS A 182     -64.664   5.022 -13.909  1.00 54.22           O
ANISOU 1443  O   LYS A 182     6791   3922   9890    270  -1204    182       O
ATOM   1444  CB  LYS A 182     -62.009   3.671 -14.905  1.00 43.49           C
ANISOU 1444  CB  LYS A 182     5259   2480   8785    652  -1417    -57       C
ATOM   1445  CG  LYS A 182     -60.952   3.136 -15.851  1.00 69.87           C
ANISOU 1445  CG  LYS A 182     8463   5826  12258    806  -1450   -229       C
ATOM   1446  CD  LYS A 182     -59.573   3.165 -15.211  1.00 63.48           C
ANISOU 1446  CD  LYS A 182     7589   5030  11502    967  -1602   -240       C
ATOM   1447  CE  LYS A 182     -59.513   2.276 -13.981  1.00 58.94           C
ANISOU 1447  CE  LYS A 182     7233   4288  10875   1011  -1751    -92       C
ATOM   1448  NZ  LYS A 182     -58.201   2.384 -13.287  1.00 58.06           N
ANISOU 1448  NZ  LYS A 182     7055   4202  10804   1168  -1918   -101       N
ATOM   1449  N   VAL A 183     -65.071   2.805 -14.024  1.00 45.28           N
ANISOU 1449  N   VAL A 183     5886   2526   8791    274  -1246    188       N
ATOM   1450  CA  VAL A 183     -66.057   2.785 -12.949  1.00 48.69           C
ANISOU 1450  CA  VAL A 183     6503   2906   9091    120  -1203    346       C
ATOM   1451  C   VAL A 183     -65.662   1.692 -11.968  1.00 54.41           C
ANISOU 1451  C   VAL A 183     7451   3441   9782    176  -1316    452       C
ATOM   1452  O   VAL A 183     -65.582   0.516 -12.345  1.00 54.37           O
ANISOU 1452  O   VAL A 183     7529   3294   9835    222  -1343    410       O
ATOM   1453  CB  VAL A 183     -67.484   2.553 -13.473  1.00 50.84           C
ANISOU 1453  CB  VAL A 183     6804   3179   9334    -58  -1055    322       C
ATOM   1454  CG1 VAL A 183     -68.434   2.295 -12.316  1.00 51.96           C
ANISOU 1454  CG1 VAL A 183     7153   3243   9346   -219  -1000    472       C
ATOM   1455  CG2 VAL A 183     -67.951   3.751 -14.285  1.00 40.85           C
ANISOU 1455  CG2 VAL A 183     5337   2108   8076   -113   -951    238       C
ATOM   1456  N   ASP A 184     -65.418   2.080 -10.715  1.00 53.62           N
ANISOU 1456  N   ASP A 184     6232   4780   9360    763  -1865    843       N
ATOM   1457  CA  ASP A 184     -65.031   1.150  -9.653  1.00 61.30           C
ANISOU 1457  CA  ASP A 184     7245   5704  10343    818  -2031   1003       C
ATOM   1458  C   ASP A 184     -63.825   0.309 -10.065  1.00 59.79           C
ANISOU 1458  C   ASP A 184     7016   5340  10361    930  -2156    906       C
ATOM   1459  O   ASP A 184     -63.771  -0.900  -9.831  1.00 62.52           O
ANISOU 1459  O   ASP A 184     7419   5568  10767    935  -2257   1013       O
ATOM   1460  CB  ASP A 184     -66.208   0.264  -9.242  1.00 71.85           C
ANISOU 1460  CB  ASP A 184     8677   6985  11640    726  -2060   1249       C
ATOM   1461  CG  ASP A 184     -67.301   1.044  -8.535  1.00 81.52           C
ANISOU 1461  CG  ASP A 184     9926   8412  12636    633  -1958   1362       C
ATOM   1462  OD1 ASP A 184     -66.973   2.025  -7.835  1.00 84.76           O
ANISOU 1462  OD1 ASP A 184    10300   9004  12900    669  -1934   1310       O
ATOM   1463  OD2 ASP A 184     -68.487   0.678  -8.680  1.00 83.68           O
ANISOU 1463  OD2 ASP A 184    10248   8664  12881    526  -1904   1494       O
ATOM   1464  N   GLY A 185     -62.845   0.963 -10.688  1.00 56.74           N
ANISOU 1464  N   GLY A 185     6533   4981  10044    997  -2113    679       N
ATOM   1465  CA  GLY A 185     -61.638   0.305 -11.134  1.00 55.94           C
ANISOU 1465  CA  GLY A 185     6382   4795  10078   1078  -2172    534       C
ATOM   1466  C   GLY A 185     -61.747  -0.422 -12.455  1.00 54.03           C
ANISOU 1466  C   GLY A 185     6147   4434   9947   1042  -2107    428       C
ATOM   1467  O   GLY A 185     -60.716  -0.843 -12.997  1.00 55.53           O
ANISOU 1467  O   GLY A 185     6279   4583  10237   1105  -2128    271       O
ATOM   1468  N   VAL A 186     -62.950  -0.582 -12.997  1.00 52.98           N
ANISOU 1468  N   VAL A 186     6077   4256   9795    944  -2032    501       N
ATOM   1469  CA  VAL A 186     -63.168  -1.320 -14.235  1.00 53.70           C
ANISOU 1469  CA  VAL A 186     6181   4247   9974    908  -1981    406       C
ATOM   1470  C   VAL A 186     -63.313  -0.328 -15.380  1.00 48.90           C
ANISOU 1470  C   VAL A 186     5520   3701   9358    879  -1825    239       C
ATOM   1471  O   VAL A 186     -64.142   0.589 -15.317  1.00 45.25           O
ANISOU 1471  O   VAL A 186     5073   3305   8813    821  -1742    291       O
ATOM   1472  CB  VAL A 186     -64.407  -2.224 -14.133  1.00 54.51           C
ANISOU 1472  CB  VAL A 186     6384   4261  10066    813  -2007    588       C
ATOM   1473  CG1 VAL A 186     -64.665  -2.921 -15.461  1.00 54.76           C
ANISOU 1473  CG1 VAL A 186     6420   4204  10181    780  -1960    470       C
ATOM   1474  CG2 VAL A 186     -64.231  -3.241 -13.015  1.00 55.69           C
ANISOU 1474  CG2 VAL A 186     6591   4346  10224    834  -2159    763       C
ATOM   1475  N   VAL A 187     -62.506  -0.512 -16.426  1.00 46.19           N
ANISOU 1475  N   VAL A 187     5115   3340   9096    921  -1785     42       N
ATOM   1476  CA  VAL A 187     -62.627   0.309 -17.623  1.00 42.81           C
ANISOU 1476  CA  VAL A 187     4644   2969   8653    889  -1635   -111       C
ATOM   1477  C   VAL A 187     -63.972   0.044 -18.283  1.00 47.76           C
ANISOU 1477  C   VAL A 187     5349   3553   9246    794  -1574    -46       C
ATOM   1478  O   VAL A 187     -64.430  -1.103 -18.368  1.00 58.88           O
ANISOU 1478  O   VAL A 187     6814   4862  10694    771  -1642     24       O
ATOM   1479  CB  VAL A 187     -61.467   0.021 -18.590  1.00 46.97           C
ANISOU 1479  CB  VAL A 187     5086   3492   9266    955  -1613   -320       C
ATOM   1480  CG1 VAL A 187     -61.548   0.927 -19.810  1.00 46.99           C
ANISOU 1480  CG1 VAL A 187     5046   3569   9240    920  -1452   -465       C
ATOM   1481  CG2 VAL A 187     -60.132   0.186 -17.881  1.00 50.61           C
ANISOU 1481  CG2 VAL A 187     5463   3995   9770   1047  -1685   -381       C
ATOM   1482  N   GLN A 188     -64.615   1.108 -18.749  1.00 45.93           N
ANISOU 1482  N   GLN A 188     5117   3392   8942    737  -1451    -72       N
ATOM   1483  CA  GLN A 188     -65.918   1.012 -19.386  1.00 49.31           C
ANISOU 1483  CA  GLN A 188     5611   3799   9327    646  -1387    -20       C
ATOM   1484  C   GLN A 188     -65.784   1.137 -20.898  1.00 51.44           C
ANISOU 1484  C   GLN A 188     5853   4084   9608    642  -1286   -198       C
ATOM   1485  O   GLN A 188     -64.867   1.785 -21.407  1.00 58.46           O
ANISOU 1485  O   GLN A 188     6671   5034  10507    687  -1220   -346       O
ATOM   1486  CB  GLN A 188     -66.861   2.097 -18.863  1.00 55.04           C
ANISOU 1486  CB  GLN A 188     6363   4594   9956    583  -1325     86       C
ATOM   1487  CG  GLN A 188     -67.012   2.100 -17.356  1.00 61.49           C
ANISOU 1487  CG  GLN A 188     7202   5420  10741    593  -1420    267       C
ATOM   1488  CD  GLN A 188     -67.547   0.787 -16.826  1.00 66.94           C
ANISOU 1488  CD  GLN A 188     7959   6020  11456    559  -1525    432       C
ATOM   1489  OE1 GLN A 188     -68.710   0.446 -17.039  1.00 69.65           O
ANISOU 1489  OE1 GLN A 188     8355   6333  11775    470  -1501    526       O
ATOM   1490  NE2 GLN A 188     -66.696   0.037 -16.134  1.00 68.05           N
ANISOU 1490  NE2 GLN A 188     8094   6116  11646    625  -1644    467       N
ATOM   1491  N   GLN A 189     -66.710   0.504 -21.611  1.00 49.46           N
ANISOU 1491  N   GLN A 189     5656   3783   9352    587  -1275   -180       N
ATOM   1492  CA  GLN A 189     -66.821   0.650 -23.057  1.00 53.49           C
ANISOU 1492  CA  GLN A 189     6158   4317   9849    577  -1181   -328       C
ATOM   1493  C   GLN A 189     -67.913   1.674 -23.340  1.00 48.75           C
ANISOU 1493  C   GLN A 189     5594   3782   9148    496  -1077   -287       C
ATOM   1494  O   GLN A 189     -69.089   1.435 -23.045  1.00 51.13           O
ANISOU 1494  O   GLN A 189     5952   4057   9417    426  -1098   -159       O
ATOM   1495  CB  GLN A 189     -67.130  -0.686 -23.729  1.00 62.58           C
ANISOU 1495  CB  GLN A 189     7341   5375  11062    578  -1245   -354       C
ATOM   1496  CG  GLN A 189     -67.339  -0.570 -25.233  1.00 72.01           C
ANISOU 1496  CG  GLN A 189     8532   6596  12231    573  -1157   -502       C
ATOM   1497  CD  GLN A 189     -67.469  -1.918 -25.913  1.00 82.96           C
ANISOU 1497  CD  GLN A 189     9940   7889  13694    594  -1233   -556       C
ATOM   1498  OE1 GLN A 189     -67.349  -2.964 -25.275  1.00 85.53           O
ANISOU 1498  OE1 GLN A 189    10279   8119  14099    611  -1353   -486       O
ATOM   1499  NE2 GLN A 189     -67.713  -1.899 -27.218  1.00 86.41           N
ANISOU 1499  NE2 GLN A 189    10381   8347  14105    594  -1170   -683       N
ATOM   1500  N   LEU A 190     -67.523   2.812 -23.901  1.00 44.30           N
ANISOU 1500  N   LEU A 190     4991   3302   8537    503   -967   -392       N
ATOM   1501  CA  LEU A 190     -68.481   3.875 -24.154  1.00 39.71           C
ANISOU 1501  CA  LEU A 190     4444   2782   7862    432   -873   -360       C
ATOM   1502  C   LEU A 190     -69.377   3.507 -25.335  1.00 38.60           C
ANISOU 1502  C   LEU A 190     4350   2626   7689    389   -836   -398       C
ATOM   1503  O   LEU A 190     -68.904   2.934 -26.322  1.00 41.07           O
ANISOU 1503  O   LEU A 190     4648   2918   8038    428   -831   -521       O
ATOM   1504  CB  LEU A 190     -67.755   5.192 -24.421  1.00 40.70           C
ANISOU 1504  CB  LEU A 190     4517   2992   7955    448   -771   -459       C
ATOM   1505  CG  LEU A 190     -66.936   5.712 -23.237  1.00 39.23           C
ANISOU 1505  CG  LEU A 190     4278   2830   7798    490   -808   -430       C
ATOM   1506  CD1 LEU A 190     -66.232   7.014 -23.581  1.00 36.54           C
ANISOU 1506  CD1 LEU A 190     3880   2595   7409    486   -700   -533       C
ATOM   1507  CD2 LEU A 190     -67.818   5.889 -22.009  1.00 37.34           C
ANISOU 1507  CD2 LEU A 190     4083   2618   7485    446   -856   -259       C
ATOM   1508  N   PRO A 191     -70.667   3.820 -25.268  1.00 40.42           N
ANISOU 1508  N   PRO A 191     4632   2869   7855    315   -816   -304       N
ATOM   1509  CA  PRO A 191     -71.600   3.373 -26.304  1.00 44.15           C
ANISOU 1509  CA  PRO A 191     5148   3321   8304    275   -803   -333       C
ATOM   1510  C   PRO A 191     -71.510   4.232 -27.558  1.00 41.96           C
ANISOU 1510  C   PRO A 191     4871   3106   7964    278   -695   -463       C
ATOM   1511  O   PRO A 191     -70.893   5.297 -27.580  1.00 41.16           O
ANISOU 1511  O   PRO A 191     4742   3068   7831    292   -618   -511       O
ATOM   1512  CB  PRO A 191     -72.965   3.532 -25.628  1.00 42.83           C
ANISOU 1512  CB  PRO A 191     5021   3158   8096    194   -819   -179       C
ATOM   1513  CG  PRO A 191     -72.767   4.687 -24.705  1.00 37.83           C
ANISOU 1513  CG  PRO A 191     4367   2587   7420    192   -779   -123       C
ATOM   1514  CD  PRO A 191     -71.348   4.578 -24.202  1.00 36.65           C
ANISOU 1514  CD  PRO A 191     4170   2427   7330    268   -811   -170       C
ATOM   1515  N   GLU A 192     -72.140   3.732 -28.621  1.00 42.33           N
ANISOU 1515  N   GLU A 192     4954   3132   7999    263   -694   -518       N
ATOM   1516  CA  GLU A 192     -72.332   4.539 -29.817  1.00 38.00           C
ANISOU 1516  CA  GLU A 192     4424   2638   7377    255   -600   -617       C
ATOM   1517  C   GLU A 192     -73.151   5.773 -29.471  1.00 34.38           C
ANISOU 1517  C   GLU A 192     3990   2239   6835    194   -543   -533       C
ATOM   1518  O   GLU A 192     -74.188   5.677 -28.809  1.00 40.01           O
ANISOU 1518  O   GLU A 192     4725   2942   7536    143   -584   -415       O
ATOM   1519  CB  GLU A 192     -73.040   3.732 -30.905  1.00 34.33           C
ANISOU 1519  CB  GLU A 192     3998   2133   6913    248   -631   -678       C
ATOM   1520  CG  GLU A 192     -72.178   2.699 -31.602  1.00 35.20           C
ANISOU 1520  CG  GLU A 192     4085   2197   7094    320   -669   -809       C
ATOM   1521  CD  GLU A 192     -72.846   2.146 -32.847  1.00 42.44           C
ANISOU 1521  CD  GLU A 192     5041   3089   7994    319   -684   -900       C
ATOM   1522  OE1 GLU A 192     -73.936   2.640 -33.203  1.00 40.43           O
ANISOU 1522  OE1 GLU A 192     4832   2857   7673    263   -663   -864       O
ATOM   1523  OE2 GLU A 192     -72.281   1.222 -33.469  1.00 50.01           O
ANISOU 1523  OE2 GLU A 192     5984   4007   9010    380   -725  -1016       O
ATOM   1524  N   THR A 193     -72.686   6.935 -29.917  1.00 30.31           N
ANISOU 1524  N   THR A 193     3466   1783   6267    200   -448   -597       N
ATOM   1525  CA  THR A 193     -73.355   8.180 -29.576  1.00 32.05           C
ANISOU 1525  CA  THR A 193     3707   2055   6414    151   -397   -528       C
ATOM   1526  C   THR A 193     -73.257   9.163 -30.731  1.00 35.66           C
ANISOU 1526  C   THR A 193     4187   2588   6774    141   -297   -606       C
ATOM   1527  O   THR A 193     -72.253   9.201 -31.448  1.00 32.60           O
ANISOU 1527  O   THR A 193     3775   2217   6395    175   -244   -712       O
ATOM   1528  CB  THR A 193     -72.762   8.811 -28.309  1.00 29.76           C
ANISOU 1528  CB  THR A 193     3374   1816   6116    156   -393   -462       C
ATOM   1529  OG1 THR A 193     -73.359  10.094 -28.088  1.00 32.45           O
ANISOU 1529  OG1 THR A 193     3734   2247   6348    114   -336   -411       O
ATOM   1530  CG2 THR A 193     -71.259   8.974 -28.441  1.00 29.02           C
ANISOU 1530  CG2 THR A 193     3224   1737   6065    206   -355   -559       C
ATOM   1531  N   TYR A 194     -74.319   9.940 -30.913  1.00 35.76           N
ANISOU 1531  N   TYR A 194     4245   2649   6694     95   -273   -551       N
ATOM   1532  CA  TYR A 194     -74.245  11.136 -31.727  1.00 31.33           C
ANISOU 1532  CA  TYR A 194     3711   2164   6028     79   -182   -586       C
ATOM   1533  C   TYR A 194     -73.661  12.277 -30.899  1.00 31.58           C
ANISOU 1533  C   TYR A 194     3712   2253   6033     68   -138   -545       C
ATOM   1534  O   TYR A 194     -73.520  12.184 -29.677  1.00 32.56           O
ANISOU 1534  O   TYR A 194     3800   2372   6199     74   -180   -487       O
ATOM   1535  CB  TYR A 194     -75.624  11.520 -32.260  1.00 28.68           C
ANISOU 1535  CB  TYR A 194     3437   1849   5612     44   -190   -547       C
ATOM   1536  CG  TYR A 194     -76.227  10.526 -33.228  1.00 31.40           C
ANISOU 1536  CG  TYR A 194     3814   2143   5972     51   -235   -604       C
ATOM   1537  CD1 TYR A 194     -75.875  10.536 -34.572  1.00 30.99           C
ANISOU 1537  CD1 TYR A 194     3792   2113   5868     70   -189   -706       C
ATOM   1538  CD2 TYR A 194     -77.162   9.591 -32.802  1.00 31.82           C
ANISOU 1538  CD2 TYR A 194     3866   2133   6091     34   -325   -555       C
ATOM   1539  CE1 TYR A 194     -76.429   9.633 -35.463  1.00 34.07           C
ANISOU 1539  CE1 TYR A 194     4213   2462   6270     83   -239   -774       C
ATOM   1540  CE2 TYR A 194     -77.722   8.685 -33.686  1.00 34.07           C
ANISOU 1540  CE2 TYR A 194     4178   2363   6404     37   -378   -616       C
ATOM   1541  CZ  TYR A 194     -77.352   8.711 -35.015  1.00 35.64           C
ANISOU 1541  CZ  TYR A 194     4408   2583   6549     67   -338   -734       C
ATOM   1542  OH  TYR A 194     -77.906   7.811 -35.897  1.00 35.89           O
ANISOU 1542  OH  TYR A 194     4468   2565   6606     77   -400   -811       O
ATOM   1543  N   PHE A 195     -73.319  13.367 -31.576  1.00 30.85           N
ANISOU 1543  N   PHE A 195     3636   2214   5869     50    -55   -574       N
ATOM   1544  CA  PHE A 195     -72.792  14.545 -30.906  1.00 28.36           C
ANISOU 1544  CA  PHE A 195     3297   1943   5537     32    -16   -545       C
ATOM   1545  C   PHE A 195     -73.508  15.788 -31.404  1.00 32.07           C
ANISOU 1545  C   PHE A 195     3827   2449   5910     -4     24   -510       C
ATOM   1546  O   PHE A 195     -73.739  15.944 -32.607  1.00 29.84           O
ANISOU 1546  O   PHE A 195     3595   2177   5567    -17     64   -536       O
ATOM   1547  CB  PHE A 195     -71.282  14.690 -31.121  1.00 28.12           C
ANISOU 1547  CB  PHE A 195     3205   1930   5549     43     45   -620       C
ATOM   1548  CG  PHE A 195     -70.471  13.635 -30.430  1.00 29.70           C
ANISOU 1548  CG  PHE A 195     3336   2094   5855     90     -7   -654       C
ATOM   1549  CD1 PHE A 195     -70.513  13.507 -29.052  1.00 26.74           C
ANISOU 1549  CD1 PHE A 195     2931   1707   5522    104    -78   -592       C
ATOM   1550  CD2 PHE A 195     -69.663  12.775 -31.155  1.00 27.84           C
ANISOU 1550  CD2 PHE A 195     3064   1842   5672    127     11   -750       C
ATOM   1551  CE1 PHE A 195     -69.769  12.537 -28.409  1.00 27.27           C
ANISOU 1551  CE1 PHE A 195     2941   1736   5685    152   -137   -613       C
ATOM   1552  CE2 PHE A 195     -68.914  11.803 -30.518  1.00 28.37           C
ANISOU 1552  CE2 PHE A 195     3067   1865   5847    181    -50   -784       C
ATOM   1553  CZ  PHE A 195     -68.967  11.684 -29.144  1.00 32.02           C
ANISOU 1553  CZ  PHE A 195     3507   2306   6353    192   -128   -709       C
ATOM   1554  N   THR A 196     -73.865  16.665 -30.470  1.00 33.67           N
ANISOU 1554  N   THR A 196     4027   2670   6098    -15      5   -452       N
ATOM   1555  CA  THR A 196     -74.409  17.959 -30.838  1.00 31.20           C
ANISOU 1555  CA  THR A 196     3766   2378   5711    -42     33   -423       C
ATOM   1556  C   THR A 196     -73.307  18.841 -31.418  1.00 30.26           C
ANISOU 1556  C   THR A 196     3642   2268   5588    -71    113   -456       C
ATOM   1557  O   THR A 196     -72.119  18.667 -31.135  1.00 29.33           O
ANISOU 1557  O   THR A 196     3459   2153   5530    -70    140   -498       O
ATOM   1558  CB  THR A 196     -75.059  18.635 -29.630  1.00 31.28           C
ANISOU 1558  CB  THR A 196     3765   2406   5713    -34    -14   -371       C
ATOM   1559  OG1 THR A 196     -74.154  18.610 -28.520  1.00 31.28           O
ANISOU 1559  OG1 THR A 196     3699   2415   5772    -21    -27   -382       O
ATOM   1560  CG2 THR A 196     -76.341  17.917 -29.247  1.00 24.15           C
ANISOU 1560  CG2 THR A 196     2870   1510   4795    -20    -77   -326       C
ATOM   1561  N   GLN A 197     -73.717  19.798 -32.247  1.00 30.07           N
ANISOU 1561  N   GLN A 197     3685   2248   5492   -100    147   -432       N
ATOM   1562  CA  GLN A 197     -72.774  20.618 -32.995  1.00 29.59           C
ANISOU 1562  CA  GLN A 197     3631   2196   5416   -144    230   -444       C
ATOM   1563  C   GLN A 197     -72.353  21.885 -32.261  1.00 29.26           C
ANISOU 1563  C   GLN A 197     3571   2138   5411   -173    233   -420       C
ATOM   1564  O   GLN A 197     -71.373  22.516 -32.671  1.00 33.58           O
ANISOU 1564  O   GLN A 197     4100   2686   5974   -221    301   -429       O
ATOM   1565  CB  GLN A 197     -73.371  20.986 -34.356  1.00 32.58           C
ANISOU 1565  CB  GLN A 197     4101   2585   5694   -165    263   -419       C
ATOM   1566  CG  GLN A 197     -73.673  19.780 -35.228  1.00 32.13           C
ANISOU 1566  CG  GLN A 197     4062   2548   5598   -137    263   -464       C
ATOM   1567  CD  GLN A 197     -72.432  18.969 -35.547  1.00 38.64           C
ANISOU 1567  CD  GLN A 197     4820   3399   6463   -132    323   -543       C
ATOM   1568  OE1 GLN A 197     -71.390  19.520 -35.899  1.00 44.46           O
ANISOU 1568  OE1 GLN A 197     5528   4165   7199   -169    406   -556       O
ATOM   1569  NE2 GLN A 197     -72.536  17.652 -35.416  1.00 40.66           N
ANISOU 1569  NE2 GLN A 197     5044   3642   6764    -86    278   -596       N
ATOM   1570  N   SER A 198     -73.068  22.272 -31.202  1.00 26.63           N
ANISOU 1570  N   SER A 198     3237   1791   5091   -147    161   -394       N
ATOM   1571  CA  SER A 198     -72.682  23.400 -30.349  1.00 28.17           C
ANISOU 1571  CA  SER A 198     3407   1966   5329   -162    145   -392       C
ATOM   1572  C   SER A 198     -72.591  24.708 -31.135  1.00 34.41           C
ANISOU 1572  C   SER A 198     4259   2719   6098   -214    184   -359       C
ATOM   1573  O   SER A 198     -71.713  25.537 -30.892  1.00 38.20           O
ANISOU 1573  O   SER A 198     4707   3172   6634   -256    207   -369       O
ATOM   1574  CB  SER A 198     -71.364  23.117 -29.625  1.00 27.95           C
ANISOU 1574  CB  SER A 198     3283   1951   5387   -166    158   -442       C
ATOM   1575  OG  SER A 198     -71.428  21.902 -28.899  1.00 30.69           O
ANISOU 1575  OG  SER A 198     3582   2323   5756   -115    113   -459       O
ATOM   1576  N   ARG A 199     -73.504  24.899 -32.080  1.00 35.40           N
ANISOU 1576  N   ARG A 199     4471   2835   6143   -216    184   -316       N
ATOM   1577  CA  ARG A 199     -73.557  26.137 -32.843  1.00 37.23           C
ANISOU 1577  CA  ARG A 199     4777   3021   6346   -262    207   -265       C
ATOM   1578  C   ARG A 199     -74.535  27.118 -32.197  1.00 42.38           C
ANISOU 1578  C   ARG A 199     5469   3627   7004   -228    122   -243       C
ATOM   1579  O   ARG A 199     -75.243  26.793 -31.241  1.00 44.07           O
ANISOU 1579  O   ARG A 199     5651   3865   7228   -169     57   -268       O
ATOM   1580  CB  ARG A 199     -73.945  25.851 -34.295  1.00 33.58           C
ANISOU 1580  CB  ARG A 199     4395   2581   5785   -277    249   -229       C
ATOM   1581  CG  ARG A 199     -72.875  25.098 -35.072  1.00 33.14           C
ANISOU 1581  CG  ARG A 199     4301   2576   5715   -312    344   -261       C
ATOM   1582  CD  ARG A 199     -73.376  24.618 -36.425  1.00 34.63           C
ANISOU 1582  CD  ARG A 199     4565   2805   5790   -308    374   -247       C
ATOM   1583  NE  ARG A 199     -74.323  23.514 -36.301  1.00 33.60           N
ANISOU 1583  NE  ARG A 199     4435   2694   5639   -242    309   -282       N
ATOM   1584  CZ  ARG A 199     -74.715  22.748 -37.314  1.00 32.25           C
ANISOU 1584  CZ  ARG A 199     4305   2561   5386   -225    319   -303       C
ATOM   1585  NH1 ARG A 199     -74.238  22.962 -38.533  1.00 30.15           N
ANISOU 1585  NH1 ARG A 199     4085   2335   5034   -261    396   -292       N
ATOM   1586  NH2 ARG A 199     -75.583  21.767 -37.109  1.00 32.77           N
ANISOU 1586  NH2 ARG A 199     4364   2630   5456   -173    250   -336       N
ATOM   1587  N   ASN A 200     -74.559  28.342 -32.722  1.00 42.80           N
ANISOU 1587  N   ASN A 200     5591   3617   7055   -266    122   -195       N
ATOM   1588  CA  ASN A 200     -75.465  29.372 -32.236  1.00 43.76           C
ANISOU 1588  CA  ASN A 200     5756   3681   7189   -227     36   -182       C
ATOM   1589  C   ASN A 200     -76.171  30.037 -33.411  1.00 41.15           C
ANISOU 1589  C   ASN A 200     5539   3304   6790   -238     24   -107       C
ATOM   1590  O   ASN A 200     -75.758  29.909 -34.566  1.00 39.24           O
ANISOU 1590  O   ASN A 200     5346   3073   6492   -292     92    -58       O
ATOM   1591  CB  ASN A 200     -74.734  30.427 -31.390  1.00 47.55           C
ANISOU 1591  CB  ASN A 200     6200   4096   7770   -252     14   -208       C
ATOM   1592  CG  ASN A 200     -73.650  31.145 -32.162  1.00 54.08           C
ANISOU 1592  CG  ASN A 200     7051   4864   8634   -352     82   -161       C
ATOM   1593  OD1 ASN A 200     -73.930  32.031 -32.969  1.00 58.52           O
ANISOU 1593  OD1 ASN A 200     7704   5356   9174   -386     76    -89       O
ATOM   1594  ND2 ASN A 200     -72.400  30.774 -31.911  1.00 55.64           N
ANISOU 1594  ND2 ASN A 200     7162   5092   8888   -402    146   -197       N
ATOM   1595  N   LEU A 201     -77.243  30.765 -33.090  1.00 45.22           N
ANISOU 1595  N   LEU A 201     6097   3777   7307   -180    -67   -103       N
ATOM   1596  CA  LEU A 201     -78.120  31.323 -34.117  1.00 46.88           C
ANISOU 1596  CA  LEU A 201     6415   3947   7450   -167   -105    -36       C
ATOM   1597  C   LEU A 201     -77.404  32.367 -34.965  1.00 51.74           C
ANISOU 1597  C   LEU A 201     7110   4474   8075   -248    -71     46       C
ATOM   1598  O   LEU A 201     -77.381  32.274 -36.198  1.00 58.75           O
ANISOU 1598  O   LEU A 201     8073   5375   8875   -287    -27    118       O
ATOM   1599  CB  LEU A 201     -79.363  31.932 -33.467  1.00 44.77           C
ANISOU 1599  CB  LEU A 201     6158   3651   7200    -77   -217    -63       C
ATOM   1600  CG  LEU A 201     -80.449  30.959 -33.018  1.00 42.58           C
ANISOU 1600  CG  LEU A 201     5828   3468   6881     -1   -255   -111       C
ATOM   1601  CD1 LEU A 201     -81.656  31.723 -32.510  1.00 41.70           C
ANISOU 1601  CD1 LEU A 201     5725   3335   6785     86   -359   -138       C
ATOM   1602  CD2 LEU A 201     -80.831  30.056 -34.171  1.00 44.41           C
ANISOU 1602  CD2 LEU A 201     6102   3752   7019    -12   -226    -74       C
ATOM   1603  N   GLN A 202     -76.832  33.384 -34.316  1.00 48.38           N
ANISOU 1603  N   GLN A 202     6669   3959   7752   -277    -94     39       N
ATOM   1604  CA  GLN A 202     -76.230  34.494 -35.048  1.00 59.20           C
ANISOU 1604  CA  GLN A 202     8117   5226   9151   -363    -74    130       C
ATOM   1605  C   GLN A 202     -75.130  34.016 -35.986  1.00 59.73           C
ANISOU 1605  C   GLN A 202     8178   5347   9168   -467     57    183       C
ATOM   1606  O   GLN A 202     -75.016  34.496 -37.119  1.00 62.36           O
ANISOU 1606  O   GLN A 202     8603   5650   9439   -529     93    288       O
ATOM   1607  CB  GLN A 202     -75.678  35.525 -34.064  1.00 72.93           C
ANISOU 1607  CB  GLN A 202     9818   6861  11032   -384   -122     91       C
ATOM   1608  CG  GLN A 202     -76.743  36.317 -33.327  1.00 84.29           C
ANISOU 1608  CG  GLN A 202    11282   8225  12519   -284   -257     45       C
ATOM   1609  CD  GLN A 202     -77.311  37.444 -34.166  1.00 92.77           C
ANISOU 1609  CD  GLN A 202    12486   9172  13592   -289   -325    142       C
ATOM   1610  OE1 GLN A 202     -76.759  37.797 -35.209  1.00 96.49           O
ANISOU 1610  OE1 GLN A 202    13031   9595  14037   -385   -269    255       O
ATOM   1611  NE2 GLN A 202     -78.418  38.020 -33.712  1.00 93.19           N
ANISOU 1611  NE2 GLN A 202    12567   9173  13670   -182   -447     98       N
ATOM   1612  N   GLU A 203     -74.317  33.064 -35.535  1.00 57.04           N
ANISOU 1612  N   GLU A 203     7730   5094   8849   -482    129    112       N
ATOM   1613  CA  GLU A 203     -73.140  32.619 -36.268  1.00 57.91           C
ANISOU 1613  CA  GLU A 203     7806   5265   8932   -573    258    136       C
ATOM   1614  C   GLU A 203     -73.284  31.186 -36.772  1.00 49.15           C
ANISOU 1614  C   GLU A 203     6671   4281   7721   -534    312     95       C
ATOM   1615  O   GLU A 203     -72.300  30.446 -36.838  1.00 51.88           O
ANISOU 1615  O   GLU A 203     6936   4700   8077   -569    401     52       O
ATOM   1616  CB  GLU A 203     -71.899  32.752 -35.388  1.00 71.03           C
ANISOU 1616  CB  GLU A 203     9353   6915  10722   -626    294     77       C
ATOM   1617  CG  GLU A 203     -71.696  34.146 -34.811  1.00 84.82           C
ANISOU 1617  CG  GLU A 203    11114   8527  12587   -666    230     98       C
ATOM   1618  CD  GLU A 203     -71.134  34.120 -33.402  1.00 93.09           C
ANISOU 1618  CD  GLU A 203    12046   9568  13758   -643    190    -12       C
ATOM   1619  OE1 GLU A 203     -71.921  33.946 -32.448  1.00 95.24           O
ANISOU 1619  OE1 GLU A 203    12302   9847  14039   -542     99    -82       O
ATOM   1620  OE2 GLU A 203     -69.903  34.267 -33.248  1.00 95.63           O
ANISOU 1620  OE2 GLU A 203    12287   9887  14162   -726    250    -28       O
ATOM   1621  N   PHE A 204     -74.499  30.781 -37.130  1.00 42.47           N
ANISOU 1621  N   PHE A 204     5889   3459   6787   -460    253    101       N
ATOM   1622  CA  PHE A 204     -74.719  29.418 -37.594  1.00 39.96           C
ANISOU 1622  CA  PHE A 204     5551   3246   6387   -421    286     54       C
ATOM   1623  C   PHE A 204     -74.086  29.218 -38.964  1.00 39.37           C
ANISOU 1623  C   PHE A 204     5517   3233   6208   -485    392     99       C
ATOM   1624  O   PHE A 204     -74.273  30.032 -39.873  1.00 45.62           O
ANISOU 1624  O   PHE A 204     6410   3996   6926   -526    400    196       O
ATOM   1625  CB  PHE A 204     -76.213  29.107 -37.654  1.00 44.39           C
ANISOU 1625  CB  PHE A 204     6165   3814   6888   -334    189     49       C
ATOM   1626  CG  PHE A 204     -76.520  27.644 -37.821  1.00 47.77           C
ANISOU 1626  CG  PHE A 204     6552   4329   7268   -289    198    -18       C
ATOM   1627  CD1 PHE A 204     -76.515  27.056 -39.077  1.00 48.02           C
ANISOU 1627  CD1 PHE A 204     6633   4423   7187   -300    246     -9       C
ATOM   1628  CD2 PHE A 204     -76.812  26.857 -36.720  1.00 46.13           C
ANISOU 1628  CD2 PHE A 204     6260   4141   7128   -237    154    -88       C
ATOM   1629  CE1 PHE A 204     -76.794  25.712 -39.229  1.00 45.42           C
ANISOU 1629  CE1 PHE A 204     6268   4159   6830   -257    242    -82       C
ATOM   1630  CE2 PHE A 204     -77.094  25.512 -36.868  1.00 44.18           C
ANISOU 1630  CE2 PHE A 204     5978   3953   6854   -203    153   -141       C
ATOM   1631  CZ  PHE A 204     -77.085  24.940 -38.123  1.00 44.75           C
ANISOU 1631  CZ  PHE A 204     6099   4073   6830   -212    193   -144       C
ATOM   1632  N   LYS A 205     -73.337  28.126 -39.110  1.00 36.34           N
ANISOU 1632  N   LYS A 205     5056   2938   5815   -490    471     29       N
ATOM   1633  CA  LYS A 205     -72.687  27.790 -40.365  1.00 45.22           C
ANISOU 1633  CA  LYS A 205     6200   4148   6834   -538    582     45       C
ATOM   1634  C   LYS A 205     -73.014  26.337 -40.708  1.00 39.79           C
ANISOU 1634  C   LYS A 205     5487   3546   6084   -468    581    -47       C
ATOM   1635  O   LYS A 205     -72.901  25.458 -39.837  1.00 36.39           O
ANISOU 1635  O   LYS A 205     4967   3120   5740   -421    553   -135       O
ATOM   1636  CB  LYS A 205     -71.167  27.993 -40.281  1.00 54.07           C
ANISOU 1636  CB  LYS A 205     7229   5295   8020   -624    696     35       C
ATOM   1637  CG  LYS A 205     -70.748  29.265 -39.558  1.00 59.99           C
ANISOU 1637  CG  LYS A 205     7966   5941   8886   -689    676     92       C
ATOM   1638  CD  LYS A 205     -69.623  29.979 -40.286  1.00 66.84           C
ANISOU 1638  CD  LYS A 205     8825   6827   9742   -812    797    165       C
ATOM   1639  CE  LYS A 205     -70.109  30.555 -41.605  1.00 70.07           C
ANISOU 1639  CE  LYS A 205     9373   7247  10003   -853    823    288       C
ATOM   1640  NZ  LYS A 205     -71.254  31.487 -41.406  1.00 67.96           N
ANISOU 1640  NZ  LYS A 205     9222   6856   9744   -821    694    367       N
ATOM   1641  N   PRO A 206     -73.418  26.050 -41.941  1.00 39.02           N
ANISOU 1641  N   PRO A 206     5470   3514   5843   -459    602    -30       N
ATOM   1642  CA  PRO A 206     -73.745  24.666 -42.300  1.00 39.71           C
ANISOU 1642  CA  PRO A 206     5535   3671   5880   -392    590   -131       C
ATOM   1643  C   PRO A 206     -72.496  23.805 -42.389  1.00 44.41           C
ANISOU 1643  C   PRO A 206     6026   4342   6504   -404    692   -224       C
ATOM   1644  O   PRO A 206     -71.426  24.259 -42.802  1.00 46.49           O
ANISOU 1644  O   PRO A 206     6262   4653   6750   -474    804   -200       O
ATOM   1645  CB  PRO A 206     -74.424  24.807 -43.667  1.00 33.29           C
ANISOU 1645  CB  PRO A 206     4844   2911   4895   -385    586    -83       C
ATOM   1646  CG  PRO A 206     -73.835  26.054 -44.238  1.00 43.44           C
ANISOU 1646  CG  PRO A 206     6187   4194   6124   -474    662     36       C
ATOM   1647  CD  PRO A 206     -73.602  26.977 -43.071  1.00 40.42           C
ANISOU 1647  CD  PRO A 206     5765   3699   5892   -509    631     83       C
ATOM   1648  N   ARG A 207     -72.644  22.539 -41.993  1.00 42.22           N
ANISOU 1648  N   ARG A 207     5687   4076   6280   -335    650   -332       N
ATOM   1649  CA  ARG A 207     -71.532  21.596 -41.978  1.00 38.17           C
ANISOU 1649  CA  ARG A 207     5068   3620   5814   -324    723   -438       C
ATOM   1650  C   ARG A 207     -71.789  20.383 -42.867  1.00 37.71           C
ANISOU 1650  C   ARG A 207     5023   3630   5675   -263    720   -539       C
ATOM   1651  O   ARG A 207     -71.110  19.362 -42.727  1.00 38.86           O
ANISOU 1651  O   ARG A 207     5081   3803   5883   -224    742   -650       O
ATOM   1652  CB  ARG A 207     -71.226  21.160 -40.544  1.00 37.69           C
ANISOU 1652  CB  ARG A 207     4905   3496   5920   -296    670   -483       C
ATOM   1653  CG  ARG A 207     -70.699  22.289 -39.672  1.00 42.20           C
ANISOU 1653  CG  ARG A 207     5442   4016   6578   -355    683   -415       C
ATOM   1654  CD  ARG A 207     -70.515  21.861 -38.225  1.00 43.63           C
ANISOU 1654  CD  ARG A 207     5533   4143   6903   -318    616   -457       C
ATOM   1655  NE  ARG A 207     -69.962  22.943 -37.414  1.00 45.20           N
ANISOU 1655  NE  ARG A 207     5694   4298   7182   -370    624   -411       N
ATOM   1656  CZ  ARG A 207     -69.833  22.901 -36.092  1.00 45.15           C
ANISOU 1656  CZ  ARG A 207     5623   4247   7286   -346    560   -431       C
ATOM   1657  NH1 ARG A 207     -70.223  21.828 -35.418  1.00 46.41           N
ANISOU 1657  NH1 ARG A 207     5748   4398   7486   -276    489   -479       N
ATOM   1658  NH2 ARG A 207     -69.317  23.935 -35.442  1.00 45.08           N
ANISOU 1658  NH2 ARG A 207     5583   4200   7345   -394    563   -401       N
ATOM   1659  N   SER A 208     -72.754  20.476 -43.779  1.00 33.21           N
ANISOU 1659  N   SER A 208     4561   3084   4973   -247    682   -510       N
ATOM   1660  CA  SER A 208     -73.010  19.414 -44.741  1.00 33.91           C
ANISOU 1660  CA  SER A 208     4671   3243   4970   -190    675   -613       C
ATOM   1661  C   SER A 208     -73.781  20.002 -45.911  1.00 34.76           C
ANISOU 1661  C   SER A 208     4908   3402   4898   -200    668   -547       C
ATOM   1662  O   SER A 208     -74.445  21.034 -45.782  1.00 46.43           O
ANISOU 1662  O   SER A 208     6460   4828   6352   -230    624   -426       O
ATOM   1663  CB  SER A 208     -73.789  18.251 -44.117  1.00 35.61           C
ANISOU 1663  CB  SER A 208     4856   3388   5284   -119    553   -693       C
ATOM   1664  OG  SER A 208     -75.154  18.589 -43.934  1.00 39.04           O
ANISOU 1664  OG  SER A 208     5366   3764   5704   -108    444   -624       O
ATOM   1665  N   GLN A 209     -73.684  19.327 -47.060  1.00 35.96           N
ANISOU 1665  N   GLN A 209     5085   3657   4920   -167    703   -634       N
ATOM   1666  CA  GLN A 209     -74.423  19.771 -48.239  1.00 36.95           C
ANISOU 1666  CA  GLN A 209     5337   3847   4855   -166    687   -581       C
ATOM   1667  C   GLN A 209     -75.925  19.760 -47.990  1.00 43.93           C
ANISOU 1667  C   GLN A 209     6288   4647   5757   -124    530   -550       C
ATOM   1668  O   GLN A 209     -76.651  20.600 -48.533  1.00 45.29           O
ANISOU 1668  O   GLN A 209     6566   4824   5818   -136    491   -449       O
ATOM   1669  CB  GLN A 209     -74.076  18.892 -49.442  1.00 42.04           C
ANISOU 1669  CB  GLN A 209     5988   4627   5358   -122    741   -709       C
ATOM   1670  CG  GLN A 209     -74.729  19.330 -50.745  1.00 44.71           C
ANISOU 1670  CG  GLN A 209     6459   5058   5473   -118    731   -659       C
ATOM   1671  CD  GLN A 209     -74.175  20.642 -51.268  1.00 48.64           C
ANISOU 1671  CD  GLN A 209     7017   5617   5846   -207    844   -501       C
ATOM   1672  OE1 GLN A 209     -72.965  20.871 -51.246  1.00 50.37           O
ANISOU 1672  OE1 GLN A 209     7166   5895   6076   -264    983   -493       O
ATOM   1673  NE2 GLN A 209     -75.060  21.513 -51.741  1.00 49.33           N
ANISOU 1673  NE2 GLN A 209     7234   5688   5823   -221    780   -372       N
ATOM   1674  N   MET A 210     -76.406  18.823 -47.170  1.00 34.91           N
ANISOU 1674  N   MET A 210     5081   3427   4755    -76    437   -631       N
ATOM   1675  CA  MET A 210     -77.818  18.817 -46.806  1.00 42.83           C
ANISOU 1675  CA  MET A 210     6123   4354   5794    -45    296   -600       C
ATOM   1676  C   MET A 210     -78.187  20.076 -46.031  1.00 46.89           C
ANISOU 1676  C   MET A 210     6662   4795   6359    -83    271   -460       C
ATOM   1677  O   MET A 210     -79.225  20.694 -46.292  1.00 46.50           O
ANISOU 1677  O   MET A 210     6690   4726   6250    -71    191   -392       O
ATOM   1678  CB  MET A 210     -78.143  17.565 -45.992  1.00 39.74           C
ANISOU 1678  CB  MET A 210     5647   3895   5557     -4    215   -700       C
ATOM   1679  CG  MET A 210     -79.602  17.447 -45.591  1.00 43.58           C
ANISOU 1679  CG  MET A 210     6152   4316   6090     20     77   -675       C
ATOM   1680  SD  MET A 210     -79.913  16.039 -44.509  1.00 48.54           S
ANISOU 1680  SD  MET A 210     6675   4856   6911     45     -7   -758       S
ATOM   1681  CE  MET A 210     -79.455  14.679 -45.580  1.00 47.48           C
ANISOU 1681  CE  MET A 210     6536   4769   6735     91     -2   -927       C
ATOM   1682  N   GLU A 211     -77.343  20.474 -45.075  1.00 51.26           N
ANISOU 1682  N   GLU A 211     7145   5306   7025   -123    331   -426       N
ATOM   1683  CA  GLU A 211     -77.589  21.713 -44.346  1.00 32.03           C
ANISOU 1683  CA  GLU A 211     4730   2798   4640   -157    309   -309       C
ATOM   1684  C   GLU A 211     -77.465  22.923 -45.261  1.00 41.53           C
ANISOU 1684  C   GLU A 211     6038   4030   5712   -202    355   -200       C
ATOM   1685  O   GLU A 211     -78.234  23.883 -45.136  1.00 43.93           O
ANISOU 1685  O   GLU A 211     6408   4276   6007   -202    286   -107       O
ATOM   1686  CB  GLU A 211     -76.623  21.834 -43.168  1.00 31.30           C
ANISOU 1686  CB  GLU A 211     4537   2662   4692   -189    361   -311       C
ATOM   1687  CG  GLU A 211     -76.815  20.782 -42.094  1.00 39.02           C
ANISOU 1687  CG  GLU A 211     5423   3599   5805   -148    302   -388       C
ATOM   1688  CD  GLU A 211     -76.063  21.111 -40.821  1.00 41.42           C
ANISOU 1688  CD  GLU A 211     5643   3856   6241   -173    326   -371       C
ATOM   1689  OE1 GLU A 211     -75.098  21.900 -40.885  1.00 44.27           O
ANISOU 1689  OE1 GLU A 211     5994   4226   6600   -225    410   -334       O
ATOM   1690  OE2 GLU A 211     -76.444  20.587 -39.753  1.00 43.91           O
ANISOU 1690  OE2 GLU A 211     5899   4127   6658   -143    260   -393       O
ATOM   1691  N   ILE A 212     -76.499  22.899 -46.182  1.00 39.25           N
ANISOU 1691  N   ILE A 212     5762   3831   5320   -239    471   -207       N
ATOM   1692  CA  ILE A 212     -76.372  23.979 -47.155  1.00 39.18           C
ANISOU 1692  CA  ILE A 212     5859   3859   5167   -291    521    -88       C
ATOM   1693  C   ILE A 212     -77.631  24.070 -48.006  1.00 40.00           C
ANISOU 1693  C   ILE A 212     6080   3981   5138   -241    418    -58       C
ATOM   1694  O   ILE A 212     -78.164  25.161 -48.239  1.00 42.50           O
ANISOU 1694  O   ILE A 212     6492   4251   5405   -257    370     65       O
ATOM   1695  CB  ILE A 212     -75.116  23.773 -48.022  1.00 47.34           C
ANISOU 1695  CB  ILE A 212     6871   5016   6099   -340    675   -112       C
ATOM   1696  CG1 ILE A 212     -73.853  23.851 -47.163  1.00 48.48           C
ANISOU 1696  CG1 ILE A 212     6894   5140   6386   -395    772   -131       C
ATOM   1697  CG2 ILE A 212     -75.062  24.803 -49.141  1.00 48.78           C
ANISOU 1697  CG2 ILE A 212     7175   5254   6107   -397    727     24       C
ATOM   1698  CD1 ILE A 212     -72.575  23.591 -47.931  1.00 48.94           C
ANISOU 1698  CD1 ILE A 212     6902   5330   6363   -440    930   -171       C
ATOM   1699  N   ASP A 213     -78.132  22.925 -48.474  1.00 41.63           N
ANISOU 1699  N   ASP A 213     6279   4246   5293   -175    371   -176       N
ATOM   1700  CA  ASP A 213     -79.366  22.926 -49.251  1.00 41.79           C
ANISOU 1700  CA  ASP A 213     6398   4286   5196   -122    258   -165       C
ATOM   1701  C   ASP A 213     -80.568  23.300 -48.395  1.00 40.32           C
ANISOU 1701  C   ASP A 213     6211   3988   5120    -86    120   -128       C
ATOM   1702  O   ASP A 213     -81.512  23.920 -48.896  1.00 40.85           O
ANISOU 1702  O   ASP A 213     6371   4043   5105    -59     29    -60       O
ATOM   1703  CB  ASP A 213     -79.579  21.561 -49.903  1.00 44.00           C
ANISOU 1703  CB  ASP A 213     6657   4647   5414    -63    233   -318       C
ATOM   1704  CG  ASP A 213     -78.540  21.253 -50.963  1.00 49.82           C
ANISOU 1704  CG  ASP A 213     7408   5521   6000    -81    363   -365       C
ATOM   1705  OD1 ASP A 213     -77.706  22.137 -51.252  1.00 50.74           O
ANISOU 1705  OD1 ASP A 213     7554   5676   6048   -149    476   -262       O
ATOM   1706  OD2 ASP A 213     -78.558  20.129 -51.507  1.00 52.08           O
ANISOU 1706  OD2 ASP A 213     7672   5877   6238    -29    352   -510       O
ATOM   1707  N   PHE A 214     -80.554  22.939 -47.109  1.00 38.77           N
ANISOU 1707  N   PHE A 214     5909   3717   5104    -82    100   -171       N
ATOM   1708  CA  PHE A 214     -81.668  23.294 -46.236  1.00 38.85           C
ANISOU 1708  CA  PHE A 214     5905   3642   5215    -48    -18   -142       C
ATOM   1709  C   PHE A 214     -81.815  24.804 -46.118  1.00 41.96           C
ANISOU 1709  C   PHE A 214     6370   3974   5601    -70    -36     -9       C
ATOM   1710  O   PHE A 214     -82.932  25.333 -46.158  1.00 47.85           O
ANISOU 1710  O   PHE A 214     7165   4682   6334    -26   -147     32       O
ATOM   1711  CB  PHE A 214     -81.478  22.667 -44.855  1.00 35.81           C
ANISOU 1711  CB  PHE A 214     5394   3205   5007    -47    -18   -201       C
ATOM   1712  CG  PHE A 214     -82.519  23.083 -43.854  1.00 34.14           C
ANISOU 1712  CG  PHE A 214     5152   2925   4895    -17   -119   -172       C
ATOM   1713  CD1 PHE A 214     -83.740  22.432 -43.793  1.00 32.20           C
ANISOU 1713  CD1 PHE A 214     4884   2683   4667     32   -225   -221       C
ATOM   1714  CD2 PHE A 214     -82.278  24.127 -42.976  1.00 34.76           C
ANISOU 1714  CD2 PHE A 214     5217   2939   5050    -37   -108   -103       C
ATOM   1715  CE1 PHE A 214     -84.698  22.815 -42.875  1.00 34.81           C
ANISOU 1715  CE1 PHE A 214     5173   2971   5083     60   -308   -199       C
ATOM   1716  CE2 PHE A 214     -83.232  24.514 -42.057  1.00 33.95           C
ANISOU 1716  CE2 PHE A 214     5081   2790   5030      0   -196    -91       C
ATOM   1717  CZ  PHE A 214     -84.444  23.858 -42.006  1.00 34.57           C
ANISOU 1717  CZ  PHE A 214     5131   2888   5117     49   -291   -137       C
ATOM   1718  N   LEU A 215     -80.698  25.514 -45.972  1.00 41.98           N
ANISOU 1718  N   LEU A 215     6373   3957   5619   -136     67     56       N
ATOM   1719  CA  LEU A 215     -80.748  26.963 -45.827  1.00 43.63           C
ANISOU 1719  CA  LEU A 215     6650   4085   5842   -165     47    182       C
ATOM   1720  C   LEU A 215     -80.994  27.664 -47.156  1.00 46.01           C
ANISOU 1720  C   LEU A 215     7093   4417   5972   -175     34    284       C
ATOM   1721  O   LEU A 215     -81.658  28.706 -47.186  1.00 47.56           O
ANISOU 1721  O   LEU A 215     7368   4536   6167   -159    -52    378       O
ATOM   1722  CB  LEU A 215     -79.449  27.464 -45.196  1.00 44.22           C
ANISOU 1722  CB  LEU A 215     6670   4124   6009   -243    155    214       C
ATOM   1723  CG  LEU A 215     -79.150  26.895 -43.807  1.00 44.59           C
ANISOU 1723  CG  LEU A 215     6583   4138   6222   -232    159    126       C
ATOM   1724  CD1 LEU A 215     -77.730  27.229 -43.378  1.00 44.90           C
ANISOU 1724  CD1 LEU A 215     6562   4166   6334   -310    273    140       C
ATOM   1725  CD2 LEU A 215     -80.159  27.419 -42.796  1.00 40.74           C
ANISOU 1725  CD2 LEU A 215     6080   3564   5835   -180     42    134       C
ATOM   1726  N   GLU A 216     -80.480  27.113 -48.256  1.00 49.28           N
ANISOU 1726  N   GLU A 216     7542   4944   6237   -196    114    266       N
ATOM   1727  CA  GLU A 216     -80.639  27.762 -49.552  1.00 56.58           C
ANISOU 1727  CA  GLU A 216     8607   5916   6975   -210    111    374       C
ATOM   1728  C   GLU A 216     -82.016  27.496 -50.149  1.00 57.54           C
ANISOU 1728  C   GLU A 216     8798   6060   7005   -120    -33    349       C
ATOM   1729  O   GLU A 216     -82.697  28.425 -50.595  1.00 60.96           O
ANISOU 1729  O   GLU A 216     9341   6450   7373   -101   -121    458       O
ATOM   1730  CB  GLU A 216     -79.545  27.294 -50.513  1.00 66.00           C
ANISOU 1730  CB  GLU A 216     9808   7246   8025   -265    260    359       C
ATOM   1731  CG  GLU A 216     -78.151  27.798 -50.176  1.00 77.08           C
ANISOU 1731  CG  GLU A 216    11158   8638   9489   -368    407    416       C
ATOM   1732  CD  GLU A 216     -77.108  27.342 -51.181  1.00 86.35           C
ANISOU 1732  CD  GLU A 216    12328   9970  10510   -417    561    396       C
ATOM   1733  OE1 GLU A 216     -77.360  26.348 -51.897  1.00 87.88           O
ANISOU 1733  OE1 GLU A 216    12527  10279  10586   -358    556    288       O
ATOM   1734  OE2 GLU A 216     -76.036  27.980 -51.259  1.00 88.42           O
ANISOU 1734  OE2 GLU A 216    12577  10246  10774   -516    686    482       O
ATOM   1735  N   LEU A 217     -82.441  26.236 -50.164  1.00 55.03           N
ANISOU 1735  N   LEU A 217     8415   5803   6690    -64    -68    204       N
ATOM   1736  CA  LEU A 217     -83.679  25.866 -50.830  1.00 54.43           C
ANISOU 1736  CA  LEU A 217     8394   5765   6524     15   -201    163       C
ATOM   1737  C   LEU A 217     -84.890  26.217 -49.968  1.00 54.71           C
ANISOU 1737  C   LEU A 217     8398   5698   6692     72   -345    166       C
ATOM   1738  O   LEU A 217     -84.778  26.542 -48.782  1.00 55.11           O
ANISOU 1738  O   LEU A 217     8373   5661   6907     57   -338    174       O
ATOM   1739  CB  LEU A 217     -83.687  24.374 -51.157  1.00 51.38           C
ANISOU 1739  CB  LEU A 217     7944   5469   6108     48   -193     -1       C
ATOM   1740  CG  LEU A 217     -82.513  23.840 -51.976  1.00 49.23           C
ANISOU 1740  CG  LEU A 217     7679   5316   5710     10    -51    -46       C
ATOM   1741  CD1 LEU A 217     -82.629  22.334 -52.145  1.00 44.27           C
ANISOU 1741  CD1 LEU A 217     6978   4748   5094     58    -71   -229       C
ATOM   1742  CD2 LEU A 217     -82.441  24.534 -53.327  1.00 51.53           C
ANISOU 1742  CD2 LEU A 217     8114   5699   5767     -1    -30     56       C
ATOM   1743  N   ALA A 218     -86.064  26.146 -50.589  1.00 55.21           N
ANISOU 1743  N   ALA A 218     8516   5785   6677    141   -478    151       N
ATOM   1744  CA  ALA A 218     -87.320  26.333 -49.885  1.00 55.72           C
ANISOU 1744  CA  ALA A 218     8535   5779   6856    206   -619    131       C
ATOM   1745  C   ALA A 218     -87.758  25.025 -49.229  1.00 58.08           C
ANISOU 1745  C   ALA A 218     8701   6099   7270    227   -645    -15       C
ATOM   1746  O   ALA A 218     -87.176  23.960 -49.451  1.00 63.35           O
ANISOU 1746  O   ALA A 218     9326   6824   7918    204   -577   -105       O
ATOM   1747  CB  ALA A 218     -88.399  26.844 -50.838  1.00 55.15           C
ANISOU 1747  CB  ALA A 218     8571   5725   6659    273   -759    179       C
ATOM   1748  N   MET A 219     -88.810  25.115 -48.413  1.00 54.61           N
ANISOU 1748  N   MET A 219     8190   5607   6952    272   -749    -39       N
ATOM   1749  CA  MET A 219     -89.261  23.953 -47.651  1.00 51.22           C
ANISOU 1749  CA  MET A 219     7627   5187   6649    279   -773   -154       C
ATOM   1750  C   MET A 219     -89.757  22.844 -48.572  1.00 50.08           C
ANISOU 1750  C   MET A 219     7486   5115   6426    303   -833   -255       C
ATOM   1751  O   MET A 219     -89.301  21.699 -48.482  1.00 48.86           O
ANISOU 1751  O   MET A 219     7271   4985   6311    276   -783   -347       O
ATOM   1752  CB  MET A 219     -90.354  24.366 -46.667  1.00 51.25           C
ANISOU 1752  CB  MET A 219     7553   5141   6779    321   -868   -150       C
ATOM   1753  CG  MET A 219     -90.922  23.212 -45.861  1.00 54.03           C
ANISOU 1753  CG  MET A 219     7764   5507   7258    317   -895   -248       C
ATOM   1754  SD  MET A 219     -92.080  23.758 -44.594  1.00 55.54           S
ANISOU 1754  SD  MET A 219     7847   5668   7590    360   -976   -241       S
ATOM   1755  CE  MET A 219     -93.397  24.426 -45.607  1.00 57.67           C
ANISOU 1755  CE  MET A 219     8188   5957   7769    445  -1136   -230       C
ATOM   1756  N   ASP A 220     -90.696  23.168 -49.464  1.00 55.46           N
ANISOU 1756  N   ASP A 220     8241   5829   7002    360   -952   -246       N
ATOM   1757  CA  ASP A 220     -91.244  22.156 -50.362  1.00 60.38           C
ANISOU 1757  CA  ASP A 220     8868   6523   7551    389  -1028   -354       C
ATOM   1758  C   ASP A 220     -90.170  21.592 -51.282  1.00 61.85           C
ANISOU 1758  C   ASP A 220     9120   6780   7602    361   -930   -394       C
ATOM   1759  O   ASP A 220     -90.168  20.393 -51.585  1.00 62.57           O
ANISOU 1759  O   ASP A 220     9166   6909   7698    363   -942   -521       O
ATOM   1760  CB  ASP A 220     -92.392  22.746 -51.179  1.00 67.76           C
ANISOU 1760  CB  ASP A 220     9878   7484   8385    460  -1179   -328       C
ATOM   1761  CG  ASP A 220     -93.614  23.048 -50.335  1.00 72.76           C
ANISOU 1761  CG  ASP A 220    10418   8068   9159    500  -1292   -331       C
ATOM   1762  OD1 ASP A 220     -93.673  22.576 -49.180  1.00 72.50           O
ANISOU 1762  OD1 ASP A 220    10255   7998   9292    469  -1257   -369       O
ATOM   1763  OD2 ASP A 220     -94.515  23.759 -50.828  1.00 75.34           O
ANISOU 1763  OD2 ASP A 220    10799   8401   9427    566  -1416   -295       O
ATOM   1764  N   GLU A 221     -89.246  22.441 -51.735  1.00 62.34           N
ANISOU 1764  N   GLU A 221     9280   6860   7546    334   -833   -291       N
ATOM   1765  CA  GLU A 221     -88.197  21.976 -52.636  1.00 63.60           C
ANISOU 1765  CA  GLU A 221     9494   7109   7562    308   -725   -328       C
ATOM   1766  C   GLU A 221     -87.186  21.104 -51.902  1.00 55.90           C
ANISOU 1766  C   GLU A 221     8413   6117   6709    260   -604   -407       C
ATOM   1767  O   GLU A 221     -86.663  20.137 -52.470  1.00 54.26           O
ANISOU 1767  O   GLU A 221     8194   5978   6445    263   -560   -518       O
ATOM   1768  CB  GLU A 221     -87.508  23.173 -53.290  1.00 72.95           C
ANISOU 1768  CB  GLU A 221    10805   8321   8590    279   -649   -179       C
ATOM   1769  CG  GLU A 221     -86.555  22.813 -54.415  1.00 83.21           C
ANISOU 1769  CG  GLU A 221    12172   9746   9696    258   -542   -207       C
ATOM   1770  CD  GLU A 221     -85.972  24.039 -55.091  1.00 91.62           C
ANISOU 1770  CD  GLU A 221    13367  10844  10602    218   -470    -36       C
ATOM   1771  OE1 GLU A 221     -86.227  25.162 -54.606  1.00 93.54           O
ANISOU 1771  OE1 GLU A 221    13644  10988  10908    204   -505    101       O
ATOM   1772  OE2 GLU A 221     -85.261  23.882 -56.106  1.00 95.72           O
ANISOU 1772  OE2 GLU A 221    13950  11487  10930    200   -380    -38       O
ATOM   1773  N   PHE A 222     -86.902  21.424 -50.638  1.00 51.77           N
ANISOU 1773  N   PHE A 222     7810   5505   6354    224   -558   -358       N
ATOM   1774  CA  PHE A 222     -85.938  20.639 -49.873  1.00 51.18           C
ANISOU 1774  CA  PHE A 222     7635   5409   6402    183   -455   -423       C
ATOM   1775  C   PHE A 222     -86.504  19.275 -49.499  1.00 51.84           C
ANISOU 1775  C   PHE A 222     7621   5473   6602    205   -528   -558       C
ATOM   1776  O   PHE A 222     -85.807  18.259 -49.601  1.00 51.85           O
ANISOU 1776  O   PHE A 222     7579   5495   6627    198   -474   -659       O
ATOM   1777  CB  PHE A 222     -85.514  21.406 -48.621  1.00 49.51           C
ANISOU 1777  CB  PHE A 222     7372   5113   6327    143   -399   -333       C
ATOM   1778  CG  PHE A 222     -84.559  20.653 -47.742  1.00 50.72           C
ANISOU 1778  CG  PHE A 222     7419   5241   6610    107   -307   -391       C
ATOM   1779  CD1 PHE A 222     -83.204  20.636 -48.025  1.00 53.40           C
ANISOU 1779  CD1 PHE A 222     7763   5621   6904     68   -173   -394       C
ATOM   1780  CD2 PHE A 222     -85.014  19.965 -46.628  1.00 50.00           C
ANISOU 1780  CD2 PHE A 222     7221   5091   6686    112   -356   -438       C
ATOM   1781  CE1 PHE A 222     -82.320  19.945 -47.217  1.00 52.74           C
ANISOU 1781  CE1 PHE A 222     7580   5513   6946     44   -100   -452       C
ATOM   1782  CE2 PHE A 222     -84.136  19.272 -45.818  1.00 49.29           C
ANISOU 1782  CE2 PHE A 222     7041   4974   6712     84   -284   -483       C
ATOM   1783  CZ  PHE A 222     -82.787  19.262 -46.112  1.00 48.97           C
ANISOU 1783  CZ  PHE A 222     7007   4967   6631     55   -161   -494       C
ATOM   1784  N   ILE A 223     -87.764  19.234 -49.058  1.00 48.26           N
ANISOU 1784  N   ILE A 223     7128   4978   6230    231   -653   -560       N
ATOM   1785  CA  ILE A 223     -88.376  17.967 -48.671  1.00 44.26           C
ANISOU 1785  CA  ILE A 223     6525   4444   5848    237   -728   -672       C
ATOM   1786  C   ILE A 223     -88.500  17.038 -49.872  1.00 44.36           C
ANISOU 1786  C   ILE A 223     6576   4518   5759    269   -778   -797       C
ATOM   1787  O   ILE A 223     -88.360  15.816 -49.741  1.00 46.24           O
ANISOU 1787  O   ILE A 223     6748   4733   6087    262   -791   -910       O
ATOM   1788  CB  ILE A 223     -89.739  18.228 -47.999  1.00 40.82           C
ANISOU 1788  CB  ILE A 223     6032   3969   5510    253   -844   -640       C
ATOM   1789  CG1 ILE A 223     -89.546  19.041 -46.716  1.00 37.54           C
ANISOU 1789  CG1 ILE A 223     5565   3498   5200    228   -790   -541       C
ATOM   1790  CG2 ILE A 223     -90.458  16.922 -47.695  1.00 38.54           C
ANISOU 1790  CG2 ILE A 223     5642   3654   5346    246   -927   -744       C
ATOM   1791  CD1 ILE A 223     -90.834  19.389 -46.009  1.00 34.77           C
ANISOU 1791  CD1 ILE A 223     5148   3126   4937    250   -889   -514       C
ATOM   1792  N   GLU A 224     -88.742  17.595 -51.061  1.00 49.01           N
ANISOU 1792  N   GLU A 224     7278   5185   6160    305   -813   -781       N
ATOM   1793  CA  GLU A 224     -88.827  16.766 -52.258  1.00 52.88           C
ANISOU 1793  CA  GLU A 224     7812   5752   6530    343   -861   -911       C
ATOM   1794  C   GLU A 224     -87.459  16.223 -52.654  1.00 52.66           C
ANISOU 1794  C   GLU A 224     7793   5773   6441    331   -730   -980       C
ATOM   1795  O   GLU A 224     -87.338  15.057 -53.046  1.00 53.59           O
ANISOU 1795  O   GLU A 224     7880   5907   6575    352   -757  -1132       O
ATOM   1796  CB  GLU A 224     -89.437  17.564 -53.410  1.00 57.23           C
ANISOU 1796  CB  GLU A 224     8486   6384   6876    390   -935   -864       C
ATOM   1797  CG  GLU A 224     -89.437  16.829 -54.740  1.00 65.88           C
ANISOU 1797  CG  GLU A 224     9643   7582   7806    436   -979   -997       C
ATOM   1798  CD  GLU A 224     -89.869  17.711 -55.894  1.00 77.38           C
ANISOU 1798  CD  GLU A 224    11237   9134   9031    480  -1036   -929       C
ATOM   1799  OE1 GLU A 224     -90.205  18.889 -55.649  1.00 80.17           O
ANISOU 1799  OE1 GLU A 224    11637   9456   9369    476  -1052   -776       O
ATOM   1800  OE2 GLU A 224     -89.870  17.228 -57.046  1.00 81.60           O
ANISOU 1800  OE2 GLU A 224    11836   9774   9396    523  -1072  -1030       O
ATOM   1801  N   ARG A 225     -86.418  17.054 -52.554  1.00 53.21           N
ANISOU 1801  N   ARG A 225     7899   5866   6451    297   -591   -878       N
ATOM   1802  CA  ARG A 225     -85.091  16.637 -52.999  1.00 57.13           C
ANISOU 1802  CA  ARG A 225     8398   6433   6877    286   -456   -942       C
ATOM   1803  C   ARG A 225     -84.562  15.475 -52.168  1.00 54.65           C
ANISOU 1803  C   ARG A 225     7963   6047   6753    276   -430  -1052       C
ATOM   1804  O   ARG A 225     -83.985  14.525 -52.710  1.00 57.25           O
ANISOU 1804  O   ARG A 225     8275   6423   7054    303   -402  -1193       O
ATOM   1805  CB  ARG A 225     -84.123  17.818 -52.943  1.00 61.13           C
ANISOU 1805  CB  ARG A 225     8950   6968   7307    237   -314   -796       C
ATOM   1806  CG  ARG A 225     -82.675  17.442 -53.214  1.00 66.63           C
ANISOU 1806  CG  ARG A 225     9619   7737   7958    216   -158   -855       C
ATOM   1807  CD  ARG A 225     -81.825  18.672 -53.470  1.00 71.22           C
ANISOU 1807  CD  ARG A 225    10262   8373   8424    160    -26   -706       C
ATOM   1808  NE  ARG A 225     -82.357  19.466 -54.572  1.00 80.02           N
ANISOU 1808  NE  ARG A 225    11513   9569   9324    173    -64   -619       N
ATOM   1809  CZ  ARG A 225     -81.769  20.550 -55.066  1.00 87.33           C
ANISOU 1809  CZ  ARG A 225    12520  10553  10110    124     34   -476       C
ATOM   1810  NH1 ARG A 225     -80.620  20.974 -54.558  1.00 87.71           N
ANISOU 1810  NH1 ARG A 225    12518  10588  10219     54    178   -413       N
ATOM   1811  NH2 ARG A 225     -82.330  21.210 -56.070  1.00 90.91           N
ANISOU 1811  NH2 ARG A 225    13103  11074  10364    141    -18   -391       N
ATOM   1812  N   TYR A 226     -84.749  15.528 -50.852  1.00 49.89           N
ANISOU 1812  N   TYR A 226     7278   5333   6344    242   -442   -991       N
ATOM   1813  CA  TYR A 226     -84.254  14.492 -49.958  1.00 48.12           C
ANISOU 1813  CA  TYR A 226     6946   5031   6306    229   -424  -1067       C
ATOM   1814  C   TYR A 226     -85.328  13.480 -49.581  1.00 52.18           C
ANISOU 1814  C   TYR A 226     7399   5466   6961    240   -566  -1144       C
ATOM   1815  O   TYR A 226     -85.128  12.700 -48.644  1.00 54.31           O
ANISOU 1815  O   TYR A 226     7579   5648   7408    220   -571  -1171       O
ATOM   1816  CB  TYR A 226     -83.644  15.129 -48.708  1.00 45.26           C
ANISOU 1816  CB  TYR A 226     6528   4607   6060    180   -340   -952       C
ATOM   1817  CG  TYR A 226     -82.358  15.874 -48.996  1.00 43.49           C
ANISOU 1817  CG  TYR A 226     6335   4448   5739    156   -190   -900       C
ATOM   1818  CD1 TYR A 226     -81.124  15.256 -48.838  1.00 40.80           C
ANISOU 1818  CD1 TYR A 226     5934   4120   5449    152    -93   -975       C
ATOM   1819  CD2 TYR A 226     -82.379  17.189 -49.444  1.00 43.22           C
ANISOU 1819  CD2 TYR A 226     6389   4462   5570    136   -151   -777       C
ATOM   1820  CE1 TYR A 226     -79.947  15.930 -49.107  1.00 41.45           C
ANISOU 1820  CE1 TYR A 226     6029   4271   5449    122     48   -931       C
ATOM   1821  CE2 TYR A 226     -81.207  17.870 -49.717  1.00 42.60           C
ANISOU 1821  CE2 TYR A 226     6334   4441   5411     99    -12   -720       C
ATOM   1822  CZ  TYR A 226     -79.995  17.236 -49.546  1.00 43.73           C
ANISOU 1822  CZ  TYR A 226     6404   4607   5605     89     92   -800       C
ATOM   1823  OH  TYR A 226     -78.828  17.911 -49.816  1.00 52.51           O
ANISOU 1823  OH  TYR A 226     7523   5786   6644     45    235   -746       O
ATOM   1824  N   LYS A 227     -86.458  13.476 -50.294  1.00 55.84           N
ANISOU 1824  N   LYS A 227     7907   5958   7351    269   -684  -1174       N
ATOM   1825  CA  LYS A 227     -87.484  12.439 -50.166  1.00 56.81           C
ANISOU 1825  CA  LYS A 227     7972   6018   7596    276   -825  -1266       C
ATOM   1826  C   LYS A 227     -87.973  12.312 -48.724  1.00 50.47           C
ANISOU 1826  C   LYS A 227     7067   5109   6999    226   -852  -1188       C
ATOM   1827  O   LYS A 227     -88.065  11.217 -48.166  1.00 51.21           O
ANISOU 1827  O   LYS A 227     7082   5120   7254    205   -897  -1249       O
ATOM   1828  CB  LYS A 227     -86.964  11.097 -50.689  1.00 66.11           C
ANISOU 1828  CB  LYS A 227     9129   7184   8805    302   -841  -1441       C
ATOM   1829  CG  LYS A 227     -86.276  11.183 -52.043  1.00 76.41           C
ANISOU 1829  CG  LYS A 227    10523   8614   9895    354   -786  -1530       C
ATOM   1830  CD  LYS A 227     -87.241  11.625 -53.130  1.00 85.66           C
ANISOU 1830  CD  LYS A 227    11782   9873  10893    392   -882  -1542       C
ATOM   1831  CE  LYS A 227     -86.524  11.837 -54.454  1.00 92.82           C
ANISOU 1831  CE  LYS A 227    12785  10927  11554    439   -811  -1605       C
ATOM   1832  NZ  LYS A 227     -85.571  12.981 -54.396  1.00 95.10           N
ANISOU 1832  NZ  LYS A 227    13121  11281  11731    410   -651  -1462       N
ATOM   1833  N   LEU A 228     -88.294  13.454 -48.119  1.00 46.74           N
ANISOU 1833  N   LEU A 228     6600   4643   6518    209   -828  -1049       N
ATOM   1834  CA  LEU A 228     -88.675  13.514 -46.715  1.00 46.53           C
ANISOU 1834  CA  LEU A 228     6479   4544   6656    167   -833   -966       C
ATOM   1835  C   LEU A 228     -90.184  13.596 -46.514  1.00 46.59           C
ANISOU 1835  C   LEU A 228     6445   4544   6714    166   -957   -946       C
ATOM   1836  O   LEU A 228     -90.636  14.039 -45.453  1.00 49.70           O
ANISOU 1836  O   LEU A 228     6774   4915   7196    141   -954   -858       O
ATOM   1837  CB  LEU A 228     -87.986  14.699 -46.036  1.00 47.40           C
ANISOU 1837  CB  LEU A 228     6606   4663   6743    153   -724   -842       C
ATOM   1838  CG  LEU A 228     -86.477  14.562 -45.839  1.00 46.84           C
ANISOU 1838  CG  LEU A 228     6534   4586   6678    138   -597   -850       C
ATOM   1839  CD1 LEU A 228     -85.858  15.899 -45.467  1.00 50.17           C
ANISOU 1839  CD1 LEU A 228     6990   5026   7047    124   -503   -734       C
ATOM   1840  CD2 LEU A 228     -86.181  13.522 -44.772  1.00 45.10           C
ANISOU 1840  CD2 LEU A 228     6212   4286   6636    109   -596   -877       C
ATOM   1841  N   GLU A 229     -90.969  13.181 -47.505  1.00 47.18           N
ANISOU 1841  N   GLU A 229     6546   4647   6732    194  -1065  -1035       N
ATOM   1842  CA  GLU A 229     -92.419  13.190 -47.359  1.00 51.32           C
ANISOU 1842  CA  GLU A 229     7015   5170   7316    192  -1190  -1030       C
ATOM   1843  C   GLU A 229     -92.847  12.192 -46.289  1.00 47.37           C
ANISOU 1843  C   GLU A 229     6385   4592   7022    131  -1222  -1037       C
ATOM   1844  O   GLU A 229     -92.370  11.053 -46.260  1.00 48.01           O
ANISOU 1844  O   GLU A 229     6439   4612   7190    105  -1223  -1112       O
ATOM   1845  CB  GLU A 229     -93.097  12.860 -48.689  1.00 59.24           C
ANISOU 1845  CB  GLU A 229     8071   6220   8218    236  -1308  -1139       C
ATOM   1846  CG  GLU A 229     -92.851  13.868 -49.803  1.00 67.81           C
ANISOU 1846  CG  GLU A 229     9290   7396   9080    297  -1293  -1116       C
ATOM   1847  CD  GLU A 229     -91.711  13.465 -50.718  1.00 78.00           C
ANISOU 1847  CD  GLU A 229    10663   8727  10246    318  -1222  -1196       C
ATOM   1848  OE1 GLU A 229     -90.553  13.438 -50.254  1.00 80.09           O
ANISOU 1848  OE1 GLU A 229    10923   8970  10536    293  -1093  -1168       O
ATOM   1849  OE2 GLU A 229     -91.975  13.163 -51.901  1.00 83.96           O
ANISOU 1849  OE2 GLU A 229    11482   9544  10876    363  -1296  -1296       O
ATOM   1850  N   GLY A 230     -93.746  12.622 -45.409  1.00 42.46           N
ANISOU 1850  N   GLY A 230     5683   3972   6479    107  -1250   -957       N
ATOM   1851  CA  GLY A 230     -94.265  11.765 -44.365  1.00 44.04           C
ANISOU 1851  CA  GLY A 230     5756   4116   6862     39  -1276   -940       C
ATOM   1852  C   GLY A 230     -93.495  11.779 -43.065  1.00 45.54           C
ANISOU 1852  C   GLY A 230     5900   4269   7136     -1  -1167   -850       C
ATOM   1853  O   GLY A 230     -93.799  10.972 -42.178  1.00 51.75           O
ANISOU 1853  O   GLY A 230     6589   5006   8067    -64  -1182   -824       O
ATOM   1854  N   TYR A 231     -92.511  12.664 -42.919  1.00 41.39           N
ANISOU 1854  N   TYR A 231     5440   3765   6522     28  -1063   -796       N
ATOM   1855  CA  TYR A 231     -91.715  12.753 -41.703  1.00 38.80           C
ANISOU 1855  CA  TYR A 231     5071   3408   6262     -3   -965   -717       C
ATOM   1856  C   TYR A 231     -91.955  14.040 -40.925  1.00 39.20           C
ANISOU 1856  C   TYR A 231     5106   3509   6279     14   -921   -620       C
ATOM   1857  O   TYR A 231     -91.277  14.270 -39.917  1.00 38.93           O
ANISOU 1857  O   TYR A 231     5044   3463   6284     -4   -841   -559       O
ATOM   1858  CB  TYR A 231     -90.226  12.610 -42.037  1.00 38.97           C
ANISOU 1858  CB  TYR A 231     5163   3406   6238     12   -877   -748       C
ATOM   1859  CG  TYR A 231     -89.861  11.248 -42.585  1.00 44.48           C
ANISOU 1859  CG  TYR A 231     5860   4044   6995      3   -915   -854       C
ATOM   1860  CD1 TYR A 231     -89.592  10.184 -41.733  1.00 43.96           C
ANISOU 1860  CD1 TYR A 231     5723   3897   7081    -43   -920   -848       C
ATOM   1861  CD2 TYR A 231     -89.791  11.023 -43.954  1.00 51.08           C
ANISOU 1861  CD2 TYR A 231     6771   4905   7732     44   -954   -961       C
ATOM   1862  CE1 TYR A 231     -89.261   8.935 -42.228  1.00 43.43           C
ANISOU 1862  CE1 TYR A 231     5658   3758   7086    -44   -968   -952       C
ATOM   1863  CE2 TYR A 231     -89.461   9.777 -44.460  1.00 51.92           C
ANISOU 1863  CE2 TYR A 231     6876   4956   7897     46   -996  -1078       C
ATOM   1864  CZ  TYR A 231     -89.197   8.737 -43.592  1.00 48.01           C
ANISOU 1864  CZ  TYR A 231     6307   4363   7571      3  -1006  -1076       C
ATOM   1865  OH  TYR A 231     -88.867   7.495 -44.088  1.00 44.74           O
ANISOU 1865  OH  TYR A 231     5893   3876   7231     11  -1061  -1199       O
ATOM   1866  N   ALA A 232     -92.888  14.884 -41.372  1.00 39.40           N
ANISOU 1866  N   ALA A 232     5149   3587   6236     54   -980   -614       N
ATOM   1867  CA  ALA A 232     -93.334  16.064 -40.625  1.00 39.84           C
ANISOU 1867  CA  ALA A 232     5176   3684   6279     79   -963   -541       C
ATOM   1868  C   ALA A 232     -92.196  17.052 -40.377  1.00 39.72           C
ANISOU 1868  C   ALA A 232     5231   3660   6200    100   -865   -488       C
ATOM   1869  O   ALA A 232     -92.094  17.650 -39.304  1.00 39.07           O
ANISOU 1869  O   ALA A 232     5103   3587   6155     99   -819   -431       O
ATOM   1870  CB  ALA A 232     -94.000  15.663 -39.306  1.00 35.92           C
ANISOU 1870  CB  ALA A 232     4542   3201   5903     34   -964   -500       C
ATOM   1871  N   PHE A 233     -91.336  17.240 -41.381  1.00 41.32           N
ANISOU 1871  N   PHE A 233     5542   3851   6305    117   -832   -509       N
ATOM   1872  CA  PHE A 233     -90.261  18.216 -41.243  1.00 40.38           C
ANISOU 1872  CA  PHE A 233     5489   3724   6131    126   -740   -456       C
ATOM   1873  C   PHE A 233     -90.793  19.641 -41.252  1.00 42.20           C
ANISOU 1873  C   PHE A 233     5759   3970   6305    172   -769   -399       C
ATOM   1874  O   PHE A 233     -90.182  20.532 -40.651  1.00 43.74           O
ANISOU 1874  O   PHE A 233     5968   4147   6504    174   -708   -345       O
ATOM   1875  CB  PHE A 233     -89.227  18.025 -42.350  1.00 42.47           C
ANISOU 1875  CB  PHE A 233     5849   3988   6300    126   -689   -491       C
ATOM   1876  CG  PHE A 233     -88.040  17.216 -41.927  1.00 45.14           C
ANISOU 1876  CG  PHE A 233     6155   4297   6700     89   -605   -517       C
ATOM   1877  CD1 PHE A 233     -88.205  16.067 -41.172  1.00 48.19           C
ANISOU 1877  CD1 PHE A 233     6449   4649   7210     59   -626   -546       C
ATOM   1878  CD2 PHE A 233     -86.759  17.601 -42.282  1.00 48.54           C
ANISOU 1878  CD2 PHE A 233     6644   4732   7069     83   -508   -508       C
ATOM   1879  CE1 PHE A 233     -87.114  15.318 -40.777  1.00 51.99           C
ANISOU 1879  CE1 PHE A 233     6904   5095   7756     36   -563   -570       C
ATOM   1880  CE2 PHE A 233     -85.663  16.856 -41.892  1.00 51.33           C
ANISOU 1880  CE2 PHE A 233     6957   5061   7486     59   -438   -542       C
ATOM   1881  CZ  PHE A 233     -85.841  15.712 -41.138  1.00 53.10           C
ANISOU 1881  CZ  PHE A 233     7096   5245   7836     41   -471   -574       C
ATOM   1882  N   GLU A 234     -91.921  19.875 -41.927  1.00 44.47           N
ANISOU 1882  N   GLU A 234     6064   4286   6548    213   -870   -416       N
ATOM   1883  CA  GLU A 234     -92.570  21.179 -41.859  1.00 49.14           C
ANISOU 1883  CA  GLU A 234     6681   4883   7108    268   -919   -369       C
ATOM   1884  C   GLU A 234     -92.880  21.560 -40.418  1.00 51.27           C
ANISOU 1884  C   GLU A 234     6846   5156   7479    271   -901   -344       C
ATOM   1885  O   GLU A 234     -92.762  22.729 -40.034  1.00 59.37           O
ANISOU 1885  O   GLU A 234     7899   6162   8496    306   -891   -301       O
ATOM   1886  CB  GLU A 234     -93.854  21.174 -42.690  1.00 53.94           C
ANISOU 1886  CB  GLU A 234     7295   5526   7674    316  -1047   -405       C
ATOM   1887  CG  GLU A 234     -93.707  20.612 -44.095  1.00 59.66           C
ANISOU 1887  CG  GLU A 234     8109   6266   8292    318  -1081   -450       C
ATOM   1888  CD  GLU A 234     -93.875  19.106 -44.150  1.00 64.33           C
ANISOU 1888  CD  GLU A 234     8628   6866   8950    274  -1100   -534       C
ATOM   1889  OE1 GLU A 234     -93.962  18.473 -43.076  1.00 66.04           O
ANISOU 1889  OE1 GLU A 234     8732   7068   9293    230  -1071   -539       O
ATOM   1890  OE2 GLU A 234     -93.924  18.555 -45.269  1.00 66.32           O
ANISOU 1890  OE2 GLU A 234     8938   7137   9124    284  -1147   -596       O
ATOM   1891  N   HIS A 235     -93.277  20.583 -39.605  1.00 44.61           N
ANISOU 1891  N   HIS A 235     5884   4337   6730    233   -898   -371       N
ATOM   1892  CA  HIS A 235     -93.597  20.858 -38.211  1.00 34.68           C
ANISOU 1892  CA  HIS A 235     4520   3106   5552    234   -875   -348       C
ATOM   1893  C   HIS A 235     -92.347  20.786 -37.339  1.00 35.52           C
ANISOU 1893  C   HIS A 235     4623   3184   5690    195   -769   -317       C
ATOM   1894  O   HIS A 235     -92.035  21.731 -36.606  1.00 36.04           O
ANISOU 1894  O   HIS A 235     4686   3246   5759    220   -736   -290       O
ATOM   1895  CB  HIS A 235     -94.670  19.875 -37.731  1.00 30.54           C
ANISOU 1895  CB  HIS A 235     3865   2632   5108    204   -920   -375       C
ATOM   1896  CG  HIS A 235     -94.969  19.963 -36.268  1.00 31.99           C
ANISOU 1896  CG  HIS A 235     3930   2866   5359    193   -881   -349       C
ATOM   1897  ND1 HIS A 235     -95.998  20.728 -35.761  1.00 31.95           N
ANISOU 1897  ND1 HIS A 235     3850   2927   5364    247   -923   -357       N
ATOM   1898  CD2 HIS A 235     -94.385  19.365 -35.203  1.00 32.28           C
ANISOU 1898  CD2 HIS A 235     3907   2907   5449    140   -807   -317       C
ATOM   1899  CE1 HIS A 235     -96.028  20.606 -34.446  1.00 34.69           C
ANISOU 1899  CE1 HIS A 235     4096   3328   5759    225   -867   -335       C
ATOM   1900  NE2 HIS A 235     -95.059  19.785 -34.082  1.00 32.47           N
ANISOU 1900  NE2 HIS A 235     3826   3009   5501    158   -799   -304       N
ATOM   1901  N   ILE A 236     -91.603  19.684 -37.439  1.00 36.41           N
ANISOU 1901  N   ILE A 236     4736   3272   5828    140   -725   -329       N
ATOM   1902  CA  ILE A 236     -90.501  19.424 -36.514  1.00 36.00           C
ANISOU 1902  CA  ILE A 236     4658   3198   5821    104   -639   -304       C
ATOM   1903  C   ILE A 236     -89.360  20.412 -36.730  1.00 36.35           C
ANISOU 1903  C   ILE A 236     4791   3207   5813    118   -577   -284       C
ATOM   1904  O   ILE A 236     -88.812  20.972 -35.772  1.00 33.95           O
ANISOU 1904  O   ILE A 236     4462   2900   5537    120   -530   -258       O
ATOM   1905  CB  ILE A 236     -90.017  17.971 -36.666  1.00 38.13           C
ANISOU 1905  CB  ILE A 236     4909   3439   6141     51   -623   -330       C
ATOM   1906  CG1 ILE A 236     -91.153  16.999 -36.352  1.00 27.27           C
ANISOU 1906  CG1 ILE A 236     3439   2086   4837     20   -687   -338       C
ATOM   1907  CG2 ILE A 236     -88.817  17.709 -35.774  1.00 35.01           C
ANISOU 1907  CG2 ILE A 236     4493   3019   5792     23   -544   -306       C
ATOM   1908  CD1 ILE A 236     -90.857  15.580 -36.758  1.00 38.92           C
ANISOU 1908  CD1 ILE A 236     4910   3510   6369    -26   -703   -375       C
ATOM   1909  N   VAL A 237     -88.971  20.628 -37.981  1.00 36.47           N
ANISOU 1909  N   VAL A 237     4908   3201   5750    125   -576   -294       N
ATOM   1910  CA  VAL A 237     -87.777  21.404 -38.304  1.00 34.78           C
ANISOU 1910  CA  VAL A 237     4772   2953   5488    118   -505   -267       C
ATOM   1911  C   VAL A 237     -88.119  22.843 -38.661  1.00 32.10           C
ANISOU 1911  C   VAL A 237     4506   2598   5091    159   -538   -225       C
ATOM   1912  O   VAL A 237     -87.523  23.779 -38.129  1.00 35.49           O
ANISOU 1912  O   VAL A 237     4950   2997   5540    159   -501   -191       O
ATOM   1913  CB  VAL A 237     -86.987  20.716 -39.440  1.00 39.59           C
ANISOU 1913  CB  VAL A 237     5445   3560   6038     94   -465   -299       C
ATOM   1914  CG1 VAL A 237     -85.678  21.443 -39.690  1.00 38.90           C
ANISOU 1914  CG1 VAL A 237     5418   3451   5909     72   -375   -267       C
ATOM   1915  CG2 VAL A 237     -86.738  19.257 -39.099  1.00 42.49           C
ANISOU 1915  CG2 VAL A 237     5741   3924   6479     64   -453   -350       C
ATOM   1916  N   TYR A 238     -89.077  23.039 -39.569  1.00 32.34           N
ANISOU 1916  N   TYR A 238     4585   2644   5060    196   -619   -229       N
ATOM   1917  CA  TYR A 238     -89.406  24.387 -40.016  1.00 33.66           C
ANISOU 1917  CA  TYR A 238     4834   2783   5173    240   -666   -182       C
ATOM   1918  C   TYR A 238     -90.268  25.136 -39.008  1.00 36.90           C
ANISOU 1918  C   TYR A 238     5177   3192   5651    292   -723   -182       C
ATOM   1919  O   TYR A 238     -90.189  26.367 -38.928  1.00 38.05           O
ANISOU 1919  O   TYR A 238     5376   3289   5793    324   -742   -144       O
ATOM   1920  CB  TYR A 238     -90.107  24.333 -41.374  1.00 33.61           C
ANISOU 1920  CB  TYR A 238     4907   2798   5066    270   -743   -186       C
ATOM   1921  CG  TYR A 238     -89.228  23.826 -42.496  1.00 34.89           C
ANISOU 1921  CG  TYR A 238     5152   2973   5131    232   -685   -188       C
ATOM   1922  CD1 TYR A 238     -88.452  24.701 -43.244  1.00 41.08           C
ANISOU 1922  CD1 TYR A 238     6051   3735   5824    218   -641   -121       C
ATOM   1923  CD2 TYR A 238     -89.174  22.474 -42.806  1.00 37.01           C
ANISOU 1923  CD2 TYR A 238     5381   3278   5401    208   -676   -260       C
ATOM   1924  CE1 TYR A 238     -87.647  24.243 -44.271  1.00 42.15           C
ANISOU 1924  CE1 TYR A 238     6253   3905   5857    184   -577   -128       C
ATOM   1925  CE2 TYR A 238     -88.372  22.006 -43.830  1.00 38.12           C
ANISOU 1925  CE2 TYR A 238     5591   3444   5449    185   -622   -282       C
ATOM   1926  CZ  TYR A 238     -87.612  22.896 -44.559  1.00 41.74           C
ANISOU 1926  CZ  TYR A 238     6156   3901   5803    174   -568   -216       C
ATOM   1927  OH  TYR A 238     -86.812  22.437 -45.580  1.00 45.43           O
ANISOU 1927  OH  TYR A 238     6684   4415   6164    152   -504   -241       O
ATOM   1928  N   GLY A 239     -91.088  24.426 -38.239  1.00 35.49           N
ANISOU 1928  N   GLY A 239     4882   3066   5536    299   -751   -224       N
ATOM   1929  CA  GLY A 239     -91.924  25.063 -37.241  1.00 32.67           C
ANISOU 1929  CA  GLY A 239     4444   2733   5235    352   -795   -237       C
ATOM   1930  C   GLY A 239     -93.246  25.568 -37.782  1.00 35.75           C
ANISOU 1930  C   GLY A 239     4838   3143   5604    424   -909   -254       C
ATOM   1931  O   GLY A 239     -93.319  26.053 -38.916  1.00 38.00           O
ANISOU 1931  O   GLY A 239     5231   3391   5817    449   -960   -230       O
ATOM   1932  N   ASP A 240     -94.298  25.463 -36.976  1.00 39.65           N
ANISOU 1932  N   ASP A 240     5209   3703   6153    458   -950   -293       N
ATOM   1933  CA  ASP A 240     -95.638  25.904 -37.346  1.00 42.67           C
ANISOU 1933  CA  ASP A 240     5564   4118   6532    535  -1062   -323       C
ATOM   1934  C   ASP A 240     -95.946  27.197 -36.603  1.00 43.85           C
ANISOU 1934  C   ASP A 240     5691   4254   6714    617  -1095   -336       C
ATOM   1935  O   ASP A 240     -95.961  27.218 -35.367  1.00 43.75           O
ANISOU 1935  O   ASP A 240     5576   4290   6755    620  -1048   -363       O
ATOM   1936  CB  ASP A 240     -96.674  24.827 -37.021  1.00 46.73           C
ANISOU 1936  CB  ASP A 240     5937   4726   7093    513  -1088   -368       C
ATOM   1937  CG  ASP A 240     -98.054  25.156 -37.562  1.00 50.58           C
ANISOU 1937  CG  ASP A 240     6387   5254   7578    588  -1210   -408       C
ATOM   1938  OD1 ASP A 240     -98.205  26.190 -38.246  1.00 52.06           O
ANISOU 1938  OD1 ASP A 240     6670   5391   7721    662  -1284   -398       O
ATOM   1939  OD2 ASP A 240     -98.992  24.373 -37.302  1.00 53.18           O
ANISOU 1939  OD2 ASP A 240     6588   5663   7954    569  -1237   -447       O
ATOM   1940  N   PHE A 241     -96.198  28.268 -37.355  1.00 41.98           N
ANISOU 1940  N   PHE A 241     5552   3953   6444    688  -1180   -320       N
ATOM   1941  CA  PHE A 241     -96.440  29.588 -36.788  1.00 40.08           C
ANISOU 1941  CA  PHE A 241     5313   3672   6244    777  -1229   -337       C
ATOM   1942  C   PHE A 241     -97.855  30.090 -37.046  1.00 41.57           C
ANISOU 1942  C   PHE A 241     5453   3893   6448    884  -1360   -386       C
ATOM   1943  O   PHE A 241     -98.152  31.252 -36.750  1.00 42.75           O
ANISOU 1943  O   PHE A 241     5615   3996   6633    977  -1426   -408       O
ATOM   1944  CB  PHE A 241     -95.429  30.594 -37.343  1.00 38.10           C
ANISOU 1944  CB  PHE A 241     5223   3289   5964    772  -1225   -268       C
ATOM   1945  CG  PHE A 241     -93.997  30.189 -37.143  1.00 35.49           C
ANISOU 1945  CG  PHE A 241     4933   2927   5624    670  -1099   -225       C
ATOM   1946  CD1 PHE A 241     -93.347  29.400 -38.078  1.00 37.68           C
ANISOU 1946  CD1 PHE A 241     5283   3203   5832    592  -1047   -180       C
ATOM   1947  CD2 PHE A 241     -93.300  30.603 -36.022  1.00 34.31           C
ANISOU 1947  CD2 PHE A 241     4744   2757   5534    659  -1038   -242       C
ATOM   1948  CE1 PHE A 241     -92.029  29.027 -37.896  1.00 34.07           C
ANISOU 1948  CE1 PHE A 241     4849   2723   5372    507   -933   -151       C
ATOM   1949  CE2 PHE A 241     -91.981  30.233 -35.834  1.00 33.28           C
ANISOU 1949  CE2 PHE A 241     4642   2601   5402    570   -930   -208       C
ATOM   1950  CZ  PHE A 241     -91.345  29.445 -36.773  1.00 32.80           C
ANISOU 1950  CZ  PHE A 241     4646   2539   5279    494   -876   -163       C
ATOM   1951  N   SER A 242     -98.734  29.247 -37.588  1.00 41.86           N
ANISOU 1951  N   SER A 242     5433   4006   6468    879  -1408   -411       N
ATOM   1952  CA  SER A 242    -100.073  29.692 -37.952  1.00 41.82           C
ANISOU 1952  CA  SER A 242     5380   4036   6476    982  -1542   -460       C
ATOM   1953  C   SER A 242    -101.003  29.827 -36.753  1.00 41.20           C
ANISOU 1953  C   SER A 242     5117   4059   6476   1043  -1550   -546       C
ATOM   1954  O   SER A 242    -102.026  30.512 -36.857  1.00 45.92           O
ANISOU 1954  O   SER A 242     5669   4676   7102   1154  -1662   -600       O
ATOM   1955  CB  SER A 242    -100.688  28.728 -38.968  1.00 44.63           C
ANISOU 1955  CB  SER A 242     5729   4440   6790    952  -1598   -467       C
ATOM   1956  OG  SER A 242    -100.791  27.422 -38.429  1.00 50.00           O
ANISOU 1956  OG  SER A 242     6282   5211   7505    862  -1520   -494       O
ATOM   1957  N   HIS A 243    -100.678  29.200 -35.628  1.00 39.80           N
ANISOU 1957  N   HIS A 243     4832   3957   6332    978  -1435   -561       N
ATOM   1958  CA  HIS A 243    -101.537  29.199 -34.455  1.00 41.95           C
ANISOU 1958  CA  HIS A 243     4921   4358   6662   1022  -1422   -638       C
ATOM   1959  C   HIS A 243    -100.850  29.924 -33.304  1.00 42.50           C
ANISOU 1959  C   HIS A 243     4983   4415   6750   1048  -1354   -656       C
ATOM   1960  O   HIS A 243     -99.663  30.253 -33.365  1.00 43.67           O
ANISOU 1960  O   HIS A 243     5257   4457   6880   1011  -1308   -604       O
ATOM   1961  CB  HIS A 243    -101.902  27.766 -34.048  1.00 46.33           C
ANISOU 1961  CB  HIS A 243     5337   5034   7232    919  -1351   -637       C
ATOM   1962  CG  HIS A 243    -102.437  26.941 -35.176  1.00 57.26           C
ANISOU 1962  CG  HIS A 243     6734   6419   8605    878  -1416   -626       C
ATOM   1963  ND1 HIS A 243    -103.690  27.139 -35.714  1.00 62.14           N
ANISOU 1963  ND1 HIS A 243     7284   7086   9241    952  -1535   -682       N
ATOM   1964  CD2 HIS A 243    -101.886  25.918 -35.872  1.00 60.55           C
ANISOU 1964  CD2 HIS A 243     7218   6794   8994    776  -1386   -578       C
ATOM   1965  CE1 HIS A 243    -103.890  26.272 -36.691  1.00 63.70           C
ANISOU 1965  CE1 HIS A 243     7510   7272   9422    894  -1578   -668       C
ATOM   1966  NE2 HIS A 243    -102.811  25.520 -36.807  1.00 61.78           N
ANISOU 1966  NE2 HIS A 243     7350   6974   9150    789  -1488   -608       N
ATOM   1967  N   SER A 244    -101.623  30.175 -32.243  1.00 42.26           N
ANISOU 1967  N   SER A 244     4796   4504   6756   1113  -1349   -737       N
ATOM   1968  CA  SER A 244    -101.086  30.894 -31.092  1.00 41.82           C
ANISOU 1968  CA  SER A 244     4721   4456   6714   1155  -1297   -778       C
ATOM   1969  C   SER A 244     -99.964  30.109 -30.427  1.00 39.15           C
ANISOU 1969  C   SER A 244     4394   4131   6351   1035  -1165   -719       C
ATOM   1970  O   SER A 244     -98.965  30.689 -29.989  1.00 42.43           O
ANISOU 1970  O   SER A 244     4884   4472   6767   1037  -1130   -713       O
ATOM   1971  CB  SER A 244    -102.199  31.189 -30.087  1.00 43.89           C
ANISOU 1971  CB  SER A 244     4795   4876   7003   1248  -1310   -887       C
ATOM   1972  OG  SER A 244    -102.620  30.005 -29.434  1.00 47.86           O
ANISOU 1972  OG  SER A 244     5146   5545   7494   1162  -1219   -877       O
ATOM   1973  N   GLN A 245    -100.112  28.791 -30.341  1.00 36.93           N
ANISOU 1973  N   GLN A 245     4037   3937   6059    932  -1100   -677       N
ATOM   1974  CA  GLN A 245     -99.070  27.928 -29.805  1.00 35.51           C
ANISOU 1974  CA  GLN A 245     3872   3760   5861    819   -988   -614       C
ATOM   1975  C   GLN A 245     -98.119  27.538 -30.928  1.00 36.71           C
ANISOU 1975  C   GLN A 245     4180   3773   5995    745   -984   -538       C
ATOM   1976  O   GLN A 245     -98.545  26.970 -31.941  1.00 38.02           O
ANISOU 1976  O   GLN A 245     4372   3920   6156    715  -1029   -517       O
ATOM   1977  CB  GLN A 245     -99.671  26.686 -29.151  1.00 37.56           C
ANISOU 1977  CB  GLN A 245     3979   4168   6125    741   -925   -596       C
ATOM   1978  CG  GLN A 245    -100.080  26.899 -27.708  1.00 46.19           C
ANISOU 1978  CG  GLN A 245     4926   5416   7208    779   -871   -646       C
ATOM   1979  CD  GLN A 245     -98.905  27.291 -26.835  1.00 55.21           C
ANISOU 1979  CD  GLN A 245     6123   6530   8324    778   -807   -640       C
ATOM   1980  OE1 GLN A 245     -97.856  26.647 -26.863  1.00 56.84           O
ANISOU 1980  OE1 GLN A 245     6404   6671   8522    689   -751   -568       O
ATOM   1981  NE2 GLN A 245     -99.070  28.359 -26.063  1.00 57.11           N
ANISOU 1981  NE2 GLN A 245     6324   6818   8556    885   -822   -728       N
ATOM   1982  N   LEU A 246     -96.839  27.852 -30.753  1.00 33.22           N
ANISOU 1982  N   LEU A 246     3837   3243   5543    717   -933   -507       N
ATOM   1983  CA  LEU A 246     -95.839  27.481 -31.741  1.00 32.86           C
ANISOU 1983  CA  LEU A 246     3926   3083   5475    644   -912   -440       C
ATOM   1984  C   LEU A 246     -95.716  25.965 -31.810  1.00 32.17           C
ANISOU 1984  C   LEU A 246     3794   3040   5387    541   -856   -401       C
ATOM   1985  O   LEU A 246     -95.657  25.282 -30.784  1.00 34.12           O
ANISOU 1985  O   LEU A 246     3944   3368   5651    498   -792   -395       O
ATOM   1986  CB  LEU A 246     -94.493  28.117 -31.395  1.00 33.85           C
ANISOU 1986  CB  LEU A 246     4138   3121   5602    631   -861   -421       C
ATOM   1987  CG  LEU A 246     -93.449  28.216 -32.511  1.00 38.49           C
ANISOU 1987  CG  LEU A 246     4878   3584   6165    581   -848   -362       C
ATOM   1988  CD1 LEU A 246     -92.561  29.424 -32.279  1.00 42.49           C
ANISOU 1988  CD1 LEU A 246     5463   3992   6690    606   -844   -359       C
ATOM   1989  CD2 LEU A 246     -92.606  26.953 -32.607  1.00 37.98           C
ANISOU 1989  CD2 LEU A 246     4815   3526   6089    478   -764   -321       C
ATOM   1990  N   GLY A 247     -95.684  25.439 -33.031  1.00 34.38           N
ANISOU 1990  N   GLY A 247     4150   3266   5647    505   -885   -376       N
ATOM   1991  CA  GLY A 247     -95.648  24.008 -33.264  1.00 35.25           C
ANISOU 1991  CA  GLY A 247     4226   3398   5768    416   -855   -353       C
ATOM   1992  C   GLY A 247     -94.266  23.563 -33.731  1.00 35.75           C
ANISOU 1992  C   GLY A 247     4395   3375   5812    352   -794   -315       C
ATOM   1993  O   GLY A 247     -93.710  24.128 -34.673  1.00 36.75           O
ANISOU 1993  O   GLY A 247     4644   3424   5895    367   -808   -303       O
ATOM   1994  N   GLY A 248     -93.738  22.549 -33.051  1.00 33.51           N
ANISOU 1994  N   GLY A 248     4059   3111   5561    281   -728   -293       N
ATOM   1995  CA  GLY A 248     -92.487  21.947 -33.481  1.00 32.26           C
ANISOU 1995  CA  GLY A 248     3979   2880   5397    224   -674   -270       C
ATOM   1996  C   GLY A 248     -91.305  22.880 -33.296  1.00 34.56           C
ANISOU 1996  C   GLY A 248     4346   3116   5668    240   -624   -257       C
ATOM   1997  O   GLY A 248     -91.151  23.533 -32.258  1.00 34.32           O
ANISOU 1997  O   GLY A 248     4276   3111   5654    267   -602   -260       O
ATOM   1998  N   LEU A 249     -90.455  22.935 -34.324  1.00 33.80           N
ANISOU 1998  N   LEU A 249     4358   2949   5536    222   -606   -247       N
ATOM   1999  CA  LEU A 249     -89.239  23.749 -34.336  1.00 33.31           C
ANISOU 1999  CA  LEU A 249     4371   2827   5460    218   -553   -229       C
ATOM   2000  C   LEU A 249     -88.296  23.322 -33.205  1.00 36.85           C
ANISOU 2000  C   LEU A 249     4760   3285   5957    182   -483   -224       C
ATOM   2001  O   LEU A 249     -88.110  24.013 -32.202  1.00 36.16           O
ANISOU 2001  O   LEU A 249     4637   3209   5892    206   -472   -229       O
ATOM   2002  CB  LEU A 249     -89.583  25.241 -34.250  1.00 37.07           C
ANISOU 2002  CB  LEU A 249     4883   3278   5924    281   -597   -227       C
ATOM   2003  CG  LEU A 249     -88.484  26.236 -34.623  1.00 36.15           C
ANISOU 2003  CG  LEU A 249     4866   3078   5793    271   -563   -198       C
ATOM   2004  CD1 LEU A 249     -88.244  26.243 -36.126  1.00 37.84           C
ANISOU 2004  CD1 LEU A 249     5193   3251   5935    250   -567   -165       C
ATOM   2005  CD2 LEU A 249     -88.838  27.626 -34.124  1.00 34.18           C
ANISOU 2005  CD2 LEU A 249     4626   2795   5567    335   -614   -206       C
ATOM   2006  N   HIS A 250     -87.694  22.148 -33.406  1.00 37.54           N
ANISOU 2006  N   HIS A 250     4840   3364   6061    130   -445   -223       N
ATOM   2007  CA  HIS A 250     -86.863  21.520 -32.388  1.00 32.66           C
ANISOU 2007  CA  HIS A 250     4163   2754   5492     98   -394   -216       C
ATOM   2008  C   HIS A 250     -85.401  21.371 -32.790  1.00 32.13           C
ANISOU 2008  C   HIS A 250     4146   2633   5429     66   -332   -220       C
ATOM   2009  O   HIS A 250     -84.591  20.943 -31.960  1.00 32.79           O
ANISOU 2009  O   HIS A 250     4184   2718   5556     47   -295   -217       O
ATOM   2010  CB  HIS A 250     -87.435  20.143 -32.017  1.00 28.35           C
ANISOU 2010  CB  HIS A 250     3542   2242   4986     65   -412   -208       C
ATOM   2011  CG  HIS A 250     -88.843  20.194 -31.508  1.00 30.41           C
ANISOU 2011  CG  HIS A 250     3729   2574   5251     84   -460   -201       C
ATOM   2012  ND1 HIS A 250     -89.164  20.660 -30.251  1.00 29.39           N
ANISOU 2012  ND1 HIS A 250     3526   2514   5126    107   -452   -190       N
ATOM   2013  CD2 HIS A 250     -90.016  19.842 -32.088  1.00 31.04           C
ANISOU 2013  CD2 HIS A 250     3787   2678   5328     85   -517   -212       C
ATOM   2014  CE1 HIS A 250     -90.472  20.593 -30.078  1.00 29.17           C
ANISOU 2014  CE1 HIS A 250     3430   2555   5097    120   -493   -192       C
ATOM   2015  NE2 HIS A 250     -91.012  20.098 -31.178  1.00 29.36           N
ANISOU 2015  NE2 HIS A 250     3482   2550   5125    105   -535   -204       N
ATOM   2016  N   LEU A 251     -85.036  21.702 -34.025  1.00 33.75           N
ANISOU 2016  N   LEU A 251     4438   2802   5586     61   -318   -225       N
ATOM   2017  CA  LEU A 251     -83.650  21.661 -34.472  1.00 31.55           C
ANISOU 2017  CA  LEU A 251     4197   2488   5303     30   -248   -232       C
ATOM   2018  C   LEU A 251     -83.113  23.076 -34.614  1.00 35.22           C
ANISOU 2018  C   LEU A 251     4718   2920   5745     32   -224   -209       C
ATOM   2019  O   LEU A 251     -83.780  23.948 -35.180  1.00 42.79           O
ANISOU 2019  O   LEU A 251     5736   3864   6657     55   -263   -187       O
ATOM   2020  CB  LEU A 251     -83.511  20.922 -35.806  1.00 34.39           C
ANISOU 2020  CB  LEU A 251     4609   2843   5614     15   -238   -258       C
ATOM   2021  CG  LEU A 251     -83.328  19.405 -35.752  1.00 37.49           C
ANISOU 2021  CG  LEU A 251     4953   3237   6056     -1   -239   -297       C
ATOM   2022  CD1 LEU A 251     -82.979  18.875 -37.132  1.00 44.17           C
ANISOU 2022  CD1 LEU A 251     5858   4081   6844     -6   -221   -343       C
ATOM   2023  CD2 LEU A 251     -82.257  19.020 -34.743  1.00 32.76           C
ANISOU 2023  CD2 LEU A 251     4291   2625   5531    -17   -193   -299       C
ATOM   2024  N   LEU A 252     -81.895  23.293 -34.108  1.00 32.83           N
ANISOU 2024  N   LEU A 252     4392   2598   5483      5   -165   -212       N
ATOM   2025  CA  LEU A 252     -81.306  24.629 -34.128  1.00 35.41           C
ANISOU 2025  CA  LEU A 252     4762   2881   5811     -6   -144   -188       C
ATOM   2026  C   LEU A 252     -81.185  25.178 -35.544  1.00 34.33           C
ANISOU 2026  C   LEU A 252     4726   2718   5600    -28   -123   -154       C
ATOM   2027  O   LEU A 252     -81.316  26.390 -35.751  1.00 38.68           O
ANISOU 2027  O   LEU A 252     5336   3222   6138    -25   -144   -114       O
ATOM   2028  CB  LEU A 252     -79.934  24.608 -33.455  1.00 37.62           C
ANISOU 2028  CB  LEU A 252     4990   3150   6153    -40    -83   -206       C
ATOM   2029  CG  LEU A 252     -79.221  25.960 -33.380  1.00 39.82           C
ANISOU 2029  CG  LEU A 252     5299   3375   6457    -65    -62   -186       C
ATOM   2030  CD1 LEU A 252     -79.985  26.915 -32.479  1.00 39.34           C
ANISOU 2030  CD1 LEU A 252     5230   3293   6423    -18   -134   -189       C
ATOM   2031  CD2 LEU A 252     -77.788  25.802 -32.906  1.00 39.84           C
ANISOU 2031  CD2 LEU A 252     5243   3374   6522   -106      1   -211       C
ATOM   2032  N   ILE A 253     -80.936  24.311 -36.528  1.00 34.40           N
ANISOU 2032  N   ILE A 253     4758   2755   5556    -47    -87   -167       N
ATOM   2033  CA  ILE A 253     -80.824  24.787 -37.902  1.00 33.86           C
ANISOU 2033  CA  ILE A 253     4789   2683   5393    -68    -63   -131       C
ATOM   2034  C   ILE A 253     -82.158  25.340 -38.389  1.00 32.57           C
ANISOU 2034  C   ILE A 253     4693   2511   5172    -23   -153    -98       C
ATOM   2035  O   ILE A 253     -82.193  26.264 -39.211  1.00 37.67           O
ANISOU 2035  O   ILE A 253     5431   3129   5752    -32   -158    -40       O
ATOM   2036  CB  ILE A 253     -80.297  23.665 -38.817  1.00 33.07           C
ANISOU 2036  CB  ILE A 253     4692   2633   5240    -86     -7   -174       C
ATOM   2037  CG1 ILE A 253     -80.036  24.200 -40.226  1.00 35.73           C
ANISOU 2037  CG1 ILE A 253     5130   2988   5458   -111     34   -132       C
ATOM   2038  CG2 ILE A 253     -81.263  22.491 -38.847  1.00 32.49           C
ANISOU 2038  CG2 ILE A 253     4589   2588   5167    -46    -73   -225       C
ATOM   2039  CD1 ILE A 253     -79.400  23.193 -41.152  1.00 37.59           C
ANISOU 2039  CD1 ILE A 253     5365   3288   5629   -124    100   -188       C
ATOM   2040  N   GLY A 254     -83.272  24.805 -37.886  1.00 33.27           N
ANISOU 2040  N   GLY A 254     4733   2622   5287     23   -227   -130       N
ATOM   2041  CA  GLY A 254     -84.566  25.371 -38.226  1.00 29.23           C
ANISOU 2041  CA  GLY A 254     4265   2106   4736     73   -320   -110       C
ATOM   2042  C   GLY A 254     -84.759  26.752 -37.634  1.00 30.49           C
ANISOU 2042  C   GLY A 254     4442   2210   4934     99   -358    -75       C
ATOM   2043  O   GLY A 254     -85.360  27.628 -38.260  1.00 36.56           O
ANISOU 2043  O   GLY A 254     5288   2944   5657    130   -418    -35       O
ATOM   2044  N   LEU A 255     -84.250  26.966 -36.418  1.00 28.41           N
ANISOU 2044  N   LEU A 255     4107   1932   4754     93   -332    -94       N
ATOM   2045  CA  LEU A 255     -84.285  28.299 -35.828  1.00 30.61           C
ANISOU 2045  CA  LEU A 255     4401   2149   5079    118   -368    -78       C
ATOM   2046  C   LEU A 255     -83.357  29.251 -36.572  1.00 35.38           C
ANISOU 2046  C   LEU A 255     5100   2678   5666     67   -330    -15       C
ATOM   2047  O   LEU A 255     -83.671  30.437 -36.728  1.00 39.77           O
ANISOU 2047  O   LEU A 255     5720   3160   6231     90   -387     24       O
ATOM   2048  CB  LEU A 255     -83.904  28.236 -34.347  1.00 31.00           C
ANISOU 2048  CB  LEU A 255     4350   2214   5213    123   -351   -125       C
ATOM   2049  CG  LEU A 255     -84.897  27.707 -33.308  1.00 34.59           C
ANISOU 2049  CG  LEU A 255     4707   2741   5692    177   -396   -173       C
ATOM   2050  CD1 LEU A 255     -85.044  26.198 -33.382  1.00 33.47           C
ANISOU 2050  CD1 LEU A 255     4514   2669   5536    152   -368   -185       C
ATOM   2051  CD2 LEU A 255     -84.465  28.128 -31.912  1.00 37.07           C
ANISOU 2051  CD2 LEU A 255     4952   3062   6071    192   -389   -210       C
ATOM   2052  N   ALA A 256     -82.210  28.750 -37.036  1.00 35.69           N
ANISOU 2052  N   ALA A 256     5144   2733   5685     -3   -234     -2       N
ATOM   2053  CA  ALA A 256     -81.267  29.597 -37.758  1.00 34.36           C
ANISOU 2053  CA  ALA A 256     5053   2507   5496    -68   -180     66       C
ATOM   2054  C   ALA A 256     -81.861  30.088 -39.071  1.00 36.08           C
ANISOU 2054  C   ALA A 256     5393   2708   5610    -60   -218    140       C
ATOM   2055  O   ALA A 256     -81.728  31.268 -39.415  1.00 41.38           O
ANISOU 2055  O   ALA A 256     6145   3296   6282    -81   -240    216       O
ATOM   2056  CB  ALA A 256     -79.964  28.838 -38.006  1.00 30.31           C
ANISOU 2056  CB  ALA A 256     4500   2039   4976   -138    -63     51       C
ATOM   2057  N   LYS A 257     -82.519  29.197 -39.816  1.00 37.41           N
ANISOU 2057  N   LYS A 257     5577   2947   5688    -32   -236    121       N
ATOM   2058  CA  LYS A 257     -83.149  29.601 -41.068  1.00 40.32           C
ANISOU 2058  CA  LYS A 257     6063   3313   5944    -15   -285    186       C
ATOM   2059  C   LYS A 257     -84.236  30.640 -40.823  1.00 44.78           C
ANISOU 2059  C   LYS A 257     6669   3806   6541     54   -409    214       C
ATOM   2060  O   LYS A 257     -84.343  31.626 -41.562  1.00 46.36           O
ANISOU 2060  O   LYS A 257     6979   3942   6693     51   -449    304       O
ATOM   2061  CB  LYS A 257     -83.719  28.375 -41.780  1.00 34.64           C
ANISOU 2061  CB  LYS A 257     5338   2688   5137     12   -296    134       C
ATOM   2062  CG  LYS A 257     -84.266  28.652 -43.170  1.00 34.14           C
ANISOU 2062  CG  LYS A 257     5395   2643   4933     29   -343    192       C
ATOM   2063  CD  LYS A 257     -84.857  27.391 -43.780  1.00 34.88           C
ANISOU 2063  CD  LYS A 257     5470   2828   4954     61   -368    117       C
ATOM   2064  CE  LYS A 257     -85.311  27.625 -45.212  1.00 41.00           C
ANISOU 2064  CE  LYS A 257     6369   3638   5570     80   -413    168       C
ATOM   2065  NZ  LYS A 257     -84.171  27.989 -46.098  1.00 47.33           N
ANISOU 2065  NZ  LYS A 257     7254   4462   6266     10   -306    242       N
ATOM   2066  N   ARG A 258     -85.046  30.440 -39.781  1.00 43.73           N
ANISOU 2066  N   ARG A 258     6445   3682   6487    119   -473    141       N
ATOM   2067  CA  ARG A 258     -86.093  31.401 -39.453  1.00 40.10           C
ANISOU 2067  CA  ARG A 258     6004   3164   6068    199   -592    145       C
ATOM   2068  C   ARG A 258     -85.504  32.724 -38.982  1.00 44.39           C
ANISOU 2068  C   ARG A 258     6583   3590   6691    182   -600    187       C
ATOM   2069  O   ARG A 258     -86.045  33.794 -39.285  1.00 46.51           O
ANISOU 2069  O   ARG A 258     6931   3773   6967    227   -693    235       O
ATOM   2070  CB  ARG A 258     -87.016  30.814 -38.384  1.00 39.67           C
ANISOU 2070  CB  ARG A 258     5825   3171   6076    264   -639     50       C
ATOM   2071  CG  ARG A 258     -88.050  31.783 -37.828  1.00 44.86           C
ANISOU 2071  CG  ARG A 258     6470   3785   6790    357   -752     27       C
ATOM   2072  CD  ARG A 258     -89.215  31.971 -38.784  1.00 49.38           C
ANISOU 2072  CD  ARG A 258     7105   4362   7296    422   -858     48       C
ATOM   2073  NE  ARG A 258     -90.282  32.772 -38.189  1.00 49.91           N
ANISOU 2073  NE  ARG A 258     7135   4403   7427    525   -971      5       N
ATOM   2074  CZ  ARG A 258     -91.454  33.004 -38.771  1.00 52.26           C
ANISOU 2074  CZ  ARG A 258     7457   4708   7692    605  -1084      2       C
ATOM   2075  NH1 ARG A 258     -91.713  32.494 -39.967  1.00 58.25           N
ANISOU 2075  NH1 ARG A 258     8283   5501   8350    591  -1103     43       N
ATOM   2076  NH2 ARG A 258     -92.368  33.744 -38.159  1.00 49.23           N
ANISOU 2076  NH2 ARG A 258     7024   4304   7376    706  -1182    -52       N
ATOM   2077  N   PHE A 259     -84.390  32.673 -38.249  1.00 45.07           N
ANISOU 2077  N   PHE A 259     6613   3665   6846    121   -514    168       N
ATOM   2078  CA  PHE A 259     -83.829  33.887 -37.668  1.00 44.08           C
ANISOU 2078  CA  PHE A 259     6505   3425   6817    104   -531    188       C
ATOM   2079  C   PHE A 259     -83.303  34.838 -38.734  1.00 48.28           C
ANISOU 2079  C   PHE A 259     7170   3860   7315     41   -525    311       C
ATOM   2080  O   PHE A 259     -83.332  36.059 -38.540  1.00 54.12           O
ANISOU 2080  O   PHE A 259     7962   4473   8128     52   -593    347       O
ATOM   2081  CB  PHE A 259     -82.720  33.530 -36.681  1.00 47.47           C
ANISOU 2081  CB  PHE A 259     6838   3876   7324     49   -443    134       C
ATOM   2082  CG  PHE A 259     -82.280  34.679 -35.827  1.00 54.66           C
ANISOU 2082  CG  PHE A 259     7739   4680   8351     47   -478    118       C
ATOM   2083  CD1 PHE A 259     -83.055  35.097 -34.757  1.00 56.14           C
ANISOU 2083  CD1 PHE A 259     7870   4855   8607    140   -567     35       C
ATOM   2084  CD2 PHE A 259     -81.094  35.341 -36.089  1.00 59.24           C
ANISOU 2084  CD2 PHE A 259     8359   5176   8974    -49   -423    179       C
ATOM   2085  CE1 PHE A 259     -82.656  36.155 -33.966  1.00 58.54           C
ANISOU 2085  CE1 PHE A 259     8165   5058   9019    146   -610      2       C
ATOM   2086  CE2 PHE A 259     -80.689  36.399 -35.301  1.00 65.37           C
ANISOU 2086  CE2 PHE A 259     9124   5842   9871    -54   -466    156       C
ATOM   2087  CZ  PHE A 259     -81.471  36.807 -34.238  1.00 64.52           C
ANISOU 2087  CZ  PHE A 259     8967   5717   9831     48   -565     62       C
ATOM   2088  N   LYS A 260     -82.818  34.307 -39.858  1.00 50.59           N
ANISOU 2088  N   LYS A 260     7518   4208   7495    -25   -445    376       N
ATOM   2089  CA  LYS A 260     -82.351  35.171 -40.935  1.00 55.36           C
ANISOU 2089  CA  LYS A 260     8252   4739   8043    -93   -431    510       C
ATOM   2090  C   LYS A 260     -83.504  35.930 -41.579  1.00 59.71           C
ANISOU 2090  C   LYS A 260     8914   5224   8549    -18   -566    574       C
ATOM   2091  O   LYS A 260     -83.318  37.057 -42.051  1.00 61.68           O
ANISOU 2091  O   LYS A 260     9271   5355   8809    -50   -605    686       O
ATOM   2092  CB  LYS A 260     -81.602  34.347 -41.982  1.00 59.11           C
ANISOU 2092  CB  LYS A 260     8751   5320   8389   -172   -308    552       C
ATOM   2093  CG  LYS A 260     -80.293  34.968 -42.441  1.00 65.14           C
ANISOU 2093  CG  LYS A 260     9558   6040   9152   -297   -204    653       C
ATOM   2094  CD  LYS A 260     -79.642  34.142 -43.541  1.00 67.49           C
ANISOU 2094  CD  LYS A 260     9875   6467   9303   -361    -80    682       C
ATOM   2095  CE  LYS A 260     -78.310  34.742 -43.968  1.00 65.17           C
ANISOU 2095  CE  LYS A 260     9604   6149   9008   -494     38    782       C
ATOM   2096  NZ  LYS A 260     -77.713  34.013 -45.122  1.00 61.54           N
ANISOU 2096  NZ  LYS A 260     9166   5831   8386   -550    163    811       N
ATOM   2097  N   GLU A 261     -84.697  35.336 -41.598  1.00 64.53           N
ANISOU 2097  N   GLU A 261     9497   5904   9116     81   -645    508       N
ATOM   2098  CA  GLU A 261     -85.857  35.995 -42.188  1.00 70.45           C
ANISOU 2098  CA  GLU A 261    10339   6601   9826    168   -786    554       C
ATOM   2099  C   GLU A 261     -86.508  36.953 -41.197  1.00 66.49           C
ANISOU 2099  C   GLU A 261     9808   5992   9464    254   -904    505       C
ATOM   2100  O   GLU A 261     -86.630  38.153 -41.461  1.00 67.66           O
ANISOU 2100  O   GLU A 261    10055   6003   9651    270   -990    584       O
ATOM   2101  CB  GLU A 261     -86.871  34.948 -42.657  1.00 84.47           C
ANISOU 2101  CB  GLU A 261    12088   8504  11504    235   -825    494       C
ATOM   2102  CG  GLU A 261     -86.251  33.690 -43.234  1.00 97.41           C
ANISOU 2102  CG  GLU A 261    13702  10270  13038    168   -704    476       C
ATOM   2103  CD  GLU A 261     -87.280  32.608 -43.498  1.00107.36           C
ANISOU 2103  CD  GLU A 261    14914  11641  14237    234   -756    394       C
ATOM   2104  OE1 GLU A 261     -87.118  31.857 -44.483  1.00110.57           O
ANISOU 2104  OE1 GLU A 261    15361  12132  14517    206   -713    403       O
ATOM   2105  OE2 GLU A 261     -88.254  32.510 -42.721  1.00110.30           O
ANISOU 2105  OE2 GLU A 261    15203  12020  14687    314   -838    314       O
ATOM   2106  N   SER A 262     -86.934  36.432 -40.047  1.00 61.42           N
ANISOU 2106  N   SER A 262     9029   5411   8897    313   -911    372       N
ATOM   2107  CA  SER A 262     -87.648  37.206 -39.048  1.00 61.65           C
ANISOU 2107  CA  SER A 262     9007   5373   9044    412  -1018    296       C
ATOM   2108  C   SER A 262     -87.036  36.979 -37.673  1.00 54.80           C
ANISOU 2108  C   SER A 262     8014   4532   8275    393   -950    197       C
ATOM   2109  O   SER A 262     -86.606  35.864 -37.359  1.00 58.06           O
ANISOU 2109  O   SER A 262     8344   5059   8659    346   -849    154       O
ATOM   2110  CB  SER A 262     -89.135  36.822 -39.024  1.00 68.21           C
ANISOU 2110  CB  SER A 262     9785   6284   9847    532  -1119    223       C
ATOM   2111  OG  SER A 262     -89.826  37.527 -38.009  1.00 78.61           O
ANISOU 2111  OG  SER A 262    11036   7559  11274    636  -1212    132       O
ATOM   2112  N   PRO A 263     -86.980  38.011 -36.838  1.00 53.38           N
ANISOU 2112  N   PRO A 263     7822   4247   8213    433  -1013    155       N
ATOM   2113  CA  PRO A 263     -86.436  37.844 -35.488  1.00 50.76           C
ANISOU 2113  CA  PRO A 263     7372   3949   7966    426   -962     52       C
ATOM   2114  C   PRO A 263     -87.460  37.236 -34.540  1.00 47.04           C
ANISOU 2114  C   PRO A 263     6772   3606   7497    527   -993    -73       C
ATOM   2115  O   PRO A 263     -88.661  37.197 -34.813  1.00 51.73           O
ANISOU 2115  O   PRO A 263     7360   4237   8058    616  -1074    -94       O
ATOM   2116  CB  PRO A 263     -86.090  39.278 -35.076  1.00 57.26           C
ANISOU 2116  CB  PRO A 263     8241   4611   8905    438  -1033     51       C
ATOM   2117  CG  PRO A 263     -87.101  40.107 -35.803  1.00 60.14           C
ANISOU 2117  CG  PRO A 263     8692   4913   9247    517  -1153     97       C
ATOM   2118  CD  PRO A 263     -87.346  39.410 -37.120  1.00 56.56           C
ANISOU 2118  CD  PRO A 263     8326   4484   8679    486  -1141    202       C
ATOM   2119  N   PHE A 264     -86.956  36.757 -33.407  1.00 38.01           N
ANISOU 2119  N   PHE A 264     5518   2534   6388    510   -927   -153       N
ATOM   2120  CA  PHE A 264     -87.805  36.191 -32.367  1.00 37.48           C
ANISOU 2120  CA  PHE A 264     5320   2600   6320    592   -940   -263       C
ATOM   2121  C   PHE A 264     -87.045  36.227 -31.050  1.00 40.34           C
ANISOU 2121  C   PHE A 264     5597   2988   6742    579   -895   -342       C
ATOM   2122  O   PHE A 264     -85.833  36.451 -31.014  1.00 42.42           O
ANISOU 2122  O   PHE A 264     5891   3181   7044    497   -844   -311       O
ATOM   2123  CB  PHE A 264     -88.247  34.764 -32.709  1.00 40.62           C
ANISOU 2123  CB  PHE A 264     5666   3140   6629    567   -881   -248       C
ATOM   2124  CG  PHE A 264     -87.133  33.885 -33.194  1.00 47.33           C
ANISOU 2124  CG  PHE A 264     6538   4007   7437    450   -768   -184       C
ATOM   2125  CD1 PHE A 264     -86.297  33.238 -32.298  1.00 49.76           C
ANISOU 2125  CD1 PHE A 264     6764   4373   7767    402   -685   -220       C
ATOM   2126  CD2 PHE A 264     -86.922  33.704 -34.550  1.00 52.67           C
ANISOU 2126  CD2 PHE A 264     7316   4650   8047    396   -749    -94       C
ATOM   2127  CE1 PHE A 264     -85.270  32.429 -32.747  1.00 52.18           C
ANISOU 2127  CE1 PHE A 264     7084   4696   8045    306   -588   -174       C
ATOM   2128  CE2 PHE A 264     -85.899  32.898 -35.005  1.00 55.73           C
ANISOU 2128  CE2 PHE A 264     7716   5065   8395    299   -643    -51       C
ATOM   2129  CZ  PHE A 264     -85.072  32.259 -34.104  1.00 55.00           C
ANISOU 2129  CZ  PHE A 264     7535   5022   8340    256   -564    -95       C
ATOM   2130  N   GLU A 265     -87.775  36.000 -29.963  1.00 39.72           N
ANISOU 2130  N   GLU A 265     5404   3021   6666    661   -916   -445       N
ATOM   2131  CA  GLU A 265     -87.216  36.070 -28.621  1.00 39.63           C
ANISOU 2131  CA  GLU A 265     5307   3056   6695    670   -890   -532       C
ATOM   2132  C   GLU A 265     -87.002  34.664 -28.080  1.00 41.22           C
ANISOU 2132  C   GLU A 265     5416   3413   6835    622   -792   -531       C
ATOM   2133  O   GLU A 265     -87.894  33.815 -28.174  1.00 43.16           O
ANISOU 2133  O   GLU A 265     5608   3769   7021    641   -780   -524       O
ATOM   2134  CB  GLU A 265     -88.135  36.858 -27.688  1.00 46.29           C
ANISOU 2134  CB  GLU A 265     6086   3928   7573    802   -980   -655       C
ATOM   2135  CG  GLU A 265     -87.417  37.476 -26.501  1.00 57.26           C
ANISOU 2135  CG  GLU A 265     7432   5300   9024    823   -989   -752       C
ATOM   2136  CD  GLU A 265     -86.505  38.621 -26.904  1.00 67.67           C
ANISOU 2136  CD  GLU A 265     8852   6434  10426    775  -1028   -721       C
ATOM   2137  OE1 GLU A 265     -86.899  39.420 -27.781  1.00 69.45           O
ANISOU 2137  OE1 GLU A 265     9164   6568  10656    785  -1087   -664       O
ATOM   2138  OE2 GLU A 265     -85.390  38.718 -26.349  1.00 73.11           O
ANISOU 2138  OE2 GLU A 265     9525   7107  11146    712   -986   -737       O
ATOM   2139  N   LEU A 266     -85.820  34.423 -27.517  1.00 43.14           N
ANISOU 2139  N   LEU A 266     5637   3656   7100    557   -730   -535       N
ATOM   2140  CA  LEU A 266     -85.480  33.150 -26.894  1.00 41.73           C
ANISOU 2140  CA  LEU A 266     5375   3606   6875    514   -649   -532       C
ATOM   2141  C   LEU A 266     -85.147  33.398 -25.431  1.00 42.27           C
ANISOU 2141  C   LEU A 266     5361   3738   6964    555   -656   -625       C
ATOM   2142  O   LEU A 266     -84.161  34.077 -25.122  1.00 46.80           O
ANISOU 2142  O   LEU A 266     5956   4229   7598    533   -664   -654       O
ATOM   2143  CB  LEU A 266     -84.306  32.476 -27.607  1.00 40.69           C
ANISOU 2143  CB  LEU A 266     5288   3431   6743    403   -569   -452       C
ATOM   2144  CG  LEU A 266     -84.613  31.687 -28.883  1.00 44.89           C
ANISOU 2144  CG  LEU A 266     5871   3964   7220    358   -537   -370       C
ATOM   2145  CD1 LEU A 266     -83.361  30.988 -29.377  1.00 47.83           C
ANISOU 2145  CD1 LEU A 266     6265   4316   7592    260   -452   -319       C
ATOM   2146  CD2 LEU A 266     -85.728  30.678 -28.655  1.00 43.04           C
ANISOU 2146  CD2 LEU A 266     5565   3856   6932    392   -540   -379       C
ATOM   2147  N   GLU A 267     -85.967  32.855 -24.538  1.00 38.96           N
ANISOU 2147  N   GLU A 267     4844   3470   6489    611   -653   -671       N
ATOM   2148  CA  GLU A 267     -85.776  33.000 -23.100  1.00 40.14           C
ANISOU 2148  CA  GLU A 267     4909   3715   6627    660   -657   -760       C
ATOM   2149  C   GLU A 267     -85.089  31.740 -22.588  1.00 34.71           C
ANISOU 2149  C   GLU A 267     4171   3120   5897    591   -580   -712       C
ATOM   2150  O   GLU A 267     -85.710  30.677 -22.499  1.00 34.08           O
ANISOU 2150  O   GLU A 267     4040   3151   5757    576   -542   -665       O
ATOM   2151  CB  GLU A 267     -87.112  33.230 -22.396  1.00 48.35           C
ANISOU 2151  CB  GLU A 267     5869   4882   7621    767   -697   -839       C
ATOM   2152  CG  GLU A 267     -87.131  34.396 -21.423  1.00 62.86           C
ANISOU 2152  CG  GLU A 267     7676   6721   9486    865   -763   -975       C
ATOM   2153  CD  GLU A 267     -87.071  33.950 -19.977  1.00 75.66           C
ANISOU 2153  CD  GLU A 267     9192   8522  11034    897   -731  -1038       C
ATOM   2154  OE1 GLU A 267     -86.066  34.259 -19.305  1.00 79.07           O
ANISOU 2154  OE1 GLU A 267     9625   8930  11488    888   -739  -1086       O
ATOM   2155  OE2 GLU A 267     -88.026  33.287 -19.515  1.00 80.03           O
ANISOU 2155  OE2 GLU A 267     9658   9244  11504    927   -699  -1035       O
ATOM   2156  N   ASP A 268     -83.805  31.861 -22.259  1.00 32.47           N
ANISOU 2156  N   ASP A 268     3899   2784   5653    547   -564   -722       N
ATOM   2157  CA  ASP A 268     -83.004  30.735 -21.781  1.00 31.40           C
ANISOU 2157  CA  ASP A 268     3722   2717   5491    488   -505   -679       C
ATOM   2158  C   ASP A 268     -83.169  30.623 -20.264  1.00 32.35           C
ANISOU 2158  C   ASP A 268     3752   2985   5553    548   -517   -746       C
ATOM   2159  O   ASP A 268     -82.299  30.993 -19.476  1.00 37.47           O
ANISOU 2159  O   ASP A 268     4382   3635   6221    558   -536   -806       O
ATOM   2160  CB  ASP A 268     -81.548  30.922 -22.191  1.00 35.06           C
ANISOU 2160  CB  ASP A 268     4231   3062   6028    416   -485   -663       C
ATOM   2161  CG  ASP A 268     -80.687  29.723 -21.871  1.00 38.98           C
ANISOU 2161  CG  ASP A 268     4688   3613   6510    360   -431   -618       C
ATOM   2162  OD1 ASP A 268     -81.237  28.684 -21.444  1.00 40.84           O
ANISOU 2162  OD1 ASP A 268     4876   3962   6682    368   -410   -581       O
ATOM   2163  OD2 ASP A 268     -79.455  29.820 -22.048  1.00 42.32           O
ANISOU 2163  OD2 ASP A 268     5124   3963   6993    308   -413   -618       O
ATOM   2164  N   PHE A 269     -84.326  30.091 -19.861  1.00 32.89           N
ANISOU 2164  N   PHE A 269     3761   3192   5544    587   -507   -735       N
ATOM   2165  CA  PHE A 269     -84.685  30.109 -18.447  1.00 36.30           C
ANISOU 2165  CA  PHE A 269     4106   3787   5899    654   -516   -800       C
ATOM   2166  C   PHE A 269     -83.926  29.078 -17.622  1.00 34.58           C
ANISOU 2166  C   PHE A 269     3848   3658   5633    610   -477   -750       C
ATOM   2167  O   PHE A 269     -84.013  29.114 -16.389  1.00 35.66           O
ANISOU 2167  O   PHE A 269     3920   3934   5694    661   -485   -800       O
ATOM   2168  CB  PHE A 269     -86.198  29.926 -18.276  1.00 38.69           C
ANISOU 2168  CB  PHE A 269     4345   4222   6133    705   -510   -804       C
ATOM   2169  CG  PHE A 269     -86.747  28.661 -18.881  1.00 39.43           C
ANISOU 2169  CG  PHE A 269     4428   4350   6205    633   -459   -684       C
ATOM   2170  CD1 PHE A 269     -86.921  27.528 -18.105  1.00 37.75           C
ANISOU 2170  CD1 PHE A 269     4145   4279   5919    599   -412   -617       C
ATOM   2171  CD2 PHE A 269     -87.123  28.615 -20.216  1.00 38.77           C
ANISOU 2171  CD2 PHE A 269     4402   4156   6172    601   -466   -638       C
ATOM   2172  CE1 PHE A 269     -87.438  26.367 -18.649  1.00 37.79           C
ANISOU 2172  CE1 PHE A 269     4138   4300   5922    528   -376   -510       C
ATOM   2173  CE2 PHE A 269     -87.643  27.455 -20.767  1.00 35.25           C
ANISOU 2173  CE2 PHE A 269     3942   3738   5713    538   -430   -544       C
ATOM   2174  CZ  PHE A 269     -87.800  26.330 -19.981  1.00 37.19           C
ANISOU 2174  CZ  PHE A 269     4116   4110   5903    500   -387   -482       C
ATOM   2175  N   ILE A 270     -83.191  28.170 -18.255  1.00 33.32           N
ANISOU 2175  N   ILE A 270     3723   3425   5511    524   -440   -656       N
ATOM   2176  CA  ILE A 270     -82.227  27.336 -17.542  1.00 29.59           C
ANISOU 2176  CA  ILE A 270     3225   2997   5020    489   -423   -617       C
ATOM   2177  C   ILE A 270     -80.859  27.599 -18.160  1.00 30.90           C
ANISOU 2177  C   ILE A 270     3444   3013   5284    442   -426   -627       C
ATOM   2178  O   ILE A 270     -80.389  26.802 -18.985  1.00 32.27           O
ANISOU 2178  O   ILE A 270     3647   3114   5498    374   -391   -553       O
ATOM   2179  CB  ILE A 270     -82.600  25.847 -17.604  1.00 34.69           C
ANISOU 2179  CB  ILE A 270     3848   3706   5628    434   -379   -497       C
ATOM   2180  CG1 ILE A 270     -84.060  25.642 -17.201  1.00 38.49           C
ANISOU 2180  CG1 ILE A 270     4270   4327   6026    464   -367   -479       C
ATOM   2181  CG2 ILE A 270     -81.699  25.040 -16.683  1.00 35.34           C
ANISOU 2181  CG2 ILE A 270     3900   3844   5682    416   -378   -458       C
ATOM   2182  CD1 ILE A 270     -84.500  24.194 -17.223  1.00 40.72           C
ANISOU 2182  CD1 ILE A 270     4526   4665   6282    400   -330   -355       C
ATOM   2183  N   PRO A 271     -80.195  28.704 -17.805  1.00 29.87           N
ANISOU 2183  N   PRO A 271     3321   2833   5197    473   -469   -724       N
ATOM   2184  CA  PRO A 271     -78.930  29.051 -18.467  1.00 30.52           C
ANISOU 2184  CA  PRO A 271     3444   2770   5381    416   -467   -732       C
ATOM   2185  C   PRO A 271     -77.777  28.149 -18.054  1.00 32.47           C
ANISOU 2185  C   PRO A 271     3658   3039   5641    377   -450   -701       C
ATOM   2186  O   PRO A 271     -77.054  28.438 -17.096  1.00 39.00           O
ANISOU 2186  O   PRO A 271     4446   3904   6470    403   -489   -767       O
ATOM   2187  CB  PRO A 271     -78.695  30.501 -18.029  1.00 27.24           C
ANISOU 2187  CB  PRO A 271     3032   2306   5012    464   -530   -851       C
ATOM   2188  CG  PRO A 271     -79.390  30.607 -16.717  1.00 27.78           C
ANISOU 2188  CG  PRO A 271     3040   2530   4983    553   -565   -919       C
ATOM   2189  CD  PRO A 271     -80.595  29.709 -16.805  1.00 29.48           C
ANISOU 2189  CD  PRO A 271     3236   2856   5109    561   -523   -839       C
ATOM   2190  N   MET A 272     -77.599  27.052 -18.783  1.00 29.87           N
ANISOU 2190  N   MET A 272     3343   2683   5323    320   -402   -610       N
ATOM   2191  CA  MET A 272     -76.521  26.114 -18.510  1.00 29.86           C
ANISOU 2191  CA  MET A 272     3311   2689   5347    289   -391   -579       C
ATOM   2192  C   MET A 272     -76.196  25.370 -19.793  1.00 30.79           C
ANISOU 2192  C   MET A 272     3464   2718   5517    223   -338   -514       C
ATOM   2193  O   MET A 272     -76.972  25.382 -20.752  1.00 35.22           O
ANISOU 2193  O   MET A 272     4072   3241   6070    205   -311   -479       O
ATOM   2194  CB  MET A 272     -76.897  25.127 -17.401  1.00 28.02           C
ANISOU 2194  CB  MET A 272     3030   2590   5025    320   -406   -532       C
ATOM   2195  CG  MET A 272     -78.103  24.268 -17.739  1.00 31.06           C
ANISOU 2195  CG  MET A 272     3425   3021   5356    306   -376   -442       C
ATOM   2196  SD  MET A 272     -78.423  22.993 -16.511  1.00 39.43           S
ANISOU 2196  SD  MET A 272     4433   4224   6324    318   -387   -355       S
ATOM   2197  CE  MET A 272     -76.991  21.938 -16.723  1.00 40.39           C
ANISOU 2197  CE  MET A 272     4557   4262   6529    278   -393   -312       C
ATOM   2198  N   ASP A 273     -75.037  24.721 -19.796  1.00 34.61           N
ANISOU 2198  N   ASP A 273     3922   3175   6052    196   -328   -507       N
ATOM   2199  CA  ASP A 273     -74.636  23.886 -20.919  1.00 34.77           C
ANISOU 2199  CA  ASP A 273     3964   3128   6118    145   -279   -461       C
ATOM   2200  C   ASP A 273     -75.316  22.528 -20.792  1.00 35.66           C
ANISOU 2200  C   ASP A 273     4072   3289   6188    150   -280   -383       C
ATOM   2201  O   ASP A 273     -75.095  21.806 -19.813  1.00 35.20           O
ANISOU 2201  O   ASP A 273     3974   3291   6111    173   -312   -358       O
ATOM   2202  CB  ASP A 273     -73.117  23.732 -20.957  1.00 33.85           C
ANISOU 2202  CB  ASP A 273     3808   2970   6083    122   -270   -498       C
ATOM   2203  CG  ASP A 273     -72.604  23.358 -22.334  1.00 34.23           C
ANISOU 2203  CG  ASP A 273     3880   2942   6184     69   -206   -484       C
ATOM   2204  OD1 ASP A 273     -73.314  23.626 -23.326  1.00 32.70           O
ANISOU 2204  OD1 ASP A 273     3746   2712   5965     46   -172   -458       O
ATOM   2205  OD2 ASP A 273     -71.493  22.793 -22.425  1.00 32.85           O
ANISOU 2205  OD2 ASP A 273     3661   2751   6069     56   -193   -504       O
ATOM   2206  N   SER A 274     -76.153  22.188 -21.768  1.00 24.18           N
ANISOU 2206  N   SER A 274     2662   1806   4720    127   -251   -342       N
ATOM   2207  CA  SER A 274     -76.830  20.902 -21.769  1.00 27.31           C
ANISOU 2207  CA  SER A 274     3054   2228   5094    120   -256   -270       C
ATOM   2208  C   SER A 274     -77.056  20.462 -23.207  1.00 26.58           C
ANISOU 2208  C   SER A 274     3009   2061   5028     83   -220   -256       C
ATOM   2209  O   SER A 274     -77.120  21.289 -24.121  1.00 25.34           O
ANISOU 2209  O   SER A 274     2896   1861   4872     70   -193   -286       O
ATOM   2210  CB  SER A 274     -78.161  20.958 -21.008  1.00 32.18           C
ANISOU 2210  CB  SER A 274     3655   2940   5631    144   -278   -233       C
ATOM   2211  OG  SER A 274     -79.047  21.893 -21.595  1.00 45.60           O
ANISOU 2211  OG  SER A 274     5387   4634   7305    152   -269   -260       O
ATOM   2212  N   THR A 275     -77.168  19.145 -23.395  1.00 31.18           N
ANISOU 2212  N   THR A 275     3587   2629   5632     68   -227   -210       N
ATOM   2213  CA  THR A 275     -77.360  18.599 -24.735  1.00 31.93           C
ANISOU 2213  CA  THR A 275     3723   2659   5749     40   -203   -211       C
ATOM   2214  C   THR A 275     -78.673  19.076 -25.342  1.00 30.80           C
ANISOU 2214  C   THR A 275     3619   2530   5554     34   -202   -198       C
ATOM   2215  O   THR A 275     -78.721  19.448 -26.521  1.00 34.01           O
ANISOU 2215  O   THR A 275     4075   2893   5954     21   -175   -224       O
ATOM   2216  CB  THR A 275     -77.308  17.072 -24.687  1.00 35.33           C
ANISOU 2216  CB  THR A 275     4138   3063   6225     30   -229   -171       C
ATOM   2217  OG1 THR A 275     -76.010  16.651 -24.247  1.00 38.43           O
ANISOU 2217  OG1 THR A 275     4496   3432   6675     45   -237   -192       O
ATOM   2218  CG2 THR A 275     -77.588  16.481 -26.060  1.00 36.78           C
ANISOU 2218  CG2 THR A 275     4363   3184   6428      8   -214   -189       C
ATOM   2219  N   VAL A 276     -79.744  19.081 -24.555  1.00 29.47           N
ANISOU 2219  N   VAL A 276     3424   2432   5342     47   -230   -158       N
ATOM   2220  CA  VAL A 276     -81.037  19.610 -24.972  1.00 29.06           C
ANISOU 2220  CA  VAL A 276     3391   2408   5244     52   -238   -154       C
ATOM   2221  C   VAL A 276     -81.277  20.917 -24.230  1.00 26.60           C
ANISOU 2221  C   VAL A 276     3065   2152   4890     94   -246   -187       C
ATOM   2222  O   VAL A 276     -81.195  20.963 -22.997  1.00 27.20           O
ANISOU 2222  O   VAL A 276     3091   2300   4944    116   -259   -181       O
ATOM   2223  CB  VAL A 276     -82.175  18.610 -24.704  1.00 31.08           C
ANISOU 2223  CB  VAL A 276     3612   2708   5489     33   -262    -93       C
ATOM   2224  CG1 VAL A 276     -83.525  19.264 -24.962  1.00 33.54           C
ANISOU 2224  CG1 VAL A 276     3921   3068   5754     48   -274   -100       C
ATOM   2225  CG2 VAL A 276     -82.009  17.376 -25.572  1.00 26.02           C
ANISOU 2225  CG2 VAL A 276     2992   1991   4902     -5   -268    -77       C
ATOM   2226  N   LYS A 277     -81.564  21.976 -24.980  1.00 29.45           N
ANISOU 2226  N   LYS A 277     3472   2477   5239    108   -244   -224       N
ATOM   2227  CA  LYS A 277     -81.873  23.277 -24.408  1.00 32.56           C
ANISOU 2227  CA  LYS A 277     3860   2903   5608    154   -264   -267       C
ATOM   2228  C   LYS A 277     -83.372  23.531 -24.476  1.00 33.25           C
ANISOU 2228  C   LYS A 277     3935   3046   5652    186   -291   -264       C
ATOM   2229  O   LYS A 277     -84.031  23.173 -25.457  1.00 33.17           O
ANISOU 2229  O   LYS A 277     3954   3008   5639    168   -295   -241       O
ATOM   2230  CB  LYS A 277     -81.119  24.391 -25.138  1.00 35.77           C
ANISOU 2230  CB  LYS A 277     4328   3217   6046    150   -255   -307       C
ATOM   2231  CG  LYS A 277     -79.616  24.377 -24.912  1.00 36.53           C
ANISOU 2231  CG  LYS A 277     4414   3272   6191    123   -229   -326       C
ATOM   2232  CD  LYS A 277     -79.275  24.618 -23.449  1.00 35.89           C
ANISOU 2232  CD  LYS A 277     4272   3257   6108    158   -255   -360       C
ATOM   2233  CE  LYS A 277     -79.772  25.975 -22.978  1.00 34.29           C
ANISOU 2233  CE  LYS A 277     4073   3064   5890    208   -294   -416       C
ATOM   2234  NZ  LYS A 277     -79.481  26.200 -21.535  1.00 37.30           N
ANISOU 2234  NZ  LYS A 277     4393   3525   6254    250   -324   -463       N
ATOM   2235  N   ASN A 278     -83.907  24.144 -23.425  1.00 33.32           N
ANISOU 2235  N   ASN A 278     3893   3140   5625    237   -313   -296       N
ATOM   2236  CA  ASN A 278     -85.322  24.484 -23.338  1.00 30.87           C
ANISOU 2236  CA  ASN A 278     3551   2903   5276    279   -338   -308       C
ATOM   2237  C   ASN A 278     -85.458  25.999 -23.319  1.00 32.31           C
ANISOU 2237  C   ASN A 278     3759   3056   5462    345   -374   -386       C
ATOM   2238  O   ASN A 278     -84.857  26.670 -22.472  1.00 27.94           O
ANISOU 2238  O   ASN A 278     3190   2515   4910    377   -383   -438       O
ATOM   2239  CB  ASN A 278     -85.961  23.866 -22.095  1.00 34.91           C
ANISOU 2239  CB  ASN A 278     3967   3561   5735    289   -330   -285       C
ATOM   2240  CG  ASN A 278     -86.017  22.352 -22.161  1.00 46.98           C
ANISOU 2240  CG  ASN A 278     5474   5104   7274    219   -308   -195       C
ATOM   2241  OD1 ASN A 278     -86.115  21.770 -23.242  1.00 49.43           O
ANISOU 2241  OD1 ASN A 278     5824   5335   7622    177   -308   -166       O
ATOM   2242  ND2 ASN A 278     -85.957  21.706 -21.002  1.00 52.59           N
ANISOU 2242  ND2 ASN A 278     6123   5912   7948    208   -294   -151       N
ATOM   2243  N   TYR A 279     -86.246  26.533 -24.249  1.00 36.10           N
ANISOU 2243  N   TYR A 279     4279   3490   5947    367   -404   -395       N
ATOM   2244  CA  TYR A 279     -86.411  27.970 -24.402  1.00 34.81           C
ANISOU 2244  CA  TYR A 279     4155   3269   5803    430   -452   -460       C
ATOM   2245  C   TYR A 279     -87.885  28.345 -24.369  1.00 35.73           C
ANISOU 2245  C   TYR A 279     4228   3456   5893    500   -497   -494       C
ATOM   2246  O   TYR A 279     -88.738  27.602 -24.865  1.00 36.10           O
ANISOU 2246  O   TYR A 279     4252   3545   5920    482   -494   -454       O
ATOM   2247  CB  TYR A 279     -85.802  28.471 -25.718  1.00 32.38           C
ANISOU 2247  CB  TYR A 279     3956   2811   5534    395   -458   -433       C
ATOM   2248  CG  TYR A 279     -84.312  28.255 -25.854  1.00 33.89           C
ANISOU 2248  CG  TYR A 279     4183   2933   5760    328   -411   -410       C
ATOM   2249  CD1 TYR A 279     -83.415  28.948 -25.053  1.00 37.27           C
ANISOU 2249  CD1 TYR A 279     4599   3338   6224    338   -415   -459       C
ATOM   2250  CD2 TYR A 279     -83.803  27.379 -26.802  1.00 32.39           C
ANISOU 2250  CD2 TYR A 279     4032   2704   5570    259   -366   -352       C
ATOM   2251  CE1 TYR A 279     -82.051  28.760 -25.180  1.00 39.21           C
ANISOU 2251  CE1 TYR A 279     4862   3526   6509    276   -374   -444       C
ATOM   2252  CE2 TYR A 279     -82.441  27.186 -26.939  1.00 32.49           C
ANISOU 2252  CE2 TYR A 279     4063   2664   5617    204   -320   -341       C
ATOM   2253  CZ  TYR A 279     -81.570  27.879 -26.126  1.00 37.17           C
ANISOU 2253  CZ  TYR A 279     4636   3238   6251    210   -323   -384       C
ATOM   2254  OH  TYR A 279     -80.213  27.690 -26.257  1.00 43.48           O
ANISOU 2254  OH  TYR A 279     5438   3992   7092    154   -278   -379       O
ATOM   2255  N   PHE A 280     -88.172  29.501 -23.777  1.00 36.16           N
ANISOU 2255  N   PHE A 280     4266   3520   5954    584   -543   -578       N
ATOM   2256  CA  PHE A 280     -89.458  30.170 -23.938  1.00 32.71           C
ANISOU 2256  CA  PHE A 280     3803   3115   5511    669   -602   -631       C
ATOM   2257  C   PHE A 280     -89.325  31.076 -25.157  1.00 32.59           C
ANISOU 2257  C   PHE A 280     3903   2933   5546    679   -657   -621       C
ATOM   2258  O   PHE A 280     -88.605  32.079 -25.118  1.00 36.72           O
ANISOU 2258  O   PHE A 280     4486   3348   6116    696   -688   -655       O
ATOM   2259  CB  PHE A 280     -89.821  30.953 -22.677  1.00 30.14           C
ANISOU 2259  CB  PHE A 280     3399   2885   5169    765   -629   -740       C
ATOM   2260  CG  PHE A 280     -91.273  31.362 -22.590  1.00 33.38           C
ANISOU 2260  CG  PHE A 280     3738   3384   5561    858   -676   -804       C
ATOM   2261  CD1 PHE A 280     -92.022  31.619 -23.728  1.00 38.97           C
ANISOU 2261  CD1 PHE A 280     4491   4018   6298    879   -728   -785       C
ATOM   2262  CD2 PHE A 280     -91.885  31.496 -21.354  1.00 35.19           C
ANISOU 2262  CD2 PHE A 280     3851   3782   5739    931   -667   -887       C
ATOM   2263  CE1 PHE A 280     -93.350  31.999 -23.637  1.00 38.16           C
ANISOU 2263  CE1 PHE A 280     4311   4000   6188    972   -778   -853       C
ATOM   2264  CE2 PHE A 280     -93.214  31.875 -21.256  1.00 36.93           C
ANISOU 2264  CE2 PHE A 280     3988   4097   5946   1023   -705   -958       C
ATOM   2265  CZ  PHE A 280     -93.946  32.126 -22.399  1.00 36.52           C
ANISOU 2265  CZ  PHE A 280     3976   3962   5938   1044   -763   -942       C
ATOM   2266  N   ILE A 281     -90.006  30.717 -26.239  1.00 34.50           N
ANISOU 2266  N   ILE A 281     4178   3153   5778    664   -675   -570       N
ATOM   2267  CA  ILE A 281     -89.835  31.368 -27.531  1.00 35.55           C
ANISOU 2267  CA  ILE A 281     4432   3137   5937    657   -720   -532       C
ATOM   2268  C   ILE A 281     -91.081  32.179 -27.856  1.00 35.19           C
ANISOU 2268  C   ILE A 281     4384   3086   5900    757   -813   -578       C
ATOM   2269  O   ILE A 281     -92.209  31.726 -27.628  1.00 37.05           O
ANISOU 2269  O   ILE A 281     4527   3440   6110    798   -827   -606       O
ATOM   2270  CB  ILE A 281     -89.538  30.335 -28.637  1.00 35.01           C
ANISOU 2270  CB  ILE A 281     4418   3044   5840    566   -676   -442       C
ATOM   2271  CG1 ILE A 281     -89.530  31.002 -30.014  1.00 41.49           C
ANISOU 2271  CG1 ILE A 281     5364   3739   6662    566   -724   -397       C
ATOM   2272  CG2 ILE A 281     -90.538  29.188 -28.584  1.00 38.28           C
ANISOU 2272  CG2 ILE A 281     4744   3581   6219    558   -664   -433       C
ATOM   2273  CD1 ILE A 281     -89.141  30.070 -31.137  1.00 48.34           C
ANISOU 2273  CD1 ILE A 281     6291   4587   7488    484   -680   -323       C
ATOM   2274  N   THR A 282     -90.872  33.388 -28.376  1.00 33.89           N
ANISOU 2274  N   THR A 282     4316   2779   5779    796   -882   -583       N
ATOM   2275  CA  THR A 282     -91.948  34.249 -28.853  1.00 31.45           C
ANISOU 2275  CA  THR A 282     4029   2430   5491    897   -989   -618       C
ATOM   2276  C   THR A 282     -91.566  34.770 -30.229  1.00 35.14           C
ANISOU 2276  C   THR A 282     4649   2737   5966    863  -1030   -528       C
ATOM   2277  O   THR A 282     -90.554  35.464 -30.371  1.00 39.84           O
ANISOU 2277  O   THR A 282     5332   3203   6601    823  -1026   -497       O
ATOM   2278  CB  THR A 282     -92.203  35.415 -27.892  1.00 34.64           C
ANISOU 2278  CB  THR A 282     4392   2819   5950   1008  -1056   -732       C
ATOM   2279  OG1 THR A 282     -92.578  34.908 -26.606  1.00 38.74           O
ANISOU 2279  OG1 THR A 282     4766   3515   6439   1040  -1009   -813       O
ATOM   2280  CG2 THR A 282     -93.318  36.304 -28.423  1.00 32.94           C
ANISOU 2280  CG2 THR A 282     4198   2550   5766   1123  -1179   -771       C
ATOM   2281  N   ASP A 283     -92.367  34.433 -31.237  1.00 31.98           N
ANISOU 2281  N   ASP A 283     4277   2348   5524    874  -1071   -485       N
ATOM   2282  CA  ASP A 283     -92.108  34.888 -32.596  1.00 34.27           C
ANISOU 2282  CA  ASP A 283     4717   2506   5798    846  -1114   -392       C
ATOM   2283  C   ASP A 283     -92.631  36.308 -32.773  1.00 40.19           C
ANISOU 2283  C   ASP A 283     5528   3136   6604    951  -1243   -415       C
ATOM   2284  O   ASP A 283     -93.808  36.582 -32.518  1.00 44.27           O
ANISOU 2284  O   ASP A 283     5976   3705   7139   1062  -1327   -491       O
ATOM   2285  CB  ASP A 283     -92.759  33.947 -33.608  1.00 36.02           C
ANISOU 2285  CB  ASP A 283     4948   2794   5945    823  -1117   -344       C
ATOM   2286  CG  ASP A 283     -92.470  34.346 -35.041  1.00 39.63           C
ANISOU 2286  CG  ASP A 283     5563   3139   6358    793  -1155   -243       C
ATOM   2287  OD1 ASP A 283     -91.310  34.192 -35.480  1.00 40.48           O
ANISOU 2287  OD1 ASP A 283     5749   3193   6440    695  -1077   -171       O
ATOM   2288  OD2 ASP A 283     -93.401  34.814 -35.730  1.00 42.18           O
ANISOU 2288  OD2 ASP A 283     5927   3434   6666    869  -1264   -235       O
ATOM   2289  N   ALA A 284     -91.754  37.211 -33.217  1.00 38.71           N
ANISOU 2289  N   ALA A 284     5468   2788   6454    914  -1260   -350       N
ATOM   2290  CA  ALA A 284     -92.121  38.619 -33.317  1.00 36.99           C
ANISOU 2290  CA  ALA A 284     5318   2425   6311   1007  -1391   -366       C
ATOM   2291  C   ALA A 284     -93.011  38.907 -34.519  1.00 35.78           C
ANISOU 2291  C   ALA A 284     5252   2223   6120   1063  -1498   -303       C
ATOM   2292  O   ALA A 284     -93.832  39.830 -34.467  1.00 45.08           O
ANISOU 2292  O   ALA A 284     6430   3362   7338   1170  -1613   -349       O
ATOM   2293  CB  ALA A 284     -90.863  39.487 -33.380  1.00 38.25           C
ANISOU 2293  CB  ALA A 284     5574   2442   6516    924  -1363   -303       C
ATOM   2294  N   GLN A 285     -92.873  38.140 -35.601  1.00 35.44           N
ANISOU 2294  N   GLN A 285     5273   2215   5979    985  -1452   -203       N
ATOM   2295  CA  GLN A 285     -93.643  38.431 -36.805  1.00 41.62           C
ANISOU 2295  CA  GLN A 285     6152   2952   6711   1035  -1560   -135       C
ATOM   2296  C   GLN A 285     -95.103  38.020 -36.658  1.00 41.71           C
ANISOU 2296  C   GLN A 285     6050   3087   6712   1147  -1638   -229       C
ATOM   2297  O   GLN A 285     -96.004  38.773 -37.044  1.00 45.96           O
ANISOU 2297  O   GLN A 285     6621   3566   7275   1259  -1779   -241       O
ATOM   2298  CB  GLN A 285     -93.016  37.733 -38.013  1.00 41.19           C
ANISOU 2298  CB  GLN A 285     6199   2911   6540    921  -1486    -11       C
ATOM   2299  CG  GLN A 285     -93.682  38.070 -39.338  1.00 48.05           C
ANISOU 2299  CG  GLN A 285     7189   3733   7336    965  -1598     74       C
ATOM   2300  CD  GLN A 285     -93.573  39.543 -39.686  1.00 57.57           C
ANISOU 2300  CD  GLN A 285     8529   4747   8597   1007  -1710    151       C
ATOM   2301  OE1 GLN A 285     -92.494  40.038 -40.013  1.00 59.95           O
ANISOU 2301  OE1 GLN A 285     8939   4939   8900    912  -1659    256       O
ATOM   2302  NE2 GLN A 285     -94.694  40.253 -39.614  1.00 58.58           N
ANISOU 2302  NE2 GLN A 285     8646   4830   8780   1148  -1866     98       N
ATOM   2303  N   THR A 286     -95.358  36.836 -36.103  1.00 43.42           N
ANISOU 2303  N   THR A 286     6128   3470   6899   1117  -1552   -293       N
ATOM   2304  CA  THR A 286     -96.703  36.279 -36.055  1.00 42.26           C
ANISOU 2304  CA  THR A 286     5863   3455   6739   1195  -1608   -369       C
ATOM   2305  C   THR A 286     -97.346  36.327 -34.679  1.00 41.59           C
ANISOU 2305  C   THR A 286     5606   3475   6723   1274  -1605   -505       C
ATOM   2306  O   THR A 286     -98.573  36.410 -34.591  1.00 44.63           O
ANISOU 2306  O   THR A 286     5897   3933   7126   1377  -1690   -581       O
ATOM   2307  CB  THR A 286     -96.690  34.823 -36.534  1.00 38.48           C
ANISOU 2307  CB  THR A 286     5348   3096   6178   1099  -1525   -339       C
ATOM   2308  OG1 THR A 286     -95.967  34.016 -35.597  1.00 36.61           O
ANISOU 2308  OG1 THR A 286     5025   2935   5951   1014  -1388   -362       O
ATOM   2309  CG2 THR A 286     -96.026  34.720 -37.897  1.00 38.91           C
ANISOU 2309  CG2 THR A 286     5568   3072   6146   1025  -1517   -218       C
ATOM   2310  N   GLY A 287     -96.558  36.278 -33.610  1.00 40.26           N
ANISOU 2310  N   GLY A 287     5386   3326   6586   1230  -1509   -540       N
ATOM   2311  CA  GLY A 287     -97.100  36.191 -32.273  1.00 37.20           C
ANISOU 2311  CA  GLY A 287     4831   3068   6235   1294  -1487   -664       C
ATOM   2312  C   GLY A 287     -97.236  34.785 -31.735  1.00 36.58           C
ANISOU 2312  C   GLY A 287     4622   3167   6109   1216  -1373   -674       C
ATOM   2313  O   GLY A 287     -97.723  34.613 -30.610  1.00 36.96           O
ANISOU 2313  O   GLY A 287     4524   3349   6172   1259  -1342   -765       O
ATOM   2314  N   SER A 288     -96.834  33.776 -32.501  1.00 32.90           N
ANISOU 2314  N   SER A 288     4204   2709   5587   1106  -1314   -585       N
ATOM   2315  CA  SER A 288     -96.865  32.404 -32.017  1.00 35.10           C
ANISOU 2315  CA  SER A 288     4373   3130   5836   1022  -1212   -583       C
ATOM   2316  C   SER A 288     -95.769  32.195 -30.980  1.00 36.51           C
ANISOU 2316  C   SER A 288     4529   3322   6021    959  -1105   -583       C
ATOM   2317  O   SER A 288     -94.644  32.678 -31.138  1.00 30.84           O
ANISOU 2317  O   SER A 288     3918   2487   5313    921  -1081   -542       O
ATOM   2318  CB  SER A 288     -96.693  31.432 -33.182  1.00 34.00           C
ANISOU 2318  CB  SER A 288     4300   2974   5643    932  -1194   -500       C
ATOM   2319  OG  SER A 288     -97.179  30.146 -32.849  1.00 43.33           O
ANISOU 2319  OG  SER A 288     5360   4289   6814    876  -1141   -512       O
ATOM   2320  N   SER A 289     -96.099  31.477 -29.908  1.00 35.48           N
ANISOU 2320  N   SER A 289     4255   3342   5886    946  -1041   -625       N
ATOM   2321  CA  SER A 289     -95.171  31.313 -28.799  1.00 35.72           C
ANISOU 2321  CA  SER A 289     4252   3403   5915    904   -953   -634       C
ATOM   2322  C   SER A 289     -95.367  29.943 -28.164  1.00 33.20           C
ANISOU 2322  C   SER A 289     3817   3232   5566    828   -868   -611       C
ATOM   2323  O   SER A 289     -96.371  29.264 -28.391  1.00 34.32           O
ANISOU 2323  O   SER A 289     3878   3463   5699    822   -881   -609       O
ATOM   2324  CB  SER A 289     -95.349  32.426 -27.760  1.00 30.88           C
ANISOU 2324  CB  SER A 289     3588   2813   5332   1011   -989   -737       C
ATOM   2325  OG  SER A 289     -96.665  32.429 -27.236  1.00 31.67           O
ANISOU 2325  OG  SER A 289     3549   3058   5427   1094  -1019   -817       O
ATOM   2326  N   LYS A 290     -94.383  29.545 -27.358  1.00 28.96           N
ANISOU 2326  N   LYS A 290     3272   2714   5019    769   -787   -591       N
ATOM   2327  CA  LYS A 290     -94.430  28.277 -26.637  1.00 31.83           C
ANISOU 2327  CA  LYS A 290     3536   3203   5356    695   -709   -555       C
ATOM   2328  C   LYS A 290     -93.525  28.378 -25.418  1.00 28.28           C
ANISOU 2328  C   LYS A 290     3062   2791   4892    687   -650   -571       C
ATOM   2329  O   LYS A 290     -92.376  28.815 -25.534  1.00 27.86           O
ANISOU 2329  O   LYS A 290     3102   2626   4856    670   -642   -562       O
ATOM   2330  CB  LYS A 290     -94.002  27.111 -27.536  1.00 29.34           C
ANISOU 2330  CB  LYS A 290     3276   2831   5041    588   -678   -468       C
ATOM   2331  CG  LYS A 290     -94.024  25.754 -26.847  1.00 28.97           C
ANISOU 2331  CG  LYS A 290     3138   2885   4984    505   -610   -418       C
ATOM   2332  CD  LYS A 290     -94.098  24.614 -27.853  1.00 31.04           C
ANISOU 2332  CD  LYS A 290     3431   3102   5262    423   -612   -359       C
ATOM   2333  CE  LYS A 290     -92.930  24.644 -28.824  1.00 33.77           C
ANISOU 2333  CE  LYS A 290     3916   3303   5611    388   -606   -330       C
ATOM   2334  NZ  LYS A 290     -92.976  23.505 -29.783  1.00 34.00           N
ANISOU 2334  NZ  LYS A 290     3973   3295   5651    318   -610   -292       N
ATOM   2335  N   CYS A 291     -94.043  27.969 -24.258  1.00 29.34           N
ANISOU 2335  N   CYS A 291     3068   3089   4989    697   -610   -592       N
ATOM   2336  CA  CYS A 291     -93.304  28.132 -23.009  1.00 28.60           C
ANISOU 2336  CA  CYS A 291     2944   3056   4865    706   -565   -619       C
ATOM   2337  C   CYS A 291     -92.053  27.265 -22.983  1.00 27.71           C
ANISOU 2337  C   CYS A 291     2888   2884   4755    606   -510   -535       C
ATOM   2338  O   CYS A 291     -90.977  27.722 -22.581  1.00 34.03           O
ANISOU 2338  O   CYS A 291     3739   3629   5563    611   -503   -556       O
ATOM   2339  CB  CYS A 291     -94.201  27.798 -21.818  1.00 38.02           C
ANISOU 2339  CB  CYS A 291     3986   4462   5999    733   -528   -647       C
ATOM   2340  SG  CYS A 291     -95.577  28.931 -21.576  1.00 45.76           S
ANISOU 2340  SG  CYS A 291     4872   5540   6973    876   -588   -779       S
ATOM   2341  N   VAL A 292     -92.176  26.006 -23.386  1.00 34.99           N
ANISOU 2341  N   VAL A 292     3798   3817   5680    517   -478   -447       N
ATOM   2342  CA  VAL A 292     -91.070  25.056 -23.347  1.00 31.94           C
ANISOU 2342  CA  VAL A 292     3453   3379   5303    429   -432   -372       C
ATOM   2343  C   VAL A 292     -90.885  24.524 -24.760  1.00 36.60           C
ANISOU 2343  C   VAL A 292     4127   3844   5935    372   -446   -326       C
ATOM   2344  O   VAL A 292     -91.633  23.645 -25.208  1.00 40.22           O
ANISOU 2344  O   VAL A 292     4550   4329   6403    329   -450   -286       O
ATOM   2345  CB  VAL A 292     -91.315  23.916 -22.355  1.00 32.79           C
ANISOU 2345  CB  VAL A 292     3465   3618   5376    374   -382   -308       C
ATOM   2346  CG1 VAL A 292     -90.071  23.054 -22.234  1.00 32.58           C
ANISOU 2346  CG1 VAL A 292     3486   3524   5367    303   -350   -241       C
ATOM   2347  CG2 VAL A 292     -91.722  24.466 -21.004  1.00 34.03           C
ANISOU 2347  CG2 VAL A 292     3528   3935   5467    439   -366   -360       C
ATOM   2348  N   CYS A 293     -89.890  25.045 -25.466  1.00 37.31           N
ANISOU 2348  N   CYS A 293     4324   3803   6050    369   -452   -334       N
ATOM   2349  CA  CYS A 293     -89.537  24.571 -26.799  1.00 38.79           C
ANISOU 2349  CA  CYS A 293     4596   3882   6259    318   -456   -296       C
ATOM   2350  C   CYS A 293     -88.186  23.872 -26.692  1.00 36.51           C
ANISOU 2350  C   CYS A 293     4340   3542   5991    256   -405   -260       C
ATOM   2351  O   CYS A 293     -87.145  24.526 -26.586  1.00 30.56           O
ANISOU 2351  O   CYS A 293     3633   2729   5249    262   -390   -279       O
ATOM   2352  CB  CYS A 293     -89.502  25.722 -27.800  1.00 45.54           C
ANISOU 2352  CB  CYS A 293     5547   4639   7118    361   -499   -325       C
ATOM   2353  SG  CYS A 293     -89.438  25.188 -29.523  1.00 54.38           S
ANISOU 2353  SG  CYS A 293     6764   5668   8232    313   -512   -285       S
ATOM   2354  N   SER A 294     -88.210  22.542 -26.705  1.00 38.23           N
ANISOU 2354  N   SER A 294     4526   3778   6221    196   -386   -211       N
ATOM   2355  CA  SER A 294     -86.982  21.762 -26.624  1.00 35.11           C
ANISOU 2355  CA  SER A 294     4155   3333   5854    145   -348   -182       C
ATOM   2356  C   SER A 294     -86.234  21.843 -27.949  1.00 31.85           C
ANISOU 2356  C   SER A 294     3836   2809   5455    125   -340   -193       C
ATOM   2357  O   SER A 294     -86.781  21.502 -29.003  1.00 33.83           O
ANISOU 2357  O   SER A 294     4121   3032   5700    113   -362   -191       O
ATOM   2358  CB  SER A 294     -87.297  20.312 -26.270  1.00 37.29           C
ANISOU 2358  CB  SER A 294     4372   3646   6151     91   -343   -126       C
ATOM   2359  OG  SER A 294     -87.922  20.222 -25.001  1.00 39.28           O
ANISOU 2359  OG  SER A 294     4534   4015   6376     99   -338   -101       O
ATOM   2360  N   VAL A 295     -84.985  22.296 -27.894  1.00 31.83           N
ANISOU 2360  N   VAL A 295     3872   2755   5468    122   -309   -208       N
ATOM   2361  CA  VAL A 295     -84.163  22.495 -29.080  1.00 32.59           C
ANISOU 2361  CA  VAL A 295     4050   2764   5567     99   -285   -216       C
ATOM   2362  C   VAL A 295     -82.865  21.721 -28.907  1.00 31.48           C
ANISOU 2362  C   VAL A 295     3899   2596   5466     62   -241   -214       C
ATOM   2363  O   VAL A 295     -82.284  21.699 -27.816  1.00 30.70           O
ANISOU 2363  O   VAL A 295     3751   2523   5390     67   -232   -215       O
ATOM   2364  CB  VAL A 295     -83.878  23.992 -29.329  1.00 33.14           C
ANISOU 2364  CB  VAL A 295     4177   2789   5627    126   -290   -237       C
ATOM   2365  CG1 VAL A 295     -83.053  24.182 -30.593  1.00 32.54           C
ANISOU 2365  CG1 VAL A 295     4185   2638   5543     90   -255   -229       C
ATOM   2366  CG2 VAL A 295     -85.181  24.772 -29.416  1.00 30.99           C
ANISOU 2366  CG2 VAL A 295     3909   2539   5326    178   -347   -247       C
ATOM   2367  N   ILE A 296     -82.417  21.078 -29.982  1.00 29.63           N
ANISOU 2367  N   ILE A 296     3707   2316   5235     32   -219   -218       N
ATOM   2368  CA  ILE A 296     -81.154  20.352 -29.997  1.00 32.17           C
ANISOU 2368  CA  ILE A 296     4017   2608   5599      6   -179   -231       C
ATOM   2369  C   ILE A 296     -80.429  20.694 -31.292  1.00 32.85           C
ANISOU 2369  C   ILE A 296     4170   2649   5662    -12   -134   -254       C
ATOM   2370  O   ILE A 296     -81.059  20.891 -32.336  1.00 33.54           O
ANISOU 2370  O   ILE A 296     4316   2729   5699    -11   -145   -253       O
ATOM   2371  CB  ILE A 296     -81.374  18.830 -29.849  1.00 31.74           C
ANISOU 2371  CB  ILE A 296     3924   2555   5582     -9   -200   -219       C
ATOM   2372  CG1 ILE A 296     -80.043  18.107 -29.644  1.00 28.38           C
ANISOU 2372  CG1 ILE A 296     3474   2097   5212    -19   -172   -238       C
ATOM   2373  CG2 ILE A 296     -82.120  18.264 -31.050  1.00 29.48           C
ANISOU 2373  CG2 ILE A 296     3678   2248   5274    -18   -222   -231       C
ATOM   2374  CD1 ILE A 296     -80.198  16.641 -29.333  1.00 24.79           C
ANISOU 2374  CD1 ILE A 296     2983   1625   4812    -30   -207   -219       C
ATOM   2375  N   ASP A 297     -79.101  20.792 -31.218  1.00 31.03           N
ANISOU 2375  N   ASP A 297     3927   2398   5465    -29    -84   -275       N
ATOM   2376  CA  ASP A 297     -78.287  21.144 -32.380  1.00 32.21           C
ANISOU 2376  CA  ASP A 297     4127   2524   5589    -56    -25   -293       C
ATOM   2377  C   ASP A 297     -77.600  19.884 -32.896  1.00 35.77           C
ANISOU 2377  C   ASP A 297     4556   2973   6063    -63      5   -334       C
ATOM   2378  O   ASP A 297     -76.429  19.619 -32.629  1.00 37.89           O
ANISOU 2378  O   ASP A 297     4778   3237   6382    -71     44   -364       O
ATOM   2379  CB  ASP A 297     -77.278  22.231 -32.030  1.00 30.89           C
ANISOU 2379  CB  ASP A 297     3950   2339   5449    -77     15   -294       C
ATOM   2380  CG  ASP A 297     -76.448  22.661 -33.226  1.00 36.76           C
ANISOU 2380  CG  ASP A 297     4739   3067   6161   -118     88   -296       C
ATOM   2381  OD1 ASP A 297     -76.836  22.347 -34.373  1.00 37.29           O
ANISOU 2381  OD1 ASP A 297     4863   3144   6161   -122    101   -293       O
ATOM   2382  OD2 ASP A 297     -75.405  23.311 -33.019  1.00 43.34           O
ANISOU 2382  OD2 ASP A 297     5549   3886   7034   -150    132   -302       O
ATOM   2383  N   LEU A 298     -78.354  19.100 -33.655  1.00 32.85           N
ANISOU 2383  N   LEU A 298     4216   2604   5661    -55    -23   -345       N
ATOM   2384  CA  LEU A 298     -77.821  17.937 -34.344  1.00 29.92           C
ANISOU 2384  CA  LEU A 298     3837   2226   5307    -52     -5   -401       C
ATOM   2385  C   LEU A 298     -77.499  18.297 -35.786  1.00 32.82           C
ANISOU 2385  C   LEU A 298     4269   2612   5590    -64     52   -429       C
ATOM   2386  O   LEU A 298     -78.126  19.178 -36.380  1.00 35.79           O
ANISOU 2386  O   LEU A 298     4711   2999   5888    -71     48   -392       O
ATOM   2387  CB  LEU A 298     -78.816  16.774 -34.317  1.00 29.61           C
ANISOU 2387  CB  LEU A 298     3788   2171   5293    -38    -77   -407       C
ATOM   2388  CG  LEU A 298     -79.042  16.046 -32.993  1.00 31.08           C
ANISOU 2388  CG  LEU A 298     3906   2340   5562    -35   -128   -374       C
ATOM   2389  CD1 LEU A 298     -80.213  15.085 -33.117  1.00 29.35           C
ANISOU 2389  CD1 LEU A 298     3686   2104   5362    -39   -199   -365       C
ATOM   2390  CD2 LEU A 298     -77.783  15.304 -32.571  1.00 31.49           C
ANISOU 2390  CD2 LEU A 298     3908   2365   5692    -26   -109   -409       C
ATOM   2391  N   LEU A 299     -76.502  17.614 -36.343  1.00 35.04           N
ANISOU 2391  N   LEU A 299     4527   2902   5883    -62    103   -494       N
ATOM   2392  CA  LEU A 299     -76.291  17.676 -37.780  1.00 33.22           C
ANISOU 2392  CA  LEU A 299     4356   2712   5557    -68    156   -531       C
ATOM   2393  C   LEU A 299     -77.545  17.174 -38.479  1.00 35.85           C
ANISOU 2393  C   LEU A 299     4745   3044   5833    -46     85   -543       C
ATOM   2394  O   LEU A 299     -78.118  16.154 -38.087  1.00 38.73           O
ANISOU 2394  O   LEU A 299     5078   3375   6262    -26     14   -569       O
ATOM   2395  CB  LEU A 299     -75.079  16.837 -38.180  1.00 30.73           C
ANISOU 2395  CB  LEU A 299     3989   2416   5271    -56    215   -621       C
ATOM   2396  CG  LEU A 299     -74.692  16.881 -39.659  1.00 31.71           C
ANISOU 2396  CG  LEU A 299     4161   2608   5282    -59    289   -672       C
ATOM   2397  CD1 LEU A 299     -74.165  18.256 -40.031  1.00 29.95           C
ANISOU 2397  CD1 LEU A 299     3970   2424   4984   -113    376   -604       C
ATOM   2398  CD2 LEU A 299     -73.670  15.806 -39.985  1.00 32.77           C
ANISOU 2398  CD2 LEU A 299     4230   2763   5457    -27    329   -788       C
ATOM   2399  N   LEU A 300     -77.986  17.909 -39.502  1.00 37.77           N
ANISOU 2399  N   LEU A 300     5070   3322   5959    -54     98   -518       N
ATOM   2400  CA  LEU A 300     -79.251  17.579 -40.152  1.00 37.87           C
ANISOU 2400  CA  LEU A 300     5136   3340   5913    -32     19   -528       C
ATOM   2401  C   LEU A 300     -79.241  16.156 -40.694  1.00 38.96           C
ANISOU 2401  C   LEU A 300     5255   3476   6070     -4    -10   -630       C
ATOM   2402  O   LEU A 300     -80.251  15.447 -40.616  1.00 40.91           O
ANISOU 2402  O   LEU A 300     5498   3695   6353     11   -100   -649       O
ATOM   2403  CB  LEU A 300     -79.544  18.580 -41.268  1.00 37.21           C
ANISOU 2403  CB  LEU A 300     5150   3299   5688    -39     40   -486       C
ATOM   2404  CG  LEU A 300     -80.937  18.493 -41.890  1.00 35.17           C
ANISOU 2404  CG  LEU A 300     4949   3048   5364    -12    -56   -485       C
ATOM   2405  CD1 LEU A 300     -82.003  18.652 -40.820  1.00 32.46           C
ANISOU 2405  CD1 LEU A 300     4566   2661   5105     -3   -141   -440       C
ATOM   2406  CD2 LEU A 300     -81.099  19.545 -42.972  1.00 38.21           C
ANISOU 2406  CD2 LEU A 300     5440   3475   5604    -16    -38   -431       C
ATOM   2407  N   ASP A 301     -78.103  15.716 -41.234  1.00 36.60           N
ANISOU 2407  N   ASP A 301     4940   3209   5758      3     64   -705       N
ATOM   2408  CA  ASP A 301     -77.998  14.345 -41.723  1.00 36.35           C
ANISOU 2408  CA  ASP A 301     4887   3168   5758     40     31   -822       C
ATOM   2409  C   ASP A 301     -78.183  13.344 -40.591  1.00 35.65           C
ANISOU 2409  C   ASP A 301     4724   2991   5830     49    -43   -831       C
ATOM   2410  O   ASP A 301     -78.807  12.292 -40.777  1.00 39.93           O
ANISOU 2410  O   ASP A 301     5262   3489   6420     69   -126   -889       O
ATOM   2411  CB  ASP A 301     -76.648  14.138 -42.407  1.00 42.29           C
ANISOU 2411  CB  ASP A 301     5618   3978   6471     53    134   -906       C
ATOM   2412  CG  ASP A 301     -76.308  15.252 -43.375  1.00 49.11           C
ANISOU 2412  CG  ASP A 301     6548   4936   7176     26    228   -866       C
ATOM   2413  OD1 ASP A 301     -76.232  16.420 -42.936  1.00 50.67           O
ANISOU 2413  OD1 ASP A 301     6760   5131   7362    -18    264   -757       O
ATOM   2414  OD2 ASP A 301     -76.113  14.962 -44.574  1.00 51.30           O
ANISOU 2414  OD2 ASP A 301     6863   5290   7340     48    264   -944       O
ATOM   2415  N   ASP A 302     -77.648  13.654 -39.408  1.00 33.15           N
ANISOU 2415  N   ASP A 302     4351   2648   5598     31    -20   -770       N
ATOM   2416  CA  ASP A 302     -77.797  12.753 -38.271  1.00 35.07           C
ANISOU 2416  CA  ASP A 302     4530   2814   5980     36    -90   -757       C
ATOM   2417  C   ASP A 302     -79.248  12.673 -37.817  1.00 33.12           C
ANISOU 2417  C   ASP A 302     4294   2539   5751     18   -180   -691       C
ATOM   2418  O   ASP A 302     -79.747  11.586 -37.503  1.00 31.37           O
ANISOU 2418  O   ASP A 302     4044   2256   5619     18   -258   -705       O
ATOM   2419  CB  ASP A 302     -76.900  13.205 -37.119  1.00 36.81           C
ANISOU 2419  CB  ASP A 302     4692   3029   6264     25    -47   -706       C
ATOM   2420  CG  ASP A 302     -75.435  12.910 -37.372  1.00 41.33           C
ANISOU 2420  CG  ASP A 302     5220   3617   6866     48     23   -786       C
ATOM   2421  OD1 ASP A 302     -75.134  12.159 -38.324  1.00 44.39           O
ANISOU 2421  OD1 ASP A 302     5615   4012   7239     79     31   -889       O
ATOM   2422  OD2 ASP A 302     -74.585  13.431 -36.619  1.00 42.55           O
ANISOU 2422  OD2 ASP A 302     5327   3782   7059     38     67   -757       O
ATOM   2423  N   PHE A 303     -79.942  13.813 -37.775  1.00 32.71           N
ANISOU 2423  N   PHE A 303     4278   2528   5624      0   -172   -618       N
ATOM   2424  CA  PHE A 303     -81.345  13.801 -37.376  1.00 35.68           C
ANISOU 2424  CA  PHE A 303     4650   2894   6012    -14   -252   -564       C
ATOM   2425  C   PHE A 303     -82.195  13.032 -38.379  1.00 35.35           C
ANISOU 2425  C   PHE A 303     4640   2841   5951     -5   -321   -627       C
ATOM   2426  O   PHE A 303     -83.154  12.352 -37.995  1.00 36.83           O
ANISOU 2426  O   PHE A 303     4794   2994   6206    -22   -401   -612       O
ATOM   2427  CB  PHE A 303     -81.863  15.229 -37.217  1.00 39.01           C
ANISOU 2427  CB  PHE A 303     5103   3361   6358    -20   -235   -491       C
ATOM   2428  CG  PHE A 303     -83.320  15.305 -36.862  1.00 41.02           C
ANISOU 2428  CG  PHE A 303     5343   3623   6619    -24   -312   -448       C
ATOM   2429  CD1 PHE A 303     -83.745  15.032 -35.573  1.00 39.09           C
ANISOU 2429  CD1 PHE A 303     5026   3370   6454    -41   -341   -394       C
ATOM   2430  CD2 PHE A 303     -84.264  15.645 -37.817  1.00 41.08           C
ANISOU 2430  CD2 PHE A 303     5403   3656   6550    -12   -356   -461       C
ATOM   2431  CE1 PHE A 303     -85.085  15.096 -35.242  1.00 37.59           C
ANISOU 2431  CE1 PHE A 303     4808   3205   6271    -48   -401   -357       C
ATOM   2432  CE2 PHE A 303     -85.605  15.712 -37.493  1.00 39.58           C
ANISOU 2432  CE2 PHE A 303     5184   3480   6374    -14   -428   -430       C
ATOM   2433  CZ  PHE A 303     -86.016  15.438 -36.204  1.00 41.46           C
ANISOU 2433  CZ  PHE A 303     5340   3717   6696    -34   -445   -380       C
ATOM   2434  N   VAL A 304     -81.860  13.127 -39.667  1.00 37.01           N
ANISOU 2434  N   VAL A 304     4911   3087   6066     17   -293   -699       N
ATOM   2435  CA  VAL A 304     -82.579  12.359 -40.679  1.00 35.37           C
ANISOU 2435  CA  VAL A 304     4733   2873   5831     34   -365   -780       C
ATOM   2436  C   VAL A 304     -82.361  10.868 -40.466  1.00 36.16           C
ANISOU 2436  C   VAL A 304     4785   2894   6061     39   -418   -854       C
ATOM   2437  O   VAL A 304     -83.300  10.068 -40.566  1.00 41.85           O
ANISOU 2437  O   VAL A 304     5492   3569   6841     28   -514   -881       O
ATOM   2438  CB  VAL A 304     -82.150  12.801 -42.090  1.00 34.16           C
ANISOU 2438  CB  VAL A 304     4659   2792   5528     61   -314   -843       C
ATOM   2439  CG1 VAL A 304     -82.695  11.844 -43.137  1.00 34.18           C
ANISOU 2439  CG1 VAL A 304     4689   2793   5507     89   -391   -956       C
ATOM   2440  CG2 VAL A 304     -82.629  14.215 -42.365  1.00 31.18           C
ANISOU 2440  CG2 VAL A 304     4343   2472   5033     54   -293   -756       C
ATOM   2441  N   GLU A 305     -81.123  10.471 -40.159  1.00 36.21           N
ANISOU 2441  N   GLU A 305     4759   2877   6123     54   -364   -890       N
ATOM   2442  CA  GLU A 305     -80.836   9.060 -39.918  1.00 38.76           C
ANISOU 2442  CA  GLU A 305     5037   3107   6582     68   -424   -959       C
ATOM   2443  C   GLU A 305     -81.627   8.531 -38.729  1.00 37.08           C
ANISOU 2443  C   GLU A 305     4773   2817   6498     24   -503   -867       C
ATOM   2444  O   GLU A 305     -82.091   7.385 -38.743  1.00 39.54           O
ANISOU 2444  O   GLU A 305     5065   3043   6914     16   -594   -905       O
ATOM   2445  CB  GLU A 305     -79.337   8.859 -39.692  1.00 39.59           C
ANISOU 2445  CB  GLU A 305     5107   3206   6727     99   -352  -1005       C
ATOM   2446  CG  GLU A 305     -78.924   7.400 -39.556  1.00 42.15           C
ANISOU 2446  CG  GLU A 305     5392   3427   7196    130   -421  -1092       C
ATOM   2447  CD  GLU A 305     -77.466   7.234 -39.170  1.00 43.73           C
ANISOU 2447  CD  GLU A 305     5544   3622   7451    167   -360  -1130       C
ATOM   2448  OE1 GLU A 305     -77.065   7.760 -38.111  1.00 44.50           O
ANISOU 2448  OE1 GLU A 305     5605   3724   7578    146   -325  -1031       O
ATOM   2449  OE2 GLU A 305     -76.721   6.579 -39.928  1.00 47.48           O
ANISOU 2449  OE2 GLU A 305     6010   4092   7937    223   -351  -1269       O
ATOM   2450  N   ILE A 306     -81.797   9.355 -37.694  1.00 35.57           N
ANISOU 2450  N   ILE A 306     4558   2658   6300     -6   -470   -746       N
ATOM   2451  CA  ILE A 306     -82.517   8.917 -36.503  1.00 28.66           C
ANISOU 2451  CA  ILE A 306     3629   1736   5526    -50   -528   -648       C
ATOM   2452  C   ILE A 306     -83.995   8.721 -36.815  1.00 31.04           C
ANISOU 2452  C   ILE A 306     3930   2036   5827    -84   -606   -634       C
ATOM   2453  O   ILE A 306     -84.573   7.666 -36.526  1.00 34.46           O
ANISOU 2453  O   ILE A 306     4328   2393   6371   -119   -687   -624       O
ATOM   2454  CB  ILE A 306     -82.316   9.923 -35.356  1.00 35.97           C
ANISOU 2454  CB  ILE A 306     4527   2716   6423    -64   -470   -540       C
ATOM   2455  CG1 ILE A 306     -80.843   9.990 -34.950  1.00 30.02           C
ANISOU 2455  CG1 ILE A 306     3757   1955   5692    -35   -408   -556       C
ATOM   2456  CG2 ILE A 306     -83.192   9.555 -34.166  1.00 31.88           C
ANISOU 2456  CG2 ILE A 306     3954   2182   5978   -111   -522   -434       C
ATOM   2457  CD1 ILE A 306     -80.541  11.074 -33.933  1.00 26.70           C
ANISOU 2457  CD1 ILE A 306     3315   1593   5236    -42   -353   -472       C
ATOM   2458  N   ILE A 307     -84.628   9.732 -37.414  1.00 28.72           N
ANISOU 2458  N   ILE A 307     3674   1823   5416    -76   -589   -632       N
ATOM   2459  CA  ILE A 307     -86.069   9.676 -37.632  1.00 31.76           C
ANISOU 2459  CA  ILE A 307     4046   2221   5800   -103   -664   -617       C
ATOM   2460  C   ILE A 307     -86.423   8.640 -38.692  1.00 36.25           C
ANISOU 2460  C   ILE A 307     4635   2735   6405    -98   -747   -727       C
ATOM   2461  O   ILE A 307     -87.529   8.083 -38.679  1.00 38.91           O
ANISOU 2461  O   ILE A 307     4935   3043   6806   -137   -833   -722       O
ATOM   2462  CB  ILE A 307     -86.604  11.077 -37.989  1.00 33.01           C
ANISOU 2462  CB  ILE A 307     4241   2474   5827    -82   -635   -588       C
ATOM   2463  CG1 ILE A 307     -88.130  11.116 -37.874  1.00 33.09           C
ANISOU 2463  CG1 ILE A 307     4210   2509   5853   -110   -711   -555       C
ATOM   2464  CG2 ILE A 307     -86.154  11.493 -39.383  1.00 29.01           C
ANISOU 2464  CG2 ILE A 307     3821   2001   5199    -37   -611   -673       C
ATOM   2465  CD1 ILE A 307     -88.718  12.500 -38.039  1.00 37.36           C
ANISOU 2465  CD1 ILE A 307     4776   3134   6285    -81   -696   -520       C
ATOM   2466  N   LYS A 308     -85.503   8.348 -39.613  1.00 36.59           N
ANISOU 2466  N   LYS A 308     4728   2766   6408    -52   -725   -836       N
ATOM   2467  CA  LYS A 308     -85.740   7.296 -40.593  1.00 35.71           C
ANISOU 2467  CA  LYS A 308     4635   2600   6334    -36   -808   -963       C
ATOM   2468  C   LYS A 308     -85.458   5.904 -40.048  1.00 35.26           C
ANISOU 2468  C   LYS A 308     4530   2412   6455    -57   -871   -986       C
ATOM   2469  O   LYS A 308     -85.699   4.919 -40.753  1.00 39.91           O
ANISOU 2469  O   LYS A 308     5126   2931   7106    -48   -958  -1096       O
ATOM   2470  CB  LYS A 308     -84.891   7.530 -41.844  1.00 38.51           C
ANISOU 2470  CB  LYS A 308     5059   3011   6562     29   -757  -1083       C
ATOM   2471  CG  LYS A 308     -85.382   8.656 -42.734  1.00 44.39           C
ANISOU 2471  CG  LYS A 308     5869   3867   7129     49   -734  -1078       C
ATOM   2472  CD  LYS A 308     -84.569   8.726 -44.015  1.00 50.35           C
ANISOU 2472  CD  LYS A 308     6692   4686   7751    107   -685  -1195       C
ATOM   2473  CE  LYS A 308     -85.144   9.746 -44.981  1.00 55.05           C
ANISOU 2473  CE  LYS A 308     7364   5386   8166    125   -681  -1183       C
ATOM   2474  NZ  LYS A 308     -84.347   9.835 -46.236  1.00 61.54           N
ANISOU 2474  NZ  LYS A 308     8254   6291   8836    176   -623  -1285       N
ATOM   2475  N   SER A 309     -84.958   5.797 -38.817  1.00 32.35           N
ANISOU 2475  N   SER A 309     4116   2004   6171    -82   -838   -886       N
ATOM   2476  CA  SER A 309     -84.603   4.519 -38.222  1.00 32.41           C
ANISOU 2476  CA  SER A 309     4084   1894   6334    -98   -895   -881       C
ATOM   2477  C   SER A 309     -85.622   4.051 -37.190  1.00 36.55           C
ANISOU 2477  C   SER A 309     4547   2394   6945   -180   -950   -743       C
ATOM   2478  O   SER A 309     -85.318   3.163 -36.386  1.00 37.08           O
ANISOU 2478  O   SER A 309     4578   2418   7093   -199   -970   -674       O
ATOM   2479  CB  SER A 309     -83.215   4.607 -37.588  1.00 39.54           C
ANISOU 2479  CB  SER A 309     4977   2807   7238    -60   -817   -856       C
ATOM   2480  OG  SER A 309     -82.251   5.042 -38.531  1.00 39.77           O
ANISOU 2480  OG  SER A 309     5050   2866   7194      8   -755   -983       O
ATOM   2481  N   GLN A 310     -86.822   4.621 -37.198  1.00 38.75           N
ANISOU 2481  N   GLN A 310     4766   3076   6880    379   -561  -1731       N
ATOM   2482  CA  GLN A 310     -87.830   4.326 -36.192  1.00 34.64           C
ANISOU 2482  CA  GLN A 310     4135   2330   6698    253   -617  -1552       C
ATOM   2483  C   GLN A 310     -89.026   3.617 -36.814  1.00 37.86           C
ANISOU 2483  C   GLN A 310     4484   2644   7260    190   -863  -1697       C
ATOM   2484  O   GLN A 310     -89.268   3.693 -38.022  1.00 39.39           O
ANISOU 2484  O   GLN A 310     4741   2936   7288    233  -1022  -1954       O
ATOM   2485  CB  GLN A 310     -88.294   5.607 -35.491  1.00 32.41           C
ANISOU 2485  CB  GLN A 310     3812   2147   6354    190   -503  -1267       C
ATOM   2486  CG  GLN A 310     -87.161   6.475 -34.970  1.00 34.28           C
ANISOU 2486  CG  GLN A 310     4105   2519   6401    237   -291  -1121       C
ATOM   2487  CD  GLN A 310     -86.251   5.738 -34.005  1.00 36.16           C
ANISOU 2487  CD  GLN A 310     4326   2640   6774    240   -185  -1065       C
ATOM   2488  OE1 GLN A 310     -86.704   4.908 -33.216  1.00 36.68           O
ANISOU 2488  OE1 GLN A 310     4301   2615   7021    158   -218   -953       O
ATOM   2489  NE2 GLN A 310     -84.958   6.035 -34.069  1.00 32.52           N
ANISOU 2489  NE2 GLN A 310     3926   2284   6147    317    -63  -1062       N
ATOM   2490  N   ASP A 311     -89.772   2.920 -35.962  1.00 40.98           N
ANISOU 2490  N   ASP A 311     4738   2899   7933     82   -900  -1507       N
ATOM   2491  CA  ASP A 311     -91.015   2.272 -36.359  1.00 47.74           C
ANISOU 2491  CA  ASP A 311     5490   3642   9006      2  -1132  -1572       C
ATOM   2492  C   ASP A 311     -92.168   3.247 -36.159  1.00 45.99           C
ANISOU 2492  C   ASP A 311     5178   3446   8848    -84  -1162  -1408       C
ATOM   2493  O   ASP A 311     -92.306   3.844 -35.086  1.00 37.53           O
ANISOU 2493  O   ASP A 311     4029   2400   7830   -126   -982  -1148       O
ATOM   2494  CB  ASP A 311     -91.235   0.993 -35.549  1.00 41.40           C
ANISOU 2494  CB  ASP A 311     4543   2663   8524    -67  -1169  -1426       C
ATOM   2495  CG  ASP A 311     -92.479   0.235 -35.971  1.00 44.38           C
ANISOU 2495  CG  ASP A 311     4793   2900   9170   -145  -1422  -1485       C
ATOM   2496  OD1 ASP A 311     -93.598   0.742 -35.750  1.00 60.34           O
ANISOU 2496  OD1 ASP A 311     6703   4929  11296   -236  -1466  -1330       O
ATOM   2497  OD2 ASP A 311     -92.339  -0.873 -36.530  1.00 61.76           O
ANISOU 2497  OD2 ASP A 311     6989   4976  11501   -110  -1582  -1692       O
ATOM   2498  N   LEU A 312     -92.997   3.404 -37.191  1.00 48.66           N
ANISOU 2498  N   LEU A 312     5513   3792   9186   -108  -1400  -1579       N
ATOM   2499  CA  LEU A 312     -94.055   4.407 -37.205  1.00 46.58           C
ANISOU 2499  CA  LEU A 312     5146   3590   8963   -171  -1452  -1420       C
ATOM   2500  C   LEU A 312     -95.449   3.784 -37.171  1.00 49.73           C
ANISOU 2500  C   LEU A 312     5345   3844   9708   -294  -1663  -1365       C
ATOM   2501  O   LEU A 312     -96.403   4.362 -37.696  1.00 55.96           O
ANISOU 2501  O   LEU A 312     6045   4687  10530   -340  -1829  -1337       O
ATOM   2502  CB  LEU A 312     -93.913   5.309 -38.431  1.00 45.21           C
ANISOU 2502  CB  LEU A 312     5091   3696   8389    -95  -1537  -1508       C
ATOM   2503  CG  LEU A 312     -92.517   5.851 -38.742  1.00 43.40           C
ANISOU 2503  CG  LEU A 312     5043   3681   7767     27  -1352  -1548       C
ATOM   2504  CD1 LEU A 312     -92.553   6.720 -39.990  1.00 43.84           C
ANISOU 2504  CD1 LEU A 312     5167   4047   7444     64  -1466  -1550       C
ATOM   2505  CD2 LEU A 312     -91.953   6.625 -37.561  1.00 40.67           C
ANISOU 2505  CD2 LEU A 312     4683   3326   7445     48  -1062  -1293       C
ATOM   2506  N   SER A 313     -95.586   2.614 -36.552  1.00 53.11           N
ANISOU 2506  N   SER A 313     5678   4147  10356   -332  -1648  -1282       N
ATOM   2507  CA  SER A 313     -96.859   1.907 -36.503  1.00 57.28           C
ANISOU 2507  CA  SER A 313     6005   4552  11206   -433  -1833  -1189       C
ATOM   2508  C   SER A 313     -97.584   2.083 -35.174  1.00 58.69           C
ANISOU 2508  C   SER A 313     5955   4716  11627   -519  -1657   -825       C
ATOM   2509  O   SER A 313     -98.599   1.418 -34.943  1.00 61.53           O
ANISOU 2509  O   SER A 313     6122   4975  12282   -606  -1771   -686       O
ATOM   2510  CB  SER A 313     -96.647   0.418 -36.786  1.00 59.71           C
ANISOU 2510  CB  SER A 313     6325   4699  11664   -425  -1984  -1339       C
ATOM   2511  OG  SER A 313     -95.848  -0.182 -35.782  1.00 61.98           O
ANISOU 2511  OG  SER A 313     6597   4924  12029   -411  -1798  -1184       O
ATOM   2512  N   VAL A 314     -97.095   2.960 -34.302  1.00 57.75           N
ANISOU 2512  N   VAL A 314     5847   4708  11387   -495  -1381   -677       N
ATOM   2513  CA  VAL A 314     -97.670   3.169 -32.979  1.00 62.39           C
ANISOU 2513  CA  VAL A 314     6218   5338  12151   -571  -1173   -370       C
ATOM   2514  C   VAL A 314     -98.024   4.642 -32.830  1.00 57.24           C
ANISOU 2514  C   VAL A 314     5498   4810  11441   -546  -1035   -339       C
ATOM   2515  O   VAL A 314     -97.320   5.514 -33.351  1.00 57.14           O
ANISOU 2515  O   VAL A 314     5674   4876  11161   -439  -1001   -481       O
ATOM   2516  CB  VAL A 314     -96.701   2.706 -31.869  1.00 74.74           C
ANISOU 2516  CB  VAL A 314     7821   6919  13656   -578   -961   -225       C
ATOM   2517  CG1 VAL A 314     -97.159   3.179 -30.496  1.00 80.57           C
ANISOU 2517  CG1 VAL A 314     8352   7789  14473   -659   -703     65       C
ATOM   2518  CG2 VAL A 314     -96.572   1.190 -31.886  1.00 79.62           C
ANISOU 2518  CG2 VAL A 314     8417   7377  14458   -613  -1120   -193       C
ATOM   2519  N   VAL A 315     -99.131   4.911 -32.131  1.00 53.54           N
ANISOU 2519  N   VAL A 315     4748   4403  11192   -612   -944   -137       N
ATOM   2520  CA  VAL A 315     -99.586   6.286 -31.930  1.00 56.10           C
ANISOU 2520  CA  VAL A 315     4974   4898  11441   -521   -788   -115       C
ATOM   2521  C   VAL A 315     -98.494   7.121 -31.268  1.00 51.08           C
ANISOU 2521  C   VAL A 315     4514   4417  10477   -399   -511   -156       C
ATOM   2522  O   VAL A 315     -98.094   8.171 -31.782  1.00 51.17           O
ANISOU 2522  O   VAL A 315     4665   4480  10296   -275   -506   -271       O
ATOM   2523  CB  VAL A 315    -100.885   6.309 -31.106  1.00 63.13           C
ANISOU 2523  CB  VAL A 315     5491   5874  12621   -594   -674     99       C
ATOM   2524  CG1 VAL A 315    -101.294   7.743 -30.803  1.00 65.27           C
ANISOU 2524  CG1 VAL A 315     5657   6323  12818   -444   -482     71       C
ATOM   2525  CG2 VAL A 315    -101.995   5.580 -31.848  1.00 68.07           C
ANISOU 2525  CG2 VAL A 315     5994   6366  13502   -672   -968    149       C
ATOM   2526  N   SER A 316     -97.999   6.668 -30.118  1.00 46.71           N
ANISOU 2526  N   SER A 316     3939   3940   9868   -449   -299    -35       N
ATOM   2527  CA  SER A 316     -96.963   7.406 -29.410  1.00 45.97           C
ANISOU 2527  CA  SER A 316     3997   4001   9468   -354    -61    -81       C
ATOM   2528  C   SER A 316     -96.112   6.445 -28.597  1.00 49.00           C
ANISOU 2528  C   SER A 316     4437   4394   9787   -441     24     47       C
ATOM   2529  O   SER A 316     -96.607   5.447 -28.069  1.00 55.48           O
ANISOU 2529  O   SER A 316     5075   5184  10820   -581      8    257       O
ATOM   2530  CB  SER A 316     -97.554   8.475 -28.485  1.00 49.57           C
ANISOU 2530  CB  SER A 316     4271   4678   9885   -281    189    -68       C
ATOM   2531  OG  SER A 316     -98.068   7.891 -27.301  1.00 53.67           O
ANISOU 2531  OG  SER A 316     4556   5371  10464   -386    370    131       O
ATOM   2532  N   LYS A 317     -94.823   6.762 -28.503  1.00 44.19           N
ANISOU 2532  N   LYS A 317     4056   3820   8916   -367     97    -42       N
ATOM   2533  CA  LYS A 317     -93.905   6.005 -27.663  1.00 41.04           C
ANISOU 2533  CA  LYS A 317     3704   3450   8441   -434    178     97       C
ATOM   2534  C   LYS A 317     -92.677   6.863 -27.394  1.00 37.69           C
ANISOU 2534  C   LYS A 317     3478   3145   7698   -330    306    -14       C
ATOM   2535  O   LYS A 317     -92.502   7.936 -27.977  1.00 33.46           O
ANISOU 2535  O   LYS A 317     3049   2621   7043   -218    306   -191       O
ATOM   2536  CB  LYS A 317     -93.512   4.673 -28.307  1.00 41.16           C
ANISOU 2536  CB  LYS A 317     3781   3188   8670   -497    -44    110       C
ATOM   2537  CG  LYS A 317     -92.528   4.791 -29.458  1.00 36.83           C
ANISOU 2537  CG  LYS A 317     3485   2516   7994   -378   -166   -146       C
ATOM   2538  CD  LYS A 317     -91.996   3.421 -29.845  1.00 42.27           C
ANISOU 2538  CD  LYS A 317     4220   3037   8804   -387   -335   -170       C
ATOM   2539  CE  LYS A 317     -90.893   3.521 -30.883  1.00 49.43           C
ANISOU 2539  CE  LYS A 317     5350   3955   9476   -249   -390   -423       C
ATOM   2540  NZ  LYS A 317     -90.273   2.193 -31.154  1.00 54.87           N
ANISOU 2540  NZ  LYS A 317     6058   4527  10264   -229   -513   -475       N
ATOM   2541  N   VAL A 318     -91.825   6.371 -26.501  1.00 43.17           N
ANISOU 2541  N   VAL A 318     4199   3918   8286   -384    392    126       N
ATOM   2542  CA  VAL A 318     -90.599   7.057 -26.112  1.00 30.86           C
ANISOU 2542  CA  VAL A 318     2802   2474   6451   -315    492     52       C
ATOM   2543  C   VAL A 318     -89.434   6.439 -26.871  1.00 35.68           C
ANISOU 2543  C   VAL A 318     3583   2886   7087   -280    359      4       C
ATOM   2544  O   VAL A 318     -89.262   5.213 -26.873  1.00 37.34           O
ANISOU 2544  O   VAL A 318     3753   2942   7491   -346    258    128       O
ATOM   2545  CB  VAL A 318     -90.374   6.976 -24.593  1.00 34.50           C
ANISOU 2545  CB  VAL A 318     3166   3208   6735   -397    662    238       C
ATOM   2546  CG1 VAL A 318     -88.998   7.511 -24.230  1.00 30.63           C
ANISOU 2546  CG1 VAL A 318     2842   2804   5994   -348    707    169       C
ATOM   2547  CG2 VAL A 318     -91.460   7.745 -23.858  1.00 34.79           C
ANISOU 2547  CG2 VAL A 318     3026   3506   6687   -393    838    204       C
ATOM   2548  N   VAL A 319     -88.635   7.285 -27.516  1.00 35.81           N
ANISOU 2548  N   VAL A 319     3764   2901   6941   -172    359   -168       N
ATOM   2549  CA  VAL A 319     -87.458   6.864 -28.267  1.00 31.95           C
ANISOU 2549  CA  VAL A 319     3417   2292   6430   -112    278   -239       C
ATOM   2550  C   VAL A 319     -86.219   7.370 -27.541  1.00 33.36           C
ANISOU 2550  C   VAL A 319     3665   2596   6414    -96    383   -190       C
ATOM   2551  O   VAL A 319     -86.101   8.571 -27.265  1.00 36.70           O
ANISOU 2551  O   VAL A 319     4121   3147   6677    -67    465   -251       O
ATOM   2552  CB  VAL A 319     -87.499   7.383 -29.715  1.00 33.00           C
ANISOU 2552  CB  VAL A 319     3652   2372   6513    -17    185   -432       C
ATOM   2553  CG1 VAL A 319     -86.203   7.053 -30.433  1.00 33.74           C
ANISOU 2553  CG1 VAL A 319     3868   2429   6523     61    156   -519       C
ATOM   2554  CG2 VAL A 319     -88.691   6.794 -30.454  1.00 34.73           C
ANISOU 2554  CG2 VAL A 319     3800   2474   6921    -45     35   -493       C
ATOM   2555  N   LYS A 320     -85.302   6.458 -27.233  1.00 33.21           N
ANISOU 2555  N   LYS A 320     3651   2516   6452   -116    356    -84       N
ATOM   2556  CA  LYS A 320     -84.054   6.786 -26.556  1.00 33.29           C
ANISOU 2556  CA  LYS A 320     3705   2635   6307   -113    419    -10       C
ATOM   2557  C   LYS A 320     -82.927   6.855 -27.576  1.00 33.06           C
ANISOU 2557  C   LYS A 320     3778   2522   6259     -4    385   -132       C
ATOM   2558  O   LYS A 320     -82.725   5.910 -28.347  1.00 33.38           O
ANISOU 2558  O   LYS A 320     3821   2402   6460     52    307   -198       O
ATOM   2559  CB  LYS A 320     -83.722   5.746 -25.485  1.00 34.59           C
ANISOU 2559  CB  LYS A 320     3769   2810   6562   -209    400    246       C
ATOM   2560  CG  LYS A 320     -84.881   5.383 -24.574  1.00 40.81           C
ANISOU 2560  CG  LYS A 320     4412   3707   7388   -334    434    430       C
ATOM   2561  CD  LYS A 320     -84.718   5.994 -23.193  1.00 45.23           C
ANISOU 2561  CD  LYS A 320     4927   4599   7661   -413    553    553       C
ATOM   2562  CE  LYS A 320     -85.458   5.169 -22.151  1.00 56.11           C
ANISOU 2562  CE  LYS A 320     6118   6127   9074   -562    577    868       C
ATOM   2563  NZ  LYS A 320     -85.274   5.697 -20.772  1.00 62.83           N
ANISOU 2563  NZ  LYS A 320     6917   7387   9567   -642    696    979       N
ATOM   2564  N   VAL A 321     -82.198   7.968 -27.579  1.00 32.39           N
ANISOU 2564  N   VAL A 321     3758   2554   5996     27    444   -172       N
ATOM   2565  CA  VAL A 321     -81.075   8.175 -28.484  1.00 29.17           C
ANISOU 2565  CA  VAL A 321     3411   2134   5540    116    444   -236       C
ATOM   2566  C   VAL A 321     -79.873   8.616 -27.663  1.00 27.00           C
ANISOU 2566  C   VAL A 321     3125   1952   5182     85    481   -124       C
ATOM   2567  O   VAL A 321     -79.964   9.573 -26.887  1.00 29.59           O
ANISOU 2567  O   VAL A 321     3458   2385   5402     23    507   -109       O
ATOM   2568  CB  VAL A 321     -81.393   9.218 -29.572  1.00 29.31           C
ANISOU 2568  CB  VAL A 321     3488   2194   5455    168    443   -348       C
ATOM   2569  CG1 VAL A 321     -80.227   9.342 -30.541  1.00 31.34           C
ANISOU 2569  CG1 VAL A 321     3774   2504   5631    250    465   -370       C
ATOM   2570  CG2 VAL A 321     -82.671   8.848 -30.311  1.00 31.65           C
ANISOU 2570  CG2 VAL A 321     3783   2423   5820    182    374   -449       C
ATOM   2571  N   THR A 322     -78.750   7.923 -27.835  1.00 30.30           N
ANISOU 2571  N   THR A 322     3513   2328   5673    134    471    -71       N
ATOM   2572  CA  THR A 322     -77.524   8.260 -27.119  1.00 29.34           C
ANISOU 2572  CA  THR A 322     3355   2289   5502    100    478     56       C
ATOM   2573  C   THR A 322     -76.841   9.418 -27.834  1.00 33.36           C
ANISOU 2573  C   THR A 322     3895   2871   5910    135    517      8       C
ATOM   2574  O   THR A 322     -76.331   9.259 -28.948  1.00 35.41           O
ANISOU 2574  O   THR A 322     4145   3129   6179    232    554    -44       O
ATOM   2575  CB  THR A 322     -76.601   7.049 -27.025  1.00 31.21           C
ANISOU 2575  CB  THR A 322     3506   2434   5920    148    443    158       C
ATOM   2576  OG1 THR A 322     -77.301   5.961 -26.408  1.00 37.45           O
ANISOU 2576  OG1 THR A 322     4244   3119   6865     97    379    257       O
ATOM   2577  CG2 THR A 322     -75.374   7.383 -26.191  1.00 32.36           C
ANISOU 2577  CG2 THR A 322     3590   2678   6026     96    422    324       C
ATOM   2578  N   ILE A 323     -76.840  10.588 -27.202  1.00 28.24           N
ANISOU 2578  N   ILE A 323     3266   2295   5170     54    504     20       N
ATOM   2579  CA  ILE A 323     -76.228  11.790 -27.754  1.00 27.19           C
ANISOU 2579  CA  ILE A 323     3133   2188   5008     53    505     26       C
ATOM   2580  C   ILE A 323     -75.317  12.381 -26.691  1.00 29.29           C
ANISOU 2580  C   ILE A 323     3358   2506   5264    -40    448    100       C
ATOM   2581  O   ILE A 323     -75.716  12.501 -25.528  1.00 30.56           O
ANISOU 2581  O   ILE A 323     3533   2719   5360   -115    411     58       O
ATOM   2582  CB  ILE A 323     -77.284  12.821 -28.194  1.00 23.18           C
ANISOU 2582  CB  ILE A 323     2675   1643   4488     48    492    -69       C
ATOM   2583  CG1 ILE A 323     -78.316  12.168 -29.114  1.00 28.65           C
ANISOU 2583  CG1 ILE A 323     3404   2305   5179    119    511   -144       C
ATOM   2584  CG2 ILE A 323     -76.620  13.996 -28.893  1.00 23.62           C
ANISOU 2584  CG2 ILE A 323     2703   1695   4576     34    468      9       C
ATOM   2585  CD1 ILE A 323     -79.490  13.054 -29.443  1.00 26.70           C
ANISOU 2585  CD1 ILE A 323     3178   2013   4954    115    477   -212       C
ATOM   2586  N   ASP A 324     -74.095  12.741 -27.089  1.00 29.96           N
ANISOU 2586  N   ASP A 324     3375   2610   5397    -40    441    207       N
ATOM   2587  CA  ASP A 324     -73.109  13.320 -26.175  1.00 30.86           C
ANISOU 2587  CA  ASP A 324     3430   2761   5534   -141    351    282       C
ATOM   2588  C   ASP A 324     -72.864  12.407 -24.975  1.00 33.06           C
ANISOU 2588  C   ASP A 324     3683   3114   5764   -186    301    343       C
ATOM   2589  O   ASP A 324     -72.678  12.872 -23.849  1.00 26.67           O
ANISOU 2589  O   ASP A 324     2872   2386   4877   -293    204    326       O
ATOM   2590  CB  ASP A 324     -73.532  14.716 -25.712  1.00 31.58           C
ANISOU 2590  CB  ASP A 324     3561   2806   5633   -226    267    162       C
ATOM   2591  CG  ASP A 324     -73.632  15.705 -26.852  1.00 35.61           C
ANISOU 2591  CG  ASP A 324     4057   3219   6253   -207    272    192       C
ATOM   2592  OD1 ASP A 324     -72.985  15.478 -27.895  1.00 38.49           O
ANISOU 2592  OD1 ASP A 324     4359   3626   6640   -160    336    349       O
ATOM   2593  OD2 ASP A 324     -74.351  16.715 -26.702  1.00 37.32           O
ANISOU 2593  OD2 ASP A 324     4306   3332   6540   -236    210     70       O
ATOM   2594  N   TYR A 325     -72.879  11.096 -25.223  1.00 27.06           N
ANISOU 2594  N   TYR A 325     2893   2328   5060   -107    350    414       N
ATOM   2595  CA  TYR A 325     -72.661  10.056 -24.219  1.00 31.71           C
ANISOU 2595  CA  TYR A 325     3425   2958   5664   -148    287    555       C
ATOM   2596  C   TYR A 325     -73.762   9.994 -23.169  1.00 34.85           C
ANISOU 2596  C   TYR A 325     3882   3455   5905   -239    263    524       C
ATOM   2597  O   TYR A 325     -73.527   9.508 -22.058  1.00 39.99           O
ANISOU 2597  O   TYR A 325     4480   4231   6486   -328    184    681       O
ATOM   2598  CB  TYR A 325     -71.305  10.214 -23.520  1.00 31.61           C
ANISOU 2598  CB  TYR A 325     3305   3024   5681   -219    180    719       C
ATOM   2599  CG  TYR A 325     -70.114  10.113 -24.439  1.00 33.12           C
ANISOU 2599  CG  TYR A 325     3377   3156   6050   -127    221    798       C
ATOM   2600  CD1 TYR A 325     -69.696   8.885 -24.933  1.00 32.86           C
ANISOU 2600  CD1 TYR A 325     3245   3036   6206      3    268    869       C
ATOM   2601  CD2 TYR A 325     -69.397  11.244 -24.800  1.00 34.61           C
ANISOU 2601  CD2 TYR A 325     3526   3375   6249   -167    211    800       C
ATOM   2602  CE1 TYR A 325     -68.601   8.787 -25.771  1.00 37.24           C
ANISOU 2602  CE1 TYR A 325     3660   3583   6906    110    340    909       C
ATOM   2603  CE2 TYR A 325     -68.300  11.157 -25.637  1.00 37.77           C
ANISOU 2603  CE2 TYR A 325     3780   3778   6795    -89    276    905       C
ATOM   2604  CZ  TYR A 325     -67.907   9.927 -26.119  1.00 39.41           C
ANISOU 2604  CZ  TYR A 325     3886   3947   7140     60    357    944       C
ATOM   2605  OH  TYR A 325     -66.817   9.838 -26.953  1.00 41.11           O
ANISOU 2605  OH  TYR A 325     3927   4209   7483    161    455   1016       O
ATOM   2606  N   THR A 326     -74.964  10.472 -23.482  1.00 30.49           N
ANISOU 2606  N   THR A 326     3415   2883   5286   -221    332    348       N
ATOM   2607  CA  THR A 326     -76.086  10.365 -22.562  1.00 31.74           C
ANISOU 2607  CA  THR A 326     3593   3168   5300   -290    350    315       C
ATOM   2608  C   THR A 326     -77.331   9.960 -23.339  1.00 32.72           C
ANISOU 2608  C   THR A 326     3747   3176   5510   -221    428    234       C
ATOM   2609  O   THR A 326     -77.452  10.233 -24.536  1.00 35.79           O
ANISOU 2609  O   THR A 326     4178   3426   5996   -131    457    128       O
ATOM   2610  CB  THR A 326     -76.326  11.679 -21.795  1.00 29.21           C
ANISOU 2610  CB  THR A 326     3311   2993   4795   -356    335    125       C
ATOM   2611  OG1 THR A 326     -77.112  11.418 -20.625  1.00 35.35           O
ANISOU 2611  OG1 THR A 326     4064   4004   5363   -432    363    129       O
ATOM   2612  CG2 THR A 326     -77.053  12.693 -22.660  1.00 27.58           C
ANISOU 2612  CG2 THR A 326     3164   2648   4669   -284    385    -94       C
ATOM   2613  N   GLU A 327     -78.248   9.285 -22.650  1.00 29.00           N
ANISOU 2613  N   GLU A 327     3235   2789   4995   -277    450    312       N
ATOM   2614  CA  GLU A 327     -79.492   8.841 -23.267  1.00 36.49           C
ANISOU 2614  CA  GLU A 327     4182   3630   6054   -237    498    257       C
ATOM   2615  C   GLU A 327     -80.501   9.982 -23.270  1.00 32.40           C
ANISOU 2615  C   GLU A 327     3697   3179   5433   -223    566     42       C
ATOM   2616  O   GLU A 327     -80.932  10.442 -22.207  1.00 33.00           O
ANISOU 2616  O   GLU A 327     3738   3468   5332   -285    613     -2       O
ATOM   2617  CB  GLU A 327     -80.059   7.629 -22.532  1.00 46.17           C
ANISOU 2617  CB  GLU A 327     5305   4902   7334   -321    483    486       C
ATOM   2618  CG  GLU A 327     -79.776   6.296 -23.208  1.00 57.46           C
ANISOU 2618  CG  GLU A 327     6690   6076   9067   -276    403    611       C
ATOM   2619  CD  GLU A 327     -80.670   5.183 -22.692  1.00 69.36           C
ANISOU 2619  CD  GLU A 327     8077   7553  10724   -369    368    835       C
ATOM   2620  OE1 GLU A 327     -81.608   5.483 -21.922  1.00 73.03           O
ANISOU 2620  OE1 GLU A 327     8491   8237  11020   -461    440    891       O
ATOM   2621  OE2 GLU A 327     -80.438   4.011 -23.056  1.00 72.55           O
ANISOU 2621  OE2 GLU A 327     8416   7710  11440   -348    267    954       O
ATOM   2622  N   ILE A 328     -80.880  10.434 -24.462  1.00 29.30           N
ANISOU 2622  N   ILE A 328     3356   2626   5150   -136    568    -96       N
ATOM   2623  CA  ILE A 328     -81.883  11.478 -24.631  1.00 29.52           C
ANISOU 2623  CA  ILE A 328     3388   2655   5172   -104    606   -277       C
ATOM   2624  C   ILE A 328     -83.202  10.821 -25.012  1.00 29.68           C
ANISOU 2624  C   ILE A 328     3355   2623   5298    -93    626   -268       C
ATOM   2625  O   ILE A 328     -83.266  10.053 -25.980  1.00 27.00           O
ANISOU 2625  O   ILE A 328     3034   2140   5084    -58    571   -229       O
ATOM   2626  CB  ILE A 328     -81.452  12.505 -25.691  1.00 31.25           C
ANISOU 2626  CB  ILE A 328     3670   2743   5462    -38    560   -366       C
ATOM   2627  CG1 ILE A 328     -80.129  13.161 -25.292  1.00 29.03           C
ANISOU 2627  CG1 ILE A 328     3409   2494   5126    -71    522   -348       C
ATOM   2628  CG2 ILE A 328     -82.527  13.564 -25.871  1.00 30.81           C
ANISOU 2628  CG2 ILE A 328     3590   2639   5477      2    568   -521       C
ATOM   2629  CD1 ILE A 328     -80.215  13.973 -24.020  1.00 26.35           C
ANISOU 2629  CD1 ILE A 328     3048   2278   4686   -125    525   -485       C
ATOM   2630  N   SER A 329     -84.252  11.121 -24.253  1.00 34.74           N
ANISOU 2630  N   SER A 329     3913   3394   5893   -119    702   -326       N
ATOM   2631  CA  SER A 329     -85.574  10.563 -24.504  1.00 32.47           C
ANISOU 2631  CA  SER A 329     3532   3076   5731   -125    722   -295       C
ATOM   2632  C   SER A 329     -86.336  11.472 -25.460  1.00 33.80           C
ANISOU 2632  C   SER A 329     3706   3115   6022    -36    691   -458       C
ATOM   2633  O   SER A 329     -86.526  12.660 -25.179  1.00 35.56           O
ANISOU 2633  O   SER A 329     3912   3372   6226     11    730   -615       O
ATOM   2634  CB  SER A 329     -86.344  10.391 -23.196  1.00 38.98           C
ANISOU 2634  CB  SER A 329     4215   4158   6437   -198    843   -237       C
ATOM   2635  OG  SER A 329     -85.722   9.428 -22.363  1.00 48.06           O
ANISOU 2635  OG  SER A 329     5336   5439   7486   -302    840     -1       O
ATOM   2636  N   PHE A 330     -86.764  10.913 -26.587  1.00 35.23           N
ANISOU 2636  N   PHE A 330     3899   3140   6347    -15    598   -427       N
ATOM   2637  CA  PHE A 330     -87.603  11.608 -27.549  1.00 30.98           C
ANISOU 2637  CA  PHE A 330     3342   2502   5928     50    533   -519       C
ATOM   2638  C   PHE A 330     -89.024  11.070 -27.472  1.00 36.31           C
ANISOU 2638  C   PHE A 330     3869   3179   6749     19    533   -490       C
ATOM   2639  O   PHE A 330     -89.251   9.922 -27.078  1.00 39.00           O
ANISOU 2639  O   PHE A 330     4146   3537   7134    -60    539   -370       O
ATOM   2640  CB  PHE A 330     -87.075  11.440 -28.976  1.00 32.99           C
ANISOU 2640  CB  PHE A 330     3707   2642   6186     90    406   -514       C
ATOM   2641  CG  PHE A 330     -85.795  12.176 -29.248  1.00 30.07           C
ANISOU 2641  CG  PHE A 330     3438   2282   5704    122    408   -511       C
ATOM   2642  CD1 PHE A 330     -84.582  11.676 -28.805  1.00 28.75           C
ANISOU 2642  CD1 PHE A 330     3325   2157   5442    100    450   -458       C
ATOM   2643  CD2 PHE A 330     -85.804  13.359 -29.969  1.00 32.04           C
ANISOU 2643  CD2 PHE A 330     3701   2490   5984    166    350   -518       C
ATOM   2644  CE1 PHE A 330     -83.403  12.350 -29.064  1.00 25.75           C
ANISOU 2644  CE1 PHE A 330     3004   1792   4988    118    449   -431       C
ATOM   2645  CE2 PHE A 330     -84.628  14.036 -30.232  1.00 31.75           C
ANISOU 2645  CE2 PHE A 330     3723   2459   5880    172    343   -463       C
ATOM   2646  CZ  PHE A 330     -83.426  13.531 -29.778  1.00 25.87           C
ANISOU 2646  CZ  PHE A 330     3027   1772   5032    147    399   -428       C
ATOM   2647  N   MET A 331     -89.982  11.905 -27.856  1.00 39.29           N
ANISOU 2647  N   MET A 331     4164   3519   7247     76    509   -570       N
ATOM   2648  CA  MET A 331     -91.381  11.509 -27.929  1.00 39.28           C
ANISOU 2648  CA  MET A 331     3990   3510   7425     52    490   -536       C
ATOM   2649  C   MET A 331     -91.790  11.473 -29.394  1.00 37.42           C
ANISOU 2649  C   MET A 331     3789   3122   7306     77    288   -539       C
ATOM   2650  O   MET A 331     -91.751  12.501 -30.078  1.00 38.13           O
ANISOU 2650  O   MET A 331     3915   3158   7413    150    216   -583       O
ATOM   2651  CB  MET A 331     -92.269  12.466 -27.136  1.00 44.24           C
ANISOU 2651  CB  MET A 331     4445   4242   8124    111    625   -634       C
ATOM   2652  CG  MET A 331     -93.565  11.837 -26.660  1.00 55.39           C
ANISOU 2652  CG  MET A 331     5623   5752   9671     58    695   -550       C
ATOM   2653  SD  MET A 331     -93.269  10.422 -25.582  1.00 58.60           S
ANISOU 2653  SD  MET A 331     5983   6338   9945    -96    802   -336       S
ATOM   2654  CE  MET A 331     -94.945   9.877 -25.260  1.00 57.12           C
ANISOU 2654  CE  MET A 331     5467   6247   9988   -166    861   -192       C
ATOM   2655  N   LEU A 332     -92.166  10.291 -29.874  1.00 37.08           N
ANISOU 2655  N   LEU A 332     3726   3012   7350      8    174   -485       N
ATOM   2656  CA  LEU A 332     -92.532  10.082 -31.268  1.00 35.64           C
ANISOU 2656  CA  LEU A 332     3584   2732   7226     18    -44   -523       C
ATOM   2657  C   LEU A 332     -94.036   9.865 -31.363  1.00 35.56           C
ANISOU 2657  C   LEU A 332     3366   2683   7464    -26   -131   -482       C
ATOM   2658  O   LEU A 332     -94.579   8.971 -30.706  1.00 34.84           O
ANISOU 2658  O   LEU A 332     3139   2580   7518   -116    -96   -402       O
ATOM   2659  CB  LEU A 332     -91.784   8.888 -31.858  1.00 34.63           C
ANISOU 2659  CB  LEU A 332     3586   2534   7036    -14   -147   -570       C
ATOM   2660  CG  LEU A 332     -92.170   8.513 -33.290  1.00 36.23           C
ANISOU 2660  CG  LEU A 332     3832   2684   7248     -8   -384   -674       C
ATOM   2661  CD1 LEU A 332     -91.856   9.656 -34.244  1.00 35.32           C
ANISOU 2661  CD1 LEU A 332     3808   2677   6934     69   -437   -686       C
ATOM   2662  CD2 LEU A 332     -91.465   7.237 -33.721  1.00 38.75           C
ANISOU 2662  CD2 LEU A 332     4252   2918   7554    -19   -469   -797       C
ATOM   2663  N   TRP A 333     -94.700  10.677 -32.180  1.00 32.45           N
ANISOU 2663  N   TRP A 333     2921   2269   7139     25   -259   -497       N
ATOM   2664  CA  TRP A 333     -96.129  10.557 -32.425  1.00 34.25           C
ANISOU 2664  CA  TRP A 333     2932   2456   7625    -11   -380   -449       C
ATOM   2665  C   TRP A 333     -96.354  10.242 -33.895  1.00 35.21           C
ANISOU 2665  C   TRP A 333     3125   2529   7725    -35   -678   -485       C
ATOM   2666  O   TRP A 333     -95.814  10.927 -34.770  1.00 41.06           O
ANISOU 2666  O   TRP A 333     4003   3318   8281     24   -768   -499       O
ATOM   2667  CB  TRP A 333     -96.866  11.838 -32.034  1.00 44.08           C
ANISOU 2667  CB  TRP A 333     3998   3726   9023     81   -292   -430       C
ATOM   2668  CG  TRP A 333     -96.847  12.097 -30.565  1.00 47.16           C
ANISOU 2668  CG  TRP A 333     4282   4222   9417    108     -1   -457       C
ATOM   2669  CD1 TRP A 333     -95.825  12.636 -29.841  1.00 47.14           C
ANISOU 2669  CD1 TRP A 333     4406   4286   9219    160    173   -535       C
ATOM   2670  CD2 TRP A 333     -97.900  11.825 -29.633  1.00 51.96           C
ANISOU 2670  CD2 TRP A 333     4614   4929  10200     79    148   -409       C
ATOM   2671  NE1 TRP A 333     -96.176  12.718 -28.516  1.00 49.61           N
ANISOU 2671  NE1 TRP A 333     4559   4755   9535    169    414   -569       N
ATOM   2672  CE2 TRP A 333     -97.445  12.226 -28.362  1.00 53.64           C
ANISOU 2672  CE2 TRP A 333     4814   5309  10259    123    423   -482       C
ATOM   2673  CE3 TRP A 333     -99.184  11.284 -29.751  1.00 55.04           C
ANISOU 2673  CE3 TRP A 333     4748   5309  10856     12     73   -303       C
ATOM   2674  CZ2 TRP A 333     -98.228  12.103 -27.216  1.00 57.39           C
ANISOU 2674  CZ2 TRP A 333     5030   5991  10784    111    651   -457       C
ATOM   2675  CZ3 TRP A 333     -99.959  11.161 -28.612  1.00 56.18           C
ANISOU 2675  CZ3 TRP A 333     4616   5628  11101     -5    305   -244       C
ATOM   2676  CH2 TRP A 333     -99.479  11.569 -27.362  1.00 57.37           C
ANISOU 2676  CH2 TRP A 333     4762   5994  11043     49    604   -322       C
ATOM   2677  N   CYS A 334     -97.142   9.206 -34.161  1.00 37.05           N
ANISOU 2677  N   CYS A 334     3253   2685   8138   -133   -841   -490       N
ATOM   2678  CA  CYS A 334     -97.417   8.770 -35.520  1.00 39.05           C
ANISOU 2678  CA  CYS A 334     3566   2915   8354   -170  -1154   -580       C
ATOM   2679  C   CYS A 334     -98.910   8.551 -35.702  1.00 43.28           C
ANISOU 2679  C   CYS A 334     3845   3385   9214   -249  -1342   -507       C
ATOM   2680  O   CYS A 334     -99.623   8.192 -34.761  1.00 51.15           O
ANISOU 2680  O   CYS A 334     4623   4326  10486   -311  -1232   -402       O
ATOM   2681  CB  CYS A 334     -96.667   7.479 -35.862  1.00 38.58           C
ANISOU 2681  CB  CYS A 334     3670   2785   8204   -216  -1239   -748       C
ATOM   2682  SG  CYS A 334     -94.890   7.572 -35.609  1.00 42.89           S
ANISOU 2682  SG  CYS A 334     4472   3404   8422   -125  -1016   -821       S
ATOM   2683  N   LYS A 335     -99.373   8.774 -36.928  1.00 44.51           N
ANISOU 2683  N   LYS A 335     4009   3581   9320   -255  -1634   -540       N
ATOM   2684  CA  LYS A 335    -100.749   8.489 -37.304  1.00 49.55           C
ANISOU 2684  CA  LYS A 335     4408   4157  10262   -345  -1887   -483       C
ATOM   2685  C   LYS A 335    -100.756   7.961 -38.728  1.00 53.24           C
ANISOU 2685  C   LYS A 335     5006   4673  10551   -398  -2255   -650       C
ATOM   2686  O   LYS A 335    -100.138   8.558 -39.613  1.00 52.29           O
ANISOU 2686  O   LYS A 335     5067   4727  10074   -331  -2329   -687       O
ATOM   2687  CB  LYS A 335    -101.637   9.735 -37.191  1.00 54.11           C
ANISOU 2687  CB  LYS A 335     4758   4774  11028   -275  -1869   -294       C
ATOM   2688  CG  LYS A 335    -103.086   9.492 -37.589  1.00 63.92           C
ANISOU 2688  CG  LYS A 335     5712   5959  12614   -365  -2141   -206       C
ATOM   2689  CD  LYS A 335    -104.052  10.034 -36.547  1.00 69.67           C
ANISOU 2689  CD  LYS A 335     6094   6654  13722   -323  -1932    -42       C
ATOM   2690  CE  LYS A 335    -105.471   9.550 -36.810  1.00 78.58           C
ANISOU 2690  CE  LYS A 335     6974   7724  15160   -414  -2140     66       C
ATOM   2691  NZ  LYS A 335    -106.418   9.981 -35.745  1.00 81.89           N
ANISOU 2691  NZ  LYS A 335     7120   8154  15840   -349  -1854    214       N
ATOM   2692  N   ASP A 336    -101.440   6.834 -38.934  1.00 55.28           N
ANISOU 2692  N   ASP A 336     5159   4794  11050   -527  -2489   -750       N
ATOM   2693  CA  ASP A 336    -101.589   6.226 -40.257  1.00 59.18           C
ANISOU 2693  CA  ASP A 336     5751   5334  11401   -589  -2880   -978       C
ATOM   2694  C   ASP A 336    -100.233   5.953 -40.906  1.00 59.08           C
ANISOU 2694  C   ASP A 336     6066   5454  10927   -508  -2849  -1246       C
ATOM   2695  O   ASP A 336    -100.061   6.102 -42.118  1.00 61.56           O
ANISOU 2695  O   ASP A 336     6511   5991  10887   -489  -3074  -1393       O
ATOM   2696  CB  ASP A 336    -102.463   7.093 -41.166  1.00 64.27           C
ANISOU 2696  CB  ASP A 336     6279   6142  11999   -596  -3151   -845       C
ATOM   2697  CG  ASP A 336    -103.863   7.286 -40.614  1.00 72.64           C
ANISOU 2697  CG  ASP A 336     6984   7073  13544   -659  -3192   -603       C
ATOM   2698  OD1 ASP A 336    -104.383   6.355 -39.960  1.00 73.99           O
ANISOU 2698  OD1 ASP A 336     7068   7075  13969   -711  -3098   -581       O
ATOM   2699  OD2 ASP A 336    -104.444   8.369 -40.831  1.00 76.79           O
ANISOU 2699  OD2 ASP A 336     7351   7689  14136   -612  -3254   -391       O
ATOM   2700  N   GLY A 337     -99.258   5.557 -40.091  1.00 56.20           N
ANISOU 2700  N   GLY A 337     5813   4989  10552   -459  -2564  -1296       N
ATOM   2701  CA  GLY A 337     -97.965   5.154 -40.601  1.00 55.50           C
ANISOU 2701  CA  GLY A 337     5988   4996  10104   -374  -2511  -1562       C
ATOM   2702  C   GLY A 337     -97.006   6.275 -40.934  1.00 57.19           C
ANISOU 2702  C   GLY A 337     6368   5496   9867   -251  -2322  -1472       C
ATOM   2703  O   GLY A 337     -95.925   5.999 -41.467  1.00 61.40           O
ANISOU 2703  O   GLY A 337     7096   6169  10065   -173  -2270  -1684       O
ATOM   2704  N   HIS A 338     -97.356   7.525 -40.648  1.00 54.42           N
ANISOU 2704  N   HIS A 338     5922   5224   9529   -227  -2223  -1167       N
ATOM   2705  CA  HIS A 338     -96.466   8.649 -40.887  1.00 50.70           C
ANISOU 2705  CA  HIS A 338     5574   4970   8722   -132  -2062  -1026       C
ATOM   2706  C   HIS A 338     -96.238   9.410 -39.589  1.00 41.49           C
ANISOU 2706  C   HIS A 338     4336   3675   7753    -86  -1751   -816       C
ATOM   2707  O   HIS A 338     -97.005   9.291 -38.630  1.00 41.04           O
ANISOU 2707  O   HIS A 338     4103   3439   8051   -122  -1676   -739       O
ATOM   2708  CB  HIS A 338     -97.019   9.589 -41.968  1.00 55.70           C
ANISOU 2708  CB  HIS A 338     6159   5829   9177   -142  -2299   -853       C
ATOM   2709  CG  HIS A 338     -98.366  10.159 -41.648  1.00 67.20           C
ANISOU 2709  CG  HIS A 338     7360   7147  11025   -185  -2418   -630       C
ATOM   2710  ND1 HIS A 338     -98.569  11.072 -40.634  1.00 68.45           N
ANISOU 2710  ND1 HIS A 338     7380   7160  11468   -130  -2199   -415       N
ATOM   2711  CD2 HIS A 338     -99.578   9.955 -42.217  1.00 72.21           C
ANISOU 2711  CD2 HIS A 338     7832   7776  11828   -267  -2737   -608       C
ATOM   2712  CE1 HIS A 338     -99.848  11.401 -40.589  1.00 69.09           C
ANISOU 2712  CE1 HIS A 338     7212   7152  11888   -160  -2353   -274       C
ATOM   2713  NE2 HIS A 338    -100.482  10.736 -41.538  1.00 72.13           N
ANISOU 2713  NE2 HIS A 338     7572   7614  12218   -252  -2687   -361       N
ATOM   2714  N   VAL A 339     -95.166  10.200 -39.572  1.00 39.89           N
ANISOU 2714  N   VAL A 339     4260   3593   7305     -9  -1572   -732       N
ATOM   2715  CA  VAL A 339     -94.788  10.920 -38.363  1.00 37.42           C
ANISOU 2715  CA  VAL A 339     3908   3172   7140     38  -1295   -599       C
ATOM   2716  C   VAL A 339     -95.721  12.104 -38.154  1.00 47.61           C
ANISOU 2716  C   VAL A 339     5007   4403   8678     59  -1332   -392       C
ATOM   2717  O   VAL A 339     -95.902  12.940 -39.048  1.00 47.81           O
ANISOU 2717  O   VAL A 339     5012   4529   8626     72  -1500   -239       O
ATOM   2718  CB  VAL A 339     -93.325  11.380 -38.447  1.00 40.04           C
ANISOU 2718  CB  VAL A 339     4412   3626   7174    100  -1128   -577       C
ATOM   2719  CG1 VAL A 339     -92.953  12.193 -37.219  1.00 38.89           C
ANISOU 2719  CG1 VAL A 339     4224   3367   7185    139   -887   -471       C
ATOM   2720  CG2 VAL A 339     -92.402  10.184 -38.597  1.00 35.73           C
ANISOU 2720  CG2 VAL A 339     4018   3120   6440    107  -1074   -803       C
ATOM   2721  N   GLU A 340     -96.326  12.175 -36.967  1.00 48.93           N
ANISOU 2721  N   GLU A 340     5014   4423   9156     66  -1176   -378       N
ATOM   2722  CA  GLU A 340     -97.046  13.379 -36.564  1.00 54.00           C
ANISOU 2722  CA  GLU A 340     5461   4988  10069    130  -1144   -243       C
ATOM   2723  C   GLU A 340     -96.076  14.424 -36.026  1.00 50.21           C
ANISOU 2723  C   GLU A 340     5062   4487   9530    212   -952   -210       C
ATOM   2724  O   GLU A 340     -96.000  15.545 -36.541  1.00 49.06           O
ANISOU 2724  O   GLU A 340     4888   4316   9435    259  -1049    -65       O
ATOM   2725  CB  GLU A 340     -98.108  13.037 -35.514  1.00 60.28           C
ANISOU 2725  CB  GLU A 340     6018   5694  11191    117  -1028   -272       C
ATOM   2726  CG  GLU A 340     -99.411  12.481 -36.071  1.00 66.66           C
ANISOU 2726  CG  GLU A 340     6635   6475  12218     42  -1268   -228       C
ATOM   2727  CD  GLU A 340    -100.370  13.569 -36.520  1.00 75.91           C
ANISOU 2727  CD  GLU A 340     7591   7604  13646    106  -1425    -81       C
ATOM   2728  OE1 GLU A 340    -100.110  14.206 -37.562  1.00 80.18           O
ANISOU 2728  OE1 GLU A 340     8219   8193  14054    123  -1631     26       O
ATOM   2729  OE2 GLU A 340    -101.381  13.793 -35.822  1.00 79.30           O
ANISOU 2729  OE2 GLU A 340     7740   7968  14421    140  -1340    -52       O
ATOM   2730  N   THR A 341     -95.320  14.067 -34.989  1.00 46.70           N
ANISOU 2730  N   THR A 341     4702   4040   9003    216   -707   -322       N
ATOM   2731  CA  THR A 341     -94.282  14.935 -34.455  1.00 41.85           C
ANISOU 2731  CA  THR A 341     4178   3408   8316    273   -549   -324       C
ATOM   2732  C   THR A 341     -93.206  14.072 -33.813  1.00 41.19           C
ANISOU 2732  C   THR A 341     4255   3390   8005    236   -377   -422       C
ATOM   2733  O   THR A 341     -93.373  12.864 -33.627  1.00 39.88           O
ANISOU 2733  O   THR A 341     4100   3247   7806    176   -364   -481       O
ATOM   2734  CB  THR A 341     -94.840  15.941 -33.442  1.00 42.46           C
ANISOU 2734  CB  THR A 341     4073   3375   8684    357   -421   -372       C
ATOM   2735  OG1 THR A 341     -93.827  16.901 -33.118  1.00 41.84           O
ANISOU 2735  OG1 THR A 341     4083   3242   8573    405   -343   -386       O
ATOM   2736  CG2 THR A 341     -95.273  15.231 -32.171  1.00 43.12           C
ANISOU 2736  CG2 THR A 341     4058   3516   8809    342   -207   -502       C
ATOM   2737  N   PHE A 342     -92.093  14.718 -33.468  1.00 43.66           N
ANISOU 2737  N   PHE A 342     4672   3708   8210    266   -269   -420       N
ATOM   2738  CA  PHE A 342     -90.929  14.021 -32.927  1.00 38.40           C
ANISOU 2738  CA  PHE A 342     4148   3105   7337    236   -130   -478       C
ATOM   2739  C   PHE A 342     -90.034  15.077 -32.293  1.00 42.01           C
ANISOU 2739  C   PHE A 342     4640   3534   7789    270    -26   -478       C
ATOM   2740  O   PHE A 342     -89.480  15.921 -33.004  1.00 44.77           O
ANISOU 2740  O   PHE A 342     5031   3860   8120    286   -109   -372       O
ATOM   2741  CB  PHE A 342     -90.203  13.255 -34.029  1.00 33.98           C
ANISOU 2741  CB  PHE A 342     3733   2633   6545    214   -225   -464       C
ATOM   2742  CG  PHE A 342     -89.007  12.486 -33.554  1.00 37.20           C
ANISOU 2742  CG  PHE A 342     4256   3082   6798    202    -99   -519       C
ATOM   2743  CD1 PHE A 342     -89.147  11.458 -32.640  1.00 38.65           C
ANISOU 2743  CD1 PHE A 342     4408   3224   7051    162    -18   -574       C
ATOM   2744  CD2 PHE A 342     -87.744  12.776 -34.042  1.00 40.05           C
ANISOU 2744  CD2 PHE A 342     4724   3527   6967    224    -70   -474       C
ATOM   2745  CE1 PHE A 342     -88.049  10.743 -32.210  1.00 36.04           C
ANISOU 2745  CE1 PHE A 342     4159   2910   6625    153     69   -589       C
ATOM   2746  CE2 PHE A 342     -86.640  12.064 -33.614  1.00 36.95           C
ANISOU 2746  CE2 PHE A 342     4406   3162   6473    225     37   -517       C
ATOM   2747  CZ  PHE A 342     -86.793  11.047 -32.697  1.00 36.43           C
ANISOU 2747  CZ  PHE A 342     4314   3027   6500    194     96   -577       C
ATOM   2748  N   TYR A 343     -89.902  15.038 -30.970  1.00 40.73           N
ANISOU 2748  N   TYR A 343     4447   3388   7641    269    140   -582       N
ATOM   2749  CA  TYR A 343     -89.230  16.110 -30.251  1.00 38.57           C
ANISOU 2749  CA  TYR A 343     4181   3081   7392    298    209   -644       C
ATOM   2750  C   TYR A 343     -88.519  15.546 -29.039  1.00 38.94           C
ANISOU 2750  C   TYR A 343     4278   3238   7278    258    365   -724       C
ATOM   2751  O   TYR A 343     -88.930  14.507 -28.502  1.00 35.37           O
ANISOU 2751  O   TYR A 343     3790   2889   6761    216    443   -722       O
ATOM   2752  CB  TYR A 343     -90.227  17.194 -29.815  1.00 35.95           C
ANISOU 2752  CB  TYR A 343     3686   2700   7271    359    207   -735       C
ATOM   2753  CG  TYR A 343     -91.355  16.683 -28.949  1.00 36.66           C
ANISOU 2753  CG  TYR A 343     3622   2841   7467    388    340   -864       C
ATOM   2754  CD1 TYR A 343     -92.533  16.219 -29.518  1.00 36.61           C
ANISOU 2754  CD1 TYR A 343     3490   2804   7616    395    272   -798       C
ATOM   2755  CD2 TYR A 343     -91.244  16.668 -27.564  1.00 38.80           C
ANISOU 2755  CD2 TYR A 343     3848   3236   7659    401    532  -1036       C
ATOM   2756  CE1 TYR A 343     -93.568  15.752 -28.734  1.00 34.87           C
ANISOU 2756  CE1 TYR A 343     3091   2691   7466    396    400   -858       C
ATOM   2757  CE2 TYR A 343     -92.275  16.201 -26.771  1.00 39.19           C
ANISOU 2757  CE2 TYR A 343     3726   3442   7722    405    677  -1098       C
ATOM   2758  CZ  TYR A 343     -93.435  15.746 -27.362  1.00 39.39           C
ANISOU 2758  CZ  TYR A 343     3612   3434   7919    402    617   -995       C
ATOM   2759  OH  TYR A 343     -94.466  15.280 -26.580  1.00 45.64           O
ANISOU 2759  OH  TYR A 343     4195   4398   8747    393    770  -1014       O
ATOM   2760  N   PRO A 344     -87.455  16.195 -28.571  1.00 43.40           N
ANISOU 2760  N   PRO A 344     4908   3795   7786    253    391   -764       N
ATOM   2761  CA  PRO A 344     -86.810  15.774 -27.330  1.00 44.67           C
ANISOU 2761  CA  PRO A 344     5100   4099   7775    207    512   -832       C
ATOM   2762  C   PRO A 344     -87.618  16.208 -26.118  1.00 48.64           C
ANISOU 2762  C   PRO A 344     5479   4699   8304    239    629  -1031       C
ATOM   2763  O   PRO A 344     -88.298  17.236 -26.129  1.00 50.32           O
ANISOU 2763  O   PRO A 344     5595   4804   8721    322    612  -1178       O
ATOM   2764  CB  PRO A 344     -85.453  16.491 -27.366  1.00 45.15           C
ANISOU 2764  CB  PRO A 344     5248   4102   7805    188    459   -815       C
ATOM   2765  CG  PRO A 344     -85.350  17.119 -28.737  1.00 41.11           C
ANISOU 2765  CG  PRO A 344     4752   3467   7402    209    323   -672       C
ATOM   2766  CD  PRO A 344     -86.747  17.323 -29.201  1.00 40.02           C
ANISOU 2766  CD  PRO A 344     4517   3292   7397    257    275   -683       C
ATOM   2767  N   LYS A 345     -87.529  15.408 -25.061  1.00 55.65           N
ANISOU 2767  N   LYS A 345     6351   5809   8986    178    750  -1028       N
ATOM   2768  CA  LYS A 345     -88.236  15.703 -23.828  1.00 62.63           C
ANISOU 2768  CA  LYS A 345     7104   6899   9795    201    899  -1213       C
ATOM   2769  C   LYS A 345     -87.372  16.583 -22.925  1.00 68.67           C
ANISOU 2769  C   LYS A 345     7917   7738  10436    208    911  -1429       C
ATOM   2770  O   LYS A 345     -86.263  16.989 -23.281  1.00 65.52           O
ANISOU 2770  O   LYS A 345     7637   7196  10062    186    792  -1401       O
ATOM   2771  CB  LYS A 345     -88.644  14.407 -23.129  1.00 60.52           C
ANISOU 2771  CB  LYS A 345     6761   6884   9349    109   1014  -1045       C
ATOM   2772  CG  LYS A 345     -89.576  13.539 -23.963  1.00 57.45           C
ANISOU 2772  CG  LYS A 345     6300   6391   9138     89    972   -864       C
ATOM   2773  CD  LYS A 345     -89.937  12.249 -23.247  1.00 59.04           C
ANISOU 2773  CD  LYS A 345     6399   6798   9236    -27   1057   -648       C
ATOM   2774  CE  LYS A 345     -90.671  12.524 -21.946  1.00 62.14           C
ANISOU 2774  CE  LYS A 345     6607   7534   9468    -29   1264   -734       C
ATOM   2775  NZ  LYS A 345     -91.111  11.264 -21.286  1.00 63.43           N
ANISOU 2775  NZ  LYS A 345     6627   7920   9552   -168   1342   -434       N
ATOM   2776  N   LEU A 346     -87.892  16.888 -21.738  1.00 77.78           N
ANISOU 2776  N   LEU A 346     8960   9144  11450    238   1055  -1659       N
ATOM   2777  CA  LEU A 346     -87.205  17.752 -20.784  1.00 86.34           C
ANISOU 2777  CA  LEU A 346    10075  10333  12398    251   1054  -1950       C
ATOM   2778  C   LEU A 346     -85.868  17.168 -20.347  1.00 91.22           C
ANISOU 2778  C   LEU A 346    10825  11088  12746    119    992  -1784       C
ATOM   2779  O   LEU A 346     -84.808  17.718 -20.665  1.00 89.01           O
ANISOU 2779  O   LEU A 346    10650  10614  12555     98    843  -1801       O
ATOM   2780  CB  LEU A 346     -88.091  17.996 -19.560  1.00 90.26           C
ANISOU 2780  CB  LEU A 346    10410  11180  12706    311   1253  -2245       C
ATOM   2781  CG  LEU A 346     -89.385  18.771 -19.811  1.00 92.22           C
ANISOU 2781  CG  LEU A 346    10480  11300  13259    476   1326  -2492       C
ATOM   2782  CD1 LEU A 346     -90.200  18.885 -18.531  1.00 95.14           C
ANISOU 2782  CD1 LEU A 346    10663  12107  13377    541   1570  -2790       C
ATOM   2783  CD2 LEU A 346     -89.059  20.142 -20.369  1.00 92.86           C
ANISOU 2783  CD2 LEU A 346    10616  10983  13683    559   1118  -2675       C
ATOM   2784  N   GLN A 347     -85.910  16.059 -19.617  1.00100.87           N
ANISOU 2784  N   GLN A 347    12016  12640  13672     21   1093  -1587       N
ATOM   2785  CA  GLN A 347     -84.697  15.435 -19.107  1.00107.15           C
ANISOU 2785  CA  GLN A 347    12900  13583  14228   -104   1022  -1393       C
ATOM   2786  C   GLN A 347     -84.888  13.934 -18.924  1.00113.23           C
ANISOU 2786  C   GLN A 347    13620  14528  14874   -208   1078  -1006       C
ATOM   2787  O   GLN A 347     -84.039  13.137 -19.323  1.00114.82           O
ANISOU 2787  O   GLN A 347    13892  14609  15124   -274    975   -731       O
ATOM   2788  CB  GLN A 347     -84.284  16.079 -17.782  1.00110.46           C
ANISOU 2788  CB  GLN A 347    13309  14324  14336   -131   1041  -1671       C
ATOM   2789  CG  GLN A 347     -83.061  15.455 -17.140  1.00111.09           C
ANISOU 2789  CG  GLN A 347    13456  14604  14151   -272    945  -1451       C
ATOM   2790  CD  GLN A 347     -82.812  15.982 -15.742  1.00115.71           C
ANISOU 2790  CD  GLN A 347    14015  15606  14345   -315    960  -1728       C
ATOM   2791  OE1 GLN A 347     -81.808  15.654 -15.109  1.00116.93           O
ANISOU 2791  OE1 GLN A 347    14211  15957  14261   -434    851  -1589       O
ATOM   2792  NE2 GLN A 347     -83.732  16.804 -15.249  1.00118.06           N
ANISOU 2792  NE2 GLN A 347    14228  16058  14572   -210   1090  -2143       N
TER    2793      GLN A 347
ATOM   2794  N   ALA B   0     -93.205  17.617   1.138  1.00 82.01           N
ANISOU 2794  N   ALA B   0    11458   8087  11616  -1627   -886   -922       N
ATOM   2795  CA  ALA B   0     -93.368  18.957   0.591  1.00 77.20           C
ANISOU 2795  CA  ALA B   0    10599   7827  10905  -1528   -978   -868       C
ATOM   2796  C   ALA B   0     -92.488  19.957   1.334  1.00 72.65           C
ANISOU 2796  C   ALA B   0     9823   7412  10369  -1183   -734   -735       C
ATOM   2797  O   ALA B   0     -92.994  20.875   1.981  1.00 72.98           O
ANISOU 2797  O   ALA B   0     9505   7676  10549  -1156   -727   -572       O
ATOM   2798  CB  ALA B   0     -94.823  19.389   0.651  1.00 74.38           C
ANISOU 2798  CB  ALA B   0     9866   7699  10697  -1803  -1215   -729       C
ATOM   2799  N  AMET B   1     -91.171  19.782   1.238  0.56 70.10           N
ANISOU 2799  N  AMET B   1     9734   6976   9924   -919   -535   -802       N
ATOM   2800  N  BMET B   1     -91.174  19.756   1.245  0.44 70.09           N
ANISOU 2800  N  BMET B   1     9738   6970   9925   -922   -535   -803       N
ATOM   2801  CA AMET B   1     -90.240  20.679   1.913  0.56 65.53           C
ANISOU 2801  CA AMET B   1     8978   6545   9375   -638   -338   -674       C
ATOM   2802  CA BMET B   1     -90.229  20.679   1.857  0.44 65.52           C
ANISOU 2802  CA BMET B   1     8986   6544   9366   -637   -341   -680       C
ATOM   2803  C  AMET B   1     -90.182  22.020   1.189  0.56 60.74           C
ANISOU 2803  C  AMET B   1     8225   6194   8658   -547   -409   -639       C
ATOM   2804  C  BMET B   1     -90.298  22.032   1.158  0.44 60.86           C
ANISOU 2804  C  BMET B   1     8231   6217   8677   -568   -428   -639       C
ATOM   2805  O  AMET B   1     -90.004  22.072  -0.032  0.56 60.98           O
ANISOU 2805  O  AMET B   1     8440   6249   8479   -536   -488   -740       O
ATOM   2806  O  BMET B   1     -90.359  22.107  -0.074  0.44 61.43           O
ANISOU 2806  O  BMET B   1     8460   6327   8554   -601   -549   -736       O
ATOM   2807  CB AMET B   1     -88.849  20.047   1.979  0.56 66.51           C
ANISOU 2807  CB AMET B   1     9347   6502   9422   -393   -117   -713       C
ATOM   2808  CB BMET B   1     -88.815  20.090   1.797  0.44 66.66           C
ANISOU 2808  CB BMET B   1     9387   6528   9411   -386   -126   -730       C
ATOM   2809  CG AMET B   1     -87.902  20.706   2.972  0.56 63.96           C
ANISOU 2809  CG AMET B   1     8820   6309   9173   -168     61   -549       C
ATOM   2810  CG BMET B   1     -87.723  21.016   1.262  0.44 66.64           C
ANISOU 2810  CG BMET B   1     9354   6705   9263   -133    -19   -695       C
ATOM   2811  SD AMET B   1     -88.491  20.552   4.670  0.56 59.97           S
ANISOU 2811  SD AMET B   1     8087   5807   8893   -269     99   -393       S
ATOM   2812  SD BMET B   1     -87.492  20.871  -0.524  0.44 71.40           S
ANISOU 2812  SD BMET B   1    10281   7299   9550    -97    -72   -879       S
ATOM   2813  CE AMET B   1     -88.529  18.771   4.866  0.56 60.86           C
ANISOU 2813  CE AMET B   1     8496   5557   9070   -347    154   -434       C
ATOM   2814  CE BMET B   1     -86.014  21.853  -0.770  0.44 69.92           C
ANISOU 2814  CE BMET B   1     9984   7322   9261    222    140   -744       C
ATOM   2815  N   SER B   2     -90.322  23.104   1.948  1.00 51.76           N
ANISOU 2815  N   SER B   2     6787   5232   7647   -477   -371   -494       N
ATOM   2816  CA  SER B   2     -90.407  24.439   1.375  1.00 42.81           C
ANISOU 2816  CA  SER B   2     5504   4300   6462   -403   -443   -427       C
ATOM   2817  C   SER B   2     -89.991  25.473   2.406  1.00 36.59           C
ANISOU 2817  C   SER B   2     4510   3597   5796   -258   -312   -307       C
ATOM   2818  O   SER B   2     -90.057  25.237   3.615  1.00 36.84           O
ANISOU 2818  O   SER B   2     4454   3590   5954   -259   -213   -268       O
ATOM   2819  CB  SER B   2     -91.820  24.746   0.873  1.00 45.84           C
ANISOU 2819  CB  SER B   2     5723   4804   6889   -586   -674   -393       C
ATOM   2820  OG  SER B   2     -92.652  25.209   1.925  1.00 44.71           O
ANISOU 2820  OG  SER B   2     5280   4740   6969   -611   -651   -271       O
ATOM   2821  N   LEU B   3     -89.576  26.635   1.899  1.00 29.13           N
ANISOU 2821  N   LEU B   3     3512   2761   4794   -147   -320   -246       N
ATOM   2822  CA  LEU B   3     -89.209  27.745   2.771  1.00 30.67           C
ANISOU 2822  CA  LEU B   3     3556   3004   5095    -41   -229   -156       C
ATOM   2823  C   LEU B   3     -90.399  28.220   3.596  1.00 32.74           C
ANISOU 2823  C   LEU B   3     3609   3305   5527    -80   -255   -110       C
ATOM   2824  O   LEU B   3     -90.270  28.472   4.800  1.00 33.99           O
ANISOU 2824  O   LEU B   3     3701   3446   5766    -33   -139    -95       O
ATOM   2825  CB  LEU B   3     -88.648  28.894   1.934  1.00 33.64           C
ANISOU 2825  CB  LEU B   3     3934   3452   5396     48   -253    -82       C
ATOM   2826  CG  LEU B   3     -88.497  30.248   2.623  1.00 35.68           C
ANISOU 2826  CG  LEU B   3     4066   3717   5775    118   -212      3       C
ATOM   2827  CD1 LEU B   3     -87.419  30.193   3.694  1.00 38.69           C
ANISOU 2827  CD1 LEU B   3     4467   4055   6177    150    -84     -4       C
ATOM   2828  CD2 LEU B   3     -88.197  31.334   1.601  1.00 34.22           C
ANISOU 2828  CD2 LEU B   3     3889   3577   5536    168   -268    107       C
ATOM   2829  N   GLU B   4     -91.564  28.358   2.961  1.00 32.19           N
ANISOU 2829  N   GLU B   4     3426   3310   5495   -156   -402    -76       N
ATOM   2830  CA  GLU B   4     -92.747  28.820   3.677  1.00 28.54           C
ANISOU 2830  CA  GLU B   4     2718   2917   5209   -155   -398      1       C
ATOM   2831  C   GLU B   4     -93.191  27.817   4.732  1.00 26.80           C
ANISOU 2831  C   GLU B   4     2444   2665   5074   -257   -310    -15       C
ATOM   2832  O   GLU B   4     -93.725  28.211   5.775  1.00 28.48           O
ANISOU 2832  O   GLU B   4     2497   2923   5402   -195   -191     40       O
ATOM   2833  CB  GLU B   4     -93.883  29.097   2.691  1.00 34.88           C
ANISOU 2833  CB  GLU B   4     3365   3847   6043   -219   -599     87       C
ATOM   2834  CG  GLU B   4     -93.697  30.352   1.842  1.00 41.10           C
ANISOU 2834  CG  GLU B   4     4143   4684   6788    -83   -669    174       C
ATOM   2835  CD  GLU B   4     -92.637  30.198   0.763  1.00 46.79           C
ANISOU 2835  CD  GLU B   4     5114   5379   7283    -94   -719    121       C
ATOM   2836  OE1 GLU B   4     -92.113  29.078   0.585  1.00 46.94           O
ANISOU 2836  OE1 GLU B   4     5320   5339   7176   -189   -705     -2       O
ATOM   2837  OE2 GLU B   4     -92.326  31.204   0.090  1.00 48.70           O
ANISOU 2837  OE2 GLU B   4     5371   5654   7476      8   -752    216       O
ATOM   2838  N   ASN B   5     -92.979  26.523   4.486  1.00 29.62           N
ANISOU 2838  N   ASN B   5     2956   2930   5367   -401   -349    -84       N
ATOM   2839  CA  ASN B   5     -93.346  25.521   5.480  1.00 30.86           C
ANISOU 2839  CA  ASN B   5     3084   3028   5613   -512   -262    -65       C
ATOM   2840  C   ASN B   5     -92.383  25.539   6.659  1.00 28.17           C
ANISOU 2840  C   ASN B   5     2823   2633   5246   -380    -63    -65       C
ATOM   2841  O   ASN B   5     -92.800  25.373   7.811  1.00 35.78           O
ANISOU 2841  O   ASN B   5     3682   3630   6284   -390     57      2       O
ATOM   2842  CB  ASN B   5     -93.392  24.133   4.843  1.00 26.82           C
ANISOU 2842  CB  ASN B   5     2762   2372   5054   -711   -369   -141       C
ATOM   2843  CG  ASN B   5     -93.610  23.033   5.862  1.00 41.63           C
ANISOU 2843  CG  ASN B   5     4652   4135   7031   -829   -267    -96       C
ATOM   2844  OD1 ASN B   5     -92.693  22.276   6.180  1.00 38.89           O
ANISOU 2844  OD1 ASN B   5     4526   3623   6630   -779   -165   -137       O
ATOM   2845  ND2 ASN B   5     -94.826  22.945   6.388  1.00 40.49           N
ANISOU 2845  ND2 ASN B   5     4252   4091   7041   -973   -282     22       N
ATOM   2846  N   VAL B   6     -91.090  25.733   6.391  1.00 25.39           N
ANISOU 2846  N   VAL B   6     2643   2227   4776   -262    -29   -117       N
ATOM   2847  CA  VAL B   6     -90.120  25.846   7.475  1.00 26.46           C
ANISOU 2847  CA  VAL B   6     2824   2353   4876   -154    113    -94       C
ATOM   2848  C   VAL B   6     -90.473  27.024   8.373  1.00 28.78           C
ANISOU 2848  C   VAL B   6     2979   2747   5210    -78    179    -66       C
ATOM   2849  O   VAL B   6     -90.428  26.924   9.605  1.00 33.34           O
ANISOU 2849  O   VAL B   6     3541   3350   5775    -58    292    -37       O
ATOM   2850  CB  VAL B   6     -88.694  25.968   6.906  1.00 31.60           C
ANISOU 2850  CB  VAL B   6     3618   2974   5416    -49    121   -116       C
ATOM   2851  CG1 VAL B   6     -87.706  26.298   8.008  1.00 31.09           C
ANISOU 2851  CG1 VAL B   6     3546   2949   5319     36    214    -65       C
ATOM   2852  CG2 VAL B   6     -88.289  24.678   6.207  1.00 33.91           C
ANISOU 2852  CG2 VAL B   6     4093   3137   5653    -69    120   -159       C
ATOM   2853  N   ALA B   7     -90.853  28.151   7.768  1.00 30.82           N
ANISOU 2853  N   ALA B   7     3158   3051   5502    -22    117    -72       N
ATOM   2854  CA  ALA B   7     -91.229  29.321   8.551  1.00 26.15           C
ANISOU 2854  CA  ALA B   7     2481   2500   4956     82    197    -69       C
ATOM   2855  C   ALA B   7     -92.512  29.082   9.335  1.00 30.84           C
ANISOU 2855  C   ALA B   7     2905   3171   5642     72    293    -20       C
ATOM   2856  O   ALA B   7     -92.663  29.604  10.445  1.00 33.74           O
ANISOU 2856  O   ALA B   7     3262   3566   5991    164    437    -34       O
ATOM   2857  CB  ALA B   7     -91.376  30.536   7.637  1.00 24.75           C
ANISOU 2857  CB  ALA B   7     2269   2315   4821    162    113    -56       C
ATOM   2858  N   PHE B   8     -93.442  28.301   8.778  1.00 31.46           N
ANISOU 2858  N   PHE B   8     2853   3292   5807    -50    216     43       N
ATOM   2859  CA  PHE B   8     -94.664  27.977   9.506  1.00 31.11           C
ANISOU 2859  CA  PHE B   8     2595   3352   5874    -89    315    138       C
ATOM   2860  C   PHE B   8     -94.350  27.213  10.785  1.00 36.78           C
ANISOU 2860  C   PHE B   8     3390   4060   6525   -123    476    155       C
ATOM   2861  O   PHE B   8     -94.911  27.508  11.846  1.00 43.69           O
ANISOU 2861  O   PHE B   8     4163   5032   7406    -42    656    204       O
ATOM   2862  CB  PHE B   8     -95.610  27.169   8.617  1.00 29.40           C
ANISOU 2862  CB  PHE B   8     2227   3180   5765   -287    152    215       C
ATOM   2863  CG  PHE B   8     -96.828  26.654   9.335  1.00 32.38           C
ANISOU 2863  CG  PHE B   8     2344   3680   6280   -384    246    359       C
ATOM   2864  CD1 PHE B   8     -97.983  27.415   9.403  1.00 35.60           C
ANISOU 2864  CD1 PHE B   8     2436   4262   6826   -286    293    481       C
ATOM   2865  CD2 PHE B   8     -96.820  25.406   9.939  1.00 37.24           C
ANISOU 2865  CD2 PHE B   8     3013   4238   6900   -561    302    405       C
ATOM   2866  CE1 PHE B   8     -99.106  26.945  10.063  1.00 37.37           C
ANISOU 2866  CE1 PHE B   8     2372   4640   7188   -370    406    651       C
ATOM   2867  CE2 PHE B   8     -97.936  24.932  10.604  1.00 41.98           C
ANISOU 2867  CE2 PHE B   8     3352   4964   7633   -674    402    575       C
ATOM   2868  CZ  PHE B   8     -99.081  25.701  10.664  1.00 40.16           C
ANISOU 2868  CZ  PHE B   8     2776   4945   7537   -583    459    702       C
ATOM   2869  N   ASN B   9     -93.461  26.221  10.700  1.00 34.23           N
ANISOU 2869  N   ASN B   9     3254   3624   6126   -219    430    131       N
ATOM   2870  CA  ASN B   9     -93.103  25.451  11.885  1.00 30.80           C
ANISOU 2870  CA  ASN B   9     2900   3180   5625   -243    565    189       C
ATOM   2871  C   ASN B   9     -92.420  26.327  12.924  1.00 27.86           C
ANISOU 2871  C   ASN B   9     2612   2869   5106    -85    680    142       C
ATOM   2872  O   ASN B   9     -92.666  26.185  14.126  1.00 33.66           O
ANISOU 2872  O   ASN B   9     3333   3688   5768    -62    834    202       O
ATOM   2873  CB  ASN B   9     -92.202  24.279  11.496  1.00 30.02           C
ANISOU 2873  CB  ASN B   9     2995   2920   5490   -325    492    185       C
ATOM   2874  CG  ASN B   9     -92.968  23.138  10.863  1.00 25.78           C
ANISOU 2874  CG  ASN B   9     2439   2280   5076   -531    408    228       C
ATOM   2875  OD1 ASN B   9     -93.306  22.159  11.529  1.00 41.71           O
ANISOU 2875  OD1 ASN B   9     4458   4245   7146   -647    480    340       O
ATOM   2876  ND2 ASN B   9     -93.246  23.255   9.571  1.00 27.48           N
ANISOU 2876  ND2 ASN B   9     2654   2460   5326   -598    240    148       N
ATOM   2877  N   VAL B  10     -91.566  27.248  12.477  1.00 22.60           N
ANISOU 2877  N   VAL B  10     2045   2164   4379      5    601     39       N
ATOM   2878  CA  VAL B  10     -90.825  28.087  13.413  1.00 28.61           C
ANISOU 2878  CA  VAL B  10     2921   2957   4993     99    660    -25       C
ATOM   2879  C   VAL B  10     -91.773  28.982  14.200  1.00 33.62           C
ANISOU 2879  C   VAL B  10     3492   3666   5616    206    811    -63       C
ATOM   2880  O   VAL B  10     -91.642  29.128  15.421  1.00 37.34           O
ANISOU 2880  O   VAL B  10     4054   4204   5931    249    933    -85       O
ATOM   2881  CB  VAL B  10     -89.760  28.907  12.663  1.00 28.17           C
ANISOU 2881  CB  VAL B  10     2962   2831   4912    128    529   -101       C
ATOM   2882  CG1 VAL B  10     -89.155  29.957  13.579  1.00 29.56           C
ANISOU 2882  CG1 VAL B  10     3258   3019   4957    177    553   -185       C
ATOM   2883  CG2 VAL B  10     -88.679  27.989  12.118  1.00 20.05           C
ANISOU 2883  CG2 VAL B  10     1999   1762   3857     75    443    -49       C
ATOM   2884  N   VAL B  11     -92.750  29.583  13.521  1.00 33.93           N
ANISOU 2884  N   VAL B  11     3379   3706   5806    270    815    -61       N
ATOM   2885  CA  VAL B  11     -93.633  30.520  14.208  1.00 34.26           C
ANISOU 2885  CA  VAL B  11     3359   3802   5855    436    993    -93       C
ATOM   2886  C   VAL B  11     -94.645  29.788  15.084  1.00 34.81           C
ANISOU 2886  C   VAL B  11     3268   4027   5932    430   1190     27       C
ATOM   2887  O   VAL B  11     -95.081  30.323  16.109  1.00 37.71           O
ANISOU 2887  O   VAL B  11     3659   4468   6200    578   1406     -6       O
ATOM   2888  CB  VAL B  11     -94.329  31.448  13.196  1.00 40.29           C
ANISOU 2888  CB  VAL B  11     3986   4524   6798    547    938    -84       C
ATOM   2889  CG1 VAL B  11     -93.298  32.263  12.429  1.00 42.03           C
ANISOU 2889  CG1 VAL B  11     4383   4590   6998    551    774   -176       C
ATOM   2890  CG2 VAL B  11     -95.193  30.655  12.237  1.00 46.80           C
ANISOU 2890  CG2 VAL B  11     4555   5432   7796    434    832     62       C
ATOM   2891  N   ASN B  12     -95.025  28.564  14.719  1.00 34.81           N
ANISOU 2891  N   ASN B  12     3123   4069   6034    256   1131    169       N
ATOM   2892  CA  ASN B  12     -96.032  27.824  15.469  1.00 37.54           C
ANISOU 2892  CA  ASN B  12     3278   4563   6422    205   1310    332       C
ATOM   2893  C   ASN B  12     -95.444  26.855  16.482  1.00 40.75           C
ANISOU 2893  C   ASN B  12     3836   4985   6662    110   1387    395       C
ATOM   2894  O   ASN B  12     -96.069  26.611  17.520  1.00 46.02           O
ANISOU 2894  O   ASN B  12     4424   5798   7262    138   1610    507       O
ATOM   2895  CB  ASN B  12     -96.945  27.044  14.514  1.00 40.90           C
ANISOU 2895  CB  ASN B  12     3442   5015   7083     22   1185    479       C
ATOM   2896  CG  ASN B  12     -97.866  27.946  13.719  1.00 44.27           C
ANISOU 2896  CG  ASN B  12     3625   5514   7681    130   1142    503       C
ATOM   2897  OD1 ASN B  12     -98.940  28.325  14.188  1.00 49.34           O
ANISOU 2897  OD1 ASN B  12     4011   6323   8414    251   1329    618       O
ATOM   2898  ND2 ASN B  12     -97.455  28.286  12.504  1.00 41.21           N
ANISOU 2898  ND2 ASN B  12     3303   5021   7336    106    907    422       N
ATOM   2899  N   LYS B  13     -94.267  26.292  16.211  1.00 35.78           N
ANISOU 2899  N   LYS B  13     3408   4225   5962     17   1225    354       N
ATOM   2900  CA  LYS B  13     -93.672  25.293  17.086  1.00 33.36           C
ANISOU 2900  CA  LYS B  13     3232   3923   5522    -59   1274    459       C
ATOM   2901  C   LYS B  13     -92.336  25.720  17.677  1.00 32.87           C
ANISOU 2901  C   LYS B  13     3409   3855   5224     23   1225    361       C
ATOM   2902  O   LYS B  13     -91.726  24.936  18.412  1.00 35.43           O
ANISOU 2902  O   LYS B  13     3840   4202   5420    -18   1240    472       O
ATOM   2903  CB  LYS B  13     -93.493  23.968  16.333  1.00 35.64           C
ANISOU 2903  CB  LYS B  13     3529   4056   5957   -241   1138    558       C
ATOM   2904  CG  LYS B  13     -94.791  23.368  15.818  1.00 42.66           C
ANISOU 2904  CG  LYS B  13     4191   4946   7070   -406   1140    674       C
ATOM   2905  CD  LYS B  13     -95.717  22.991  16.963  1.00 49.15           C
ANISOU 2905  CD  LYS B  13     4858   5932   7886   -446   1370    873       C
ATOM   2906  CE  LYS B  13     -97.008  22.373  16.451  1.00 52.07           C
ANISOU 2906  CE  LYS B  13     4950   6324   8508   -658   1349   1028       C
ATOM   2907  NZ  LYS B  13     -97.887  21.923  17.567  1.00 55.06           N
ANISOU 2907  NZ  LYS B  13     5147   6879   8894   -716   1597   1272       N
ATOM   2908  N   GLY B  14     -91.867  26.933  17.389  1.00 33.28           N
ANISOU 2908  N   GLY B  14     3543   3878   5223    122   1153    182       N
ATOM   2909  CA  GLY B  14     -90.572  27.380  17.854  1.00 30.36           C
ANISOU 2909  CA  GLY B  14     3375   3508   4654    143   1058     98       C
ATOM   2910  C   GLY B  14     -89.393  26.810  17.099  1.00 32.31           C
ANISOU 2910  C   GLY B  14     3666   3661   4952     78    869    140       C
ATOM   2911  O   GLY B  14     -88.266  27.280  17.298  1.00 34.26           O
ANISOU 2911  O   GLY B  14     4020   3923   5073     81    758     93       O
ATOM   2912  N   HIS B  15     -89.614  25.824  16.243  1.00 31.34           N
ANISOU 2912  N   HIS B  15     3465   3441   5002     16    832    228       N
ATOM   2913  CA  HIS B  15     -88.576  25.172  15.448  1.00 24.45           C
ANISOU 2913  CA  HIS B  15     2648   2462   4181      0    705    266       C
ATOM   2914  C   HIS B  15     -89.290  24.324  14.401  1.00 23.00           C
ANISOU 2914  C   HIS B  15     2410   2142   4185    -75    686    288       C
ATOM   2915  O   HIS B  15     -90.522  24.347  14.301  1.00 26.25           O
ANISOU 2915  O   HIS B  15     2704   2572   4696   -137    736    290       O
ATOM   2916  CB  HIS B  15     -87.648  24.327  16.320  1.00 26.07           C
ANISOU 2916  CB  HIS B  15     2936   2706   4265     12    711    415       C
ATOM   2917  CG  HIS B  15     -88.301  23.097  16.869  1.00 30.32           C
ANISOU 2917  CG  HIS B  15     3470   3207   4842    -43    821    578       C
ATOM   2918  ND1 HIS B  15     -87.755  21.840  16.729  1.00 32.40           N
ANISOU 2918  ND1 HIS B  15     3803   3339   5170    -41    809    726       N
ATOM   2919  CD2 HIS B  15     -89.460  22.931  17.549  1.00 30.95           C
ANISOU 2919  CD2 HIS B  15     3483   3355   4921   -101    960    640       C
ATOM   2920  CE1 HIS B  15     -88.548  20.952  17.301  1.00 34.73           C
ANISOU 2920  CE1 HIS B  15     4092   3595   5508   -123    917    871       C
ATOM   2921  NE2 HIS B  15     -89.589  21.589  17.809  1.00 34.10           N
ANISOU 2921  NE2 HIS B  15     3911   3658   5387   -170   1012    833       N
ATOM   2922  N   PHE B  16     -88.524  23.561  13.628  1.00 29.38           N
ANISOU 2922  N   PHE B  16     3306   2820   5038    -71    615    308       N
ATOM   2923  CA  PHE B  16     -89.119  22.659  12.652  1.00 32.98           C
ANISOU 2923  CA  PHE B  16     3786   3113   5632   -165    578    296       C
ATOM   2924  C   PHE B  16     -89.644  21.420  13.367  1.00 36.14           C
ANISOU 2924  C   PHE B  16     4212   3429   6090   -266    661    442       C
ATOM   2925  O   PHE B  16     -88.873  20.676  13.983  1.00 38.80           O
ANISOU 2925  O   PHE B  16     4653   3711   6379   -208    710    562       O
ATOM   2926  CB  PHE B  16     -88.110  22.273  11.575  1.00 22.57           C
ANISOU 2926  CB  PHE B  16     2602   1664   4309    -94    510    244       C
ATOM   2927  CG  PHE B  16     -88.702  21.446  10.469  1.00 31.46           C
ANISOU 2927  CG  PHE B  16     3821   2606   5527   -201    450    175       C
ATOM   2928  CD1 PHE B  16     -89.408  22.048   9.440  1.00 31.10           C
ANISOU 2928  CD1 PHE B  16     3716   2593   5506   -275    342     62       C
ATOM   2929  CD2 PHE B  16     -88.564  20.068  10.463  1.00 28.58           C
ANISOU 2929  CD2 PHE B  16     3623   2021   5214   -236    487    227       C
ATOM   2930  CE1 PHE B  16     -89.961  21.292   8.423  1.00 30.59           C
ANISOU 2930  CE1 PHE B  16     3759   2377   5486   -410    247    -16       C
ATOM   2931  CE2 PHE B  16     -89.114  19.306   9.449  1.00 32.60           C
ANISOU 2931  CE2 PHE B  16     4273   2328   5787   -369    410    127       C
ATOM   2932  CZ  PHE B  16     -89.813  19.919   8.427  1.00 35.15           C
ANISOU 2932  CZ  PHE B  16     4536   2716   6102   -471    277     -2       C
ATOM   2933  N   ASP B  17     -90.957  21.201  13.287  1.00 36.66           N
ANISOU 2933  N   ASP B  17     4164   3494   6272   -423    672    466       N
ATOM   2934  CA  ASP B  17     -91.602  20.071  13.944  1.00 36.11           C
ANISOU 2934  CA  ASP B  17     4089   3344   6286   -569    754    634       C
ATOM   2935  C   ASP B  17     -92.314  19.161  12.951  1.00 39.33           C
ANISOU 2935  C   ASP B  17     4538   3540   6865   -784    646    609       C
ATOM   2936  O   ASP B  17     -93.096  18.296  13.365  1.00 45.12           O
ANISOU 2936  O   ASP B  17     5231   4198   7714   -974    689    754       O
ATOM   2937  CB  ASP B  17     -92.585  20.574  15.008  1.00 45.68           C
ANISOU 2937  CB  ASP B  17     5094   4785   7477   -596    895    741       C
ATOM   2938  CG  ASP B  17     -92.931  19.514  16.038  1.00 57.26           C
ANISOU 2938  CG  ASP B  17     6567   6226   8964   -702   1028    974       C
ATOM   2939  OD1 ASP B  17     -92.010  19.028  16.726  1.00 60.04           O
ANISOU 2939  OD1 ASP B  17     7076   6534   9202   -612   1074   1073       O
ATOM   2940  OD2 ASP B  17     -94.126  19.173  16.162  1.00 62.03           O
ANISOU 2940  OD2 ASP B  17     6997   6868   9702   -879   1084   1092       O
ATOM   2941  N   GLY B  18     -92.066  19.329  11.654  1.00 36.28           N
ANISOU 2941  N   GLY B  18     4244   3058   6482   -780    501    433       N
ATOM   2942  CA  GLY B  18     -92.695  18.492  10.654  1.00 35.54           C
ANISOU 2942  CA  GLY B  18     4243   2760   6500  -1005    363    369       C
ATOM   2943  C   GLY B  18     -94.163  18.759  10.416  1.00 39.69           C
ANISOU 2943  C   GLY B  18     4506   3424   7151  -1236    269    408       C
ATOM   2944  O   GLY B  18     -94.830  17.937   9.782  1.00 47.16           O
ANISOU 2944  O   GLY B  18     5510   4219   8191  -1495    130    391       O
ATOM   2945  N   GLN B  19     -94.690  19.878  10.904  1.00 38.67           N
ANISOU 2945  N   GLN B  19     4096   3581   7017  -1143    336    463       N
ATOM   2946  CA  GLN B  19     -96.090  20.204  10.698  1.00 33.63           C
ANISOU 2946  CA  GLN B  19     3144   3117   6516  -1310    269    543       C
ATOM   2947  C   GLN B  19     -96.302  20.799   9.309  1.00 39.01           C
ANISOU 2947  C   GLN B  19     3801   3837   7185  -1333     44    402       C
ATOM   2948  O   GLN B  19     -95.389  21.359   8.697  1.00 38.81           O
ANISOU 2948  O   GLN B  19     3946   3777   7023  -1153      2    253       O
ATOM   2949  CB  GLN B  19     -96.577  21.184  11.766  1.00 37.48           C
ANISOU 2949  CB  GLN B  19     3360   3883   6998  -1142    471    659       C
ATOM   2950  CG  GLN B  19     -96.235  20.772  13.190  1.00 42.79           C
ANISOU 2950  CG  GLN B  19     4090   4568   7599  -1075    702    790       C
ATOM   2951  CD  GLN B  19     -96.915  19.483  13.609  1.00 51.94           C
ANISOU 2951  CD  GLN B  19     5200   5634   8899  -1349    738    992       C
ATOM   2952  OE1 GLN B  19     -97.991  19.145  13.116  1.00 56.73           O
ANISOU 2952  OE1 GLN B  19     5657   6301   9597  -1552    614   1037       O
ATOM   2953  NE2 GLN B  19     -96.286  18.754  14.523  1.00 55.72           N
ANISOU 2953  NE2 GLN B  19     5858   6008   9303  -1321    871   1098       N
ATOM   2954  N   GLN B  20     -97.527  20.667   8.811  1.00 41.55           N
ANISOU 2954  N   GLN B  20     3886   4254   7646  -1571   -109    481       N
ATOM   2955  CA  GLN B  20     -97.890  21.219   7.516  1.00 47.83           C
ANISOU 2955  CA  GLN B  20     4619   5134   8418  -1618   -352    393       C
ATOM   2956  C   GLN B  20     -98.486  22.613   7.674  1.00 45.96           C
ANISOU 2956  C   GLN B  20     4041   5192   8231  -1411   -295    488       C
ATOM   2957  O   GLN B  20     -99.170  22.912   8.655  1.00 44.98           O
ANISOU 2957  O   GLN B  20     3650   5239   8201  -1340   -111    648       O
ATOM   2958  CB  GLN B  20     -98.884  20.312   6.790  1.00 56.13           C
ANISOU 2958  CB  GLN B  20     5674   6191   9462  -1940   -574    403       C
ATOM   2959  CG  GLN B  20     -98.247  19.134   6.077  1.00 67.57           C
ANISOU 2959  CG  GLN B  20     7559   7321  10793  -2106   -692    216       C
ATOM   2960  CD  GLN B  20     -99.206  18.445   5.128  1.00 87.16           C
ANISOU 2960  CD  GLN B  20    10059   9815  13241  -2425   -941    167       C
ATOM   2961  OE1 GLN B  20    -100.415  18.676   5.173  1.00 95.64           O
ANISOU 2961  OE1 GLN B  20    10787  11141  14411  -2550  -1019    317       O
ATOM   2962  NE2 GLN B  20     -98.670  17.599   4.256  1.00 92.62           N
ANISOU 2962  NE2 GLN B  20    11158  10237  13795  -2535  -1054    -51       N
ATOM   2963  N   GLY B  21     -98.223  23.457   6.692  1.00 44.12           N
ANISOU 2963  N   GLY B  21     3849   5009   7905  -1285   -433    394       N
ATOM   2964  CA  GLY B  21     -98.692  24.830   6.687  1.00 44.90           C
ANISOU 2964  CA  GLY B  21     3681   5326   8055  -1057   -392    478       C
ATOM   2965  C   GLY B  21     -97.647  25.746   6.079  1.00 39.35           C
ANISOU 2965  C   GLY B  21     3202   4558   7190   -826   -410    340       C
ATOM   2966  O   GLY B  21     -96.458  25.435   6.026  1.00 35.40           O
ANISOU 2966  O   GLY B  21     3019   3888   6544   -781   -368    201       O
ATOM   2967  N   GLU B  22     -98.106  26.901   5.604  1.00 40.81           N
ANISOU 2967  N   GLU B  22     3198   4889   7417   -671   -469    414       N
ATOM   2968  CA  GLU B  22     -97.228  27.885   4.989  1.00 40.32           C
ANISOU 2968  CA  GLU B  22     3316   4774   7231   -470   -490    333       C
ATOM   2969  C   GLU B  22     -97.578  29.272   5.505  1.00 40.76           C
ANISOU 2969  C   GLU B  22     3187   4907   7392   -191   -344    424       C
ATOM   2970  O   GLU B  22     -98.737  29.566   5.805  1.00 46.42           O
ANISOU 2970  O   GLU B  22     3580   5780   8277   -143   -308    579       O
ATOM   2971  CB  GLU B  22     -97.327  27.867   3.455  1.00 47.27           C
ANISOU 2971  CB  GLU B  22     4253   5699   8008   -583   -778    326       C
ATOM   2972  CG  GLU B  22     -96.700  26.655   2.786  1.00 52.50           C
ANISOU 2972  CG  GLU B  22     5228   6223   8498   -797   -899    169       C
ATOM   2973  CD  GLU B  22     -97.618  25.450   2.770  1.00 65.55           C
ANISOU 2973  CD  GLU B  22     6796   7880  10230  -1115  -1042    190       C
ATOM   2974  OE1 GLU B  22     -98.802  25.596   3.138  1.00 72.24           O
ANISOU 2974  OE1 GLU B  22     7280   8899  11269  -1189  -1078    363       O
ATOM   2975  OE2 GLU B  22     -97.155  24.355   2.387  1.00 69.31           O
ANISOU 2975  OE2 GLU B  22     7568   8179  10588  -1291  -1111     43       O
ATOM   2976  N   VAL B  23     -96.559  30.120   5.608  1.00 35.38           N
ANISOU 2976  N   VAL B  23     2715   4106   6620     -7   -252    335       N
ATOM   2977  CA  VAL B  23     -96.740  31.527   5.959  1.00 35.92           C
ANISOU 2977  CA  VAL B  23     2707   4166   6773    259   -129    385       C
ATOM   2978  C   VAL B  23     -95.950  32.369   4.963  1.00 38.38           C
ANISOU 2978  C   VAL B  23     3192   4390   7000    334   -246    371       C
ATOM   2979  O   VAL B  23     -94.913  31.915   4.457  1.00 37.15           O
ANISOU 2979  O   VAL B  23     3263   4163   6688    226   -316    280       O
ATOM   2980  CB  VAL B  23     -96.307  31.811   7.407  1.00 32.33           C
ANISOU 2980  CB  VAL B  23     2360   3624   6300    387    135    291       C
ATOM   2981  CG1 VAL B  23     -97.213  31.086   8.390  1.00 34.86           C
ANISOU 2981  CG1 VAL B  23     2480   4068   6699    340    283    356       C
ATOM   2982  CG2 VAL B  23     -94.862  31.410   7.620  1.00 30.48           C
ANISOU 2982  CG2 VAL B  23     2430   3256   5894    304    143    147       C
ATOM   2983  N   PRO B  24     -96.396  33.584   4.645  1.00 42.19           N
ANISOU 2983  N   PRO B  24     3573   4871   7586    531   -252    482       N
ATOM   2984  CA  PRO B  24     -95.669  34.398   3.663  1.00 40.46           C
ANISOU 2984  CA  PRO B  24     3515   4566   7293    585   -362    513       C
ATOM   2985  C   PRO B  24     -94.314  34.838   4.196  1.00 35.15           C
ANISOU 2985  C   PRO B  24     3122   3697   6534    612   -236    379       C
ATOM   2986  O   PRO B  24     -94.174  35.210   5.364  1.00 35.02           O
ANISOU 2986  O   PRO B  24     3163   3579   6565    702    -57    290       O
ATOM   2987  CB  PRO B  24     -96.602  35.591   3.432  1.00 43.37           C
ANISOU 2987  CB  PRO B  24     3690   4950   7839    818   -363    694       C
ATOM   2988  CG  PRO B  24     -97.414  35.680   4.681  1.00 44.58           C
ANISOU 2988  CG  PRO B  24     3696   5124   8118    949   -142    677       C
ATOM   2989  CD  PRO B  24     -97.605  34.264   5.143  1.00 44.47           C
ANISOU 2989  CD  PRO B  24     3586   5237   8075    734   -142    614       C
ATOM   2990  N   VAL B  25     -93.310  34.795   3.322  1.00 30.30           N
ANISOU 2990  N   VAL B  25     2679   3055   5780    525   -335    374       N
ATOM   2991  CA  VAL B  25     -91.921  35.037   3.696  1.00 29.35           C
ANISOU 2991  CA  VAL B  25     2775   2800   5575    496   -252    284       C
ATOM   2992  C   VAL B  25     -91.317  36.064   2.749  1.00 31.96           C
ANISOU 2992  C   VAL B  25     3198   3060   5887    537   -321    401       C
ATOM   2993  O   VAL B  25     -91.550  36.018   1.536  1.00 32.43           O
ANISOU 2993  O   VAL B  25     3224   3223   5876    521   -456    518       O
ATOM   2994  CB  VAL B  25     -91.097  33.731   3.673  1.00 31.13           C
ANISOU 2994  CB  VAL B  25     3101   3083   5646    343   -254    188       C
ATOM   2995  CG1 VAL B  25     -89.624  34.017   3.921  1.00 28.47           C
ANISOU 2995  CG1 VAL B  25     2922   2662   5234    319   -190    156       C
ATOM   2996  CG2 VAL B  25     -91.631  32.749   4.702  1.00 27.93           C
ANISOU 2996  CG2 VAL B  25     2626   2713   5273    292   -174    104       C
ATOM   2997  N   SER B  26     -90.544  36.993   3.308  1.00 33.86           N
ANISOU 2997  N   SER B  26     3566   3123   6176    567   -240    377       N
ATOM   2998  CA  SER B  26     -89.770  37.958   2.539  1.00 32.24           C
ANISOU 2998  CA  SER B  26     3463   2819   5966    559   -287    504       C
ATOM   2999  C   SER B  26     -88.294  37.782   2.861  1.00 30.85           C
ANISOU 2999  C   SER B  26     3408   2614   5699    417   -244    449       C
ATOM   3000  O   SER B  26     -87.911  37.752   4.035  1.00 31.22           O
ANISOU 3000  O   SER B  26     3512   2584   5766    375   -172    316       O
ATOM   3001  CB  SER B  26     -90.204  39.393   2.842  1.00 33.28           C
ANISOU 3001  CB  SER B  26     3640   2721   6283    703   -250    565       C
ATOM   3002  OG  SER B  26     -91.481  39.666   2.298  1.00 46.35           O
ANISOU 3002  OG  SER B  26     5142   4432   8037    867   -302    697       O
ATOM   3003  N   ILE B  27     -87.471  37.669   1.823  1.00 29.32           N
ANISOU 3003  N   ILE B  27     3240   2509   5392    348   -286    570       N
ATOM   3004  CA  ILE B  27     -86.025  37.552   1.962  1.00 25.18           C
ANISOU 3004  CA  ILE B  27     2767   2003   4799    228   -240    586       C
ATOM   3005  C   ILE B  27     -85.390  38.847   1.482  1.00 31.79           C
ANISOU 3005  C   ILE B  27     3658   2711   5711    177   -264    763       C
ATOM   3006  O   ILE B  27     -85.630  39.281   0.348  1.00 35.28           O
ANISOU 3006  O   ILE B  27     4098   3184   6125    224   -308    937       O
ATOM   3007  CB  ILE B  27     -85.474  36.351   1.174  1.00 29.26           C
ANISOU 3007  CB  ILE B  27     3266   2729   5125    209   -217    602       C
ATOM   3008  CG1 ILE B  27     -86.070  35.046   1.701  1.00 35.69           C
ANISOU 3008  CG1 ILE B  27     4060   3609   5891    229   -199    430       C
ATOM   3009  CG2 ILE B  27     -83.957  36.321   1.252  1.00 22.86           C
ANISOU 3009  CG2 ILE B  27     2449   1968   4269    123   -148    678       C
ATOM   3010  CD1 ILE B  27     -85.771  34.787   3.155  1.00 38.60           C
ANISOU 3010  CD1 ILE B  27     4422   3918   6326    191   -137    312       C
ATOM   3011  N   ILE B  28     -84.581  39.463   2.341  1.00 25.36           N
ANISOU 3011  N   ILE B  28     2900   1753   4982     58   -252    734       N
ATOM   3012  CA  ILE B  28     -83.863  40.680   1.986  1.00 36.57           C
ANISOU 3012  CA  ILE B  28     4381   3017   6499    -53   -285    909       C
ATOM   3013  C   ILE B  28     -82.714  40.844   2.971  1.00 34.12           C
ANISOU 3013  C   ILE B  28     4092   2654   6219   -257   -300    854       C
ATOM   3014  O   ILE B  28     -82.849  40.528   4.157  1.00 33.16           O
ANISOU 3014  O   ILE B  28     4012   2498   6089   -272   -300    648       O
ATOM   3015  CB  ILE B  28     -84.809  41.909   1.969  1.00 39.90           C
ANISOU 3015  CB  ILE B  28     4915   3155   7091     50   -316    940       C
ATOM   3016  CG1 ILE B  28     -84.088  43.149   1.437  1.00 38.60           C
ANISOU 3016  CG1 ILE B  28     4835   2806   7026    -77   -353   1156       C
ATOM   3017  CG2 ILE B  28     -85.397  42.169   3.343  1.00 39.69           C
ANISOU 3017  CG2 ILE B  28     4995   2932   7153    102   -286    694       C
ATOM   3018  CD1 ILE B  28     -84.955  44.386   1.403  1.00 47.55           C
ANISOU 3018  CD1 ILE B  28     6109   3715   8242     49   -353   1152       C
ATOM   3019  N  AASN B  29     -81.559  41.267   2.462  0.50 39.86           N
ANISOU 3019  N  AASN B  29     4765   3418   6960   -425   -318   1061       N
ATOM   3020  N  BASN B  29     -81.613  41.399   2.479  0.50 40.33           N
ANISOU 3020  N  BASN B  29     4842   3447   7037   -427   -324   1062       N
ATOM   3021  CA AASN B  29     -80.400  41.613   3.295  0.50 43.39           C
ANISOU 3021  CA AASN B  29     5199   3824   7462   -675   -381   1068       C
ATOM   3022  CA BASN B  29     -80.311  41.413   3.156  0.50 43.15           C
ANISOU 3022  CA BASN B  29     5133   3856   7406   -662   -366   1091       C
ATOM   3023  C  AASN B  29     -79.999  40.484   4.251  0.50 41.40           C
ANISOU 3023  C  AASN B  29     4857   3773   7100   -687   -372    918       C
ATOM   3024  C  BASN B  29     -79.932  39.944   3.352  0.50 41.16           C
ANISOU 3024  C  BASN B  29     4727   3912   7000   -586   -298   1034       C
ATOM   3025  O  AASN B  29     -79.757  40.706   5.439  0.50 40.01           O
ANISOU 3025  O  AASN B  29     4755   3504   6942   -822   -454    775       O
ATOM   3026  O  BASN B  29     -80.163  39.123   2.451  0.50 38.87           O
ANISOU 3026  O  BASN B  29     4371   3806   6594   -423   -206   1087       O
ATOM   3027  CB AASN B  29     -80.664  42.902   4.078  0.50 50.12           C
ANISOU 3027  CB AASN B  29     6275   4324   8444   -783   -466    948       C
ATOM   3028  CB BASN B  29     -80.374  42.252   4.424  0.50 45.86           C
ANISOU 3028  CB BASN B  29     5658   3913   7856   -807   -465    909       C
ATOM   3029  CG AASN B  29     -81.031  44.067   3.183  0.50 55.02           C
ANISOU 3029  CG AASN B  29     7002   4773   9131   -734   -457   1090       C
ATOM   3030  CG BASN B  29     -80.915  43.650   4.174  0.50 53.33           C
ANISOU 3030  CG BASN B  29     6808   4573   8884   -785   -481    909       C
ATOM   3031  OD1AASN B  29     -82.058  44.717   3.381  0.50 57.15           O
ANISOU 3031  OD1AASN B  29     7443   4828   9442   -581   -436    969       O
ATOM   3032  OD1BASN B  29     -80.508  44.327   3.230  0.50 56.27           O
ANISOU 3032  OD1BASN B  29     7156   4928   9295   -849   -484   1135       O
ATOM   3033  ND2AASN B  29     -80.191  44.340   2.192  0.50 58.59           N
ANISOU 3033  ND2AASN B  29     7341   5334   9587   -850   -454   1371       N
ATOM   3034  ND2BASN B  29     -81.847  44.083   5.017  0.50 53.44           N
ANISOU 3034  ND2BASN B  29     7025   4376   8904   -670   -463    666       N
ATOM   3035  N  AASN B  30     -79.925  39.258   3.722  0.50 36.06           N
ANISOU 3035  N  AASN B  30     4045   3363   6294   -542   -276    953       N
ATOM   3036  N  BASN B  30     -79.359  39.574   4.491  0.50 36.88           N
ANISOU 3036  N  BASN B  30     4150   3423   6441   -696   -346    932       N
ATOM   3037  CA AASN B  30     -79.437  38.091   4.470  0.50 33.27           C
ANISOU 3037  CA AASN B  30     3591   3204   5847   -524   -248    876       C
ATOM   3038  CA BASN B  30     -79.208  38.171   4.859  0.50 32.90           C
ANISOU 3038  CA BASN B  30     3539   3150   5812   -584   -279    862       C
ATOM   3039  C  AASN B  30     -80.230  37.856   5.757  0.50 29.19           C
ANISOU 3039  C  AASN B  30     3195   2582   5316   -493   -284    620       C
ATOM   3040  C  BASN B  30     -80.260  37.766   5.877  0.50 29.14           C
ANISOU 3040  C  BASN B  30     3190   2580   5301   -488   -284    601       C
ATOM   3041  O  AASN B  30     -79.705  37.334   6.744  0.50 28.06           O
ANISOU 3041  O  AASN B  30     3010   2534   5119   -559   -318    568       O
ATOM   3042  O  BASN B  30     -79.963  37.021   6.815  0.50 27.78           O
ANISOU 3042  O  BASN B  30     2981   2514   5059   -503   -292    526       O
ATOM   3043  CB AASN B  30     -77.940  38.217   4.775  0.50 37.18           C
ANISOU 3043  CB AASN B  30     3920   3839   6370   -724   -299   1053       C
ATOM   3044  CB BASN B  30     -77.805  37.910   5.401  0.50 37.07           C
ANISOU 3044  CB BASN B  30     3892   3860   6334   -746   -327    992       C
ATOM   3045  CG AASN B  30     -77.185  36.919   4.550  0.50 36.92           C
ANISOU 3045  CG AASN B  30     3692   4099   6238   -601   -186   1158       C
ATOM   3046  CG BASN B  30     -77.024  36.919   4.560  0.50 37.17           C
ANISOU 3046  CG BASN B  30     3698   4151   6272   -616   -188   1183       C
ATOM   3047  OD1AASN B  30     -77.680  36.004   3.891  0.50 34.81           O
ANISOU 3047  OD1AASN B  30     3451   3903   5874   -382    -58   1112       O
ATOM   3048  OD1BASN B  30     -77.600  36.046   3.910  0.50 35.40           O
ANISOU 3048  OD1BASN B  30     3515   3982   5953   -395    -63   1124       O
ATOM   3049  ND2AASN B  30     -75.975  36.837   5.092  0.50 39.95           N
ANISOU 3049  ND2AASN B  30     3885   4645   6650   -743   -240   1306       N
ATOM   3050  ND2BASN B  30     -75.702  37.047   4.573  0.50 40.79           N
ANISOU 3050  ND2BASN B  30     3937   4787   6773   -756   -207   1416       N
ATOM   3051  N   THR B  31     -81.499  38.245   5.740  1.00 29.63           N
ANISOU 3051  N   THR B  31     3382   2463   5411   -379   -269    490       N
ATOM   3052  CA  THR B  31     -82.453  38.080   6.825  1.00 28.05           C
ANISOU 3052  CA  THR B  31     3288   2175   5195   -304   -251    268       C
ATOM   3053  C   THR B  31     -83.752  37.502   6.284  1.00 28.14           C
ANISOU 3053  C   THR B  31     3272   2217   5202   -103   -175    223       C
ATOM   3054  O   THR B  31     -84.155  37.802   5.157  1.00 30.29           O
ANISOU 3054  O   THR B  31     3520   2474   5513    -32   -180    330       O
ATOM   3055  CB  THR B  31     -82.716  39.423   7.527  1.00 30.83           C
ANISOU 3055  CB  THR B  31     3834   2248   5634   -376   -304    158       C
ATOM   3056  OG1 THR B  31     -81.467  40.024   7.892  1.00 33.63           O
ANISOU 3056  OG1 THR B  31     4215   2563   5999   -630   -421    217       O
ATOM   3057  CG2 THR B  31     -83.555  39.227   8.782  1.00 30.68           C
ANISOU 3057  CG2 THR B  31     3931   2174   5551   -288   -247    -73       C
ATOM   3058  N   VAL B  32     -84.394  36.658   7.089  1.00 27.18           N
ANISOU 3058  N   VAL B  32     3144   2157   5026    -32   -121     89       N
ATOM   3059  CA  VAL B  32     -85.684  36.067   6.756  1.00 27.00           C
ANISOU 3059  CA  VAL B  32     3068   2173   5018    110    -69     51       C
ATOM   3060  C   VAL B  32     -86.763  36.797   7.541  1.00 29.11           C
ANISOU 3060  C   VAL B  32     3397   2300   5363    205    -17    -62       C
ATOM   3061  O   VAL B  32     -86.681  36.908   8.771  1.00 26.90           O
ANISOU 3061  O   VAL B  32     3208   1977   5037    181     27   -187       O
ATOM   3062  CB  VAL B  32     -85.707  34.560   7.065  1.00 29.56           C
ANISOU 3062  CB  VAL B  32     3329   2651   5250    117    -23     14       C
ATOM   3063  CG1 VAL B  32     -87.014  33.944   6.589  1.00 30.92           C
ANISOU 3063  CG1 VAL B  32     3433   2864   5452    199     -5     -3       C
ATOM   3064  CG2 VAL B  32     -84.516  33.865   6.429  1.00 27.59           C
ANISOU 3064  CG2 VAL B  32     3044   2516   4923     72    -32    115       C
ATOM   3065  N   TYR B  33     -87.774  37.296   6.834  1.00 28.37           N
ANISOU 3065  N   TYR B  33     3256   2151   5373    331    -16     -6       N
ATOM   3066  CA  TYR B  33     -88.897  37.985   7.448  1.00 24.34           C
ANISOU 3066  CA  TYR B  33     2766   1519   4962    488     70    -77       C
ATOM   3067  C   TYR B  33     -90.190  37.236   7.160  1.00 26.15           C
ANISOU 3067  C   TYR B  33     2798   1904   5233    598    103    -32       C
ATOM   3068  O   TYR B  33     -90.282  36.446   6.217  1.00 24.29           O
ANISOU 3068  O   TYR B  33     2451   1816   4964    542     16     57       O
ATOM   3069  CB  TYR B  33     -89.026  39.426   6.938  1.00 26.28           C
ANISOU 3069  CB  TYR B  33     3105   1536   5344    572     45     -5       C
ATOM   3070  CG  TYR B  33     -87.835  40.306   7.231  1.00 27.10           C
ANISOU 3070  CG  TYR B  33     3412   1446   5437    420     -6    -38       C
ATOM   3071  CD1 TYR B  33     -86.753  40.350   6.364  1.00 31.88           C
ANISOU 3071  CD1 TYR B  33     3999   2090   6023    258   -112    109       C
ATOM   3072  CD2 TYR B  33     -87.798  41.103   8.367  1.00 28.91           C
ANISOU 3072  CD2 TYR B  33     3860   1494   5632    420     51   -208       C
ATOM   3073  CE1 TYR B  33     -85.664  41.157   6.624  1.00 36.42           C
ANISOU 3073  CE1 TYR B  33     4718   2502   6618     74   -176    115       C
ATOM   3074  CE2 TYR B  33     -86.713  41.915   8.635  1.00 49.12           C
ANISOU 3074  CE2 TYR B  33     6615   3876   8172    225    -35   -240       C
ATOM   3075  CZ  TYR B  33     -85.648  41.938   7.759  1.00 43.82           C
ANISOU 3075  CZ  TYR B  33     5873   3241   7537     38   -157    -65       C
ATOM   3076  OH  TYR B  33     -84.562  42.744   8.018  1.00 42.56           O
ANISOU 3076  OH  TYR B  33     5866   2937   7369   -196   -254    -64       O
ATOM   3077  N   THR B  34     -91.196  37.500   7.989  1.00 26.90           N
ANISOU 3077  N   THR B  34     2856   1969   5397    748    233    -94       N
ATOM   3078  CA  THR B  34     -92.542  37.006   7.752  1.00 33.70           C
ANISOU 3078  CA  THR B  34     3476   2982   6347    853    266     -8       C
ATOM   3079  C   THR B  34     -93.531  38.093   8.142  1.00 31.14           C
ANISOU 3079  C   THR B  34     3140   2577   6114   1081    391      6       C
ATOM   3080  O   THR B  34     -93.248  38.935   8.998  1.00 30.84           O
ANISOU 3080  O   THR B  34     3322   2375   6020   1149    497   -121       O
ATOM   3081  CB  THR B  34     -92.833  35.711   8.530  1.00 39.51           C
ANISOU 3081  CB  THR B  34     4120   3889   7005    767    340    -62       C
ATOM   3082  OG1 THR B  34     -94.045  35.123   8.043  1.00 37.26           O
ANISOU 3082  OG1 THR B  34     3567   3770   6819    789    312     62       O
ATOM   3083  CG2 THR B  34     -92.979  35.993  10.019  1.00 42.06           C
ANISOU 3083  CG2 THR B  34     4542   4161   7276    860    541   -192       C
ATOM   3084  N   LYS B  35     -94.691  38.077   7.493  1.00 33.96           N
ANISOU 3084  N   LYS B  35     3261   3074   6571   1184    360    165       N
ATOM   3085  CA  LYS B  35     -95.706  39.096   7.712  1.00 38.10           C
ANISOU 3085  CA  LYS B  35     3752   3570   7154   1419    469    220       C
ATOM   3086  C   LYS B  35     -96.622  38.653   8.846  1.00 43.01           C
ANISOU 3086  C   LYS B  35     4246   4328   7769   1520    671    173       C
ATOM   3087  O   LYS B  35     -97.241  37.586   8.772  1.00 45.55           O
ANISOU 3087  O   LYS B  35     4306   4871   8132   1434    653    262       O
ATOM   3088  CB  LYS B  35     -96.501  39.352   6.431  1.00 45.16           C
ANISOU 3088  CB  LYS B  35     4433   4577   8150   1483    321    449       C
ATOM   3089  CG  LYS B  35     -96.909  40.806   6.247  1.00 53.36           C
ANISOU 3089  CG  LYS B  35     5567   5462   9246   1712    367    516       C
ATOM   3090  CD  LYS B  35     -97.266  41.130   4.800  1.00 59.86           C
ANISOU 3090  CD  LYS B  35     6249   6362  10134   1732    172    754       C
ATOM   3091  CE  LYS B  35     -98.653  40.631   4.430  1.00 67.22           C
ANISOU 3091  CE  LYS B  35     6814   7583  11142   1794    119    931       C
ATOM   3092  NZ  LYS B  35     -99.075  41.123   3.088  1.00 69.43           N
ANISOU 3092  NZ  LYS B  35     6976   7943  11462   1842    -77   1171       N
ATOM   3093  N   VAL B  36     -96.695  39.462   9.894  1.00 48.23           N
ANISOU 3093  N   VAL B  36     5104   4854   8367   1687    858     35       N
ATOM   3094  CA  VAL B  36     -97.570  39.205  11.035  1.00 50.63           C
ANISOU 3094  CA  VAL B  36     5314   5289   8634   1823   1089     -8       C
ATOM   3095  C   VAL B  36     -98.516  40.396  11.129  1.00 59.02           C
ANISOU 3095  C   VAL B  36     6373   6290   9763   2119   1203     29       C
ATOM   3096  O   VAL B  36     -98.188  41.427  11.725  1.00 63.93           O
ANISOU 3096  O   VAL B  36     7298   6673  10319   2255   1294   -137       O
ATOM   3097  CB  VAL B  36     -96.795  38.997  12.337  1.00 45.53           C
ANISOU 3097  CB  VAL B  36     4931   4557   7811   1771   1231   -235       C
ATOM   3098  CG1 VAL B  36     -97.756  38.721  13.481  1.00 47.90           C
ANISOU 3098  CG1 VAL B  36     5127   5027   8047   1922   1490   -252       C
ATOM   3099  CG2 VAL B  36     -95.807  37.858  12.184  1.00 34.75           C
ANISOU 3099  CG2 VAL B  36     3562   3235   6406   1498   1110   -257       C
ATOM   3100  N   ASP B  37     -99.700  40.256  10.530  1.00 63.53           N
ANISOU 3100  N   ASP B  37     6600   7068  10472   2211   1182    247       N
ATOM   3101  CA  ASP B  37    -100.725  41.301  10.531  1.00 68.39           C
ANISOU 3101  CA  ASP B  37     7140   7657  11187   2512   1290    326       C
ATOM   3102  C   ASP B  37    -100.191  42.603   9.936  1.00 63.14           C
ANISOU 3102  C   ASP B  37     6744   6688  10560   2616   1196    294       C
ATOM   3103  O   ASP B  37    -100.251  43.668  10.554  1.00 66.98           O
ANISOU 3103  O   ASP B  37     7463   6947  11038   2831   1336    163       O
ATOM   3104  CB  ASP B  37    -101.284  41.528  11.938  1.00 81.33           C
ANISOU 3104  CB  ASP B  37     8838   9310  12754   2716   1593    193       C
ATOM   3105  CG  ASP B  37    -102.261  40.446  12.359  1.00 92.05           C
ANISOU 3105  CG  ASP B  37     9829  11011  14134   2676   1709    333       C
ATOM   3106  OD1 ASP B  37    -103.104  40.046  11.528  1.00 95.92           O
ANISOU 3106  OD1 ASP B  37     9955  11719  14771   2634   1589    578       O
ATOM   3107  OD2 ASP B  37    -102.183  39.993  13.520  1.00 94.95           O
ANISOU 3107  OD2 ASP B  37    10277  11436  14364   2666   1907    208       O
ATOM   3108  N   GLY B  38     -99.654  42.509   8.719  1.00 58.11           N
ANISOU 3108  N   GLY B  38     6084   6035   9962   2453    954    418       N
ATOM   3109  CA  GLY B  38     -99.295  43.660   7.927  1.00 66.10           C
ANISOU 3109  CA  GLY B  38     7276   6808  11032   2533    845    475       C
ATOM   3110  C   GLY B  38     -97.812  43.976   7.876  1.00 69.11           C
ANISOU 3110  C   GLY B  38     8020   6922  11318   2345    753    329       C
ATOM   3111  O   GLY B  38     -97.326  44.427   6.833  1.00 72.48           O
ANISOU 3111  O   GLY B  38     8507   7251  11784   2277    590    454       O
ATOM   3112  N   VAL B  39     -97.082  43.760   8.968  1.00 49.82           N
ANISOU 3112  N   VAL B  39     5586   6061   7282   1355    524    700       N
ATOM   3113  CA  VAL B  39     -95.690  44.185   9.063  1.00 41.25           C
ANISOU 3113  CA  VAL B  39     4681   4868   6125   1299    459    602       C
ATOM   3114  C   VAL B  39     -94.775  42.969   9.040  1.00 35.28           C
ANISOU 3114  C   VAL B  39     3899   4116   5391   1144    418    558       C
ATOM   3115  O   VAL B  39     -95.161  41.859   9.424  1.00 31.98           O
ANISOU 3115  O   VAL B  39     3374   3760   5017   1112    464    591       O
ATOM   3116  CB  VAL B  39     -95.437  45.031  10.328  1.00 41.56           C
ANISOU 3116  CB  VAL B  39     4908   4818   6065   1435    515    570       C
ATOM   3117  CG1 VAL B  39     -96.175  46.357  10.232  1.00 46.22           C
ANISOU 3117  CG1 VAL B  39     5555   5380   6625   1590    540    601       C
ATOM   3118  CG2 VAL B  39     -95.862  44.266  11.571  1.00 38.45           C
ANISOU 3118  CG2 VAL B  39     4491   4466   5654   1500    625    602       C
ATOM   3119  N   ASP B  40     -93.544  43.193   8.585  1.00 34.60           N
ANISOU 3119  N   ASP B  40     3909   3960   5278   1052    333    490       N
ATOM   3120  CA  ASP B  40     -92.542  42.140   8.529  1.00 34.39           C
ANISOU 3120  CA  ASP B  40     3872   3928   5266    916    294    446       C
ATOM   3121  C   ASP B  40     -91.851  42.005   9.880  1.00 34.80           C
ANISOU 3121  C   ASP B  40     4043   3917   5262    940    328    409       C
ATOM   3122  O   ASP B  40     -91.423  43.002  10.471  1.00 33.00           O
ANISOU 3122  O   ASP B  40     3968   3602   4968   1008    317    379       O
ATOM   3123  CB  ASP B  40     -91.515  42.438   7.438  1.00 36.45           C
ANISOU 3123  CB  ASP B  40     4172   4151   5528    817    200    408       C
ATOM   3124  CG  ASP B  40     -92.135  42.510   6.059  1.00 44.56           C
ANISOU 3124  CG  ASP B  40     5096   5241   6595    792    158    441       C
ATOM   3125  OD1 ASP B  40     -93.087  41.746   5.795  1.00 48.39           O
ANISOU 3125  OD1 ASP B  40     5446   5807   7131    784    176    480       O
ATOM   3126  OD2 ASP B  40     -91.673  43.331   5.239  1.00 49.33           O
ANISOU 3126  OD2 ASP B  40     5753   5810   7180    777    102    434       O
ATOM   3127  N   VAL B  41     -91.749  40.772  10.367  1.00 31.48           N
ANISOU 3127  N   VAL B  41     3560   3534   4868    884    359    412       N
ATOM   3128  CA  VAL B  41     -91.063  40.463  11.614  1.00 28.86           C
ANISOU 3128  CA  VAL B  41     3330   3151   4483    895    385    381       C
ATOM   3129  C   VAL B  41     -89.867  39.585  11.283  1.00 29.02           C
ANISOU 3129  C   VAL B  41     3340   3154   4531    751    320    338       C
ATOM   3130  O   VAL B  41     -90.008  38.577  10.582  1.00 25.63           O
ANISOU 3130  O   VAL B  41     2787   2785   4168    665    310    352       O
ATOM   3131  CB  VAL B  41     -91.995  39.764  12.621  1.00 29.92           C
ANISOU 3131  CB  VAL B  41     3403   3345   4619    971    493    436       C
ATOM   3132  CG1 VAL B  41     -91.279  39.541  13.944  1.00 25.58           C
ANISOU 3132  CG1 VAL B  41     2983   2738   3996    997    517    403       C
ATOM   3133  CG2 VAL B  41     -93.259  40.579  12.824  1.00 26.71           C
ANISOU 3133  CG2 VAL B  41     2980   2973   4197   1123    571    495       C
ATOM   3134  N   GLU B  42     -88.693  39.975  11.776  1.00 35.18           N
ANISOU 3134  N   GLU B  42     4254   3848   5264    728    270    291       N
ATOM   3135  CA  GLU B  42     -87.482  39.208  11.519  1.00 32.61           C
ANISOU 3135  CA  GLU B  42     3918   3504   4967    604    214    260       C
ATOM   3136  C   GLU B  42     -87.534  37.870  12.245  1.00 35.54           C
ANISOU 3136  C   GLU B  42     4234   3912   5356    577    263    269       C
ATOM   3137  O   GLU B  42     -87.788  37.815  13.451  1.00 36.65           O
ANISOU 3137  O   GLU B  42     4436   4040   5450    650    315    277       O
ATOM   3138  CB  GLU B  42     -86.249  39.993  11.959  1.00 34.66           C
ANISOU 3138  CB  GLU B  42     4325   3661   5185    587    141    223       C
ATOM   3139  CG  GLU B  42     -85.003  39.133  12.105  1.00 42.25           C
ANISOU 3139  CG  GLU B  42     5280   4602   6170    482     99    204       C
ATOM   3140  CD  GLU B  42     -83.822  39.897  12.668  1.00 50.29           C
ANISOU 3140  CD  GLU B  42     6434   5516   7157    462     16    181       C
ATOM   3141  OE1 GLU B  42     -83.657  41.084  12.319  1.00 53.95           O
ANISOU 3141  OE1 GLU B  42     6968   5922   7610    478    -38    180       O
ATOM   3142  OE2 GLU B  42     -83.062  39.308  13.467  1.00 52.87           O
ANISOU 3142  OE2 GLU B  42     6797   5814   7476    427     -5    168       O
ATOM   3143  N   LEU B  43     -87.290  36.790  11.506  1.00 35.33           N
ANISOU 3143  N   LEU B  43     4103   3929   5392    478    246    269       N
ATOM   3144  CA  LEU B  43     -87.234  35.453  12.080  1.00 36.03           C
ANISOU 3144  CA  LEU B  43     4138   4041   5509    437    280    278       C
ATOM   3145  C   LEU B  43     -85.825  34.907  12.216  1.00 37.30           C
ANISOU 3145  C   LEU B  43     4343   4156   5672    355    231    242       C
ATOM   3146  O   LEU B  43     -85.577  34.097  13.111  1.00 39.58           O
ANISOU 3146  O   LEU B  43     4642   4438   5958    346    256    246       O
ATOM   3147  CB  LEU B  43     -88.053  34.472  11.234  1.00 37.39           C
ANISOU 3147  CB  LEU B  43     4164   4285   5757    386    291    305       C
ATOM   3148  CG  LEU B  43     -89.556  34.722  11.120  1.00 37.84           C
ANISOU 3148  CG  LEU B  43     4135   4402   5840    454    339    363       C
ATOM   3149  CD1 LEU B  43     -90.201  33.620  10.297  1.00 36.60           C
ANISOU 3149  CD1 LEU B  43     3837   4299   5768    378    319    388       C
ATOM   3150  CD2 LEU B  43     -90.188  34.812  12.499  1.00 39.54           C
ANISOU 3150  CD2 LEU B  43     4376   4626   6022    553    430    408       C
ATOM   3151  N   PHE B  44     -84.897  35.334  11.362  1.00 31.69           N
ANISOU 3151  N   PHE B  44     3654   3418   4969    301    166    218       N
ATOM   3152  CA  PHE B  44     -83.575  34.727  11.321  1.00 28.85           C
ANISOU 3152  CA  PHE B  44     3305   3029   4628    223    126    200       C
ATOM   3153  C   PHE B  44     -82.620  35.658  10.592  1.00 27.70           C
ANISOU 3153  C   PHE B  44     3201   2845   4480    192     63    194       C
ATOM   3154  O   PHE B  44     -82.897  36.072   9.463  1.00 24.69           O
ANISOU 3154  O   PHE B  44     2780   2491   4109    187     54    201       O
ATOM   3155  CB  PHE B  44     -83.636  33.363  10.626  1.00 27.93           C
ANISOU 3155  CB  PHE B  44     3086   2960   4565    161    140    197       C
ATOM   3156  CG  PHE B  44     -82.296  32.715  10.425  1.00 25.34           C
ANISOU 3156  CG  PHE B  44     2761   2609   4260     95    109    183       C
ATOM   3157  CD1 PHE B  44     -81.659  32.073  11.472  1.00 20.29           C
ANISOU 3157  CD1 PHE B  44     2151   1939   3621     82    113    184       C
ATOM   3158  CD2 PHE B  44     -81.685  32.728   9.182  1.00 25.96           C
ANISOU 3158  CD2 PHE B  44     2810   2700   4354     56     82    177       C
ATOM   3159  CE1 PHE B  44     -80.431  31.468  11.287  1.00 20.12           C
ANISOU 3159  CE1 PHE B  44     2120   1898   3626     29     87    180       C
ATOM   3160  CE2 PHE B  44     -80.458  32.124   8.991  1.00 25.70           C
ANISOU 3160  CE2 PHE B  44     2771   2651   4342     10     68    176       C
ATOM   3161  CZ  PHE B  44     -79.829  31.494  10.045  1.00 22.58           C
ANISOU 3161  CZ  PHE B  44     2396   2224   3958     -4     69    178       C
ATOM   3162  N   GLU B  45     -81.506  35.984  11.240  1.00 24.46           N
ANISOU 3162  N   GLU B  45     2866   2370   4059    170     16    192       N
ATOM   3163  CA  GLU B  45     -80.425  36.743  10.627  1.00 28.45           C
ANISOU 3163  CA  GLU B  45     3393   2833   4582    123    -49    206       C
ATOM   3164  C   GLU B  45     -79.285  35.782  10.322  1.00 30.55           C
ANISOU 3164  C   GLU B  45     3601   3112   4895     51    -58    217       C
ATOM   3165  O   GLU B  45     -78.685  35.215  11.241  1.00 32.10           O
ANISOU 3165  O   GLU B  45     3820   3281   5097     33    -71    215       O
ATOM   3166  CB  GLU B  45     -79.952  37.873  11.541  1.00 31.57           C
ANISOU 3166  CB  GLU B  45     3913   3137   4946    143   -115    205       C
ATOM   3167  CG  GLU B  45     -78.816  38.697  10.956  1.00 43.41           C
ANISOU 3167  CG  GLU B  45     5427   4585   6483     83   -193    238       C
ATOM   3168  CD  GLU B  45     -78.253  39.700  11.943  1.00 55.28           C
ANISOU 3168  CD  GLU B  45     7062   5978   7965     86   -285    236       C
ATOM   3169  OE1 GLU B  45     -78.818  39.830  13.049  1.00 60.42           O
ANISOU 3169  OE1 GLU B  45     7810   6595   8553    153   -281    200       O
ATOM   3170  OE2 GLU B  45     -77.241  40.355  11.613  1.00 59.38           O
ANISOU 3170  OE2 GLU B  45     7590   6442   8530     24   -364    274       O
ATOM   3171  N   ASN B  46     -78.993  35.599   9.037  1.00 28.67           N
ANISOU 3171  N   ASN B  46     3293   2915   4684     19    -48    232       N
ATOM   3172  CA  ASN B  46     -77.995  34.624   8.612  1.00 25.72           C
ANISOU 3172  CA  ASN B  46     2861   2562   4349    -29    -39    245       C
ATOM   3173  C   ASN B  46     -76.605  35.102   9.010  1.00 28.74           C
ANISOU 3173  C   ASN B  46     3266   2889   4763    -71    -95    287       C
ATOM   3174  O   ASN B  46     -76.087  36.072   8.448  1.00 32.16           O
ANISOU 3174  O   ASN B  46     3705   3302   5213    -89   -131    328       O
ATOM   3175  CB  ASN B  46     -78.085  34.398   7.106  1.00 23.27           C
ANISOU 3175  CB  ASN B  46     2490   2310   4041    -32    -10    251       C
ATOM   3176  CG  ASN B  46     -77.087  33.371   6.612  1.00 22.38           C
ANISOU 3176  CG  ASN B  46     2327   2219   3955    -60     13    263       C
ATOM   3177  OD1 ASN B  46     -76.598  32.546   7.383  1.00 28.50           O
ANISOU 3177  OD1 ASN B  46     3098   2977   4754    -75     16    258       O
ATOM   3178  ND2 ASN B  46     -76.778  33.418   5.322  1.00 23.01           N
ANISOU 3178  ND2 ASN B  46     2376   2338   4027    -55     33    283       N
ATOM   3179  N   LYS B  47     -75.999  34.423   9.981  1.00 29.76           N
ANISOU 3179  N   LYS B  47     3405   2992   4909    -90   -110    286       N
ATOM   3180  CA  LYS B  47     -74.627  34.687  10.383  1.00 25.26           C
ANISOU 3180  CA  LYS B  47     2840   2373   4384   -139   -174    335       C
ATOM   3181  C   LYS B  47     -73.648  33.687   9.785  1.00 29.23           C
ANISOU 3181  C   LYS B  47     3251   2915   4938   -167   -140    370       C
ATOM   3182  O   LYS B  47     -72.471  33.687  10.158  1.00 31.59           O
ANISOU 3182  O   LYS B  47     3531   3184   5288   -207   -187    421       O
ATOM   3183  CB  LYS B  47     -74.511  34.681  11.910  1.00 26.43           C
ANISOU 3183  CB  LYS B  47     3070   2459   4512   -136   -228    317       C
ATOM   3184  CG  LYS B  47     -75.411  35.685  12.606  1.00 35.01           C
ANISOU 3184  CG  LYS B  47     4268   3499   5534    -88   -256    282       C
ATOM   3185  CD  LYS B  47     -75.087  37.099  12.158  1.00 47.91           C
ANISOU 3185  CD  LYS B  47     5942   5080   7182   -107   -326    312       C
ATOM   3186  CE  LYS B  47     -73.657  37.471  12.514  1.00 59.97           C
ANISOU 3186  CE  LYS B  47     7478   6539   8768   -178   -430    366       C
ATOM   3187  NZ  LYS B  47     -73.183  38.660  11.753  1.00 65.66           N
ANISOU 3187  NZ  LYS B  47     8193   7221   9533   -218   -488    420       N
ATOM   3188  N   THR B  48     -74.104  32.841   8.867  1.00 30.60           N
ANISOU 3188  N   THR B  48     3373   3153   5100   -144    -66    346       N
ATOM   3189  CA  THR B  48     -73.288  31.786   8.289  1.00 27.08           C
ANISOU 3189  CA  THR B  48     2858   2743   4688   -148    -23    367       C
ATOM   3190  C   THR B  48     -72.785  32.188   6.906  1.00 28.67           C
ANISOU 3190  C   THR B  48     3012   2984   4897   -142      8    415       C
ATOM   3191  O   THR B  48     -73.145  33.232   6.358  1.00 32.70           O
ANISOU 3191  O   THR B  48     3539   3497   5388   -139     -6    429       O
ATOM   3192  CB  THR B  48     -74.084  30.480   8.195  1.00 30.51           C
ANISOU 3192  CB  THR B  48     3285   3208   5098   -121     31    306       C
ATOM   3193  OG1 THR B  48     -74.837  30.468   6.976  1.00 28.81           O
ANISOU 3193  OG1 THR B  48     3060   3039   4849    -95     67    278       O
ATOM   3194  CG2 THR B  48     -75.044  30.359   9.368  1.00 29.54           C
ANISOU 3194  CG2 THR B  48     3213   3060   4953   -115     17    264       C
ATOM   3195  N   THR B  49     -71.935  31.333   6.344  1.00 32.79           N
ANISOU 3195  N   THR B  49     3477   3538   5442   -130     56    445       N
ATOM   3196  CA  THR B  49     -71.432  31.505   4.988  1.00 31.50           C
ANISOU 3196  CA  THR B  49     3270   3425   5272   -103    108    494       C
ATOM   3197  C   THR B  49     -72.299  30.806   3.949  1.00 28.98           C
ANISOU 3197  C   THR B  49     2974   3154   4885    -51    164    427       C
ATOM   3198  O   THR B  49     -71.935  30.785   2.769  1.00 24.53           O
ANISOU 3198  O   THR B  49     2392   2636   4294    -12    216    458       O
ATOM   3199  CB  THR B  49     -69.993  30.987   4.885  1.00 35.41           C
ANISOU 3199  CB  THR B  49     3694   3934   5827   -100    139    574       C
ATOM   3200  OG1 THR B  49     -69.968  29.578   5.145  1.00 40.47           O
ANISOU 3200  OG1 THR B  49     4335   4579   6463    -71    176    525       O
ATOM   3201  CG2 THR B  49     -69.102  31.696   5.891  1.00 37.84           C
ANISOU 3201  CG2 THR B  49     3974   4189   6213   -163     61    649       C
ATOM   3202  N   LEU B  50     -73.422  30.235   4.359  1.00 24.24           N
ANISOU 3202  N   LEU B  50     2413   2542   4256    -49    151    344       N
ATOM   3203  CA  LEU B  50     -74.372  29.579   3.478  1.00 26.72           C
ANISOU 3203  CA  LEU B  50     2752   2887   4514    -14    175    278       C
ATOM   3204  C   LEU B  50     -75.410  30.574   2.983  1.00 27.25           C
ANISOU 3204  C   LEU B  50     2842   2970   4541    -11    149    264       C
ATOM   3205  O   LEU B  50     -75.562  31.662   3.547  1.00 28.99           O
ANISOU 3205  O   LEU B  50     3069   3167   4777    -33    115    291       O
ATOM   3206  CB  LEU B  50     -75.059  28.433   4.218  1.00 28.25           C
ANISOU 3206  CB  LEU B  50     2961   3055   4718    -24    165    213       C
ATOM   3207  CG  LEU B  50     -74.167  27.290   4.701  1.00 30.86           C
ANISOU 3207  CG  LEU B  50     3276   3365   5086    -21    189    218       C
ATOM   3208  CD1 LEU B  50     -74.945  26.368   5.622  1.00 33.70           C
ANISOU 3208  CD1 LEU B  50     3651   3691   5464    -41    171    168       C
ATOM   3209  CD2 LEU B  50     -73.606  26.516   3.521  1.00 31.34           C
ANISOU 3209  CD2 LEU B  50     3340   3451   5117     32    239    211       C
ATOM   3210  N   PRO B  51     -76.131  30.241   1.910  1.00 20.94           N
ANISOU 3210  N   PRO B  51     2063   2206   3688     20    159    222       N
ATOM   3211  CA  PRO B  51     -77.261  31.082   1.502  1.00 19.87           C
ANISOU 3211  CA  PRO B  51     1944   2087   3520     24    127    208       C
ATOM   3212  C   PRO B  51     -78.271  31.227   2.630  1.00 26.57           C
ANISOU 3212  C   PRO B  51     2792   2907   4396      0     93    181       C
ATOM   3213  O   PRO B  51     -78.400  30.359   3.496  1.00 26.51           O
ANISOU 3213  O   PRO B  51     2778   2876   4419    -18     94    155       O
ATOM   3214  CB  PRO B  51     -77.851  30.327   0.307  1.00 23.48           C
ANISOU 3214  CB  PRO B  51     2426   2576   3918     57    128    157       C
ATOM   3215  CG  PRO B  51     -76.689  29.591  -0.263  1.00 20.62           C
ANISOU 3215  CG  PRO B  51     2072   2225   3537     90    178    170       C
ATOM   3216  CD  PRO B  51     -75.837  29.195   0.915  1.00 20.29           C
ANISOU 3216  CD  PRO B  51     1996   2147   3564     62    195    194       C
ATOM   3217  N   VAL B  52     -78.996  32.348   2.606  1.00 32.06           N
ANISOU 3217  N   VAL B  52     3497   3607   5079      7     69    195       N
ATOM   3218  CA  VAL B  52     -79.834  32.725   3.743  1.00 34.89           C
ANISOU 3218  CA  VAL B  52     3861   3939   5458      3     52    186       C
ATOM   3219  C   VAL B  52     -80.934  31.693   3.973  1.00 28.05           C
ANISOU 3219  C   VAL B  52     2970   3086   4602      0     51    143       C
ATOM   3220  O   VAL B  52     -81.181  31.268   5.108  1.00 33.01           O
ANISOU 3220  O   VAL B  52     3593   3692   5259     -8     60    138       O
ATOM   3221  CB  VAL B  52     -80.406  34.141   3.538  1.00 37.26           C
ANISOU 3221  CB  VAL B  52     4180   4238   5737     27     31    211       C
ATOM   3222  CG1 VAL B  52     -81.025  34.286   2.152  1.00 29.91           C
ANISOU 3222  CG1 VAL B  52     3239   3357   4769     48     22    206       C
ATOM   3223  CG2 VAL B  52     -81.417  34.476   4.624  1.00 19.44           C
ANISOU 3223  CG2 VAL B  52     1935   1962   3488     47     26    200       C
ATOM   3224  N   ASN B  53     -81.605  31.264   2.901  1.00 25.30           N
ANISOU 3224  N   ASN B  53     2607   2772   4233      6     35    118       N
ATOM   3225  CA  ASN B  53     -82.697  30.308   3.055  1.00 21.77           C
ANISOU 3225  CA  ASN B  53     2129   2331   3813     -9     17     89       C
ATOM   3226  C   ASN B  53     -82.189  28.931   3.459  1.00 24.78           C
ANISOU 3226  C   ASN B  53     2508   2684   4222    -37     28     64       C
ATOM   3227  O   ASN B  53     -82.903  28.181   4.135  1.00 27.78           O
ANISOU 3227  O   ASN B  53     2859   3052   4646    -59     23     58       O
ATOM   3228  CB  ASN B  53     -83.501  30.212   1.759  1.00 22.09           C
ANISOU 3228  CB  ASN B  53     2164   2406   3825     -3    -28     69       C
ATOM   3229  CG  ASN B  53     -82.660  29.749   0.588  1.00 22.42           C
ANISOU 3229  CG  ASN B  53     2250   2454   3815      8    -31     42       C
ATOM   3230  OD1 ASN B  53     -81.563  30.256   0.360  1.00 27.03           O
ANISOU 3230  OD1 ASN B  53     2859   3040   4371     28      5     67       O
ATOM   3231  ND2 ASN B  53     -83.168  28.774  -0.156  1.00 23.67           N
ANISOU 3231  ND2 ASN B  53     2421   2612   3960     -1    -77     -2       N
ATOM   3232  N   VAL B  54     -80.969  28.581   3.055  1.00 23.09           N
ANISOU 3232  N   VAL B  54     2323   2460   3989    -31     47     57       N
ATOM   3233  CA  VAL B  54     -80.407  27.286   3.422  1.00 23.84           C
ANISOU 3233  CA  VAL B  54     2423   2524   4112    -47     60     35       C
ATOM   3234  C   VAL B  54     -80.061  27.259   4.905  1.00 27.51           C
ANISOU 3234  C   VAL B  54     2875   2959   4620    -64     83     62       C
ATOM   3235  O   VAL B  54     -80.475  26.354   5.640  1.00 25.36           O
ANISOU 3235  O   VAL B  54     2587   2663   4385    -85     82     53       O
ATOM   3236  CB  VAL B  54     -79.180  26.970   2.549  1.00 22.52           C
ANISOU 3236  CB  VAL B  54     2287   2360   3910    -18     86     30       C
ATOM   3237  CG1 VAL B  54     -78.533  25.681   3.003  1.00 24.62           C
ANISOU 3237  CG1 VAL B  54     2560   2588   4207    -24    104     13       C
ATOM   3238  CG2 VAL B  54     -79.582  26.885   1.085  1.00 20.38           C
ANISOU 3238  CG2 VAL B  54     2050   2116   3577     10     62     -3       C
ATOM   3239  N   ALA B  55     -79.293  28.251   5.366  1.00 25.51           N
ANISOU 3239  N   ALA B  55     2631   2701   4359    -56     95    100       N
ATOM   3240  CA  ALA B  55     -78.945  28.323   6.780  1.00 23.07           C
ANISOU 3240  CA  ALA B  55     2329   2360   4077    -67    101    123       C
ATOM   3241  C   ALA B  55     -80.185  28.451   7.653  1.00 24.82           C
ANISOU 3241  C   ALA B  55     2545   2581   4305    -62    102    123       C
ATOM   3242  O   ALA B  55     -80.215  27.926   8.772  1.00 26.42           O
ANISOU 3242  O   ALA B  55     2752   2761   4527    -68    115    131       O
ATOM   3243  CB  ALA B  55     -77.994  29.495   7.026  1.00 23.25           C
ANISOU 3243  CB  ALA B  55     2372   2368   4092    -64     90    163       C
ATOM   3244  N   PHE B  56     -81.212  29.144   7.159  1.00 24.66           N
ANISOU 3244  N   PHE B  56     2514   2590   4268    -45     93    122       N
ATOM   3245  CA  PHE B  56     -82.464  29.243   7.898  1.00 22.73           C
ANISOU 3245  CA  PHE B  56     2248   2355   4033    -28    107    135       C
ATOM   3246  C   PHE B  56     -83.087  27.870   8.103  1.00 24.26           C
ANISOU 3246  C   PHE B  56     2396   2550   4274    -57    113    131       C
ATOM   3247  O   PHE B  56     -83.569  27.554   9.197  1.00 26.35           O
ANISOU 3247  O   PHE B  56     2646   2807   4557    -50    142    157       O
ATOM   3248  CB  PHE B  56     -83.425  30.173   7.158  1.00 25.43           C
ANISOU 3248  CB  PHE B  56     2573   2732   4356     -1     93    142       C
ATOM   3249  CG  PHE B  56     -84.812  30.195   7.730  1.00 26.90           C
ANISOU 3249  CG  PHE B  56     2715   2941   4564     23    113    169       C
ATOM   3250  CD1 PHE B  56     -85.039  30.656   9.015  1.00 26.43           C
ANISOU 3250  CD1 PHE B  56     2682   2869   4491     67    154    196       C
ATOM   3251  CD2 PHE B  56     -85.893  29.772   6.975  1.00 28.69           C
ANISOU 3251  CD2 PHE B  56     2875   3204   4824      9     90    174       C
ATOM   3252  CE1 PHE B  56     -86.317  30.686   9.543  1.00 21.93           C
ANISOU 3252  CE1 PHE B  56     2064   2329   3939    104    190    236       C
ATOM   3253  CE2 PHE B  56     -87.174  29.799   7.495  1.00 26.64           C
ANISOU 3253  CE2 PHE B  56     2553   2971   4597     32    114    218       C
ATOM   3254  CZ  PHE B  56     -87.387  30.256   8.782  1.00 21.66           C
ANISOU 3254  CZ  PHE B  56     1940   2336   3953     85    174    254       C
ATOM   3255  N   GLU B  57     -83.071  27.034   7.063  1.00 27.93           N
ANISOU 3255  N   GLU B  57     2844   3016   4753    -86     84    100       N
ATOM   3256  CA  GLU B  57     -83.627  25.692   7.181  1.00 23.10           C
ANISOU 3256  CA  GLU B  57     2196   2387   4193   -124     72     94       C
ATOM   3257  C   GLU B  57     -82.807  24.835   8.136  1.00 24.06           C
ANISOU 3257  C   GLU B  57     2336   2468   4337   -137     98    100       C
ATOM   3258  O   GLU B  57     -83.368  24.086   8.944  1.00 28.44           O
ANISOU 3258  O   GLU B  57     2860   3009   4937   -156    112    126       O
ATOM   3259  CB  GLU B  57     -83.706  25.040   5.801  1.00 26.14           C
ANISOU 3259  CB  GLU B  57     2589   2769   4576   -145     19     49       C
ATOM   3260  CG  GLU B  57     -84.168  23.592   5.820  1.00 32.57           C
ANISOU 3260  CG  GLU B  57     3383   3544   5449   -192    -15     36       C
ATOM   3261  CD  GLU B  57     -84.378  23.033   4.426  1.00 41.15           C
ANISOU 3261  CD  GLU B  57     4498   4617   6520   -207    -87    -17       C
ATOM   3262  OE1 GLU B  57     -84.330  23.818   3.457  1.00 46.67           O
ANISOU 3262  OE1 GLU B  57     5223   5350   7161   -178   -104    -36       O
ATOM   3263  OE2 GLU B  57     -84.593  21.809   4.298  1.00 45.65           O
ANISOU 3263  OE2 GLU B  57     5074   5137   7132   -246   -131    -40       O
ATOM   3264  N   LEU B  58     -81.477  24.934   8.063  1.00 23.47           N
ANISOU 3264  N   LEU B  58     2305   2377   4236   -126    107     86       N
ATOM   3265  CA  LEU B  58     -80.630  24.144   8.950  1.00 23.79           C
ANISOU 3265  CA  LEU B  58     2361   2380   4298   -135    126     96       C
ATOM   3266  C   LEU B  58     -80.805  24.566  10.401  1.00 21.37           C
ANISOU 3266  C   LEU B  58     2062   2070   3988   -122    152    137       C
ATOM   3267  O   LEU B  58     -80.861  23.717  11.298  1.00 22.15           O
ANISOU 3267  O   LEU B  58     2155   2145   4115   -133    169    157       O
ATOM   3268  CB  LEU B  58     -79.168  24.272   8.529  1.00 25.78           C
ANISOU 3268  CB  LEU B  58     2642   2622   4530   -121    128     88       C
ATOM   3269  CG  LEU B  58     -78.849  23.770   7.123  1.00 28.28           C
ANISOU 3269  CG  LEU B  58     2969   2943   4833   -112    118     50       C
ATOM   3270  CD1 LEU B  58     -77.365  23.894   6.834  1.00 30.16           C
ANISOU 3270  CD1 LEU B  58     3220   3180   5058    -87    140     65       C
ATOM   3271  CD2 LEU B  58     -79.309  22.335   6.966  1.00 31.96           C
ANISOU 3271  CD2 LEU B  58     3437   3373   5334   -133    101     18       C
ATOM   3272  N   TRP B  59     -80.889  25.873  10.652  1.00 18.99           N
ANISOU 3272  N   TRP B  59     1784   1786   3646    -92    155    150       N
ATOM   3273  CA  TRP B  59     -81.101  26.344  12.014  1.00 27.29           C
ANISOU 3273  CA  TRP B  59     2867   2828   4673    -62    177    181       C
ATOM   3274  C   TRP B  59     -82.451  25.886  12.549  1.00 28.63           C
ANISOU 3274  C   TRP B  59     2993   3019   4864    -52    215    212       C
ATOM   3275  O   TRP B  59     -82.568  25.507  13.719  1.00 28.10           O
ANISOU 3275  O   TRP B  59     2941   2940   4794    -36    248    245       O
ATOM   3276  CB  TRP B  59     -80.989  27.865  12.064  1.00 24.15           C
ANISOU 3276  CB  TRP B  59     2517   2433   4224    -26    163    182       C
ATOM   3277  CG  TRP B  59     -81.398  28.440  13.375  1.00 24.75           C
ANISOU 3277  CG  TRP B  59     2648   2497   4257     23    185    205       C
ATOM   3278  CD1 TRP B  59     -80.680  28.431  14.535  1.00 24.03           C
ANISOU 3278  CD1 TRP B  59     2623   2368   4138     35    175    215       C
ATOM   3279  CD2 TRP B  59     -82.624  29.115  13.666  1.00 26.34           C
ANISOU 3279  CD2 TRP B  59     2850   2725   4431     79    221    223       C
ATOM   3280  NE1 TRP B  59     -81.386  29.058  15.533  1.00 28.35           N
ANISOU 3280  NE1 TRP B  59     3229   2915   4629    100    204    232       N
ATOM   3281  CE2 TRP B  59     -82.583  29.488  15.024  1.00 28.36           C
ANISOU 3281  CE2 TRP B  59     3188   2957   4632    133    240    240       C
ATOM   3282  CE3 TRP B  59     -83.754  29.440  12.911  1.00 24.42           C
ANISOU 3282  CE3 TRP B  59     2550   2526   4204     96    237    231       C
ATOM   3283  CZ2 TRP B  59     -83.627  30.169  15.642  1.00 29.90           C
ANISOU 3283  CZ2 TRP B  59     3410   3170   4780    214    290    264       C
ATOM   3284  CZ3 TRP B  59     -84.789  30.116  13.525  1.00 29.04           C
ANISOU 3284  CZ3 TRP B  59     3145   3132   4757    169    283    262       C
ATOM   3285  CH2 TRP B  59     -84.720  30.474  14.877  1.00 34.10           C
ANISOU 3285  CH2 TRP B  59     3871   3748   5337    233    316    278       C
ATOM   3286  N   ALA B  60     -83.483  25.907  11.703  1.00 27.20           N
ANISOU 3286  N   ALA B  60     2755   2871   4709    -60    210    212       N
ATOM   3287  CA  ALA B  60     -84.794  25.437  12.136  1.00 25.18           C
ANISOU 3287  CA  ALA B  60     2433   2639   4495    -58    242    260       C
ATOM   3288  C   ALA B  60     -84.778  23.949  12.452  1.00 24.98           C
ANISOU 3288  C   ALA B  60     2374   2584   4531   -108    244    276       C
ATOM   3289  O   ALA B  60     -85.531  23.489  13.317  1.00 24.03           O
ANISOU 3289  O   ALA B  60     2214   2474   4443   -102    287    337       O
ATOM   3290  CB  ALA B  60     -85.841  25.739  11.065  1.00 25.75           C
ANISOU 3290  CB  ALA B  60     2442   2749   4594    -66    216    261       C
ATOM   3291  N   LYS B  61     -83.928  23.185  11.769  1.00 28.95           N
ANISOU 3291  N   LYS B  61     2896   3051   5053   -150    201    230       N
ATOM   3292  CA  LYS B  61     -83.821  21.750  11.975  1.00 26.09           C
ANISOU 3292  CA  LYS B  61     2516   2647   4751   -196    192    237       C
ATOM   3293  C   LYS B  61     -82.693  21.381  12.929  1.00 27.73           C
ANISOU 3293  C   LYS B  61     2776   2820   4939   -184    215    243       C
ATOM   3294  O   LYS B  61     -82.286  20.215  12.975  1.00 27.32           O
ANISOU 3294  O   LYS B  61     2726   2724   4929   -215    203    239       O
ATOM   3295  CB  LYS B  61     -83.635  21.042  10.634  1.00 23.07           C
ANISOU 3295  CB  LYS B  61     2135   2236   4394   -236    130    180       C
ATOM   3296  CG  LYS B  61     -84.786  21.256   9.668  1.00 22.11           C
ANISOU 3296  CG  LYS B  61     1964   2141   4297   -258     86    176       C
ATOM   3297  CD  LYS B  61     -84.551  20.530   8.357  1.00 24.31           C
ANISOU 3297  CD  LYS B  61     2273   2383   4582   -289     14    110       C
ATOM   3298  CE  LYS B  61     -85.774  20.609   7.455  1.00 25.48           C
ANISOU 3298  CE  LYS B  61     2373   2549   4760   -320    -51    110       C
ATOM   3299  NZ  LYS B  61     -85.586  19.817   6.208  1.00 28.33           N
ANISOU 3299  NZ  LYS B  61     2787   2862   5116   -346   -134     39       N
ATOM   3300  N   ARG B  62     -82.182  22.347  13.689  1.00 20.01           N
ANISOU 3300  N   ARG B  62     1847   1856   3899   -138    239    253       N
ATOM   3301  CA  ARG B  62     -81.115  22.072  14.638  1.00 24.31           C
ANISOU 3301  CA  ARG B  62     2444   2369   4424   -127    245    264       C
ATOM   3302  C   ARG B  62     -81.593  21.105  15.718  1.00 26.66           C
ANISOU 3302  C   ARG B  62     2726   2652   4752   -132    283    320       C
ATOM   3303  O   ARG B  62     -82.787  20.996  16.016  1.00 25.75           O
ANISOU 3303  O   ARG B  62     2564   2562   4659   -128    319    366       O
ATOM   3304  CB  ARG B  62     -80.622  23.369  15.278  1.00 23.52           C
ANISOU 3304  CB  ARG B  62     2409   2277   4250    -81    243    265       C
ATOM   3305  CG  ARG B  62     -81.592  23.954  16.288  1.00 23.53           C
ANISOU 3305  CG  ARG B  62     2431   2303   4207    -29    290    306       C
ATOM   3306  CD  ARG B  62     -81.299  25.415  16.565  1.00 26.11           C
ANISOU 3306  CD  ARG B  62     2834   2628   4457     20    272    289       C
ATOM   3307  NE  ARG B  62     -82.297  26.004  17.452  1.00 31.18           N
ANISOU 3307  NE  ARG B  62     3508   3295   5046     91    326    324       N
ATOM   3308  CZ  ARG B  62     -83.505  26.399  17.061  1.00 26.92           C
ANISOU 3308  CZ  ARG B  62     2916   2797   4515    120    366    342       C
ATOM   3309  NH1 ARG B  62     -83.875  26.265  15.794  1.00 23.44           N
ANISOU 3309  NH1 ARG B  62     2396   2378   4133     74    344    324       N
ATOM   3310  NH2 ARG B  62     -84.346  26.925  17.940  1.00 23.68           N
ANISOU 3310  NH2 ARG B  62     2537   2411   4051    201    428    383       N
ATOM   3311  N   ASN B  63     -80.637  20.393  16.306  1.00 31.71           N
ANISOU 3311  N   ASN B  63     3399   3253   5397   -139    275    326       N
ATOM   3312  CA  ASN B  63     -80.952  19.454  17.373  1.00 26.29           C
ANISOU 3312  CA  ASN B  63     2706   2548   4736   -142    311    386       C
ATOM   3313  C   ASN B  63     -81.256  20.213  18.658  1.00 26.68           C
ANISOU 3313  C   ASN B  63     2804   2625   4710    -81    356    432       C
ATOM   3314  O   ASN B  63     -80.447  21.024  19.120  1.00 32.12           O
ANISOU 3314  O   ASN B  63     3568   3308   5329    -46    332    412       O
ATOM   3315  CB  ASN B  63     -79.789  18.487  17.584  1.00 26.76           C
ANISOU 3315  CB  ASN B  63     2791   2555   4821   -160    286    380       C
ATOM   3316  CG  ASN B  63     -80.181  17.268  18.392  1.00 31.46           C
ANISOU 3316  CG  ASN B  63     3368   3121   5465   -178    314    442       C
ATOM   3317  OD1 ASN B  63     -80.820  17.377  19.438  1.00 34.82           O
ANISOU 3317  OD1 ASN B  63     3798   3569   5862   -151    364    505       O
ATOM   3318  ND2 ASN B  63     -79.806  16.093  17.902  1.00 30.65           N
ANISOU 3318  ND2 ASN B  63     3250   2966   5431   -217    288    428       N
ATOM   3319  N   ILE B  64     -82.425  19.950  19.236  1.00 29.79           N
ANISOU 3319  N   ILE B  64     3157   3045   5116    -66    417    499       N
ATOM   3320  CA  ILE B  64     -82.880  20.644  20.433  1.00 30.71           C
ANISOU 3320  CA  ILE B  64     3326   3193   5149     13    477    548       C
ATOM   3321  C   ILE B  64     -82.770  19.764  21.671  1.00 31.62           C
ANISOU 3321  C   ILE B  64     3467   3292   5254     29    519    618       C
ATOM   3322  O   ILE B  64     -83.358  20.082  22.710  1.00 35.89           O
ANISOU 3322  O   ILE B  64     4042   3864   5729    101    589    678       O
ATOM   3323  CB  ILE B  64     -84.312  21.174  20.257  1.00 31.03           C
ANISOU 3323  CB  ILE B  64     3301   3290   5198     46    537    591       C
ATOM   3324  CG1 ILE B  64     -85.279  20.013  20.027  1.00 32.89           C
ANISOU 3324  CG1 ILE B  64     3418   3533   5547    -12    565    661       C
ATOM   3325  CG2 ILE B  64     -84.373  22.161  19.098  1.00 30.56           C
ANISOU 3325  CG2 ILE B  64     3231   3247   5134     40    492    523       C
ATOM   3326  CD1 ILE B  64     -86.733  20.401  20.146  1.00 32.25           C
ANISOU 3326  CD1 ILE B  64     3255   3514   5485     27    637    740       C
ATOM   3327  N   LYS B  65     -82.045  18.667  21.587  1.00 31.00           N
ANISOU 3327  N   LYS B  65     3378   3166   5235    -26    482    614       N
ATOM   3328  CA  LYS B  65     -81.763  17.822  22.732  1.00 29.05           C
ANISOU 3328  CA  LYS B  65     3164   2896   4977    -13    510    678       C
ATOM   3329  C   LYS B  65     -80.352  18.086  23.237  1.00 27.88           C
ANISOU 3329  C   LYS B  65     3116   2715   4762      8    451    638       C
ATOM   3330  O   LYS B  65     -79.542  18.706  22.543  1.00 29.03           O
ANISOU 3330  O   LYS B  65     3282   2849   4900     -7    386    567       O
ATOM   3331  CB  LYS B  65     -81.925  16.345  22.353  1.00 36.41           C
ANISOU 3331  CB  LYS B  65     4019   3786   6030    -88    503    711       C
ATOM   3332  CG  LYS B  65     -83.344  15.974  21.949  1.00 50.32           C
ANISOU 3332  CG  LYS B  65     5672   5571   7875   -123    545    769       C
ATOM   3333  CD  LYS B  65     -83.527  14.469  21.841  1.00 63.15           C
ANISOU 3333  CD  LYS B  65     7238   7138   9618   -197    531    818       C
ATOM   3334  CE  LYS B  65     -82.662  13.876  20.741  1.00 71.59           C
ANISOU 3334  CE  LYS B  65     8319   8141  10743   -255    442    726       C
ATOM   3335  NZ  LYS B  65     -82.864  12.405  20.617  1.00 78.04           N
ANISOU 3335  NZ  LYS B  65     9094   8883  11672   -324    417    767       N
ATOM   3336  N   PRO B  66     -80.028  17.662  24.461  1.00 29.91           N
ANISOU 3336  N   PRO B  66     3436   2959   4972     43    468    693       N
ATOM   3337  CA  PRO B  66     -78.647  17.812  24.945  1.00 27.05           C
ANISOU 3337  CA  PRO B  66     3160   2560   4560     53    394    664       C
ATOM   3338  C   PRO B  66     -77.668  17.105  24.020  1.00 29.51           C
ANISOU 3338  C   PRO B  66     3418   2829   4966    -14    331    623       C
ATOM   3339  O   PRO B  66     -77.761  15.897  23.793  1.00 34.39           O
ANISOU 3339  O   PRO B  66     3981   3419   5669    -53    347    650       O
ATOM   3340  CB  PRO B  66     -78.689  17.167  26.334  1.00 26.47           C
ANISOU 3340  CB  PRO B  66     3143   2479   4435     95    432    744       C
ATOM   3341  CG  PRO B  66     -80.100  17.320  26.765  1.00 29.04           C
ANISOU 3341  CG  PRO B  66     3449   2855   4729    144    537    808       C
ATOM   3342  CD  PRO B  66     -80.927  17.171  25.521  1.00 28.58           C
ANISOU 3342  CD  PRO B  66     3267   2814   4779     85    558    792       C
ATOM   3343  N   VAL B  67     -76.732  17.875  23.476  1.00 27.79           N
ANISOU 3343  N   VAL B  67     3220   2603   4734    -22    261    563       N
ATOM   3344  CA  VAL B  67     -75.773  17.354  22.504  1.00 28.78           C
ANISOU 3344  CA  VAL B  67     3294   2700   4941    -66    215    528       C
ATOM   3345  C   VAL B  67     -74.369  17.658  22.998  1.00 29.87           C
ANISOU 3345  C   VAL B  67     3481   2815   5054    -57    140    532       C
ATOM   3346  O   VAL B  67     -74.159  18.592  23.791  1.00 27.86           O
ANISOU 3346  O   VAL B  67     3305   2565   4716    -27    101    535       O
ATOM   3347  CB  VAL B  67     -76.012  17.949  21.095  1.00 32.07           C
ANISOU 3347  CB  VAL B  67     3659   3138   5388    -90    211    468       C
ATOM   3348  CG1 VAL B  67     -77.321  17.440  20.520  1.00 32.16           C
ANISOU 3348  CG1 VAL B  67     3611   3163   5446   -112    265    470       C
ATOM   3349  CG2 VAL B  67     -76.008  19.467  21.155  1.00 34.00           C
ANISOU 3349  CG2 VAL B  67     3951   3410   5557    -64    184    442       C
ATOM   3350  N   PRO B  68     -73.379  16.876  22.563  1.00 29.47           N
ANISOU 3350  N   PRO B  68     3388   2735   5075    -79    111    534       N
ATOM   3351  CA  PRO B  68     -71.994  17.167  22.944  1.00 30.02           C
ANISOU 3351  CA  PRO B  68     3479   2787   5141    -76     32    551       C
ATOM   3352  C   PRO B  68     -71.569  18.545  22.464  1.00 31.84           C
ANISOU 3352  C   PRO B  68     3716   3035   5345    -84    -21    518       C
ATOM   3353  O   PRO B  68     -72.032  19.039  21.433  1.00 32.36           O
ANISOU 3353  O   PRO B  68     3745   3126   5424    -95      6    477       O
ATOM   3354  CB  PRO B  68     -71.192  16.064  22.244  1.00 26.61           C
ANISOU 3354  CB  PRO B  68     2978   2328   4803    -88     36    558       C
ATOM   3355  CG  PRO B  68     -72.166  14.963  22.033  1.00 25.59           C
ANISOU 3355  CG  PRO B  68     2829   2183   4712    -94    105    557       C
ATOM   3356  CD  PRO B  68     -73.486  15.626  21.790  1.00 26.11           C
ANISOU 3356  CD  PRO B  68     2899   2284   4738   -102    146    529       C
ATOM   3357  N   GLU B  69     -70.684  19.170  23.232  1.00 29.67           N
ANISOU 3357  N   GLU B  69     3493   2744   5036    -81   -108    542       N
ATOM   3358  CA  GLU B  69     -70.149  20.460  22.829  1.00 29.59           C
ANISOU 3358  CA  GLU B  69     3489   2736   5018   -100   -177    524       C
ATOM   3359  C   GLU B  69     -69.276  20.302  21.590  1.00 29.22           C
ANISOU 3359  C   GLU B  69     3334   2700   5067   -127   -178    530       C
ATOM   3360  O   GLU B  69     -68.651  19.261  21.372  1.00 33.42           O
ANISOU 3360  O   GLU B  69     3808   3226   5666   -124   -159    558       O
ATOM   3361  CB  GLU B  69     -69.359  21.091  23.974  1.00 33.36           C
ANISOU 3361  CB  GLU B  69     4051   3179   5445   -100   -293    553       C
ATOM   3362  CG  GLU B  69     -70.244  21.565  25.119  1.00 37.59           C
ANISOU 3362  CG  GLU B  69     4721   3706   5857    -55   -292    538       C
ATOM   3363  CD  GLU B  69     -69.485  22.362  26.161  1.00 44.31           C
ANISOU 3363  CD  GLU B  69     5684   4511   6642    -52   -428    552       C
ATOM   3364  OE1 GLU B  69     -68.676  21.764  26.901  1.00 48.78           O
ANISOU 3364  OE1 GLU B  69     6264   5053   7218    -56   -491    597       O
ATOM   3365  OE2 GLU B  69     -69.696  23.591  26.236  1.00 49.23           O
ANISOU 3365  OE2 GLU B  69     6387   5116   7204    -45   -480    516       O
ATOM   3366  N   VAL B  70     -69.249  21.353  20.767  1.00 30.95           N
ANISOU 3366  N   VAL B  70     3534   2937   5290   -144   -193    507       N
ATOM   3367  CA  VAL B  70     -68.619  21.262  19.452  1.00 29.81           C
ANISOU 3367  CA  VAL B  70     3290   2814   5221   -156   -167    514       C
ATOM   3368  C   VAL B  70     -67.135  20.945  19.583  1.00 28.74           C
ANISOU 3368  C   VAL B  70     3094   2667   5160   -166   -222    583       C
ATOM   3369  O   VAL B  70     -66.569  20.209  18.764  1.00 29.97           O
ANISOU 3369  O   VAL B  70     3167   2837   5381   -149   -173    603       O
ATOM   3370  CB  VAL B  70     -68.862  22.559  18.658  1.00 34.74           C
ANISOU 3370  CB  VAL B  70     3912   3459   5830   -172   -178    490       C
ATOM   3371  CG1 VAL B  70     -68.183  22.492  17.299  1.00 36.39           C
ANISOU 3371  CG1 VAL B  70     4022   3698   6106   -174   -143    508       C
ATOM   3372  CG2 VAL B  70     -70.355  22.805  18.497  1.00 30.24           C
ANISOU 3372  CG2 VAL B  70     3388   2906   5195   -154   -120    430       C
ATOM   3373  N   LYS B  71     -66.482  21.483  20.617  1.00 28.61           N
ANISOU 3373  N   LYS B  71     3120   2620   5132   -187   -329    623       N
ATOM   3374  CA  LYS B  71     -65.068  21.184  20.823  1.00 28.68           C
ANISOU 3374  CA  LYS B  71     3060   2617   5222   -201   -396    703       C
ATOM   3375  C   LYS B  71     -64.838  19.693  21.029  1.00 29.11           C
ANISOU 3375  C   LYS B  71     3081   2668   5312   -165   -341    725       C
ATOM   3376  O   LYS B  71     -63.817  19.158  20.585  1.00 31.30           O
ANISOU 3376  O   LYS B  71     3263   2954   5674   -153   -333    783       O
ATOM   3377  CB  LYS B  71     -64.525  21.984  22.010  1.00 29.28           C
ANISOU 3377  CB  LYS B  71     3207   2650   5270   -236   -542    738       C
ATOM   3378  CG  LYS B  71     -65.235  21.729  23.329  1.00 30.55           C
ANISOU 3378  CG  LYS B  71     3500   2781   5328   -211   -564    706       C
ATOM   3379  CD  LYS B  71     -64.624  22.563  24.445  1.00 31.79           C
ANISOU 3379  CD  LYS B  71     3746   2887   5446   -239   -726    734       C
ATOM   3380  CE  LYS B  71     -65.349  22.354  25.764  1.00 31.01           C
ANISOU 3380  CE  LYS B  71     3798   2763   5223   -197   -739    704       C
ATOM   3381  NZ  LYS B  71     -64.782  23.201  26.852  1.00 31.97           N
ANISOU 3381  NZ  LYS B  71     4036   2825   5286   -216   -910    718       N
ATOM   3382  N   ILE B  72     -65.777  19.007  21.683  1.00 28.82           N
ANISOU 3382  N   ILE B  72     3120   2617   5215   -143   -299    687       N
ATOM   3383  CA  ILE B  72     -65.672  17.558  21.829  1.00 28.39           C
ANISOU 3383  CA  ILE B  72     3041   2548   5197   -111   -245    705       C
ATOM   3384  C   ILE B  72     -65.759  16.884  20.466  1.00 28.26           C
ANISOU 3384  C   ILE B  72     2952   2549   5236    -86   -146    679       C
ATOM   3385  O   ILE B  72     -64.923  16.045  20.112  1.00 31.30           O
ANISOU 3385  O   ILE B  72     3274   2927   5690    -56   -124    717       O
ATOM   3386  CB  ILE B  72     -66.759  17.037  22.787  1.00 27.58           C
ANISOU 3386  CB  ILE B  72     3031   2427   5022    -98   -216    682       C
ATOM   3387  CG1 ILE B  72     -66.543  17.599  24.194  1.00 28.45           C
ANISOU 3387  CG1 ILE B  72     3232   2517   5062   -103   -314    712       C
ATOM   3388  CG2 ILE B  72     -66.771  15.518  22.802  1.00 23.23           C
ANISOU 3388  CG2 ILE B  72     2455   1852   4518    -72   -156    699       C
ATOM   3389  CD1 ILE B  72     -65.200  17.247  24.792  1.00 24.06           C
ANISOU 3389  CD1 ILE B  72     2647   1938   4557   -107   -404    786       C
ATOM   3390  N   LEU B  73     -66.771  17.251  19.677  1.00 25.17           N
ANISOU 3390  N   LEU B  73     2575   2178   4809    -91    -90    613       N
ATOM   3391  CA  LEU B  73     -66.922  16.670  18.347  1.00 22.75           C
ANISOU 3391  CA  LEU B  73     2223   1883   4537    -64     -9    577       C
ATOM   3392  C   LEU B  73     -65.739  17.020  17.456  1.00 24.45           C
ANISOU 3392  C   LEU B  73     2355   2127   4807    -46     -8    619       C
ATOM   3393  O   LEU B  73     -65.314  16.207  16.627  1.00 28.83           O
ANISOU 3393  O   LEU B  73     2870   2683   5403      3     53    621       O
ATOM   3394  CB  LEU B  73     -68.228  17.146  17.714  1.00 25.17           C
ANISOU 3394  CB  LEU B  73     2562   2209   4792    -79     31    506       C
ATOM   3395  CG  LEU B  73     -69.494  16.940  18.547  1.00 28.34           C
ANISOU 3395  CG  LEU B  73     3028   2595   5145    -94     40    481       C
ATOM   3396  CD1 LEU B  73     -70.718  17.428  17.790  1.00 29.93           C
ANISOU 3396  CD1 LEU B  73     3239   2821   5312   -106     78    423       C
ATOM   3397  CD2 LEU B  73     -69.649  15.480  18.936  1.00 31.58           C
ANISOU 3397  CD2 LEU B  73     3447   2962   5589    -81     70    493       C
ATOM   3398  N   ASN B  74     -65.195  18.229  17.609  1.00 26.61           N
ANISOU 3398  N   ASN B  74     2606   2421   5084    -79    -73    658       N
ATOM   3399  CA  ASN B  74     -64.022  18.613  16.831  1.00 28.10           C
ANISOU 3399  CA  ASN B  74     2697   2641   5338    -67    -72    724       C
ATOM   3400  C   ASN B  74     -62.814  17.772  17.216  1.00 32.33           C
ANISOU 3400  C   ASN B  74     3167   3165   5951    -36    -85    806       C
ATOM   3401  O   ASN B  74     -62.117  17.234  16.348  1.00 35.40           O
ANISOU 3401  O   ASN B  74     3483   3576   6392     20    -16    841       O
ATOM   3402  CB  ASN B  74     -63.722  20.100  17.023  1.00 37.42           C
ANISOU 3402  CB  ASN B  74     3869   3832   6518   -124   -158    759       C
ATOM   3403  CG  ASN B  74     -64.773  20.996  16.397  1.00 39.05           C
ANISOU 3403  CG  ASN B  74     4122   4055   6659   -141   -134    690       C
ATOM   3404  OD1 ASN B  74     -65.535  20.567  15.532  1.00 38.85           O
ANISOU 3404  OD1 ASN B  74     4109   4049   6605   -109    -47    629       O
ATOM   3405  ND2 ASN B  74     -64.813  22.251  16.829  1.00 38.44           N
ANISOU 3405  ND2 ASN B  74     4078   3966   6561   -190   -219    700       N
ATOM   3406  N   ASN B  75     -62.552  17.643  18.519  1.00 32.12           N
ANISOU 3406  N   ASN B  75     3172   3106   5927    -63   -171    841       N
ATOM   3407  CA  ASN B  75     -61.402  16.871  18.973  1.00 30.78           C
ANISOU 3407  CA  ASN B  75     2937   2924   5834    -35   -197    927       C
ATOM   3408  C   ASN B  75     -61.496  15.410  18.562  1.00 32.86           C
ANISOU 3408  C   ASN B  75     3198   3171   6115     38    -97    905       C
ATOM   3409  O   ASN B  75     -60.465  14.738  18.459  1.00 37.67           O
ANISOU 3409  O   ASN B  75     3731   3782   6798     88    -81    977       O
ATOM   3410  CB  ASN B  75     -61.258  16.978  20.491  1.00 31.07           C
ANISOU 3410  CB  ASN B  75     3032   2924   5850    -76   -315    957       C
ATOM   3411  CG  ASN B  75     -60.955  18.390  20.949  1.00 29.49           C
ANISOU 3411  CG  ASN B  75     2843   2721   5639   -144   -439    986       C
ATOM   3412  OD1 ASN B  75     -60.592  19.250  20.147  1.00 33.54           O
ANISOU 3412  OD1 ASN B  75     3289   3262   6191   -167   -442   1012       O
ATOM   3413  ND2 ASN B  75     -61.098  18.635  22.245  1.00 28.07           N
ANISOU 3413  ND2 ASN B  75     2757   2504   5405   -175   -544    985       N
ATOM   3414  N   LEU B  76     -62.701  14.906  18.322  1.00 30.56           N
ANISOU 3414  N   LEU B  76     2988   2860   5763     47    -36    812       N
ATOM   3415  CA  LEU B  76     -62.891  13.541  17.857  1.00 28.58           C
ANISOU 3415  CA  LEU B  76     2753   2577   5528    109     46    780       C
ATOM   3416  C   LEU B  76     -62.876  13.427  16.340  1.00 31.37           C
ANISOU 3416  C   LEU B  76     3080   2954   5884    164    136    742       C
ATOM   3417  O   LEU B  76     -62.937  12.310  15.818  1.00 38.19           O
ANISOU 3417  O   LEU B  76     3969   3782   6758    228    199    710       O
ATOM   3418  CB  LEU B  76     -64.205  12.976  18.404  1.00 28.89           C
ANISOU 3418  CB  LEU B  76     2890   2573   5514     83     53    711       C
ATOM   3419  CG  LEU B  76     -64.243  12.812  19.924  1.00 33.34           C
ANISOU 3419  CG  LEU B  76     3496   3108   6063     52    -15    752       C
ATOM   3420  CD1 LEU B  76     -65.603  12.315  20.390  1.00 30.35           C
ANISOU 3420  CD1 LEU B  76     3199   2697   5634     29     10    701       C
ATOM   3421  CD2 LEU B  76     -63.141  11.870  20.378  1.00 39.85           C
ANISOU 3421  CD2 LEU B  76     4281   3906   6956     97    -31    828       C
ATOM   3422  N   GLY B  77     -62.800  14.546  15.625  1.00 32.12           N
ANISOU 3422  N   GLY B  77     3139   3102   5965    147    140    744       N
ATOM   3423  CA  GLY B  77     -62.703  14.499  14.180  1.00 35.15           C
ANISOU 3423  CA  GLY B  77     3502   3516   6339    209    228    719       C
ATOM   3424  C   GLY B  77     -64.010  14.292  13.455  1.00 34.53           C
ANISOU 3424  C   GLY B  77     3511   3419   6189    208    267    605       C
ATOM   3425  O   GLY B  77     -64.011  13.758  12.341  1.00 39.49           O
ANISOU 3425  O   GLY B  77     4159   4047   6800    278    338    566       O
ATOM   3426  N   VAL B  78     -65.130  14.700  14.052  1.00 32.36           N
ANISOU 3426  N   VAL B  78     3293   3131   5871    135    220    554       N
ATOM   3427  CA  VAL B  78     -66.424  14.550  13.400  1.00 29.46           C
ANISOU 3427  CA  VAL B  78     2994   2750   5449    123    244    459       C
ATOM   3428  C   VAL B  78     -66.538  15.554  12.262  1.00 29.21           C
ANISOU 3428  C   VAL B  78     2944   2774   5379    130    270    439       C
ATOM   3429  O   VAL B  78     -66.261  16.749  12.433  1.00 32.79           O
ANISOU 3429  O   VAL B  78     3358   3270   5831     93    238    481       O
ATOM   3430  CB  VAL B  78     -67.564  14.726  14.413  1.00 28.26           C
ANISOU 3430  CB  VAL B  78     2890   2578   5271     52    198    433       C
ATOM   3431  CG1 VAL B  78     -68.911  14.710  13.706  1.00 25.42           C
ANISOU 3431  CG1 VAL B  78     2578   2213   4869     32    215    351       C
ATOM   3432  CG2 VAL B  78     -67.501  13.635  15.472  1.00 24.30           C
ANISOU 3432  CG2 VAL B  78     2411   2020   4802     52    182    458       C
ATOM   3433  N   ASP B  79     -66.945  15.069  11.088  1.00 30.01           N
ANISOU 3433  N   ASP B  79     3086   2868   5446    177    320    375       N
ATOM   3434  CA  ASP B  79     -67.114  15.914   9.916  1.00 31.44           C
ANISOU 3434  CA  ASP B  79     3264   3102   5580    194    348    353       C
ATOM   3435  C   ASP B  79     -68.567  16.200   9.577  1.00 30.06           C
ANISOU 3435  C   ASP B  79     3148   2921   5351    147    323    271       C
ATOM   3436  O   ASP B  79     -68.841  17.201   8.909  1.00 35.62           O
ANISOU 3436  O   ASP B  79     3844   3673   6016    137    326    263       O
ATOM   3437  CB  ASP B  79     -66.453  15.267   8.691  1.00 39.51           C
ANISOU 3437  CB  ASP B  79     4298   4130   6585    299    424    345       C
ATOM   3438  CG  ASP B  79     -65.077  14.720   8.993  1.00 47.08           C
ANISOU 3438  CG  ASP B  79     5195   5088   7605    363    461    430       C
ATOM   3439  OD1 ASP B  79     -64.229  15.476   9.512  1.00 52.86           O
ANISOU 3439  OD1 ASP B  79     5835   5861   8387    338    444    526       O
ATOM   3440  OD2 ASP B  79     -64.850  13.525   8.716  1.00 51.26           O
ANISOU 3440  OD2 ASP B  79     5769   5569   8137    439    500    403       O
ATOM   3441  N   ILE B  80     -69.496  15.355  10.019  1.00 28.83           N
ANISOU 3441  N   ILE B  80     3044   2709   5201    116    297    220       N
ATOM   3442  CA  ILE B  80     -70.885  15.442   9.589  1.00 24.97           C
ANISOU 3442  CA  ILE B  80     2600   2212   4676     77    272    150       C
ATOM   3443  C   ILE B  80     -71.730  14.627  10.555  1.00 29.34           C
ANISOU 3443  C   ILE B  80     3176   2708   5266     25    239    140       C
ATOM   3444  O   ILE B  80     -71.241  13.691  11.191  1.00 31.97           O
ANISOU 3444  O   ILE B  80     3514   2992   5640     39    242    165       O
ATOM   3445  CB  ILE B  80     -71.031  14.947   8.127  1.00 27.61           C
ANISOU 3445  CB  ILE B  80     2991   2534   4967    134    294     84       C
ATOM   3446  CG1 ILE B  80     -72.396  15.323   7.549  1.00 29.47           C
ANISOU 3446  CG1 ILE B  80     3258   2775   5164     89    255     23       C
ATOM   3447  CG2 ILE B  80     -70.802  13.447   8.043  1.00 33.79           C
ANISOU 3447  CG2 ILE B  80     3829   3235   5773    179    300     53       C
ATOM   3448  CD1 ILE B  80     -72.504  15.068   6.062  1.00 26.16           C
ANISOU 3448  CD1 ILE B  80     2906   2351   4682    148    263    -42       C
ATOM   3449  N   ALA B  81     -73.004  14.993  10.675  1.00 28.59           N
ANISOU 3449  N   ALA B  81     3086   2619   5157    -32    210    116       N
ATOM   3450  CA  ALA B  81     -73.932  14.321  11.571  1.00 27.57           C
ANISOU 3450  CA  ALA B  81     2963   2446   5066    -83    187    124       C
ATOM   3451  C   ALA B  81     -74.931  13.493  10.774  1.00 32.50           C
ANISOU 3451  C   ALA B  81     3624   3020   5705   -104    157     66       C
ATOM   3452  O   ALA B  81     -75.238  13.799   9.618  1.00 37.44           O
ANISOU 3452  O   ALA B  81     4272   3662   6293    -92    144     14       O
ATOM   3453  CB  ALA B  81     -74.675  15.329  12.452  1.00 20.75           C
ANISOU 3453  CB  ALA B  81     2069   1629   4186   -126    180    159       C
ATOM   3454  N   ALA B  82     -75.438  12.440  11.410  1.00 31.11           N
ANISOU 3454  N   ALA B  82     3457   2777   5585   -140    137     81       N
ATOM   3455  CA  ALA B  82     -76.375  11.521  10.774  1.00 29.16           C
ANISOU 3455  CA  ALA B  82     3246   2461   5372   -176     88     36       C
ATOM   3456  C   ALA B  82     -77.800  11.980  11.058  1.00 32.39           C
ANISOU 3456  C   ALA B  82     3605   2899   5802   -248     63     60       C
ATOM   3457  O   ALA B  82     -78.293  11.841  12.183  1.00 35.37           O
ANISOU 3457  O   ALA B  82     3942   3276   6221   -286     76    127       O
ATOM   3458  CB  ALA B  82     -76.151  10.096  11.271  1.00 30.84           C
ANISOU 3458  CB  ALA B  82     3493   2577   5650   -180     74     50       C
ATOM   3459  N   ASN B  83     -78.455  12.537  10.038  1.00 30.13           N
ANISOU 3459  N   ASN B  83     3321   2641   5485   -258     31     14       N
ATOM   3460  CA  ASN B  83     -79.884  12.849  10.078  1.00 33.49           C
ANISOU 3460  CA  ASN B  83     3694   3087   5942   -323     -4     36       C
ATOM   3461  C   ASN B  83     -80.226  13.876  11.155  1.00 30.69           C
ANISOU 3461  C   ASN B  83     3273   2812   5575   -328     50    107       C
ATOM   3462  O   ASN B  83     -81.303  13.826  11.754  1.00 28.09           O
ANISOU 3462  O   ASN B  83     2888   2492   5294   -374     49    163       O
ATOM   3463  CB  ASN B  83     -80.716  11.576  10.265  1.00 36.92           C
ANISOU 3463  CB  ASN B  83     4126   3433   6470   -390    -61     54       C
ATOM   3464  CG  ASN B  83     -80.368  10.503   9.251  1.00 43.08           C
ANISOU 3464  CG  ASN B  83     4999   4115   7256   -378   -125    -25       C
ATOM   3465  OD1 ASN B  83     -79.876   9.433   9.608  1.00 49.42           O
ANISOU 3465  OD1 ASN B  83     5843   4836   8099   -373   -130    -21       O
ATOM   3466  ND2 ASN B  83     -80.619  10.787   7.978  1.00 42.54           N
ANISOU 3466  ND2 ASN B  83     4975   4051   7139   -366   -177    -98       N
ATOM   3467  N   THR B  84     -79.322  14.820  11.402  1.00 32.92           N
ANISOU 3467  N   THR B  84     3564   3150   5796   -277     95    110       N
ATOM   3468  CA  THR B  84     -79.583  15.904  12.339  1.00 31.70           C
ANISOU 3468  CA  THR B  84     3373   3059   5611   -270    134    162       C
ATOM   3469  C   THR B  84     -78.623  17.043  12.032  1.00 29.74           C
ANISOU 3469  C   THR B  84     3145   2858   5295   -223    150    142       C
ATOM   3470  O   THR B  84     -77.742  16.926  11.176  1.00 32.90           O
ANISOU 3470  O   THR B  84     3573   3249   5678   -196    143    102       O
ATOM   3471  CB  THR B  84     -79.439  15.446  13.795  1.00 34.83           C
ANISOU 3471  CB  THR B  84     3764   3438   6031   -272    168    230       C
ATOM   3472  OG1 THR B  84     -79.812  16.517  14.673  1.00 35.39           O
ANISOU 3472  OG1 THR B  84     3821   3568   6057   -253    204    274       O
ATOM   3473  CG2 THR B  84     -78.005  15.041  14.085  1.00 36.66           C
ANISOU 3473  CG2 THR B  84     4036   3640   6253   -239    174    226       C
ATOM   3474  N   VAL B  85     -78.810  18.154  12.740  1.00 25.00           N
ANISOU 3474  N   VAL B  85     2535   2308   4658   -211    172    175       N
ATOM   3475  CA  VAL B  85     -77.951  19.325  12.610  1.00 23.04           C
ANISOU 3475  CA  VAL B  85     2304   2094   4355   -179    174    169       C
ATOM   3476  C   VAL B  85     -77.483  19.724  14.000  1.00 24.82           C
ANISOU 3476  C   VAL B  85     2551   2320   4561   -164    186    216       C
ATOM   3477  O   VAL B  85     -78.307  19.997  14.882  1.00 27.55           O
ANISOU 3477  O   VAL B  85     2898   2679   4890   -161    204    247       O
ATOM   3478  CB  VAL B  85     -78.665  20.503  11.927  1.00 19.50           C
ANISOU 3478  CB  VAL B  85     1844   1694   3870   -173    168    151       C
ATOM   3479  CG1 VAL B  85     -77.760  21.726  11.902  1.00 19.12           C
ANISOU 3479  CG1 VAL B  85     1818   1671   3778   -147    164    156       C
ATOM   3480  CG2 VAL B  85     -79.081  20.126  10.522  1.00 25.67           C
ANISOU 3480  CG2 VAL B  85     2618   2475   4661   -184    144    103       C
ATOM   3481  N   ILE B  86     -76.170  19.751  14.197  1.00 26.56           N
ANISOU 3481  N   ILE B  86     2787   2526   4778   -151    173    225       N
ATOM   3482  CA  ILE B  86     -75.576  20.282  15.417  1.00 27.06           C
ANISOU 3482  CA  ILE B  86     2882   2584   4813   -139    159    265       C
ATOM   3483  C   ILE B  86     -75.295  21.760  15.176  1.00 29.01           C
ANISOU 3483  C   ILE B  86     3146   2858   5018   -130    133    259       C
ATOM   3484  O   ILE B  86     -74.460  22.115  14.341  1.00 29.23           O
ANISOU 3484  O   ILE B  86     3154   2894   5057   -131    117    254       O
ATOM   3485  CB  ILE B  86     -74.300  19.526  15.801  1.00 29.02           C
ANISOU 3485  CB  ILE B  86     3132   2800   5095   -135    143    290       C
ATOM   3486  CG1 ILE B  86     -74.606  18.042  16.007  1.00 29.66           C
ANISOU 3486  CG1 ILE B  86     3205   2844   5221   -143    166    296       C
ATOM   3487  CG2 ILE B  86     -73.682  20.127  17.054  1.00 27.54           C
ANISOU 3487  CG2 ILE B  86     2985   2604   4875   -128    107    331       C
ATOM   3488  CD1 ILE B  86     -75.643  17.779  17.075  1.00 29.34           C
ANISOU 3488  CD1 ILE B  86     3179   2798   5169   -151    187    328       C
ATOM   3489  N   TRP B  87     -76.001  22.624  15.897  1.00 27.74           N
ANISOU 3489  N   TRP B  87     3023   2708   4807   -116    132    266       N
ATOM   3490  CA  TRP B  87     -75.861  24.060  15.712  1.00 24.54           C
ANISOU 3490  CA  TRP B  87     2647   2314   4362   -106    100    259       C
ATOM   3491  C   TRP B  87     -74.753  24.594  16.609  1.00 29.66           C
ANISOU 3491  C   TRP B  87     3348   2931   4993   -106     40    286       C
ATOM   3492  O   TRP B  87     -74.771  24.381  17.825  1.00 31.11           O
ANISOU 3492  O   TRP B  87     3583   3092   5145    -91     30    305       O
ATOM   3493  CB  TRP B  87     -77.178  24.777  16.010  1.00 22.03           C
ANISOU 3493  CB  TRP B  87     2357   2018   3996    -76    126    252       C
ATOM   3494  CG  TRP B  87     -77.156  26.209  15.595  1.00 21.80           C
ANISOU 3494  CG  TRP B  87     2357   1995   3931    -64     96    238       C
ATOM   3495  CD1 TRP B  87     -76.990  27.295  16.401  1.00 19.51           C
ANISOU 3495  CD1 TRP B  87     2150   1679   3586    -37     57    243       C
ATOM   3496  CD2 TRP B  87     -77.284  26.713  14.262  1.00 20.88           C
ANISOU 3496  CD2 TRP B  87     2200   1904   3830    -75     94    218       C
ATOM   3497  NE1 TRP B  87     -77.016  28.446  15.654  1.00 25.98           N
ANISOU 3497  NE1 TRP B  87     2976   2500   4394    -36     31    230       N
ATOM   3498  CE2 TRP B  87     -77.196  28.116  14.336  1.00 22.27           C
ANISOU 3498  CE2 TRP B  87     2427   2068   3966    -58     58    218       C
ATOM   3499  CE3 TRP B  87     -77.472  26.114  13.012  1.00 22.51           C
ANISOU 3499  CE3 TRP B  87     2343   2137   4072    -93    115    198       C
ATOM   3500  CZ2 TRP B  87     -77.288  28.930  13.211  1.00 23.67           C
ANISOU 3500  CZ2 TRP B  87     2584   2264   4145    -62     48    209       C
ATOM   3501  CZ3 TRP B  87     -77.562  26.923  11.896  1.00 22.91           C
ANISOU 3501  CZ3 TRP B  87     2381   2212   4113    -91    106    185       C
ATOM   3502  CH2 TRP B  87     -77.469  28.316  12.002  1.00 26.97           C
ANISOU 3502  CH2 TRP B  87     2935   2718   4593    -77     76    195       C
ATOM   3503  N   ASP B  88     -73.787  25.282  16.002  1.00 25.47           N
ANISOU 3503  N   ASP B  88     2800   2395   4483   -126     -5    295       N
ATOM   3504  CA  ASP B  88     -72.692  25.909  16.738  1.00 25.16           C
ANISOU 3504  CA  ASP B  88     2799   2318   4442   -141    -86    329       C
ATOM   3505  C   ASP B  88     -73.162  27.293  17.164  1.00 27.27           C
ANISOU 3505  C   ASP B  88     3150   2564   4646   -126   -129    314       C
ATOM   3506  O   ASP B  88     -73.145  28.240  16.374  1.00 26.88           O
ANISOU 3506  O   ASP B  88     3090   2520   4603   -137   -146    310       O
ATOM   3507  CB  ASP B  88     -71.433  25.979  15.882  1.00 30.24           C
ANISOU 3507  CB  ASP B  88     3370   2965   5153   -171   -112    366       C
ATOM   3508  CG  ASP B  88     -70.186  26.295  16.692  1.00 37.03           C
ANISOU 3508  CG  ASP B  88     4244   3784   6040   -198   -204    419       C
ATOM   3509  OD1 ASP B  88     -70.305  26.903  17.777  1.00 38.69           O
ANISOU 3509  OD1 ASP B  88     4545   3954   6201   -198   -272    415       O
ATOM   3510  OD2 ASP B  88     -69.080  25.936  16.236  1.00 39.50           O
ANISOU 3510  OD2 ASP B  88     4479   4105   6425   -216   -213    469       O
ATOM   3511  N   TYR B  89     -73.589  27.411  18.422  1.00 28.75           N
ANISOU 3511  N   TYR B  89     3430   2726   4769    -94   -145    308       N
ATOM   3512  CA  TYR B  89     -74.093  28.685  18.918  1.00 28.91           C
ANISOU 3512  CA  TYR B  89     3553   2718   4714    -60   -182    288       C
ATOM   3513  C   TYR B  89     -72.987  29.708  19.134  1.00 33.64           C
ANISOU 3513  C   TYR B  89     4205   3256   5321    -96   -305    304       C
ATOM   3514  O   TYR B  89     -73.272  30.911  19.149  1.00 38.65           O
ANISOU 3514  O   TYR B  89     4914   3857   5913    -80   -348    285       O
ATOM   3515  CB  TYR B  89     -74.873  28.468  20.213  1.00 27.84           C
ANISOU 3515  CB  TYR B  89     3512   2574   4492      2   -152    280       C
ATOM   3516  CG  TYR B  89     -76.234  27.851  19.997  1.00 31.67           C
ANISOU 3516  CG  TYR B  89     3948   3116   4969     41    -35    275       C
ATOM   3517  CD1 TYR B  89     -77.369  28.644  19.914  1.00 34.30           C
ANISOU 3517  CD1 TYR B  89     4314   3468   5250     96     10    258       C
ATOM   3518  CD2 TYR B  89     -76.384  26.476  19.864  1.00 31.51           C
ANISOU 3518  CD2 TYR B  89     3845   3125   5001     20     24    294       C
ATOM   3519  CE1 TYR B  89     -78.617  28.089  19.714  1.00 34.37           C
ANISOU 3519  CE1 TYR B  89     4260   3531   5267    126    109    269       C
ATOM   3520  CE2 TYR B  89     -77.629  25.911  19.665  1.00 28.64           C
ANISOU 3520  CE2 TYR B  89     3430   2806   4647     42    115    301       C
ATOM   3521  CZ  TYR B  89     -78.741  26.723  19.590  1.00 33.15           C
ANISOU 3521  CZ  TYR B  89     4020   3402   5174     92    156    293       C
ATOM   3522  OH  TYR B  89     -79.985  26.170  19.391  1.00 35.50           O
ANISOU 3522  OH  TYR B  89     4247   3746   5494    108    240    314       O
ATOM   3523  N   LYS B  90     -71.737  29.268  19.306  1.00 35.53           N
ANISOU 3523  N   LYS B  90     4405   3475   5620   -145   -369    346       N
ATOM   3524  CA  LYS B  90     -70.640  30.219  19.427  1.00 38.49           C
ANISOU 3524  CA  LYS B  90     4806   3790   6027   -194   -499    379       C
ATOM   3525  C   LYS B  90     -70.277  30.839  18.087  1.00 37.73           C
ANISOU 3525  C   LYS B  90     4618   3713   6003   -235   -495    404       C
ATOM   3526  O   LYS B  90     -69.688  31.924  18.054  1.00 43.69           O
ANISOU 3526  O   LYS B  90     5403   4415   6780   -274   -596    430       O
ATOM   3527  CB  LYS B  90     -69.416  29.542  20.039  1.00 45.94           C
ANISOU 3527  CB  LYS B  90     5721   4712   7024   -233   -571    431       C
ATOM   3528  CG  LYS B  90     -69.613  29.133  21.482  1.00 53.06           C
ANISOU 3528  CG  LYS B  90     6736   5580   7843   -195   -604    415       C
ATOM   3529  CD  LYS B  90     -68.300  28.756  22.132  1.00 58.28           C
ANISOU 3529  CD  LYS B  90     7382   6205   8556   -240   -714    472       C
ATOM   3530  CE  LYS B  90     -68.448  28.695  23.638  1.00 61.83           C
ANISOU 3530  CE  LYS B  90     7985   6607   8902   -201   -780    454       C
ATOM   3531  NZ  LYS B  90     -69.573  27.808  24.043  1.00 63.53           N
ANISOU 3531  NZ  LYS B  90     8229   6868   9041   -128   -647    422       N
ATOM   3532  N   ARG B  91     -70.614  30.172  16.987  1.00 31.83           N
ANISOU 3532  N   ARG B  91     3769   3036   5291   -226   -387    401       N
ATOM   3533  CA  ARG B  91     -70.418  30.707  15.652  1.00 27.64           C
ANISOU 3533  CA  ARG B  91     3160   2534   4809   -248   -364    424       C
ATOM   3534  C   ARG B  91     -71.718  31.133  14.988  1.00 31.26           C
ANISOU 3534  C   ARG B  91     3640   3025   5214   -208   -294    371       C
ATOM   3535  O   ARG B  91     -71.671  31.740  13.912  1.00 36.65           O
ANISOU 3535  O   ARG B  91     4278   3728   5921   -220   -281    388       O
ATOM   3536  CB  ARG B  91     -69.714  29.670  14.763  1.00 28.10           C
ANISOU 3536  CB  ARG B  91     3092   2645   4938   -257   -298    462       C
ATOM   3537  CG  ARG B  91     -68.258  29.427  15.122  1.00 30.95           C
ANISOU 3537  CG  ARG B  91     3398   2984   5378   -298   -366    540       C
ATOM   3538  CD  ARG B  91     -67.683  28.234  14.365  1.00 36.19           C
ANISOU 3538  CD  ARG B  91     3952   3701   6098   -280   -281    572       C
ATOM   3539  NE  ARG B  91     -67.998  28.272  12.939  1.00 40.55           N
ANISOU 3539  NE  ARG B  91     4450   4308   6650   -256   -192    563       N
ATOM   3540  CZ  ARG B  91     -68.856  27.452  12.338  1.00 35.63           C
ANISOU 3540  CZ  ARG B  91     3829   3723   5987   -212   -100    502       C
ATOM   3541  NH1 ARG B  91     -69.083  27.564  11.037  1.00 35.41           N
ANISOU 3541  NH1 ARG B  91     3766   3739   5948   -188    -37    495       N
ATOM   3542  NH2 ARG B  91     -69.483  26.515  13.037  1.00 32.66           N
ANISOU 3542  NH2 ARG B  91     3493   3336   5582   -194    -80    452       N
ATOM   3543  N   ASP B  92     -72.867  30.843  15.603  1.00 31.69           N
ANISOU 3543  N   ASP B  92     3754   3086   5199   -159   -249    320       N
ATOM   3544  CA  ASP B  92     -74.178  31.094  15.005  1.00 33.94           C
ANISOU 3544  CA  ASP B  92     4040   3410   5444   -118   -179    281       C
ATOM   3545  C   ASP B  92     -74.248  30.490  13.604  1.00 30.12           C
ANISOU 3545  C   ASP B  92     3452   2987   5005   -130   -113    282       C
ATOM   3546  O   ASP B  92     -74.678  31.126  12.640  1.00 32.65           O
ANISOU 3546  O   ASP B  92     3754   3332   5320   -124    -96    276       O
ATOM   3547  CB  ASP B  92     -74.498  32.590  14.984  1.00 40.32           C
ANISOU 3547  CB  ASP B  92     4925   4181   6216   -103   -228    272       C
ATOM   3548  CG  ASP B  92     -74.600  33.184  16.377  1.00 50.02           C
ANISOU 3548  CG  ASP B  92     6288   5341   7377    -71   -292    255       C
ATOM   3549  OD1 ASP B  92     -75.102  32.491  17.287  1.00 54.55           O
ANISOU 3549  OD1 ASP B  92     6899   5924   7904    -30   -253    238       O
ATOM   3550  OD2 ASP B  92     -74.175  34.344  16.564  1.00 53.76           O
ANISOU 3550  OD2 ASP B  92     6837   5748   7840    -84   -383    262       O
ATOM   3551  N   ALA B  93     -73.813  29.239  13.503  1.00 24.84           N
ANISOU 3551  N   ALA B  93     2725   2338   4373   -142    -78    290       N
ATOM   3552  CA  ALA B  93     -73.688  28.559  12.223  1.00 23.96           C
ANISOU 3552  CA  ALA B  93     2536   2273   4296   -144    -24    288       C
ATOM   3553  C   ALA B  93     -73.728  27.061  12.473  1.00 23.19           C
ANISOU 3553  C   ALA B  93     2412   2182   4218   -138     17    274       C
ATOM   3554  O   ALA B  93     -73.481  26.612  13.598  1.00 26.09           O
ANISOU 3554  O   ALA B  93     2806   2519   4587   -142     -2    286       O
ATOM   3555  CB  ALA B  93     -72.385  28.956  11.510  1.00 25.98           C
ANISOU 3555  CB  ALA B  93     2741   2531   4598   -168    -47    344       C
ATOM   3556  N   PRO B  94     -74.050  26.262  11.456  1.00 24.71           N
ANISOU 3556  N   PRO B  94     2563   2404   4420   -128     67    249       N
ATOM   3557  CA  PRO B  94     -73.983  24.807  11.627  1.00 23.82           C
ANISOU 3557  CA  PRO B  94     2433   2283   4334   -124     96    237       C
ATOM   3558  C   PRO B  94     -72.561  24.372  11.940  1.00 27.22           C
ANISOU 3558  C   PRO B  94     2840   2695   4808   -127     83    282       C
ATOM   3559  O   PRO B  94     -71.592  24.919  11.410  1.00 31.62           O
ANISOU 3559  O   PRO B  94     3365   3264   5386   -129     73    322       O
ATOM   3560  CB  PRO B  94     -74.452  24.265  10.272  1.00 22.32           C
ANISOU 3560  CB  PRO B  94     2222   2120   4141   -109    133    199       C
ATOM   3561  CG  PRO B  94     -75.225  25.380   9.658  1.00 25.07           C
ANISOU 3561  CG  PRO B  94     2577   2496   4451   -107    125    185       C
ATOM   3562  CD  PRO B  94     -74.560  26.635  10.125  1.00 24.13           C
ANISOU 3562  CD  PRO B  94     2472   2369   4328   -116     90    227       C
ATOM   3563  N   ALA B  95     -72.440  23.380  12.822  1.00 24.57           N
ANISOU 3563  N   ALA B  95     2513   2332   4492   -128     85    287       N
ATOM   3564  CA  ALA B  95     -71.119  22.888  13.184  1.00 21.99           C
ANISOU 3564  CA  ALA B  95     2157   1986   4210   -127     69    336       C
ATOM   3565  C   ALA B  95     -70.449  22.134  12.044  1.00 24.50           C
ANISOU 3565  C   ALA B  95     2427   2320   4560    -96    118    340       C
ATOM   3566  O   ALA B  95     -69.231  21.935  12.083  1.00 26.92           O
ANISOU 3566  O   ALA B  95     2690   2626   4911    -85    115    396       O
ATOM   3567  CB  ALA B  95     -71.208  21.994  14.421  1.00 21.33           C
ANISOU 3567  CB  ALA B  95     2102   1868   4134   -130     59    343       C
ATOM   3568  N   HIS B  96     -71.206  21.720  11.031  1.00 24.59           N
ANISOU 3568  N   HIS B  96     2449   2347   4548    -76    160    286       N
ATOM   3569  CA  HIS B  96     -70.668  20.935   9.933  1.00 28.90           C
ANISOU 3569  CA  HIS B  96     2977   2901   5101    -28    209    277       C
ATOM   3570  C   HIS B  96     -71.170  21.485   8.605  1.00 33.58           C
ANISOU 3570  C   HIS B  96     3580   3532   5648     -9    231    243       C
ATOM   3571  O   HIS B  96     -72.224  22.121   8.525  1.00 38.79           O
ANISOU 3571  O   HIS B  96     4262   4202   6274    -36    210    210       O
ATOM   3572  CB  HIS B  96     -71.040  19.455  10.076  1.00 29.43           C
ANISOU 3572  CB  HIS B  96     3075   2925   5184    -13    225    236       C
ATOM   3573  CG  HIS B  96     -70.654  18.866  11.396  1.00 27.94           C
ANISOU 3573  CG  HIS B  96     2881   2698   5035    -30    204    272       C
ATOM   3574  ND1 HIS B  96     -71.581  18.496  12.346  1.00 25.36           N
ANISOU 3574  ND1 HIS B  96     2584   2342   4708    -64    184    256       N
ATOM   3575  CD2 HIS B  96     -69.439  18.605  11.934  1.00 24.96           C
ANISOU 3575  CD2 HIS B  96     2470   2311   4700    -14    199    332       C
ATOM   3576  CE1 HIS B  96     -70.955  18.020  13.407  1.00 25.30           C
ANISOU 3576  CE1 HIS B  96     2574   2308   4731    -66    168    300       C
ATOM   3577  NE2 HIS B  96     -69.654  18.075  13.183  1.00 28.34           N
ANISOU 3577  NE2 HIS B  96     2920   2702   5145    -39    171    344       N
ATOM   3578  N   ILE B  97     -70.391  21.222   7.555  1.00 37.53           N
ANISOU 3578  N   ILE B  97     4065   4054   6140     46    279    257       N
ATOM   3579  CA  ILE B  97     -70.681  21.789   6.241  1.00 45.87           C
ANISOU 3579  CA  ILE B  97     5135   5151   7141     76    305    237       C
ATOM   3580  C   ILE B  97     -71.887  21.099   5.614  1.00 47.73           C
ANISOU 3580  C   ILE B  97     5437   5369   7331     84    295    146       C
ATOM   3581  O   ILE B  97     -72.916  21.730   5.341  1.00 48.50           O
ANISOU 3581  O   ILE B  97     5551   5481   7396     55    265    114       O
ATOM   3582  CB  ILE B  97     -69.444  21.691   5.331  1.00 54.65           C
ANISOU 3582  CB  ILE B  97     6215   6298   8252    149    371    292       C
ATOM   3583  CG1 ILE B  97     -68.261  22.429   5.960  1.00 59.94           C
ANISOU 3583  CG1 ILE B  97     6802   6986   8988    126    365    400       C
ATOM   3584  CG2 ILE B  97     -69.752  22.238   3.945  1.00 57.73           C
ANISOU 3584  CG2 ILE B  97     6632   6733   8569    190    404    275       C
ATOM   3585  CD1 ILE B  97     -68.522  23.900   6.211  1.00 64.00           C
ANISOU 3585  CD1 ILE B  97     7297   7514   9505     63    314    433       C
ATOM   3586  N   SER B  98     -71.776  19.799   5.372  1.00 39.20           N
ANISOU 3586  N   SER B  98     4394   4249   6252    122    312    106       N
ATOM   3587  CA  SER B  98     -72.812  19.037   4.694  1.00 31.82           C
ANISOU 3587  CA  SER B  98     3529   3281   5280    127    286     21       C
ATOM   3588  C   SER B  98     -73.739  18.369   5.703  1.00 28.20           C
ANISOU 3588  C   SER B  98     3075   2768   4870     61    236     -4       C
ATOM   3589  O   SER B  98     -73.498  18.369   6.913  1.00 25.46           O
ANISOU 3589  O   SER B  98     2690   2410   4573     28    233     40       O
ATOM   3590  CB  SER B  98     -72.184  17.990   3.770  1.00 36.71           C
ANISOU 3590  CB  SER B  98     4209   3874   5865    214    325    -13       C
ATOM   3591  OG  SER B  98     -71.314  18.599   2.833  1.00 38.18           O
ANISOU 3591  OG  SER B  98     4385   4120   6002    288    388     26       O
ATOM   3592  N   THR B  99     -74.820  17.793   5.182  1.00 30.55           N
ANISOU 3592  N   THR B  99     3420   3033   5154     43    191    -69       N
ATOM   3593  CA  THR B  99     -75.808  17.092   5.987  1.00 30.89           C
ANISOU 3593  CA  THR B  99     3460   3025   5252    -22    144    -81       C
ATOM   3594  C   THR B  99     -76.095  15.732   5.366  1.00 30.85           C
ANISOU 3594  C   THR B  99     3527   2943   5252    -10    107   -145       C
ATOM   3595  O   THR B  99     -75.685  15.434   4.240  1.00 34.02           O
ANISOU 3595  O   THR B  99     3997   3334   5596     54    114   -192       O
ATOM   3596  CB  THR B  99     -77.110  17.897   6.115  1.00 30.83           C
ANISOU 3596  CB  THR B  99     3418   3050   5245    -80    106    -78       C
ATOM   3597  OG1 THR B  99     -77.604  18.223   4.810  1.00 34.89           O
ANISOU 3597  OG1 THR B  99     3967   3585   5703    -63     77   -126       O
ATOM   3598  CG2 THR B  99     -76.876  19.179   6.900  1.00 31.13           C
ANISOU 3598  CG2 THR B  99     3404   3145   5280    -89    135    -20       C
ATOM   3599  N   ILE B 100     -76.808  14.900   6.120  1.00 29.42           N
ANISOU 3599  N   ILE B 100     3338   2702   5137    -70     67   -142       N
ATOM   3600  CA  ILE B 100     -77.232  13.580   5.670  1.00 29.77           C
ANISOU 3600  CA  ILE B 100     3453   2652   5205    -79      9   -197       C
ATOM   3601  C   ILE B 100     -78.728  13.475   5.924  1.00 31.77           C
ANISOU 3601  C   ILE B 100     3671   2886   5514   -172    -64   -191       C
ATOM   3602  O   ILE B 100     -79.159  13.400   7.081  1.00 30.93           O
ANISOU 3602  O   ILE B 100     3499   2779   5475   -226    -55   -130       O
ATOM   3603  CB  ILE B 100     -76.480  12.447   6.381  1.00 31.74           C
ANISOU 3603  CB  ILE B 100     3724   2830   5505    -60     31   -181       C
ATOM   3604  CG1 ILE B 100     -74.990  12.494   6.037  1.00 33.12           C
ANISOU 3604  CG1 ILE B 100     3924   3028   5634     42    104   -177       C
ATOM   3605  CG2 ILE B 100     -77.070  11.099   5.997  1.00 27.87           C
ANISOU 3605  CG2 ILE B 100     3311   2226   5051    -84    -46   -236       C
ATOM   3606  CD1 ILE B 100     -74.157  11.474   6.784  1.00 27.01           C
ANISOU 3606  CD1 ILE B 100     3159   2192   4911     71    131   -150       C
ATOM   3607  N   GLY B 101     -79.517  13.473   4.854  1.00 32.65           N
ANISOU 3607  N   GLY B 101     3823   2984   5597   -187   -136   -246       N
ATOM   3608  CA  GLY B 101     -80.960  13.345   4.990  1.00 37.04           C
ANISOU 3608  CA  GLY B 101     4331   3522   6219   -278   -216   -230       C
ATOM   3609  C   GLY B 101     -81.604  14.451   5.796  1.00 38.59           C
ANISOU 3609  C   GLY B 101     4417   3806   6440   -315   -177   -154       C
ATOM   3610  O   GLY B 101     -82.494  14.182   6.614  1.00 39.59           O
ANISOU 3610  O   GLY B 101     4473   3921   6649   -381   -194    -96       O
ATOM   3611  N   VAL B 102     -81.175  15.695   5.588  1.00 38.89           N
ANISOU 3611  N   VAL B 102     4440   3930   6407   -267   -124   -149       N
ATOM   3612  CA  VAL B 102     -81.702  16.827   6.344  1.00 33.22           C
ANISOU 3612  CA  VAL B 102     3637   3287   5697   -283    -85    -85       C
ATOM   3613  C   VAL B 102     -82.225  17.896   5.394  1.00 30.49           C
ANISOU 3613  C   VAL B 102     3286   3003   5298   -270   -109   -104       C
ATOM   3614  O   VAL B 102     -83.421  18.206   5.389  1.00 36.61           O
ANISOU 3614  O   VAL B 102     4003   3799   6106   -312   -148    -78       O
ATOM   3615  CB  VAL B 102     -80.634  17.413   7.286  1.00 36.26           C
ANISOU 3615  CB  VAL B 102     4010   3706   6060   -243     -1    -45       C
ATOM   3616  CG1 VAL B 102     -81.187  18.626   8.011  1.00 38.23           C
ANISOU 3616  CG1 VAL B 102     4201   4023   6302   -248     31      8       C
ATOM   3617  CG2 VAL B 102     -80.162  16.362   8.279  1.00 37.54           C
ANISOU 3617  CG2 VAL B 102     4176   3811   6275   -255     19    -18       C
ATOM   3618  N   CYS B 103     -81.334  18.470   4.588  1.00 28.96           N
ANISOU 3618  N   CYS B 103     3143   2839   5023   -209    -83   -139       N
ATOM   3619  CA  CYS B 103     -81.673  19.565   3.689  1.00 28.83           C
ANISOU 3619  CA  CYS B 103     3126   2882   4944   -188    -97   -150       C
ATOM   3620  C   CYS B 103     -81.173  19.247   2.289  1.00 32.13           C
ANISOU 3620  C   CYS B 103     3636   3285   5286   -138   -124   -216       C
ATOM   3621  O   CYS B 103     -80.005  18.888   2.114  1.00 36.94           O
ANISOU 3621  O   CYS B 103     4296   3880   5861    -83    -75   -232       O
ATOM   3622  CB  CYS B 103     -81.068  20.885   4.176  1.00 31.43           C
ANISOU 3622  CB  CYS B 103     3424   3276   5244   -155    -27   -103       C
ATOM   3623  SG  CYS B 103     -81.149  22.235   2.978  1.00 40.63           S
ANISOU 3623  SG  CYS B 103     4604   4507   6327   -115    -32   -111       S
ATOM   3624  N   SER B 104     -82.053  19.403   1.296  1.00 31.75           N
ANISOU 3624  N   SER B 104     3611   3245   5207   -149   -199   -250       N
ATOM   3625  CA  SER B 104     -81.700  19.065  -0.080  1.00 38.31           C
ANISOU 3625  CA  SER B 104     4550   4058   5947    -93   -233   -319       C
ATOM   3626  C   SER B 104     -80.497  19.857  -0.572  1.00 38.77           C
ANISOU 3626  C   SER B 104     4637   4174   5918     -8   -142   -306       C
ATOM   3627  O   SER B 104     -79.708  19.351  -1.378  1.00 41.50           O
ANISOU 3627  O   SER B 104     5075   4502   6193     64   -121   -348       O
ATOM   3628  CB  SER B 104     -82.895  19.311  -1.000  1.00 46.72           C
ANISOU 3628  CB  SER B 104     5630   5133   6990   -122   -338   -347       C
ATOM   3629  OG  SER B 104     -84.070  18.721  -0.474  1.00 61.37           O
ANISOU 3629  OG  SER B 104     7426   6944   8947   -212   -422   -332       O
ATOM   3630  N   MET B 105     -80.336  21.094  -0.100  1.00 36.64           N
ANISOU 3630  N   MET B 105     4294   3971   5655     -9    -87   -243       N
ATOM   3631  CA  MET B 105     -79.250  21.934  -0.592  1.00 37.06           C
ANISOU 3631  CA  MET B 105     4362   4079   5643     59    -10   -213       C
ATOM   3632  C   MET B 105     -77.896  21.507  -0.040  1.00 35.81           C
ANISOU 3632  C   MET B 105     4197   3905   5503     94     70   -186       C
ATOM   3633  O   MET B 105     -76.877  21.666  -0.721  1.00 40.14           O
ANISOU 3633  O   MET B 105     4777   4481   5995    167    131   -170       O
ATOM   3634  CB  MET B 105     -79.528  23.397  -0.252  1.00 35.86           C
ANISOU 3634  CB  MET B 105     4139   3985   5500     38      8   -153       C
ATOM   3635  CG  MET B 105     -80.134  24.162  -1.406  1.00 37.59           C
ANISOU 3635  CG  MET B 105     4386   4248   5648     61    -29   -164       C
ATOM   3636  SD  MET B 105     -79.078  24.028  -2.859  1.00 44.75           S
ANISOU 3636  SD  MET B 105     5388   5177   6436    160     17   -182       S
ATOM   3637  CE  MET B 105     -80.148  24.685  -4.122  1.00 45.15           C
ANISOU 3637  CE  MET B 105     5484   5266   6405    173    -59   -207       C
ATOM   3638  N   THR B 106     -77.858  20.963   1.176  1.00 31.52           N
ANISOU 3638  N   THR B 106     3611   3322   5041     49     72   -169       N
ATOM   3639  CA  THR B 106     -76.603  20.573   1.803  1.00 32.25           C
ANISOU 3639  CA  THR B 106     3690   3400   5163     77    137   -135       C
ATOM   3640  C   THR B 106     -76.417  19.067   1.917  1.00 33.24           C
ANISOU 3640  C   THR B 106     3866   3452   5312     90    125   -179       C
ATOM   3641  O   THR B 106     -75.342  18.627   2.340  1.00 34.13           O
ANISOU 3641  O   THR B 106     3971   3551   5447    125    179   -151       O
ATOM   3642  CB  THR B 106     -76.490  21.193   3.203  1.00 29.30           C
ANISOU 3642  CB  THR B 106     3238   3038   4856     27    152    -72       C
ATOM   3643  OG1 THR B 106     -77.598  20.768   4.005  1.00 27.44           O
ANISOU 3643  OG1 THR B 106     2984   2770   4674    -36    105    -85       O
ATOM   3644  CG2 THR B 106     -76.489  22.706   3.112  1.00 28.86           C
ANISOU 3644  CG2 THR B 106     3147   3041   4779     23    163    -27       C
ATOM   3645  N   ASP B 107     -77.420  18.270   1.561  1.00 33.98           N
ANISOU 3645  N   ASP B 107     4009   3494   5409     60     49   -242       N
ATOM   3646  CA  ASP B 107     -77.300  16.824   1.684  1.00 29.58           C
ANISOU 3646  CA  ASP B 107     3510   2849   4881     66     25   -284       C
ATOM   3647  C   ASP B 107     -76.291  16.282   0.685  1.00 32.37           C
ANISOU 3647  C   ASP B 107     3958   3186   5155    173     68   -323       C
ATOM   3648  O   ASP B 107     -76.350  16.592  -0.509  1.00 38.30           O
ANISOU 3648  O   ASP B 107     4776   3963   5814    228     61   -360       O
ATOM   3649  CB  ASP B 107     -78.652  16.149   1.466  1.00 32.51           C
ANISOU 3649  CB  ASP B 107     3913   3159   5282     -2    -85   -336       C
ATOM   3650  CG  ASP B 107     -79.457  16.032   2.740  1.00 38.06           C
ANISOU 3650  CG  ASP B 107     4526   3846   6090    -96   -109   -286       C
ATOM   3651  OD1 ASP B 107     -78.972  16.488   3.795  1.00 39.91           O
ANISOU 3651  OD1 ASP B 107     4691   4115   6358   -102    -44   -224       O
ATOM   3652  OD2 ASP B 107     -80.577  15.483   2.682  1.00 40.88           O
ANISOU 3652  OD2 ASP B 107     4882   4155   6496   -162   -197   -304       O
ATOM   3653  N   ILE B 108     -75.353  15.477   1.182  1.00 30.66           N
ANISOU 3653  N   ILE B 108     3750   2928   4970    214    117   -309       N
ATOM   3654  CA  ILE B 108     -74.550  14.633   0.308  1.00 30.58           C
ANISOU 3654  CA  ILE B 108     3846   2879   4893    325    152   -355       C
ATOM   3655  C   ILE B 108     -75.148  13.237   0.188  1.00 35.54           C
ANISOU 3655  C   ILE B 108     4577   3387   5539    310     65   -436       C
ATOM   3656  O   ILE B 108     -74.772  12.486  -0.724  1.00 35.99           O
ANISOU 3656  O   ILE B 108     4761   3392   5521    405     66   -501       O
ATOM   3657  CB  ILE B 108     -73.099  14.539   0.809  1.00 30.23           C
ANISOU 3657  CB  ILE B 108     3752   2858   4874    394    258   -285       C
ATOM   3658  CG1 ILE B 108     -73.068  13.935   2.212  1.00 26.89           C
ANISOU 3658  CG1 ILE B 108     3271   2385   4562    326    242   -251       C
ATOM   3659  CG2 ILE B 108     -72.443  15.911   0.799  1.00 24.71           C
ANISOU 3659  CG2 ILE B 108     2958   2268   4162    407    330   -199       C
ATOM   3660  CD1 ILE B 108     -71.679  13.744   2.753  1.00 27.69           C
ANISOU 3660  CD1 ILE B 108     3321   2501   4698    390    327   -181       C
ATOM   3661  N   ALA B 109     -76.068  12.877   1.079  1.00 35.49           N
ANISOU 3661  N   ALA B 109     4524   3331   5628    197     -9   -430       N
ATOM   3662  CA  ALA B 109     -76.719  11.577   1.072  1.00 33.03           C
ANISOU 3662  CA  ALA B 109     4294   2897   5359    158   -106   -491       C
ATOM   3663  C   ALA B 109     -77.964  11.665   1.940  1.00 34.17           C
ANISOU 3663  C   ALA B 109     4347   3030   5607     20   -181   -454       C
ATOM   3664  O   ALA B 109     -78.095  12.560   2.777  1.00 36.91           O
ANISOU 3664  O   ALA B 109     4575   3455   5993    -26   -136   -381       O
ATOM   3665  CB  ALA B 109     -75.787  10.475   1.583  1.00 31.52           C
ANISOU 3665  CB  ALA B 109     4141   2630   5204    213    -62   -487       C
ATOM   3666  N   LYS B 110     -78.881  10.726   1.724  1.00 39.98           N
ANISOU 3666  N   LYS B 110     5142   3664   6387    -41   -298   -502       N
ATOM   3667  CA  LYS B 110     -80.057  10.619   2.573  1.00 40.20           C
ANISOU 3667  CA  LYS B 110     5074   3673   6529   -170   -364   -450       C
ATOM   3668  C   LYS B 110     -79.855   9.638   3.717  1.00 39.81           C
ANISOU 3668  C   LYS B 110     4997   3548   6580   -207   -350   -404       C
ATOM   3669  O   LYS B 110     -80.520   9.763   4.751  1.00 39.06           O
ANISOU 3669  O   LYS B 110     4792   3472   6576   -292   -349   -326       O
ATOM   3670  CB  LYS B 110     -81.272  10.200   1.741  1.00 44.18           C
ANISOU 3670  CB  LYS B 110     5632   4108   7047   -237   -515   -504       C
ATOM   3671  CG  LYS B 110     -81.122  10.475   0.255  1.00 53.41           C
ANISOU 3671  CG  LYS B 110     6925   5285   8084   -158   -554   -594       C
ATOM   3672  CD  LYS B 110     -82.402  11.030  -0.345  1.00 64.47           C
ANISOU 3672  CD  LYS B 110     8295   6711   9488   -233   -666   -601       C
ATOM   3673  CE  LYS B 110     -82.705  12.419   0.197  1.00 72.58           C
ANISOU 3673  CE  LYS B 110     9170   7876  10531   -258   -588   -516       C
ATOM   3674  NZ  LYS B 110     -83.856  13.055  -0.503  1.00 77.82           N
ANISOU 3674  NZ  LYS B 110     9806   8577  11186   -309   -686   -520       N
ATOM   3675  N   LYS B 111     -78.945   8.680   3.557  1.00 43.20           N
ANISOU 3675  N   LYS B 111     5526   3896   6992   -135   -333   -446       N
ATOM   3676  CA  LYS B 111     -78.637   7.685   4.567  1.00 44.94           C
ANISOU 3676  CA  LYS B 111     5736   4038   7301   -157   -320   -405       C
ATOM   3677  C   LYS B 111     -77.134   7.644   4.805  1.00 40.27           C
ANISOU 3677  C   LYS B 111     5164   3473   6666    -43   -205   -393       C
ATOM   3678  O   LYS B 111     -76.349   7.787   3.858  1.00 39.71           O
ANISOU 3678  O   LYS B 111     5171   3419   6497     66   -165   -447       O
ATOM   3679  CB  LYS B 111     -79.128   6.294   4.139  1.00 52.50           C
ANISOU 3679  CB  LYS B 111     6809   4834   8305   -190   -442   -467       C
ATOM   3680  CG  LYS B 111     -80.620   6.213   3.861  1.00 61.65           C
ANISOU 3680  CG  LYS B 111     7945   5953   9528   -314   -579   -469       C
ATOM   3681  CD  LYS B 111     -81.431   6.474   5.118  1.00 71.02           C
ANISOU 3681  CD  LYS B 111     8967   7184  10832   -426   -563   -351       C
ATOM   3682  CE  LYS B 111     -82.919   6.304   4.858  1.00 78.59           C
ANISOU 3682  CE  LYS B 111     9884   8101  11876   -550   -699   -333       C
ATOM   3683  NZ  LYS B 111     -83.731   6.545   6.084  1.00 80.99           N
ANISOU 3683  NZ  LYS B 111    10021   8456  12295   -645   -666   -203       N
ATOM   3684  N   PRO B 112     -76.700   7.455   6.054  1.00 36.46           N
ANISOU 3684  N   PRO B 112     4606   2996   6252    -61   -149   -314       N
ATOM   3685  CA  PRO B 112     -75.256   7.355   6.321  1.00 37.18           C
ANISOU 3685  CA  PRO B 112     4702   3107   6315     42    -52   -291       C
ATOM   3686  C   PRO B 112     -74.606   6.137   5.691  1.00 43.74           C
ANISOU 3686  C   PRO B 112     5666   3826   7128    134    -63   -355       C
ATOM   3687  O   PRO B 112     -73.380   6.127   5.525  1.00 49.34           O
ANISOU 3687  O   PRO B 112     6392   4561   7794    248     23   -347       O
ATOM   3688  CB  PRO B 112     -75.180   7.292   7.853  1.00 33.09           C
ANISOU 3688  CB  PRO B 112     4087   2602   5882    -16    -21   -194       C
ATOM   3689  CG  PRO B 112     -76.493   7.836   8.330  1.00 33.16           C
ANISOU 3689  CG  PRO B 112     4019   2647   5933   -130    -66   -158       C
ATOM   3690  CD  PRO B 112     -77.495   7.443   7.292  1.00 33.70           C
ANISOU 3690  CD  PRO B 112     4154   2650   5999   -170   -164   -231       C
ATOM   3691  N   THR B 113     -75.381   5.112   5.340  1.00 44.06           N
ANISOU 3691  N   THR B 113     5802   3736   7202     90   -168   -414       N
ATOM   3692  CA  THR B 113     -74.832   3.906   4.738  1.00 45.75           C
ANISOU 3692  CA  THR B 113     6167   3822   7393    182   -190   -486       C
ATOM   3693  C   THR B 113     -74.439   4.093   3.280  1.00 46.28           C
ANISOU 3693  C   THR B 113     6360   3898   7327    304   -179   -580       C
ATOM   3694  O   THR B 113     -73.783   3.209   2.719  1.00 53.20           O
ANISOU 3694  O   THR B 113     7372   4683   8157    419   -170   -640       O
ATOM   3695  CB  THR B 113     -75.840   2.760   4.845  1.00 51.24           C
ANISOU 3695  CB  THR B 113     6934   4360   8176     85   -327   -517       C
ATOM   3696  OG1 THR B 113     -77.120   3.204   4.374  1.00 49.44           O
ANISOU 3696  OG1 THR B 113     6689   4142   7954    -20   -429   -542       O
ATOM   3697  CG2 THR B 113     -75.962   2.293   6.285  1.00 53.02           C
ANISOU 3697  CG2 THR B 113     7061   4557   8527      1   -316   -416       C
ATOM   3698  N   GLU B 114     -74.821   5.204   2.657  1.00 41.70           N
ANISOU 3698  N   GLU B 114     5744   3424   6678    291   -175   -592       N
ATOM   3699  CA  GLU B 114     -74.495   5.422   1.257  1.00 41.36           C
ANISOU 3699  CA  GLU B 114     5823   3396   6495    409   -162   -674       C
ATOM   3700  C   GLU B 114     -72.983   5.522   1.069  1.00 41.86           C
ANISOU 3700  C   GLU B 114     5893   3518   6494    572    -13   -645       C
ATOM   3701  O   GLU B 114     -72.233   5.860   1.990  1.00 42.05           O
ANISOU 3701  O   GLU B 114     5788   3611   6576    575     79   -550       O
ATOM   3702  CB  GLU B 114     -75.187   6.681   0.736  1.00 41.27           C
ANISOU 3702  CB  GLU B 114     5753   3497   6432    358   -180   -672       C
ATOM   3703  CG  GLU B 114     -76.705   6.625   0.840  1.00 50.01           C
ANISOU 3703  CG  GLU B 114     6839   4554   7606    204   -326   -689       C
ATOM   3704  CD  GLU B 114     -77.387   7.800   0.168  1.00 58.99           C
ANISOU 3704  CD  GLU B 114     7938   5793   8682    173   -352   -696       C
ATOM   3705  OE1 GLU B 114     -76.772   8.413  -0.731  1.00 63.75           O
ANISOU 3705  OE1 GLU B 114     8591   6467   9163    281   -286   -722       O
ATOM   3706  OE2 GLU B 114     -78.537   8.114   0.542  1.00 60.01           O
ANISOU 3706  OE2 GLU B 114     7982   5932   8886     43   -433   -666       O
ATOM   3707  N   THR B 115     -72.543   5.214  -0.154  1.00 42.03           N
ANISOU 3707  N   THR B 115     6070   3510   6392    715      8   -724       N
ATOM   3708  CA  THR B 115     -71.115   5.119  -0.442  1.00 46.47           C
ANISOU 3708  CA  THR B 115     6652   4114   6892    891    154   -694       C
ATOM   3709  C   THR B 115     -70.386   6.425  -0.148  1.00 48.97           C
ANISOU 3709  C   THR B 115     6793   4603   7210    902    278   -581       C
ATOM   3710  O   THR B 115     -69.226   6.407   0.284  1.00 48.77           O
ANISOU 3710  O   THR B 115     6693   4624   7215    984    390   -500       O
ATOM   3711  CB  THR B 115     -70.908   4.714  -1.904  1.00 50.81           C
ANISOU 3711  CB  THR B 115     7406   4615   7284   1051    159   -798       C
ATOM   3712  OG1 THR B 115     -71.673   3.535  -2.185  1.00 54.76           O
ANISOU 3712  OG1 THR B 115     8083   4937   7785   1024     13   -910       O
ATOM   3713  CG2 THR B 115     -69.443   4.429  -2.187  1.00 55.89           C
ANISOU 3713  CG2 THR B 115     8077   5289   7870   1252    319   -760       C
ATOM   3714  N   ILE B 116     -71.052   7.563  -0.356  1.00 50.04           N
ANISOU 3714  N   ILE B 116     6859   4831   7324    818    251   -569       N
ATOM   3715  CA  ILE B 116     -70.395   8.856  -0.222  1.00 45.28           C
ANISOU 3715  CA  ILE B 116     6110   4378   6714    829    355   -468       C
ATOM   3716  C   ILE B 116     -69.972   9.143   1.216  1.00 42.61           C
ANISOU 3716  C   ILE B 116     5605   4080   6503    748    385   -362       C
ATOM   3717  O   ILE B 116     -69.039   9.924   1.440  1.00 39.50           O
ANISOU 3717  O   ILE B 116     5099   3786   6121    784    478   -266       O
ATOM   3718  CB  ILE B 116     -71.325   9.961  -0.763  1.00 43.10           C
ANISOU 3718  CB  ILE B 116     5814   4174   6389    754    303   -487       C
ATOM   3719  CG1 ILE B 116     -70.561  11.274  -0.953  1.00 43.21           C
ANISOU 3719  CG1 ILE B 116     5714   4332   6371    794    412   -392       C
ATOM   3720  CG2 ILE B 116     -72.514  10.158   0.158  1.00 38.80           C
ANISOU 3720  CG2 ILE B 116     5192   3608   5943    578    196   -482       C
ATOM   3721  CD1 ILE B 116     -69.498  11.205  -2.026  1.00 50.07           C
ANISOU 3721  CD1 ILE B 116     6652   5241   7133    974    528   -383       C
ATOM   3722  N   CYS B 117     -70.620   8.524   2.200  1.00 40.98           N
ANISOU 3722  N   CYS B 117     5383   3794   6392    640    304   -368       N
ATOM   3723  CA  CYS B 117     -70.357   8.831   3.599  1.00 38.80           C
ANISOU 3723  CA  CYS B 117     4967   3555   6222    559    321   -273       C
ATOM   3724  C   CYS B 117     -69.258   7.976   4.213  1.00 42.80           C
ANISOU 3724  C   CYS B 117     5462   4020   6782    633    377   -224       C
ATOM   3725  O   CYS B 117     -68.888   8.212   5.368  1.00 44.05           O
ANISOU 3725  O   CYS B 117     5509   4210   7019    580    390   -139       O
ATOM   3726  CB  CYS B 117     -71.636   8.662   4.425  1.00 40.70           C
ANISOU 3726  CB  CYS B 117     5184   3744   6534    409    218   -285       C
ATOM   3727  SG  CYS B 117     -73.062   9.570   3.800  1.00 44.96           S
ANISOU 3727  SG  CYS B 117     5724   4325   7031    316    139   -333       S
ATOM   3728  N   ALA B 118     -68.731   6.998   3.476  1.00 44.72           N
ANISOU 3728  N   ALA B 118     5822   4191   6979    761    408   -274       N
ATOM   3729  CA  ALA B 118     -67.770   6.063   4.059  1.00 45.10           C
ANISOU 3729  CA  ALA B 118     5868   4185   7084    837    456   -231       C
ATOM   3730  C   ALA B 118     -66.484   6.731   4.534  1.00 42.47           C
ANISOU 3730  C   ALA B 118     5389   3962   6786    890    558   -106       C
ATOM   3731  O   ALA B 118     -66.078   6.481   5.682  1.00 42.72           O
ANISOU 3731  O   ALA B 118     5339   3983   6909    849    552    -34       O
ATOM   3732  CB  ALA B 118     -67.485   4.934   3.061  1.00 46.73           C
ANISOU 3732  CB  ALA B 118     6247   4288   7219    984    472   -317       C
ATOM   3733  N   PRO B 119     -65.796   7.567   3.744  1.00 41.99           N
ANISOU 3733  N   PRO B 119     5286   4005   6664    974    645    -66       N
ATOM   3734  CA  PRO B 119     -64.551   8.172   4.242  1.00 42.37           C
ANISOU 3734  CA  PRO B 119     5180   4150   6768   1009    727     69       C
ATOM   3735  C   PRO B 119     -64.758   9.258   5.286  1.00 41.44           C
ANISOU 3735  C   PRO B 119     4924   4102   6720    860    677    143       C
ATOM   3736  O   PRO B 119     -63.766   9.795   5.793  1.00 40.21           O
ANISOU 3736  O   PRO B 119     4639   4016   6622    869    718    257       O
ATOM   3737  CB  PRO B 119     -63.914   8.750   2.971  1.00 42.08           C
ANISOU 3737  CB  PRO B 119     5147   4200   6642   1137    832     92       C
ATOM   3738  CG  PRO B 119     -65.063   9.057   2.100  1.00 41.09           C
ANISOU 3738  CG  PRO B 119     5133   4061   6420   1100    777    -18       C
ATOM   3739  CD  PRO B 119     -66.062   7.965   2.348  1.00 42.22           C
ANISOU 3739  CD  PRO B 119     5403   4066   6571   1045    672   -131       C
ATOM   3740  N   LEU B 120     -65.997   9.596   5.630  1.00 42.13           N
ANISOU 3740  N   LEU B 120     5034   4169   6805    730    586     85       N
ATOM   3741  CA  LEU B 120     -66.286  10.668   6.569  1.00 35.37           C
ANISOU 3741  CA  LEU B 120     4072   3373   5994    604    540    143       C
ATOM   3742  C   LEU B 120     -66.620  10.108   7.946  1.00 34.14           C
ANISOU 3742  C   LEU B 120     3900   3157   5915    519    477    160       C
ATOM   3743  O   LEU B 120     -67.223   9.039   8.075  1.00 37.35           O
ANISOU 3743  O   LEU B 120     4390   3468   6334    509    440    100       O
ATOM   3744  CB  LEU B 120     -67.448  11.529   6.070  1.00 30.20           C
ANISOU 3744  CB  LEU B 120     3443   2748   5282    527    495     83       C
ATOM   3745  CG  LEU B 120     -67.243  12.260   4.743  1.00 29.80           C
ANISOU 3745  CG  LEU B 120     3408   2767   5147    598    550     72       C
ATOM   3746  CD1 LEU B 120     -68.529  12.936   4.311  1.00 27.65           C
ANISOU 3746  CD1 LEU B 120     3174   2508   4824    519    488      6       C
ATOM   3747  CD2 LEU B 120     -66.117  13.275   4.855  1.00 26.71           C
ANISOU 3747  CD2 LEU B 120     2892   2473   4784    620    611    190       C
ATOM   3748  N   THR B 121     -66.223  10.848   8.978  1.00 30.95           N
ANISOU 3748  N   THR B 121     3395   2804   5561    457    460    245       N
ATOM   3749  CA  THR B 121     -66.545  10.494  10.358  1.00 29.37           C
ANISOU 3749  CA  THR B 121     3180   2561   5417    378    402    271       C
ATOM   3750  C   THR B 121     -67.944  11.012  10.663  1.00 28.72           C
ANISOU 3750  C   THR B 121     3122   2480   5312    271    345    224       C
ATOM   3751  O   THR B 121     -68.148  12.212  10.861  1.00 29.48           O
ANISOU 3751  O   THR B 121     3171   2642   5388    219    329    247       O
ATOM   3752  CB  THR B 121     -65.515  11.072  11.321  1.00 26.26           C
ANISOU 3752  CB  THR B 121     2685   2217   5074    365    396    380       C
ATOM   3753  OG1 THR B 121     -64.234  10.488  11.056  1.00 29.45           O
ANISOU 3753  OG1 THR B 121     3053   2621   5515    468    452    437       O
ATOM   3754  CG2 THR B 121     -65.908  10.779  12.759  1.00 24.53           C
ANISOU 3754  CG2 THR B 121     2468   1959   4892    289    335    405       C
ATOM   3755  N   VAL B 122     -68.911  10.104  10.697  1.00 30.43           N
ANISOU 3755  N   VAL B 122     3410   2618   5536    240    312    165       N
ATOM   3756  CA  VAL B 122     -70.314  10.452  10.879  1.00 26.32           C
ANISOU 3756  CA  VAL B 122     2903   2095   5003    148    264    128       C
ATOM   3757  C   VAL B 122     -70.666  10.370  12.357  1.00 29.21           C
ANISOU 3757  C   VAL B 122     3238   2449   5413     79    236    186       C
ATOM   3758  O   VAL B 122     -70.298   9.414  13.048  1.00 33.84           O
ANISOU 3758  O   VAL B 122     3835   2976   6045     91    233    218       O
ATOM   3759  CB  VAL B 122     -71.214   9.526  10.040  1.00 28.02           C
ANISOU 3759  CB  VAL B 122     3206   2230   5212    145    232     44       C
ATOM   3760  CG1 VAL B 122     -72.672   9.912  10.200  1.00 23.81           C
ANISOU 3760  CG1 VAL B 122     2665   1703   4681     47    180     23       C
ATOM   3761  CG2 VAL B 122     -70.803   9.571   8.577  1.00 28.77           C
ANISOU 3761  CG2 VAL B 122     3355   2334   5242    232    261    -16       C
ATOM   3762  N   PHE B 123     -71.387  11.373  12.846  1.00 30.70           N
ANISOU 3762  N   PHE B 123     3393   2692   5579     16    218    201       N
ATOM   3763  CA  PHE B 123     -71.832  11.401  14.232  1.00 27.44           C
ANISOU 3763  CA  PHE B 123     2964   2277   5187    -37    201    255       C
ATOM   3764  C   PHE B 123     -73.194  10.730  14.349  1.00 27.56           C
ANISOU 3764  C   PHE B 123     3000   2242   5228    -94    181    236       C
ATOM   3765  O   PHE B 123     -74.141  11.104  13.650  1.00 25.20           O
ANISOU 3765  O   PHE B 123     2703   1960   4913   -124    167    194       O
ATOM   3766  CB  PHE B 123     -71.902  12.838  14.750  1.00 29.28           C
ANISOU 3766  CB  PHE B 123     3162   2587   5376    -62    195    284       C
ATOM   3767  CG  PHE B 123     -72.492  12.958  16.126  1.00 30.38           C
ANISOU 3767  CG  PHE B 123     3304   2729   5511   -101    184    333       C
ATOM   3768  CD1 PHE B 123     -71.755  12.604  17.243  1.00 29.66           C
ANISOU 3768  CD1 PHE B 123     3216   2619   5433    -89    175    393       C
ATOM   3769  CD2 PHE B 123     -73.783  13.427  16.302  1.00 35.62           C
ANISOU 3769  CD2 PHE B 123     3967   3415   6152   -141    187    326       C
ATOM   3770  CE1 PHE B 123     -72.295  12.712  18.510  1.00 33.65           C
ANISOU 3770  CE1 PHE B 123     3739   3128   5917   -112    170    440       C
ATOM   3771  CE2 PHE B 123     -74.329  13.539  17.567  1.00 36.95           C
ANISOU 3771  CE2 PHE B 123     4143   3591   6306   -158    193    378       C
ATOM   3772  CZ  PHE B 123     -73.583  13.181  18.672  1.00 37.34           C
ANISOU 3772  CZ  PHE B 123     4210   3622   6356   -142    186    433       C
ATOM   3773  N   PHE B 124     -73.287   9.743  15.235  1.00 30.91           N
ANISOU 3773  N   PHE B 124     3436   2606   5701   -110    175    279       N
ATOM   3774  CA  PHE B 124     -74.517   9.003  15.470  1.00 26.06           C
ANISOU 3774  CA  PHE B 124     2830   1939   5134   -171    155    287       C
ATOM   3775  C   PHE B 124     -74.997   9.245  16.893  1.00 29.61           C
ANISOU 3775  C   PHE B 124     3250   2417   5584   -204    173    370       C
ATOM   3776  O   PHE B 124     -74.194   9.287  17.832  1.00 30.94           O
ANISOU 3776  O   PHE B 124     3422   2598   5738   -176    185    420       O
ATOM   3777  CB  PHE B 124     -74.316   7.502  15.235  1.00 25.79           C
ANISOU 3777  CB  PHE B 124     2844   1792   5163   -162    133    274       C
ATOM   3778  CG  PHE B 124     -73.863   7.159  13.844  1.00 25.80           C
ANISOU 3778  CG  PHE B 124     2899   1754   5150   -110    120    188       C
ATOM   3779  CD1 PHE B 124     -74.786   6.901  12.843  1.00 26.83           C
ANISOU 3779  CD1 PHE B 124     3065   1842   5286   -144     74    121       C
ATOM   3780  CD2 PHE B 124     -72.513   7.087  13.538  1.00 29.92           C
ANISOU 3780  CD2 PHE B 124     3437   2282   5650    -22    152    179       C
ATOM   3781  CE1 PHE B 124     -74.371   6.582  11.562  1.00 27.76           C
ANISOU 3781  CE1 PHE B 124     3255   1920   5371    -83     60     37       C
ATOM   3782  CE2 PHE B 124     -72.092   6.768  12.259  1.00 29.14           C
ANISOU 3782  CE2 PHE B 124     3396   2151   5524     45    156    106       C
ATOM   3783  CZ  PHE B 124     -73.022   6.515  11.271  1.00 26.53           C
ANISOU 3783  CZ  PHE B 124     3123   1775   5182     19    109     29       C
ATOM   3784  N   ASP B 125     -76.308   9.403  17.046  1.00 35.21           N
ANISOU 3784  N   ASP B 125     3931   3140   6306   -259    173    390       N
ATOM   3785  CA  ASP B 125     -76.945   9.620  18.342  1.00 36.36           C
ANISOU 3785  CA  ASP B 125     4052   3319   6444   -278    205    475       C
ATOM   3786  C   ASP B 125     -77.674   8.335  18.721  1.00 35.38           C
ANISOU 3786  C   ASP B 125     3918   3117   6406   -327    198    531       C
ATOM   3787  O   ASP B 125     -78.755   8.047  18.200  1.00 38.14           O
ANISOU 3787  O   ASP B 125     4236   3443   6810   -383    177    529       O
ATOM   3788  CB  ASP B 125     -77.894  10.814  18.284  1.00 41.70           C
ANISOU 3788  CB  ASP B 125     4694   4077   7075   -290    224    475       C
ATOM   3789  CG  ASP B 125     -78.477  11.170  19.642  1.00 48.04           C
ANISOU 3789  CG  ASP B 125     5484   4924   7846   -283    273    563       C
ATOM   3790  OD1 ASP B 125     -78.199  10.457  20.630  1.00 49.57           O
ANISOU 3790  OD1 ASP B 125     5696   5085   8052   -276    289    628       O
ATOM   3791  OD2 ASP B 125     -79.216  12.174  19.720  1.00 49.95           O
ANISOU 3791  OD2 ASP B 125     5704   5232   8043   -275    299    571       O
ATOM   3792  N   GLY B 126     -77.084   7.572  19.642  1.00 33.36           N
ANISOU 3792  N   GLY B 126     3686   2818   6169   -311    209    588       N
ATOM   3793  CA  GLY B 126     -77.672   6.317  20.084  1.00 33.85           C
ANISOU 3793  CA  GLY B 126     3742   2800   6320   -357    203    655       C
ATOM   3794  C   GLY B 126     -79.035   6.455  20.729  1.00 40.23           C
ANISOU 3794  C   GLY B 126     4491   3643   7153   -406    239    744       C
ATOM   3795  O   GLY B 126     -79.727   5.443  20.893  1.00 49.40           O
ANISOU 3795  O   GLY B 126     5628   4734   8408   -463    226    806       O
ATOM   3796  N   ARG B 127     -79.435   7.671  21.102  1.00 37.79           N
ANISOU 3796  N   ARG B 127     4157   3437   6766   -381    284    759       N
ATOM   3797  CA  ARG B 127     -80.769   7.895  21.644  1.00 37.12           C
ANISOU 3797  CA  ARG B 127     4007   3398   6699   -410    333    850       C
ATOM   3798  C   ARG B 127     -81.854   7.814  20.580  1.00 39.51           C
ANISOU 3798  C   ARG B 127     4245   3686   7081   -478    294    827       C
ATOM   3799  O   ARG B 127     -83.039   7.790  20.930  1.00 46.50           O
ANISOU 3799  O   ARG B 127     5054   4598   8015   -514    327    919       O
ATOM   3800  CB  ARG B 127     -80.829   9.255  22.338  1.00 34.84           C
ANISOU 3800  CB  ARG B 127     3729   3218   6292   -344    393    864       C
ATOM   3801  CG  ARG B 127     -79.862   9.396  23.498  1.00 36.34           C
ANISOU 3801  CG  ARG B 127     3990   3421   6395   -280    416    894       C
ATOM   3802  CD  ARG B 127     -79.807  10.827  23.999  1.00 37.80           C
ANISOU 3802  CD  ARG B 127     4214   3695   6455   -214    448    880       C
ATOM   3803  NE  ARG B 127     -79.290  11.738  22.982  1.00 36.55           N
ANISOU 3803  NE  ARG B 127     4065   3556   6265   -208    401    771       N
ATOM   3804  CZ  ARG B 127     -79.052  13.030  23.187  1.00 34.39           C
ANISOU 3804  CZ  ARG B 127     3833   3340   5893   -159    403    738       C
ATOM   3805  NH1 ARG B 127     -79.285  13.567  24.376  1.00 31.86           N
ANISOU 3805  NH1 ARG B 127     3562   3060   5482   -103    448    794       N
ATOM   3806  NH2 ARG B 127     -78.580  13.784  22.203  1.00 32.66           N
ANISOU 3806  NH2 ARG B 127     3616   3134   5661   -162    359    652       N
ATOM   3807  N   VAL B 128     -81.485   7.773  19.305  1.00 32.98           N
ANISOU 3807  N   VAL B 128     3445   2819   6266   -492    223    716       N
ATOM   3808  CA  VAL B 128     -82.436   7.700  18.203  1.00 31.81           C
ANISOU 3808  CA  VAL B 128     3252   2650   6183   -556    164    682       C
ATOM   3809  C   VAL B 128     -82.461   6.272  17.678  1.00 37.31           C
ANISOU 3809  C   VAL B 128     3976   3214   6987   -618     84    668       C
ATOM   3810  O   VAL B 128     -81.414   5.622  17.566  1.00 38.84           O
ANISOU 3810  O   VAL B 128     4247   3338   7172   -586     63    619       O
ATOM   3811  CB  VAL B 128     -82.070   8.699  17.089  1.00 29.92           C
ANISOU 3811  CB  VAL B 128     3041   2458   5868   -522    137    566       C
ATOM   3812  CG1 VAL B 128     -83.147   8.729  16.018  1.00 29.72           C
ANISOU 3812  CG1 VAL B 128     2971   2422   5899   -584     71    539       C
ATOM   3813  CG2 VAL B 128     -81.844  10.083  17.671  1.00 28.04           C
ANISOU 3813  CG2 VAL B 128     2799   2332   5524   -456    207    575       C
ATOM   3814  N   ASP B 129     -83.660   5.783  17.360  1.00 41.96           N
ANISOU 3814  N   ASP B 129     4500   3761   7681   -706     33    717       N
ATOM   3815  CA  ASP B 129     -83.825   4.405  16.914  1.00 45.29           C
ANISOU 3815  CA  ASP B 129     4963   4078   8168   -756    -62    698       C
ATOM   3816  C   ASP B 129     -83.007   4.133  15.658  1.00 43.10           C
ANISOU 3816  C   ASP B 129     4791   3711   7872   -736   -141    554       C
ATOM   3817  O   ASP B 129     -83.045   4.905  14.695  1.00 41.28           O
ANISOU 3817  O   ASP B 129     4570   3505   7609   -727   -168    472       O
ATOM   3818  CB  ASP B 129     -85.302   4.109  16.650  1.00 57.08           C
ANISOU 3818  CB  ASP B 129     6373   5582   9732   -838   -121    757       C
ATOM   3819  CG  ASP B 129     -86.115   4.000  17.926  1.00 65.75           C
ANISOU 3819  CG  ASP B 129     7373   6745  10865   -852    -44    916       C
ATOM   3820  OD1 ASP B 129     -85.524   4.116  19.020  1.00 68.25           O
ANISOU 3820  OD1 ASP B 129     7699   7090  11143   -799     52    974       O
ATOM   3821  OD2 ASP B 129     -87.344   3.796  17.833  1.00 68.31           O
ANISOU 3821  OD2 ASP B 129     7610   7090  11254   -912    -79    988       O
ATOM   3822  N   GLY B 130     -82.264   3.029  15.676  1.00 42.00           N
ANISOU 3822  N   GLY B 130     4738   3473   7747   -718   -172    526       N
ATOM   3823  CA  GLY B 130     -81.527   2.576  14.516  1.00 41.15           C
ANISOU 3823  CA  GLY B 130     4745   3267   7624   -684   -242    397       C
ATOM   3824  C   GLY B 130     -80.172   3.213  14.306  1.00 36.08           C
ANISOU 3824  C   GLY B 130     4158   2661   6891   -577   -179    325       C
ATOM   3825  O   GLY B 130     -79.460   2.813  13.377  1.00 38.75           O
ANISOU 3825  O   GLY B 130     4595   2932   7194   -522   -217    224       O
ATOM   3826  N   GLN B 131     -79.784   4.185  15.134  1.00 35.14           N
ANISOU 3826  N   GLN B 131     3983   2664   6705   -533    -85    374       N
ATOM   3827  CA  GLN B 131     -78.508   4.862  14.926  1.00 36.22           C
ANISOU 3827  CA  GLN B 131     4159   2863   6740   -434    -35    315       C
ATOM   3828  C   GLN B 131     -77.325   4.023  15.391  1.00 36.40           C
ANISOU 3828  C   GLN B 131     4237   2821   6771   -374    -14    325       C
ATOM   3829  O   GLN B 131     -76.230   4.143  14.829  1.00 37.30           O
ANISOU 3829  O   GLN B 131     4400   2941   6830   -291      2    262       O
ATOM   3830  CB  GLN B 131     -78.508   6.212  15.641  1.00 35.76           C
ANISOU 3830  CB  GLN B 131     4033   2943   6611   -413     37    361       C
ATOM   3831  CG  GLN B 131     -79.565   7.177  15.132  1.00 40.10           C
ANISOU 3831  CG  GLN B 131     4528   3565   7141   -452     27    348       C
ATOM   3832  CD  GLN B 131     -79.020   8.189  14.142  1.00 44.75           C
ANISOU 3832  CD  GLN B 131     5142   4218   7641   -397     30    260       C
ATOM   3833  OE1 GLN B 131     -78.231   9.065  14.502  1.00 46.03           O
ANISOU 3833  OE1 GLN B 131     5300   4455   7735   -343     81    264       O
ATOM   3834  NE2 GLN B 131     -79.443   8.077  12.889  1.00 43.95           N
ANISOU 3834  NE2 GLN B 131     5071   4085   7543   -414    -32    184       N
ATOM   3835  N   VAL B 132     -77.516   3.180  16.409  1.00 36.21           N
ANISOU 3835  N   VAL B 132     4201   2740   6818   -409    -10    414       N
ATOM   3836  CA  VAL B 132     -76.434   2.306  16.856  1.00 34.78           C
ANISOU 3836  CA  VAL B 132     4073   2489   6653   -351      2    430       C
ATOM   3837  C   VAL B 132     -76.075   1.307  15.764  1.00 37.14           C
ANISOU 3837  C   VAL B 132     4469   2660   6981   -321    -58    340       C
ATOM   3838  O   VAL B 132     -74.894   1.052  15.497  1.00 38.74           O
ANISOU 3838  O   VAL B 132     4726   2842   7151   -227    -36    300       O
ATOM   3839  CB  VAL B 132     -76.822   1.598  18.168  1.00 38.32           C
ANISOU 3839  CB  VAL B 132     4490   2899   7170   -399     18    553       C
ATOM   3840  CG1 VAL B 132     -75.778   0.559  18.542  1.00 29.28           C
ANISOU 3840  CG1 VAL B 132     3406   1666   6053   -342     17    569       C
ATOM   3841  CG2 VAL B 132     -76.991   2.613  19.287  1.00 36.20           C
ANISOU 3841  CG2 VAL B 132     4152   2759   6844   -396     87    635       C
ATOM   3842  N   ASP B 133     -77.089   0.733  15.110  1.00 38.86           N
ANISOU 3842  N   ASP B 133     4714   2788   7262   -396   -139    309       N
ATOM   3843  CA  ASP B 133     -76.832  -0.201  14.018  1.00 42.72           C
ANISOU 3843  CA  ASP B 133     5322   3142   7766   -364   -212    210       C
ATOM   3844  C   ASP B 133     -76.123   0.486  12.859  1.00 41.19           C
ANISOU 3844  C   ASP B 133     5182   3006   7464   -268   -192     98       C
ATOM   3845  O   ASP B 133     -75.201  -0.081  12.261  1.00 45.80           O
ANISOU 3845  O   ASP B 133     5863   3523   8016   -169   -188     33       O
ATOM   3846  CB  ASP B 133     -78.141  -0.832  13.544  1.00 53.17           C
ANISOU 3846  CB  ASP B 133     6664   4408   9129   -468   -318    196       C
ATOM   3847  CG  ASP B 133     -78.563  -2.006  14.399  1.00 68.20           C
ANISOU 3847  CG  ASP B 133     8565   6255  11093   -527   -347    282       C
ATOM   3848  OD1 ASP B 133     -79.212  -1.782  15.442  1.00 74.17           O
ANISOU 3848  OD1 ASP B 133     9214   7088  11880   -589   -309    397       O
ATOM   3849  OD2 ASP B 133     -78.240  -3.155  14.029  1.00 75.02           O
ANISOU 3849  OD2 ASP B 133     9539   6996  11970   -504   -404    237       O
ATOM   3850  N   LEU B 134     -76.549   1.706  12.522  1.00 35.82           N
ANISOU 3850  N   LEU B 134     4439   2448   6724   -287   -173     83       N
ATOM   3851  CA  LEU B 134     -75.866   2.466  11.482  1.00 33.69           C
ANISOU 3851  CA  LEU B 134     4207   2246   6349   -196   -142     -4       C
ATOM   3852  C   LEU B 134     -74.414   2.729  11.851  1.00 33.51           C
ANISOU 3852  C   LEU B 134     4172   2283   6278    -87    -51     19       C
ATOM   3853  O   LEU B 134     -73.542   2.746  10.974  1.00 35.23           O
ANISOU 3853  O   LEU B 134     4451   2501   6433     16    -23    -44       O
ATOM   3854  CB  LEU B 134     -76.601   3.784  11.230  1.00 32.67           C
ANISOU 3854  CB  LEU B 134     4000   2239   6173   -242   -136     -5       C
ATOM   3855  CG  LEU B 134     -78.013   3.679  10.649  1.00 34.96           C
ANISOU 3855  CG  LEU B 134     4290   2487   6505   -341   -232    -30       C
ATOM   3856  CD1 LEU B 134     -78.750   5.000  10.792  1.00 35.83           C
ANISOU 3856  CD1 LEU B 134     4296   2731   6587   -386   -206      5       C
ATOM   3857  CD2 LEU B 134     -77.959   3.253   9.193  1.00 35.94           C
ANISOU 3857  CD2 LEU B 134     4541   2531   6583   -298   -307   -151       C
ATOM   3858  N   PHE B 135     -74.136   2.931  13.141  1.00 30.67           N
ANISOU 3858  N   PHE B 135     3734   1973   5946   -106     -4    117       N
ATOM   3859  CA  PHE B 135     -72.758   3.101  13.585  1.00 30.48           C
ANISOU 3859  CA  PHE B 135     3692   1996   5894    -14     63    153       C
ATOM   3860  C   PHE B 135     -71.954   1.823  13.381  1.00 38.73           C
ANISOU 3860  C   PHE B 135     4820   2923   6972     65     60    134       C
ATOM   3861  O   PHE B 135     -70.782   1.875  12.990  1.00 44.16           O
ANISOU 3861  O   PHE B 135     5522   3634   7623    174    110    121       O
ATOM   3862  CB  PHE B 135     -72.734   3.530  15.051  1.00 31.78           C
ANISOU 3862  CB  PHE B 135     3773   2226   6076    -56     92    259       C
ATOM   3863  CG  PHE B 135     -71.356   3.598  15.645  1.00 33.81           C
ANISOU 3863  CG  PHE B 135     4008   2518   6321     22    137    309       C
ATOM   3864  CD1 PHE B 135     -70.498   4.635  15.324  1.00 26.14           C
ANISOU 3864  CD1 PHE B 135     2994   1645   5290     77    174    303       C
ATOM   3865  CD2 PHE B 135     -70.923   2.631  16.538  1.00 41.89           C
ANISOU 3865  CD2 PHE B 135     5044   3472   7399     36    136    373       C
ATOM   3866  CE1 PHE B 135     -69.231   4.703  15.875  1.00 26.19           C
ANISOU 3866  CE1 PHE B 135     2966   1683   5301    140    202    363       C
ATOM   3867  CE2 PHE B 135     -69.657   2.693  17.093  1.00 46.80           C
ANISOU 3867  CE2 PHE B 135     5639   4128   8017    107    166    427       C
ATOM   3868  CZ  PHE B 135     -68.811   3.732  16.762  1.00 26.72           C
ANISOU 3868  CZ  PHE B 135     3046   1685   5422    156    195    424       C
ATOM   3869  N   ARG B 136     -72.570   0.665  13.635  1.00 34.65           N
ANISOU 3869  N   ARG B 136     4357   2277   6532     14      2    141       N
ATOM   3870  CA  ARG B 136     -71.882  -0.602  13.414  1.00 33.81           C
ANISOU 3870  CA  ARG B 136     4347   2039   6458     92     -9    117       C
ATOM   3871  C   ARG B 136     -71.560  -0.815  11.941  1.00 32.58           C
ANISOU 3871  C   ARG B 136     4303   1835   6242    186    -20     -1       C
ATOM   3872  O   ARG B 136     -70.548  -1.444  11.612  1.00 33.06           O
ANISOU 3872  O   ARG B 136     4432   1842   6288    309     15    -23       O
ATOM   3873  CB  ARG B 136     -72.728  -1.762  13.940  1.00 35.49           C
ANISOU 3873  CB  ARG B 136     4600   2112   6773      4    -82    151       C
ATOM   3874  CG  ARG B 136     -72.973  -1.747  15.441  1.00 32.63           C
ANISOU 3874  CG  ARG B 136     4145   1786   6468    -68    -60    279       C
ATOM   3875  CD  ARG B 136     -73.748  -2.985  15.870  1.00 35.20           C
ANISOU 3875  CD  ARG B 136     4510   2014   6849   -147   -126    316       C
ATOM   3876  NE  ARG B 136     -73.936  -3.055  17.316  1.00 38.01           N
ANISOU 3876  NE  ARG B 136     4787   2424   7229   -197    -94    443       N
ATOM   3877  CZ  ARG B 136     -73.064  -3.604  18.155  1.00 38.34           C
ANISOU 3877  CZ  ARG B 136     4837   2452   7279   -141    -61    506       C
ATOM   3878  NH1 ARG B 136     -71.937  -4.126  17.693  1.00 37.19           N
ANISOU 3878  NH1 ARG B 136     4763   2244   7126    -31    -52    459       N
ATOM   3879  NH2 ARG B 136     -73.315  -3.629  19.457  1.00 36.12           N
ANISOU 3879  NH2 ARG B 136     4494   2220   7010   -186    -35    620       N
ATOM   3880  N   ASN B 137     -72.401  -0.302  11.045  1.00 34.34           N
ANISOU 3880  N   ASN B 137     4549   2078   6422    141    -65    -73       N
ATOM   3881  CA  ASN B 137     -72.208  -0.471   9.612  1.00 41.40           C
ANISOU 3881  CA  ASN B 137     5566   2925   7239    230    -82   -189       C
ATOM   3882  C   ASN B 137     -71.380   0.640   8.982  1.00 43.97           C
ANISOU 3882  C   ASN B 137     5851   3393   7462    329      9   -204       C
ATOM   3883  O   ASN B 137     -70.958   0.496   7.830  1.00 47.70           O
ANISOU 3883  O   ASN B 137     6427   3842   7856    438     24   -286       O
ATOM   3884  CB  ASN B 137     -73.564  -0.552   8.905  1.00 49.09           C
ANISOU 3884  CB  ASN B 137     6596   3836   8220    129   -197   -259       C
ATOM   3885  CG  ASN B 137     -74.375  -1.755   9.340  1.00 63.29           C
ANISOU 3885  CG  ASN B 137     8444   5471  10130     32   -302   -244       C
ATOM   3886  OD1 ASN B 137     -73.842  -2.854   9.495  1.00 66.46           O
ANISOU 3886  OD1 ASN B 137     8933   5748  10569     88   -312   -249       O
ATOM   3887  ND2 ASN B 137     -75.671  -1.552   9.548  1.00 69.18           N
ANISOU 3887  ND2 ASN B 137     9130   6218  10938   -114   -380   -214       N
ATOM   3888  N   ALA B 138     -71.139   1.733   9.698  1.00 42.99           N
ANISOU 3888  N   ALA B 138     5589   3411   7335    295     68   -124       N
ATOM   3889  CA  ALA B 138     -70.366   2.838   9.154  1.00 42.86           C
ANISOU 3889  CA  ALA B 138     5522   3526   7237    372    146   -122       C
ATOM   3890  C   ALA B 138     -68.873   2.545   9.238  1.00 44.27           C
ANISOU 3890  C   ALA B 138     5690   3719   7412    508    232    -78       C
ATOM   3891  O   ALA B 138     -68.395   1.897  10.173  1.00 43.97           O
ANISOU 3891  O   ALA B 138     5628   3638   7442    514    240    -14       O
ATOM   3892  CB  ALA B 138     -70.686   4.135   9.897  1.00 43.52           C
ANISOU 3892  CB  ALA B 138     5471   3740   7323    282    161    -54       C
ATOM   3893  N   ARG B 139     -68.135   3.033   8.241  1.00 41.00           N
ANISOU 3893  N   ARG B 139     5289   3369   6919    620    300   -103       N
ATOM   3894  CA  ARG B 139     -66.689   2.838   8.220  1.00 37.49           C
ANISOU 3894  CA  ARG B 139     4815   2954   6475    759    394    -46       C
ATOM   3895  C   ARG B 139     -65.994   3.750   9.224  1.00 34.73           C
ANISOU 3895  C   ARG B 139     4301   2722   6170    721    431     74       C
ATOM   3896  O   ARG B 139     -65.183   3.291  10.035  1.00 32.48           O
ANISOU 3896  O   ARG B 139     3968   2424   5948    756    452    151       O
ATOM   3897  CB  ARG B 139     -66.152   3.075   6.808  1.00 44.13           C
ANISOU 3897  CB  ARG B 139     5720   3832   7216    899    465    -97       C
ATOM   3898  CG  ARG B 139     -64.662   2.841   6.670  1.00 51.84           C
ANISOU 3898  CG  ARG B 139     6659   4844   8195   1061    576    -27       C
ATOM   3899  CD  ARG B 139     -64.265   2.630   5.220  1.00 59.93           C
ANISOU 3899  CD  ARG B 139     7799   5860   9111   1227    648    -94       C
ATOM   3900  NE  ARG B 139     -62.877   2.196   5.099  1.00 67.52           N
ANISOU 3900  NE  ARG B 139     8734   6841  10082   1400    762    -22       N
ATOM   3901  CZ  ARG B 139     -62.469   0.943   5.273  1.00 69.63           C
ANISOU 3901  CZ  ARG B 139     9086   6991  10379   1497    770    -36       C
ATOM   3902  NH1 ARG B 139     -63.345  -0.006   5.578  1.00 68.66           N
ANISOU 3902  NH1 ARG B 139     9085   6719  10284   1426    664   -118       N
ATOM   3903  NH2 ARG B 139     -61.186   0.637   5.144  1.00 72.34           N
ANISOU 3903  NH2 ARG B 139     9388   7365  10732   1664    885     43       N
ATOM   3904  N   ASN B 140     -66.297   5.043   9.181  1.00 33.22           N
ANISOU 3904  N   ASN B 140     4032   2641   5949    652    430     91       N
ATOM   3905  CA  ASN B 140     -65.797   6.010  10.146  1.00 32.38           C
ANISOU 3905  CA  ASN B 140     3788   2633   5880    596    438    194       C
ATOM   3906  C   ASN B 140     -66.983   6.654  10.844  1.00 33.47           C
ANISOU 3906  C   ASN B 140     3904   2792   6023    451    369    185       C
ATOM   3907  O   ASN B 140     -67.962   7.036  10.195  1.00 34.19           O
ANISOU 3907  O   ASN B 140     4034   2887   6068    405    342    116       O
ATOM   3908  CB  ASN B 140     -64.943   7.086   9.469  1.00 27.51           C
ANISOU 3908  CB  ASN B 140     3095   2133   5226    657    505    238       C
ATOM   3909  CG  ASN B 140     -63.793   6.505   8.678  1.00 37.46           C
ANISOU 3909  CG  ASN B 140     4370   3388   6474    819    594    258       C
ATOM   3910  OD1 ASN B 140     -62.706   6.286   9.213  1.00 39.88           O
ANISOU 3910  OD1 ASN B 140     4599   3713   6840    875    629    351       O
ATOM   3911  ND2 ASN B 140     -64.024   6.251   7.395  1.00 36.18           N
ANISOU 3911  ND2 ASN B 140     4312   3204   6232    904    630    174       N
ATOM   3912  N   GLY B 141     -66.905   6.770  12.164  1.00 26.11           N
ANISOU 3912  N   GLY B 141     2910   1870   5140    387    341    258       N
ATOM   3913  CA  GLY B 141     -68.032   7.328  12.888  1.00 26.09           C
ANISOU 3913  CA  GLY B 141     2893   1885   5136    268    290    258       C
ATOM   3914  C   GLY B 141     -67.718   7.568  14.346  1.00 27.20           C
ANISOU 3914  C   GLY B 141     2975   2051   5311    223    268    346       C
ATOM   3915  O   GLY B 141     -66.703   7.111  14.879  1.00 30.08           O
ANISOU 3915  O   GLY B 141     3313   2401   5714    272    278    408       O
ATOM   3916  N   VAL B 142     -68.622   8.310  14.984  1.00 24.23           N
ANISOU 3916  N   VAL B 142     2582   1710   4913    137    238    353       N
ATOM   3917  CA  VAL B 142     -68.592   8.576  16.417  1.00 27.18           C
ANISOU 3917  CA  VAL B 142     2928   2102   5296     92    211    426       C
ATOM   3918  C   VAL B 142     -70.002   8.379  16.954  1.00 27.77           C
ANISOU 3918  C   VAL B 142     3033   2151   5369     18    194    416       C
ATOM   3919  O   VAL B 142     -70.966   8.897  16.379  1.00 35.24           O
ANISOU 3919  O   VAL B 142     3982   3120   6287    -20    192    368       O
ATOM   3920  CB  VAL B 142     -68.084   9.996  16.732  1.00 29.26           C
ANISOU 3920  CB  VAL B 142     3138   2457   5523     79    197    462       C
ATOM   3921  CG1 VAL B 142     -68.324  10.338  18.195  1.00 24.80           C
ANISOU 3921  CG1 VAL B 142     2578   1904   4943     32    160    519       C
ATOM   3922  CG2 VAL B 142     -66.608  10.117  16.391  1.00 33.03           C
ANISOU 3922  CG2 VAL B 142     3564   2960   6027    145    210    506       C
ATOM   3923  N   LEU B 143     -70.124   7.628  18.045  1.00 26.86           N
ANISOU 3923  N   LEU B 143     2930   1989   5285      0    183    472       N
ATOM   3924  CA  LEU B 143     -71.417   7.294  18.624  1.00 24.27           C
ANISOU 3924  CA  LEU B 143     2619   1634   4968    -65    178    488       C
ATOM   3925  C   LEU B 143     -71.480   7.762  20.070  1.00 30.76           C
ANISOU 3925  C   LEU B 143     3433   2498   5756    -82    176    566       C
ATOM   3926  O   LEU B 143     -70.513   7.613  20.823  1.00 29.02           O
ANISOU 3926  O   LEU B 143     3214   2276   5536    -49    163    618       O
ATOM   3927  CB  LEU B 143     -71.678   5.785  18.555  1.00 28.93           C
ANISOU 3927  CB  LEU B 143     3248   2114   5631    -70    169    491       C
ATOM   3928  CG  LEU B 143     -72.952   5.270  19.230  1.00 30.73           C
ANISOU 3928  CG  LEU B 143     3477   2304   5895   -142    164    536       C
ATOM   3929  CD1 LEU B 143     -74.190   5.822  18.544  1.00 28.90           C
ANISOU 3929  CD1 LEU B 143     3226   2101   5654   -198    158    492       C
ATOM   3930  CD2 LEU B 143     -72.981   3.750  19.250  1.00 31.50           C
ANISOU 3930  CD2 LEU B 143     3616   2278   6074   -147    144    552       C
ATOM   3931  N   ILE B 144     -72.620   8.332  20.449  1.00 33.92           N
ANISOU 3931  N   ILE B 144     3828   2937   6125   -127    188    576       N
ATOM   3932  CA  ILE B 144     -72.913   8.663  21.837  1.00 29.56           C
ANISOU 3932  CA  ILE B 144     3288   2417   5527   -133    198    650       C
ATOM   3933  C   ILE B 144     -74.156   7.895  22.258  1.00 29.71           C
ANISOU 3933  C   ILE B 144     3304   2400   5585   -176    226    697       C
ATOM   3934  O   ILE B 144     -75.113   7.768  21.485  1.00 30.45           O
ANISOU 3934  O   ILE B 144     3372   2481   5716   -217    232    665       O
ATOM   3935  CB  ILE B 144     -73.104  10.179  22.056  1.00 29.94           C
ANISOU 3935  CB  ILE B 144     3338   2550   5488   -129    197    636       C
ATOM   3936  CG1 ILE B 144     -74.310  10.700  21.271  1.00 31.11           C
ANISOU 3936  CG1 ILE B 144     3460   2728   5632   -161    220    592       C
ATOM   3937  CG2 ILE B 144     -71.845  10.935  21.665  1.00 29.88           C
ANISOU 3937  CG2 ILE B 144     3323   2570   5458    -99    159    607       C
ATOM   3938  CD1 ILE B 144     -74.839  12.022  21.779  1.00 27.75           C
ANISOU 3938  CD1 ILE B 144     3046   2375   5122   -152    233    598       C
ATOM   3939  N   THR B 145     -74.127   7.356  23.474  1.00 26.33           N
ANISOU 3939  N   THR B 145     2897   1954   5153   -168    239    782       N
ATOM   3940  CA  THR B 145     -75.270   6.660  24.044  1.00 27.79           C
ANISOU 3940  CA  THR B 145     3070   2113   5377   -207    276    856       C
ATOM   3941  C   THR B 145     -75.402   7.052  25.507  1.00 30.68           C
ANISOU 3941  C   THR B 145     3467   2529   5661   -175    310    944       C
ATOM   3942  O   THR B 145     -74.455   7.537  26.131  1.00 33.03           O
ANISOU 3942  O   THR B 145     3810   2854   5888   -128    286    947       O
ATOM   3943  CB  THR B 145     -75.144   5.132  23.933  1.00 29.24           C
ANISOU 3943  CB  THR B 145     3259   2187   5663   -229    259    885       C
ATOM   3944  OG1 THR B 145     -73.963   4.696  24.617  1.00 36.63           O
ANISOU 3944  OG1 THR B 145     4232   3097   6587   -180    242    919       O
ATOM   3945  CG2 THR B 145     -75.079   4.690  22.477  1.00 28.63           C
ANISOU 3945  CG2 THR B 145     3176   2048   5653   -249    221    792       C
ATOM   3946  N   GLU B 146     -76.596   6.834  26.051  1.00 30.96           N
ANISOU 3946  N   GLU B 146     3480   2577   5707   -198    366   1021       N
ATOM   3947  CA  GLU B 146     -76.823   7.048  27.473  1.00 33.81           C
ANISOU 3947  CA  GLU B 146     3880   2982   5984   -155    414   1117       C
ATOM   3948  C   GLU B 146     -76.474   5.824  28.303  1.00 42.07           C
ANISOU 3948  C   GLU B 146     4950   3964   7070   -152    417   1208       C
ATOM   3949  O   GLU B 146     -76.074   5.964  29.464  1.00 48.36           O
ANISOU 3949  O   GLU B 146     5809   4787   7778    -98    428   1269       O
ATOM   3950  CB  GLU B 146     -78.282   7.437  27.722  1.00 35.65           C
ANISOU 3950  CB  GLU B 146     4070   3272   6204   -164    492   1178       C
ATOM   3951  CG  GLU B 146     -78.760   8.602  26.878  1.00 39.67           C
ANISOU 3951  CG  GLU B 146     4550   3840   6682   -167    492   1097       C
ATOM   3952  CD  GLU B 146     -80.165   9.040  27.236  1.00 49.82           C
ANISOU 3952  CD  GLU B 146     5789   5191   7950   -158    576   1171       C
ATOM   3953  OE1 GLU B 146     -80.329  10.180  27.721  1.00 51.93           O
ANISOU 3953  OE1 GLU B 146     6100   5531   8100    -92    612   1164       O
ATOM   3954  OE2 GLU B 146     -81.104   8.241  27.042  1.00 55.82           O
ANISOU 3954  OE2 GLU B 146     6468   5924   8816   -216    605   1242       O
ATOM   3955  N   GLY B 147     -76.611   4.630  27.731  1.00 42.68           N
ANISOU 3955  N   GLY B 147     4990   3952   7274   -206    400   1219       N
ATOM   3956  CA  GLY B 147     -76.291   3.406  28.436  1.00 41.51           C
ANISOU 3956  CA  GLY B 147     4865   3730   7178   -207    398   1306       C
ATOM   3957  C   GLY B 147     -75.280   2.552  27.701  1.00 40.14           C
ANISOU 3957  C   GLY B 147     4706   3461   7086   -211    331   1245       C
ATOM   3958  O   GLY B 147     -74.551   3.045  26.835  1.00 36.75           O
ANISOU 3958  O   GLY B 147     4280   3041   6644   -192    290   1140       O
ATOM   3959  N   SER B 148     -75.236   1.266  28.033  1.00 43.60           N
ANISOU 3959  N   SER B 148     5153   3805   7608   -229    325   1317       N
ATOM   3960  CA  SER B 148     -74.253   0.364  27.454  1.00 38.04           C
ANISOU 3960  CA  SER B 148     4476   3001   6977   -214    268   1270       C
ATOM   3961  C   SER B 148     -74.736  -0.186  26.120  1.00 37.05           C
ANISOU 3961  C   SER B 148     4332   2812   6935   -266    232   1180       C
ATOM   3962  O   SER B 148     -75.929  -0.436  25.927  1.00 41.89           O
ANISOU 3962  O   SER B 148     4909   3423   7585   -333    240   1200       O
ATOM   3963  CB  SER B 148     -73.964  -0.792  28.411  1.00 38.07           C
ANISOU 3963  CB  SER B 148     4512   2949   7003   -200    268   1367       C
ATOM   3964  OG  SER B 148     -75.115  -1.599  28.596  1.00 41.35           O
ANISOU 3964  OG  SER B 148     4900   3341   7468   -263    288   1428       O
ATOM   3965  N   VAL B 149     -73.797  -0.367  25.196  1.00 35.89           N
ANISOU 3965  N   VAL B 149     4212   2618   6806   -228    190   1084       N
ATOM   3966  CA  VAL B 149     -74.030  -1.084  23.949  1.00 35.75           C
ANISOU 3966  CA  VAL B 149     4213   2523   6848   -253    145    992       C
ATOM   3967  C   VAL B 149     -73.299  -2.414  24.047  1.00 41.12           C
ANISOU 3967  C   VAL B 149     4949   3107   7567   -217    115   1000       C
ATOM   3968  O   VAL B 149     -72.122  -2.452  24.427  1.00 47.46           O
ANISOU 3968  O   VAL B 149     5772   3911   8352   -143    121   1016       O
ATOM   3969  CB  VAL B 149     -73.551  -0.278  22.731  1.00 32.78           C
ANISOU 3969  CB  VAL B 149     3839   2162   6456   -221    133    877       C
ATOM   3970  CG1 VAL B 149     -73.963  -0.972  21.444  1.00 34.91           C
ANISOU 3970  CG1 VAL B 149     4146   2348   6772   -246     83    783       C
ATOM   3971  CG2 VAL B 149     -74.104   1.134  22.784  1.00 33.30           C
ANISOU 3971  CG2 VAL B 149     3854   2346   6452   -242    164    869       C
ATOM   3972  N   LYS B 150     -73.994  -3.501  23.717  1.00 37.37           N
ANISOU 3972  N   LYS B 150     4499   2548   7151   -269     77    995       N
ATOM   3973  CA  LYS B 150     -73.428  -4.831  23.907  1.00 40.36           C
ANISOU 3973  CA  LYS B 150     4939   2826   7569   -240     48   1012       C
ATOM   3974  C   LYS B 150     -72.178  -5.015  23.054  1.00 41.00           C
ANISOU 3974  C   LYS B 150     5077   2856   7646   -145     32    921       C
ATOM   3975  O   LYS B 150     -72.210  -4.828  21.833  1.00 35.68           O
ANISOU 3975  O   LYS B 150     4431   2152   6974   -134      9    815       O
ATOM   3976  CB  LYS B 150     -74.467  -5.906  23.582  1.00 39.38           C
ANISOU 3976  CB  LYS B 150     4839   2611   7512   -322     -3   1015       C
ATOM   3977  CG  LYS B 150     -75.247  -5.692  22.294  1.00 34.70           C
ANISOU 3977  CG  LYS B 150     4253   1993   6938   -374    -52    916       C
ATOM   3978  CD  LYS B 150     -76.061  -6.930  21.949  1.00 36.20           C
ANISOU 3978  CD  LYS B 150     4486   2068   7200   -447   -127    916       C
ATOM   3979  CE  LYS B 150     -77.230  -6.600  21.033  1.00 57.91           C
ANISOU 3979  CE  LYS B 150     7209   4822   9972   -531   -179    865       C
ATOM   3980  NZ  LYS B 150     -76.800  -5.970  19.756  1.00 55.68           N
ANISOU 3980  NZ  LYS B 150     6974   4535   9648   -483   -201    728       N
ATOM   3981  N   GLY B 151     -71.071  -5.367  23.709  1.00 43.91           N
ANISOU 3981  N   GLY B 151     5461   3216   8006    -69     47    969       N
ATOM   3982  CA  GLY B 151     -69.824  -5.650  23.039  1.00 39.74           C
ANISOU 3982  CA  GLY B 151     4974   2643   7480     36     44    908       C
ATOM   3983  C   GLY B 151     -68.902  -4.462  22.851  1.00 38.00           C
ANISOU 3983  C   GLY B 151     4703   2516   7220    103     77    890       C
ATOM   3984  O   GLY B 151     -67.715  -4.660  22.570  1.00 39.82           O
ANISOU 3984  O   GLY B 151     4943   2731   7455    202     86    877       O
ATOM   3985  N   LEU B 152     -69.404  -3.239  23.001  1.00 33.51           N
ANISOU 3985  N   LEU B 152     4076   2042   6614     55     94    896       N
ATOM   3986  CA  LEU B 152     -68.626  -2.033  22.748  1.00 32.77           C
ANISOU 3986  CA  LEU B 152     3933   2030   6487    105    116    877       C
ATOM   3987  C   LEU B 152     -68.087  -1.483  24.062  1.00 35.08           C
ANISOU 3987  C   LEU B 152     4186   2398   6743    116    119    978       C
ATOM   3988  O   LEU B 152     -68.860  -1.186  24.980  1.00 37.74           O
ANISOU 3988  O   LEU B 152     4517   2774   7050     56    124   1039       O
ATOM   3989  CB  LEU B 152     -69.473  -0.980  22.035  1.00 29.83           C
ANISOU 3989  CB  LEU B 152     3534   1723   6076     50    124    808       C
ATOM   3990  CG  LEU B 152     -70.025  -1.373  20.663  1.00 35.37           C
ANISOU 3990  CG  LEU B 152     4281   2349   6809     38    106    703       C
ATOM   3991  CD1 LEU B 152     -70.707  -0.189  19.994  1.00 31.36           C
ANISOU 3991  CD1 LEU B 152     3739   1936   6242     -5    113    639       C
ATOM   3992  CD2 LEU B 152     -68.919  -1.921  19.783  1.00 30.63           C
ANISOU 3992  CD2 LEU B 152     3727   1692   6221    148    112    645       C
ATOM   3993  N   GLN B 153     -66.769  -1.340  24.145  1.00 33.06           N
ANISOU 3993  N   GLN B 153     3908   2174   6480    197    113    997       N
ATOM   3994  CA  GLN B 153     -66.139  -0.805  25.348  1.00 34.35           C
ANISOU 3994  CA  GLN B 153     4041   2413   6597    208     91   1084       C
ATOM   3995  C   GLN B 153     -66.368   0.699  25.424  1.00 35.40           C
ANISOU 3995  C   GLN B 153     4139   2668   6642    170     86   1058       C
ATOM   3996  O   GLN B 153     -65.904   1.433  24.541  1.00 34.96           O
ANISOU 3996  O   GLN B 153     4045   2664   6574    193     90    997       O
ATOM   3997  CB  GLN B 153     -64.649  -1.122  25.352  1.00 38.50           C
ANISOU 3997  CB  GLN B 153     4539   2932   7158    301     74   1121       C
ATOM   3998  CG  GLN B 153     -64.345  -2.605  25.228  1.00 41.39           C
ANISOU 3998  CG  GLN B 153     4948   3188   7589    353     81   1133       C
ATOM   3999  CD  GLN B 153     -65.140  -3.441  26.212  1.00 40.93           C
ANISOU 3999  CD  GLN B 153     4943   3084   7523    297     71   1189       C
ATOM   4000  OE1 GLN B 153     -65.981  -4.250  25.820  1.00 40.79           O
ANISOU 4000  OE1 GLN B 153     4974   2993   7530    260     80   1149       O
ATOM   4001  NE2 GLN B 153     -64.877  -3.248  27.499  1.00 43.96           N
ANISOU 4001  NE2 GLN B 153     5320   3512   7872    292     46   1286       N
ATOM   4002  N   PRO B 154     -67.057   1.197  26.444  1.00 32.12           N
ANISOU 4002  N   PRO B 154     3740   2300   6163    122     81   1106       N
ATOM   4003  CA  PRO B 154     -67.458   2.605  26.450  1.00 33.55           C
ANISOU 4003  CA  PRO B 154     3906   2581   6259     88     79   1070       C
ATOM   4004  C   PRO B 154     -66.352   3.533  26.927  1.00 37.92           C
ANISOU 4004  C   PRO B 154     4440   3207   6762    120     25   1094       C
ATOM   4005  O   PRO B 154     -65.374   3.125  27.559  1.00 34.36           O
ANISOU 4005  O   PRO B 154     3985   2740   6330    160    -16   1160       O
ATOM   4006  CB  PRO B 154     -68.637   2.620  27.427  1.00 34.41           C
ANISOU 4006  CB  PRO B 154     4053   2702   6320     42    104   1123       C
ATOM   4007  CG  PRO B 154     -68.296   1.542  28.400  1.00 33.58           C
ANISOU 4007  CG  PRO B 154     3980   2535   6244     66     94   1220       C
ATOM   4008  CD  PRO B 154     -67.588   0.467  27.607  1.00 32.23           C
ANISOU 4008  CD  PRO B 154     3796   2273   6178    101     86   1198       C
ATOM   4009  N   SER B 155     -66.533   4.810  26.600  1.00 38.51           N
ANISOU 4009  N   SER B 155     4498   3357   6777     96     16   1043       N
ATOM   4010  CA  SER B 155     -65.722   5.896  27.132  1.00 33.65           C
ANISOU 4010  CA  SER B 155     3875   2807   6105    104    -51   1065       C
ATOM   4011  C   SER B 155     -66.665   6.918  27.742  1.00 31.14           C
ANISOU 4011  C   SER B 155     3610   2542   5681     69    -52   1051       C
ATOM   4012  O   SER B 155     -67.491   7.503  27.034  1.00 31.79           O
ANISOU 4012  O   SER B 155     3682   2651   5745     41    -12    986       O
ATOM   4013  CB  SER B 155     -64.858   6.538  26.044  1.00 32.91           C
ANISOU 4013  CB  SER B 155     3709   2747   6049    119    -66   1022       C
ATOM   4014  OG  SER B 155     -64.158   7.659  26.553  1.00 37.64           O
ANISOU 4014  OG  SER B 155     4298   3401   6603    110   -146   1048       O
ATOM   4015  N   VAL B 156     -66.556   7.121  29.053  1.00 31.13           N
ANISOU 4015  N   VAL B 156     3671   2552   5604     80    -98   1112       N
ATOM   4016  CA  VAL B 156     -67.452   8.038  29.748  1.00 34.96           C
ANISOU 4016  CA  VAL B 156     4228   3084   5973     68    -90   1104       C
ATOM   4017  C   VAL B 156     -67.068   9.468  29.394  1.00 41.33           C
ANISOU 4017  C   VAL B 156     5030   3940   6734     56   -150   1049       C
ATOM   4018  O   VAL B 156     -65.938   9.904  29.644  1.00 43.79           O
ANISOU 4018  O   VAL B 156     5335   4256   7047     62   -245   1069       O
ATOM   4019  CB  VAL B 156     -67.407   7.808  31.264  1.00 35.71           C
ANISOU 4019  CB  VAL B 156     4411   3173   5982     99   -122   1186       C
ATOM   4020  CG1 VAL B 156     -68.337   8.780  31.969  1.00 28.06           C
ANISOU 4020  CG1 VAL B 156     3531   2253   4879    109   -102   1176       C
ATOM   4021  CG2 VAL B 156     -67.785   6.372  31.592  1.00 35.53           C
ANISOU 4021  CG2 VAL B 156     4388   3098   6016    107    -61   1253       C
ATOM   4022  N   GLY B 157     -68.009  10.204  28.810  1.00 41.38           N
ANISOU 4022  N   GLY B 157     5035   3979   6708     36   -100    986       N
ATOM   4023  CA  GLY B 157     -67.764  11.563  28.396  1.00 25.55           C
ANISOU 4023  CA  GLY B 157     3029   2013   4666     21   -149    933       C
ATOM   4024  C   GLY B 157     -67.900  12.553  29.534  1.00 34.05           C
ANISOU 4024  C   GLY B 157     4215   3110   5612     38   -209    944       C
ATOM   4025  O   GLY B 157     -67.995  12.179  30.707  1.00 32.32           O
ANISOU 4025  O   GLY B 157     4075   2879   5325     69   -221    998       O
ATOM   4026  N   PRO B 158     -67.907  13.842  29.205  1.00 34.40           N
ANISOU 4026  N   PRO B 158     4277   3181   5615     25   -251    891       N
ATOM   4027  CA  PRO B 158     -68.028  14.868  30.245  1.00 28.85           C
ANISOU 4027  CA  PRO B 158     3701   2484   4779     49   -319    888       C
ATOM   4028  C   PRO B 158     -69.416  14.877  30.866  1.00 27.58           C
ANISOU 4028  C   PRO B 158     3620   2344   4514     92   -222    889       C
ATOM   4029  O   PRO B 158     -70.387  14.358  30.310  1.00 28.64           O
ANISOU 4029  O   PRO B 158     3696   2494   4690     86   -108    884       O
ATOM   4030  CB  PRO B 158     -67.747  16.172  29.492  1.00 25.57           C
ANISOU 4030  CB  PRO B 158     3266   2080   4368     18   -378    830       C
ATOM   4031  CG  PRO B 158     -68.108  15.871  28.077  1.00 24.71           C
ANISOU 4031  CG  PRO B 158     3038   1991   4359     -9   -286    793       C
ATOM   4032  CD  PRO B 158     -67.764  14.426  27.860  1.00 24.81           C
ANISOU 4032  CD  PRO B 158     2976   1983   4466     -8   -242    834       C
ATOM   4033  N   LYS B 159     -69.494  15.483  32.053  1.00 28.42           N
ANISOU 4033  N   LYS B 159     3868   2449   4483    139   -272    902       N
ATOM   4034  CA  LYS B 159     -70.772  15.573  32.751  1.00 29.38           C
ANISOU 4034  CA  LYS B 159     4076   2599   4490    201   -170    917       C
ATOM   4035  C   LYS B 159     -71.748  16.491  32.032  1.00 31.72           C
ANISOU 4035  C   LYS B 159     4356   2928   4767    204   -104    856       C
ATOM   4036  O   LYS B 159     -72.965  16.288  32.117  1.00 34.30           O
ANISOU 4036  O   LYS B 159     4676   3289   5066    238     20    878       O
ATOM   4037  CB  LYS B 159     -70.564  16.070  34.182  1.00 29.67           C
ANISOU 4037  CB  LYS B 159     4289   2622   4362    269   -243    939       C
ATOM   4038  CG  LYS B 159     -69.898  15.079  35.115  1.00 35.15           C
ANISOU 4038  CG  LYS B 159     5018   3291   5045    285   -287   1017       C
ATOM   4039  CD  LYS B 159     -69.853  15.628  36.533  1.00 46.53           C
ANISOU 4039  CD  LYS B 159     6659   4723   6297    365   -354   1033       C
ATOM   4040  CE  LYS B 159     -69.280  14.613  37.508  1.00 58.30           C
ANISOU 4040  CE  LYS B 159     8192   6193   7765    389   -391   1119       C
ATOM   4041  NZ  LYS B 159     -69.290  15.123  38.909  1.00 63.02           N
ANISOU 4041  NZ  LYS B 159     9004   6783   8159    478   -454   1134       N
ATOM   4042  N   GLN B 160     -71.245  17.498  31.328  1.00 29.40           N
ANISOU 4042  N   GLN B 160     4049   2627   4495    170   -183    791       N
ATOM   4043  CA  GLN B 160     -72.081  18.545  30.765  1.00 32.71           C
ANISOU 4043  CA  GLN B 160     4478   3072   4878    182   -140    733       C
ATOM   4044  C   GLN B 160     -72.265  18.358  29.264  1.00 31.85           C
ANISOU 4044  C   GLN B 160     4216   2981   4903    120    -90    699       C
ATOM   4045  O   GLN B 160     -71.454  17.726  28.582  1.00 30.10           O
ANISOU 4045  O   GLN B 160     3898   2744   4794     68   -120    705       O
ATOM   4046  CB  GLN B 160     -71.480  19.926  31.046  1.00 32.57           C
ANISOU 4046  CB  GLN B 160     4572   3025   4779    191   -270    684       C
ATOM   4047  CG  GLN B 160     -70.241  20.261  30.221  1.00 39.58           C
ANISOU 4047  CG  GLN B 160     5379   3884   5775    111   -387    663       C
ATOM   4048  CD  GLN B 160     -68.960  19.678  30.794  1.00 43.74           C
ANISOU 4048  CD  GLN B 160     5905   4376   6339     86   -499    714       C
ATOM   4049  OE1 GLN B 160     -68.985  18.705  31.546  1.00 46.74           O
ANISOU 4049  OE1 GLN B 160     6307   4756   6697    115   -469    765       O
ATOM   4050  NE2 GLN B 160     -67.830  20.281  30.441  1.00 44.82           N
ANISOU 4050  NE2 GLN B 160     6009   4483   6537     31   -630    710       N
ATOM   4051  N   ALA B 161     -73.358  18.927  28.760  1.00 31.36           N
ANISOU 4051  N   ALA B 161     4140   2953   4821    136    -12    667       N
ATOM   4052  CA  ALA B 161     -73.641  18.939  27.334  1.00 29.56           C
ANISOU 4052  CA  ALA B 161     3790   2744   4696     85     26    628       C
ATOM   4053  C   ALA B 161     -74.348  20.244  27.005  1.00 31.66           C
ANISOU 4053  C   ALA B 161     4094   3034   4901    111     38    579       C
ATOM   4054  O   ALA B 161     -74.752  20.997  27.894  1.00 34.89           O
ANISOU 4054  O   ALA B 161     4622   3444   5190    176     36    578       O
ATOM   4055  CB  ALA B 161     -74.481  17.730  26.914  1.00 27.81           C
ANISOU 4055  CB  ALA B 161     3473   2540   4555     67    130    660       C
ATOM   4056  N   SER B 162     -74.497  20.506  25.711  1.00 30.48           N
ANISOU 4056  N   SER B 162     3852   2900   4827     68     51    538       N
ATOM   4057  CA  SER B 162     -75.111  21.736  25.231  1.00 30.21           C
ANISOU 4057  CA  SER B 162     3841   2886   4752     87     58    493       C
ATOM   4058  C   SER B 162     -76.580  21.479  24.927  1.00 29.33           C
ANISOU 4058  C   SER B 162     3675   2821   4649    110    175    506       C
ATOM   4059  O   SER B 162     -76.909  20.586  24.140  1.00 33.85           O
ANISOU 4059  O   SER B 162     4140   3406   5316     66    219    514       O
ATOM   4060  CB  SER B 162     -74.388  22.257  23.990  1.00 29.39           C
ANISOU 4060  CB  SER B 162     3670   2775   4721     30     -1    451       C
ATOM   4061  OG  SER B 162     -75.025  23.416  23.483  1.00 35.66           O
ANISOU 4061  OG  SER B 162     4483   3587   5480     48      8    412       O
ATOM   4062  N   LEU B 163     -77.457  22.258  25.551  1.00 29.00           N
ANISOU 4062  N   LEU B 163     3710   2800   4510    183    219    511       N
ATOM   4063  CA  LEU B 163     -78.895  22.195  25.303  1.00 32.04           C
ANISOU 4063  CA  LEU B 163     4035   3236   4904    214    329    537       C
ATOM   4064  C   LEU B 163     -79.340  23.562  24.794  1.00 33.66           C
ANISOU 4064  C   LEU B 163     4270   3455   5065    247    322    488       C
ATOM   4065  O   LEU B 163     -79.480  24.506  25.579  1.00 37.56           O
ANISOU 4065  O   LEU B 163     4888   3940   5444    327    315    478       O
ATOM   4066  CB  LEU B 163     -79.659  21.795  26.560  1.00 34.03           C
ANISOU 4066  CB  LEU B 163     4340   3512   5080    291    417    610       C
ATOM   4067  CG  LEU B 163     -81.181  21.786  26.407  1.00 34.39           C
ANISOU 4067  CG  LEU B 163     4311   3617   5141    331    538    660       C
ATOM   4068  CD1 LEU B 163     -81.603  20.819  25.312  1.00 31.33           C
ANISOU 4068  CD1 LEU B 163     3760   3241   4904    238    558    677       C
ATOM   4069  CD2 LEU B 163     -81.860  21.443  27.721  1.00 34.44           C
ANISOU 4069  CD2 LEU B 163     4371   3651   5064    421    637    750       C
ATOM   4070  N   ASN B 164     -79.555  23.663  23.481  1.00 29.47           N
ANISOU 4070  N   ASN B 164     3637   2941   4619    192    319    457       N
ATOM   4071  CA  ASN B 164     -79.996  24.904  22.843  1.00 30.80           C
ANISOU 4071  CA  ASN B 164     3818   3124   4761    217    311    416       C
ATOM   4072  C   ASN B 164     -79.024  26.047  23.129  1.00 36.94           C
ANISOU 4072  C   ASN B 164     4716   3850   5469    232    211    370       C
ATOM   4073  O   ASN B 164     -79.427  27.165  23.454  1.00 42.40           O
ANISOU 4073  O   ASN B 164     5500   4534   6077    300    209    351       O
ATOM   4074  CB  ASN B 164     -81.414  25.276  23.279  1.00 30.98           C
ANISOU 4074  CB  ASN B 164     3848   3194   4731    304    412    455       C
ATOM   4075  CG  ASN B 164     -82.403  24.154  23.050  1.00 34.29           C
ANISOU 4075  CG  ASN B 164     4135   3658   5235    279    500    519       C
ATOM   4076  OD1 ASN B 164     -82.375  23.488  22.015  1.00 39.13           O
ANISOU 4076  OD1 ASN B 164     4640   4273   5953    195    479    507       O
ATOM   4077  ND2 ASN B 164     -83.278  23.930  24.023  1.00 34.31           N
ANISOU 4077  ND2 ASN B 164     4151   3694   5190    353    595    592       N
ATOM   4078  N   GLY B 165     -77.731  25.761  23.010  1.00 34.78           N
ANISOU 4078  N   GLY B 165     4441   3537   5236    168    124    358       N
ATOM   4079  CA  GLY B 165     -76.706  26.746  23.270  1.00 28.39           C
ANISOU 4079  CA  GLY B 165     3729   2673   4386    161      9    329       C
ATOM   4080  C   GLY B 165     -76.352  26.936  24.725  1.00 28.04           C
ANISOU 4080  C   GLY B 165     3833   2586   4236    215    -40    339       C
ATOM   4081  O   GLY B 165     -75.462  27.741  25.026  1.00 34.71           O
ANISOU 4081  O   GLY B 165     4769   3370   5048    202   -159    317       O
ATOM   4082  N   VAL B 166     -77.011  26.227  25.636  1.00 28.79           N
ANISOU 4082  N   VAL B 166     3958   2705   4276    274     41    376       N
ATOM   4083  CA  VAL B 166     -76.760  26.342  27.067  1.00 30.19           C
ANISOU 4083  CA  VAL B 166     4292   2847   4333    342      5    389       C
ATOM   4084  C   VAL B 166     -76.021  25.091  27.518  1.00 27.27           C
ANISOU 4084  C   VAL B 166     3884   2472   4007    298    -14    433       C
ATOM   4085  O   VAL B 166     -76.571  23.983  27.467  1.00 31.91           O
ANISOU 4085  O   VAL B 166     4379   3101   4645    293     85    479       O
ATOM   4086  CB  VAL B 166     -78.062  26.530  27.858  1.00 34.80           C
ANISOU 4086  CB  VAL B 166     4952   3467   4802    463    123    412       C
ATOM   4087  CG1 VAL B 166     -77.756  26.774  29.328  1.00 36.78           C
ANISOU 4087  CG1 VAL B 166     5397   3676   4902    548     78    417       C
ATOM   4088  CG2 VAL B 166     -78.877  27.673  27.275  1.00 25.09           C
ANISOU 4088  CG2 VAL B 166     3735   2249   3547    510    156    376       C
ATOM   4089  N   THR B 167     -74.777  25.266  27.952  1.00 26.06           N
ANISOU 4089  N   THR B 167     3798   2261   3844    264   -148    425       N
ATOM   4090  CA  THR B 167     -73.989  24.159  28.472  1.00 32.19           C
ANISOU 4090  CA  THR B 167     4550   3026   4656    232   -180    471       C
ATOM   4091  C   THR B 167     -74.318  23.945  29.944  1.00 35.15           C
ANISOU 4091  C   THR B 167     5069   3394   4892    322   -159    502       C
ATOM   4092  O   THR B 167     -74.225  24.875  30.751  1.00 36.09           O
ANISOU 4092  O   THR B 167     5357   3472   4882    384   -231    473       O
ATOM   4093  CB  THR B 167     -72.497  24.435  28.293  1.00 35.27           C
ANISOU 4093  CB  THR B 167     4934   3363   5105    157   -336    464       C
ATOM   4094  OG1 THR B 167     -72.210  24.613  26.901  1.00 44.64           O
ANISOU 4094  OG1 THR B 167     5983   4564   6413     86   -336    446       O
ATOM   4095  CG2 THR B 167     -71.675  23.276  28.829  1.00 28.04           C
ANISOU 4095  CG2 THR B 167     3986   2437   4230    132   -369    518       C
ATOM   4096  N   LEU B 168     -74.696  22.718  30.294  1.00 33.45           N
ANISOU 4096  N   LEU B 168     4798   3214   4699    334    -65    562       N
ATOM   4097  CA  LEU B 168     -75.197  22.449  31.633  1.00 35.66           C
ANISOU 4097  CA  LEU B 168     5203   3502   4844    431    -11    608       C
ATOM   4098  C   LEU B 168     -74.999  20.981  31.979  1.00 34.31           C
ANISOU 4098  C   LEU B 168     4960   3344   4734    405     32    683       C
ATOM   4099  O   LEU B 168     -74.932  20.123  31.096  1.00 33.26           O
ANISOU 4099  O   LEU B 168     4670   3223   4744    329     67    698       O
ATOM   4100  CB  LEU B 168     -76.680  22.825  31.745  1.00 40.28           C
ANISOU 4100  CB  LEU B 168     5807   4141   5357    523    136    621       C
ATOM   4101  CG  LEU B 168     -77.596  22.278  30.642  1.00 38.13           C
ANISOU 4101  CG  LEU B 168     5346   3924   5217    476    255    644       C
ATOM   4102  CD1 LEU B 168     -78.177  20.916  31.005  1.00 37.02           C
ANISOU 4102  CD1 LEU B 168     5122   3820   5123    477    367    737       C
ATOM   4103  CD2 LEU B 168     -78.706  23.266  30.316  1.00 36.64           C
ANISOU 4103  CD2 LEU B 168     5169   3772   4982    542    332    621       C
ATOM   4104  N   ILE B 169     -74.914  20.709  33.277  1.00 33.14           N
ANISOU 4104  N   ILE B 169     4941   3186   4466    476     27    727       N
ATOM   4105  CA  ILE B 169     -74.966  19.349  33.799  1.00 33.59           C
ANISOU 4105  CA  ILE B 169     4950   3257   4554    476     92    814       C
ATOM   4106  C   ILE B 169     -76.424  19.058  34.129  1.00 38.78           C
ANISOU 4106  C   ILE B 169     5593   3975   5166    552    269    878       C
ATOM   4107  O   ILE B 169     -76.976  19.607  35.086  1.00 43.74           O
ANISOU 4107  O   ILE B 169     6364   4622   5634    666    317    896       O
ATOM   4108  CB  ILE B 169     -74.068  19.177  35.029  1.00 35.52           C
ANISOU 4108  CB  ILE B 169     5340   3462   4695    512    -12    840       C
ATOM   4109  CG1 ILE B 169     -72.617  19.505  34.675  1.00 37.50           C
ANISOU 4109  CG1 ILE B 169     5584   3655   5010    430   -196    792       C
ATOM   4110  CG2 ILE B 169     -74.183  17.761  35.571  1.00 31.09           C
ANISOU 4110  CG2 ILE B 169     4731   2915   4166    516     64    939       C
ATOM   4111  CD1 ILE B 169     -71.666  19.382  35.842  1.00 41.94           C
ANISOU 4111  CD1 ILE B 169     6283   4172   5480    456   -326    819       C
ATOM   4112  N   GLY B 170     -77.049  18.198  33.332  1.00 36.78           N
ANISOU 4112  N   GLY B 170     5168   3751   5055    492    365    918       N
ATOM   4113  CA  GLY B 170     -78.487  18.042  33.405  1.00 38.71           C
ANISOU 4113  CA  GLY B 170     5359   4056   5292    544    525    984       C
ATOM   4114  C   GLY B 170     -78.953  17.415  34.706  1.00 41.22           C
ANISOU 4114  C   GLY B 170     5750   4400   5512    632    619   1094       C
ATOM   4115  O   GLY B 170     -78.289  16.562  35.296  1.00 39.15           O
ANISOU 4115  O   GLY B 170     5514   4109   5254    616    581   1140       O
ATOM   4116  N   GLU B 171     -80.124  17.861  35.155  1.00 40.06           N
ANISOU 4116  N   GLU B 171     5634   4311   5275    736    751   1145       N
ATOM   4117  CA  GLU B 171     -80.822  17.278  36.294  1.00 40.03           C
ANISOU 4117  CA  GLU B 171     5673   4350   5185    832    881   1274       C
ATOM   4118  C   GLU B 171     -82.153  16.667  35.889  1.00 41.30           C
ANISOU 4118  C   GLU B 171     5656   4572   5464    815   1039   1382       C
ATOM   4119  O   GLU B 171     -82.440  15.518  36.246  1.00 43.50           O
ANISOU 4119  O   GLU B 171     5859   4859   5810    790   1109   1499       O
ATOM   4120  CB  GLU B 171     -81.040  18.339  37.383  1.00 46.31           C
ANISOU 4120  CB  GLU B 171     6683   5165   5746    998    911   1262       C
ATOM   4121  CG  GLU B 171     -79.765  19.015  37.855  1.00 53.72           C
ANISOU 4121  CG  GLU B 171     7815   6034   6563   1013    733   1158       C
ATOM   4122  CD  GLU B 171     -80.028  20.090  38.892  1.00 63.66           C
ANISOU 4122  CD  GLU B 171     9308   7298   7581   1183    751   1135       C
ATOM   4123  OE1 GLU B 171     -81.176  20.183  39.376  1.00 66.83           O
ANISOU 4123  OE1 GLU B 171     9726   7767   7898   1307    923   1216       O
ATOM   4124  OE2 GLU B 171     -79.087  20.845  39.220  1.00 66.05           O
ANISOU 4124  OE2 GLU B 171     9782   7534   7780   1196    589   1039       O
ATOM   4125  N   ALA B 172     -82.979  17.409  35.152  1.00 39.81           N
ANISOU 4125  N   ALA B 172     5395   4422   5308    825   1090   1353       N
ATOM   4126  CA  ALA B 172     -84.189  16.856  34.560  1.00 43.09           C
ANISOU 4126  CA  ALA B 172     5615   4888   5869    783   1208   1450       C
ATOM   4127  C   ALA B 172     -83.913  16.107  33.265  1.00 40.10           C
ANISOU 4127  C   ALA B 172     5072   4465   5701    614   1124   1408       C
ATOM   4128  O   ALA B 172     -84.822  15.463  32.731  1.00 42.55           O
ANISOU 4128  O   ALA B 172     5216   4798   6152    553   1191   1488       O
ATOM   4129  CB  ALA B 172     -85.208  17.970  34.305  1.00 44.04           C
ANISOU 4129  CB  ALA B 172     5723   5070   5939    871   1294   1442       C
ATOM   4130  N   VAL B 173     -82.684  16.183  32.751  1.00 38.64           N
ANISOU 4130  N   VAL B 173     4931   4215   5537    541    977   1290       N
ATOM   4131  CA  VAL B 173     -82.269  15.472  31.550  1.00 42.94           C
ANISOU 4131  CA  VAL B 173     5348   4711   6257    400    896   1241       C
ATOM   4132  C   VAL B 173     -80.841  14.993  31.773  1.00 43.10           C
ANISOU 4132  C   VAL B 173     5440   4664   6271    362    781   1194       C
ATOM   4133  O   VAL B 173     -80.129  15.484  32.652  1.00 48.11           O
ANISOU 4133  O   VAL B 173     6222   5289   6770    430    735   1172       O
ATOM   4134  CB  VAL B 173     -82.367  16.361  30.287  1.00 48.16           C
ANISOU 4134  CB  VAL B 173     5956   5377   6965    359    844   1133       C
ATOM   4135  CG1 VAL B 173     -81.223  17.367  30.249  1.00 44.96           C
ANISOU 4135  CG1 VAL B 173     5678   4939   6464    379    730   1015       C
ATOM   4136  CG2 VAL B 173     -82.409  15.513  29.020  1.00 54.49           C
ANISOU 4136  CG2 VAL B 173     6609   6145   7948    231    801   1113       C
ATOM   4137  N   LYS B 174     -80.425  14.012  30.979  1.00 40.40           N
ANISOU 4137  N   LYS B 174     5000   4272   6078    255    729   1181       N
ATOM   4138  CA  LYS B 174     -79.097  13.427  31.107  1.00 42.85           C
ANISOU 4138  CA  LYS B 174     5354   4521   6407    220    630   1151       C
ATOM   4139  C   LYS B 174     -78.161  14.041  30.074  1.00 38.33           C
ANISOU 4139  C   LYS B 174     4775   3921   5868    172    520   1027       C
ATOM   4140  O   LYS B 174     -78.467  14.046  28.877  1.00 36.07           O
ANISOU 4140  O   LYS B 174     4392   3633   5679    112    515    979       O
ATOM   4141  CB  LYS B 174     -79.151  11.907  30.947  1.00 49.16           C
ANISOU 4141  CB  LYS B 174     6063   5274   7343    150    646   1221       C
ATOM   4142  CG  LYS B 174     -77.993  11.181  31.614  1.00 56.73           C
ANISOU 4142  CG  LYS B 174     7086   6179   8288    153    582   1242       C
ATOM   4143  CD  LYS B 174     -78.355   9.743  31.948  1.00 60.65           C
ANISOU 4143  CD  LYS B 174     7526   6638   8879    118    633   1352       C
ATOM   4144  CE  LYS B 174     -77.676   8.764  31.008  1.00 64.10           C
ANISOU 4144  CE  LYS B 174     7895   6995   9463     34    561   1310       C
ATOM   4145  NZ  LYS B 174     -76.192   8.837  31.110  1.00 66.61           N
ANISOU 4145  NZ  LYS B 174     8279   7280   9750     49    460   1252       N
ATOM   4146  N   THR B 175     -77.026  14.560  30.543  1.00 37.69           N
ANISOU 4146  N   THR B 175     4796   3820   5706    199    428    984       N
ATOM   4147  CA  THR B 175     -76.036  15.196  29.683  1.00 32.52           C
ANISOU 4147  CA  THR B 175     4133   3142   5081    158    323    888       C
ATOM   4148  C   THR B 175     -74.718  14.436  29.620  1.00 34.19           C
ANISOU 4148  C   THR B 175     4330   3301   5358    118    237    888       C
ATOM   4149  O   THR B 175     -73.822  14.842  28.873  1.00 36.90           O
ANISOU 4149  O   THR B 175     4647   3628   5743     84    158    827       O
ATOM   4150  CB  THR B 175     -75.773  16.635  30.147  1.00 26.62           C
ANISOU 4150  CB  THR B 175     3505   2408   4200    215    267    839       C
ATOM   4151  OG1 THR B 175     -75.367  16.633  31.521  1.00 27.24           O
ANISOU 4151  OG1 THR B 175     3715   2474   4160    278    236    882       O
ATOM   4152  CG2 THR B 175     -77.025  17.485  29.994  1.00 25.82           C
ANISOU 4152  CG2 THR B 175     3410   2357   4045    261    351    828       C
ATOM   4153  N   GLN B 176     -74.571  13.352  30.377  1.00 35.73           N
ANISOU 4153  N   GLN B 176     4536   3472   5566    126    256    964       N
ATOM   4154  CA  GLN B 176     -73.361  12.541  30.360  1.00 33.77           C
ANISOU 4154  CA  GLN B 176     4270   3173   5386     99    182    975       C
ATOM   4155  C   GLN B 176     -73.602  11.311  29.493  1.00 35.38           C
ANISOU 4155  C   GLN B 176     4366   3342   5735     45    226    987       C
ATOM   4156  O   GLN B 176     -74.552  10.557  29.730  1.00 36.86           O
ANISOU 4156  O   GLN B 176     4527   3525   5952     38    305   1048       O
ATOM   4157  CB  GLN B 176     -72.952  12.135  31.775  1.00 37.61           C
ANISOU 4157  CB  GLN B 176     4853   3647   5791    148    159   1051       C
ATOM   4158  CG  GLN B 176     -71.637  11.378  31.838  1.00 37.21           C
ANISOU 4158  CG  GLN B 176     4785   3547   5806    128     73   1070       C
ATOM   4159  CD  GLN B 176     -71.000  11.437  33.210  1.00 43.51           C
ANISOU 4159  CD  GLN B 176     5700   4337   6496    179      5   1124       C
ATOM   4160  OE1 GLN B 176     -71.687  11.403  34.231  1.00 49.49           O
ANISOU 4160  OE1 GLN B 176     6543   5113   7146    234     60   1180       O
ATOM   4161  NE2 GLN B 176     -69.677  11.540  33.242  1.00 45.85           N
ANISOU 4161  NE2 GLN B 176     5999   4606   6816    167   -115   1115       N
ATOM   4162  N   PHE B 177     -72.745  11.110  28.496  1.00 36.99           N
ANISOU 4162  N   PHE B 177     4511   3517   6027     10    173    934       N
ATOM   4163  CA  PHE B 177     -72.908  10.030  27.537  1.00 36.84           C
ANISOU 4163  CA  PHE B 177     4411   3453   6133    -32    202    924       C
ATOM   4164  C   PHE B 177     -71.697   9.109  27.546  1.00 34.31           C
ANISOU 4164  C   PHE B 177     4082   3077   5879    -27    152    944       C
ATOM   4165  O   PHE B 177     -70.614   9.467  28.016  1.00 34.55           O
ANISOU 4165  O   PHE B 177     4140   3112   5874     -1     85    954       O
ATOM   4166  CB  PHE B 177     -73.105  10.564  26.111  1.00 35.09           C
ANISOU 4166  CB  PHE B 177     4131   3247   5956    -63    202    836       C
ATOM   4167  CG  PHE B 177     -74.041  11.729  26.018  1.00 34.41           C
ANISOU 4167  CG  PHE B 177     4053   3220   5800    -60    232    807       C
ATOM   4168  CD1 PHE B 177     -75.387  11.578  26.304  1.00 33.85           C
ANISOU 4168  CD1 PHE B 177     3970   3170   5723    -64    305    848       C
ATOM   4169  CD2 PHE B 177     -73.578  12.975  25.625  1.00 32.72           C
ANISOU 4169  CD2 PHE B 177     3854   3040   5536    -50    187    748       C
ATOM   4170  CE1 PHE B 177     -76.252  12.651  26.212  1.00 37.54           C
ANISOU 4170  CE1 PHE B 177     4441   3693   6128    -49    339    828       C
ATOM   4171  CE2 PHE B 177     -74.437  14.052  25.529  1.00 29.95           C
ANISOU 4171  CE2 PHE B 177     3518   2738   5123    -40    214    720       C
ATOM   4172  CZ  PHE B 177     -75.775  13.890  25.823  1.00 33.05           C
ANISOU 4172  CZ  PHE B 177     3901   3154   5504    -34    292    759       C
ATOM   4173  N   ASN B 178     -71.906   7.908  27.019  1.00 32.86           N
ANISOU 4173  N   ASN B 178     3856   2833   5794    -50    180    953       N
ATOM   4174  CA  ASN B 178     -70.803   7.066  26.590  1.00 33.42           C
ANISOU 4174  CA  ASN B 178     3905   2847   5944    -37    144    948       C
ATOM   4175  C   ASN B 178     -70.390   7.465  25.180  1.00 34.34           C
ANISOU 4175  C   ASN B 178     3975   2972   6101    -42    131    860       C
ATOM   4176  O   ASN B 178     -71.217   7.884  24.366  1.00 34.44           O
ANISOU 4176  O   ASN B 178     3967   3004   6114    -70    158    804       O
ATOM   4177  CB  ASN B 178     -71.196   5.589  26.621  1.00 35.79           C
ANISOU 4177  CB  ASN B 178     4202   3066   6332    -53    173    992       C
ATOM   4178  CG  ASN B 178     -71.469   5.086  28.022  1.00 33.49           C
ANISOU 4178  CG  ASN B 178     3953   2764   6006    -42    190   1097       C
ATOM   4179  OD1 ASN B 178     -70.922   5.600  28.996  1.00 33.53           O
ANISOU 4179  OD1 ASN B 178     4004   2808   5927     -6    160   1136       O
ATOM   4180  ND2 ASN B 178     -72.317   4.071  28.131  1.00 30.62           N
ANISOU 4180  ND2 ASN B 178     3582   2346   5708    -74    232   1149       N
ATOM   4181  N   TYR B 179     -69.100   7.342  24.895  1.00 31.99           N
ANISOU 4181  N   TYR B 179     3657   2662   5836     -8     92    857       N
ATOM   4182  CA  TYR B 179     -68.559   7.725  23.601  1.00 27.83           C
ANISOU 4182  CA  TYR B 179     3085   2150   5340      4     91    790       C
ATOM   4183  C   TYR B 179     -67.913   6.523  22.930  1.00 26.46           C
ANISOU 4183  C   TYR B 179     2895   1907   5251     42    104    785       C
ATOM   4184  O   TYR B 179     -67.282   5.693  23.592  1.00 32.15           O
ANISOU 4184  O   TYR B 179     3625   2584   6006     72     88    846       O
ATOM   4185  CB  TYR B 179     -67.547   8.864  23.742  1.00 26.83           C
ANISOU 4185  CB  TYR B 179     2936   2083   5177     18     38    800       C
ATOM   4186  CG  TYR B 179     -68.189  10.222  23.911  1.00 33.06           C
ANISOU 4186  CG  TYR B 179     3745   2932   5883    -12     26    771       C
ATOM   4187  CD1 TYR B 179     -68.730  10.610  25.129  1.00 32.76           C
ANISOU 4187  CD1 TYR B 179     3770   2910   5768    -20     11    806       C
ATOM   4188  CD2 TYR B 179     -68.256  11.116  22.850  1.00 40.05           C
ANISOU 4188  CD2 TYR B 179     4597   3856   6763    -23     33    711       C
ATOM   4189  CE1 TYR B 179     -69.320  11.850  25.286  1.00 35.30           C
ANISOU 4189  CE1 TYR B 179     4124   3279   6008    -32      3    777       C
ATOM   4190  CE2 TYR B 179     -68.843  12.360  22.998  1.00 43.10           C
ANISOU 4190  CE2 TYR B 179     5008   4290   7077    -46     21    686       C
ATOM   4191  CZ  TYR B 179     -69.374  12.721  24.218  1.00 41.86           C
ANISOU 4191  CZ  TYR B 179     4919   4143   6845    -48      5    716       C
ATOM   4192  OH  TYR B 179     -69.958  13.958  24.371  1.00 42.41           O
ANISOU 4192  OH  TYR B 179     5025   4252   6837    -55     -4    687       O
ATOM   4193  N   TYR B 180     -68.085   6.436  21.613  1.00 29.82           N
ANISOU 4193  N   TYR B 180     3307   2320   5703     50    131    712       N
ATOM   4194  CA  TYR B 180     -67.528   5.359  20.809  1.00 32.09           C
ANISOU 4194  CA  TYR B 180     3599   2537   6055    102    149    690       C
ATOM   4195  C   TYR B 180     -67.049   5.942  19.488  1.00 33.09           C
ANISOU 4195  C   TYR B 180     3697   2704   6172    141    170    628       C
ATOM   4196  O   TYR B 180     -67.642   6.887  18.963  1.00 32.37           O
ANISOU 4196  O   TYR B 180     3596   2666   6036    106    175    581       O
ATOM   4197  CB  TYR B 180     -68.559   4.250  20.555  1.00 29.76           C
ANISOU 4197  CB  TYR B 180     3355   2151   5802     73    161    662       C
ATOM   4198  CG  TYR B 180     -69.325   3.824  21.789  1.00 29.82           C
ANISOU 4198  CG  TYR B 180     3382   2132   5815     22    153    731       C
ATOM   4199  CD1 TYR B 180     -70.491   4.478  22.167  1.00 29.37           C
ANISOU 4199  CD1 TYR B 180     3320   2122   5718    -42    162    737       C
ATOM   4200  CD2 TYR B 180     -68.886   2.766  22.573  1.00 32.81           C
ANISOU 4200  CD2 TYR B 180     3784   2443   6240     45    145    800       C
ATOM   4201  CE1 TYR B 180     -71.193   4.095  23.291  1.00 26.55           C
ANISOU 4201  CE1 TYR B 180     2977   1749   5361    -77    172    815       C
ATOM   4202  CE2 TYR B 180     -69.585   2.373  23.699  1.00 34.16           C
ANISOU 4202  CE2 TYR B 180     3973   2594   6412      3    146    876       C
ATOM   4203  CZ  TYR B 180     -70.737   3.042  24.054  1.00 31.46           C
ANISOU 4203  CZ  TYR B 180     3623   2305   6025    -56    164    886       C
ATOM   4204  OH  TYR B 180     -71.435   2.656  25.174  1.00 30.28           O
ANISOU 4204  OH  TYR B 180     3488   2144   5873    -86    182    975       O
ATOM   4205  N   LYS B 181     -65.971   5.372  18.952  1.00 34.25           N
ANISOU 4205  N   LYS B 181     3829   2825   6359    222    190    636       N
ATOM   4206  CA  LYS B 181     -65.370   5.883  17.728  1.00 31.54           C
ANISOU 4206  CA  LYS B 181     3455   2526   6004    277    224    598       C
ATOM   4207  C   LYS B 181     -64.866   4.734  16.868  1.00 30.01           C
ANISOU 4207  C   LYS B 181     3299   2259   5846    373    266    569       C
ATOM   4208  O   LYS B 181     -64.272   3.779  17.376  1.00 29.21           O
ANISOU 4208  O   LYS B 181     3206   2098   5795    420    265    617       O
ATOM   4209  CB  LYS B 181     -64.215   6.846  18.033  1.00 33.22           C
ANISOU 4209  CB  LYS B 181     3580   2822   6218    296    210    670       C
ATOM   4210  CG  LYS B 181     -63.589   7.470  16.797  1.00 35.84           C
ANISOU 4210  CG  LYS B 181     3864   3212   6542    351    255    652       C
ATOM   4211  CD  LYS B 181     -62.392   8.335  17.155  1.00 43.13           C
ANISOU 4211  CD  LYS B 181     4686   4208   7492    359    231    746       C
ATOM   4212  CE  LYS B 181     -61.784   8.971  15.915  1.00 51.13           C
ANISOU 4212  CE  LYS B 181     5640   5284   8503    413    286    748       C
ATOM   4213  NZ  LYS B 181     -60.570   9.774  16.233  1.00 58.97           N
ANISOU 4213  NZ  LYS B 181     6517   6343   9546    414    256    858       N
ATOM   4214  N   LYS B 182     -65.105   4.838  15.563  1.00 32.49           N
ANISOU 4214  N   LYS B 182     3644   2573   6127    408    301    489       N
ATOM   4215  CA  LYS B 182     -64.614   3.881  14.583  1.00 30.45           C
ANISOU 4215  CA  LYS B 182     3442   2249   5878    519    347    448       C
ATOM   4216  C   LYS B 182     -63.788   4.611  13.536  1.00 31.26           C
ANISOU 4216  C   LYS B 182     3497   2433   5945    603    408    448       C
ATOM   4217  O   LYS B 182     -64.157   5.701  13.091  1.00 30.72           O
ANISOU 4217  O   LYS B 182     3400   2441   5829    558    409    425       O
ATOM   4218  CB  LYS B 182     -65.761   3.135  13.897  1.00 33.96           C
ANISOU 4218  CB  LYS B 182     4002   2596   6306    496    325    345       C
ATOM   4219  CG  LYS B 182     -66.480   2.138  14.781  1.00 44.73           C
ANISOU 4219  CG  LYS B 182     5415   3856   7724    431    273    357       C
ATOM   4220  CD  LYS B 182     -67.634   1.487  14.037  1.00 45.07           C
ANISOU 4220  CD  LYS B 182     5562   3800   7763    392    233    262       C
ATOM   4221  CE  LYS B 182     -67.142   0.722  12.821  1.00 39.47           C
ANISOU 4221  CE  LYS B 182     4952   3014   7032    513    257    186       C
ATOM   4222  NZ  LYS B 182     -68.269   0.191  12.005  1.00 33.97           N
ANISOU 4222  NZ  LYS B 182     4368   2217   6323    470    195     84       N
ATOM   4223  N   VAL B 183     -62.670   4.004  13.148  1.00 34.50           N
ANISOU 4223  N   VAL B 183     3898   2830   6382    731    466    484       N
ATOM   4224  CA  VAL B 183     -61.811   4.523  12.091  1.00 34.13           C
ANISOU 4224  CA  VAL B 183     3806   2858   6305    835    545    500       C
ATOM   4225  C   VAL B 183     -61.521   3.382  11.129  1.00 38.88           C
ANISOU 4225  C   VAL B 183     4512   3377   6885    981    608    443       C
ATOM   4226  O   VAL B 183     -60.926   2.371  11.523  1.00 44.73           O
ANISOU 4226  O   VAL B 183     5268   4049   7677   1056    622    480       O
ATOM   4227  CB  VAL B 183     -60.502   5.114  12.641  1.00 35.99           C
ANISOU 4227  CB  VAL B 183     3892   3182   6599    863    565    637       C
ATOM   4228  CG1 VAL B 183     -59.581   5.509  11.499  1.00 34.35           C
ANISOU 4228  CG1 VAL B 183     3629   3050   6374    985    663    673       C
ATOM   4229  CG2 VAL B 183     -60.792   6.313  13.527  1.00 32.63           C
ANISOU 4229  CG2 VAL B 183     3389   2828   6182    724    490    680       C
ATOM   4230  N   ASP B 184     -61.949   3.539   9.875  1.00 39.89           N
ANISOU 4230  N   ASP B 184     4698   3448   7012     34    322    474       N
ATOM   4231  CA  ASP B 184     -61.739   2.535   8.829  1.00 42.95           C
ANISOU 4231  CA  ASP B 184     5153   3796   7369     32    403    382       C
ATOM   4232  C   ASP B 184     -62.358   1.192   9.213  1.00 40.70           C
ANISOU 4232  C   ASP B 184     5032   3408   7024    109    259    431       C
ATOM   4233  O   ASP B 184     -61.768   0.130   9.004  1.00 41.84           O
ANISOU 4233  O   ASP B 184     5214   3471   7215    221    234    309       O
ATOM   4234  CB  ASP B 184     -60.253   2.378   8.502  1.00 48.56           C
ANISOU 4234  CB  ASP B 184     5664   4548   8237     93    514    127       C
ATOM   4235  CG  ASP B 184     -59.616   3.677   8.048  1.00 52.47           C
ANISOU 4235  CG  ASP B 184     6049   5146   8742    -83    718     42       C
ATOM   4236  OD1 ASP B 184     -60.336   4.527   7.483  1.00 50.66           O
ANISOU 4236  OD1 ASP B 184     6004   4898   8348   -253    789    193       O
ATOM   4237  OD2 ASP B 184     -58.396   3.848   8.256  1.00 55.21           O
ANISOU 4237  OD2 ASP B 184     6146   5586   9246    -55    794   -201       O
ATOM   4238  N   GLY B 185     -63.562   1.240   9.780  1.00 38.50           N
ANISOU 4238  N   GLY B 185     4868   3132   6626     32    170    577       N
ATOM   4239  CA  GLY B 185     -64.279   0.043  10.164  1.00 33.27           C
ANISOU 4239  CA  GLY B 185     4420   2375   5845      2     77    612       C
ATOM   4240  C   GLY B 185     -63.794  -0.628  11.430  1.00 32.07           C
ANISOU 4240  C   GLY B 185     4386   2078   5722    120    -92    593       C
ATOM   4241  O   GLY B 185     -64.342  -1.673  11.802  1.00 44.22           O
ANISOU 4241  O   GLY B 185     6208   3485   7110     55   -167    621       O
ATOM   4242  N   VAL B 186     -62.795  -0.068  12.106  1.00 32.34           N
ANISOU 4242  N   VAL B 186     4257   2115   5914    272   -164    536       N
ATOM   4243  CA  VAL B 186     -62.232  -0.646  13.320  1.00 37.79           C
ANISOU 4243  CA  VAL B 186     5087   2645   6626    430   -385    504       C
ATOM   4244  C   VAL B 186     -62.541   0.281  14.486  1.00 37.34           C
ANISOU 4244  C   VAL B 186     4975   2647   6564    355   -436    595       C
ATOM   4245  O   VAL B 186     -62.274   1.487  14.417  1.00 39.09           O
ANISOU 4245  O   VAL B 186     4926   3025   6903    341   -344    590       O
ATOM   4246  CB  VAL B 186     -60.716  -0.873  13.186  1.00 40.60           C
ANISOU 4246  CB  VAL B 186     5267   2973   7188    714   -474    290       C
ATOM   4247  CG1 VAL B 186     -60.162  -1.520  14.447  1.00 37.36           C
ANISOU 4247  CG1 VAL B 186     5056   2360   6779    937   -788    243       C
ATOM   4248  CG2 VAL B 186     -60.415  -1.724  11.963  1.00 42.11           C
ANISOU 4248  CG2 VAL B 186     5477   3129   7394    776   -389    161       C
ATOM   4249  N   VAL B 187     -63.101  -0.281  15.556  1.00 37.43           N
ANISOU 4249  N   VAL B 187     5290   2517   6414    275   -568    669       N
ATOM   4250  CA  VAL B 187     -63.417   0.506  16.741  1.00 33.50           C
ANISOU 4250  CA  VAL B 187     4774   2064   5889    179   -609    736       C
ATOM   4251  C   VAL B 187     -62.127   0.926  17.430  1.00 40.09           C
ANISOU 4251  C   VAL B 187     5468   2865   6898    417   -772    663       C
ATOM   4252  O   VAL B 187     -61.259   0.093  17.722  1.00 51.18           O
ANISOU 4252  O   VAL B 187     7024   4091   8330    645   -989    572       O
ATOM   4253  CB  VAL B 187     -64.319  -0.293  17.693  1.00 33.27           C
ANISOU 4253  CB  VAL B 187     5165   1880   5596    -36   -675    798       C
ATOM   4254  CG1 VAL B 187     -64.599   0.508  18.956  1.00 32.83           C
ANISOU 4254  CG1 VAL B 187     5098   1872   5505   -157   -700    840       C
ATOM   4255  CG2 VAL B 187     -65.614  -0.675  16.999  1.00 34.66           C
ANISOU 4255  CG2 VAL B 187     5410   2151   5608   -306   -492    806       C
ATOM   4256  N  AGLN B 188     -61.994   2.225  17.677  0.73 42.21           N
ANISOU 4256  N  AGLN B 188     5452   3304   7282    382   -688    674       N
ATOM   4257  N  BGLN B 188     -61.994   2.220  17.703  0.27 41.82           N
ANISOU 4257  N  BGLN B 188     5406   3252   7231    383   -692    675       N
ATOM   4258  CA AGLN B 188     -60.855   2.773  18.394  0.73 43.79           C
ANISOU 4258  CA AGLN B 188     5480   3519   7638    554   -818    586       C
ATOM   4259  CA BGLN B 188     -60.819   2.750  18.380  0.27 44.06           C
ANISOU 4259  CA BGLN B 188     5513   3552   7677    562   -822    581       C
ATOM   4260  C  AGLN B 188     -61.159   2.820  19.883  0.73 45.84           C
ANISOU 4260  C  AGLN B 188     5970   3670   7778    491   -980    670       C
ATOM   4261  C  BGLN B 188     -61.103   2.956  19.862  0.27 45.65           C
ANISOU 4261  C  BGLN B 188     5903   3667   7774    494   -968    665       C
ATOM   4262  O  AGLN B 188     -62.298   3.068  20.289  0.73 47.72           O
ANISOU 4262  O  AGLN B 188     6334   3935   7864    248   -880    781       O
ATOM   4263  O  BGLN B 188     -62.170   3.447  20.240  0.27 45.91           O
ANISOU 4263  O  BGLN B 188     5995   3761   7689    261   -851    772       O
ATOM   4264  CB AGLN B 188     -60.528   4.181  17.893  0.73 44.20           C
ANISOU 4264  CB AGLN B 188     5167   3787   7838    498   -623    550       C
ATOM   4265  CB BGLN B 188     -60.364   4.069  17.753  0.27 44.87           C
ANISOU 4265  CB BGLN B 188     5236   3871   7943    528   -626    523       C
ATOM   4266  CG AGLN B 188     -60.131   4.254  16.431  0.73 47.14           C
ANISOU 4266  CG AGLN B 188     5361   4257   8292    502   -438    450       C
ATOM   4267  CG BGLN B 188     -59.418   3.902  16.577  0.27 49.05           C
ANISOU 4267  CG BGLN B 188     5549   4476   8612    630   -526    340       C
ATOM   4268  CD AGLN B 188     -58.734   3.725  16.181  0.73 51.41           C
ANISOU 4268  CD AGLN B 188     5725   4807   9002    717   -514    203       C
ATOM   4269  CD BGLN B 188     -58.548   5.123  16.356  0.27 49.94           C
ANISOU 4269  CD BGLN B 188     5339   4765   8869    582   -377    210       C
ATOM   4270  OE1AGLN B 188     -58.549   2.545  15.885  0.73 54.37           O
ANISOU 4270  OE1AGLN B 188     6224   5068   9368    866   -623    126       O
ATOM   4271  OE1BGLN B 188     -58.779   6.179  16.946  0.27 47.58           O
ANISOU 4271  OE1BGLN B 188     5002   4521   8556    472   -339    298       O
ATOM   4272  NE2AGLN B 188     -57.740   4.599  16.300  0.73 52.26           N
ANISOU 4272  NE2AGLN B 188     5532   5061   9262    732   -456     38       N
ATOM   4273  NE2BGLN B 188     -57.535   4.984  15.508  0.27 52.56           N
ANISOU 4273  NE2BGLN B 188     5449   5193   9327    637   -274    -30       N
ATOM   4274  N   GLN B 189     -60.137   2.577  20.696  1.00 43.97           N
ANISOU 4274  N   GLN B 189     5781   3321   7604    708  -1238    581       N
ATOM   4275  CA  GLN B 189     -60.247   2.764  22.136  1.00 44.21           C
ANISOU 4275  CA  GLN B 189     6028   3283   7488    639  -1384    639       C
ATOM   4276  C   GLN B 189     -59.914   4.215  22.461  1.00 45.84           C
ANISOU 4276  C   GLN B 189     5874   3663   7882    608  -1299    631       C
ATOM   4277  O   GLN B 189     -58.804   4.680  22.180  1.00 47.43           O
ANISOU 4277  O   GLN B 189     5743   3982   8294    785  -1325    475       O
ATOM   4278  CB  GLN B 189     -59.317   1.817  22.889  1.00 45.73           C
ANISOU 4278  CB  GLN B 189     6473   3340   7563    876  -1696    520       C
ATOM   4279  CG  GLN B 189     -59.433   1.946  24.399  1.00 52.31           C
ANISOU 4279  CG  GLN B 189     7597   4078   8202    781  -1854    583       C
ATOM   4280  CD  GLN B 189     -58.246   1.360  25.134  1.00 69.49           C
ANISOU 4280  CD  GLN B 189     9900   6166  10337   1069  -2205    426       C
ATOM   4281  OE1 GLN B 189     -57.488   0.563  24.581  1.00 75.40           O
ANISOU 4281  OE1 GLN B 189    10618   6892  11139   1327  -2345    268       O
ATOM   4282  NE2 GLN B 189     -58.073   1.761  26.388  1.00 75.85           N
ANISOU 4282  NE2 GLN B 189    10848   6922  11048   1029  -2364    447       N
ATOM   4283  N   LEU B 190     -60.872   4.928  23.040  1.00 43.63           N
ANISOU 4283  N   LEU B 190     5644   3440   7492    357  -1165    752       N
ATOM   4284  CA  LEU B 190     -60.660   6.334  23.344  1.00 36.98           C
ANISOU 4284  CA  LEU B 190     4509   2769   6772    305  -1058    744       C
ATOM   4285  C   LEU B 190     -59.713   6.478  24.533  1.00 39.13           C
ANISOU 4285  C   LEU B 190     4815   2972   7082    429  -1301    685       C
ATOM   4286  O   LEU B 190     -59.779   5.689  25.482  1.00 41.22           O
ANISOU 4286  O   LEU B 190     5452   3028   7180    442  -1530    722       O
ATOM   4287  CB  LEU B 190     -61.992   7.025  23.633  1.00 34.63           C
ANISOU 4287  CB  LEU B 190     4249   2554   6357     43   -872    844       C
ATOM   4288  CG  LEU B 190     -62.906   7.153  22.412  1.00 38.88           C
ANISOU 4288  CG  LEU B 190     4680   3206   6888    -38   -664    861       C
ATOM   4289  CD1 LEU B 190     -64.177   7.922  22.738  1.00 40.67           C
ANISOU 4289  CD1 LEU B 190     4871   3548   7034   -230   -530    878       C
ATOM   4290  CD2 LEU B 190     -62.158   7.814  21.264  1.00 37.98           C
ANISOU 4290  CD2 LEU B 190     4295   3192   6946     82   -565    812       C
ATOM   4291  N   PRO B 191     -58.822   7.465  24.514  1.00 39.11           N
ANISOU 4291  N   PRO B 191     4471   3124   7264    499  -1266    580       N
ATOM   4292  CA  PRO B 191     -57.798   7.560  25.556  1.00 42.22           C
ANISOU 4292  CA  PRO B 191     4841   3485   7718    650  -1528    472       C
ATOM   4293  C   PRO B 191     -58.342   8.136  26.854  1.00 40.76           C
ANISOU 4293  C   PRO B 191     4853   3243   7389    470  -1560    595       C
ATOM   4294  O   PRO B 191     -59.358   8.833  26.887  1.00 40.20           O
ANISOU 4294  O   PRO B 191     4793   3237   7244    232  -1327    712       O
ATOM   4295  CB  PRO B 191     -56.759   8.499  24.935  1.00 43.77           C
ANISOU 4295  CB  PRO B 191     4565   3917   8147    698  -1392    280       C
ATOM   4296  CG  PRO B 191     -57.569   9.387  24.054  1.00 32.49           C
ANISOU 4296  CG  PRO B 191     3046   2599   6701    466  -1039    393       C
ATOM   4297  CD  PRO B 191     -58.678   8.527  23.501  1.00 31.49           C
ANISOU 4297  CD  PRO B 191     3166   2361   6436    422   -991    534       C
ATOM   4298  N   GLU B 192     -57.638   7.818  27.939  1.00 44.89           N
ANISOU 4298  N   GLU B 192     5540   3641   7873    607  -1879    537       N
ATOM   4299  CA  GLU B 192     -57.915   8.443  29.225  1.00 47.10           C
ANISOU 4299  CA  GLU B 192     5988   3878   8029    439  -1924    619       C
ATOM   4300  C   GLU B 192     -57.667   9.941  29.119  1.00 45.41           C
ANISOU 4300  C   GLU B 192     5366   3906   7981    334  -1692    575       C
ATOM   4301  O   GLU B 192     -56.608  10.374  28.657  1.00 50.70           O
ANISOU 4301  O   GLU B 192     5675   4733   8856    470  -1694    402       O
ATOM   4302  CB  GLU B 192     -57.028   7.829  30.308  1.00 59.21           C
ANISOU 4302  CB  GLU B 192     7782   5222   9493    653  -2366    539       C
ATOM   4303  CG  GLU B 192     -57.683   7.703  31.672  1.00 71.91           C
ANISOU 4303  CG  GLU B 192     9904   6615  10802    434  -2478    683       C
ATOM   4304  CD  GLU B 192     -58.386   6.371  31.860  1.00 83.26           C
ANISOU 4304  CD  GLU B 192    11886   7879  11871    324  -2512    740       C
ATOM   4305  OE1 GLU B 192     -58.803   5.765  30.850  1.00 84.79           O
ANISOU 4305  OE1 GLU B 192    12046   8098  12070    332  -2364    749       O
ATOM   4306  OE2 GLU B 192     -58.512   5.925  33.020  1.00 88.96           O
ANISOU 4306  OE2 GLU B 192    13085   8436  12282    212  -2684    766       O
ATOM   4307  N   THR B 193     -58.646  10.738  29.538  1.00 41.54           N
ANISOU 4307  N   THR B 193     4944   3448   7390     76  -1482    697       N
ATOM   4308  CA  THR B 193     -58.608  12.168  29.276  1.00 41.29           C
ANISOU 4308  CA  THR B 193     4608   3600   7481    -28  -1242    676       C
ATOM   4309  C   THR B 193     -59.200  12.948  30.440  1.00 41.99           C
ANISOU 4309  C   THR B 193     4830   3670   7455   -227  -1195    744       C
ATOM   4310  O   THR B 193     -60.047  12.446  31.184  1.00 31.49           O
ANISOU 4310  O   THR B 193     3807   2226   5933   -366  -1228    818       O
ATOM   4311  CB  THR B 193     -59.370  12.520  27.989  1.00 40.50           C
ANISOU 4311  CB  THR B 193     4382   3588   7420    -92   -964    719       C
ATOM   4312  OG1 THR B 193     -59.358  13.939  27.793  1.00 44.49           O
ANISOU 4312  OG1 THR B 193     4711   4201   7992   -190   -771    706       O
ATOM   4313  CG2 THR B 193     -60.809  12.040  28.071  1.00 39.54           C
ANISOU 4313  CG2 THR B 193     4488   3403   7131   -227   -888    821       C
ATOM   4314  N   TYR B 194     -58.724  14.180  30.595  1.00 41.49           N
ANISOU 4314  N   TYR B 194     4552   3721   7493   -274  -1097    693       N
ATOM   4315  CA  TYR B 194     -59.398  15.187  31.397  1.00 38.95           C
ANISOU 4315  CA  TYR B 194     4293   3412   7094   -462   -972    741       C
ATOM   4316  C   TYR B 194     -60.454  15.885  30.545  1.00 35.70           C
ANISOU 4316  C   TYR B 194     3806   3064   6695   -530   -713    777       C
ATOM   4317  O   TYR B 194     -60.471  15.778  29.317  1.00 33.21           O
ANISOU 4317  O   TYR B 194     3384   2785   6450   -446   -627    774       O
ATOM   4318  CB  TYR B 194     -58.405  16.217  31.941  1.00 38.45           C
ANISOU 4318  CB  TYR B 194     4071   3421   7116   -484   -993    660       C
ATOM   4319  CG  TYR B 194     -57.400  15.689  32.943  1.00 41.73           C
ANISOU 4319  CG  TYR B 194     4550   3789   7516   -395  -1300    588       C
ATOM   4320  CD1 TYR B 194     -57.732  15.557  34.286  1.00 44.57           C
ANISOU 4320  CD1 TYR B 194     5204   4028   7703   -504  -1439    648       C
ATOM   4321  CD2 TYR B 194     -56.111  15.351  32.551  1.00 43.18           C
ANISOU 4321  CD2 TYR B 194     4501   4054   7850   -201  -1464    421       C
ATOM   4322  CE1 TYR B 194     -56.813  15.083  35.207  1.00 45.00           C
ANISOU 4322  CE1 TYR B 194     5380   4004   7715   -394  -1780    580       C
ATOM   4323  CE2 TYR B 194     -55.186  14.878  33.465  1.00 45.19           C
ANISOU 4323  CE2 TYR B 194     4799   4270   8101    -55  -1813    308       C
ATOM   4324  CZ  TYR B 194     -55.541  14.746  34.792  1.00 46.07           C
ANISOU 4324  CZ  TYR B 194     5264   4221   8019   -138  -1993    406       C
ATOM   4325  OH  TYR B 194     -54.623  14.275  35.705  1.00 49.14           O
ANISOU 4325  OH  TYR B 194     5759   4536   8375     34  -2398    295       O
ATOM   4326  N   PHE B 195     -61.341  16.619  31.209  1.00 35.33           N
ANISOU 4326  N   PHE B 195     3824   3026   6572   -667   -608    784       N
ATOM   4327  CA  PHE B 195     -62.356  17.401  30.520  1.00 34.78           C
ANISOU 4327  CA  PHE B 195     3685   3011   6520   -670   -430    767       C
ATOM   4328  C   PHE B 195     -62.355  18.826  31.047  1.00 38.67           C
ANISOU 4328  C   PHE B 195     4150   3512   7029   -727   -349    732       C
ATOM   4329  O   PHE B 195     -62.260  19.051  32.257  1.00 40.32           O
ANISOU 4329  O   PHE B 195     4429   3708   7182   -844   -382    714       O
ATOM   4330  CB  PHE B 195     -63.751  16.791  30.684  1.00 31.84           C
ANISOU 4330  CB  PHE B 195     3391   2668   6039   -755   -377    728       C
ATOM   4331  CG  PHE B 195     -63.929  15.486  29.965  1.00 32.24           C
ANISOU 4331  CG  PHE B 195     3495   2701   6055   -716   -420    758       C
ATOM   4332  CD1 PHE B 195     -63.829  15.423  28.585  1.00 30.99           C
ANISOU 4332  CD1 PHE B 195     3225   2564   5984   -565   -390    779       C
ATOM   4333  CD2 PHE B 195     -64.207  14.325  30.667  1.00 30.86           C
ANISOU 4333  CD2 PHE B 195     3542   2461   5724   -856   -487    762       C
ATOM   4334  CE1 PHE B 195     -63.994  14.224  27.919  1.00 32.43           C
ANISOU 4334  CE1 PHE B 195     3464   2728   6132   -534   -424    801       C
ATOM   4335  CE2 PHE B 195     -64.375  13.122  30.008  1.00 32.15           C
ANISOU 4335  CE2 PHE B 195     3803   2580   5833   -832   -526    788       C
ATOM   4336  CZ  PHE B 195     -64.269  13.071  28.631  1.00 35.39           C
ANISOU 4336  CZ  PHE B 195     4047   3036   6363   -660   -493    805       C
ATOM   4337  N   THR B 196     -62.451  19.784  30.131  1.00 39.12           N
ANISOU 4337  N   THR B 196     4164   3563   7139   -651   -254    722       N
ATOM   4338  CA  THR B 196     -62.633  21.168  30.534  1.00 35.12           C
ANISOU 4338  CA  THR B 196     3701   3021   6620   -684   -184    682       C
ATOM   4339  C   THR B 196     -64.028  21.358  31.119  1.00 32.12           C
ANISOU 4339  C   THR B 196     3329   2682   6194   -687   -156    586       C
ATOM   4340  O   THR B 196     -64.966  20.623  30.800  1.00 27.70           O
ANISOU 4340  O   THR B 196     2722   2189   5615   -651   -157    533       O
ATOM   4341  CB  THR B 196     -62.415  22.113  29.351  1.00 37.05           C
ANISOU 4341  CB  THR B 196     4016   3187   6876   -608   -116    694       C
ATOM   4342  OG1 THR B 196     -63.225  21.699  28.243  1.00 40.27           O
ANISOU 4342  OG1 THR B 196     4436   3589   7276   -467   -132    698       O
ATOM   4343  CG2 THR B 196     -60.958  22.108  28.931  1.00 28.27           C
ANISOU 4343  CG2 THR B 196     2864   2078   5798   -696    -79    710       C
ATOM   4344  N   GLN B 197     -64.156  22.352  31.994  1.00 32.07           N
ANISOU 4344  N   GLN B 197     3362   2655   6168   -750   -118    525       N
ATOM   4345  CA  GLN B 197     -65.401  22.559  32.721  1.00 32.18           C
ANISOU 4345  CA  GLN B 197     3338   2743   6147   -782    -70    364       C
ATOM   4346  C   GLN B 197     -66.401  23.431  31.972  1.00 36.96           C
ANISOU 4346  C   GLN B 197     3910   3342   6793   -561    -73    228       C
ATOM   4347  O   GLN B 197     -67.579  23.454  32.348  1.00 42.36           O
ANISOU 4347  O   GLN B 197     4474   4143   7477   -542    -43     15       O
ATOM   4348  CB  GLN B 197     -65.106  23.169  34.093  1.00 37.32           C
ANISOU 4348  CB  GLN B 197     4051   3377   6750   -954    -32    330       C
ATOM   4349  CG  GLN B 197     -64.223  22.290  34.965  1.00 36.87           C
ANISOU 4349  CG  GLN B 197     4073   3310   6624  -1143    -94    432       C
ATOM   4350  CD  GLN B 197     -64.842  20.932  35.236  1.00 44.78           C
ANISOU 4350  CD  GLN B 197     5122   4364   7528  -1261   -106    407       C
ATOM   4351  OE1 GLN B 197     -65.992  20.835  35.665  1.00 49.27           O
ANISOU 4351  OE1 GLN B 197     5670   5021   8028  -1379      3    245       O
ATOM   4352  NE2 GLN B 197     -64.083  19.873  34.979  1.00 46.83           N
ANISOU 4352  NE2 GLN B 197     5454   4570   7768  -1244   -232    532       N
ATOM   4353  N   SER B 198     -65.960  24.147  30.935  1.00 35.41           N
ANISOU 4353  N   SER B 198     3835   3006   6613   -402   -120    312       N
ATOM   4354  CA  SER B 198     -66.852  24.897  30.045  1.00 35.86           C
ANISOU 4354  CA  SER B 198     3955   2993   6675   -134   -204    200       C
ATOM   4355  C   SER B 198     -67.661  25.952  30.799  1.00 36.89           C
ANISOU 4355  C   SER B 198     4084   3117   6816    -34   -223    -10       C
ATOM   4356  O   SER B 198     -68.843  26.165  30.526  1.00 39.66           O
ANISOU 4356  O   SER B 198     4332   3534   7204    194   -314   -237       O
ATOM   4357  CB  SER B 198     -67.782  23.955  29.276  1.00 40.00           C
ANISOU 4357  CB  SER B 198     4324   3647   7226    -11   -260    114       C
ATOM   4358  OG  SER B 198     -67.043  23.025  28.504  1.00 43.82           O
ANISOU 4358  OG  SER B 198     4834   4115   7700    -79   -247    297       O
ATOM   4359  N   ARG B 199     -67.023  26.621  31.751  1.00 36.27           N
ANISOU 4359  N   ARG B 199     4097   2972   6710   -191   -151     28       N
ATOM   4360  CA  ARG B 199     -67.659  27.723  32.454  1.00 40.86           C
ANISOU 4360  CA  ARG B 199     4713   3515   7296    -95   -163   -169       C
ATOM   4361  C   ARG B 199     -67.355  29.042  31.750  1.00 45.21           C
ANISOU 4361  C   ARG B 199     5615   3780   7784     95   -262   -117       C
ATOM   4362  O   ARG B 199     -66.441  29.141  30.929  1.00 49.45           O
ANISOU 4362  O   ARG B 199     6380   4160   8249     37   -259     87       O
ATOM   4363  CB  ARG B 199     -67.194  27.776  33.910  1.00 40.56           C
ANISOU 4363  CB  ARG B 199     4636   3540   7234   -385    -31   -166       C
ATOM   4364  CG  ARG B 199     -67.785  26.678  34.776  1.00 44.85           C
ANISOU 4364  CG  ARG B 199     4946   4317   7776   -588     61   -287       C
ATOM   4365  CD  ARG B 199     -67.070  26.558  36.110  1.00 44.38           C
ANISOU 4365  CD  ARG B 199     4951   4268   7644   -906    153   -211       C
ATOM   4366  NE  ARG B 199     -65.734  25.990  35.962  1.00 43.24           N
ANISOU 4366  NE  ARG B 199     4904   4054   7472  -1026    108     55       N
ATOM   4367  CZ  ARG B 199     -64.984  25.570  36.975  1.00 45.31           C
ANISOU 4367  CZ  ARG B 199     5230   4324   7663  -1266    111    140       C
ATOM   4368  NH1 ARG B 199     -65.438  25.652  38.219  1.00 44.91           N
ANISOU 4368  NH1 ARG B 199     5208   4325   7531  -1464    188     16       N
ATOM   4369  NH2 ARG B 199     -63.779  25.066  36.746  1.00 44.47           N
ANISOU 4369  NH2 ARG B 199     5161   4176   7561  -1303     24    318       N
ATOM   4370  N   ASN B 200     -68.150  30.057  32.069  1.00 43.37           N
ANISOU 4370  N   ASN B 200     5451   3470   7558    312   -348   -335       N
ATOM   4371  CA  ASN B 200     -67.945  31.394  31.538  1.00 47.66           C
ANISOU 4371  CA  ASN B 200     6432   3680   7995    497   -470   -306       C
ATOM   4372  C   ASN B 200     -67.485  32.328  32.649  1.00 47.67           C
ANISOU 4372  C   ASN B 200     6569   3590   7955    331   -365   -324       C
ATOM   4373  O   ASN B 200     -67.641  32.043  33.840  1.00 46.35           O
ANISOU 4373  O   ASN B 200     6127   3628   7857    157   -239   -428       O
ATOM   4374  CB  ASN B 200     -69.218  31.935  30.876  1.00 56.19           C
ANISOU 4374  CB  ASN B 200     7578   4672   9098    973   -736   -563       C
ATOM   4375  CG  ASN B 200     -70.372  32.055  31.844  1.00 64.53           C
ANISOU 4375  CG  ASN B 200     8272   5956  10291   1123   -752   -944       C
ATOM   4376  OD1 ASN B 200     -70.489  33.045  32.564  1.00 67.87           O
ANISOU 4376  OD1 ASN B 200     8817   6270  10703   1186   -762  -1082       O
ATOM   4377  ND2 ASN B 200     -71.238  31.049  31.860  1.00 67.71           N
ANISOU 4377  ND2 ASN B 200     8230   6687  10812   1151   -734  -1149       N
ATOM   4378  N   LEU B 201     -66.910  33.458  32.237  1.00 45.26           N
ANISOU 4378  N   LEU B 201     6743   2952   7501    351   -410   -224       N
ATOM   4379  CA  LEU B 201     -66.280  34.356  33.198  1.00 52.07           C
ANISOU 4379  CA  LEU B 201     7785   3704   8294    134   -290   -207       C
ATOM   4380  C   LEU B 201     -67.315  35.072  34.054  1.00 60.75           C
ANISOU 4380  C   LEU B 201     8817   4807   9458    370   -368   -500       C
ATOM   4381  O   LEU B 201     -67.120  35.243  35.263  1.00 62.12           O
ANISOU 4381  O   LEU B 201     8857   5087   9657    152   -220   -557       O
ATOM   4382  CB  LEU B 201     -65.401  35.366  32.465  1.00 54.70           C
ANISOU 4382  CB  LEU B 201     8706   3666   8410     37   -290    -46       C
ATOM   4383  CG  LEU B 201     -64.276  35.931  33.323  1.00 56.80           C
ANISOU 4383  CG  LEU B 201     9093   3898   8592   -365    -82     40       C
ATOM   4384  CD1 LEU B 201     -63.472  34.779  33.891  1.00 56.85           C
ANISOU 4384  CD1 LEU B 201     8642   4244   8713   -690     86    139       C
ATOM   4385  CD2 LEU B 201     -63.396  36.864  32.512  1.00 59.23           C
ANISOU 4385  CD2 LEU B 201    10001   3857   8648   -548    -32    167       C
ATOM   4386  N   GLN B 202     -68.419  35.498  33.441  1.00 65.57           N
ANISOU 4386  N   GLN B 202     9513   5306  10093    827   -615   -720       N
ATOM   4387  CA  GLN B 202     -69.463  36.208  34.171  1.00 72.81           C
ANISOU 4387  CA  GLN B 202    10325   6244  11094   1115   -717  -1083       C
ATOM   4388  C   GLN B 202     -70.104  35.314  35.226  1.00 73.54           C
ANISOU 4388  C   GLN B 202     9798   6780  11362    961   -543  -1315       C
ATOM   4389  O   GLN B 202     -70.120  35.644  36.417  1.00 74.91           O
ANISOU 4389  O   GLN B 202     9865   7041  11556    782   -390  -1444       O
ATOM   4390  CB  GLN B 202     -70.513  36.728  33.188  1.00 83.74           C
ANISOU 4390  CB  GLN B 202    11890   7443  12484   1697  -1082  -1318       C
ATOM   4391  CG  GLN B 202     -71.855  37.057  33.818  1.00 96.98           C
ANISOU 4391  CG  GLN B 202    13215   9300  14332   2071  -1216  -1824       C
ATOM   4392  CD  GLN B 202     -72.982  37.049  32.805  1.00108.06           C
ANISOU 4392  CD  GLN B 202    14541  10753  15764   2592  -1560  -2070       C
ATOM   4393  OE1 GLN B 202     -74.150  37.224  33.153  1.00115.29           O
ANISOU 4393  OE1 GLN B 202    15078  11944  16784   2862  -1668  -2490       O
ATOM   4394  NE2 GLN B 202     -72.635  36.840  31.540  1.00107.94           N
ANISOU 4394  NE2 GLN B 202    14836  10604  15572   2609  -1677  -1761       N
ATOM   4395  N   GLU B 203     -70.635  34.168  34.804  1.00 73.47           N
ANISOU 4395  N   GLU B 203     9420   7045  11452    987   -548  -1376       N
ATOM   4396  CA  GLU B 203     -71.382  33.267  35.680  1.00 72.46           C
ANISOU 4396  CA  GLU B 203     8763   7325  11442    812   -377  -1641       C
ATOM   4397  C   GLU B 203     -70.524  32.113  36.184  1.00 60.16           C
ANISOU 4397  C   GLU B 203     7095   5928   9836    314   -139  -1353       C
ATOM   4398  O   GLU B 203     -70.984  30.969  36.240  1.00 62.07           O
ANISOU 4398  O   GLU B 203     7026   6439  10120    176    -54  -1435       O
ATOM   4399  CB  GLU B 203     -72.614  32.739  34.953  1.00 85.70           C
ANISOU 4399  CB  GLU B 203    10108   9215  13237   1138   -534  -1962       C
ATOM   4400  CG  GLU B 203     -73.533  33.826  34.414  1.00100.14           C
ANISOU 4400  CG  GLU B 203    12032  10892  15125   1722   -857  -2307       C
ATOM   4401  CD  GLU B 203     -74.484  33.310  33.352  1.00107.62           C
ANISOU 4401  CD  GLU B 203    12746  11982  16161   2088  -1094  -2535       C
ATOM   4402  OE1 GLU B 203     -74.233  33.557  32.153  1.00109.17           O
ANISOU 4402  OE1 GLU B 203    13319  11889  16273   2363  -1354  -2325       O
ATOM   4403  OE2 GLU B 203     -75.477  32.647  33.717  1.00110.90           O
ANISOU 4403  OE2 GLU B 203    12618  12809  16711   2064  -1007  -2942       O
ATOM   4404  N   PHE B 204     -69.277  32.379  36.561  1.00 44.12           N
ANISOU 4404  N   PHE B 204     5201   4851   6712   -209    660    -45       N
ATOM   4405  CA  PHE B 204     -68.405  31.314  37.035  1.00 38.92           C
ANISOU 4405  CA  PHE B 204     4711   4233   5843   -290    635     56       C
ATOM   4406  C   PHE B 204     -68.847  30.833  38.410  1.00 41.45           C
ANISOU 4406  C   PHE B 204     5137   4591   6021   -379    852     34       C
ATOM   4407  O   PHE B 204     -69.161  31.629  39.299  1.00 46.27           O
ANISOU 4407  O   PHE B 204     5796   5207   6576   -380   1001    -74       O
ATOM   4408  CB  PHE B 204     -66.954  31.789  37.094  1.00 39.65           C
ANISOU 4408  CB  PHE B 204     4955   4326   5784   -268    480     86       C
ATOM   4409  CG  PHE B 204     -65.969  30.690  37.383  1.00 42.21           C
ANISOU 4409  CG  PHE B 204     5416   4675   5947   -326    401    201       C
ATOM   4410  CD1 PHE B 204     -65.345  30.015  36.348  1.00 42.68           C
ANISOU 4410  CD1 PHE B 204     5436   4717   6063   -310    252    286       C
ATOM   4411  CD2 PHE B 204     -65.671  30.328  38.688  1.00 42.64           C
ANISOU 4411  CD2 PHE B 204     5647   4758   5795   -396    473    223       C
ATOM   4412  CE1 PHE B 204     -64.441  29.002  36.607  1.00 42.66           C
ANISOU 4412  CE1 PHE B 204     5538   4717   5953   -344    179    385       C
ATOM   4413  CE2 PHE B 204     -64.769  29.315  38.954  1.00 40.98           C
ANISOU 4413  CE2 PHE B 204     5558   4551   5462   -436    370    342       C
ATOM   4414  CZ  PHE B 204     -64.152  28.653  37.911  1.00 42.71           C
ANISOU 4414  CZ  PHE B 204     5707   4744   5778   -400    223    421       C
ATOM   4415  N   LYS B 205     -68.867  29.511  38.584  1.00 43.44           N
ANISOU 4415  N   LYS B 205     5443   4858   6204   -465    876    136       N
ATOM   4416  CA  LYS B 205     -69.271  28.895  39.840  1.00 50.92           C
ANISOU 4416  CA  LYS B 205     6520   5834   6992   -577   1077    144       C
ATOM   4417  C   LYS B 205     -68.315  27.748  40.152  1.00 46.05           C
ANISOU 4417  C   LYS B 205     6096   5213   6187   -642    965    294       C
ATOM   4418  O   LYS B 205     -68.126  26.854  39.306  1.00 41.21           O
ANISOU 4418  O   LYS B 205     5422   4569   5665   -637    846    386       O
ATOM   4419  CB  LYS B 205     -70.718  28.394  39.769  1.00 61.10           C
ANISOU 4419  CB  LYS B 205     7634   7125   8456   -633   1276    108       C
ATOM   4420  CG  LYS B 205     -71.739  29.503  39.536  1.00 69.35           C
ANISOU 4420  CG  LYS B 205     8460   8161   9727   -557   1390    -45       C
ATOM   4421  CD  LYS B 205     -73.129  28.954  39.257  1.00 75.95           C
ANISOU 4421  CD  LYS B 205     9063   8996  10797   -604   1540    -72       C
ATOM   4422  CE  LYS B 205     -74.102  30.078  38.926  1.00 80.69           C
ANISOU 4422  CE  LYS B 205     9411   9572  11676   -502   1611   -218       C
ATOM   4423  NZ  LYS B 205     -75.464  29.565  38.606  1.00 86.87           N
ANISOU 4423  NZ  LYS B 205     9924  10353  12729   -546   1732   -248       N
ATOM   4424  N   PRO B 206     -67.702  27.739  41.333  1.00 48.50           N
ANISOU 4424  N   PRO B 206     6644   5542   6242   -704    987    322       N
ATOM   4425  CA  PRO B 206     -66.736  26.684  41.658  1.00 48.68           C
ANISOU 4425  CA  PRO B 206     6848   5544   6104   -752    842    478       C
ATOM   4426  C   PRO B 206     -67.409  25.326  41.793  1.00 53.84           C
ANISOU 4426  C   PRO B 206     7523   6168   6766   -853    946    574       C
ATOM   4427  O   PRO B 206     -68.611  25.212  42.038  1.00 58.37           O
ANISOU 4427  O   PRO B 206     8024   6756   7397   -926   1174    518       O
ATOM   4428  CB  PRO B 206     -66.142  27.144  42.993  1.00 47.86           C
ANISOU 4428  CB  PRO B 206     7000   5469   5718   -811    850    470       C
ATOM   4429  CG  PRO B 206     -67.203  27.997  43.598  1.00 49.95           C
ANISOU 4429  CG  PRO B 206     7245   5768   5965   -848   1116    314       C
ATOM   4430  CD  PRO B 206     -67.879  28.690  42.445  1.00 49.74           C
ANISOU 4430  CD  PRO B 206     6925   5731   6242   -737   1140    209       C
ATOM   4431  N   ARG B 207     -66.598  24.276  41.626  1.00 52.80           N
ANISOU 4431  N   ARG B 207     7484   5983   6595   -857    777    718       N
ATOM   4432  CA  ARG B 207     -67.102  22.907  41.631  1.00 51.05           C
ANISOU 4432  CA  ARG B 207     7293   5704   6398   -949    838    824       C
ATOM   4433  C   ARG B 207     -66.272  21.988  42.522  1.00 50.10           C
ANISOU 4433  C   ARG B 207     7441   5530   6065  -1012    732    985       C
ATOM   4434  O   ARG B 207     -66.363  20.763  42.392  1.00 49.16           O
ANISOU 4434  O   ARG B 207     7367   5330   5981  -1064    712   1100       O
ATOM   4435  CB  ARG B 207     -67.162  22.354  40.205  1.00 48.91           C
ANISOU 4435  CB  ARG B 207     6827   5384   6374   -882    734    836       C
ATOM   4436  CG  ARG B 207     -68.156  23.084  39.316  1.00 50.36           C
ANISOU 4436  CG  ARG B 207     6756   5605   6772   -843    821    703       C
ATOM   4437  CD  ARG B 207     -68.103  22.604  37.878  1.00 51.68           C
ANISOU 4437  CD  ARG B 207     6772   5725   7140   -789    686    714       C
ATOM   4438  NE  ARG B 207     -69.074  23.312  37.048  1.00 53.23           N
ANISOU 4438  NE  ARG B 207     6741   5952   7533   -758    732    603       N
ATOM   4439  CZ  ARG B 207     -69.201  23.147  35.735  1.00 50.31           C
ANISOU 4439  CZ  ARG B 207     6235   5552   7330   -720    616    588       C
ATOM   4440  NH1 ARG B 207     -68.414  22.296  35.091  1.00 47.54           N
ANISOU 4440  NH1 ARG B 207     5949   5141   6974   -708    480    658       N
ATOM   4441  NH2 ARG B 207     -70.115  23.836  35.066  1.00 50.59           N
ANISOU 4441  NH2 ARG B 207     6074   5610   7537   -696    631    501       N
ATOM   4442  N   SER B 208     -65.470  22.549  43.423  1.00 49.05           N
ANISOU 4442  N   SER B 208     7493   5427   5716  -1013    647   1000       N
ATOM   4443  CA  SER B 208     -64.715  21.749  44.376  1.00 47.05           C
ANISOU 4443  CA  SER B 208     7513   5119   5244  -1080    519   1163       C
ATOM   4444  C   SER B 208     -64.350  22.626  45.563  1.00 48.10           C
ANISOU 4444  C   SER B 208     7860   5316   5101  -1135    520   1128       C
ATOM   4445  O   SER B 208     -64.325  23.855  45.465  1.00 48.77           O
ANISOU 4445  O   SER B 208     7860   5470   5202  -1080    551    982       O
ATOM   4446  CB  SER B 208     -63.454  21.150  43.745  1.00 45.44           C
ANISOU 4446  CB  SER B 208     7277   4838   5151   -965    225   1271       C
ATOM   4447  OG  SER B 208     -62.460  22.141  43.552  1.00 44.63           O
ANISOU 4447  OG  SER B 208     7115   4782   5059   -860     56   1209       O
ATOM   4448  N   GLN B 209     -64.068  21.970  46.693  1.00 49.34           N
ANISOU 4448  N   GLN B 209     8316   5436   4995  -1252    475   1266       N
ATOM   4449  CA  GLN B 209     -63.654  22.701  47.886  1.00 50.68           C
ANISOU 4449  CA  GLN B 209     8742   5658   4858  -1328    446   1246       C
ATOM   4450  C   GLN B 209     -62.382  23.497  47.626  1.00 50.19           C
ANISOU 4450  C   GLN B 209     8621   5615   4833  -1202    163   1216       C
ATOM   4451  O   GLN B 209     -62.221  24.612  48.138  1.00 49.79           O
ANISOU 4451  O   GLN B 209     8644   5630   4643  -1220    181   1099       O
ATOM   4452  CB  GLN B 209     -63.455  21.734  49.053  1.00 55.61           C
ANISOU 4452  CB  GLN B 209     9722   6221   5187  -1479    387   1435       C
ATOM   4453  CG  GLN B 209     -62.902  22.384  50.313  1.00 63.01           C
ANISOU 4453  CG  GLN B 209    10972   7203   5768  -1574    302   1435       C
ATOM   4454  CD  GLN B 209     -63.783  23.506  50.827  1.00 70.17           C
ANISOU 4454  CD  GLN B 209    11915   8208   6537  -1657    619   1224       C
ATOM   4455  OE1 GLN B 209     -65.009  23.437  50.742  1.00 70.93           O
ANISOU 4455  OE1 GLN B 209    11925   8328   6698  -1721    954   1136       O
ATOM   4456  NE2 GLN B 209     -63.160  24.550  51.362  1.00 74.72           N
ANISOU 4456  NE2 GLN B 209    12610   8836   6943  -1655    515   1134       N
ATOM   4457  N   MET B 210     -61.470  22.944  46.825  1.00 46.65           N
ANISOU 4457  N   MET B 210     8037   5104   4583  -1080    -88   1311       N
ATOM   4458  CA  MET B 210     -60.275  23.686  46.446  1.00 45.45           C
ANISOU 4458  CA  MET B 210     7779   4972   4517   -963   -334   1274       C
ATOM   4459  C   MET B 210     -60.635  24.937  45.654  1.00 51.11           C
ANISOU 4459  C   MET B 210     8269   5761   5390   -889   -207   1076       C
ATOM   4460  O   MET B 210     -60.068  26.011  45.884  1.00 49.21           O
ANISOU 4460  O   MET B 210     8043   5566   5086   -872   -292    989       O
ATOM   4461  CB  MET B 210     -59.337  22.790  45.639  1.00 45.76           C
ANISOU 4461  CB  MET B 210     7682   4925   4782   -844   -570   1394       C
ATOM   4462  CG  MET B 210     -58.083  23.487  45.149  1.00 48.27           C
ANISOU 4462  CG  MET B 210     7849   5261   5231   -728   -802   1353       C
ATOM   4463  SD  MET B 210     -57.056  22.415  44.129  1.00 54.70           S
ANISOU 4463  SD  MET B 210     8468   5967   6348   -582  -1015   1460       S
ATOM   4464  CE  MET B 210     -56.649  21.115  45.292  1.00 56.48           C
ANISOU 4464  CE  MET B 210     8972   6080   6408   -643  -1211   1693       C
ATOM   4465  N   GLU B 211     -61.583  24.818  44.721  1.00 46.63           N
ANISOU 4465  N   GLU B 211     7497   5193   5028   -853    -19   1008       N
ATOM   4466  CA  GLU B 211     -62.015  25.986  43.961  1.00 43.48           C
ANISOU 4466  CA  GLU B 211     6893   4845   4781   -783     88    836       C
ATOM   4467  C   GLU B 211     -62.743  26.985  44.852  1.00 48.82           C
ANISOU 4467  C   GLU B 211     7682   5579   5289   -860    289    703       C
ATOM   4468  O   GLU B 211     -62.624  28.200  44.655  1.00 52.19           O
ANISOU 4468  O   GLU B 211     8036   6035   5757   -808    291    571       O
ATOM   4469  CB  GLU B 211     -62.901  25.559  42.792  1.00 43.22           C
ANISOU 4469  CB  GLU B 211     6632   4792   5000   -737    212    808       C
ATOM   4470  CG  GLU B 211     -62.167  24.785  41.712  1.00 49.19           C
ANISOU 4470  CG  GLU B 211     7257   5488   5943   -649     35    891       C
ATOM   4471  CD  GLU B 211     -62.956  24.692  40.422  1.00 57.45           C
ANISOU 4471  CD  GLU B 211     8080   6524   7225   -603    129    828       C
ATOM   4472  OE1 GLU B 211     -64.180  24.942  40.451  1.00 60.31           O
ANISOU 4472  OE1 GLU B 211     8382   6913   7620   -649    324    752       O
ATOM   4473  OE2 GLU B 211     -62.350  24.377  39.377  1.00 60.62           O
ANISOU 4473  OE2 GLU B 211     8363   6888   7781   -526      5    848       O
ATOM   4474  N   ILE B 212     -63.502  26.493  45.833  1.00 49.04           N
ANISOU 4474  N   ILE B 212     7894   5612   5125   -990    473    729       N
ATOM   4475  CA  ILE B 212     -64.137  27.389  46.796  1.00 50.81           C
ANISOU 4475  CA  ILE B 212     8257   5885   5162  -1076    690    590       C
ATOM   4476  C   ILE B 212     -63.081  28.148  47.586  1.00 54.33           C
ANISOU 4476  C   ILE B 212     8911   6350   5381  -1098    509    572       C
ATOM   4477  O   ILE B 212     -63.202  29.359  47.814  1.00 54.72           O
ANISOU 4477  O   ILE B 212     8969   6429   5395  -1089    592    408       O
ATOM   4478  CB  ILE B 212     -65.078  26.597  47.723  1.00 48.18           C
ANISOU 4478  CB  ILE B 212     8107   5553   4644  -1236    937    635       C
ATOM   4479  CG1 ILE B 212     -66.240  26.003  46.923  1.00 49.95           C
ANISOU 4479  CG1 ILE B 212     8090   5763   5125  -1224   1136    621       C
ATOM   4480  CG2 ILE B 212     -65.595  27.483  48.847  1.00 50.52           C
ANISOU 4480  CG2 ILE B 212     8596   5898   4701  -1341   1172    486       C
ATOM   4481  CD1 ILE B 212     -67.193  25.172  47.757  1.00 52.59           C
ANISOU 4481  CD1 ILE B 212     8577   6095   5311  -1397   1397    667       C
ATOM   4482  N   ASP B 213     -62.022  27.453  48.004  1.00 54.54           N
ANISOU 4482  N   ASP B 213     9104   6350   5269  -1127    244    738       N
ATOM   4483  CA  ASP B 213     -60.948  28.103  48.747  1.00 53.54           C
ANISOU 4483  CA  ASP B 213     9166   6239   4938  -1159     23    735       C
ATOM   4484  C   ASP B 213     -60.228  29.133  47.885  1.00 54.61           C
ANISOU 4484  C   ASP B 213     9082   6385   5284  -1032   -125    636       C
ATOM   4485  O   ASP B 213     -59.947  30.247  48.340  1.00 59.87           O
ANISOU 4485  O   ASP B 213     9835   7076   5838  -1058   -144    514       O
ATOM   4486  CB  ASP B 213     -59.965  27.055  49.270  1.00 54.80           C
ANISOU 4486  CB  ASP B 213     9507   6354   4961  -1200   -267    953       C
ATOM   4487  CG  ASP B 213     -60.590  26.128  50.296  1.00 62.45           C
ANISOU 4487  CG  ASP B 213    10768   7302   5658  -1358   -141   1065       C
ATOM   4488  OD1 ASP B 213     -61.722  26.408  50.741  1.00 65.16           O
ANISOU 4488  OD1 ASP B 213    11194   7682   5884  -1455    189    954       O
ATOM   4489  OD2 ASP B 213     -59.949  25.118  50.656  1.00 65.02           O
ANISOU 4489  OD2 ASP B 213    11241   7567   5899  -1387   -366   1266       O
ATOM   4490  N   PHE B 214     -59.930  28.778  46.632  1.00 53.04           N
ANISOU 4490  N   PHE B 214     8612   6159   5382   -905   -221    683       N
ATOM   4491  CA  PHE B 214     -59.170  29.670  45.759  1.00 49.84           C
ANISOU 4491  CA  PHE B 214     8009   5758   5171   -801   -362    610       C
ATOM   4492  C   PHE B 214     -59.856  31.021  45.608  1.00 52.09           C
ANISOU 4492  C   PHE B 214     8234   6064   5494   -787   -176    414       C
ATOM   4493  O   PHE B 214     -59.195  32.066  45.607  1.00 53.74           O
ANISOU 4493  O   PHE B 214     8440   6276   5701   -773   -284    331       O
ATOM   4494  CB  PHE B 214     -58.973  29.018  44.390  1.00 45.57           C
ANISOU 4494  CB  PHE B 214     7207   5184   4924   -687   -422    674       C
ATOM   4495  CG  PHE B 214     -58.291  29.905  43.384  1.00 44.18           C
ANISOU 4495  CG  PHE B 214     6829   5010   4946   -597   -524    600       C
ATOM   4496  CD1 PHE B 214     -59.029  30.678  42.500  1.00 43.83           C
ANISOU 4496  CD1 PHE B 214     6624   4968   5061   -544   -372    480       C
ATOM   4497  CD2 PHE B 214     -56.910  29.959  43.317  1.00 43.29           C
ANISOU 4497  CD2 PHE B 214     6687   4891   4872   -571   -777    655       C
ATOM   4498  CE1 PHE B 214     -58.400  31.490  41.573  1.00 45.11           C
ANISOU 4498  CE1 PHE B 214     6632   5123   5384   -480   -463    426       C
ATOM   4499  CE2 PHE B 214     -56.277  30.767  42.392  1.00 40.50           C
ANISOU 4499  CE2 PHE B 214     6153   4539   4696   -511   -846    587       C
ATOM   4500  CZ  PHE B 214     -57.023  31.535  41.521  1.00 40.49           C
ANISOU 4500  CZ  PHE B 214     6026   4537   4821   -471   -685    476       C
ATOM   4501  N   LEU B 215     -61.183  31.019  45.476  1.00 55.45           N
ANISOU 4501  N   LEU B 215     8601   6493   5975   -790    100    337       N
ATOM   4502  CA  LEU B 215     -61.925  32.265  45.332  1.00 55.84           C
ANISOU 4502  CA  LEU B 215     8576   6541   6100   -759    282    150       C
ATOM   4503  C   LEU B 215     -62.024  33.016  46.653  1.00 62.96           C
ANISOU 4503  C   LEU B 215     9736   7458   6729   -861    382     35       C
ATOM   4504  O   LEU B 215     -61.979  34.251  46.671  1.00 66.08           O
ANISOU 4504  O   LEU B 215    10125   7835   7148   -834    408   -114       O
ATOM   4505  CB  LEU B 215     -63.321  31.980  44.781  1.00 52.73           C
ANISOU 4505  CB  LEU B 215     8007   6141   5887   -725    531    104       C
ATOM   4506  CG  LEU B 215     -63.362  31.292  43.416  1.00 46.51           C
ANISOU 4506  CG  LEU B 215     6977   5332   5360   -637    446    195       C
ATOM   4507  CD1 LEU B 215     -64.793  30.983  43.003  1.00 45.81           C
ANISOU 4507  CD1 LEU B 215     6730   5239   5436   -628    675    150       C
ATOM   4508  CD2 LEU B 215     -62.672  32.157  42.376  1.00 41.66           C
ANISOU 4508  CD2 LEU B 215     6213   4696   4921   -536    282    157       C
ATOM   4509  N   GLU B 216     -62.166  32.292  47.764  1.00 67.87           N
ANISOU 4509  N   GLU B 216    10606   8104   7079   -988    444    101       N
ATOM   4510  CA  GLU B 216     -62.303  32.949  49.059  1.00 74.52           C
ANISOU 4510  CA  GLU B 216    11735   8962   7619  -1109    561    -16       C
ATOM   4511  C   GLU B 216     -60.953  33.374  49.624  1.00 73.69           C
ANISOU 4511  C   GLU B 216    11820   8858   7320  -1159    260     16       C
ATOM   4512  O   GLU B 216     -60.821  34.484  50.152  1.00 75.23           O
ANISOU 4512  O   GLU B 216    12142   9047   7397  -1198    288   -140       O
ATOM   4513  CB  GLU B 216     -63.015  32.026  50.046  1.00 85.31           C
ANISOU 4513  CB  GLU B 216    13326  10351   8738  -1252    760     44       C
ATOM   4514  CG  GLU B 216     -64.240  32.640  50.710  1.00 97.41           C
ANISOU 4514  CG  GLU B 216    14935  11894  10182  -1321   1152   -155       C
ATOM   4515  CD  GLU B 216     -65.503  32.481  49.880  1.00106.62           C
ANISOU 4515  CD  GLU B 216    15792  13052  11667  -1236   1415   -217       C
ATOM   4516  OE1 GLU B 216     -65.668  33.214  48.880  1.00107.35           O
ANISOU 4516  OE1 GLU B 216    15608  13116  12064  -1088   1394   -306       O
ATOM   4517  OE2 GLU B 216     -66.330  31.613  50.228  1.00110.97           O
ANISOU 4517  OE2 GLU B 216    16380  13620  12163  -1327   1631   -170       O
ATOM   4518  N   LEU B 217     -59.944  32.516  49.517  1.00 72.59           N
ANISOU 4518  N   LEU B 217    11694   8719   7167  -1157    -35    208       N
ATOM   4519  CA  LEU B 217     -58.686  32.722  50.218  1.00 73.16           C
ANISOU 4519  CA  LEU B 217    11960   8796   7042  -1226   -344    264       C
ATOM   4520  C   LEU B 217     -57.761  33.661  49.449  1.00 74.67           C
ANISOU 4520  C   LEU B 217    11954   8973   7444  -1135   -545    202       C
ATOM   4521  O   LEU B 217     -57.886  33.854  48.238  1.00 73.29           O
ANISOU 4521  O   LEU B 217    11488   8781   7577  -1009   -506    177       O
ATOM   4522  CB  LEU B 217     -57.978  31.387  50.454  1.00 68.80           C
ANISOU 4522  CB  LEU B 217    11488   8232   6420  -1252   -592    503       C
ATOM   4523  CG  LEU B 217     -58.117  30.716  51.821  1.00 71.10           C
ANISOU 4523  CG  LEU B 217    12161   8529   6325  -1420   -596    601       C
ATOM   4524  CD1 LEU B 217     -59.393  31.140  52.534  1.00 73.13           C
ANISOU 4524  CD1 LEU B 217    12605   8812   6371  -1531   -205    443       C
ATOM   4525  CD2 LEU B 217     -58.077  29.207  51.649  1.00 70.56           C
ANISOU 4525  CD2 LEU B 217    12077   8422   6311  -1403   -684    826       C
ATOM   4526  N   ALA B 218     -56.820  34.247  50.183  1.00 76.05           N
ANISOU 4526  N   ALA B 218    12306   9152   7437  -1218   -767    179       N
ATOM   4527  CA  ALA B 218     -55.774  35.047  49.574  1.00 71.70           C
ANISOU 4527  CA  ALA B 218    11587   8586   7068  -1164   -993    142       C
ATOM   4528  C   ALA B 218     -54.719  34.137  48.955  1.00 70.18           C
ANISOU 4528  C   ALA B 218    11208   8393   7063  -1093  -1278    331       C
ATOM   4529  O   ALA B 218     -54.660  32.933  49.223  1.00 71.30           O
ANISOU 4529  O   ALA B 218    11410   8534   7146  -1100  -1354    495       O
ATOM   4530  CB  ALA B 218     -55.137  35.983  50.602  1.00 70.48           C
ANISOU 4530  CB  ALA B 218    11686   8433   6661  -1294  -1142     44       C
ATOM   4531  N   MET B 219     -53.877  34.733  48.110  1.00 66.86           N
ANISOU 4531  N   MET B 219    10559   7962   6884  -1027  -1423    303       N
ATOM   4532  CA  MET B 219     -52.906  33.951  47.352  1.00 65.22           C
ANISOU 4532  CA  MET B 219    10121   7747   6913   -943  -1641    448       C
ATOM   4533  C   MET B 219     -51.931  33.230  48.276  1.00 65.81           C
ANISOU 4533  C   MET B 219    10339   7824   6843  -1007  -1959    598       C
ATOM   4534  O   MET B 219     -51.714  32.020  48.148  1.00 67.15           O
ANISOU 4534  O   MET B 219    10455   7973   7087   -952  -2055    759       O
ATOM   4535  CB  MET B 219     -52.157  34.859  46.379  1.00 67.57           C
ANISOU 4535  CB  MET B 219    10174   8035   7466   -893  -1714    371       C
ATOM   4536  CG  MET B 219     -51.183  34.128  45.480  1.00 69.77           C
ANISOU 4536  CG  MET B 219    10184   8306   8019   -804  -1881    489       C
ATOM   4537  SD  MET B 219     -50.339  35.234  44.337  1.00 72.94           S
ANISOU 4537  SD  MET B 219    10318   8698   8699   -778  -1921    393       S
ATOM   4538  CE  MET B 219     -49.286  36.145  45.462  1.00 75.88           C
ANISOU 4538  CE  MET B 219    10836   9080   8916   -917  -2201    344       C
ATOM   4539  N   ASP B 220     -51.336  33.961  49.221  1.00 68.68           N
ANISOU 4539  N   ASP B 220    10893   8199   7001  -1125  -2143    548       N
ATOM   4540  CA  ASP B 220     -50.372  33.348  50.127  1.00 72.59           C
ANISOU 4540  CA  ASP B 220    11533   8692   7357  -1194  -2495    696       C
ATOM   4541  C   ASP B 220     -51.035  32.357  51.074  1.00 70.74           C
ANISOU 4541  C   ASP B 220    11599   8450   6829  -1262  -2452    816       C
ATOM   4542  O   ASP B 220     -50.403  31.378  51.485  1.00 69.01           O
ANISOU 4542  O   ASP B 220    11436   8204   6582  -1263  -2719   1003       O
ATOM   4543  CB  ASP B 220     -49.634  34.430  50.913  1.00 80.38           C
ANISOU 4543  CB  ASP B 220    12672   9693   8176  -1326  -2708    601       C
ATOM   4544  CG  ASP B 220     -48.898  35.401  50.010  1.00 86.18           C
ANISOU 4544  CG  ASP B 220    13117  10425   9204  -1282  -2765    495       C
ATOM   4545  OD1 ASP B 220     -48.345  34.955  48.982  1.00 86.61           O
ANISOU 4545  OD1 ASP B 220    12848  10471   9591  -1162  -2818    567       O
ATOM   4546  OD2 ASP B 220     -48.878  36.610  50.323  1.00 88.91           O
ANISOU 4546  OD2 ASP B 220    13568  10769   9444  -1375  -2741    336       O
ATOM   4547  N   GLU B 221     -52.299  32.584  51.431  1.00 72.11           N
ANISOU 4547  N   GLU B 221    11964   8640   6796  -1320  -2119    715       N
ATOM   4548  CA  GLU B 221     -52.992  31.630  52.289  1.00 75.79           C
ANISOU 4548  CA  GLU B 221    12716   9097   6983  -1404  -2033    827       C
ATOM   4549  C   GLU B 221     -53.355  30.365  51.522  1.00 70.02           C
ANISOU 4549  C   GLU B 221    11800   8331   6473  -1286  -1951    972       C
ATOM   4550  O   GLU B 221     -53.249  29.255  52.057  1.00 71.29           O
ANISOU 4550  O   GLU B 221    12119   8454   6513  -1322  -2080   1158       O
ATOM   4551  CB  GLU B 221     -54.239  32.275  52.889  1.00 85.93           C
ANISOU 4551  CB  GLU B 221    14235  10409   8005  -1508  -1665    654       C
ATOM   4552  CG  GLU B 221     -53.942  33.435  53.820  1.00100.47           C
ANISOU 4552  CG  GLU B 221    16334  12269   9569  -1648  -1732    503       C
ATOM   4553  CD  GLU B 221     -55.028  34.488  53.791  1.00108.57           C
ANISOU 4553  CD  GLU B 221    17391  13305  10558  -1664  -1339    255       C
ATOM   4554  OE1 GLU B 221     -54.740  35.654  54.135  1.00111.43           O
ANISOU 4554  OE1 GLU B 221    17850  13662  10827  -1726  -1371     89       O
ATOM   4555  OE2 GLU B 221     -56.169  34.151  53.410  1.00109.89           O
ANISOU 4555  OE2 GLU B 221    17472  13473  10809  -1610  -1003    223       O
ATOM   4556  N   PHE B 222     -53.768  30.511  50.262  1.00 63.73           N
ANISOU 4556  N   PHE B 222    10685   7534   5994  -1153  -1752    894       N
ATOM   4557  CA  PHE B 222     -54.185  29.354  49.477  1.00 61.21           C
ANISOU 4557  CA  PHE B 222    10198   7178   5883  -1052  -1655   1007       C
ATOM   4558  C   PHE B 222     -52.997  28.473  49.108  1.00 61.21           C
ANISOU 4558  C   PHE B 222    10044   7124   6088   -961  -1979   1178       C
ATOM   4559  O   PHE B 222     -53.091  27.241  49.164  1.00 61.84           O
ANISOU 4559  O   PHE B 222    10165   7146   6188   -937  -2022   1337       O
ATOM   4560  CB  PHE B 222     -54.924  29.819  48.222  1.00 57.91           C
ANISOU 4560  CB  PHE B 222     9500   6773   5731   -948  -1382    871       C
ATOM   4561  CG  PHE B 222     -55.388  28.697  47.336  1.00 58.21           C
ANISOU 4561  CG  PHE B 222     9365   6771   5982   -856  -1278    962       C
ATOM   4562  CD1 PHE B 222     -56.581  28.041  47.592  1.00 59.99           C
ANISOU 4562  CD1 PHE B 222     9701   6987   6104   -907  -1035    987       C
ATOM   4563  CD2 PHE B 222     -54.638  28.307  46.239  1.00 56.45           C
ANISOU 4563  CD2 PHE B 222     8869   6516   6065   -730  -1409   1012       C
ATOM   4564  CE1 PHE B 222     -57.013  27.013  46.775  1.00 58.35           C
ANISOU 4564  CE1 PHE B 222     9342   6735   6094   -836   -951   1064       C
ATOM   4565  CE2 PHE B 222     -55.063  27.279  45.420  1.00 54.81           C
ANISOU 4565  CE2 PHE B 222     8524   6261   6040   -654  -1311   1080       C
ATOM   4566  CZ  PHE B 222     -56.252  26.631  45.688  1.00 55.44           C
ANISOU 4566  CZ  PHE B 222     8722   6328   6014   -708  -1094   1108       C
ATOM   4567  N   ILE B 223     -51.873  29.085  48.731  1.00 60.08           N
ANISOU 4567  N   ILE B 223     9718   6991   6118   -911  -2201   1142       N
ATOM   4568  CA  ILE B 223     -50.719  28.314  48.277  1.00 59.86           C
ANISOU 4568  CA  ILE B 223     9484   6910   6350   -806  -2482   1277       C
ATOM   4569  C   ILE B 223     -50.134  27.493  49.420  1.00 65.80           C
ANISOU 4569  C   ILE B 223    10472   7613   6916   -867  -2795   1467       C
ATOM   4570  O   ILE B 223     -49.747  26.332  49.234  1.00 68.52           O
ANISOU 4570  O   ILE B 223    10742   7876   7415   -781  -2938   1627       O
ATOM   4571  CB  ILE B 223     -49.676  29.254  47.645  1.00 55.62           C
ANISOU 4571  CB  ILE B 223     8687   6402   6045   -761  -2620   1179       C
ATOM   4572  CG1 ILE B 223     -50.218  29.827  46.332  1.00 54.13           C
ANISOU 4572  CG1 ILE B 223     8257   6237   6074   -685  -2329   1034       C
ATOM   4573  CG2 ILE B 223     -48.358  28.531  47.415  1.00 55.74           C
ANISOU 4573  CG2 ILE B 223     8498   6364   6315   -670  -2937   1309       C
ATOM   4574  CD1 ILE B 223     -49.276  30.785  45.643  1.00 57.45           C
ANISOU 4574  CD1 ILE B 223     8438   6680   6711   -661  -2419    936       C
ATOM   4575  N   GLU B 224     -50.066  28.071  50.621  1.00 70.05           N
ANISOU 4575  N   GLU B 224    11315   8187   7115  -1018  -2914   1454       N
ATOM   4576  CA  GLU B 224     -49.588  27.310  51.769  1.00 74.80           C
ANISOU 4576  CA  GLU B 224    12195   8737   7487  -1099  -3226   1648       C
ATOM   4577  C   GLU B 224     -50.595  26.248  52.195  1.00 75.01           C
ANISOU 4577  C   GLU B 224    12468   8715   7316  -1148  -3050   1771       C
ATOM   4578  O   GLU B 224     -50.200  25.176  52.668  1.00 78.69           O
ANISOU 4578  O   GLU B 224    13058   9094   7746  -1144  -3292   1983       O
ATOM   4579  CB  GLU B 224     -49.280  28.249  52.936  1.00 79.96           C
ANISOU 4579  CB  GLU B 224    13145   9444   7794  -1273  -3394   1589       C
ATOM   4580  CG  GLU B 224     -48.787  27.538  54.189  1.00 89.50           C
ANISOU 4580  CG  GLU B 224    14690  10600   8714  -1383  -3750   1796       C
ATOM   4581  CD  GLU B 224     -48.483  28.493  55.325  1.00 98.34           C
ANISOU 4581  CD  GLU B 224    16080  11769   9513  -1559  -3869   1698       C
ATOM   4582  OE1 GLU B 224     -48.144  29.662  55.047  1.00100.84           O
ANISOU 4582  OE1 GLU B 224    16292  12146   9876  -1580  -3899   1535       O
ATOM   4583  OE2 GLU B 224     -48.585  28.074  56.498  1.00103.12           O
ANISOU 4583  OE2 GLU B 224    16997  12346   9838  -1681  -3913   1771       O
ATOM   4584  N   ARG B 225     -51.891  26.521  52.026  1.00 72.36           N
ANISOU 4584  N   ARG B 225    12196   8424   6872  -1193  -2637   1645       N
ATOM   4585  CA  ARG B 225     -52.915  25.566  52.438  1.00 73.97           C
ANISOU 4585  CA  ARG B 225    12626   8587   6891  -1264  -2434   1747       C
ATOM   4586  C   ARG B 225     -52.810  24.270  51.645  1.00 72.58           C
ANISOU 4586  C   ARG B 225    12252   8312   7015  -1126  -2477   1899       C
ATOM   4587  O   ARG B 225     -52.764  23.177  52.220  1.00 76.79           O
ANISOU 4587  O   ARG B 225    12987   8754   7436  -1166  -2614   2100       O
ATOM   4588  CB  ARG B 225     -54.304  26.183  52.270  1.00 76.06           C
ANISOU 4588  CB  ARG B 225    12915   8922   7063  -1322  -1972   1557       C
ATOM   4589  CG  ARG B 225     -55.438  25.332  52.819  1.00 78.44           C
ANISOU 4589  CG  ARG B 225    13463   9195   7144  -1435  -1721   1637       C
ATOM   4590  CD  ARG B 225     -56.781  25.833  52.315  1.00 79.85           C
ANISOU 4590  CD  ARG B 225    13525   9432   7384  -1438  -1266   1445       C
ATOM   4591  NE  ARG B 225     -57.900  25.310  53.094  1.00 84.27           N
ANISOU 4591  NE  ARG B 225    14360   9989   7670  -1597   -988   1476       N
ATOM   4592  CZ  ARG B 225     -58.488  25.971  54.085  1.00 89.04           C
ANISOU 4592  CZ  ARG B 225    15249  10651   7933  -1760   -786   1363       C
ATOM   4593  NH1 ARG B 225     -58.064  27.183  54.419  1.00 85.96           N
ANISOU 4593  NH1 ARG B 225    14913  10316   7433  -1782   -850   1209       N
ATOM   4594  NH2 ARG B 225     -59.502  25.424  54.742  1.00 95.99           N
ANISOU 4594  NH2 ARG B 225    16363  11527   8584  -1912   -505   1394       N
ATOM   4595  N   TYR B 226     -52.773  24.372  50.317  1.00 68.21           N
ANISOU 4595  N   TYR B 226    11321   7763   6835   -970  -2361   1804       N
ATOM   4596  CA  TYR B 226     -52.681  23.207  49.448  1.00 65.93           C
ANISOU 4596  CA  TYR B 226    10829   7374   6847   -836  -2373   1910       C
ATOM   4597  C   TYR B 226     -51.246  22.898  49.037  1.00 64.86           C
ANISOU 4597  C   TYR B 226    10465   7174   7005   -695  -2722   1992       C
ATOM   4598  O   TYR B 226     -51.032  22.204  48.037  1.00 61.44           O
ANISOU 4598  O   TYR B 226     9779   6670   6896   -554  -2700   2012       O
ATOM   4599  CB  TYR B 226     -53.570  23.396  48.219  1.00 60.86           C
ANISOU 4599  CB  TYR B 226     9936   6766   6421   -764  -2024   1759       C
ATOM   4600  CG  TYR B 226     -55.047  23.349  48.542  1.00 58.85           C
ANISOU 4600  CG  TYR B 226     9858   6544   5958   -881  -1680   1710       C
ATOM   4601  CD1 TYR B 226     -55.720  22.137  48.625  1.00 57.85           C
ANISOU 4601  CD1 TYR B 226     9837   6335   5810   -914  -1578   1836       C
ATOM   4602  CD2 TYR B 226     -55.766  24.513  48.775  1.00 56.68           C
ANISOU 4602  CD2 TYR B 226     9636   6372   5527   -961  -1452   1532       C
ATOM   4603  CE1 TYR B 226     -57.067  22.086  48.925  1.00 59.31           C
ANISOU 4603  CE1 TYR B 226    10156   6552   5827  -1034  -1251   1787       C
ATOM   4604  CE2 TYR B 226     -57.115  24.472  49.076  1.00 55.50           C
ANISOU 4604  CE2 TYR B 226     9613   6250   5223  -1063  -1123   1474       C
ATOM   4605  CZ  TYR B 226     -57.760  23.257  49.150  1.00 58.43           C
ANISOU 4605  CZ  TYR B 226    10070   6552   5580  -1105  -1020   1603       C
ATOM   4606  OH  TYR B 226     -59.102  23.212  49.450  1.00 61.84           O
ANISOU 4606  OH  TYR B 226    10602   7013   5880  -1218   -679   1541       O
ATOM   4607  N   LYS B 227     -50.267  23.390  49.797  1.00 70.61           N
ANISOU 4607  N   LYS B 227    11276   7922   7632   -737  -3041   2030       N
ATOM   4608  CA  LYS B 227     -48.856  23.027  49.657  1.00 76.50           C
ANISOU 4608  CA  LYS B 227    11826   8597   8643   -621  -3422   2133       C
ATOM   4609  C   LYS B 227     -48.378  23.183  48.212  1.00 73.12           C
ANISOU 4609  C   LYS B 227    10959   8173   8652   -454  -3328   2013       C
ATOM   4610  O   LYS B 227     -47.910  22.239  47.573  1.00 75.00           O
ANISOU 4610  O   LYS B 227    10997   8306   9192   -313  -3400   2091       O
ATOM   4611  CB  LYS B 227     -48.608  21.602  50.164  1.00 84.37           C
ANISOU 4611  CB  LYS B 227    12969   9442   9645   -587  -3652   2378       C
ATOM   4612  CG  LYS B 227     -49.457  21.195  51.366  1.00 92.28           C
ANISOU 4612  CG  LYS B 227    14406  10433  10224   -761  -3579   2475       C
ATOM   4613  CD  LYS B 227     -50.598  20.277  50.941  1.00 96.42           C
ANISOU 4613  CD  LYS B 227    15007  10884  10744   -761  -3293   2537       C
ATOM   4614  CE  LYS B 227     -51.650  20.139  52.029  1.00100.45           C
ANISOU 4614  CE  LYS B 227    15929  11419  10816   -967  -3110   2579       C
ATOM   4615  NZ  LYS B 227     -52.880  19.465  51.522  1.00 98.67           N
ANISOU 4615  NZ  LYS B 227    15726  11153  10610   -988  -2759   2584       N
ATOM   4616  N   LEU B 228     -48.498  24.409  47.702  1.00 65.75           N
ANISOU 4616  N   LEU B 228     9891   7352   7740   -478  -3156   1818       N
ATOM   4617  CA  LEU B 228     -48.171  24.710  46.314  1.00 60.70           C
ANISOU 4617  CA  LEU B 228     8880   6729   7455   -357  -3019   1690       C
ATOM   4618  C   LEU B 228     -46.919  25.570  46.175  1.00 64.30           C
ANISOU 4618  C   LEU B 228     9120   7229   8083   -340  -3236   1623       C
ATOM   4619  O   LEU B 228     -46.757  26.260  45.164  1.00 67.48           O
ANISOU 4619  O   LEU B 228     9277   7680   8683   -300  -3080   1480       O
ATOM   4620  CB  LEU B 228     -49.356  25.388  45.628  1.00 53.53           C
ANISOU 4620  CB  LEU B 228     7961   5896   6482   -391  -2632   1526       C
ATOM   4621  CG  LEU B 228     -50.519  24.478  45.232  1.00 51.33           C
ANISOU 4621  CG  LEU B 228     7743   5570   6190   -370  -2375   1559       C
ATOM   4622  CD1 LEU B 228     -51.719  25.299  44.798  1.00 46.82           C
ANISOU 4622  CD1 LEU B 228     7186   5080   5524   -425  -2041   1401       C
ATOM   4623  CD2 LEU B 228     -50.092  23.534  44.122  1.00 52.90           C
ANISOU 4623  CD2 LEU B 228     7684   5680   6734   -223  -2370   1592       C
ATOM   4624  N   GLU B 229     -46.030  25.543  47.165  1.00 62.70           N
ANISOU 4624  N   GLU B 229     9009   7006   7807   -382  -3600   1729       N
ATOM   4625  CA  GLU B 229     -44.788  26.297  47.065  1.00 63.98           C
ANISOU 4625  CA  GLU B 229     8942   7204   8162   -376  -3832   1673       C
ATOM   4626  C   GLU B 229     -43.914  25.735  45.951  1.00 62.10           C
ANISOU 4626  C   GLU B 229     8299   6905   8390   -207  -3854   1671       C
ATOM   4627  O   GLU B 229     -43.798  24.518  45.782  1.00 64.72           O
ANISOU 4627  O   GLU B 229     8576   7129   8887    -90  -3910   1791       O
ATOM   4628  CB  GLU B 229     -44.026  26.266  48.391  1.00 73.05           C
ANISOU 4628  CB  GLU B 229    10279   8334   9144   -459  -4260   1804       C
ATOM   4629  CG  GLU B 229     -44.707  27.003  49.534  1.00 81.78           C
ANISOU 4629  CG  GLU B 229    11792   9508   9772   -652  -4252   1774       C
ATOM   4630  CD  GLU B 229     -45.706  26.141  50.281  1.00 91.64           C
ANISOU 4630  CD  GLU B 229    13407  10710  10702   -708  -4169   1902       C
ATOM   4631  OE1 GLU B 229     -46.018  25.031  49.799  1.00 93.15           O
ANISOU 4631  OE1 GLU B 229    13530  10817  11046   -597  -4074   2000       O
ATOM   4632  OE2 GLU B 229     -46.175  26.571  51.355  1.00 96.69           O
ANISOU 4632  OE2 GLU B 229    14413  11391  10932   -874  -4188   1901       O
ATOM   4633  N   GLY B 230     -43.299  26.633  45.185  1.00 59.20           N
ANISOU 4633  N   GLY B 230     7655   6599   8237   -202  -3793   1527       N
ATOM   4634  CA  GLY B 230     -42.434  26.231  44.097  1.00 58.21           C
ANISOU 4634  CA  GLY B 230     7139   6430   8549    -63  -3770   1494       C
ATOM   4635  C   GLY B 230     -43.142  25.805  42.833  1.00 57.27           C
ANISOU 4635  C   GLY B 230     6913   6289   8557     23  -3397   1417       C
ATOM   4636  O   GLY B 230     -42.501  25.218  41.953  1.00 60.18           O
ANISOU 4636  O   GLY B 230     6996   6598   9271    147  -3356   1399       O
ATOM   4637  N   TYR B 231     -44.440  26.079  42.707  1.00 54.22           N
ANISOU 4637  N   TYR B 231     6744   5946   7911    -42  -3125   1363       N
ATOM   4638  CA  TYR B 231     -45.193  25.706  41.516  1.00 53.25           C
ANISOU 4638  CA  TYR B 231     6542   5806   7885     22  -2794   1292       C
ATOM   4639  C   TYR B 231     -45.693  26.912  40.731  1.00 49.75           C
ANISOU 4639  C   TYR B 231     6059   5455   7388    -49  -2537   1128       C
ATOM   4640  O   TYR B 231     -46.490  26.743  39.800  1.00 50.26           O
ANISOU 4640  O   TYR B 231     6107   5517   7474    -22  -2271   1067       O
ATOM   4641  CB  TYR B 231     -46.359  24.788  41.891  1.00 54.45           C
ANISOU 4641  CB  TYR B 231     6947   5904   7837     22  -2694   1384       C
ATOM   4642  CG  TYR B 231     -45.906  23.391  42.247  1.00 55.38           C
ANISOU 4642  CG  TYR B 231     7064   5890   8087    123  -2888   1544       C
ATOM   4643  CD1 TYR B 231     -45.554  22.485  41.255  1.00 56.40           C
ANISOU 4643  CD1 TYR B 231     6972   5925   8535    260  -2808   1535       C
ATOM   4644  CD2 TYR B 231     -45.817  22.982  43.571  1.00 57.94           C
ANISOU 4644  CD2 TYR B 231     7625   6173   8217     77  -3155   1704       C
ATOM   4645  CE1 TYR B 231     -45.133  21.207  41.570  1.00 59.36           C
ANISOU 4645  CE1 TYR B 231     7343   6153   9059    365  -2989   1678       C
ATOM   4646  CE2 TYR B 231     -45.396  21.703  43.896  1.00 60.92           C
ANISOU 4646  CE2 TYR B 231     8014   6406   8726    173  -3357   1868       C
ATOM   4647  CZ  TYR B 231     -45.056  20.821  42.891  1.00 59.69           C
ANISOU 4647  CZ  TYR B 231     7617   6145   8918    325  -3274   1853       C
ATOM   4648  OH  TYR B 231     -44.637  19.548  43.205  1.00 57.94           O
ANISOU 4648  OH  TYR B 231     7405   5756   8854    434  -3476   2012       O
ATOM   4649  N   ALA B 232     -45.244  28.120  41.082  1.00 47.32           N
ANISOU 4649  N   ALA B 232     5746   5219   7014   -143  -2628   1059       N
ATOM   4650  CA  ALA B 232     -45.470  29.325  40.281  1.00 47.36           C
ANISOU 4650  CA  ALA B 232     5682   5288   7024   -204  -2426    911       C
ATOM   4651  C   ALA B 232     -46.956  29.603  40.064  1.00 45.35           C
ANISOU 4651  C   ALA B 232     5621   5056   6554   -238  -2165    859       C
ATOM   4652  O   ALA B 232     -47.368  30.071  39.001  1.00 45.44           O
ANISOU 4652  O   ALA B 232     5550   5082   6631   -235  -1948    767       O
ATOM   4653  CB  ALA B 232     -44.737  29.239  38.940  1.00 41.91           C
ANISOU 4653  CB  ALA B 232     4684   4583   6655   -140  -2310    844       C
ATOM   4654  N   PHE B 233     -47.772  29.319  41.080  1.00 47.45           N
ANISOU 4654  N   PHE B 233     6146   5320   6562   -275  -2189    920       N
ATOM   4655  CA  PHE B 233     -49.191  29.635  40.974  1.00 48.77           C
ANISOU 4655  CA  PHE B 233     6473   5510   6549   -310  -1942    861       C
ATOM   4656  C   PHE B 233     -49.432  31.138  40.990  1.00 48.57           C
ANISOU 4656  C   PHE B 233     6495   5535   6426   -393  -1868    731       C
ATOM   4657  O   PHE B 233     -50.401  31.613  40.387  1.00 46.23           O
ANISOU 4657  O   PHE B 233     6214   5247   6105   -393  -1648    651       O
ATOM   4658  CB  PHE B 233     -49.971  28.951  42.094  1.00 53.37           C
ANISOU 4658  CB  PHE B 233     7316   6077   6886   -347  -1959    952       C
ATOM   4659  CG  PHE B 233     -50.711  27.726  41.646  1.00 53.26           C
ANISOU 4659  CG  PHE B 233     7302   6010   6926   -282  -1823   1022       C
ATOM   4660  CD1 PHE B 233     -50.057  26.725  40.948  1.00 56.68           C
ANISOU 4660  CD1 PHE B 233     7557   6376   7602   -181  -1882   1086       C
ATOM   4661  CD2 PHE B 233     -52.060  27.573  41.921  1.00 51.07           C
ANISOU 4661  CD2 PHE B 233     7194   5741   6471   -328  -1626   1013       C
ATOM   4662  CE1 PHE B 233     -50.734  25.594  40.529  1.00 55.93           C
ANISOU 4662  CE1 PHE B 233     7476   6217   7557   -131  -1760   1141       C
ATOM   4663  CE2 PHE B 233     -52.743  26.445  41.507  1.00 51.29           C
ANISOU 4663  CE2 PHE B 233     7217   5714   6556   -286  -1507   1075       C
ATOM   4664  CZ  PHE B 233     -52.079  25.454  40.810  1.00 52.39           C
ANISOU 4664  CZ  PHE B 233     7202   5781   6924   -190  -1581   1140       C
ATOM   4665  N   GLU B 234     -48.558  31.899  41.657  1.00 52.64           N
ANISOU 4665  N   GLU B 234     7030   6072   6898   -463  -2063    708       N
ATOM   4666  CA  GLU B 234     -48.659  33.354  41.621  1.00 56.16           C
ANISOU 4666  CA  GLU B 234     7514   6544   7282   -543  -2005    578       C
ATOM   4667  C   GLU B 234     -48.582  33.881  40.195  1.00 52.12           C
ANISOU 4667  C   GLU B 234     6795   6025   6983   -511  -1848    503       C
ATOM   4668  O   GLU B 234     -49.113  34.957  39.899  1.00 55.81           O
ANISOU 4668  O   GLU B 234     7312   6490   7404   -552  -1721    403       O
ATOM   4669  CB  GLU B 234     -47.551  33.985  42.468  1.00 67.20           C
ANISOU 4669  CB  GLU B 234     8936   7958   8640   -632  -2270    569       C
ATOM   4670  CG  GLU B 234     -47.327  33.334  43.825  1.00 75.86           C
ANISOU 4670  CG  GLU B 234    10226   9056   9542   -670  -2498    673       C
ATOM   4671  CD  GLU B 234     -46.283  32.234  43.782  1.00 80.50           C
ANISOU 4671  CD  GLU B 234    10641   9616  10328   -596  -2726    808       C
ATOM   4672  OE1 GLU B 234     -45.993  31.726  42.678  1.00 80.63           O
ANISOU 4672  OE1 GLU B 234    10408   9612  10617   -496  -2637    818       O
ATOM   4673  OE2 GLU B 234     -45.745  31.882  44.854  1.00 84.20           O
ANISOU 4673  OE2 GLU B 234    11231  10078  10683   -639  -3000    901       O
ATOM   4674  N   HIS B 235     -47.928  33.139  39.304  1.00 46.72           N
ANISOU 4674  N   HIS B 235     5895   5327   6530   -440  -1851    548       N
ATOM   4675  CA  HIS B 235     -47.776  33.514  37.905  1.00 41.98           C
ANISOU 4675  CA  HIS B 235     5118   4720   6115   -424  -1696    486       C
ATOM   4676  C   HIS B 235     -48.752  32.780  36.995  1.00 42.38           C
ANISOU 4676  C   HIS B 235     5163   4749   6191   -351  -1490    499       C
ATOM   4677  O   HIS B 235     -49.454  33.411  36.200  1.00 43.37           O
ANISOU 4677  O   HIS B 235     5304   4869   6304   -367  -1329    436       O
ATOM   4678  CB  HIS B 235     -46.336  33.243  37.455  1.00 40.41           C
ANISOU 4678  CB  HIS B 235     4670   4518   6164   -411  -1807    502       C
ATOM   4679  CG  HIS B 235     -46.091  33.523  36.006  1.00 44.54           C
ANISOU 4679  CG  HIS B 235     5025   5035   6863   -412  -1628    440       C
ATOM   4680  ND1 HIS B 235     -45.883  34.795  35.519  1.00 47.21           N
ANISOU 4680  ND1 HIS B 235     5343   5380   7214   -506  -1569    359       N
ATOM   4681  CD2 HIS B 235     -46.021  32.694  34.937  1.00 45.80           C
ANISOU 4681  CD2 HIS B 235     5053   5172   7176   -344  -1489    445       C
ATOM   4682  CE1 HIS B 235     -45.694  34.738  34.212  1.00 47.74           C
ANISOU 4682  CE1 HIS B 235     5282   5436   7421   -503  -1402    328       C
ATOM   4683  NE2 HIS B 235     -45.773  33.475  33.835  1.00 45.93           N
ANISOU 4683  NE2 HIS B 235     4985   5193   7274   -406  -1346    371       N
ATOM   4684  N   ILE B 236     -48.820  31.453  37.109  1.00 46.18           N
ANISOU 4684  N   ILE B 236     5630   5207   6710   -277  -1511    583       N
ATOM   4685  CA  ILE B 236     -49.607  30.656  36.173  1.00 44.13           C
ANISOU 4685  CA  ILE B 236     5347   4918   6501   -217  -1333    591       C
ATOM   4686  C   ILE B 236     -51.096  30.933  36.345  1.00 42.64           C
ANISOU 4686  C   ILE B 236     5327   4739   6137   -238  -1198    568       C
ATOM   4687  O   ILE B 236     -51.810  31.205  35.373  1.00 39.28           O
ANISOU 4687  O   ILE B 236     4879   4306   5738   -236  -1046    518       O
ATOM   4688  CB  ILE B 236     -49.293  29.160  36.352  1.00 39.89           C
ANISOU 4688  CB  ILE B 236     4769   4333   6055   -136  -1401    686       C
ATOM   4689  CG1 ILE B 236     -47.813  28.888  36.079  1.00 38.21           C
ANISOU 4689  CG1 ILE B 236     4342   4100   6075    -95  -1521    693       C
ATOM   4690  CG2 ILE B 236     -50.173  28.322  35.442  1.00 37.55           C
ANISOU 4690  CG2 ILE B 236     4474   3999   5796    -90  -1221    685       C
ATOM   4691  CD1 ILE B 236     -47.374  27.490  36.454  1.00 39.74           C
ANISOU 4691  CD1 ILE B 236     4495   4224   6381     -2  -1639    794       C
ATOM   4692  N   VAL B 237     -51.586  30.865  37.576  1.00 42.51           N
ANISOU 4692  N   VAL B 237     5480   4734   5940   -265  -1252    602       N
ATOM   4693  CA  VAL B 237     -53.014  30.958  37.854  1.00 40.14           C
ANISOU 4693  CA  VAL B 237     5319   4438   5495   -283  -1104    579       C
ATOM   4694  C   VAL B 237     -53.425  32.377  38.218  1.00 43.83           C
ANISOU 4694  C   VAL B 237     5871   4928   5854   -339  -1061    480       C
ATOM   4695  O   VAL B 237     -54.408  32.900  37.692  1.00 45.38           O
ANISOU 4695  O   VAL B 237     6068   5116   6058   -332   -913    416       O
ATOM   4696  CB  VAL B 237     -53.405  29.956  38.963  1.00 39.10           C
ANISOU 4696  CB  VAL B 237     5339   4297   5221   -292  -1141    672       C
ATOM   4697  CG1 VAL B 237     -54.908  29.962  39.175  1.00 40.83           C
ANISOU 4697  CG1 VAL B 237     5668   4523   5323   -316   -950    640       C
ATOM   4698  CG2 VAL B 237     -52.918  28.562  38.605  1.00 38.80           C
ANISOU 4698  CG2 VAL B 237     5218   4209   5315   -227  -1202    772       C
ATOM   4699  N   TYR B 238     -52.684  33.019  39.123  1.00 42.89           N
ANISOU 4699  N   TYR B 238     5826   4826   5644   -395  -1202    462       N
ATOM   4700  CA  TYR B 238     -53.055  34.357  39.567  1.00 40.36           C
ANISOU 4700  CA  TYR B 238     5612   4508   5214   -453  -1161    355       C
ATOM   4701  C   TYR B 238     -52.686  35.430  38.550  1.00 41.62           C
ANISOU 4701  C   TYR B 238     5651   4646   5516   -459  -1141    281       C
ATOM   4702  O   TYR B 238     -53.418  36.415  38.405  1.00 40.48           O
ANISOU 4702  O   TYR B 238     5559   4474   5347   -469  -1036    194       O
ATOM   4703  CB  TYR B 238     -52.406  34.660  40.918  1.00 41.16           C
ANISOU 4703  CB  TYR B 238     5866   4628   5144   -530  -1329    355       C
ATOM   4704  CG  TYR B 238     -52.967  33.844  42.060  1.00 47.99           C
ANISOU 4704  CG  TYR B 238     6925   5507   5801   -556  -1325    417       C
ATOM   4705  CD1 TYR B 238     -54.057  34.296  42.791  1.00 50.99           C
ANISOU 4705  CD1 TYR B 238     7489   5891   5994   -601  -1166    338       C
ATOM   4706  CD2 TYR B 238     -52.410  32.620  42.405  1.00 50.20           C
ANISOU 4706  CD2 TYR B 238     7208   5786   6080   -538  -1469    553       C
ATOM   4707  CE1 TYR B 238     -54.574  33.554  43.836  1.00 50.64           C
ANISOU 4707  CE1 TYR B 238     7641   5861   5740   -648  -1134    394       C
ATOM   4708  CE2 TYR B 238     -52.921  31.869  43.447  1.00 52.56           C
ANISOU 4708  CE2 TYR B 238     7713   6086   6171   -579  -1467    626       C
ATOM   4709  CZ  TYR B 238     -54.002  32.343  44.160  1.00 54.28           C
ANISOU 4709  CZ  TYR B 238     8126   6320   6178   -644  -1291    547       C
ATOM   4710  OH  TYR B 238     -54.515  31.599  45.198  1.00 58.58           O
ANISOU 4710  OH  TYR B 238     8893   6866   6497   -707  -1262    619       O
ATOM   4711  N   GLY B 239     -51.576  35.264  37.847  1.00 44.40           N
ANISOU 4711  N   GLY B 239     5845   5001   6025   -455  -1230    314       N
ATOM   4712  CA  GLY B 239     -51.201  36.227  36.822  1.00 42.90           C
ANISOU 4712  CA  GLY B 239     5554   4786   5959   -482  -1193    256       C
ATOM   4713  C   GLY B 239     -50.387  37.380  37.374  1.00 43.39           C
ANISOU 4713  C   GLY B 239     5650   4842   5994   -571  -1314    196       C
ATOM   4714  O   GLY B 239     -50.542  37.807  38.518  1.00 44.89           O
ANISOU 4714  O   GLY B 239     5993   5034   6029   -614  -1379    158       O
ATOM   4715  N   ASP B 240     -49.499  37.898  36.530  1.00 42.12           N
ANISOU 4715  N   ASP B 240     5353   4668   5982   -614  -1333    179       N
ATOM   4716  CA  ASP B 240     -48.616  39.004  36.879  1.00 46.10           C
ANISOU 4716  CA  ASP B 240     5858   5157   6499   -717  -1448    122       C
ATOM   4717  C   ASP B 240     -49.029  40.236  36.085  1.00 43.79           C
ANISOU 4717  C   ASP B 240     5604   4798   6236   -759  -1337     55       C
ATOM   4718  O   ASP B 240     -49.042  40.208  34.849  1.00 40.28           O
ANISOU 4718  O   ASP B 240     5068   4336   5902   -749  -1232     75       O
ATOM   4719  CB  ASP B 240     -47.156  38.646  36.600  1.00 52.02           C
ANISOU 4719  CB  ASP B 240     6403   5939   7424   -752  -1565    158       C
ATOM   4720  CG  ASP B 240     -46.190  39.726  37.054  1.00 56.99           C
ANISOU 4720  CG  ASP B 240     7017   6556   8080   -876  -1707    101       C
ATOM   4721  OD1 ASP B 240     -46.608  40.631  37.806  1.00 60.41           O
ANISOU 4721  OD1 ASP B 240     7633   6958   8364   -932  -1744     36       O
ATOM   4722  OD2 ASP B 240     -45.009  39.670  36.653  1.00 59.67           O
ANISOU 4722  OD2 ASP B 240     7156   6913   8601   -923  -1774    112       O
ATOM   4723  N   PHE B 241     -49.358  41.313  36.795  1.00 45.57           N
ANISOU 4723  N   PHE B 241     5983   4975   6355   -810  -1363    -26       N
ATOM   4724  CA  PHE B 241     -49.788  42.562  36.182  1.00 44.79           C
ANISOU 4724  CA  PHE B 241     5947   4784   6288   -844  -1282    -88       C
ATOM   4725  C   PHE B 241     -48.809  43.701  36.432  1.00 48.49           C
ANISOU 4725  C   PHE B 241     6431   5207   6788   -975  -1391   -149       C
ATOM   4726  O   PHE B 241     -49.094  44.844  36.060  1.00 49.67           O
ANISOU 4726  O   PHE B 241     6658   5256   6958  -1016  -1344   -203       O
ATOM   4727  CB  PHE B 241     -51.176  42.951  36.694  1.00 43.56           C
ANISOU 4727  CB  PHE B 241     5957   4576   6017   -779  -1187   -151       C
ATOM   4728  CG  PHE B 241     -52.185  41.845  36.611  1.00 44.23           C
ANISOU 4728  CG  PHE B 241     6028   4707   6070   -668  -1084   -100       C
ATOM   4729  CD1 PHE B 241     -52.954  41.677  35.472  1.00 43.95           C
ANISOU 4729  CD1 PHE B 241     5932   4642   6125   -602   -973    -63       C
ATOM   4730  CD2 PHE B 241     -52.369  40.976  37.674  1.00 50.53           C
ANISOU 4730  CD2 PHE B 241     6887   5572   6741   -645  -1108    -83       C
ATOM   4731  CE1 PHE B 241     -53.886  40.659  35.393  1.00 44.54           C
ANISOU 4731  CE1 PHE B 241     5986   4756   6182   -516   -888    -21       C
ATOM   4732  CE2 PHE B 241     -53.299  39.956  37.601  1.00 50.51           C
ANISOU 4732  CE2 PHE B 241     6873   5603   6716   -562  -1006    -34       C
ATOM   4733  CZ  PHE B 241     -54.058  39.798  36.459  1.00 47.26           C
ANISOU 4733  CZ  PHE B 241     6380   5164   6414   -497   -895     -8       C
ATOM   4734  N   SER B 242     -47.664  43.417  37.055  1.00 50.08           N
ANISOU 4734  N   SER B 242     6555   5468   7006  -1044  -1549   -137       N
ATOM   4735  CA  SER B 242     -46.726  44.473  37.414  1.00 46.96           C
ANISOU 4735  CA  SER B 242     6171   5032   6640  -1186  -1675   -201       C
ATOM   4736  C   SER B 242     -46.015  45.062  36.204  1.00 45.71           C
ANISOU 4736  C   SER B 242     5874   4832   6662  -1271  -1620   -188       C
ATOM   4737  O   SER B 242     -45.540  46.200  36.276  1.00 49.23           O
ANISOU 4737  O   SER B 242     6366   5205   7136  -1396  -1672   -250       O
ATOM   4738  CB  SER B 242     -45.697  43.938  38.410  1.00 47.98           C
ANISOU 4738  CB  SER B 242     6237   5238   6754  -1238  -1892   -181       C
ATOM   4739  OG  SER B 242     -45.065  42.772  37.909  1.00 49.69           O
ANISOU 4739  OG  SER B 242     6233   5532   7114  -1182  -1910    -86       O
ATOM   4740  N   HIS B 243     -45.933  44.326  35.102  1.00 41.94           N
ANISOU 4740  N   HIS B 243     5247   4392   6296  -1220  -1508   -116       N
ATOM   4741  CA  HIS B 243     -45.209  44.756  33.917  1.00 41.01           C
ANISOU 4741  CA  HIS B 243     5005   4247   6331  -1316  -1427   -100       C
ATOM   4742  C   HIS B 243     -46.183  45.103  32.798  1.00 39.80           C
ANISOU 4742  C   HIS B 243     4952   4018   6151  -1280  -1259    -77       C
ATOM   4743  O   HIS B 243     -47.376  44.793  32.858  1.00 38.53           O
ANISOU 4743  O   HIS B 243     4900   3844   5894  -1160  -1205    -66       O
ATOM   4744  CB  HIS B 243     -44.230  43.670  33.457  1.00 51.62           C
ANISOU 4744  CB  HIS B 243     6100   5685   7830  -1306  -1418    -49       C
ATOM   4745  CG  HIS B 243     -43.184  43.332  34.473  1.00 67.72           C
ANISOU 4745  CG  HIS B 243     8008   7786   9936  -1340  -1619    -57       C
ATOM   4746  ND1 HIS B 243     -43.492  42.857  35.730  1.00 71.35           N
ANISOU 4746  ND1 HIS B 243     8562   8280  10266  -1272  -1773    -51       N
ATOM   4747  CD2 HIS B 243     -41.833  43.401  34.419  1.00 73.63           C
ANISOU 4747  CD2 HIS B 243     8538   8566  10872  -1442  -1701    -67       C
ATOM   4748  CE1 HIS B 243     -42.376  42.649  36.406  1.00 73.89           C
ANISOU 4748  CE1 HIS B 243     8743   8647  10683  -1328  -1970    -47       C
ATOM   4749  NE2 HIS B 243     -41.355  42.971  35.633  1.00 75.12           N
ANISOU 4749  NE2 HIS B 243     8689   8804  11051  -1425  -1934    -60       N
ATOM   4750  N   SER B 244     -45.651  45.760  31.764  1.00 38.88           N
ANISOU 4750  N   SER B 244     4798   3849   6124  -1396  -1183    -65       N
ATOM   4751  CA  SER B 244     -46.481  46.144  30.627  1.00 39.33           C
ANISOU 4751  CA  SER B 244     4969   3824   6150  -1384  -1054    -25       C
ATOM   4752  C   SER B 244     -47.054  44.919  29.931  1.00 41.43           C
ANISOU 4752  C   SER B 244     5184   4159   6398  -1267   -952     34       C
ATOM   4753  O   SER B 244     -48.213  44.924  29.498  1.00 40.30           O
ANISOU 4753  O   SER B 244     5160   3967   6185  -1186   -904     62       O
ATOM   4754  CB  SER B 244     -45.672  46.987  29.642  1.00 40.21           C
ANISOU 4754  CB  SER B 244     5064   3872   6344  -1558   -988    -10       C
ATOM   4755  OG  SER B 244     -44.760  46.180  28.916  1.00 44.48           O
ANISOU 4755  OG  SER B 244     5413   4504   6983  -1607   -891     17       O
ATOM   4756  N   GLN B 245     -46.261  43.859  29.816  1.00 42.57           N
ANISOU 4756  N   GLN B 245     5145   4407   6623  -1257   -926     49       N
ATOM   4757  CA  GLN B 245     -46.717  42.610  29.226  1.00 39.32           C
ANISOU 4757  CA  GLN B 245     4684   4053   6203  -1150   -832     92       C
ATOM   4758  C   GLN B 245     -47.287  41.724  30.326  1.00 37.24           C
ANISOU 4758  C   GLN B 245     4424   3844   5883  -1011   -918     94       C
ATOM   4759  O   GLN B 245     -46.600  41.424  31.310  1.00 39.69           O
ANISOU 4759  O   GLN B 245     4648   4204   6227  -1007  -1033     79       O
ATOM   4760  CB  GLN B 245     -45.578  41.905  28.493  1.00 42.86           C
ANISOU 4760  CB  GLN B 245     4937   4563   6786  -1204   -737     95       C
ATOM   4761  CG  GLN B 245     -46.033  40.773  27.582  1.00 50.82           C
ANISOU 4761  CG  GLN B 245     5929   5601   7778  -1126   -604    125       C
ATOM   4762  CD  GLN B 245     -46.813  41.264  26.372  1.00 56.51           C
ANISOU 4762  CD  GLN B 245     6820   6255   8396  -1176   -497    155       C
ATOM   4763  OE1 GLN B 245     -46.861  42.463  26.089  1.00 57.30           O
ANISOU 4763  OE1 GLN B 245     7033   6279   8459  -1278   -507    162       O
ATOM   4764  NE2 GLN B 245     -47.426  40.334  25.649  1.00 57.84           N
ANISOU 4764  NE2 GLN B 245     7018   6441   8518  -1110   -410    178       N
ATOM   4765  N   LEU B 246     -48.543  41.318  30.161  1.00 36.79           N
ANISOU 4765  N   LEU B 246     4469   3773   5737   -908   -871    118       N
ATOM   4766  CA  LEU B 246     -49.198  40.470  31.146  1.00 38.55           C
ANISOU 4766  CA  LEU B 246     4714   4041   5894   -793   -921    126       C
ATOM   4767  C   LEU B 246     -48.519  39.107  31.203  1.00 44.47           C
ANISOU 4767  C   LEU B 246     5312   4866   6718   -745   -926    159       C
ATOM   4768  O   LEU B 246     -48.174  38.523  30.172  1.00 48.58           O
ANISOU 4768  O   LEU B 246     5741   5398   7318   -749   -827    177       O
ATOM   4769  CB  LEU B 246     -50.679  40.319  30.801  1.00 36.16           C
ANISOU 4769  CB  LEU B 246     4520   3703   5516   -708   -851    142       C
ATOM   4770  CG  LEU B 246     -51.663  40.084  31.949  1.00 37.38           C
ANISOU 4770  CG  LEU B 246     4758   3867   5576   -622   -881    125       C
ATOM   4771  CD1 LEU B 246     -53.061  40.502  31.530  1.00 40.13           C
ANISOU 4771  CD1 LEU B 246     5197   4151   5899   -567   -816    118       C
ATOM   4772  CD2 LEU B 246     -51.661  38.632  32.396  1.00 34.18           C
ANISOU 4772  CD2 LEU B 246     4291   3536   5159   -552   -884    167       C
ATOM   4773  N   GLY B 247     -48.320  38.604  32.418  1.00 44.44           N
ANISOU 4773  N   GLY B 247     5298   4903   6685   -701  -1044    167       N
ATOM   4774  CA  GLY B 247     -47.619  37.351  32.641  1.00 42.73           C
ANISOU 4774  CA  GLY B 247     4942   4736   6558   -646  -1091    209       C
ATOM   4775  C   GLY B 247     -48.549  36.293  33.215  1.00 46.14           C
ANISOU 4775  C   GLY B 247     5455   5181   6896   -541  -1094    256       C
ATOM   4776  O   GLY B 247     -49.264  36.543  34.186  1.00 48.99           O
ANISOU 4776  O   GLY B 247     5958   5541   7115   -530  -1144    251       O
ATOM   4777  N   GLY B 248     -48.523  35.114  32.594  1.00 44.94           N
ANISOU 4777  N   GLY B 248     5216   5034   6826   -474  -1024    293       N
ATOM   4778  CA  GLY B 248     -49.282  33.986  33.110  1.00 44.66           C
ANISOU 4778  CA  GLY B 248     5244   5001   6725   -387  -1030    346       C
ATOM   4779  C   GLY B 248     -50.776  34.127  32.887  1.00 41.75           C
ANISOU 4779  C   GLY B 248     5013   4615   6236   -368   -922    338       C
ATOM   4780  O   GLY B 248     -51.234  34.540  31.815  1.00 37.89           O
ANISOU 4780  O   GLY B 248     4530   4104   5763   -388   -816    312       O
ATOM   4781  N   LEU B 249     -51.549  33.767  33.916  1.00 43.49           N
ANISOU 4781  N   LEU B 249     5345   4843   6337   -336   -952    365       N
ATOM   4782  CA  LEU B 249     -53.012  33.820  33.894  1.00 44.27           C
ANISOU 4782  CA  LEU B 249     5547   4929   6345   -315   -849    353       C
ATOM   4783  C   LEU B 249     -53.571  32.912  32.792  1.00 46.36           C
ANISOU 4783  C   LEU B 249     5760   5175   6679   -276   -746    378       C
ATOM   4784  O   LEU B 249     -54.102  33.361  31.773  1.00 43.33           O
ANISOU 4784  O   LEU B 249     5372   4770   6322   -289   -672    350       O
ATOM   4785  CB  LEU B 249     -53.499  35.265  33.727  1.00 42.52           C
ANISOU 4785  CB  LEU B 249     5386   4683   6088   -354   -815    283       C
ATOM   4786  CG  LEU B 249     -54.935  35.578  34.159  1.00 41.98           C
ANISOU 4786  CG  LEU B 249     5417   4598   5938   -328   -735    250       C
ATOM   4787  CD1 LEU B 249     -55.074  35.516  35.674  1.00 43.08           C
ANISOU 4787  CD1 LEU B 249     5667   4762   5940   -339   -767    239       C
ATOM   4788  CD2 LEU B 249     -55.363  36.937  33.631  1.00 40.59           C
ANISOU 4788  CD2 LEU B 249     5266   4367   5790   -344   -706    188       C
ATOM   4789  N   HIS B 250     -53.445  31.607  33.035  1.00 44.63           N
ANISOU 4789  N   HIS B 250     5519   4955   6484   -233   -759    435       N
ATOM   4790  CA  HIS B 250     -53.827  30.602  32.052  1.00 41.58           C
ANISOU 4790  CA  HIS B 250     5090   4541   6168   -203   -673    452       C
ATOM   4791  C   HIS B 250     -54.990  29.721  32.488  1.00 38.14           C
ANISOU 4791  C   HIS B 250     4727   4091   5672   -180   -627    492       C
ATOM   4792  O   HIS B 250     -55.410  28.855  31.712  1.00 32.57           O
ANISOU 4792  O   HIS B 250     4000   3355   5020   -166   -563    501       O
ATOM   4793  CB  HIS B 250     -52.622  29.717  31.706  1.00 40.25           C
ANISOU 4793  CB  HIS B 250     4812   4353   6129   -171   -703    472       C
ATOM   4794  CG  HIS B 250     -51.469  30.473  31.126  1.00 41.31           C
ANISOU 4794  CG  HIS B 250     4843   4500   6353   -207   -713    425       C
ATOM   4795  ND1 HIS B 250     -51.448  30.909  29.819  1.00 40.44           N
ANISOU 4795  ND1 HIS B 250     4706   4381   6276   -251   -606    374       N
ATOM   4796  CD2 HIS B 250     -50.300  30.878  31.677  1.00 40.74           C
ANISOU 4796  CD2 HIS B 250     4690   4446   6342   -220   -817    424       C
ATOM   4797  CE1 HIS B 250     -50.315  31.549  29.588  1.00 39.57           C
ANISOU 4797  CE1 HIS B 250     4504   4285   6246   -295   -619    341       C
ATOM   4798  NE2 HIS B 250     -49.601  31.543  30.699  1.00 41.76           N
ANISOU 4798  NE2 HIS B 250     4731   4581   6556   -274   -751    367       N
ATOM   4799  N   LEU B 251     -55.521  29.907  33.692  1.00 38.25           N
ANISOU 4799  N   LEU B 251     4835   4125   5572   -190   -647    508       N
ATOM   4800  CA  LEU B 251     -56.669  29.147  34.166  1.00 39.87           C
ANISOU 4800  CA  LEU B 251     5110   4321   5718   -191   -576    541       C
ATOM   4801  C   LEU B 251     -57.859  30.078  34.338  1.00 43.18           C
ANISOU 4801  C   LEU B 251     5567   4758   6081   -213   -489    480       C
ATOM   4802  O   LEU B 251     -57.728  31.152  34.935  1.00 49.28           O
ANISOU 4802  O   LEU B 251     6385   5550   6788   -229   -510    432       O
ATOM   4803  CB  LEU B 251     -56.360  28.433  35.482  1.00 40.85           C
ANISOU 4803  CB  LEU B 251     5329   4445   5748   -196   -645    617       C
ATOM   4804  CG  LEU B 251     -55.887  26.986  35.333  1.00 44.38           C
ANISOU 4804  CG  LEU B 251     5753   4837   6274   -160   -689    700       C
ATOM   4805  CD1 LEU B 251     -54.451  26.927  34.831  1.00 43.17           C
ANISOU 4805  CD1 LEU B 251     5484   4666   6252   -115   -792    700       C
ATOM   4806  CD2 LEU B 251     -56.044  26.231  36.643  1.00 51.87           C
ANISOU 4806  CD2 LEU B 251     6840   5768   7099   -181   -738    794       C
ATOM   4807  N   LEU B 252     -59.016  29.654  33.823  1.00 40.39           N
ANISOU 4807  N   LEU B 252     5186   4389   5770   -213   -397    476       N
ATOM   4808  CA  LEU B 252     -60.200  30.507  33.829  1.00 41.67           C
ANISOU 4808  CA  LEU B 252     5340   4557   5938   -217   -317    412       C
ATOM   4809  C   LEU B 252     -60.604  30.916  35.238  1.00 44.49           C
ANISOU 4809  C   LEU B 252     5789   4938   6178   -237   -259    384       C
ATOM   4810  O   LEU B 252     -61.115  32.025  35.438  1.00 47.33           O
ANISOU 4810  O   LEU B 252     6150   5294   6537   -229   -213    305       O
ATOM   4811  CB  LEU B 252     -61.361  29.794  33.136  1.00 38.31           C
ANISOU 4811  CB  LEU B 252     4851   4111   5595   -221   -246    422       C
ATOM   4812  CG  LEU B 252     -62.646  30.605  32.977  1.00 40.34           C
ANISOU 4812  CG  LEU B 252     5050   4362   5916   -212   -180    358       C
ATOM   4813  CD1 LEU B 252     -62.439  31.742  31.989  1.00 42.04           C
ANISOU 4813  CD1 LEU B 252     5227   4550   6196   -187   -256    321       C
ATOM   4814  CD2 LEU B 252     -63.794  29.715  32.544  1.00 41.44           C
ANISOU 4814  CD2 LEU B 252     5118   4488   6140   -233   -122    375       C
ATOM   4815  N   ILE B 253     -60.391  30.043  36.225  1.00 42.48           N
ANISOU 4815  N   ILE B 253     5627   4696   5816   -267   -257    445       N
ATOM   4816  CA  ILE B 253     -60.742  30.390  37.598  1.00 41.34           C
ANISOU 4816  CA  ILE B 253     5611   4577   5518   -310   -190    416       C
ATOM   4817  C   ILE B 253     -59.893  31.555  38.088  1.00 37.92           C
ANISOU 4817  C   ILE B 253     5242   4157   5007   -315   -277    361       C
ATOM   4818  O   ILE B 253     -60.354  32.378  38.887  1.00 36.99           O
ANISOU 4818  O   ILE B 253     5209   4049   4798   -340   -198    279       O
ATOM   4819  CB  ILE B 253     -60.614  29.152  38.511  1.00 40.82           C
ANISOU 4819  CB  ILE B 253     5666   4512   5331   -358   -195    517       C
ATOM   4820  CG1 ILE B 253     -61.133  29.463  39.916  1.00 47.22           C
ANISOU 4820  CG1 ILE B 253     6642   5351   5949   -428    -92    484       C
ATOM   4821  CG2 ILE B 253     -59.176  28.652  38.553  1.00 36.08           C
ANISOU 4821  CG2 ILE B 253     5091   3897   4719   -340   -385    603       C
ATOM   4822  CD1 ILE B 253     -61.137  28.268  40.843  1.00 50.06           C
ANISOU 4822  CD1 ILE B 253     7156   5702   6163   -498    -86    597       C
ATOM   4823  N   GLY B 254     -58.651  31.658  37.609  1.00 36.66           N
ANISOU 4823  N   GLY B 254     5040   3993   4895   -297   -428    392       N
ATOM   4824  CA  GLY B 254     -57.843  32.820  37.926  1.00 34.38           C
ANISOU 4824  CA  GLY B 254     4790   3711   4564   -315   -518    334       C
ATOM   4825  C   GLY B 254     -58.385  34.092  37.312  1.00 38.49           C
ANISOU 4825  C   GLY B 254     5258   4203   5164   -294   -453    233       C
ATOM   4826  O   GLY B 254     -58.283  35.166  37.910  1.00 44.37           O
ANISOU 4826  O   GLY B 254     6081   4937   5842   -318   -458    153       O
ATOM   4827  N   LEU B 255     -58.972  33.992  36.116  1.00 36.10           N
ANISOU 4827  N   LEU B 255     4839   3875   5003   -254   -405    237       N
ATOM   4828  CA  LEU B 255     -59.602  35.157  35.507  1.00 32.46           C
ANISOU 4828  CA  LEU B 255     4335   3369   4630   -227   -365    161       C
ATOM   4829  C   LEU B 255     -60.870  35.547  36.253  1.00 36.79           C
ANISOU 4829  C   LEU B 255     4916   3903   5158   -212   -227     83       C
ATOM   4830  O   LEU B 255     -61.155  36.738  36.424  1.00 39.11           O
ANISOU 4830  O   LEU B 255     5233   4152   5476   -194   -200     -8       O
ATOM   4831  CB  LEU B 255     -59.915  34.886  34.035  1.00 31.43           C
ANISOU 4831  CB  LEU B 255     4092   3213   4637   -200   -376    198       C
ATOM   4832  CG  LEU B 255     -58.799  34.923  32.988  1.00 35.72           C
ANISOU 4832  CG  LEU B 255     4596   3748   5227   -219   -470    238       C
ATOM   4833  CD1 LEU B 255     -57.922  33.684  33.054  1.00 34.35           C
ANISOU 4833  CD1 LEU B 255     4405   3613   5035   -230   -505    305       C
ATOM   4834  CD2 LEU B 255     -59.389  35.086  31.594  1.00 36.44           C
ANISOU 4834  CD2 LEU B 255     4630   3799   5419   -207   -469    248       C
ATOM   4835  N   ALA B 256     -61.644  34.556  36.702  1.00 38.73           N
ANISOU 4835  N   ALA B 256     5162   4181   5374   -221   -125    110       N
ATOM   4836  CA  ALA B 256     -62.880  34.849  37.420  1.00 40.60           C
ANISOU 4836  CA  ALA B 256     5409   4410   5608   -216     44     26       C
ATOM   4837  C   ALA B 256     -62.595  35.554  38.737  1.00 41.76           C
ANISOU 4837  C   ALA B 256     5717   4564   5586   -256     91    -56       C
ATOM   4838  O   ALA B 256     -63.362  36.427  39.162  1.00 46.35           O
ANISOU 4838  O   ALA B 256     6308   5110   6193   -235    217   -175       O
ATOM   4839  CB  ALA B 256     -63.667  33.560  37.656  1.00 42.72           C
ANISOU 4839  CB  ALA B 256     5652   4713   5868   -245    152     82       C
ATOM   4840  N   LYS B 257     -61.495  35.191  39.398  1.00 39.33           N
ANISOU 4840  N   LYS B 257     5539   4294   5111   -315    -16      0       N
ATOM   4841  CA  LYS B 257     -61.132  35.856  40.643  1.00 42.24           C
ANISOU 4841  CA  LYS B 257     6091   4669   5290   -373     -6    -76       C
ATOM   4842  C   LYS B 257     -60.751  37.310  40.397  1.00 46.17           C
ANISOU 4842  C   LYS B 257     6588   5109   5846   -350    -64   -177       C
ATOM   4843  O   LYS B 257     -61.172  38.203  41.140  1.00 48.60           O
ANISOU 4843  O   LYS B 257     6994   5384   6090   -364     40   -306       O
ATOM   4844  CB  LYS B 257     -59.988  35.104  41.321  1.00 40.87           C
ANISOU 4844  CB  LYS B 257     6045   4540   4944   -441   -162     27       C
ATOM   4845  CG  LYS B 257     -59.645  35.611  42.708  1.00 41.41           C
ANISOU 4845  CG  LYS B 257     6341   4623   4771   -528   -173    -36       C
ATOM   4846  CD  LYS B 257     -58.558  34.763  43.346  1.00 43.84           C
ANISOU 4846  CD  LYS B 257     6766   4968   4923   -591   -367     91       C
ATOM   4847  CE  LYS B 257     -58.285  35.205  44.774  1.00 51.83           C
ANISOU 4847  CE  LYS B 257     8042   5995   5657   -698   -394     35       C
ATOM   4848  NZ  LYS B 257     -59.501  35.098  45.627  1.00 58.53           N
ANISOU 4848  NZ  LYS B 257     9039   6853   6348   -752   -137    -37       N
ATOM   4849  N   ARG B 258     -59.961  37.566  39.352  1.00 46.96           N
ANISOU 4849  N   ARG B 258     6586   5187   6068   -324   -214   -127       N
ATOM   4850  CA  ARG B 258     -59.566  38.934  39.035  1.00 47.17           C
ANISOU 4850  CA  ARG B 258     6618   5145   6159   -317   -274   -207       C
ATOM   4851  C   ARG B 258     -60.748  39.765  38.554  1.00 45.83           C
ANISOU 4851  C   ARG B 258     6375   4893   6144   -240   -153   -297       C
ATOM   4852  O   ARG B 258     -60.801  40.973  38.813  1.00 47.35           O
ANISOU 4852  O   ARG B 258     6629   5007   6354   -233   -136   -406       O
ATOM   4853  CB  ARG B 258     -58.458  38.921  37.980  1.00 48.70           C
ANISOU 4853  CB  ARG B 258     6719   5337   6446   -324   -438   -123       C
ATOM   4854  CG  ARG B 258     -58.026  40.294  37.478  1.00 57.12           C
ANISOU 4854  CG  ARG B 258     7788   6323   7593   -334   -502   -184       C
ATOM   4855  CD  ARG B 258     -57.057  40.974  38.434  1.00 63.10           C
ANISOU 4855  CD  ARG B 258     8674   7077   8224   -417   -594   -244       C
ATOM   4856  NE  ARG B 258     -56.546  42.229  37.885  1.00 64.81           N
ANISOU 4856  NE  ARG B 258     8890   7206   8529   -444   -662   -290       N
ATOM   4857  CZ  ARG B 258     -55.606  42.971  38.461  1.00 69.27           C
ANISOU 4857  CZ  ARG B 258     9544   7751   9026   -530   -766   -343       C
ATOM   4858  NH1 ARG B 258     -55.066  42.588  39.610  1.00 71.79           N
ANISOU 4858  NH1 ARG B 258     9965   8135   9177   -595   -833   -354       N
ATOM   4859  NH2 ARG B 258     -55.203  44.098  37.889  1.00 70.52           N
ANISOU 4859  NH2 ARG B 258     9700   7816   9278   -564   -816   -380       N
ATOM   4860  N   PHE B 259     -61.710  39.139  37.873  1.00 48.35           N
ANISOU 4860  N   PHE B 259     6561   5217   6591   -182    -78   -255       N
ATOM   4861  CA  PHE B 259     -62.792  39.901  37.258  1.00 53.71           C
ANISOU 4861  CA  PHE B 259     7135   5809   7462    -98    -11   -320       C
ATOM   4862  C   PHE B 259     -63.735  40.484  38.303  1.00 56.46           C
ANISOU 4862  C   PHE B 259     7530   6119   7801    -73    175   -467       C
ATOM   4863  O   PHE B 259     -64.210  41.616  38.152  1.00 58.17           O
ANISOU 4863  O   PHE B 259     7721   6229   8151     -8    205   -565       O
ATOM   4864  CB  PHE B 259     -63.562  39.021  36.276  1.00 58.33           C
ANISOU 4864  CB  PHE B 259     7561   6413   8187    -56     -5   -235       C
ATOM   4865  CG  PHE B 259     -64.549  39.778  35.439  1.00 69.87           C
ANISOU 4865  CG  PHE B 259     8899   7779   9870     31     -6   -271       C
ATOM   4866  CD1 PHE B 259     -64.138  40.447  34.298  1.00 72.78           C
ANISOU 4866  CD1 PHE B 259     9248   8075  10328     49   -160   -222       C
ATOM   4867  CD2 PHE B 259     -65.886  39.827  35.796  1.00 76.77           C
ANISOU 4867  CD2 PHE B 259     9673   8628  10869     90    144   -351       C
ATOM   4868  CE1 PHE B 259     -65.042  41.149  33.526  1.00 74.98           C
ANISOU 4868  CE1 PHE B 259     9429   8250  10808    130   -197   -236       C
ATOM   4869  CE2 PHE B 259     -66.795  40.528  35.028  1.00 81.26           C
ANISOU 4869  CE2 PHE B 259    10106   9096  11674    182    112   -378       C
ATOM   4870  CZ  PHE B 259     -66.372  41.189  33.891  1.00 80.58           C
ANISOU 4870  CZ  PHE B 259    10020   8930  11665    205    -76   -312       C
ATOM   4871  N   LYS B 260     -64.026  39.728  39.365  1.00 58.05           N
ANISOU 4871  N   LYS B 260     7809   6397   7852   -126    312   -487       N
ATOM   4872  CA  LYS B 260     -64.904  40.239  40.412  1.00 65.76           C
ANISOU 4872  CA  LYS B 260     8846   7343   8796   -121    531   -644       C
ATOM   4873  C   LYS B 260     -64.297  41.448  41.111  1.00 71.19           C
ANISOU 4873  C   LYS B 260     9706   7966   9377   -147    513   -768       C
ATOM   4874  O   LYS B 260     -65.029  42.285  41.653  1.00 73.72           O
ANISOU 4874  O   LYS B 260    10051   8211   9748   -108    680   -930       O
ATOM   4875  CB  LYS B 260     -65.213  39.137  41.425  1.00 67.07           C
ANISOU 4875  CB  LYS B 260     9103   7608   8774   -206    681   -625       C
ATOM   4876  CG  LYS B 260     -66.326  38.203  40.989  1.00 70.63           C
ANISOU 4876  CG  LYS B 260     9374   8090   9374   -178    801   -576       C
ATOM   4877  CD  LYS B 260     -67.663  38.928  40.966  1.00 72.83           C
ANISOU 4877  CD  LYS B 260     9500   8296   9876    -92    997   -722       C
ATOM   4878  CE  LYS B 260     -68.704  38.147  40.182  1.00 71.36           C
ANISOU 4878  CE  LYS B 260     9075   8125   9914    -52   1042   -661       C
ATOM   4879  NZ  LYS B 260     -68.343  38.057  38.740  1.00 67.46           N
ANISOU 4879  NZ  LYS B 260     8458   7605   9569      5    794   -537       N
ATOM   4880  N   GLU B 261     -62.969  41.560  41.103  1.00 76.27           N
ANISOU 4880  N   GLU B 261    10459   8630   9890   -214    316   -704       N
ATOM   4881  CA  GLU B 261     -62.303  42.696  41.730  1.00 79.63           C
ANISOU 4881  CA  GLU B 261    11051   8991  10214   -260    270   -817       C
ATOM   4882  C   GLU B 261     -62.272  43.899  40.792  1.00 77.87           C
ANISOU 4882  C   GLU B 261    10745   8634  10208   -185    188   -856       C
ATOM   4883  O   GLU B 261     -62.874  44.940  41.076  1.00 84.38           O
ANISOU 4883  O   GLU B 261    11602   9343  11117   -133    296  -1007       O
ATOM   4884  CB  GLU B 261     -60.886  42.297  42.147  1.00 86.35           C
ANISOU 4884  CB  GLU B 261    12035   9919  10855   -374     77   -730       C
ATOM   4885  CG  GLU B 261     -60.819  40.959  42.867  1.00 95.13           C
ANISOU 4885  CG  GLU B 261    13221  11150  11774   -441    100   -639       C
ATOM   4886  CD  GLU B 261     -59.401  40.442  43.004  1.00100.82           C
ANISOU 4886  CD  GLU B 261    14005  11935  12366   -522   -140   -517       C
ATOM   4887  OE1 GLU B 261     -59.164  39.587  43.883  1.00103.67           O
ANISOU 4887  OE1 GLU B 261    14498  12369  12524   -596   -161   -458       O
ATOM   4888  OE2 GLU B 261     -58.526  40.889  42.233  1.00101.27           O
ANISOU 4888  OE2 GLU B 261    13978  11964  12537   -514   -308   -478       O
ATOM   4889  N   SER B 262     -61.570  43.772  39.669  1.00 65.71           N
ANISOU 4889  N   SER B 262     9109   7098   8760   -182      4   -723       N
ATOM   4890  CA  SER B 262     -61.476  44.825  38.673  1.00 62.05           C
ANISOU 4890  CA  SER B 262     8588   6507   8483   -132    -92   -725       C
ATOM   4891  C   SER B 262     -61.704  44.239  37.286  1.00 56.57           C
ANISOU 4891  C   SER B 262     7722   5829   7944    -80   -169   -580       C
ATOM   4892  O   SER B 262     -61.149  43.183  36.956  1.00 54.35           O
ANISOU 4892  O   SER B 262     7399   5657   7593   -126   -234   -461       O
ATOM   4893  CB  SER B 262     -60.108  45.520  38.726  1.00 63.97           C
ANISOU 4893  CB  SER B 262     8945   6721   8640   -230   -253   -722       C
ATOM   4894  OG  SER B 262     -59.060  44.593  38.502  1.00 65.16           O
ANISOU 4894  OG  SER B 262     9069   6993   8697   -307   -378   -591       O
ATOM   4895  N   PRO B 263     -62.506  44.897  36.456  1.00 57.44           N
ANISOU 4895  N   PRO B 263     7739   5822   8263     13   -174   -589       N
ATOM   4896  CA  PRO B 263     -62.812  44.351  35.129  1.00 57.02           C
ANISOU 4896  CA  PRO B 263     7548   5780   8336     50   -259   -456       C
ATOM   4897  C   PRO B 263     -61.623  44.465  34.185  1.00 52.99           C
ANISOU 4897  C   PRO B 263     7074   5271   7789    -28   -424   -345       C
ATOM   4898  O   PRO B 263     -60.631  45.145  34.452  1.00 53.62           O
ANISOU 4898  O   PRO B 263     7258   5320   7795   -101   -483   -372       O
ATOM   4899  CB  PRO B 263     -63.983  45.215  34.655  1.00 61.24           C
ANISOU 4899  CB  PRO B 263     7998   6166   9105    169   -244   -507       C
ATOM   4900  CG  PRO B 263     -63.786  46.514  35.364  1.00 63.17           C
ANISOU 4900  CG  PRO B 263     8364   6284   9354    178   -212   -642       C
ATOM   4901  CD  PRO B 263     -63.201  46.170  36.707  1.00 61.80           C
ANISOU 4901  CD  PRO B 263     8316   6213   8952     92   -110   -725       C
ATOM   4902  N   PHE B 264     -61.748  43.774  33.055  1.00 49.51           N
ANISOU 4902  N   PHE B 264     6543   4866   7402    -24   -488   -227       N
ATOM   4903  CA  PHE B 264     -60.737  43.797  32.006  1.00 44.98           C
ANISOU 4903  CA  PHE B 264     5994   4294   6801   -102   -608   -124       C
ATOM   4904  C   PHE B 264     -61.405  43.411  30.694  1.00 41.89           C
ANISOU 4904  C   PHE B 264     5527   3883   6506    -70   -667    -28       C
ATOM   4905  O   PHE B 264     -62.568  43.004  30.663  1.00 43.30           O
ANISOU 4905  O   PHE B 264     5614   4062   6777      8   -629    -35       O
ATOM   4906  CB  PHE B 264     -59.566  42.866  32.333  1.00 43.86           C
ANISOU 4906  CB  PHE B 264     5863   4287   6516   -190   -611    -85       C
ATOM   4907  CG  PHE B 264     -59.986  41.517  32.835  1.00 48.90           C
ANISOU 4907  CG  PHE B 264     6440   5039   7100   -164   -534    -68       C
ATOM   4908  CD1 PHE B 264     -60.321  40.506  31.950  1.00 49.74           C
ANISOU 4908  CD1 PHE B 264     6464   5192   7243   -152   -539     16       C
ATOM   4909  CD2 PHE B 264     -60.042  41.258  34.195  1.00 53.89           C
ANISOU 4909  CD2 PHE B 264     7122   5724   7631   -166   -458   -135       C
ATOM   4910  CE1 PHE B 264     -60.707  39.263  32.412  1.00 53.13           C
ANISOU 4910  CE1 PHE B 264     6848   5708   7631   -138   -469     35       C
ATOM   4911  CE2 PHE B 264     -60.426  40.017  34.663  1.00 57.25           C
ANISOU 4911  CE2 PHE B 264     7514   6240   7998   -158   -386   -105       C
ATOM   4912  CZ  PHE B 264     -60.760  39.018  33.771  1.00 57.12           C
ANISOU 4912  CZ  PHE B 264     7402   6260   8041   -141   -392    -19       C
ATOM   4913  N   GLU B 265     -60.650  43.540  29.608  1.00 39.55           N
ANISOU 4913  N   GLU B 265     5274   3569   6184   -146   -758     59       N
ATOM   4914  CA  GLU B 265     -61.173  43.354  28.262  1.00 42.46           C
ANISOU 4914  CA  GLU B 265     5623   3900   6610   -143   -839    154       C
ATOM   4915  C   GLU B 265     -60.647  42.052  27.677  1.00 41.38           C
ANISOU 4915  C   GLU B 265     5457   3887   6380   -209   -819    219       C
ATOM   4916  O   GLU B 265     -59.436  41.805  27.688  1.00 38.39           O
ANISOU 4916  O   GLU B 265     5108   3568   5910   -292   -795    229       O
ATOM   4917  CB  GLU B 265     -60.788  44.531  27.362  1.00 48.45           C
ANISOU 4917  CB  GLU B 265     6492   4525   7392   -196   -947    206       C
ATOM   4918  CG  GLU B 265     -61.791  44.826  26.258  1.00 57.00           C
ANISOU 4918  CG  GLU B 265     7580   5503   8574   -152  -1069    284       C
ATOM   4919  CD  GLU B 265     -63.073  45.445  26.784  1.00 68.98           C
ANISOU 4919  CD  GLU B 265     9022   6912  10275     -9  -1088    222       C
ATOM   4920  OE1 GLU B 265     -63.084  45.910  27.944  1.00 72.77           O
ANISOU 4920  OE1 GLU B 265     9488   7372  10788     42   -995    110       O
ATOM   4921  OE2 GLU B 265     -64.073  45.469  26.035  1.00 74.90           O
ANISOU 4921  OE2 GLU B 265     9724   7594  11142     51  -1198    281       O
ATOM   4922  N   LEU B 266     -61.558  41.226  27.168  1.00 46.66           N
ANISOU 4922  N   LEU B 266     6057   4582   7088   -171   -830    256       N
ATOM   4923  CA  LEU B 266     -61.221  39.977  26.496  1.00 47.17           C
ANISOU 4923  CA  LEU B 266     6105   4738   7078   -228   -812    309       C
ATOM   4924  C   LEU B 266     -61.610  40.090  25.030  1.00 47.14           C
ANISOU 4924  C   LEU B 266     6156   4674   7081   -269   -921    388       C
ATOM   4925  O   LEU B 266     -62.791  40.260  24.709  1.00 58.41           O
ANISOU 4925  O   LEU B 266     7543   6042   8608   -211  -1003    406       O
ATOM   4926  CB  LEU B 266     -61.937  38.790  27.136  1.00 55.74           C
ANISOU 4926  CB  LEU B 266     7089   5905   8184   -177   -737    286       C
ATOM   4927  CG  LEU B 266     -61.582  38.402  28.566  1.00 64.20           C
ANISOU 4927  CG  LEU B 266     8137   7048   9208   -156   -633    228       C
ATOM   4928  CD1 LEU B 266     -62.435  37.221  28.989  1.00 70.47           C
ANISOU 4928  CD1 LEU B 266     8851   7902  10024   -125   -562    226       C
ATOM   4929  CD2 LEU B 266     -60.110  38.065  28.676  1.00 63.61           C
ANISOU 4929  CD2 LEU B 266     8104   7031   9033   -224   -621    242       C
ATOM   4930  N   GLU B 267     -60.624  39.986  24.147  1.00 39.62           N
ANISOU 4930  N   GLU B 267     5294   3735   6024   -376   -921    432       N
ATOM   4931  CA  GLU B 267     -60.848  40.008  22.707  1.00 43.19           C
ANISOU 4931  CA  GLU B 267     5846   4139   6427   -448  -1013    508       C
ATOM   4932  C   GLU B 267     -60.641  38.591  22.185  1.00 39.15           C
ANISOU 4932  C   GLU B 267     5319   3719   5836   -499   -948    510       C
ATOM   4933  O   GLU B 267     -59.512  38.090  22.158  1.00 38.64           O
ANISOU 4933  O   GLU B 267     5265   3718   5699   -560   -840    487       O
ATOM   4934  CB  GLU B 267     -59.913  41.005  22.022  1.00 53.38           C
ANISOU 4934  CB  GLU B 267     7279   5362   7641   -555  -1036    549       C
ATOM   4935  CG  GLU B 267     -60.498  41.667  20.779  1.00 65.05           C
ANISOU 4935  CG  GLU B 267     8899   6726   9091   -607  -1189    643       C
ATOM   4936  CD  GLU B 267     -60.421  40.785  19.549  1.00 76.69           C
ANISOU 4936  CD  GLU B 267    10466   8243  10429   -713  -1192    688       C
ATOM   4937  OE1 GLU B 267     -59.668  39.791  19.579  1.00 81.19           O
ANISOU 4937  OE1 GLU B 267    11000   8919  10931   -758  -1047    640       O
ATOM   4938  OE2 GLU B 267     -61.110  41.088  18.552  1.00 79.65           O
ANISOU 4938  OE2 GLU B 267    10958   8537  10768   -752  -1347    770       O
ATOM   4939  N   ASP B 268     -61.737  37.945  21.785  1.00 38.54           N
ANISOU 4939  N   ASP B 268     5208   3641   5793   -471  -1016    530       N
ATOM   4940  CA  ASP B 268     -61.707  36.567  21.293  1.00 35.01           C
ANISOU 4940  CA  ASP B 268     4757   3262   5284   -517   -964    523       C
ATOM   4941  C   ASP B 268     -61.562  36.607  19.775  1.00 31.20           C
ANISOU 4941  C   ASP B 268     4440   2739   4675   -639  -1034    575       C
ATOM   4942  O   ASP B 268     -62.529  36.505  19.019  1.00 34.03           O
ANISOU 4942  O   ASP B 268     4842   3056   5033   -658  -1172    619       O
ATOM   4943  CB  ASP B 268     -62.966  35.827  21.733  1.00 41.33           C
ANISOU 4943  CB  ASP B 268     5433   4081   6190   -443   -995    509       C
ATOM   4944  CG  ASP B 268     -62.942  34.357  21.369  1.00 47.00           C
ANISOU 4944  CG  ASP B 268     6147   4855   6857   -490   -935    493       C
ATOM   4945  OD1 ASP B 268     -61.875  33.851  20.957  1.00 50.75           O
ANISOU 4945  OD1 ASP B 268     6695   5360   7229   -557   -844    476       O
ATOM   4946  OD2 ASP B 268     -63.999  33.704  21.497  1.00 47.97           O
ANISOU 4946  OD2 ASP B 268     6184   4983   7059   -462   -973    490       O
ATOM   4947  N   PHE B 269     -60.314  36.756  19.322  1.00 30.99           N
ANISOU 4947  N   PHE B 269     4512   2727   4537   -734   -935    568       N
ATOM   4948  CA  PHE B 269     -60.065  36.940  17.896  1.00 33.90           C
ANISOU 4948  CA  PHE B 269     5075   3054   4752   -874   -972    614       C
ATOM   4949  C   PHE B 269     -60.267  35.667  17.085  1.00 37.39           C
ANISOU 4949  C   PHE B 269     5573   3532   5102   -939   -941    589       C
ATOM   4950  O   PHE B 269     -60.205  35.727  15.852  1.00 40.56           O
ANISOU 4950  O   PHE B 269     6164   3899   5347  -1069   -978    622       O
ATOM   4951  CB  PHE B 269     -58.656  37.503  17.658  1.00 37.11           C
ANISOU 4951  CB  PHE B 269     5560   3464   5075   -974   -841    603       C
ATOM   4952  CG  PHE B 269     -57.558  36.774  18.388  1.00 40.85           C
ANISOU 4952  CG  PHE B 269     5899   4026   5596   -948   -652    518       C
ATOM   4953  CD1 PHE B 269     -56.803  35.808  17.744  1.00 41.91           C
ANISOU 4953  CD1 PHE B 269     6062   4206   5655  -1025   -502    466       C
ATOM   4954  CD2 PHE B 269     -57.257  37.080  19.707  1.00 42.37           C
ANISOU 4954  CD2 PHE B 269     5944   4245   5910   -850   -632    489       C
ATOM   4955  CE1 PHE B 269     -55.784  35.145  18.406  1.00 42.06           C
ANISOU 4955  CE1 PHE B 269     5937   4289   5753   -986   -349    394       C
ATOM   4956  CE2 PHE B 269     -56.241  36.420  20.376  1.00 42.58           C
ANISOU 4956  CE2 PHE B 269     5850   4344   5986   -827   -499    427       C
ATOM   4957  CZ  PHE B 269     -55.503  35.451  19.723  1.00 40.79           C
ANISOU 4957  CZ  PHE B 269     5626   4155   5717   -887   -365    383       C
ATOM   4958  N   ILE B 270     -60.506  34.530  17.732  1.00 38.04           N
ANISOU 4958  N   ILE B 270     5517   3672   5263   -865   -874    532       N
ATOM   4959  CA  ILE B 270     -60.914  33.314  17.034  1.00 36.06           C
ANISOU 4959  CA  ILE B 270     5316   3436   4951   -918   -870    504       C
ATOM   4960  C   ILE B 270     -62.199  32.817  17.686  1.00 33.32           C
ANISOU 4960  C   ILE B 270     4826   3093   4743   -823   -971    511       C
ATOM   4961  O   ILE B 270     -62.163  31.851  18.463  1.00 31.65           O
ANISOU 4961  O   ILE B 270     4494   2924   4606   -763   -871    462       O
ATOM   4962  CB  ILE B 270     -59.818  32.238  17.069  1.00 41.04           C
ANISOU 4962  CB  ILE B 270     5927   4115   5550   -941   -659    419       C
ATOM   4963  CG1 ILE B 270     -58.455  32.842  16.728  1.00 44.55           C
ANISOU 4963  CG1 ILE B 270     6440   4567   5920  -1015   -524    400       C
ATOM   4964  CG2 ILE B 270     -60.142  31.122  16.089  1.00 37.58           C
ANISOU 4964  CG2 ILE B 270     5599   3664   5014  -1027   -648    380       C
ATOM   4965  CD1 ILE B 270     -57.317  31.844  16.761  1.00 47.41           C
ANISOU 4965  CD1 ILE B 270     6749   4968   6298  -1022   -312    308       C
ATOM   4966  N   PRO B 271     -63.348  33.444  17.413  1.00 37.30           N
ANISOU 4966  N   PRO B 271     5331   3544   5298   -808  -1169    572       N
ATOM   4967  CA  PRO B 271     -64.584  33.057  18.108  1.00 35.60           C
ANISOU 4967  CA  PRO B 271     4941   3335   5252   -718  -1243    569       C
ATOM   4968  C   PRO B 271     -65.081  31.679  17.702  1.00 37.22           C
ANISOU 4968  C   PRO B 271     5143   3560   5439   -775  -1242    536       C
ATOM   4969  O   PRO B 271     -65.819  31.531  16.723  1.00 41.12           O
ANISOU 4969  O   PRO B 271     5717   4016   5890   -853  -1405    566       O
ATOM   4970  CB  PRO B 271     -65.573  34.156  17.700  1.00 34.35           C
ANISOU 4970  CB  PRO B 271     4787   3097   5166   -696  -1469    643       C
ATOM   4971  CG  PRO B 271     -65.068  34.639  16.387  1.00 35.19           C
ANISOU 4971  CG  PRO B 271     5135   3156   5082   -825  -1556    698       C
ATOM   4972  CD  PRO B 271     -63.570  34.542  16.457  1.00 35.15           C
ANISOU 4972  CD  PRO B 271     5215   3196   4946   -876  -1337    652       C
ATOM   4973  N   MET B 272     -64.678  30.662  18.459  1.00 36.36           N
ANISOU 4973  N   MET B 272     4952   3500   5364   -741  -1075    478       N
ATOM   4974  CA  MET B 272     -65.077  29.291  18.182  1.00 35.06           C
ANISOU 4974  CA  MET B 272     4787   3338   5196   -793  -1054    440       C
ATOM   4975  C   MET B 272     -64.922  28.473  19.453  1.00 31.81           C
ANISOU 4975  C   MET B 272     4237   2964   4887   -713   -903    407       C
ATOM   4976  O   MET B 272     -64.243  28.882  20.399  1.00 35.80           O
ANISOU 4976  O   MET B 272     4684   3500   5420   -635   -805    406       O
ATOM   4977  CB  MET B 272     -64.247  28.679  17.051  1.00 33.76           C
ANISOU 4977  CB  MET B 272     4816   3158   4853   -910   -991    398       C
ATOM   4978  CG  MET B 272     -62.768  28.580  17.376  1.00 39.81           C
ANISOU 4978  CG  MET B 272     5602   3951   5572   -885   -788    353       C
ATOM   4979  SD  MET B 272     -61.865  27.569  16.193  1.00 48.21           S
ANISOU 4979  SD  MET B 272     6850   4990   6479  -1006   -650    265       S
ATOM   4980  CE  MET B 272     -62.709  25.999  16.372  1.00 48.29           C
ANISOU 4980  CE  MET B 272     6809   4970   6569  -1007   -658    222       C
ATOM   4981  N   ASP B 273     -65.560  27.308  19.460  1.00 33.11           N
ANISOU 4981  N   ASP B 273     4364   3118   5098   -746   -897    385       N
ATOM   4982  CA  ASP B 273     -65.455  26.390  20.586  1.00 37.62           C
ANISOU 4982  CA  ASP B 273     4838   3706   5749   -693   -763    368       C
ATOM   4983  C   ASP B 273     -64.165  25.589  20.458  1.00 35.88           C
ANISOU 4983  C   ASP B 273     4709   3473   5450   -701   -626    326       C
ATOM   4984  O   ASP B 273     -63.945  24.914  19.446  1.00 34.83           O
ANISOU 4984  O   ASP B 273     4694   3301   5241   -782   -618    282       O
ATOM   4985  CB  ASP B 273     -66.668  25.462  20.631  1.00 41.65           C
ANISOU 4985  CB  ASP B 273     5274   4195   6355   -739   -809    365       C
ATOM   4986  CG  ASP B 273     -66.910  24.886  22.012  1.00 42.35           C
ANISOU 4986  CG  ASP B 273     5242   4302   6545   -683   -691    374       C
ATOM   4987  OD1 ASP B 273     -66.337  25.417  22.988  1.00 43.67           O
ANISOU 4987  OD1 ASP B 273     5376   4506   6712   -600   -608    389       O
ATOM   4988  OD2 ASP B 273     -67.672  23.902  22.122  1.00 40.43           O
ANISOU 4988  OD2 ASP B 273     4954   4034   6372   -737   -683    369       O
ATOM   4989  N   SER B 274     -63.308  25.671  21.473  1.00 28.14           N
ANISOU 4989  N   SER B 274     3676   2519   4496   -618   -522    332       N
ATOM   4990  CA  SER B 274     -62.065  24.917  21.474  1.00 38.55           C
ANISOU 4990  CA  SER B 274     5039   3818   5792   -602   -402    295       C
ATOM   4991  C   SER B 274     -61.640  24.657  22.911  1.00 31.75           C
ANISOU 4991  C   SER B 274     4088   2974   5001   -510   -341    327       C
ATOM   4992  O   SER B 274     -61.987  25.412  23.823  1.00 29.25           O
ANISOU 4992  O   SER B 274     3705   2702   4707   -465   -368    366       O
ATOM   4993  CB  SER B 274     -60.955  25.649  20.708  1.00 43.25           C
ANISOU 4993  CB  SER B 274     5708   4424   6302   -626   -366    265       C
ATOM   4994  OG  SER B 274     -60.712  26.933  21.251  1.00 50.57           O
ANISOU 4994  OG  SER B 274     6587   5396   7230   -582   -400    303       O
ATOM   4995  N   THR B 275     -60.886  23.570  23.100  1.00 31.31           N
ANISOU 4995  N   THR B 275     4044   2873   4978   -485   -262    310       N
ATOM   4996  CA  THR B 275     -60.440  23.192  24.438  1.00 31.57           C
ANISOU 4996  CA  THR B 275     4019   2908   5067   -405   -232    356       C
ATOM   4997  C   THR B 275     -59.566  24.276  25.058  1.00 31.73           C
ANISOU 4997  C   THR B 275     3996   2989   5071   -350   -244    373       C
ATOM   4998  O   THR B 275     -59.706  24.593  26.246  1.00 34.70           O
ANISOU 4998  O   THR B 275     4337   3399   5447   -310   -266    420       O
ATOM   4999  CB  THR B 275     -59.693  21.857  24.380  1.00 34.88           C
ANISOU 4999  CB  THR B 275     4463   3243   5548   -378   -169    337       C
ATOM   5000  OG1 THR B 275     -60.594  20.822  23.966  1.00 35.36           O
ANISOU 5000  OG1 THR B 275     4572   3235   5626   -439   -163    323       O
ATOM   5001  CG2 THR B 275     -59.111  21.498  25.740  1.00 33.10           C
ANISOU 5001  CG2 THR B 275     4194   3007   5374   -296   -174    404       C
ATOM   5002  N   VAL B 276     -58.665  24.861  24.273  1.00 32.64           N
ANISOU 5002  N   VAL B 276     4123   3115   5162   -364   -222    329       N
ATOM   5003  CA  VAL B 276     -57.835  25.980  24.706  1.00 33.39           C
ANISOU 5003  CA  VAL B 276     4176   3262   5247   -336   -238    336       C
ATOM   5004  C   VAL B 276     -58.267  27.219  23.935  1.00 32.44           C
ANISOU 5004  C   VAL B 276     4101   3168   5056   -395   -278    326       C
ATOM   5005  O   VAL B 276     -58.407  27.176  22.706  1.00 31.39           O
ANISOU 5005  O   VAL B 276     4041   3011   4873   -465   -264    294       O
ATOM   5006  CB  VAL B 276     -56.338  25.694  24.496  1.00 34.09           C
ANISOU 5006  CB  VAL B 276     4223   3336   5396   -310   -174    299       C
ATOM   5007  CG1 VAL B 276     -55.507  26.915  24.866  1.00 37.71           C
ANISOU 5007  CG1 VAL B 276     4631   3848   5850   -306   -200    303       C
ATOM   5008  CG2 VAL B 276     -55.909  24.490  25.317  1.00 32.26           C
ANISOU 5008  CG2 VAL B 276     3944   3056   5257   -234   -170    325       C
ATOM   5009  N   LYS B 277     -58.481  28.317  24.654  1.00 32.95           N
ANISOU 5009  N   LYS B 277     4140   3270   5110   -372   -333    353       N
ATOM   5010  CA  LYS B 277     -58.909  29.577  24.065  1.00 35.97           C
ANISOU 5010  CA  LYS B 277     4565   3655   5448   -413   -390    356       C
ATOM   5011  C   LYS B 277     -57.788  30.604  24.147  1.00 36.75           C
ANISOU 5011  C   LYS B 277     4661   3771   5532   -424   -381    346       C
ATOM   5012  O   LYS B 277     -57.103  30.712  25.170  1.00 40.02           O
ANISOU 5012  O   LYS B 277     5016   4211   5978   -379   -376    348       O
ATOM   5013  CB  LYS B 277     -60.159  30.115  24.768  1.00 34.03           C
ANISOU 5013  CB  LYS B 277     4286   3414   5228   -377   -453    380       C
ATOM   5014  CG  LYS B 277     -61.412  29.292  24.529  1.00 30.74           C
ANISOU 5014  CG  LYS B 277     3855   2979   4845   -389   -472    388       C
ATOM   5015  CD  LYS B 277     -61.824  29.330  23.068  1.00 30.68           C
ANISOU 5015  CD  LYS B 277     3920   2938   4801   -463   -536    384       C
ATOM   5016  CE  LYS B 277     -62.108  30.750  22.604  1.00 29.86           C
ANISOU 5016  CE  LYS B 277     3848   2815   4682   -474   -632    404       C
ATOM   5017  NZ  LYS B 277     -62.519  30.789  21.172  1.00 29.75           N
ANISOU 5017  NZ  LYS B 277     3936   2762   4606   -560   -724    418       N
ATOM   5018  N   ASN B 278     -57.606  31.355  23.066  1.00 34.31           N
ANISOU 5018  N   ASN B 278     4427   3442   5168   -498   -390    340       N
ATOM   5019  CA  ASN B 278     -56.617  32.421  22.994  1.00 38.77           C
ANISOU 5019  CA  ASN B 278     5000   4011   5718   -536   -376    334       C
ATOM   5020  C   ASN B 278     -57.330  33.765  23.014  1.00 42.11           C
ANISOU 5020  C   ASN B 278     5477   4403   6120   -544   -475    366       C
ATOM   5021  O   ASN B 278     -58.263  33.989  22.234  1.00 42.94           O
ANISOU 5021  O   ASN B 278     5657   4468   6191   -572   -544    394       O
ATOM   5022  CB  ASN B 278     -55.761  32.292  21.733  1.00 46.61           C
ANISOU 5022  CB  ASN B 278     6057   4993   6659   -634   -284    304       C
ATOM   5023  CG  ASN B 278     -54.856  31.077  21.765  1.00 54.77           C
ANISOU 5023  CG  ASN B 278     7012   6042   7755   -611   -168    253       C
ATOM   5024  OD1 ASN B 278     -54.253  30.764  22.793  1.00 57.75           O
ANISOU 5024  OD1 ASN B 278     7273   6443   8226   -537   -166    250       O
ATOM   5025  ND2 ASN B 278     -54.759  30.382  20.639  1.00 58.46           N
ANISOU 5025  ND2 ASN B 278     7554   6486   8173   -674    -78    210       N
ATOM   5026  N   TYR B 279     -56.889  34.656  23.901  1.00 43.55           N
ANISOU 5026  N   TYR B 279     5624   4591   6332   -519   -496    362       N
ATOM   5027  CA  TYR B 279     -57.520  35.955  24.077  1.00 39.72           C
ANISOU 5027  CA  TYR B 279     5184   4054   5852   -509   -582    379       C
ATOM   5028  C   TYR B 279     -56.481  37.065  24.038  1.00 36.52           C
ANISOU 5028  C   TYR B 279     4813   3627   5435   -574   -578    373       C
ATOM   5029  O   TYR B 279     -55.349  36.890  24.502  1.00 32.46           O
ANISOU 5029  O   TYR B 279     4237   3157   4940   -592   -524    345       O
ATOM   5030  CB  TYR B 279     -58.285  36.039  25.406  1.00 37.78           C
ANISOU 5030  CB  TYR B 279     4876   3820   5660   -412   -607    361       C
ATOM   5031  CG  TYR B 279     -59.434  35.068  25.538  1.00 39.40           C
ANISOU 5031  CG  TYR B 279     5035   4040   5894   -360   -603    368       C
ATOM   5032  CD1 TYR B 279     -60.589  35.221  24.784  1.00 41.65           C
ANISOU 5032  CD1 TYR B 279     5337   4279   6208   -359   -671    392       C
ATOM   5033  CD2 TYR B 279     -59.371  34.009  26.433  1.00 39.64           C
ANISOU 5033  CD2 TYR B 279     5007   4124   5931   -322   -544    357       C
ATOM   5034  CE1 TYR B 279     -61.645  34.336  24.908  1.00 43.58           C
ANISOU 5034  CE1 TYR B 279     5520   4538   6500   -326   -669    393       C
ATOM   5035  CE2 TYR B 279     -60.420  33.122  26.566  1.00 38.17           C
ANISOU 5035  CE2 TYR B 279     4782   3945   5775   -294   -528    366       C
ATOM   5036  CZ  TYR B 279     -61.554  33.289  25.801  1.00 40.18           C
ANISOU 5036  CZ  TYR B 279     5034   4161   6072   -299   -585    378       C
ATOM   5037  OH  TYR B 279     -62.602  32.406  25.929  1.00 46.50           O
ANISOU 5037  OH  TYR B 279     5777   4970   6923   -286   -570    382       O
ATOM   5038  N   PHE B 280     -56.880  38.204  23.480  1.00 38.40           N
ANISOU 5038  N   PHE B 280     5148   3787   5657   -611   -650    404       N
ATOM   5039  CA  PHE B 280     -56.143  39.455  23.614  1.00 35.36           C
ANISOU 5039  CA  PHE B 280     4807   3353   5274   -669   -666    401       C
ATOM   5040  C   PHE B 280     -56.688  40.153  24.855  1.00 36.15           C
ANISOU 5040  C   PHE B 280     4876   3422   5437   -579   -722    368       C
ATOM   5041  O   PHE B 280     -57.822  40.643  24.852  1.00 37.25           O
ANISOU 5041  O   PHE B 280     5044   3492   5617   -516   -794    380       O
ATOM   5042  CB  PHE B 280     -56.306  40.309  22.358  1.00 37.29           C
ANISOU 5042  CB  PHE B 280     5201   3505   5462   -763   -718    462       C
ATOM   5043  CG  PHE B 280     -55.276  41.404  22.208  1.00 41.47           C
ANISOU 5043  CG  PHE B 280     5794   3986   5977   -872   -699    467       C
ATOM   5044  CD1 PHE B 280     -54.698  42.010  23.314  1.00 43.15           C
ANISOU 5044  CD1 PHE B 280     5941   4200   6253   -854   -699    418       C
ATOM   5045  CD2 PHE B 280     -54.894  41.833  20.947  1.00 42.54           C
ANISOU 5045  CD2 PHE B 280     6069   4070   6023  -1011   -680    522       C
ATOM   5046  CE1 PHE B 280     -53.760  43.017  23.164  1.00 40.54           C
ANISOU 5046  CE1 PHE B 280     5664   3817   5922   -970   -686    420       C
ATOM   5047  CE2 PHE B 280     -53.955  42.838  20.791  1.00 39.10           C
ANISOU 5047  CE2 PHE B 280     5694   3583   5578  -1132   -649    531       C
ATOM   5048  CZ  PHE B 280     -53.388  43.431  21.901  1.00 39.53           C
ANISOU 5048  CZ  PHE B 280     5661   3636   5721  -1110   -654    479       C
ATOM   5049  N   ILE B 281     -55.888  40.190  25.917  1.00 40.02           N
ANISOU 5049  N   ILE B 281     5306   3959   5941   -573   -693    319       N
ATOM   5050  CA  ILE B 281     -56.331  40.653  27.226  1.00 40.89           C
ANISOU 5050  CA  ILE B 281     5402   4056   6078   -498   -720    268       C
ATOM   5051  C   ILE B 281     -55.725  42.019  27.512  1.00 37.37           C
ANISOU 5051  C   ILE B 281     5020   3536   5644   -556   -761    238       C
ATOM   5052  O   ILE B 281     -54.547  42.259  27.226  1.00 37.28           O
ANISOU 5052  O   ILE B 281     5006   3536   5622   -656   -750    244       O
ATOM   5053  CB  ILE B 281     -55.956  39.642  28.327  1.00 45.23           C
ANISOU 5053  CB  ILE B 281     5872   4707   6608   -458   -683    238       C
ATOM   5054  CG1 ILE B 281     -56.603  38.287  28.039  1.00 54.68           C
ANISOU 5054  CG1 ILE B 281     7018   5956   7803   -408   -641    269       C
ATOM   5055  CG2 ILE B 281     -56.379  40.150  29.696  1.00 45.07           C
ANISOU 5055  CG2 ILE B 281     5876   4675   6575   -406   -696    177       C
ATOM   5056  CD1 ILE B 281     -56.453  37.286  29.161  1.00 61.07           C
ANISOU 5056  CD1 ILE B 281     7775   6839   8590   -363   -616    258       C
ATOM   5057  N   THR B 282     -56.538  42.914  28.074  1.00 34.99           N
ANISOU 5057  N   THR B 282     4769   3149   5379   -495   -798    199       N
ATOM   5058  CA  THR B 282     -56.095  44.233  28.514  1.00 36.32           C
ANISOU 5058  CA  THR B 282     5012   3224   5564   -540   -838    153       C
ATOM   5059  C   THR B 282     -56.670  44.483  29.902  1.00 38.29           C
ANISOU 5059  C   THR B 282     5267   3465   5817   -457   -821     58       C
ATOM   5060  O   THR B 282     -57.887  44.624  30.054  1.00 39.63           O
ANISOU 5060  O   THR B 282     5434   3581   6042   -356   -806     33       O
ATOM   5061  CB  THR B 282     -56.537  45.328  27.541  1.00 36.39           C
ANISOU 5061  CB  THR B 282     5120   3082   5623   -560   -900    200       C
ATOM   5062  OG1 THR B 282     -55.992  45.068  26.242  1.00 39.60           O
ANISOU 5062  OG1 THR B 282     5555   3502   5988   -661   -899    287       O
ATOM   5063  CG2 THR B 282     -56.058  46.690  28.021  1.00 32.87           C
ANISOU 5063  CG2 THR B 282     4764   2521   5206   -612   -939    148       C
ATOM   5064  N   ASP B 283     -55.802  44.535  30.910  1.00 37.95           N
ANISOU 5064  N   ASP B 283     5231   3472   5716   -506   -824      1       N
ATOM   5065  CA  ASP B 283     -56.241  44.805  32.272  1.00 35.60           C
ANISOU 5065  CA  ASP B 283     4980   3168   5380   -456   -799    -99       C
ATOM   5066  C   ASP B 283     -56.518  46.293  32.439  1.00 39.71           C
ANISOU 5066  C   ASP B 283     5604   3528   5954   -456   -822   -173       C
ATOM   5067  O   ASP B 283     -55.650  47.129  32.169  1.00 43.63           O
ANISOU 5067  O   ASP B 283     6156   3960   6464   -554   -884   -172       O
ATOM   5068  CB  ASP B 283     -55.192  44.341  33.280  1.00 38.66           C
ANISOU 5068  CB  ASP B 283     5364   3657   5667   -522   -828   -126       C
ATOM   5069  CG  ASP B 283     -55.620  44.581  34.714  1.00 45.73           C
ANISOU 5069  CG  ASP B 283     6350   4550   6476   -494   -799   -232       C
ATOM   5070  OD1 ASP B 283     -56.608  43.955  35.155  1.00 46.65           O
ANISOU 5070  OD1 ASP B 283     6459   4703   6564   -413   -713   -248       O
ATOM   5071  OD2 ASP B 283     -54.970  45.396  35.402  1.00 48.85           O
ANISOU 5071  OD2 ASP B 283     6832   4905   6824   -568   -855   -304       O
ATOM   5072  N   ALA B 284     -57.729  46.620  32.891  1.00 43.73           N
ANISOU 5072  N   ALA B 284     6134   3968   6513   -348   -765   -244       N
ATOM   5073  CA  ALA B 284     -58.157  48.013  32.943  1.00 43.73           C
ANISOU 5073  CA  ALA B 284     6222   3787   6606   -318   -781   -317       C
ATOM   5074  C   ALA B 284     -57.529  48.776  34.103  1.00 48.79           C
ANISOU 5074  C   ALA B 284     6978   4388   7170   -383   -779   -442       C
ATOM   5075  O   ALA B 284     -57.349  49.995  34.008  1.00 53.21           O
ANISOU 5075  O   ALA B 284     7633   4791   7792   -414   -824   -488       O
ATOM   5076  CB  ALA B 284     -59.681  48.088  33.036  1.00 44.42           C
ANISOU 5076  CB  ALA B 284     6260   3803   6812   -167   -708   -365       C
ATOM   5077  N   GLN B 285     -57.190  48.091  35.196  1.00 47.31           N
ANISOU 5077  N   GLN B 285     6804   4330   6841   -415   -741   -494       N
ATOM   5078  CA  GLN B 285     -56.690  48.796  36.370  1.00 49.72           C
ANISOU 5078  CA  GLN B 285     7245   4599   7047   -485   -751   -623       C
ATOM   5079  C   GLN B 285     -55.223  49.179  36.221  1.00 46.81           C
ANISOU 5079  C   GLN B 285     6903   4237   6644   -638   -883   -590       C
ATOM   5080  O   GLN B 285     -54.834  50.300  36.566  1.00 48.09           O
ANISOU 5080  O   GLN B 285     7180   4281   6813   -708   -928   -678       O
ATOM   5081  CB  GLN B 285     -56.889  47.941  37.622  1.00 53.54           C
ANISOU 5081  CB  GLN B 285     7764   5211   7367   -479   -678   -682       C
ATOM   5082  CG  GLN B 285     -56.626  48.681  38.926  1.00 61.21           C
ANISOU 5082  CG  GLN B 285     8915   6136   8206   -548   -670   -838       C
ATOM   5083  CD  GLN B 285     -57.664  49.752  39.211  1.00 72.03           C
ANISOU 5083  CD  GLN B 285    10369   7337   9664   -464   -547   -989       C
ATOM   5084  OE1 GLN B 285     -57.623  50.844  38.641  1.00 71.90           O
ANISOU 5084  OE1 GLN B 285    10378   7157   9785   -457   -592  -1014       O
ATOM   5085  NE2 GLN B 285     -58.603  49.442  40.097  1.00 78.94           N
ANISOU 5085  NE2 GLN B 285    11287   8238  10468   -400   -382  -1092       N
ATOM   5086  N   THR B 286     -54.398  48.268  35.708  1.00 47.74           N
ANISOU 5086  N   THR B 286     6908   4485   6744   -693   -941   -474       N
ATOM   5087  CA  THR B 286     -52.956  48.478  35.654  1.00 49.31           C
ANISOU 5087  CA  THR B 286     7089   4715   6932   -840  -1054   -448       C
ATOM   5088  C   THR B 286     -52.439  48.831  34.269  1.00 44.77           C
ANISOU 5088  C   THR B 286     6448   4087   6476   -902  -1077   -353       C
ATOM   5089  O   THR B 286     -51.389  49.469  34.160  1.00 48.00           O
ANISOU 5089  O   THR B 286     6864   4460   6912  -1038  -1148   -360       O
ATOM   5090  CB  THR B 286     -52.222  47.226  36.144  1.00 37.05           C
ANISOU 5090  CB  THR B 286     5443   3338   5295   -867  -1105   -396       C
ATOM   5091  OG1 THR B 286     -52.434  46.155  35.214  1.00 35.47           O
ANISOU 5091  OG1 THR B 286     5109   3218   5151   -801  -1053   -283       O
ATOM   5092  CG2 THR B 286     -52.741  46.810  37.508  1.00 37.65           C
ANISOU 5092  CG2 THR B 286     5619   3469   5219   -826  -1083   -471       C
ATOM   5093  N   GLY B 287     -53.140  48.433  33.213  1.00 40.65           N
ANISOU 5093  N   GLY B 287     5871   3558   6015   -823  -1018   -267       N
ATOM   5094  CA  GLY B 287     -52.651  48.625  31.866  1.00 36.96           C
ANISOU 5094  CA  GLY B 287     5368   3055   5619   -899  -1026   -168       C
ATOM   5095  C   GLY B 287     -51.789  47.504  31.335  1.00 38.53           C
ANISOU 5095  C   GLY B 287     5426   3404   5811   -949  -1010    -89       C
ATOM   5096  O   GLY B 287     -51.220  47.645  30.246  1.00 36.98           O
ANISOU 5096  O   GLY B 287     5203   3189   5658  -1040   -992    -21       O
ATOM   5097  N   SER B 288     -51.665  46.401  32.069  1.00 38.91           N
ANISOU 5097  N   SER B 288     5390   3588   5807   -898  -1009    -98       N
ATOM   5098  CA  SER B 288     -50.914  45.249  31.595  1.00 37.40           C
ANISOU 5098  CA  SER B 288     5052   3521   5635   -919   -990    -30       C
ATOM   5099  C   SER B 288     -51.734  44.488  30.561  1.00 36.16           C
ANISOU 5099  C   SER B 288     4871   3382   5489   -839   -907     41       C
ATOM   5100  O   SER B 288     -52.956  44.368  30.687  1.00 39.34           O
ANISOU 5100  O   SER B 288     5324   3756   5868   -734   -882     36       O
ATOM   5101  CB  SER B 288     -50.551  44.334  32.764  1.00 34.90           C
ANISOU 5101  CB  SER B 288     4675   3318   5265   -884  -1043    -52       C
ATOM   5102  OG  SER B 288     -49.563  43.394  32.389  1.00 40.20           O
ANISOU 5102  OG  SER B 288     5190   4084   5999   -914  -1049      1       O
ATOM   5103  N   SER B 289     -51.059  43.977  29.533  1.00 33.02           N
ANISOU 5103  N   SER B 289     4390   3027   5130   -899   -859     99       N
ATOM   5104  CA  SER B 289     -51.757  43.334  28.430  1.00 32.69           C
ANISOU 5104  CA  SER B 289     4352   2989   5079   -853   -789    161       C
ATOM   5105  C   SER B 289     -50.870  42.261  27.814  1.00 34.05           C
ANISOU 5105  C   SER B 289     4400   3256   5282   -891   -719    189       C
ATOM   5106  O   SER B 289     -49.683  42.148  28.126  1.00 40.66           O
ANISOU 5106  O   SER B 289     5130   4143   6175   -955   -726    166       O
ATOM   5107  CB  SER B 289     -52.180  44.355  27.369  1.00 35.98           C
ANISOU 5107  CB  SER B 289     4892   3283   5495   -910   -788    200       C
ATOM   5108  OG  SER B 289     -51.051  44.919  26.725  1.00 40.56           O
ANISOU 5108  OG  SER B 289     5474   3839   6097  -1063   -759    216       O
ATOM   5109  N   LYS B 290     -51.473  41.471  26.927  1.00 31.02           N
ANISOU 5109  N   LYS B 290     4024   2888   4873   -851   -655    230       N
ATOM   5110  CA  LYS B 290     -50.762  40.431  26.192  1.00 33.32           C
ANISOU 5110  CA  LYS B 290     4219   3248   5192   -881   -561    242       C
ATOM   5111  C   LYS B 290     -51.622  40.014  25.008  1.00 29.99           C
ANISOU 5111  C   LYS B 290     3884   2801   4708   -873   -506    284       C
ATOM   5112  O   LYS B 290     -52.824  39.785  25.166  1.00 29.65           O
ANISOU 5112  O   LYS B 290     3893   2740   4632   -782   -554    302       O
ATOM   5113  CB  LYS B 290     -50.448  39.231  27.093  1.00 35.55           C
ANISOU 5113  CB  LYS B 290     4370   3616   5519   -791   -576    224       C
ATOM   5114  CG  LYS B 290     -49.802  38.061  26.370  1.00 40.33           C
ANISOU 5114  CG  LYS B 290     4869   4272   6183   -793   -473    224       C
ATOM   5115  CD  LYS B 290     -49.142  37.103  27.349  1.00 43.08           C
ANISOU 5115  CD  LYS B 290     5073   4681   6616   -719   -521    214       C
ATOM   5116  CE  LYS B 290     -50.122  36.622  28.406  1.00 45.91           C
ANISOU 5116  CE  LYS B 290     5487   5050   6908   -610   -606    236       C
ATOM   5117  NZ  LYS B 290     -49.475  35.716  29.395  1.00 49.99           N
ANISOU 5117  NZ  LYS B 290     5898   5611   7487   -548   -680    247       N
ATOM   5118  N   CYS B 291     -51.003  39.916  23.829  1.00 33.65           N
ANISOU 5118  N   CYS B 291     4367   3264   5156   -979   -405    294       N
ATOM   5119  CA  CYS B 291     -51.764  39.676  22.606  1.00 36.60           C
ANISOU 5119  CA  CYS B 291     4868   3603   5437  -1007   -371    336       C
ATOM   5120  C   CYS B 291     -52.361  38.275  22.580  1.00 37.09           C
ANISOU 5120  C   CYS B 291     4882   3717   5493   -909   -347    327       C
ATOM   5121  O   CYS B 291     -53.534  38.097  22.233  1.00 41.84           O
ANISOU 5121  O   CYS B 291     5569   4289   6041   -866   -406    361       O
ATOM   5122  CB  CYS B 291     -50.874  39.898  21.383  1.00 40.47           C
ANISOU 5122  CB  CYS B 291     5415   4081   5882  -1169   -242    339       C
ATOM   5123  SG  CYS B 291     -50.379  41.607  21.127  1.00 49.03           S
ANISOU 5123  SG  CYS B 291     6612   5070   6945  -1320   -270    374       S
ATOM   5124  N   VAL B 292     -51.569  37.267  22.929  1.00 40.12           N
ANISOU 5124  N   VAL B 292     5126   4169   5950   -876   -271    283       N
ATOM   5125  CA  VAL B 292     -51.994  35.872  22.872  1.00 39.91           C
ANISOU 5125  CA  VAL B 292     5059   4175   5931   -794   -236    272       C
ATOM   5126  C   VAL B 292     -51.908  35.312  24.284  1.00 39.08           C
ANISOU 5126  C   VAL B 292     4830   4110   5908   -679   -301    264       C
ATOM   5127  O   VAL B 292     -50.818  34.988  24.770  1.00 41.50           O
ANISOU 5127  O   VAL B 292     5007   4450   6309   -670   -279    237       O
ATOM   5128  CB  VAL B 292     -51.147  35.045  21.899  1.00 43.48           C
ANISOU 5128  CB  VAL B 292     5476   4644   6400   -855    -77    226       C
ATOM   5129  CG1 VAL B 292     -51.657  33.610  21.844  1.00 29.53           C
ANISOU 5129  CG1 VAL B 292     3688   2886   4645   -770    -49    210       C
ATOM   5130  CG2 VAL B 292     -51.156  35.676  20.522  1.00 42.71           C
ANISOU 5130  CG2 VAL B 292     5538   4507   6183   -999     -3    236       C
ATOM   5131  N  ACYS B 293     -53.056  35.195  24.945  0.58 39.04           N
ANISOU 5131  N  ACYS B 293     4865   4098   5870   -597   -383    290       N
ATOM   5132  N  BCYS B 293     -53.050  35.189  24.951  0.42 39.01           N
ANISOU 5132  N  BCYS B 293     4861   4095   5867   -597   -383    290       N
ATOM   5133  CA ACYS B 293     -53.155  34.615  26.280  0.58 38.80           C
ANISOU 5133  CA ACYS B 293     4765   4101   5874   -504   -438    293       C
ATOM   5134  CA BCYS B 293     -53.117  34.613  26.290  0.42 38.79           C
ANISOU 5134  CA BCYS B 293     4762   4102   5876   -505   -437    293       C
ATOM   5135  C  ACYS B 293     -53.906  33.296  26.163  0.58 37.40           C
ANISOU 5135  C  ACYS B 293     4588   3928   5694   -443   -408    308       C
ATOM   5136  C  BCYS B 293     -53.901  33.309  26.206  0.42 37.39           C
ANISOU 5136  C  BCYS B 293     4585   3927   5693   -442   -411    308       C
ATOM   5137  O  ACYS B 293     -55.106  33.284  25.866  0.58 34.53           O
ANISOU 5137  O  ACYS B 293     4292   3543   5286   -431   -423    324       O
ATOM   5138  O  BCYS B 293     -55.114  33.321  25.972  0.42 34.94           O
ANISOU 5138  O  BCYS B 293     4342   3596   5338   -427   -428    325       O
ATOM   5139  CB ACYS B 293     -53.867  35.564  27.239  0.58 39.29           C
ANISOU 5139  CB ACYS B 293     4882   4150   5898   -476   -522    297       C
ATOM   5140  CB BCYS B 293     -53.759  35.585  27.277  0.42 39.44           C
ANISOU 5140  CB BCYS B 293     4895   4170   5919   -479   -523    295       C
ATOM   5141  SG ACYS B 293     -53.344  37.282  27.111  0.58 46.22           S
ANISOU 5141  SG ACYS B 293     5810   4982   6768   -562   -561    278       S
ATOM   5142  SG BCYS B 293     -53.573  35.102  29.009  0.42 37.11           S
ANISOU 5142  SG BCYS B 293     4556   3921   5623   -409   -589    295       S
ATOM   5143  N   SER B 294     -53.205  32.189  26.390  1.00 39.54           N
ANISOU 5143  N   SER B 294     4775   4215   6032   -405   -376    303       N
ATOM   5144  CA  SER B 294     -53.830  30.875  26.330  1.00 37.77           C
ANISOU 5144  CA  SER B 294     4558   3976   5817   -353   -348    317       C
ATOM   5145  C   SER B 294     -54.547  30.596  27.645  1.00 32.19           C
ANISOU 5145  C   SER B 294     3864   3283   5085   -290   -418    357       C
ATOM   5146  O   SER B 294     -53.941  30.674  28.720  1.00 30.81           O
ANISOU 5146  O   SER B 294     3654   3129   4924   -261   -480    374       O
ATOM   5147  CB  SER B 294     -52.786  29.802  26.037  1.00 44.78           C
ANISOU 5147  CB  SER B 294     5358   4851   6807   -329   -282    292       C
ATOM   5148  OG  SER B 294     -52.182  30.023  24.776  1.00 52.72           O
ANISOU 5148  OG  SER B 294     6363   5846   7822   -402   -176    240       O
ATOM   5149  N   VAL B 295     -55.839  30.285  27.560  1.00 36.67           N
ANISOU 5149  N   VAL B 295     4486   3836   5611   -280   -408    372       N
ATOM   5150  CA  VAL B 295     -56.675  30.026  28.725  1.00 35.90           C
ANISOU 5150  CA  VAL B 295     4409   3749   5480   -241   -434    403       C
ATOM   5151  C   VAL B 295     -57.348  28.673  28.546  1.00 35.39           C
ANISOU 5151  C   VAL B 295     4352   3658   5437   -228   -394    426       C
ATOM   5152  O   VAL B 295     -57.702  28.289  27.426  1.00 34.99           O
ANISOU 5152  O   VAL B 295     4312   3579   5404   -257   -360    408       O
ATOM   5153  CB  VAL B 295     -57.728  31.138  28.930  1.00 33.24           C
ANISOU 5153  CB  VAL B 295     4110   3417   5103   -249   -448    386       C
ATOM   5154  CG1 VAL B 295     -58.461  30.952  30.254  1.00 32.76           C
ANISOU 5154  CG1 VAL B 295     4071   3375   5002   -221   -437    398       C
ATOM   5155  CG2 VAL B 295     -57.077  32.511  28.870  1.00 31.39           C
ANISOU 5155  CG2 VAL B 295     3887   3184   4857   -275   -487    358       C
ATOM   5156  N   ILE B 296     -57.513  27.949  29.649  1.00 32.91           N
ANISOU 5156  N   ILE B 296     4052   3344   5110   -198   -403    469       N
ATOM   5157  CA  ILE B 296     -58.208  26.668  29.654  1.00 36.03           C
ANISOU 5157  CA  ILE B 296     4465   3700   5524   -197   -365    501       C
ATOM   5158  C   ILE B 296     -58.988  26.552  30.957  1.00 35.02           C
ANISOU 5158  C   ILE B 296     4384   3590   5333   -199   -356    542       C
ATOM   5159  O   ILE B 296     -58.512  26.969  32.019  1.00 32.43           O
ANISOU 5159  O   ILE B 296     4090   3291   4942   -188   -396    562       O
ATOM   5160  CB  ILE B 296     -57.229  25.488  29.473  1.00 37.50           C
ANISOU 5160  CB  ILE B 296     4633   3832   5783   -164   -369    521       C
ATOM   5161  CG1 ILE B 296     -57.990  24.164  29.391  1.00 35.07           C
ANISOU 5161  CG1 ILE B 296     4362   3463   5501   -173   -329    550       C
ATOM   5162  CG2 ILE B 296     -56.197  25.458  30.595  1.00 33.52           C
ANISOU 5162  CG2 ILE B 296     4119   3337   5281   -119   -447    568       C
ATOM   5163  CD1 ILE B 296     -57.125  22.986  29.008  1.00 35.65           C
ANISOU 5163  CD1 ILE B 296     4420   3453   5672   -133   -321    553       C
ATOM   5164  N   ASP B 297     -60.201  26.000  30.874  1.00 35.51           N
ANISOU 5164  N   ASP B 297     4452   3635   5404   -230   -298    549       N
ATOM   5165  CA  ASP B 297     -61.084  25.888  32.034  1.00 37.51           C
ANISOU 5165  CA  ASP B 297     4746   3907   5599   -253   -246    576       C
ATOM   5166  C   ASP B 297     -61.071  24.446  32.536  1.00 36.76           C
ANISOU 5166  C   ASP B 297     4709   3760   5500   -269   -230    651       C
ATOM   5167  O   ASP B 297     -61.990  23.663  32.302  1.00 38.20           O
ANISOU 5167  O   ASP B 297     4885   3908   5722   -313   -171    663       O
ATOM   5168  CB  ASP B 297     -62.496  26.348  31.686  1.00 36.72           C
ANISOU 5168  CB  ASP B 297     4589   3822   5542   -282   -183    531       C
ATOM   5169  CG  ASP B 297     -63.442  26.278  32.873  1.00 39.60           C
ANISOU 5169  CG  ASP B 297     4977   4209   5860   -315    -85    539       C
ATOM   5170  OD1 ASP B 297     -62.960  26.198  34.023  1.00 41.24           O
ANISOU 5170  OD1 ASP B 297     5279   4432   5958   -320    -75    574       O
ATOM   5171  OD2 ASP B 297     -64.670  26.295  32.655  1.00 43.51           O
ANISOU 5171  OD2 ASP B 297     5397   4705   6428   -344    -18    509       O
ATOM   5172  N   LEU B 298     -60.007  24.103  33.248  1.00 35.69           N
ANISOU 5172  N   LEU B 298     4630   3607   5323   -238   -299    708       N
ATOM   5173  CA  LEU B 298     -59.927  22.829  33.941  1.00 36.79           C
ANISOU 5173  CA  LEU B 298     4852   3681   5444   -250   -310    801       C
ATOM   5174  C   LEU B 298     -60.396  22.989  35.381  1.00 36.23           C
ANISOU 5174  C   LEU B 298     4897   3645   5225   -301   -279    850       C
ATOM   5175  O   LEU B 298     -60.358  24.080  35.954  1.00 40.14           O
ANISOU 5175  O   LEU B 298     5413   4210   5630   -307   -279    810       O
ATOM   5176  CB  LEU B 298     -58.497  22.284  33.923  1.00 36.68           C
ANISOU 5176  CB  LEU B 298     4834   3610   5491   -181   -426    846       C
ATOM   5177  CG  LEU B 298     -57.928  21.802  32.590  1.00 38.89           C
ANISOU 5177  CG  LEU B 298     5023   3833   5921   -135   -424    796       C
ATOM   5178  CD1 LEU B 298     -56.460  21.447  32.743  1.00 39.10           C
ANISOU 5178  CD1 LEU B 298     5010   3811   6034    -55   -530    828       C
ATOM   5179  CD2 LEU B 298     -58.715  20.609  32.071  1.00 41.40           C
ANISOU 5179  CD2 LEU B 298     5370   4065   6296   -168   -354    807       C
ATOM   5180  N   LEU B 299     -60.855  21.884  35.961  1.00 34.84           N
ANISOU 5180  N   LEU B 299     4815   3410   5014   -351   -242    934       N
ATOM   5181  CA  LEU B 299     -61.056  21.850  37.401  1.00 40.32           C
ANISOU 5181  CA  LEU B 299     5664   4122   5534   -413   -222   1003       C
ATOM   5182  C   LEU B 299     -59.720  22.089  38.089  1.00 44.14           C
ANISOU 5182  C   LEU B 299     6223   4607   5943   -366   -394   1058       C
ATOM   5183  O   LEU B 299     -58.708  21.484  37.723  1.00 48.97           O
ANISOU 5183  O   LEU B 299     6798   5151   6658   -294   -525   1108       O
ATOM   5184  CB  LEU B 299     -61.648  20.508  37.830  1.00 34.87           C
ANISOU 5184  CB  LEU B 299     5080   3347   4822   -486   -165   1104       C
ATOM   5185  CG  LEU B 299     -61.994  20.370  39.314  1.00 39.59           C
ANISOU 5185  CG  LEU B 299     5876   3957   5210   -583   -114   1186       C
ATOM   5186  CD1 LEU B 299     -63.169  21.266  39.674  1.00 38.08           C
ANISOU 5186  CD1 LEU B 299     5662   3862   4944   -658     82   1086       C
ATOM   5187  CD2 LEU B 299     -62.288  18.921  39.671  1.00 38.13           C
ANISOU 5187  CD2 LEU B 299     5817   3658   5012   -653    -98   1315       C
ATOM   5188  N   LEU B 300     -59.713  22.990  39.073  1.00 42.82           N
ANISOU 5188  N   LEU B 300     6150   4511   5607   -405   -394   1039       N
ATOM   5189  CA  LEU B 300     -58.456  23.362  39.716  1.00 43.58           C
ANISOU 5189  CA  LEU B 300     6309   4618   5632   -374   -582   1080       C
ATOM   5190  C   LEU B 300     -57.767  22.150  40.328  1.00 43.61           C
ANISOU 5190  C   LEU B 300     6430   4529   5612   -366   -734   1235       C
ATOM   5191  O   LEU B 300     -56.535  22.055  40.316  1.00 46.50           O
ANISOU 5191  O   LEU B 300     6752   4862   6054   -295   -929   1280       O
ATOM   5192  CB  LEU B 300     -58.703  24.433  40.776  1.00 45.80           C
ANISOU 5192  CB  LEU B 300     6719   4980   5704   -443   -546   1030       C
ATOM   5193  CG  LEU B 300     -57.447  25.064  41.378  1.00 45.17           C
ANISOU 5193  CG  LEU B 300     6692   4924   5548   -427   -752   1044       C
ATOM   5194  CD1 LEU B 300     -56.568  25.649  40.283  1.00 37.49           C
ANISOU 5194  CD1 LEU B 300     5509   3961   4776   -336   -838    975       C
ATOM   5195  CD2 LEU B 300     -57.818  26.128  42.397  1.00 48.67           C
ANISOU 5195  CD2 LEU B 300     7287   5438   5769   -511   -691    971       C
ATOM   5196  N   ASP B 301     -58.549  21.206  40.856  1.00 41.58           N
ANISOU 5196  N   ASP B 301     6313   4217   5270   -442   -651   1323       N
ATOM   5197  CA  ASP B 301     -57.967  19.982  41.396  1.00 39.86           C
ANISOU 5197  CA  ASP B 301     6222   3881   5041   -435   -804   1488       C
ATOM   5198  C   ASP B 301     -57.268  19.181  40.307  1.00 39.67           C
ANISOU 5198  C   ASP B 301     6034   3755   5284   -315   -890   1500       C
ATOM   5199  O   ASP B 301     -56.225  18.563  40.552  1.00 42.79           O
ANISOU 5199  O   ASP B 301     6448   4059   5752   -243  -1091   1600       O
ATOM   5200  CB  ASP B 301     -59.054  19.144  42.067  1.00 44.06           C
ANISOU 5200  CB  ASP B 301     6939   4365   5435   -559   -664   1574       C
ATOM   5201  CG  ASP B 301     -59.933  19.964  42.987  1.00 52.29           C
ANISOU 5201  CG  ASP B 301     8118   5515   6235   -685   -499   1521       C
ATOM   5202  OD1 ASP B 301     -60.518  20.961  42.513  1.00 55.11           O
ANISOU 5202  OD1 ASP B 301     8338   5968   6633   -680   -351   1368       O
ATOM   5203  OD2 ASP B 301     -60.044  19.613  44.180  1.00 58.12           O
ANISOU 5203  OD2 ASP B 301     9107   6232   6742   -792   -513   1630       O
ATOM   5204  N   ASP B 302     -57.827  19.181  39.095  1.00 40.23           N
ANISOU 5204  N   ASP B 302     5945   3832   5507   -292   -743   1392       N
ATOM   5205  CA  ASP B 302     -57.190  18.480  37.985  1.00 44.42           C
ANISOU 5205  CA  ASP B 302     6334   4269   6277   -189   -789   1373       C
ATOM   5206  C   ASP B 302     -55.862  19.128  37.622  1.00 44.73           C
ANISOU 5206  C   ASP B 302     6229   4338   6427    -85   -925   1323       C
ATOM   5207  O   ASP B 302     -54.850  18.438  37.448  1.00 49.17           O
ANISOU 5207  O   ASP B 302     6732   4801   7149      9  -1055   1371       O
ATOM   5208  CB  ASP B 302     -58.123  18.450  36.773  1.00 46.80           C
ANISOU 5208  CB  ASP B 302     6524   4581   6675   -212   -609   1260       C
ATOM   5209  CG  ASP B 302     -59.297  17.509  36.962  1.00 52.98           C
ANISOU 5209  CG  ASP B 302     7410   5298   7422   -309   -492   1314       C
ATOM   5210  OD1 ASP B 302     -59.343  16.809  37.995  1.00 57.68           O
ANISOU 5210  OD1 ASP B 302     8174   5825   7916   -357   -537   1446       O
ATOM   5211  OD2 ASP B 302     -60.173  17.467  36.073  1.00 54.62           O
ANISOU 5211  OD2 ASP B 302     7534   5517   7700   -348   -363   1229       O
ATOM   5212  N   PHE B 303     -55.844  20.458  37.509  1.00 42.84           N
ANISOU 5212  N   PHE B 303     5924   4227   6126   -103   -893   1224       N
ATOM   5213  CA  PHE B 303     -54.611  21.153  37.158  1.00 43.13           C
ANISOU 5213  CA  PHE B 303     5819   4298   6270    -29  -1006   1172       C
ATOM   5214  C   PHE B 303     -53.539  20.944  38.219  1.00 44.94           C
ANISOU 5214  C   PHE B 303     6105   4492   6477      4  -1238   1283       C
ATOM   5215  O   PHE B 303     -52.353  20.812  37.895  1.00 45.22           O
ANISOU 5215  O   PHE B 303     5997   4487   6696     94  -1364   1282       O
ATOM   5216  CB  PHE B 303     -54.889  22.642  36.955  1.00 42.62           C
ANISOU 5216  CB  PHE B 303     5709   4361   6123    -73   -933   1057       C
ATOM   5217  CG  PHE B 303     -53.666  23.446  36.622  1.00 41.86           C
ANISOU 5217  CG  PHE B 303     5474   4303   6126    -26  -1034   1002       C
ATOM   5218  CD1 PHE B 303     -53.058  23.327  35.383  1.00 42.20           C
ANISOU 5218  CD1 PHE B 303     5347   4320   6369     34   -992    933       C
ATOM   5219  CD2 PHE B 303     -53.128  24.328  37.545  1.00 41.03           C
ANISOU 5219  CD2 PHE B 303     5418   4260   5912    -57  -1162   1010       C
ATOM   5220  CE1 PHE B 303     -51.932  24.069  35.073  1.00 44.78           C
ANISOU 5220  CE1 PHE B 303     5535   4683   6798     60  -1061    879       C
ATOM   5221  CE2 PHE B 303     -52.003  25.072  37.241  1.00 41.46           C
ANISOU 5221  CE2 PHE B 303     5332   4347   6074    -30  -1256    958       C
ATOM   5222  CZ  PHE B 303     -51.405  24.943  36.003  1.00 44.32           C
ANISOU 5222  CZ  PHE B 303     5506   4685   6650     27  -1198    895       C
ATOM   5223  N   VAL B 304     -53.936  20.908  39.493  1.00 44.22           N
ANISOU 5223  N   VAL B 304     6223   4414   6166    -74  -1298   1378       N
ATOM   5224  CA  VAL B 304     -52.983  20.608  40.558  1.00 44.06           C
ANISOU 5224  CA  VAL B 304     6296   4346   6098    -57  -1554   1508       C
ATOM   5225  C   VAL B 304     -52.435  19.198  40.394  1.00 46.79           C
ANISOU 5225  C   VAL B 304     6614   4530   6635     37  -1670   1622       C
ATOM   5226  O   VAL B 304     -51.228  18.963  40.537  1.00 50.00           O
ANISOU 5226  O   VAL B 304     6926   4876   7196    128  -1890   1677       O
ATOM   5227  CB  VAL B 304     -53.642  20.807  41.935  1.00 47.07           C
ANISOU 5227  CB  VAL B 304     6956   4768   6160   -186  -1568   1586       C
ATOM   5228  CG1 VAL B 304     -52.751  20.257  43.037  1.00 44.52           C
ANISOU 5228  CG1 VAL B 304     6779   4371   5767   -182  -1860   1754       C
ATOM   5229  CG2 VAL B 304     -53.931  22.278  42.172  1.00 46.77           C
ANISOU 5229  CG2 VAL B 304     6933   4872   5965   -258  -1487   1459       C
ATOM   5230  N   GLU B 305     -53.310  18.239  40.085  1.00 48.02           N
ANISOU 5230  N   GLU B 305     6841   4601   6804     18  -1529   1654       N
ATOM   5231  CA  GLU B 305     -52.859  16.874  39.834  1.00 48.21           C
ANISOU 5231  CA  GLU B 305     6843   4444   7029    111  -1616   1746       C
ATOM   5232  C   GLU B 305     -51.902  16.822  38.650  1.00 43.77           C
ANISOU 5232  C   GLU B 305     6009   3844   6778    250  -1620   1639       C
ATOM   5233  O   GLU B 305     -50.938  16.048  38.653  1.00 48.27           O
ANISOU 5233  O   GLU B 305     6501   4280   7560    367  -1782   1705       O
ATOM   5234  CB  GLU B 305     -54.066  15.965  39.599  1.00 54.61           C
ANISOU 5234  CB  GLU B 305     7774   5177   7800     42  -1434   1772       C
ATOM   5235  CG  GLU B 305     -53.721  14.550  39.161  1.00 64.20           C
ANISOU 5235  CG  GLU B 305     8967   6185   9241    135  -1485   1839       C
ATOM   5236  CD  GLU B 305     -54.948  13.666  39.033  1.00 72.39           C
ANISOU 5236  CD  GLU B 305    10143   7139  10221     39  -1316   1872       C
ATOM   5237  OE1 GLU B 305     -55.963  13.957  39.701  1.00 75.58           O
ANISOU 5237  OE1 GLU B 305    10706   7624  10385   -106  -1213   1905       O
ATOM   5238  OE2 GLU B 305     -54.901  12.683  38.264  1.00 75.36           O
ANISOU 5238  OE2 GLU B 305    10466   7366  10801    101  -1276   1854       O
ATOM   5239  N   ILE B 306     -52.145  17.651  37.634  1.00 42.01           N
ANISOU 5239  N   ILE B 306     5641   3730   6591    237  -1439   1473       N
ATOM   5240  CA  ILE B 306     -51.281  17.665  36.458  1.00 44.10           C
ANISOU 5240  CA  ILE B 306     5666   3969   7120    341  -1398   1356       C
ATOM   5241  C   ILE B 306     -49.918  18.254  36.801  1.00 51.20           C
ANISOU 5241  C   ILE B 306     6419   4904   8132    409  -1591   1361       C
ATOM   5242  O   ILE B 306     -48.875  17.650  36.525  1.00 56.57           O
ANISOU 5242  O   ILE B 306     6942   5479   9074    530  -1687   1368       O
ATOM   5243  CB  ILE B 306     -51.952  18.441  35.310  1.00 43.60           C
ANISOU 5243  CB  ILE B 306     5529   4013   7025    284  -1166   1194       C
ATOM   5244  CG1 ILE B 306     -53.222  17.727  34.846  1.00 42.59           C
ANISOU 5244  CG1 ILE B 306     5508   3833   6841    224  -1000   1183       C
ATOM   5245  CG2 ILE B 306     -50.983  18.622  34.152  1.00 37.53           C
ANISOU 5245  CG2 ILE B 306     4538   3236   6484    364  -1110   1070       C
ATOM   5246  CD1 ILE B 306     -54.051  18.537  33.873  1.00 34.98           C
ANISOU 5246  CD1 ILE B 306     4502   2977   5812    152   -817   1050       C
ATOM   5247  N   ILE B 307     -49.908  19.443  37.411  1.00 49.48           N
ANISOU 5247  N   ILE B 307     6239   4824   7735    331  -1649   1350       N
ATOM   5248  CA  ILE B 307     -48.652  20.150  37.641  1.00 48.93           C
ANISOU 5248  CA  ILE B 307     6013   4803   7775    370  -1822   1333       C
ATOM   5249  C   ILE B 307     -47.777  19.407  38.644  1.00 49.17           C
ANISOU 5249  C   ILE B 307     6065   4727   7889    441  -2120   1489       C
ATOM   5250  O   ILE B 307     -46.544  19.468  38.565  1.00 53.00           O
ANISOU 5250  O   ILE B 307     6342   5187   8609    527  -2276   1481       O
ATOM   5251  CB  ILE B 307     -48.934  21.599  38.090  1.00 51.60           C
ANISOU 5251  CB  ILE B 307     6419   5299   7887    256  -1814   1278       C
ATOM   5252  CG1 ILE B 307     -47.639  22.411  38.168  1.00 54.91           C
ANISOU 5252  CG1 ILE B 307     6655   5771   8438    276  -1975   1238       C
ATOM   5253  CG2 ILE B 307     -49.652  21.627  39.430  1.00 53.27           C
ANISOU 5253  CG2 ILE B 307     6909   5533   7800    162  -1902   1388       C
ATOM   5254  CD1 ILE B 307     -47.001  22.682  36.826  1.00 54.57           C
ANISOU 5254  CD1 ILE B 307     6349   5738   8647    328  -1831   1102       C
ATOM   5255  N   LYS B 308     -48.381  18.681  39.583  1.00 49.41           N
ANISOU 5255  N   LYS B 308     6342   4686   7744    404  -2210   1638       N
ATOM   5256  CA  LYS B 308     -47.621  18.017  40.634  1.00 53.21           C
ANISOU 5256  CA  LYS B 308     6895   5059   8262    454  -2529   1814       C
ATOM   5257  C   LYS B 308     -47.057  16.666  40.213  1.00 59.21           C
ANISOU 5257  C   LYS B 308     7540   5619   9337    610  -2600   1877       C
ATOM   5258  O   LYS B 308     -46.422  15.999  41.037  1.00 66.94           O
ANISOU 5258  O   LYS B 308     8574   6476  10384    671  -2888   2040       O
ATOM   5259  CB  LYS B 308     -48.487  17.843  41.884  1.00 54.99           C
ANISOU 5259  CB  LYS B 308     7474   5288   8132    326  -2596   1960       C
ATOM   5260  CG  LYS B 308     -48.660  19.117  42.694  1.00 56.68           C
ANISOU 5260  CG  LYS B 308     7819   5666   8051    191  -2638   1929       C
ATOM   5261  CD  LYS B 308     -49.316  18.835  44.034  1.00 60.71           C
ANISOU 5261  CD  LYS B 308     8692   6161   8214     64  -2727   2082       C
ATOM   5262  CE  LYS B 308     -49.283  20.062  44.929  1.00 65.35           C
ANISOU 5262  CE  LYS B 308     9421   6892   8518    -64  -2806   2046       C
ATOM   5263  NZ  LYS B 308     -49.905  19.805  46.257  1.00 72.43           N
ANISOU 5263  NZ  LYS B 308    10700   7776   9044   -207  -2871   2184       N
ATOM   5264  N   SER B 309     -47.261  16.246  38.966  1.00 56.70           N
ANISOU 5264  N   SER B 309     7078   5252   9214    673  -2357   1752       N
ATOM   5265  CA  SER B 309     -46.718  14.987  38.474  1.00 60.39           C
ANISOU 5265  CA  SER B 309     7428   5515  10003    827  -2390   1776       C
ATOM   5266  C   SER B 309     -45.601  15.191  37.458  1.00 60.55           C
ANISOU 5266  C   SER B 309     7099   5531  10377    952  -2333   1622       C
ATOM   5267  O   SER B 309     -45.217  14.238  36.771  1.00 63.36           O
ANISOU 5267  O   SER B 309     7327   5726  11022   1081  -2270   1580       O
ATOM   5268  CB  SER B 309     -47.833  14.131  37.867  1.00 60.05           C
ANISOU 5268  CB  SER B 309     7522   5382   9912    796  -2152   1752       C
ATOM   5269  OG  SER B 309     -48.487  14.815  36.814  1.00 59.81           O
ANISOU 5269  OG  SER B 309     7430   5483   9812    722  -1859   1570       O
ATOM   5270  N   GLN B 310     -45.063  16.402  37.355  1.00 59.53           N
ANISOU 5270  N   GLN B 310     6817   5564  10237    910  -2340   1531       N
ATOM   5271  CA  GLN B 310     -44.044  16.727  36.370  1.00 60.61           C
ANISOU 5271  CA  GLN B 310     6624   5720  10687    993  -2244   1373       C
ATOM   5272  C   GLN B 310     -42.653  16.656  36.989  1.00 62.14           C
ANISOU 5272  C   GLN B 310     6601   5855  11154   1104  -2552   1446       C
ATOM   5273  O   GLN B 310     -42.478  16.847  38.195  1.00 61.78           O
ANISOU 5273  O   GLN B 310     6683   5842  10950   1056  -2827   1583       O
ATOM   5274  CB  GLN B 310     -44.282  18.122  35.789  1.00 60.19           C
ANISOU 5274  CB  GLN B 310     6523   5869  10476    866  -2052   1227       C
ATOM   5275  CG  GLN B 310     -45.675  18.322  35.220  1.00 60.30           C
ANISOU 5275  CG  GLN B 310     6737   5949  10225    754  -1787   1163       C
ATOM   5276  CD  GLN B 310     -45.973  17.382  34.070  1.00 64.24           C
ANISOU 5276  CD  GLN B 310     7200   6334  10874    814  -1557   1071       C
ATOM   5277  OE1 GLN B 310     -45.095  17.069  33.265  1.00 70.04           O
ANISOU 5277  OE1 GLN B 310     7712   7002  11898    911  -1476    968       O
ATOM   5278  NE2 GLN B 310     -47.215  16.921  33.988  1.00 60.08           N
ANISOU 5278  NE2 GLN B 310     6892   5780  10156    749  -1443   1097       N
ATOM   5279  N   ASP B 311     -41.662  16.374  36.144  1.00 64.51           N
ANISOU 5279  N   ASP B 311     6594   6099  11820   1220  -2458   1318       N
ATOM   5280  CA  ASP B 311     -40.269  16.372  36.571  1.00 67.52           C
ANISOU 5280  CA  ASP B 311     6747   6483  12424   1275  -2648   1312       C
ATOM   5281  C   ASP B 311     -39.732  17.797  36.503  1.00 67.41           C
ANISOU 5281  C   ASP B 311     6557   6640  12416   1190  -2673   1236       C
ATOM   5282  O   ASP B 311     -39.690  18.400  35.425  1.00 63.72           O
ANISOU 5282  O   ASP B 311     5914   6233  12064   1176  -2427   1083       O
ATOM   5283  CB  ASP B 311     -39.438  15.438  35.694  1.00 68.48           C
ANISOU 5283  CB  ASP B 311     6619   6475  12925   1418  -2497   1190       C
ATOM   5284  CG  ASP B 311     -38.140  15.016  36.358  1.00 76.36           C
ANISOU 5284  CG  ASP B 311     7444   7418  14152   1496  -2741   1234       C
ATOM   5285  OD1 ASP B 311     -37.852  13.801  36.392  1.00 81.15           O
ANISOU 5285  OD1 ASP B 311     8042   7862  14928   1611  -2773   1263       O
ATOM   5286  OD2 ASP B 311     -37.415  15.897  36.865  1.00 78.72           O
ANISOU 5286  OD2 ASP B 311     7621   7826  14464   1439  -2911   1244       O
ATOM   5287  N   LEU B 312     -39.320  18.332  37.651  1.00 71.37           N
ANISOU 5287  N   LEU B 312     7120   7214  12783   1119  -2965   1337       N
ATOM   5288  CA  LEU B 312     -38.889  19.719  37.759  1.00 71.04           C
ANISOU 5288  CA  LEU B 312     6962   7332  12699   1010  -3023   1279       C
ATOM   5289  C   LEU B 312     -37.388  19.895  37.546  1.00 72.93           C
ANISOU 5289  C   LEU B 312     6852   7577  13280   1052  -3071   1185       C
ATOM   5290  O   LEU B 312     -36.848  20.955  37.880  1.00 74.87           O
ANISOU 5290  O   LEU B 312     7010   7939  13500    953  -3185   1159       O
ATOM   5291  CB  LEU B 312     -39.291  20.288  39.123  1.00 72.94           C
ANISOU 5291  CB  LEU B 312     7485   7648  12581    887  -3300   1420       C
ATOM   5292  CG  LEU B 312     -40.687  20.899  39.292  1.00 72.00           C
ANISOU 5292  CG  LEU B 312     7668   7610  12077    770  -3213   1456       C
ATOM   5293  CD1 LEU B 312     -41.797  19.917  38.947  1.00 73.99           C
ANISOU 5293  CD1 LEU B 312     8128   7771  12213    806  -3008   1488       C
ATOM   5294  CD2 LEU B 312     -40.871  21.429  40.706  1.00 72.54           C
ANISOU 5294  CD2 LEU B 312     8001   7743  11817    649  -3499   1582       C
ATOM   5295  N   SER B 313     -36.707  18.890  36.995  1.00 77.35           N
ANISOU 5295  N   SER B 313     7216   8012  14162   1189  -2979   1128       N
ATOM   5296  CA  SER B 313     -35.256  18.910  36.866  1.00 83.06           C
ANISOU 5296  CA  SER B 313     7608   8720  15231   1240  -3032   1050       C
ATOM   5297  C   SER B 313     -34.785  19.270  35.462  1.00 85.04           C
ANISOU 5297  C   SER B 313     7562   9005  15745   1251  -2682    841       C
ATOM   5298  O   SER B 313     -33.604  19.087  35.153  1.00 91.08           O
ANISOU 5298  O   SER B 313     8035   9732  16839   1310  -2652    754       O
ATOM   5299  CB  SER B 313     -34.670  17.556  37.274  1.00 87.54           C
ANISOU 5299  CB  SER B 313     8140   9116  16008   1385  -3183   1125       C
ATOM   5300  OG  SER B 313     -34.848  16.590  36.251  1.00 88.46           O
ANISOU 5300  OG  SER B 313     8185   9112  16315   1503  -2907   1029       O
ATOM   5301  N   VAL B 314     -35.672  19.773  34.609  1.00 81.77           N
ANISOU 5301  N   VAL B 314     7217   8657  15193   1188  -2412    758       N
ATOM   5302  CA  VAL B 314     -35.334  20.148  33.241  1.00 81.88           C
ANISOU 5302  CA  VAL B 314     6996   8710  15406   1171  -2050    558       C
ATOM   5303  C   VAL B 314     -35.679  21.615  33.034  1.00 75.92           C
ANISOU 5303  C   VAL B 314     6252   8126  14469   1003  -1982    513       C
ATOM   5304  O   VAL B 314     -36.681  22.107  33.563  1.00 73.81           O
ANISOU 5304  O   VAL B 314     6234   7921  13891    928  -2097    612       O
ATOM   5305  CB  VAL B 314     -36.065  19.270  32.205  1.00 86.74           C
ANISOU 5305  CB  VAL B 314     7683   9221  16052   1252  -1743    475       C
ATOM   5306  CG1 VAL B 314     -35.082  18.342  31.508  1.00 88.17           C
ANISOU 5306  CG1 VAL B 314     7626   9282  16593   1371  -1571    347       C
ATOM   5307  CG2 VAL B 314     -37.183  18.477  32.870  1.00 89.60           C
ANISOU 5307  CG2 VAL B 314     8372   9495  16177   1299  -1892    634       C
ATOM   5308  N   VAL B 315     -34.852  22.305  32.246  1.00 74.45           N
ANISOU 5308  N   VAL B 315     5804   8009  14472    935  -1779    361       N
ATOM   5309  CA  VAL B 315     -35.054  23.733  32.016  1.00 70.96           C
ANISOU 5309  CA  VAL B 315     5359   7723  13881    754  -1708    312       C
ATOM   5310  C   VAL B 315     -36.318  23.973  31.198  1.00 64.67           C
ANISOU 5310  C   VAL B 315     4864   6972  12735    661  -1407    259       C
ATOM   5311  O   VAL B 315     -37.135  24.841  31.528  1.00 61.64           O
ANISOU 5311  O   VAL B 315     4746   6684  11991    527  -1448    307       O
ATOM   5312  CB  VAL B 315     -33.817  24.346  31.336  1.00 74.90           C
ANISOU 5312  CB  VAL B 315     5550   8276  14632    679  -1526    161       C
ATOM   5313  CG1 VAL B 315     -34.101  25.775  30.899  1.00 73.54           C
ANISOU 5313  CG1 VAL B 315     5397   8247  14299    473  -1392     98       C
ATOM   5314  CG2 VAL B 315     -32.621  24.297  32.273  1.00 78.16           C
ANISOU 5314  CG2 VAL B 315     5807   8670  15220    714  -1821    218       C
ATOM   5315  N   SER B 316     -36.493  23.220  30.115  1.00 62.82           N
ANISOU 5315  N   SER B 316     4612   6663  12592    723  -1099    151       N
ATOM   5316  CA  SER B 316     -37.670  23.370  29.269  1.00 60.70           C
ANISOU 5316  CA  SER B 316     4642   6430  11992    628   -826     99       C
ATOM   5317  C   SER B 316     -38.045  22.011  28.702  1.00 59.25           C
ANISOU 5317  C   SER B 316     4513   6106  11892    761   -672     60       C
ATOM   5318  O   SER B 316     -37.190  21.306  28.159  1.00 58.30           O
ANISOU 5318  O   SER B 316     4139   5891  12122    870   -539    -43       O
ATOM   5319  CB  SER B 316     -37.420  24.371  28.136  1.00 65.97           C
ANISOU 5319  CB  SER B 316     5250   7195  12620    465   -517    -49       C
ATOM   5320  OG  SER B 316     -36.547  23.834  27.159  1.00 74.74           O
ANISOU 5320  OG  SER B 316     6100   8245  14053    519   -251   -202       O
ATOM   5321  N   LYS B 317     -39.319  21.648  28.837  1.00 56.59           N
ANISOU 5321  N   LYS B 317     4500   5749  11252    749   -683    135       N
ATOM   5322  CA  LYS B 317     -39.832  20.382  28.336  1.00 57.39           C
ANISOU 5322  CA  LYS B 317     4703   5712  11390    850   -551    106       C
ATOM   5323  C   LYS B 317     -41.248  20.584  27.820  1.00 55.98           C
ANISOU 5323  C   LYS B 317     4856   5584  10828    730   -403    101       C
ATOM   5324  O   LYS B 317     -42.042  21.301  28.436  1.00 56.35           O
ANISOU 5324  O   LYS B 317     5097   5726  10589    638   -534    199       O
ATOM   5325  CB  LYS B 317     -39.835  19.298  29.423  1.00 59.67           C
ANISOU 5325  CB  LYS B 317     5012   5863  11798   1010   -839    257       C
ATOM   5326  CG  LYS B 317     -40.330  17.943  28.935  1.00 65.04           C
ANISOU 5326  CG  LYS B 317     5798   6375  12542   1113   -711    228       C
ATOM   5327  CD  LYS B 317     -41.078  17.188  30.021  1.00 70.90           C
ANISOU 5327  CD  LYS B 317     6762   7026  13152   1172   -972    419       C
ATOM   5328  CE  LYS B 317     -40.190  16.899  31.219  1.00 76.14           C
ANISOU 5328  CE  LYS B 317     7270   7618  14043   1296  -1326    563       C
ATOM   5329  NZ  LYS B 317     -40.922  16.140  32.272  1.00 76.26           N
ANISOU 5329  NZ  LYS B 317     7539   7534  13901   1332  -1570    761       N
ATOM   5330  N   VAL B 318     -41.559  19.954  26.690  1.00 55.38           N
ANISOU 5330  N   VAL B 318     4842   5440  10760    731   -133    -22       N
ATOM   5331  CA  VAL B 318     -42.931  19.917  26.201  1.00 53.68           C
ANISOU 5331  CA  VAL B 318     4931   5245  10220    634    -27    -20       C
ATOM   5332  C   VAL B 318     -43.673  18.791  26.906  1.00 54.35           C
ANISOU 5332  C   VAL B 318     5167   5209  10274    729   -180     95       C
ATOM   5333  O   VAL B 318     -43.134  17.695  27.109  1.00 59.57           O
ANISOU 5333  O   VAL B 318     5720   5718  11196    876   -226    101       O
ATOM   5334  CB  VAL B 318     -42.969  19.753  24.669  1.00 57.54           C
ANISOU 5334  CB  VAL B 318     5453   5713  10695    566    312   -202       C
ATOM   5335  CG1 VAL B 318     -42.302  20.940  23.992  1.00 56.98           C
ANISOU 5335  CG1 VAL B 318     5271   5765  10614    441    471   -299       C
ATOM   5336  CG2 VAL B 318     -42.309  18.447  24.240  1.00 67.61           C
ANISOU 5336  CG2 VAL B 318     6592   6818  12281    710    440   -306       C
ATOM   5337  N   VAL B 319     -44.911  19.065  27.307  1.00 50.96           N
ANISOU 5337  N   VAL B 319     4984   4839   9540    643   -259    191       N
ATOM   5338  CA  VAL B 319     -45.730  18.115  28.051  1.00 47.54           C
ANISOU 5338  CA  VAL B 319     4718   4307   9037    696   -397    314       C
ATOM   5339  C   VAL B 319     -47.063  17.978  27.333  1.00 41.19           C
ANISOU 5339  C   VAL B 319     4142   3515   7995    590   -247    275       C
ATOM   5340  O   VAL B 319     -47.797  18.963  27.187  1.00 42.18           O
ANISOU 5340  O   VAL B 319     4374   3772   7883    467   -221    278       O
ATOM   5341  CB  VAL B 319     -45.944  18.556  29.509  1.00 48.11           C
ANISOU 5341  CB  VAL B 319     4859   4442   8981    687   -670    488       C
ATOM   5342  CG1 VAL B 319     -46.885  17.598  30.218  1.00 51.76           C
ANISOU 5342  CG1 VAL B 319     5524   4806   9335    708   -772    615       C
ATOM   5343  CG2 VAL B 319     -44.612  18.639  30.239  1.00 47.93           C
ANISOU 5343  CG2 VAL B 319     4614   4399   9200    786   -863    535       C
ATOM   5344  N   LYS B 320     -47.375  16.765  26.885  1.00 42.26           N
ANISOU 5344  N   LYS B 320     4346   3501   8208    639   -162    238       N
ATOM   5345  CA  LYS B 320     -48.626  16.475  26.198  1.00 42.37           C
ANISOU 5345  CA  LYS B 320     4567   3505   8025    538    -43    199       C
ATOM   5346  C   LYS B 320     -49.609  15.865  27.188  1.00 43.82           C
ANISOU 5346  C   LYS B 320     4911   3636   8103    535   -198    351       C
ATOM   5347  O   LYS B 320     -49.312  14.843  27.814  1.00 52.54           O
ANISOU 5347  O   LYS B 320     6009   4593   9362    640   -299    428       O
ATOM   5348  CB  LYS B 320     -48.397  15.530  25.019  1.00 46.39           C
ANISOU 5348  CB  LYS B 320     5077   3880   8671    565    164     42       C
ATOM   5349  CG  LYS B 320     -47.520  16.103  23.919  1.00 53.69           C
ANISOU 5349  CG  LYS B 320     5874   4858   9667    536    372   -127       C
ATOM   5350  CD  LYS B 320     -47.332  15.101  22.790  1.00 65.66           C
ANISOU 5350  CD  LYS B 320     7421   6229  11299    556    597   -298       C
ATOM   5351  CE  LYS B 320     -46.425  15.653  21.701  1.00 73.51           C
ANISOU 5351  CE  LYS B 320     8301   7276  12354    511    840   -475       C
ATOM   5352  NZ  LYS B 320     -46.214  14.669  20.603  1.00 78.50           N
ANISOU 5352  NZ  LYS B 320     8978   7760  13087    524   1087   -664       N
ATOM   5353  N   VAL B 321     -50.773  16.494  27.329  1.00 41.02           N
ANISOU 5353  N   VAL B 321     4697   3392   7495    414   -211    397       N
ATOM   5354  CA  VAL B 321     -51.834  16.019  28.207  1.00 40.50           C
ANISOU 5354  CA  VAL B 321     4786   3296   7307    379   -312    527       C
ATOM   5355  C   VAL B 321     -53.093  15.843  27.372  1.00 38.68           C
ANISOU 5355  C   VAL B 321     4687   3070   6938    262   -191    465       C
ATOM   5356  O   VAL B 321     -53.433  16.712  26.561  1.00 36.64           O
ANISOU 5356  O   VAL B 321     4433   2922   6567    178   -107    381       O
ATOM   5357  CB  VAL B 321     -52.086  16.989  29.376  1.00 41.10           C
ANISOU 5357  CB  VAL B 321     4888   3505   7225    341   -453    643       C
ATOM   5358  CG1 VAL B 321     -53.130  16.418  30.325  1.00 40.71           C
ANISOU 5358  CG1 VAL B 321     5000   3415   7051    295   -525    773       C
ATOM   5359  CG2 VAL B 321     -50.790  17.280  30.114  1.00 44.09           C
ANISOU 5359  CG2 VAL B 321     5131   3891   7731    437   -596    693       C
ATOM   5360  N   THR B 322     -53.778  14.719  27.566  1.00 40.64           N
ANISOU 5360  N   THR B 322     5048   3192   7202    251   -199    513       N
ATOM   5361  CA  THR B 322     -55.015  14.444  26.844  1.00 37.71           C
ANISOU 5361  CA  THR B 322     4794   2814   6721    132   -112    461       C
ATOM   5362  C   THR B 322     -56.169  15.114  27.578  1.00 37.99           C
ANISOU 5362  C   THR B 322     4890   2970   6573     35   -171    555       C
ATOM   5363  O   THR B 322     -56.516  14.723  28.697  1.00 38.81           O
ANISOU 5363  O   THR B 322     5054   3042   6651     36   -250    682       O
ATOM   5364  CB  THR B 322     -55.241  12.941  26.715  1.00 37.08           C
ANISOU 5364  CB  THR B 322     4803   2533   6754    148    -87    461       C
ATOM   5365  OG1 THR B 322     -54.097  12.340  26.096  1.00 38.58           O
ANISOU 5365  OG1 THR B 322     4918   2596   7144    258    -19    360       O
ATOM   5366  CG2 THR B 322     -56.469  12.664  25.862  1.00 39.10           C
ANISOU 5366  CG2 THR B 322     5168   2780   6907      8     -6    390       C
ATOM   5367  N   ILE B 323     -56.753  16.134  26.953  1.00 34.59           N
ANISOU 5367  N   ILE B 323     4450   2672   6019    -48   -128    492       N
ATOM   5368  CA  ILE B 323     -57.872  16.883  27.511  1.00 34.57           C
ANISOU 5368  CA  ILE B 323     4476   2784   5875   -130   -163    552       C
ATOM   5369  C   ILE B 323     -58.953  16.967  26.444  1.00 33.55           C
ANISOU 5369  C   ILE B 323     4384   2676   5686   -240   -108    474       C
ATOM   5370  O   ILE B 323     -58.664  17.312  25.294  1.00 35.64           O
ANISOU 5370  O   ILE B 323     4643   2958   5941   -260    -63    372       O
ATOM   5371  CB  ILE B 323     -57.450  18.294  27.964  1.00 30.98           C
ANISOU 5371  CB  ILE B 323     3952   2472   5347   -107   -208    566       C
ATOM   5372  CG1 ILE B 323     -56.265  18.215  28.929  1.00 31.72           C
ANISOU 5372  CG1 ILE B 323     4002   2543   5507     -7   -292    635       C
ATOM   5373  CG2 ILE B 323     -58.617  19.020  28.614  1.00 30.21           C
ANISOU 5373  CG2 ILE B 323     3881   2471   5125   -177   -226    615       C
ATOM   5374  CD1 ILE B 323     -55.700  19.562  29.312  1.00 38.66           C
ANISOU 5374  CD1 ILE B 323     4813   3547   6328      8   -343    634       C
ATOM   5375  N   ASP B 324     -60.192  16.651  26.824  1.00 33.32           N
ANISOU 5375  N   ASP B 324     4398   2644   5619   -320   -116    524       N
ATOM   5376  CA  ASP B 324     -61.316  16.621  25.886  1.00 34.74           C
ANISOU 5376  CA  ASP B 324     4599   2833   5768   -431    -99    461       C
ATOM   5377  C   ASP B 324     -61.021  15.702  24.701  1.00 34.40           C
ANISOU 5377  C   ASP B 324     4623   2672   5776   -456    -54    362       C
ATOM   5378  O   ASP B 324     -61.350  16.014  23.555  1.00 32.18           O
ANISOU 5378  O   ASP B 324     4369   2417   5442   -527    -50    274       O
ATOM   5379  CB  ASP B 324     -61.678  18.028  25.402  1.00 37.08           C
ANISOU 5379  CB  ASP B 324     4842   3265   5983   -460   -128    424       C
ATOM   5380  CG  ASP B 324     -62.195  18.915  26.515  1.00 38.28           C
ANISOU 5380  CG  ASP B 324     4935   3517   6092   -449   -154    497       C
ATOM   5381  OD1 ASP B 324     -62.768  18.382  27.487  1.00 38.18           O
ANISOU 5381  OD1 ASP B 324     4933   3482   6090   -471   -136    567       O
ATOM   5382  OD2 ASP B 324     -62.033  20.150  26.412  1.00 37.99           O
ANISOU 5382  OD2 ASP B 324     4854   3573   6007   -427   -180    479       O
ATOM   5383  N   TYR B 325     -60.379  14.568  24.985  1.00 33.33           N
ANISOU 5383  N   TYR B 325     4528   2396   5741   -397    -26    375       N
ATOM   5384  CA  TYR B 325     -60.012  13.529  24.024  1.00 34.54           C
ANISOU 5384  CA  TYR B 325     4753   2402   5967   -403     38    272       C
ATOM   5385  C   TYR B 325     -58.950  13.971  23.026  1.00 37.50           C
ANISOU 5385  C   TYR B 325     5109   2797   6343   -357    109    151       C
ATOM   5386  O   TYR B 325     -58.718  13.267  22.035  1.00 37.17           O
ANISOU 5386  O   TYR B 325     5142   2649   6332   -383    190     31       O
ATOM   5387  CB  TYR B 325     -61.225  13.003  23.248  1.00 35.03           C
ANISOU 5387  CB  TYR B 325     4899   2421   5991   -550     37    217       C
ATOM   5388  CG  TYR B 325     -62.245  12.286  24.098  1.00 42.05           C
ANISOU 5388  CG  TYR B 325     5810   3254   6914   -617      3    317       C
ATOM   5389  CD1 TYR B 325     -61.957  11.055  24.670  1.00 41.71           C
ANISOU 5389  CD1 TYR B 325     5831   3040   6978   -581     21    368       C
ATOM   5390  CD2 TYR B 325     -63.502  12.833  24.315  1.00 43.11           C
ANISOU 5390  CD2 TYR B 325     5896   3494   6988   -721    -41    360       C
ATOM   5391  CE1 TYR B 325     -62.890  10.392  25.445  1.00 45.64           C
ANISOU 5391  CE1 TYR B 325     6366   3479   7494   -666      5    466       C
ATOM   5392  CE2 TYR B 325     -64.442  12.177  25.087  1.00 44.77           C
ANISOU 5392  CE2 TYR B 325     6115   3657   7237   -801    -42    443       C
ATOM   5393  CZ  TYR B 325     -64.132  10.958  25.650  1.00 44.56           C
ANISOU 5393  CZ  TYR B 325     6175   3465   7291   -783    -14    499       C
ATOM   5394  OH  TYR B 325     -65.065  10.303  26.420  1.00 47.02           O
ANISOU 5394  OH  TYR B 325     6513   3723   7630   -884     -1    590       O
ATOM   5395  N   THR B 326     -58.296  15.108  23.248  1.00 30.90           N
ANISOU 5395  N   THR B 326     3007   3047   5687    394   -206    553       N
ATOM   5396  CA  THR B 326     -57.222  15.557  22.375  1.00 31.53           C
ANISOU 5396  CA  THR B 326     3098   3228   5654    330   -150    488       C
ATOM   5397  C   THR B 326     -55.983  15.852  23.208  1.00 35.93           C
ANISOU 5397  C   THR B 326     3632   3701   6318    414   -102    468       C
ATOM   5398  O   THR B 326     -56.075  16.200  24.389  1.00 36.79           O
ANISOU 5398  O   THR B 326     3762   3704   6511    506   -146    564       O
ATOM   5399  CB  THR B 326     -57.632  16.798  21.556  1.00 40.22           C
ANISOU 5399  CB  THR B 326     4251   4445   6586    227   -237    666       C
ATOM   5400  OG1 THR B 326     -56.718  16.978  20.467  1.00 44.12           O
ANISOU 5400  OG1 THR B 326     4771   5128   6864     38   -156    610       O
ATOM   5401  CG2 THR B 326     -57.630  18.051  22.417  1.00 31.58           C
ANISOU 5401  CG2 THR B 326     3173   3214   5613    330   -304    824       C
ATOM   5402  N  AGLU B 327     -54.817  15.691  22.586  0.49 37.14           N
ANISOU 5402  N  AGLU B 327     3714   3944   6456    358     -2    301       N
ATOM   5403  N  BGLU B 327     -54.819  15.704  22.581  0.51 37.12           N
ANISOU 5403  N  BGLU B 327     3711   3942   6450    357     -2    302       N
ATOM   5404  CA AGLU B 327     -53.552  15.939  23.267  0.49 38.89           C
ANISOU 5404  CA AGLU B 327     3852   4109   6816    426     21    250       C
ATOM   5405  CA BGLU B 327     -53.548  15.941  23.254  0.51 38.91           C
ANISOU 5405  CA BGLU B 327     3854   4114   6817    424     22    249       C
ATOM   5406  C  AGLU B 327     -53.249  17.432  23.260  0.49 38.30           C
ANISOU 5406  C  AGLU B 327     3825   4095   6631    329     22    417       C
ATOM   5407  C  BGLU B 327     -53.239  17.434  23.258  0.51 38.31           C
ANISOU 5407  C  BGLU B 327     3826   4098   6633    328     22    416       C
ATOM   5408  O  AGLU B 327     -53.123  18.043  22.194  0.49 37.97           O
ANISOU 5408  O  AGLU B 327     3807   4222   6397    132     83    461       O
ATOM   5409  O  BGLU B 327     -53.101  18.048  22.194  0.51 37.98           O
ANISOU 5409  O  BGLU B 327     3806   4224   6398    131     85    460       O
ATOM   5410  CB AGLU B 327     -52.418  15.157  22.608  0.49 42.17           C
ANISOU 5410  CB AGLU B 327     4080   4608   7333    413    144    -70       C
ATOM   5411  CB BGLU B 327     -52.428  15.161  22.569  0.51 42.18           C
ANISOU 5411  CB BGLU B 327     4082   4617   7328    407    148    -73       C
ATOM   5412  CG AGLU B 327     -52.220  13.758  23.169  0.49 45.19           C
ANISOU 5412  CG AGLU B 327     4375   4750   8045    598     43   -238       C
ATOM   5413  CG BGLU B 327     -51.857  14.010  23.391  0.51 44.72           C
ANISOU 5413  CG BGLU B 327     4286   4693   8012    613     38   -220       C
ATOM   5414  CD AGLU B 327     -50.849  13.191  22.849  0.49 49.87           C
ANISOU 5414  CD AGLU B 327     4692   5354   8901    674    119   -602       C
ATOM   5415  CD BGLU B 327     -52.686  12.739  23.305  0.51 46.58           C
ANISOU 5415  CD BGLU B 327     4573   4751   8375    669    -46   -291       C
ATOM   5416  OE1AGLU B 327     -50.214  13.673  21.887  0.49 53.10           O
ANISOU 5416  OE1AGLU B 327     4965   6062   9147    519    344   -808       O
ATOM   5417  OE1BGLU B 327     -53.926  12.829  23.184  0.51 45.97           O
ANISOU 5417  OE1BGLU B 327     4649   4703   8114    585    -66   -125       O
ATOM   5418  OE2AGLU B 327     -50.403  12.270  23.565  0.49 51.48           O
ANISOU 5418  OE2AGLU B 327     4797   5272   9489    872    -62   -680       O
ATOM   5419  OE2BGLU B 327     -52.091  11.642  23.354  0.51 50.27           O
ANISOU 5419  OE2BGLU B 327     4900   5018   9180    797   -117   -528       O
ATOM   5420  N   ILE B 328     -53.132  18.015  24.450  1.00 37.69           N
ANISOU 5420  N   ILE B 328     3780   3880   6662    427    -66    513       N
ATOM   5421  CA  ILE B 328     -52.808  19.427  24.614  1.00 37.25           C
ANISOU 5421  CA  ILE B 328     3768   3792   6591    351   -103    631       C
ATOM   5422  C   ILE B 328     -51.350  19.539  25.036  1.00 41.11           C
ANISOU 5422  C   ILE B 328     4131   4302   7188    327    -74    522       C
ATOM   5423  O   ILE B 328     -50.932  18.924  26.025  1.00 40.80           O
ANISOU 5423  O   ILE B 328     4031   4192   7279    461   -145    445       O
ATOM   5424  CB  ILE B 328     -53.732  20.097  25.645  1.00 39.33           C
ANISOU 5424  CB  ILE B 328     4121   3904   6917    466   -211    713       C
ATOM   5425  CG1 ILE B 328     -55.192  19.986  25.203  1.00 42.99           C
ANISOU 5425  CG1 ILE B 328     4624   4365   7343    502   -249    783       C
ATOM   5426  CG2 ILE B 328     -53.348  21.555  25.830  1.00 38.42           C
ANISOU 5426  CG2 ILE B 328     4047   3675   6877    404   -283    776       C
ATOM   5427  CD1 ILE B 328     -55.497  20.725  23.919  1.00 42.09           C
ANISOU 5427  CD1 ILE B 328     4563   4269   7159    369   -326    941       C
ATOM   5428  N   SER B 329     -50.576  20.318  24.286  1.00 43.78           N
ANISOU 5428  N   SER B 329     4421   4747   7465    120      3    543       N
ATOM   5429  CA  SER B 329     -49.162  20.509  24.575  1.00 42.56           C
ANISOU 5429  CA  SER B 329     4083   4653   7434     53     46    417       C
ATOM   5430  C   SER B 329     -48.980  21.669  25.545  1.00 43.89           C
ANISOU 5430  C   SER B 329     4332   4648   7697     42    -99    521       C
ATOM   5431  O   SER B 329     -49.590  22.731  25.379  1.00 38.71           O
ANISOU 5431  O   SER B 329     3842   3864   7002    -47   -170    694       O
ATOM   5432  CB  SER B 329     -48.377  20.767  23.288  1.00 44.86           C
ANISOU 5432  CB  SER B 329     4249   5211   7583   -248    249    359       C
ATOM   5433  OG  SER B 329     -48.356  19.615  22.464  1.00 49.46           O
ANISOU 5433  OG  SER B 329     4702   5994   8097   -235    414    125       O
ATOM   5434  N   PHE B 330     -48.145  21.458  26.558  1.00 48.38           N
ANISOU 5434  N   PHE B 330     4774   5187   8419    135   -185    399       N
ATOM   5435  CA  PHE B 330     -47.808  22.482  27.533  1.00 47.12           C
ANISOU 5435  CA  PHE B 330     4667   4902   8337     97   -325    415       C
ATOM   5436  C   PHE B 330     -46.312  22.753  27.496  1.00 52.46           C
ANISOU 5436  C   PHE B 330     5099   5681   9151    -59   -313    305       C
ATOM   5437  O   PHE B 330     -45.510  21.864  27.194  1.00 60.81           O
ANISOU 5437  O   PHE B 330     5899   6895  10312    -21   -245    152       O
ATOM   5438  CB  PHE B 330     -48.213  22.064  28.952  1.00 43.35           C
ANISOU 5438  CB  PHE B 330     4273   4350   7848    288   -487    375       C
ATOM   5439  CG  PHE B 330     -49.693  22.091  29.198  1.00 41.74           C
ANISOU 5439  CG  PHE B 330     4266   4073   7520    387   -474    436       C
ATOM   5440  CD1 PHE B 330     -50.506  21.070  28.735  1.00 42.92           C
ANISOU 5440  CD1 PHE B 330     4441   4268   7600    475   -404    490       C
ATOM   5441  CD2 PHE B 330     -50.269  23.132  29.907  1.00 42.71           C
ANISOU 5441  CD2 PHE B 330     4506   4084   7639    388   -528    383       C
ATOM   5442  CE1 PHE B 330     -51.868  21.091  28.966  1.00 31.21           C
ANISOU 5442  CE1 PHE B 330     3074   2753   6030    544   -382    523       C
ATOM   5443  CE2 PHE B 330     -51.629  23.159  30.141  1.00 41.12           C
ANISOU 5443  CE2 PHE B 330     4397   3851   7375    490   -488    364       C
ATOM   5444  CZ  PHE B 330     -52.430  22.136  29.669  1.00 39.02           C
ANISOU 5444  CZ  PHE B 330     4133   3666   7026    558   -412    450       C
ATOM   5445  N   MET B 331     -45.941  23.991  27.804  1.00 48.05           N
ANISOU 5445  N   MET B 331     4588   5019   8651   -232   -389    344       N
ATOM   5446  CA  MET B 331     -44.545  24.371  27.958  1.00 49.42           C
ANISOU 5446  CA  MET B 331     4514   5284   8979   -412   -410    233       C
ATOM   5447  C   MET B 331     -44.214  24.412  29.443  1.00 45.56           C
ANISOU 5447  C   MET B 331     4018   4711   8580   -282   -663    122       C
ATOM   5448  O   MET B 331     -44.789  25.212  30.188  1.00 44.48           O
ANISOU 5448  O   MET B 331     4104   4398   8398   -277   -784    130       O
ATOM   5449  CB  MET B 331     -44.260  25.723  27.304  1.00 57.97           C
ANISOU 5449  CB  MET B 331     5659   6294  10074   -772   -361    370       C
ATOM   5450  CG  MET B 331     -43.966  25.639  25.816  1.00 66.39           C
ANISOU 5450  CG  MET B 331     6624   7602  10998  -1059   -105    461       C
ATOM   5451  SD  MET B 331     -42.623  24.491  25.444  1.00 75.15           S
ANISOU 5451  SD  MET B 331     7229   9124  12202  -1071    120    127       S
ATOM   5452  CE  MET B 331     -41.296  25.164  26.442  1.00 74.00           C
ANISOU 5452  CE  MET B 331     6819   8946  12354  -1189    -51    -10       C
ATOM   5453  N   LEU B 332     -43.298  23.548  29.868  1.00 48.59           N
ANISOU 5453  N   LEU B 332     4134   5227   9101   -180   -766     -7       N
ATOM   5454  CA  LEU B 332     -42.868  23.468  31.259  1.00 50.22           C
ANISOU 5454  CA  LEU B 332     4326   5407   9347    -98  -1074    -70       C
ATOM   5455  C   LEU B 332     -41.472  24.067  31.370  1.00 52.13           C
ANISOU 5455  C   LEU B 332     4260   5732   9814   -297  -1163   -205       C
ATOM   5456  O   LEU B 332     -40.500  23.487  30.876  1.00 54.87           O
ANISOU 5456  O   LEU B 332     4222   6232  10395   -291  -1119   -323       O
ATOM   5457  CB  LEU B 332     -42.883  22.025  31.757  1.00 50.54           C
ANISOU 5457  CB  LEU B 332     4300   5475   9427    160  -1251    -47       C
ATOM   5458  CG  LEU B 332     -42.319  21.819  33.164  1.00 54.25           C
ANISOU 5458  CG  LEU B 332     4753   5957   9903    196  -1650    -40       C
ATOM   5459  CD1 LEU B 332     -43.160  22.558  34.196  1.00 52.43           C
ANISOU 5459  CD1 LEU B 332     4889   5708   9326    104  -1722     -6       C
ATOM   5460  CD2 LEU B 332     -42.220  20.339  33.500  1.00 58.32           C
ANISOU 5460  CD2 LEU B 332     5188   6429  10543    424  -1896     60       C
ATOM   5461  N   TRP B 333     -41.378  25.225  32.014  1.00 50.51           N
ANISOU 5461  N   TRP B 333     4189   5427   9576   -476  -1283   -238       N
ATOM   5462  CA  TRP B 333     -40.105  25.870  32.296  1.00 54.72           C
ANISOU 5462  CA  TRP B 333     4450   6021  10319   -703  -1418   -372       C
ATOM   5463  C   TRP B 333     -39.800  25.727  33.779  1.00 54.88           C
ANISOU 5463  C   TRP B 333     4500   6066  10286   -624  -1807   -459       C
ATOM   5464  O   TRP B 333     -40.628  26.083  34.623  1.00 54.51           O
ANISOU 5464  O   TRP B 333     4794   5930   9986   -594  -1903   -469       O
ATOM   5465  CB  TRP B 333     -40.134  27.347  31.899  1.00 58.89           C
ANISOU 5465  CB  TRP B 333     5112   6379  10884  -1030  -1316   -350       C
ATOM   5466  CG  TRP B 333     -40.198  27.566  30.422  1.00 60.44           C
ANISOU 5466  CG  TRP B 333     5265   6609  11093  -1231   -996   -200       C
ATOM   5467  CD1 TRP B 333     -41.321  27.668  29.655  1.00 59.44           C
ANISOU 5467  CD1 TRP B 333     5425   6358  10802  -1194   -831     -7       C
ATOM   5468  CD2 TRP B 333     -39.087  27.712  29.529  1.00 64.98           C
ANISOU 5468  CD2 TRP B 333     5476   7406  11809  -1551   -808   -230       C
ATOM   5469  NE1 TRP B 333     -40.980  27.869  28.340  1.00 62.60           N
ANISOU 5469  NE1 TRP B 333     5714   6895  11177  -1495   -583    125       N
ATOM   5470  CE2 TRP B 333     -39.614  27.899  28.236  1.00 65.63           C
ANISOU 5470  CE2 TRP B 333     5695   7516  11726  -1738   -526    -23       C
ATOM   5471  CE3 TRP B 333     -37.699  27.703  29.697  1.00 70.31           C
ANISOU 5471  CE3 TRP B 333     5693   8297  12724  -1726   -851   -424       C
ATOM   5472  CZ2 TRP B 333     -38.802  28.076  27.118  1.00 70.87           C
ANISOU 5472  CZ2 TRP B 333     6086   8462  12380  -2142   -245     -4       C
ATOM   5473  CZ3 TRP B 333     -36.894  27.878  28.586  1.00 73.58           C
ANISOU 5473  CZ3 TRP B 333     5779   8979  13200  -2094   -546   -447       C
ATOM   5474  CH2 TRP B 333     -37.448  28.062  27.313  1.00 73.92           C
ANISOU 5474  CH2 TRP B 333     5999   9089  12998  -2323   -226   -237       C
ATOM   5475  N   CYS B 334     -38.620  25.197  34.093  1.00 56.14           N
ANISOU 5475  N   CYS B 334     4280   6375  10677   -604  -2038   -544       N
ATOM   5476  CA  CYS B 334     -38.205  25.002  35.472  1.00 58.51           C
ANISOU 5476  CA  CYS B 334     4589   6734  10908   -570  -2492   -578       C
ATOM   5477  C   CYS B 334     -36.820  25.593  35.682  1.00 72.11           C
ANISOU 5477  C   CYS B 334     5920   8555  12925   -793  -2693   -754       C
ATOM   5478  O   CYS B 334     -36.026  25.712  34.745  1.00 75.93           O
ANISOU 5478  O   CYS B 334     6005   9116  13730   -905  -2489   -848       O
ATOM   5479  CB  CYS B 334     -38.203  23.520  35.861  1.00 58.75           C
ANISOU 5479  CB  CYS B 334     4547   6807  10969   -274  -2756   -435       C
ATOM   5480  SG  CYS B 334     -39.801  22.704  35.681  1.00 65.04           S
ANISOU 5480  SG  CYS B 334     5772   7501  11440    -62  -2551   -217       S
ATOM   5481  N   LYS B 335     -36.540  25.957  36.931  1.00 73.64           N
ANISOU 5481  N   LYS B 335     6215   8792  12973   -896  -3086   -822       N
ATOM   5482  CA  LYS B 335     -35.272  26.582  37.288  1.00 79.09           C
ANISOU 5482  CA  LYS B 335     6553   9577  13921  -1139  -3344  -1006       C
ATOM   5483  C   LYS B 335     -34.990  26.279  38.750  1.00 81.09           C
ANISOU 5483  C   LYS B 335     6892   9954  13964  -1128  -3913   -998       C
ATOM   5484  O   LYS B 335     -35.773  26.669  39.620  1.00 81.78           O
ANISOU 5484  O   LYS B 335     7432  10042  13597  -1209  -3992  -1020       O
ATOM   5485  CB  LYS B 335     -35.321  28.094  37.052  1.00 84.45           C
ANISOU 5485  CB  LYS B 335     7370  10113  14603  -1492  -3134  -1159       C
ATOM   5486  CG  LYS B 335     -33.963  28.766  36.930  1.00 93.96           C
ANISOU 5486  CG  LYS B 335     8163  11408  16129  -1794  -3209  -1318       C
ATOM   5487  CD  LYS B 335     -33.457  28.721  35.496  1.00 99.58           C
ANISOU 5487  CD  LYS B 335     8549  12198  17090  -1882  -2762  -1269       C
ATOM   5488  CE  LYS B 335     -32.290  29.674  35.290  1.00108.31           C
ANISOU 5488  CE  LYS B 335     9402  13399  18352  -2268  -2691  -1385       C
ATOM   5489  NZ  LYS B 335     -31.912  29.785  33.853  1.00111.09           N
ANISOU 5489  NZ  LYS B 335     9503  13882  18825  -2478  -2216  -1328       N
ATOM   5490  N   ASP B 336     -33.886  25.576  39.011  1.00 84.07           N
ANISOU 5490  N   ASP B 336     6956  10468  14519  -1002  -4162   -948       N
ATOM   5491  CA  ASP B 336     -33.427  25.294  40.372  1.00 87.37           C
ANISOU 5491  CA  ASP B 336     7473  11031  14693  -1024  -4698   -875       C
ATOM   5492  C   ASP B 336     -34.487  24.545  41.181  1.00 84.28           C
ANISOU 5492  C   ASP B 336     7521  10650  13852   -921  -4956   -625       C
ATOM   5493  O   ASP B 336     -34.861  24.947  42.285  1.00 85.01           O
ANISOU 5493  O   ASP B 336     7948  10886  13466  -1140  -5232   -652       O
ATOM   5494  CB  ASP B 336     -33.003  26.582  41.084  1.00 90.83           C
ANISOU 5494  CB  ASP B 336     7971  11565  14976  -1395  -4842  -1123       C
ATOM   5495  CG  ASP B 336     -31.849  27.279  40.389  1.00 92.93           C
ANISOU 5495  CG  ASP B 336     7803  11849  15655  -1558  -4636  -1312       C
ATOM   5496  OD1 ASP B 336     -31.280  26.693  39.445  1.00 92.96           O
ANISOU 5496  OD1 ASP B 336     7431  11866  16024  -1384  -4406  -1275       O
ATOM   5497  OD2 ASP B 336     -31.513  28.415  40.786  1.00 94.46           O
ANISOU 5497  OD2 ASP B 336     8040  12061  15789  -1887  -4686  -1524       O
ATOM   5498  N   GLY B 337     -34.975  23.442  40.618  1.00 81.26           N
ANISOU 5498  N   GLY B 337     7150  10140  13584   -624  -4837   -400       N
ATOM   5499  CA  GLY B 337     -35.879  22.560  41.325  1.00 81.58           C
ANISOU 5499  CA  GLY B 337     7585  10186  13225   -546  -5078    -88       C
ATOM   5500  C   GLY B 337     -37.314  23.027  41.431  1.00 76.74           C
ANISOU 5500  C   GLY B 337     7432   9601  12123   -673  -4781   -113       C
ATOM   5501  O   GLY B 337     -38.120  22.344  42.075  1.00 72.56           O
ANISOU 5501  O   GLY B 337     7269   9144  11158   -680  -4903    143       O
ATOM   5502  N   HIS B 338     -37.662  24.163  40.834  1.00 72.93           N
ANISOU 5502  N   HIS B 338     6998   9057  11656   -778  -4296   -402       N
ATOM   5503  CA  HIS B 338     -39.033  24.647  40.810  1.00 70.95           C
ANISOU 5503  CA  HIS B 338     7169   8781  11007   -821  -3871   -481       C
ATOM   5504  C   HIS B 338     -39.379  25.085  39.395  1.00 64.27           C
ANISOU 5504  C   HIS B 338     6214   7705  10500   -712  -3352   -561       C
ATOM   5505  O   HIS B 338     -38.498  25.343  38.572  1.00 62.78           O
ANISOU 5505  O   HIS B 338     5665   7440  10748   -725  -3282   -628       O
ATOM   5506  CB  HIS B 338     -39.246  25.810  41.791  1.00 78.04           C
ANISOU 5506  CB  HIS B 338     8321   9814  11518  -1112  -3910   -802       C
ATOM   5507  CG  HIS B 338     -38.381  27.001  41.517  1.00 84.43           C
ANISOU 5507  CG  HIS B 338     8895  10508  12677  -1286  -3903  -1104       C
ATOM   5508  ND1 HIS B 338     -37.289  27.322  42.294  1.00 90.36           N
ANISOU 5508  ND1 HIS B 338     9473  11409  13449  -1500  -4348  -1232       N
ATOM   5509  CD2 HIS B 338     -38.448  27.951  40.553  1.00 84.35           C
ANISOU 5509  CD2 HIS B 338     8803  10236  13009  -1321  -3541  -1267       C
ATOM   5510  CE1 HIS B 338     -36.721  28.417  41.822  1.00 91.24           C
ANISOU 5510  CE1 HIS B 338     9394  11354  13920  -1666  -4227  -1490       C
ATOM   5511  NE2 HIS B 338     -37.403  28.818  40.765  1.00 87.07           N
ANISOU 5511  NE2 HIS B 338     8932  10563  13587  -1574  -3746  -1488       N
ATOM   5512  N   VAL B 339     -40.675  25.173  39.118  1.00 62.92           N
ANISOU 5512  N   VAL B 339     6345   7461  10101   -641  -2998   -548       N
ATOM   5513  CA  VAL B 339     -41.132  25.566  37.791  1.00 63.73           C
ANISOU 5513  CA  VAL B 339     6401   7353  10459   -560  -2568   -561       C
ATOM   5514  C   VAL B 339     -41.100  27.083  37.672  1.00 65.19           C
ANISOU 5514  C   VAL B 339     6638   7378  10753   -764  -2441   -819       C
ATOM   5515  O   VAL B 339     -41.344  27.812  38.642  1.00 63.53           O
ANISOU 5515  O   VAL B 339     6620   7193  10325   -897  -2549  -1061       O
ATOM   5516  CB  VAL B 339     -42.541  25.012  37.500  1.00 61.68           C
ANISOU 5516  CB  VAL B 339     6401   7058   9977   -390  -2301   -429       C
ATOM   5517  CG1 VAL B 339     -42.604  23.529  37.800  1.00 67.04           C
ANISOU 5517  CG1 VAL B 339     7082   7843  10545   -242  -2494   -162       C
ATOM   5518  CG2 VAL B 339     -43.599  25.762  38.284  1.00 59.16           C
ANISOU 5518  CG2 VAL B 339     6395   6769   9313   -474  -2194   -639       C
ATOM   5519  N   GLU B 340     -40.768  27.562  36.475  1.00 70.81           N
ANISOU 5519  N   GLU B 340     7178   7924  11804   -824  -2225   -778       N
ATOM   5520  CA  GLU B 340     -40.908  28.972  36.130  1.00 74.33           C
ANISOU 5520  CA  GLU B 340     7720   8104  12417  -1023  -2108   -920       C
ATOM   5521  C   GLU B 340     -42.329  29.264  35.658  1.00 66.02           C
ANISOU 5521  C   GLU B 340     6951   6839  11296   -884  -1859   -878       C
ATOM   5522  O   GLU B 340     -43.032  30.094  36.244  1.00 63.72           O
ANISOU 5522  O   GLU B 340     6872   6376  10964   -891  -1875  -1114       O
ATOM   5523  CB  GLU B 340     -39.892  29.356  35.047  1.00 85.41           C
ANISOU 5523  CB  GLU B 340     8825   9458  14170  -1244  -2012   -825       C
ATOM   5524  CG  GLU B 340     -38.471  29.570  35.542  1.00 97.07           C
ANISOU 5524  CG  GLU B 340     9978  11075  15830  -1464  -2266   -967       C
ATOM   5525  CD  GLU B 340     -38.147  31.037  35.750  1.00108.73           C
ANISOU 5525  CD  GLU B 340    11523  12303  17487  -1799  -2353  -1146       C
ATOM   5526  OE1 GLU B 340     -38.153  31.493  36.913  1.00113.76           O
ANISOU 5526  OE1 GLU B 340    12296  12917  18010  -1847  -2607  -1406       O
ATOM   5527  OE2 GLU B 340     -37.896  31.739  34.747  1.00112.98           O
ANISOU 5527  OE2 GLU B 340    11995  12667  18266  -2051  -2177  -1028       O
ATOM   5528  N   THR B 341     -42.761  28.582  34.600  1.00 58.76           N
ANISOU 5528  N   THR B 341     6002   5933  10392   -749  -1643   -626       N
ATOM   5529  CA  THR B 341     -44.117  28.712  34.093  1.00 57.53           C
ANISOU 5529  CA  THR B 341     6068   5607  10184   -600  -1453   -552       C
ATOM   5530  C   THR B 341     -44.553  27.367  33.530  1.00 57.39           C
ANISOU 5530  C   THR B 341     6011   5776  10018   -400  -1311   -339       C
ATOM   5531  O   THR B 341     -43.737  26.471  33.298  1.00 58.43           O
ANISOU 5531  O   THR B 341     5926   6095  10179   -384  -1337   -255       O
ATOM   5532  CB  THR B 341     -44.222  29.807  33.026  1.00 59.10           C
ANISOU 5532  CB  THR B 341     6315   5481  10658   -767  -1374   -437       C
ATOM   5533  OG1 THR B 341     -45.579  29.910  32.577  1.00 60.20           O
ANISOU 5533  OG1 THR B 341     6644   5442  10789   -588  -1269   -359       O
ATOM   5534  CG2 THR B 341     -43.326  29.482  31.841  1.00 56.64           C
ANISOU 5534  CG2 THR B 341     5786   5306  10427   -955  -1252   -195       C
ATOM   5535  N   PHE B 342     -45.862  27.238  33.313  1.00 53.74           N
ANISOU 5535  N   PHE B 342     5728   5237   9452   -239  -1177   -294       N
ATOM   5536  CA  PHE B 342     -46.427  26.002  32.774  1.00 50.27           C
ANISOU 5536  CA  PHE B 342     5279   4936   8884    -71  -1049   -114       C
ATOM   5537  C   PHE B 342     -47.766  26.365  32.134  1.00 53.00           C
ANISOU 5537  C   PHE B 342     5775   5118   9243     22   -908    -56       C
ATOM   5538  O   PHE B 342     -48.785  26.437  32.826  1.00 58.64           O
ANISOU 5538  O   PHE B 342     6605   5824   9852    139   -888   -192       O
ATOM   5539  CB  PHE B 342     -46.585  24.948  33.857  1.00 48.08           C
ANISOU 5539  CB  PHE B 342     5040   4865   8362     38  -1157   -135       C
ATOM   5540  CG  PHE B 342     -47.140  23.648  33.361  1.00 47.26           C
ANISOU 5540  CG  PHE B 342     4934   4839   8183    187  -1066     47       C
ATOM   5541  CD1 PHE B 342     -46.349  22.774  32.634  1.00 49.84           C
ANISOU 5541  CD1 PHE B 342     5059   5208   8670    230  -1075    143       C
ATOM   5542  CD2 PHE B 342     -48.452  23.295  33.625  1.00 46.43           C
ANISOU 5542  CD2 PHE B 342     4993   4766   7884    273   -965     68       C
ATOM   5543  CE1 PHE B 342     -46.858  21.573  32.177  1.00 51.22           C
ANISOU 5543  CE1 PHE B 342     5234   5401   8827    365  -1013    255       C
ATOM   5544  CE2 PHE B 342     -48.967  22.096  33.171  1.00 44.35           C
ANISOU 5544  CE2 PHE B 342     4730   4543   7577    373   -904    232       C
ATOM   5545  CZ  PHE B 342     -48.170  21.234  32.447  1.00 47.73           C
ANISOU 5545  CZ  PHE B 342     4995   4960   8182    424   -942    325       C
ATOM   5546  N   TYR B 343     -47.750  26.588  30.824  1.00 49.19           N
ANISOU 5546  N   TYR B 343     5268   4544   8878    -59   -819    136       N
ATOM   5547  CA  TYR B 343     -48.914  27.093  30.117  1.00 46.23           C
ANISOU 5547  CA  TYR B 343     5023   3970   8573     -1   -784    242       C
ATOM   5548  C   TYR B 343     -49.231  26.223  28.913  1.00 42.85           C
ANISOU 5548  C   TYR B 343     4570   3688   8024      7   -654    462       C
ATOM   5549  O   TYR B 343     -48.346  25.547  28.378  1.00 42.06           O
ANISOU 5549  O   TYR B 343     4334   3793   7855    -94   -562    509       O
ATOM   5550  CB  TYR B 343     -48.684  28.540  29.656  1.00 48.65           C
ANISOU 5550  CB  TYR B 343     5398   3946   9140   -191   -906    314       C
ATOM   5551  CG  TYR B 343     -47.482  28.718  28.754  1.00 46.96           C
ANISOU 5551  CG  TYR B 343     5093   3810   8938   -511   -870    512       C
ATOM   5552  CD1 TYR B 343     -46.217  28.935  29.286  1.00 48.19           C
ANISOU 5552  CD1 TYR B 343     5106   4044   9160   -682   -906    382       C
ATOM   5553  CD2 TYR B 343     -47.615  28.681  27.371  1.00 46.10           C
ANISOU 5553  CD2 TYR B 343     5022   3747   8748   -686   -795    813       C
ATOM   5554  CE1 TYR B 343     -45.118  29.104  28.468  1.00 48.52           C
ANISOU 5554  CE1 TYR B 343     5000   4214   9222  -1012   -828    518       C
ATOM   5555  CE2 TYR B 343     -46.520  28.849  26.545  1.00 48.52           C
ANISOU 5555  CE2 TYR B 343     5221   4215   8999  -1052   -700    958       C
ATOM   5556  CZ  TYR B 343     -45.273  29.062  27.100  1.00 48.66           C
ANISOU 5556  CZ  TYR B 343     5053   4315   9121  -1211   -696    796       C
ATOM   5557  OH  TYR B 343     -44.177  29.231  26.287  1.00 51.87           O
ANISOU 5557  OH  TYR B 343     5289   4937   9483  -1610   -558    897       O
ATOM   5558  N   PRO B 344     -50.486  26.216  28.466  1.00 44.93           N
ANISOU 5558  N   PRO B 344     4927   3863   8281    127   -647    546       N
ATOM   5559  CA  PRO B 344     -50.818  25.490  27.238  1.00 48.07           C
ANISOU 5559  CA  PRO B 344     5321   4405   8540     87   -552    741       C
ATOM   5560  C   PRO B 344     -50.414  26.285  26.009  1.00 58.13           C
ANISOU 5560  C   PRO B 344     6648   5611   9826   -198   -592    991       C
ATOM   5561  O   PRO B 344     -50.512  27.514  25.979  1.00 60.12           O
ANISOU 5561  O   PRO B 344     7003   5564  10276   -294   -765   1098       O
ATOM   5562  CB  PRO B 344     -52.341  25.331  27.325  1.00 42.06           C
ANISOU 5562  CB  PRO B 344     4619   3568   7795    296   -585    732       C
ATOM   5563  CG  PRO B 344     -52.783  26.506  28.119  1.00 38.13           C
ANISOU 5563  CG  PRO B 344     4158   2788   7541    387   -717    586       C
ATOM   5564  CD  PRO B 344     -51.684  26.785  29.114  1.00 39.43           C
ANISOU 5564  CD  PRO B 344     4298   2973   7712    312   -719    402       C
ATOM   5565  N   LYS B 345     -49.942  25.572  24.993  1.00 70.14           N
ANISOU 5565  N   LYS B 345     8102   7415  11134   -366   -436   1072       N
ATOM   5566  CA  LYS B 345     -49.647  26.226  23.731  1.00 79.48           C
ANISOU 5566  CA  LYS B 345     9360   8641  12196   -728   -443   1347       C
ATOM   5567  C   LYS B 345     -50.936  26.654  23.037  1.00 86.51           C
ANISOU 5567  C   LYS B 345    10447   9352  13070   -713   -644   1620       C
ATOM   5568  O   LYS B 345     -52.015  26.091  23.252  1.00 85.30           O
ANISOU 5568  O   LYS B 345    10299   9174  12936   -434   -681   1544       O
ATOM   5569  CB  LYS B 345     -48.844  25.308  22.810  1.00 81.21           C
ANISOU 5569  CB  LYS B 345     9421   9296  12140   -939   -171   1266       C
ATOM   5570  CG  LYS B 345     -47.372  25.194  23.161  1.00 81.66           C
ANISOU 5570  CG  LYS B 345     9224   9528  12277  -1061    -13   1049       C
ATOM   5571  CD  LYS B 345     -46.530  25.121  21.897  1.00 85.09           C
ANISOU 5571  CD  LYS B 345     9525  10356  12448  -1490    238   1065       C
ATOM   5572  CE  LYS B 345     -45.330  24.205  22.067  1.00 83.54           C
ANISOU 5572  CE  LYS B 345     8932  10465  12342  -1443    482    658       C
ATOM   5573  NZ  LYS B 345     -44.551  24.085  20.802  1.00 85.33           N
ANISOU 5573  NZ  LYS B 345     8967  11166  12289  -1880    808    563       N
ATOM   5574  N   LEU B 346     -50.801  27.670  22.182  1.00 91.34           N
ANISOU 5574  N   LEU B 346    11211   9837  13658  -1053   -806   1969       N
ATOM   5575  CA  LEU B 346     -51.951  28.207  21.462  1.00 93.01           C
ANISOU 5575  CA  LEU B 346    11611   9823  13904  -1068  -1110   2305       C
ATOM   5576  C   LEU B 346     -52.556  27.185  20.504  1.00 91.43           C
ANISOU 5576  C   LEU B 346    11419   9990  13331  -1104  -1018   2356       C
ATOM   5577  O   LEU B 346     -53.769  27.211  20.269  1.00 92.45           O
ANISOU 5577  O   LEU B 346    11613   9971  13543   -932  -1255   2482       O
ATOM   5578  CB  LEU B 346     -51.545  29.480  20.709  1.00 98.04           C
ANISOU 5578  CB  LEU B 346    12446  10233  14570  -1509  -1361   2756       C
ATOM   5579  CG  LEU B 346     -50.062  29.715  20.381  1.00100.95           C
ANISOU 5579  CG  LEU B 346    12774  10855  14726  -1989  -1138   2814       C
ATOM   5580  CD1 LEU B 346     -49.941  30.481  19.073  1.00105.49           C
ANISOU 5580  CD1 LEU B 346    13588  11465  15027  -2563  -1324   3365       C
ATOM   5581  CD2 LEU B 346     -49.349  30.466  21.505  1.00102.19           C
ANISOU 5581  CD2 LEU B 346    12856  10683  15287  -1919  -1181   2625       C
ATOM   5582  N   GLN B 347     -51.733  26.284  19.958  1.00 91.54           N
ANISOU 5582  N   GLN B 347    11329  10477  12976  -1318   -686   2206       N
ATOM   5583  CA  GLN B 347     -52.133  25.230  19.010  1.00 93.10           C
ANISOU 5583  CA  GLN B 347    11514  11068  12792  -1399   -549   2148       C
ATOM   5584  C   GLN B 347     -53.591  24.794  19.075  1.00 90.49           C
ANISOU 5584  C   GLN B 347    11224  10605  12554  -1084   -746   2156       C
ATOM   5585  O   GLN B 347     -54.099  24.177  18.142  1.00 91.27           O
ANISOU 5585  O   GLN B 347    11366  10971  12341  -1213   -745   2196       O
ATOM   5586  CB  GLN B 347     -51.259  23.990  19.216  1.00 94.22           C
ANISOU 5586  CB  GLN B 347    11406  11556  12836  -1326   -155   1691       C
ATOM   5587  CG  GLN B 347     -50.154  23.835  18.196  1.00 97.71           C
ANISOU 5587  CG  GLN B 347    11757  12463  12904  -1785    134   1619       C
ATOM   5588  CD  GLN B 347     -49.169  22.753  18.579  1.00 95.05           C
ANISOU 5588  CD  GLN B 347    11089  12357  12667  -1632    472   1104       C
ATOM   5589  OE1 GLN B 347     -49.113  22.329  19.734  1.00 89.17           O
ANISOU 5589  OE1 GLN B 347    10226  11368  12286  -1232    429    906       O
ATOM   5590  NE2 GLN B 347     -48.384  22.298  17.610  1.00 99.15           N
ANISOU 5590  NE2 GLN B 347    11443  13358  12872  -1965    791    872       N
TER    5591      GLN B 347
HETATM 5592  C1  GOL A 401     -64.442  38.584 -16.457  1.00 61.23           C
HETATM 5593  O1  GOL A 401     -63.447  39.506 -16.136  1.00 65.57           O
HETATM 5594  C2  GOL A 401     -65.154  38.214 -15.134  1.00 59.32           C
HETATM 5595  O2  GOL A 401     -65.880  39.276 -14.616  1.00 50.98           O
HETATM 5596  C3  GOL A 401     -66.053  37.005 -15.488  1.00 67.18           C
HETATM 5597  O3  GOL A 401     -66.893  36.797 -14.395  1.00 70.21           O
HETATM 5598  C1  GOL A 402     -50.548  13.597 -25.759  1.00 61.54           C
HETATM 5599  O1  GOL A 402     -50.706  14.884 -26.271  1.00 58.12           O
HETATM 5600  C2  GOL A 402     -51.955  12.955 -25.699  1.00 59.84           C
HETATM 5601  O2  GOL A 402     -52.765  13.556 -24.746  1.00 56.28           O
HETATM 5602  C3  GOL A 402     -51.703  11.458 -25.398  1.00 60.57           C
HETATM 5603  O3  GOL A 402     -51.848  10.775 -26.604  1.00 61.32           O
HETATM 5604 MG    MG A 403     -90.198  36.403 -36.300  1.00 49.76          MG
HETATM 5605  C1  GOL A 404     -71.093   9.803  -9.689  1.00 79.85           C
HETATM 5606  O1  GOL A 404     -70.631  10.942 -10.351  1.00 79.48           O
HETATM 5607  C2  GOL A 404     -71.213  10.157  -8.186  1.00 80.65           C
HETATM 5608  O2  GOL A 404     -70.028   9.927  -7.502  1.00 78.07           O
HETATM 5609  C3  GOL A 404     -71.620  11.650  -8.161  1.00 84.17           C
HETATM 5610  O3  GOL A 404     -72.624  11.810  -9.115  1.00 85.24           O
HETATM 5611  C1  GOL A 405     -71.861  28.468 -28.620  1.00 77.67           C
HETATM 5612  O1  GOL A 405     -71.236  28.262 -29.848  1.00 77.81           O
HETATM 5613  C2  GOL A 405     -72.060  27.076 -27.976  1.00 75.76           C
HETATM 5614  O2  GOL A 405     -71.239  26.894 -26.872  1.00 74.89           O
HETATM 5615  C3  GOL A 405     -73.564  27.014 -27.613  1.00 73.76           C
HETATM 5616  O3  GOL A 405     -73.895  25.665 -27.491  1.00 69.40           O
HETATM 5617  C   ACY A 406     -78.489  30.724 -29.533  1.00 62.72           C
HETATM 5618  O   ACY A 406     -78.030  30.394 -30.618  1.00 62.59           O
HETATM 5619  OXT ACY A 406     -79.066  29.934 -28.701  1.00 61.39           O
HETATM 5620  CH3 ACY A 406     -78.419  32.173 -29.038  1.00 61.36           C
HETATM 5621  C1  GOL B 401     -57.352  22.119  19.263  1.00 65.38           C
HETATM 5622  O1  GOL B 401     -56.749  20.868  19.389  1.00 66.88           O
HETATM 5623  C2  GOL B 401     -58.398  22.225  20.395  1.00 60.28           C
HETATM 5624  O2  GOL B 401     -58.128  23.280  21.256  1.00 53.91           O
HETATM 5625  C3  GOL B 401     -59.753  22.387  19.665  1.00 59.16           C
HETATM 5626  O3  GOL B 401     -60.755  22.085  20.590  1.00 50.58           O
HETATM 5627  C1  GOL B 402     -68.298  27.991  27.149  1.00 81.03           C
HETATM 5628  O1  GOL B 402     -67.028  27.836  27.697  1.00 79.72           O
HETATM 5629  C2  GOL B 402     -69.158  28.744  28.189  1.00 82.30           C
HETATM 5630  O2  GOL B 402     -68.824  30.087  28.263  1.00 81.86           O
HETATM 5631  C3  GOL B 402     -70.618  28.529  27.725  1.00 82.86           C
HETATM 5632  O3  GOL B 402     -70.735  27.186  27.374  1.00 83.39           O
HETATM 5633  C1  GOL B 403     -61.858  13.300   9.926  1.00 75.79           C
HETATM 5634  O1  GOL B 403     -61.367  12.504  10.956  1.00 73.13           O
HETATM 5635  C2  GOL B 403     -61.466  12.621   8.591  1.00 81.11           C
HETATM 5636  O2  GOL B 403     -61.468  13.520   7.536  1.00 80.59           O
HETATM 5637  C3  GOL B 403     -62.502  11.486   8.391  1.00 85.66           C
HETATM 5638  O3  GOL B 403     -61.933  10.319   8.889  1.00 89.22           O
HETATM 5639 CL    CL B 404     -71.286  -4.551  27.265  1.00 49.72          CL
HETATM 5640  C1  GOL B 405     -81.431  33.200  15.303  1.00 69.26           C
HETATM 5641  O1  GOL B 405     -82.613  33.220  14.564  1.00 70.29           O
HETATM 5642  C2  GOL B 405     -80.533  34.334  14.752  1.00 69.69           C
HETATM 5643  O2  GOL B 405     -81.249  35.224  13.964  1.00 67.55           O
HETATM 5644  C3  GOL B 405     -79.412  33.614  13.959  1.00 68.65           C
HETATM 5645  O3  GOL B 405     -78.869  32.645  14.801  1.00 67.28           O
HETATM 5646  C1 AGOL B 406     -52.335  12.285  29.278  0.58 60.14           C
HETATM 5647  C1 BGOL B 406     -52.024  11.030  28.330  0.42 63.68           C
HETATM 5648  O1 AGOL B 406     -53.123  12.023  30.386  0.58 54.46           O
HETATM 5649  O1 BGOL B 406     -53.208  10.581  27.747  0.42 64.71           O
HETATM 5650  C2 AGOL B 406     -52.210  10.967  28.493  0.58 63.89           C
HETATM 5651  C2 BGOL B 406     -51.051  11.361  27.175  0.42 63.75           C
HETATM 5652  O2 AGOL B 406     -53.442  10.505  28.051  0.58 65.10           O
HETATM 5653  O2 BGOL B 406     -51.381  12.550  26.542  0.42 61.86           O
HETATM 5654  C3 AGOL B 406     -51.264  11.323  27.331  0.58 63.97           C
HETATM 5655  C3 BGOL B 406     -51.141  10.146  26.222  0.42 64.13           C
HETATM 5656  O3 AGOL B 406     -51.080  10.165  26.592  0.58 64.60           O
HETATM 5657  O3 BGOL B 406     -50.614   9.055  26.911  0.42 63.71           O
HETATM 5658  C   ACY B 407     -72.733   7.518  31.232  1.00 63.74           C
HETATM 5659  O   ACY B 407     -71.688   7.766  30.647  1.00 64.31           O
HETATM 5660  OXT ACY B 407     -73.912   7.698  30.752  1.00 64.45           O
HETATM 5661  CH3 ACY B 407     -72.744   6.945  32.656  1.00 57.87           C
HETATM 5662  C   ACY B 408     -33.764  22.941  36.474  1.00 92.05           C
HETATM 5663  O   ACY B 408     -34.114  23.583  35.493  1.00 94.87           O
HETATM 5664  OXT ACY B 408     -34.446  22.809  37.554  1.00 93.60           O
HETATM 5665  CH3 ACY B 408     -32.419  22.199  36.514  1.00 90.75           C
HETATM 5666  O   HOH A 501     -61.432   8.298  -7.815  1.00 45.47           O
HETATM 5667  O   HOH A 502     -68.816  19.230 -27.418  1.00 32.27           O
HETATM 5668  O   HOH A 503     -87.737   3.136 -39.714  1.00 41.10           O
HETATM 5669  O   HOH A 504     -64.815  17.078 -26.378  1.00 35.23           O
HETATM 5670  O   HOH A 505     -55.542  19.878 -27.762  1.00 37.08           O
HETATM 5671  O   HOH A 506     -75.654   3.855 -28.404  1.00 38.33           O
HETATM 5672  O   HOH A 507     -63.403  26.927 -22.256  1.00 31.32           O
HETATM 5673  O   HOH A 508     -50.321  11.872 -18.558  1.00 52.63           O
HETATM 5674  O   HOH A 509     -83.180  27.016 -20.714  1.00 30.89           O
HETATM 5675  O   HOH A 510     -69.330  25.162 -41.852  1.00 54.85           O
HETATM 5676  O   HOH A 511     -52.823  47.605  -9.423  1.00 40.29           O
HETATM 5677  O   HOH A 512    -101.507  29.820 -27.191  1.00 46.33           O
HETATM 5678  O   HOH A 513     -85.206  24.360 -46.757  1.00 34.81           O
HETATM 5679  O   HOH A 514     -73.631  24.190 -17.725  1.00 34.63           O
HETATM 5680  O   HOH A 515     -75.350  10.715 -18.741  1.00 34.90           O
HETATM 5681  O   HOH A 516     -54.575  45.056  -1.356  1.00 36.13           O
HETATM 5682  O   HOH A 517     -59.700  20.640  -9.645  1.00 39.82           O
HETATM 5683  O   HOH A 518     -72.438  13.576 -10.995  1.00 45.65           O
HETATM 5684  O   HOH A 519     -60.458  29.404 -20.290  1.00 26.51           O
HETATM 5685  O   HOH A 520     -73.611  31.160 -12.073  1.00 37.93           O
HETATM 5686  O   HOH A 521     -56.469   3.730 -27.381  1.00 46.99           O
HETATM 5687  O   HOH A 522     -75.747  24.078 -24.094  1.00 36.54           O
HETATM 5688  O   HOH A 523     -63.302  16.234 -28.682  1.00 30.82           O
HETATM 5689  O   HOH A 524     -74.806  15.861 -34.971  1.00 37.75           O
HETATM 5690  O   HOH A 525     -71.108  32.337  -1.072  1.00 33.14           O
HETATM 5691  O   HOH A 526     -58.447  11.451   1.624  1.00 60.32           O
HETATM 5692  O   HOH A 527     -98.766  33.149 -28.598  1.00 32.32           O
HETATM 5693  O   HOH A 528     -71.315  35.500 -19.627  1.00 49.21           O
HETATM 5694  O   HOH A 529     -99.359  33.083 -38.174  1.00 37.10           O
HETATM 5695  O   HOH A 530     -83.166   9.370 -21.364  1.00 50.20           O
HETATM 5696  O   HOH A 531     -69.214  34.107 -20.296  1.00 48.05           O
HETATM 5697  O   HOH A 532     -94.339   4.230 -33.464  1.00 41.16           O
HETATM 5698  O   HOH A 533     -98.657  27.052 -34.568  1.00 31.00           O
HETATM 5699  O   HOH A 534     -60.067  17.284   2.519  1.00 47.33           O
HETATM 5700  O   HOH A 535     -73.307  29.806  -1.394  1.00 43.18           O
HETATM 5701  O   HOH A 536     -93.626   1.390 -33.193  1.00 48.43           O
HETATM 5702  O   HOH A 537     -71.852  27.844 -36.751  1.00 47.31           O
HETATM 5703  O   HOH A 538     -58.990  48.621  -6.060  1.00 48.11           O
HETATM 5704  O   HOH A 539     -70.730  21.089 -14.365  1.00 69.58           O
HETATM 5705  O   HOH A 540     -76.087  22.532 -26.216  1.00 36.77           O
HETATM 5706  O   HOH A 541     -88.579   7.300 -46.734  1.00 55.23           O
HETATM 5707  O   HOH A 542     -72.547  23.864 -25.874  1.00 39.14           O
HETATM 5708  O   HOH A 543     -75.292  19.305 -18.890  1.00 25.26           O
HETATM 5709  O   HOH A 544     -88.730   5.364 -42.479  1.00 48.51           O
HETATM 5710  O   HOH A 545     -96.469  32.969 -24.619  1.00 32.26           O
HETATM 5711  O   HOH A 546     -69.937  50.722  -4.272  1.00 39.50           O
HETATM 5712  O   HOH A 547     -75.600  24.841 -29.392  1.00 50.26           O
HETATM 5713  O   HOH A 548     -60.394  26.547 -22.294  1.00 30.08           O
HETATM 5714  O   HOH A 549     -80.478   3.670 -40.010  1.00 34.57           O
HETATM 5715  O   HOH A 550     -51.094  19.292  -5.716  1.00 54.04           O
HETATM 5716  O   HOH A 551     -75.151  16.304 -46.694  1.00 54.37           O
HETATM 5717  O   HOH A 552     -68.407  36.854  -1.716  1.00 29.75           O
HETATM 5718  O   HOH A 553     -85.281   1.955 -33.970  1.00 28.35           O
HETATM 5719  O   HOH A 554     -65.610  23.501 -21.296  1.00 35.45           O
HETATM 5720  O   HOH A 555     -69.992  27.967 -32.231  1.00 50.81           O
HETATM 5721  O   HOH A 556     -78.446  29.598 -25.511  1.00 51.03           O
HETATM 5722  O   HOH A 557     -55.035  28.778  -2.421  1.00 37.39           O
HETATM 5723  O   HOH A 558     -79.025  11.103 -43.212  1.00 42.50           O
HETATM 5724  O   HOH A 559     -76.877  32.853 -38.806  1.00 40.44           O
HETATM 5725  O   HOH A 560     -63.962  25.668 -20.027  1.00 27.39           O
HETATM 5726  O   HOH A 561     -64.266  21.701  -1.512  1.00 36.64           O
HETATM 5727  O   HOH A 562     -55.205  29.838 -15.591  1.00 46.89           O
HETATM 5728  O   HOH A 563     -63.017  21.731 -12.516  1.00 25.13           O
HETATM 5729  O   HOH A 564     -68.207  34.620 -11.893  1.00 27.47           O
HETATM 5730  O   HOH A 565     -77.940  21.049 -28.748  1.00 27.24           O
HETATM 5731  O   HOH A 566     -49.001   8.929 -17.605  1.00 57.14           O
HETATM 5732  O   HOH A 567     -49.230  35.350 -19.932  1.00 48.48           O
HETATM 5733  O   HOH A 568     -53.698  24.143  -3.519  1.00 41.53           O
HETATM 5734  O   HOH A 569     -95.012   6.748 -32.257  1.00 43.75           O
HETATM 5735  O   HOH A 570     -88.749   2.790 -33.415  1.00 36.80           O
HETATM 5736  O   HOH A 571     -91.343  16.310 -44.057  1.00 37.02           O
HETATM 5737  O   HOH A 572     -56.283  42.524   1.407  1.00 28.11           O
HETATM 5738  O   HOH A 573     -70.650  26.436  -9.980  1.00 36.74           O
HETATM 5739  O   HOH A 574     -82.164  24.491 -21.310  1.00 38.60           O
HETATM 5740  O   HOH A 575     -66.943  33.920 -16.995  1.00 36.85           O
HETATM 5741  O   HOH A 576     -69.824  44.959  -0.244  1.00 43.45           O
HETATM 5742  O   HOH A 577     -76.534  12.333 -45.365  1.00 52.18           O
HETATM 5743  O   HOH A 578     -71.658  28.723  -8.184  1.00 24.71           O
HETATM 5744  O   HOH A 579     -54.800  24.157 -15.726  1.00 48.63           O
HETATM 5745  O   HOH A 580     -68.315   6.020 -28.872  1.00 42.87           O
HETATM 5746  O   HOH A 581     -57.757  35.593 -15.577  1.00 57.08           O
HETATM 5747  O   HOH A 582     -61.774  26.017 -18.333  1.00 30.03           O
HETATM 5748  O   HOH A 583     -75.001  11.114 -40.916  1.00 50.01           O
HETATM 5749  O   HOH A 584     -74.091   5.618 -39.992  1.00 46.39           O
HETATM 5750  O   HOH A 585     -72.920  12.741 -34.287  1.00 44.40           O
HETATM 5751  O   HOH A 586     -66.307  18.568  -7.017  1.00 45.50           O
HETATM 5752  O   HOH A 587     -94.554  15.159 -43.622  1.00 46.72           O
HETATM 5753  O   HOH A 588     -75.850  15.457 -17.857  1.00 53.79           O
HETATM 5754  O   HOH A 589     -93.892  19.277 -31.554  1.00 41.32           O
HETATM 5755  O   HOH A 590     -71.497  15.725  -9.418  1.00 63.72           O
HETATM 5756  O   HOH A 591     -97.484  17.385 -38.114  1.00 47.71           O
HETATM 5757  O   HOH A 592     -57.965   0.608 -11.080  1.00 57.71           O
HETATM 5758  O   HOH A 593     -66.425  19.043 -26.639  1.00 28.50           O
HETATM 5759  O   HOH A 594     -99.158   4.826 -37.155  1.00 38.59           O
HETATM 5760  O   HOH A 595     -96.777  26.800 -24.232  1.00 54.84           O
HETATM 5761  O   HOH A 596     -68.826  17.487 -15.078  1.00 26.63           O
HETATM 5762  O   HOH A 597     -52.722  28.465 -14.014  1.00 62.08           O
HETATM 5763  O   HOH A 598     -91.971  27.704 -40.821  1.00 44.10           O
HETATM 5764  O   HOH A 599     -84.302  13.198 -22.174  1.00 38.03           O
HETATM 5765  O   HOH A 600     -82.699  19.656 -20.575  1.00 39.22           O
HETATM 5766  O   HOH A 601     -97.818  23.932 -27.798  1.00 52.06           O
HETATM 5767  O   HOH A 602     -79.335  21.993 -35.952  1.00 42.33           O
HETATM 5768  O   HOH A 603     -87.739  27.504 -39.915  1.00 37.55           O
HETATM 5769  O   HOH A 604     -88.754   5.813 -39.965  1.00 47.80           O
HETATM 5770  O   HOH A 605     -62.400  20.712 -10.064  1.00 28.39           O
HETATM 5771  O   HOH A 606     -75.321  21.937 -29.108  1.00 30.95           O
HETATM 5772  O   HOH A 607     -55.278  22.252 -39.595  1.00 49.57           O
HETATM 5773  O   HOH A 608     -96.023  28.931 -40.173  1.00 43.06           O
HETATM 5774  O   HOH A 609     -98.780  23.123 -34.687  1.00 41.48           O
HETATM 5775  O   HOH A 610     -72.354   8.233 -17.973  1.00 46.10           O
HETATM 5776  O   HOH A 611     -69.115  18.877  -9.092  1.00 39.45           O
HETATM 5777  O   HOH A 612     -70.985  17.486 -28.716  1.00 31.97           O
HETATM 5778  O   HOH A 613     -64.525  23.625 -11.696  1.00 29.18           O
HETATM 5779  O   HOH A 614     -41.988  34.633 -10.982  1.00 37.06           O
HETATM 5780  O   HOH A 615     -71.354  49.258  -1.196  1.00 37.04           O
HETATM 5781  O   HOH A 616     -72.826  33.320 -19.835  1.00 42.74           O
HETATM 5782  O   HOH A 617     -72.105   7.294 -20.735  1.00 65.27           O
HETATM 5783  O   HOH A 618     -70.228   6.544 -31.502  1.00 64.25           O
HETATM 5784  O   HOH A 619     -83.674  36.457 -27.612  1.00 51.68           O
HETATM 5785  O   HOH A 620     -93.068   4.472 -24.600  1.00 41.82           O
HETATM 5786  O   HOH A 621     -55.223  33.260  -2.465  1.00 48.41           O
HETATM 5787  O   HOH A 622     -65.718  23.646  -2.893  1.00 45.59           O
HETATM 5788  O   HOH A 623     -69.052  38.317 -15.752  1.00 58.47           O
HETATM 5789  O   HOH A 624     -69.131  24.457 -32.512  1.00 49.74           O
HETATM 5790  O   HOH A 625     -44.819  36.925  -4.553  1.00 49.30           O
HETATM 5791  O   HOH A 626     -67.900  26.664 -20.910  1.00 37.26           O
HETATM 5792  O   HOH A 627     -63.422  49.459 -13.836  1.00 32.39           O
HETATM 5793  O   HOH A 628     -79.852  17.682 -21.928  1.00 35.38           O
HETATM 5794  O   HOH A 629     -89.931  34.780 -25.244  1.00 37.88           O
HETATM 5795  O   HOH A 630     -80.141   5.832 -36.030  1.00 35.94           O
HETATM 5796  O   HOH A 631     -61.449  51.064  -2.972  1.00 38.90           O
HETATM 5797  O   HOH A 632     -66.922  12.813 -34.060  1.00 43.93           O
HETATM 5798  O   HOH A 633     -69.690  24.924 -24.073  1.00 49.83           O
HETATM 5799  O   HOH A 634     -68.625  17.439 -34.555  1.00 42.20           O
HETATM 5800  O   HOH A 635     -65.190   5.694 -31.314  1.00 54.58           O
HETATM 5801  O   HOH A 636     -91.053  21.389 -27.138  1.00 35.33           O
HETATM 5802  O   HOH A 637     -95.237  21.599 -30.454  1.00 39.85           O
HETATM 5803  O   HOH A 638     -96.093  18.566 -40.901  1.00 45.93           O
HETATM 5804  O   HOH A 639     -76.790  28.367 -21.773  1.00 55.25           O
HETATM 5805  O   HOH A 640     -76.255  17.855 -20.776  1.00 28.37           O
HETATM 5806  O   HOH A 641     -69.383  29.682 -23.544  1.00 68.79           O
HETATM 5807  O   HOH A 642     -63.219   4.093 -23.781  1.00 30.44           O
HETATM 5808  O   HOH A 643     -58.818  19.388 -34.176  1.00 43.08           O
HETATM 5809  O   HOH A 644     -54.260  25.850 -18.731  1.00 38.98           O
HETATM 5810  O   HOH A 645     -84.188  38.994 -38.068  1.00 55.07           O
HETATM 5811  O   HOH A 646     -55.498  19.613 -17.571  1.00 65.03           O
HETATM 5812  O   HOH A 647     -68.012   7.762 -30.946  1.00 49.20           O
HETATM 5813  O   HOH A 648     -93.680  20.850 -28.304  1.00 53.90           O
HETATM 5814  O   HOH A 649     -58.266  35.030  -2.261  1.00 48.73           O
HETATM 5815  O   HOH A 650     -95.024  24.730 -23.731  1.00 35.40           O
HETATM 5816  O   HOH A 651     -82.263  34.595 -22.074  1.00 39.19           O
HETATM 5817  O   HOH A 652     -37.122  35.164  -6.295  1.00 56.34           O
HETATM 5818  O   HOH A 653     -99.055  23.860 -32.180  1.00 46.98           O
HETATM 5819  O   HOH A 654     -61.537  54.787  -7.797  1.00 42.13           O
HETATM 5820  O   HOH A 655     -61.413  18.399 -35.105  1.00 52.06           O
HETATM 5821  O   HOH A 656     -49.346   5.251 -21.206  1.00 56.54           O
HETATM 5822  O   HOH A 657     -68.992  39.529  -1.055  1.00 34.57           O
HETATM 5823  O   HOH A 658     -68.802  29.792 -28.463  1.00 57.68           O
HETATM 5824  O   HOH A 659     -63.461  -0.737  -6.655  1.00 71.65           O
HETATM 5825  O   HOH A 660     -73.524  22.539 -15.713  1.00 51.34           O
HETATM 5826  O   HOH A 661     -68.881  -1.426 -20.216  1.00 54.19           O
HETATM 5827  O   HOH A 662     -71.637  16.835 -47.312  1.00 56.66           O
HETATM 5828  O   HOH A 663     -48.216  45.159 -11.980  1.00 52.80           O
HETATM 5829  O   HOH A 664     -45.312  18.284 -21.150  1.00 63.92           O
HETATM 5830  O   HOH A 665     -53.379  13.195 -33.185  1.00 59.93           O
HETATM 5831  O   HOH A 666     -65.089   2.650 -26.121  1.00 45.84           O
HETATM 5832  O   HOH A 667     -47.181  18.538 -18.962  1.00 43.58           O
HETATM 5833  O   HOH A 668     -46.832  32.415  -6.674  1.00 55.41           O
HETATM 5834  O   HOH A 669     -55.434  27.513 -40.090  1.00 52.64           O
HETATM 5835  O   HOH A 670     -64.238  52.047  -9.977  1.00 42.69           O
HETATM 5836  O   HOH A 671     -76.299  31.973 -16.383  1.00 49.09           O
HETATM 5837  O   HOH A 672     -68.471  24.695 -22.111  1.00 43.25           O
HETATM 5838  O   HOH A 673     -70.901  35.346  -1.912  1.00 36.02           O
HETATM 5839  O   HOH A 674     -77.758   7.777 -19.585  1.00 50.63           O
HETATM 5840  O   HOH A 675     -92.282  26.237 -49.678  1.00 44.22           O
HETATM 5841  O   HOH A 676     -63.609  43.128 -15.731  1.00 40.82           O
HETATM 5842  O   HOH A 677     -88.896  29.083 -42.198  1.00 61.01           O
HETATM 5843  O   HOH A 678     -72.292  15.153 -13.114  1.00 52.38           O
HETATM 5844  O   HOH A 679     -76.249  27.049 -23.967  1.00 47.51           O
HETATM 5845  O   HOH A 680     -79.184  24.877 -28.542  1.00 74.02           O
HETATM 5846  O   HOH A 681     -68.815  32.873 -23.276  1.00 60.77           O
HETATM 5847  O   HOH A 682     -56.814   0.317 -16.337  1.00 44.46           O
HETATM 5848  O   HOH A 683    -100.490  33.652 -26.869  1.00 35.75           O
HETATM 5849  O   HOH A 684     -99.860  18.351 -35.885  1.00 54.15           O
HETATM 5850  O   HOH A 685     -95.519  18.911 -29.218  1.00 52.60           O
HETATM 5851  O   HOH A 686     -50.813  47.557 -11.952  1.00 46.48           O
HETATM 5852  O   HOH B 501     -65.176  27.683  29.084  1.00 36.02           O
HETATM 5853  O   HOH B 502     -70.717  15.336  26.098  1.00 46.98           O
HETATM 5854  O   HOH B 503     -86.795  33.564  15.041  1.00 50.70           O
HETATM 5855  O   HOH B 504     -70.392  25.998  19.941  1.00 50.92           O
HETATM 5856  O   HOH B 505     -67.674  19.232   8.726  1.00 59.54           O
HETATM 5857  O   HOH B 506     -95.022  24.105   1.381  1.00 68.24           O
HETATM 5858  O   HOH B 507     -64.615   3.520  20.844  1.00 31.54           O
HETATM 5859  O   HOH B 508     -70.490  26.372   9.435  1.00 31.29           O
HETATM 5860  O   HOH B 509     -60.600   8.275   9.198  1.00 35.16           O
HETATM 5861  O   HOH B 510     -70.316  32.318  11.942  1.00 36.70           O
HETATM 5862  O   HOH B 511     -51.505  45.316  24.340  1.00 44.77           O
HETATM 5863  O   HOH B 512     -66.720  26.437  17.453  1.00 48.16           O
HETATM 5864  O   HOH B 513     -77.149  31.242  16.638  1.00 39.13           O
HETATM 5865  O   HOH B 514     -58.410  45.495  35.962  1.00 42.80           O
HETATM 5866  O   HOH B 515     -71.399  13.774  28.088  1.00 29.05           O
HETATM 5867  O   HOH B 516     -75.695  32.534  19.737  1.00 43.32           O
HETATM 5868  O   HOH B 517     -94.584  42.749   4.013  1.00 48.41           O
HETATM 5869  O   HOH B 518     -61.182  19.703  34.708  1.00 39.69           O
HETATM 5870  O   HOH B 519     -49.580  46.716  28.295  1.00 28.18           O
HETATM 5871  O   HOH B 520     -64.510  27.096  23.611  1.00 37.74           O
HETATM 5872  O   HOH B 521     -67.089  25.521  25.435  1.00 77.41           O
HETATM 5873  O   HOH B 522     -62.036   4.998   5.622  1.00 55.06           O
HETATM 5874  O   HOH B 523     -66.511  12.344  32.794  1.00 51.48           O
HETATM 5875  O   HOH B 524     -85.243  21.560  15.531  1.00 31.25           O
HETATM 5876  O   HOH B 525     -76.716  32.369  11.638  1.00 31.77           O
HETATM 5877  O   HOH B 526     -70.770   0.048  26.225  1.00 33.21           O
HETATM 5878  O   HOH B 527     -92.114  20.381  18.944  1.00 51.30           O
HETATM 5879  O   HOH B 528     -73.237  31.958   0.843  1.00 28.40           O
HETATM 5880  O   HOH B 529     -76.618  16.090   8.971  1.00 26.24           O
HETATM 5881  O   HOH B 530     -62.657  22.863  18.465  1.00 31.82           O
HETATM 5882  O   HOH B 531     -80.682  23.688  19.838  1.00 44.55           O
HETATM 5883  O   HOH B 532     -63.077  28.466  51.635  1.00 47.07           O
HETATM 5884  O   HOH B 533     -80.106   3.445  18.218  1.00 33.56           O
HETATM 5885  O   HOH B 534     -58.484   1.755  12.269  1.00 43.26           O
HETATM 5886  O   HOH B 535     -61.216  25.714  28.466  1.00 28.73           O
HETATM 5887  O   HOH B 536     -73.617  25.448  24.444  1.00 54.56           O
HETATM 5888  O   HOH B 537     -81.052  41.945  -0.073  1.00 37.17           O
HETATM 5889  O   HOH B 538     -61.378  20.288  46.562  1.00 59.67           O
HETATM 5890  O   HOH B 539     -51.907  23.472  22.695  1.00 49.34           O
HETATM 5891  O   HOH B 540     -70.081  28.444  36.260  1.00 39.56           O
HETATM 5892  O   HOH B 541     -61.648   7.861  27.886  1.00 33.84           O
HETATM 5893  O   HOH B 542     -69.793  18.143   6.575  1.00 32.12           O
HETATM 5894  O   HOH B 543     -67.705  19.251  26.886  1.00 40.15           O
HETATM 5895  O   HOH B 544     -68.702   6.519   7.654  1.00 28.65           O
HETATM 5896  O   HOH B 545     -93.301  23.028  19.500  1.00 45.73           O
HETATM 5897  O   HOH B 546     -78.098  -0.830  27.490  1.00 34.84           O
HETATM 5898  O   HOH B 547     -47.028  28.508  43.550  1.00 41.07           O
HETATM 5899  O   HOH B 548     -77.690  34.328   1.301  1.00 23.78           O
HETATM 5900  O   HOH B 549     -80.030  13.003  26.918  1.00 31.77           O
HETATM 5901  O   HOH B 550     -73.040  19.635   1.019  1.00 37.92           O
HETATM 5902  O   HOH B 551     -70.084   3.496  30.491  1.00 44.67           O
HETATM 5903  O   HOH B 552     -75.992  22.533  19.404  1.00 34.01           O
HETATM 5904  O   HOH B 553     -84.665  20.448   1.943  1.00 40.30           O
HETATM 5905  O   HOH B 554     -74.257  18.815  11.917  1.00 22.16           O
HETATM 5906  O   HOH B 555     -79.155  21.313  21.830  1.00 20.64           O
HETATM 5907  O   HOH B 556     -54.650  45.780  39.989  1.00 59.11           O
HETATM 5908  O   HOH B 557     -61.443  16.036  33.893  1.00 42.28           O
HETATM 5909  O   HOH B 558     -86.764  23.979   2.175  1.00 53.42           O
HETATM 5910  O   HOH B 559     -65.186  32.805  25.052  1.00 52.59           O
HETATM 5911  O   HOH B 560     -67.212  18.228  14.562  1.00 26.73           O
HETATM 5912  O   HOH B 561     -81.443   6.187  25.222  1.00 57.06           O
HETATM 5913  O   HOH B 562     -83.646  46.953   3.724  1.00 39.44           O
HETATM 5914  O   HOH B 563     -79.996  13.148  17.251  1.00 48.52           O
HETATM 5915  O   HOH B 564     -58.050  43.414  25.005  1.00 32.71           O
HETATM 5916  O   HOH B 565     -76.239  -3.236  19.691  1.00 37.86           O
HETATM 5917  O   HOH B 566     -88.480  42.284  13.332  1.00 28.53           O
HETATM 5918  O   HOH B 567     -83.330  15.720   3.086  1.00 47.31           O
HETATM 5919  O   HOH B 568     -74.098  17.674   9.560  1.00 30.95           O
HETATM 5920  O   HOH B 569     -77.095  22.984  21.645  1.00 25.28           O
HETATM 5921  O   HOH B 570     -58.317   4.400  27.510  1.00 41.91           O
HETATM 5922  O   HOH B 571     -59.067  15.762  40.593  1.00 52.66           O
HETATM 5923  O   HOH B 572     -50.166  14.607  40.945  1.00 46.75           O
HETATM 5924  O   HOH B 573     -65.348  19.122  28.334  1.00 25.59           O
HETATM 5925  O   HOH B 574     -70.494  24.700  23.775  1.00 50.21           O
HETATM 5926  O   HOH B 575     -78.686   5.965  24.366  1.00 39.46           O
HETATM 5927  O   HOH B 576     -71.882  35.593  15.491  1.00 42.40           O
HETATM 5928  O   HOH B 577     -62.771   3.753  24.766  1.00 41.44           O
HETATM 5929  O   HOH B 578     -65.045   3.795  23.243  1.00 27.68           O
HETATM 5930  O   HOH B 579     -70.122  17.982  26.097  1.00 25.22           O
HETATM 5931  O   HOH B 580     -46.530  41.399  34.140  1.00 34.95           O
HETATM 5932  O   HOH B 581     -93.778  33.577   0.806  1.00 34.27           O
HETATM 5933  O   HOH B 582     -95.858  19.062  18.412  1.00 50.22           O
HETATM 5934  O   HOH B 583     -77.938  21.653  17.927  1.00 22.72           O
HETATM 5935  O   HOH B 584     -82.419   1.326  17.959  1.00 46.32           O
HETATM 5936  O   HOH B 585     -79.112  37.209   0.610  1.00 45.08           O
HETATM 5937  O   HOH B 586     -63.805  25.058  28.792  1.00 35.15           O
HETATM 5938  O   HOH B 587     -90.916  43.414   2.480  1.00 48.40           O
HETATM 5939  O   HOH B 588     -69.713  30.741   0.954  1.00 46.22           O
HETATM 5940  O   HOH B 589     -46.427  48.325  38.000  1.00 48.44           O
HETATM 5941  O   HOH B 590     -74.024  21.093  11.225  1.00 37.83           O
HETATM 5942  O   HOH B 591     -63.221   9.335  30.516  1.00 38.80           O
HETATM 5943  O   HOH B 592     -44.662  36.595  37.468  1.00 55.15           O
HETATM 5944  O   HOH B 593     -71.129  27.926  30.987  1.00 58.83           O
HETATM 5945  O   HOH B 594     -82.729  16.566  14.971  1.00 53.98           O
HETATM 5946  O   HOH B 595     -66.866  20.387  11.289  1.00 61.79           O
HETATM 5947  O   HOH B 596     -73.271  21.576  20.610  1.00 31.26           O
HETATM 5948  O   HOH B 597     -55.080   6.557  27.215  1.00 49.83           O
HETATM 5949  O   HOH B 598     -76.508  34.782  18.488  1.00 60.59           O
HETATM 5950  O   HOH B 599     -83.936  17.750  17.987  1.00 35.36           O
HETATM 5951  O   HOH B 600     -74.314  14.559  34.087  1.00 41.82           O
HETATM 5952  O   HOH B 601     -64.366   5.682  30.411  1.00 53.78           O
HETATM 5953  O   HOH B 602     -51.623  37.147  49.371  1.00 42.95           O
HETATM 5954  O   HOH B 603     -81.606  14.581  38.925  1.00 39.07           O
HETATM 5955  O   HOH B 604     -61.743  16.450  10.788  1.00 48.71           O
HETATM 5956  O   HOH B 605     -59.292  30.852  20.686  1.00 32.17           O
HETATM 5957  O   HOH B 606     -60.540  27.116  35.477  1.00 39.37           O
HETATM 5958  O   HOH B 607     -59.634  19.938  17.422  1.00 43.11           O
HETATM 5959  O   HOH B 608     -99.527  19.284  10.577  1.00 51.17           O
HETATM 5960  O   HOH B 609     -64.194  46.893  30.520  1.00 57.14           O
HETATM 5961  O   HOH B 610     -86.353  19.204  13.419  1.00 48.07           O
HETATM 5962  O   HOH B 611     -97.321  21.987   4.192  1.00 41.18           O
HETATM 5963  O   HOH B 612     -55.804  19.965  51.869  1.00 55.78           O
HETATM 5964  O   HOH B 613     -70.842  29.257   8.208  1.00 34.22           O
HETATM 5965  O   HOH B 614     -86.242   7.121  18.116  1.00 49.16           O
HETATM 5966  O   HOH B 615    -100.370  41.737  15.177  1.00 38.08           O
HETATM 5967  O   HOH B 616     -73.236  25.237  20.479  1.00 43.96           O
HETATM 5968  O   HOH B 617     -46.513  32.345  31.059  1.00 39.27           O
HETATM 5969  O   HOH B 618     -50.222  32.602  26.725  1.00 53.12           O
HETATM 5970  O   HOH B 619     -68.013  33.339  15.669  1.00 36.98           O
HETATM 5971  O   HOH B 620     -65.522  31.056  28.752  1.00 57.76           O
HETATM 5972  O   HOH B 621     -79.928   0.846  16.799  1.00 31.07           O
HETATM 5973  O   HOH B 622     -73.176  33.982  19.421  1.00 54.35           O
HETATM 5974  O   HOH B 623     -72.052   1.706  30.046  1.00 48.94           O
HETATM 5975  O   HOH B 624     -52.946  38.545  40.544  1.00 49.41           O
HETATM 5976  O   HOH B 625     -92.810  46.004   7.587  1.00 48.82           O
HETATM 5977  O   HOH B 626     -99.961  21.644  11.340  1.00 56.35           O
HETATM 5978  O   HOH B 627     -73.441   7.491  -2.291  1.00 43.44           O
HETATM 5979  O   HOH B 628     -66.171  31.499  21.022  1.00 74.25           O
HETATM 5980  O   HOH B 629     -76.428  13.725  33.454  1.00 61.79           O
HETATM 5981  O   HOH B 630     -51.653  10.877  20.370  1.00 56.42           O
HETATM 5982  O   HOH B 631     -67.278  -1.549   9.618  1.00 49.50           O
HETATM 5983  O   HOH B 632     -55.990   2.975  18.304  1.00 42.37           O
HETATM 5984  O   HOH B 633     -99.509  30.196  11.072  1.00 50.44           O
HETATM 5985  O   HOH B 634     -64.581  18.883  47.047  1.00 52.93           O
HETATM 5986  O   HOH B 635     -72.804  22.211   2.222  1.00 48.17           O
HETATM 5987  O   HOH B 636     -75.712  23.060  35.232  1.00 40.88           O
HETATM 5988  O   HOH B 637     -72.783  28.264  23.427  1.00 52.47           O
HETATM 5989  O   HOH B 638    -101.091  37.409  10.852  1.00 42.85           O
HETATM 5990  O   HOH B 639     -89.058  44.994   9.675  1.00 34.37           O
HETATM 5991  O   HOH B 640     -59.630  10.776  13.020  1.00 53.68           O
HETATM 5992  O   HOH B 641     -62.455  30.037  28.109  1.00 53.52           O
HETATM 5993  O   HOH B 642     -93.535  19.172   6.631  1.00 50.33           O
HETATM 5994  O   HOH B 643     -86.100  16.941   7.631  1.00 46.36           O
HETATM 5995  O   HOH B 644     -82.815   4.099  20.845  1.00 53.60           O
HETATM 5996  O   HOH B 645     -57.646  11.161  39.434  1.00 56.01           O
HETATM 5997  O   HOH B 646     -74.897  34.174   1.511  1.00 37.64           O
HETATM 5998  O   HOH B 647     -39.127  18.705  24.830  1.00 57.50           O
HETATM 5999  O   HOH B 648     -64.597  39.598  21.195  1.00 38.63           O
HETATM 6000  O   HOH B 649     -77.840   0.355  29.992  1.00 46.76           O
HETATM 6001  O   HOH B 650     -85.346  36.717  15.526  1.00 43.97           O
HETATM 6002  O   HOH B 651     -61.091   9.170  31.283  1.00 38.01           O
HETATM 6003  O   HOH B 652     -61.477  12.880  34.227  1.00 57.26           O
HETATM 6004  O   HOH B 653     -71.410  24.782  39.128  1.00 54.46           O
HETATM 6005  O   HOH B 654    -100.649  29.956   8.696  1.00 52.73           O
HETATM 6006  O   HOH B 655     -67.882  -3.874  11.726  1.00 42.37           O
HETATM 6007  O   HOH B 656     -62.455  17.840  12.729  1.00 50.09           O
HETATM 6008  O   HOH B 657     -86.610   7.495  15.484  1.00 76.60           O
HETATM 6009  O   HOH B 658     -70.800  -0.485  28.538  1.00 31.13           O
HETATM 6010  O   HOH B 659     -51.960  15.254  43.333  1.00 52.93           O
HETATM 6011  O   HOH B 660     -84.931  16.940   9.891  1.00 45.05           O
ENDMDL
MODEL        2
ATOM      1  N   ALA A   0     -78.312  73.911  -0.250  1.00 84.12           N
ANISOU    1  N   ALA A   0     8694  10754  12515   1463  -1341   1365       N
ATOM      2  CA  ALA A   0     -79.064  73.751  -1.490  1.00 81.50           C
ANISOU    2  CA  ALA A   0     8258  10390  12318   1359  -1177   1154       C
ATOM      3  C   ALA A   0     -78.775  72.398  -2.131  1.00 74.88           C
ANISOU    3  C   ALA A   0     7619   9375  11458   1204  -1039   1038       C
ATOM      4  O   ALA A   0     -79.548  71.915  -2.957  1.00 72.79           O
ANISOU    4  O   ALA A   0     7302   9114  11240   1065   -950    871       O
ATOM      5  CB  ALA A   0     -78.738  74.880  -2.460  1.00 83.08           C
ANISOU    5  CB  ALA A   0     8369  10457  12741   1531   -997   1138       C
ATOM      6  N  AMET A   1     -77.644  71.806  -1.747  0.57 71.75           N
ANISOU    6  N  AMET A   1     7448   8820  10992   1231  -1018   1135       N
ATOM      7  N  BMET A   1     -77.666  71.776  -1.748  0.43 71.64           N
ANISOU    7  N  BMET A   1     7434   8809  10975   1225  -1020   1131       N
ATOM      8  CA AMET A   1     -77.276  70.485  -2.237  0.57 67.18           C
ANISOU    8  CA AMET A   1     7045   8092  10387   1096   -911   1033       C
ATOM      9  CA BMET A   1     -77.294  70.496  -2.334  0.43 67.02           C
ANISOU    9  CA BMET A   1     7022   8065  10378   1095   -898   1022       C
ATOM     10  C  AMET A   1     -78.158  69.431  -1.584  0.57 62.96           C
ANISOU   10  C  AMET A   1     6486   7726   9709    911  -1070    970       C
ATOM     11  C  BMET A   1     -77.997  69.354  -1.611  0.43 62.70           C
ANISOU   11  C  BMET A   1     6482   7665   9678    916  -1055    976       C
ATOM     12  O  AMET A   1     -78.421  69.490  -0.377  0.57 64.38           O
ANISOU   12  O  AMET A   1     6635   8088   9737    884  -1271   1070       O
ATOM     13  O  BMET A   1     -77.950  69.263  -0.379  0.43 63.70           O
ANISOU   13  O  BMET A   1     6646   7926   9631    893  -1225   1087       O
ATOM     14  CB AMET A   1     -75.800  70.203  -1.947  0.57 67.02           C
ANISOU   14  CB AMET A   1     7261   7862  10342   1163   -836   1150       C
ATOM     15  CB BMET A   1     -75.780  70.306  -2.285  0.43 66.82           C
ANISOU   15  CB BMET A   1     7228   7802  10359   1172   -784   1117       C
ATOM     16  CG AMET A   1     -75.329  70.646  -0.560  0.57 68.96           C
ANISOU   16  CG AMET A   1     7559   8181  10461   1259  -1003   1383       C
ATOM     17  CG BMET A   1     -75.068  70.779  -3.533  0.43 65.28           C
ANISOU   17  CG BMET A   1     7090   7386  10327   1240   -538   1032       C
ATOM     18  SD AMET A   1     -75.532  69.420   0.754  0.57 64.50           S
ANISOU   18  SD AMET A   1     7104   7780   9622   1078  -1195   1439       S
ATOM     19  SD BMET A   1     -75.825  70.147  -5.042  0.43 58.41           S
ANISOU   19  SD BMET A   1     6162   6504   9527   1091   -393    787       S
ATOM     20  CE AMET A   1     -73.980  68.532   0.651  0.57 60.65           C
ANISOU   20  CE AMET A   1     6946   7016   9082   1023   -980   1440       C
ATOM     21  CE BMET A   1     -75.772  68.383  -4.741  0.43 54.39           C
ANISOU   21  CE BMET A   1     5805   6003   8857    907   -451    723       C
ATOM     22  N   SER A   2     -78.636  68.479  -2.384  1.00 52.97           N
ANISOU   22  N   SER A   2     5276   6416   8436    758   -956    779       N
ATOM     23  CA  SER A   2     -79.447  67.400  -1.839  1.00 42.55           C
ANISOU   23  CA  SER A   2     4011   5218   6938    558  -1026    660       C
ATOM     24  C   SER A   2     -79.560  66.282  -2.859  1.00 34.48           C
ANISOU   24  C   SER A   2     3104   4069   5928    449   -862    500       C
ATOM     25  O   SER A   2     -79.471  66.511  -4.067  1.00 32.94           O
ANISOU   25  O   SER A   2     2886   3765   5865    489   -728    456       O
ATOM     26  CB  SER A   2     -80.843  67.890  -1.444  1.00 44.73           C
ANISOU   26  CB  SER A   2     4069   5715   7212    476  -1165    610       C
ATOM     27  OG  SER A   2     -81.785  67.668  -2.480  1.00 39.74           O
ANISOU   27  OG  SER A   2     3364   5048   6686    379  -1050    455       O
ATOM     28  N   LEU A   3     -79.769  65.068  -2.348  1.00 30.26           N
ANISOU   28  N   LEU A   3     2691   3558   5249    314   -874    416       N
ATOM     29  CA  LEU A   3     -79.954  63.917  -3.222  1.00 29.43           C
ANISOU   29  CA  LEU A   3     2674   3351   5157    230   -749    290       C
ATOM     30  C   LEU A   3     -81.221  64.055  -4.056  1.00 28.78           C
ANISOU   30  C   LEU A   3     2481   3284   5170    169   -711    205       C
ATOM     31  O   LEU A   3     -81.208  63.792  -5.264  1.00 28.45           O
ANISOU   31  O   LEU A   3     2470   3143   5196    172   -595    170       O
ATOM     32  CB  LEU A   3     -79.997  62.636  -2.389  1.00 35.11           C
ANISOU   32  CB  LEU A   3     3513   4092   5735    121   -761    219       C
ATOM     33  CG  LEU A   3     -80.488  61.371  -3.092  1.00 33.17           C
ANISOU   33  CG  LEU A   3     3320   3764   5518     49   -664    102       C
ATOM     34  CD1 LEU A   3     -79.511  60.930  -4.167  1.00 34.73           C
ANISOU   34  CD1 LEU A   3     3585   3849   5763    106   -566    118       C
ATOM     35  CD2 LEU A   3     -80.726  60.256  -2.087  1.00 27.98           C
ANISOU   35  CD2 LEU A   3     2742   3136   4755    -46   -665     14       C
ATOM     36  N   GLU A   4     -82.322  64.472  -3.429  1.00 27.95           N
ANISOU   36  N   GLU A   4     2252   3311   5055     92   -806    169       N
ATOM     37  CA  GLU A   4     -83.583  64.599  -4.151  1.00 25.41           C
ANISOU   37  CA  GLU A   4     1832   2995   4829     -1   -749     80       C
ATOM     38  C   GLU A   4     -83.524  65.706  -5.195  1.00 24.88           C
ANISOU   38  C   GLU A   4     1634   2908   4911     88   -673    122       C
ATOM     39  O   GLU A   4     -84.208  65.625  -6.222  1.00 28.97           O
ANISOU   39  O   GLU A   4     2137   3369   5501     24   -554     64       O
ATOM     40  CB  GLU A   4     -84.728  64.851  -3.169  1.00 31.88           C
ANISOU   40  CB  GLU A   4     2535   3976   5602   -139   -864      7       C
ATOM     41  CG  GLU A   4     -85.098  63.653  -2.296  1.00 39.35           C
ANISOU   41  CG  GLU A   4     3622   4916   6415   -275   -877    -99       C
ATOM     42  CD  GLU A   4     -84.077  63.361  -1.206  1.00 48.87           C
ANISOU   42  CD  GLU A   4     4932   6177   7459   -229   -961    -38       C
ATOM     43  OE1 GLU A   4     -83.116  64.145  -1.052  1.00 50.66           O
ANISOU   43  OE1 GLU A   4     5127   6444   7676    -92  -1028    106       O
ATOM     44  OE2 GLU A   4     -84.236  62.342  -0.500  1.00 50.35           O
ANISOU   44  OE2 GLU A   4     5243   6352   7537   -331   -938   -136       O
ATOM     45  N   ASN A   5     -82.722  66.744  -4.954  1.00 27.17           N
ANISOU   45  N   ASN A   5     1837   3234   5253    238   -721    228       N
ATOM     46  CA  ASN A   5     -82.576  67.801  -5.948  1.00 29.85           C
ANISOU   46  CA  ASN A   5     2052   3531   5759    341   -610    249       C
ATOM     47  C   ASN A   5     -81.748  67.328  -7.135  1.00 29.00           C
ANISOU   47  C   ASN A   5     2115   3247   5657    369   -435    223       C
ATOM     48  O   ASN A   5     -82.039  67.683  -8.282  1.00 36.57           O
ANISOU   48  O   ASN A   5     3034   4161   6698    353   -288    169       O
ATOM     49  CB  ASN A   5     -81.950  69.041  -5.311  1.00 35.87           C
ANISOU   49  CB  ASN A   5     2673   4355   6602    521   -702    380       C
ATOM     50  CG  ASN A   5     -81.558  70.087  -6.332  1.00 42.39           C
ANISOU   50  CG  ASN A   5     3442   5094   7571    645   -529    383       C
ATOM     51  OD1 ASN A   5     -80.374  70.330  -6.565  1.00 47.47           O
ANISOU   51  OD1 ASN A   5     4196   5594   8246    773   -446    441       O
ATOM     52  ND2 ASN A   5     -82.553  70.708  -6.956  1.00 40.36           N
ANISOU   52  ND2 ASN A   5     3014   4914   7407    589   -455    304       N
ATOM     53  N   VAL A   6     -80.713  66.525  -6.879  1.00 26.57           N
ANISOU   53  N   VAL A   6     1993   2854   5247    391   -444    252       N
ATOM     54  CA  VAL A   6     -79.918  65.974  -7.973  1.00 24.01           C
ANISOU   54  CA  VAL A   6     1822   2400   4900    382   -302    209       C
ATOM     55  C   VAL A   6     -80.784  65.094  -8.861  1.00 25.80           C
ANISOU   55  C   VAL A   6     2101   2628   5075    253   -244    133       C
ATOM     56  O   VAL A   6     -80.700  65.152 -10.095  1.00 31.46           O
ANISOU   56  O   VAL A   6     2860   3296   5799    228   -115     94       O
ATOM     57  CB  VAL A   6     -78.708  65.201  -7.417  1.00 26.04           C
ANISOU   57  CB  VAL A   6     2240   2594   5059    396   -331    242       C
ATOM     58  CG1 VAL A   6     -78.004  64.446  -8.533  1.00 27.19           C
ANISOU   58  CG1 VAL A   6     2521   2654   5157    341   -215    174       C
ATOM     59  CG2 VAL A   6     -77.743  66.150  -6.723  1.00 23.40           C
ANISOU   59  CG2 VAL A   6     1895   2211   4786    532   -351    347       C
ATOM     60  N   ALA A   7     -81.638  64.271  -8.250  1.00 22.11           N
ANISOU   60  N   ALA A   7     1645   2207   4550    166   -328    114       N
ATOM     61  CA  ALA A   7     -82.520  63.413  -9.030  1.00 22.85           C
ANISOU   61  CA  ALA A   7     1800   2267   4616     65   -271     75       C
ATOM     62  C   ALA A   7     -83.553  64.224  -9.800  1.00 29.32           C
ANISOU   62  C   ALA A   7     2516   3106   5519      7   -179     50       C
ATOM     63  O   ALA A   7     -83.949  63.829 -10.903  1.00 30.49           O
ANISOU   63  O   ALA A   7     2742   3204   5640    -55    -78     47       O
ATOM     64  CB  ALA A   7     -83.204  62.397  -8.116  1.00 24.32           C
ANISOU   64  CB  ALA A   7     2026   2458   4758     -4   -350     47       C
ATOM     65  N   PHE A   8     -83.996  65.353  -9.242  1.00 30.37           N
ANISOU   65  N   PHE A   8     2466   3326   5748     21   -214     40       N
ATOM     66  CA  PHE A   8     -84.906  66.231  -9.969  1.00 28.94           C
ANISOU   66  CA  PHE A   8     2147   3180   5670    -40   -103      2       C
ATOM     67  C   PHE A   8     -84.268  66.718 -11.263  1.00 27.85           C
ANISOU   67  C   PHE A   8     2046   2982   5552     10     65     -2       C
ATOM     68  O   PHE A   8     -84.901  66.711 -12.325  1.00 27.71           O
ANISOU   68  O   PHE A   8     2061   2942   5526    -88    208    -32       O
ATOM     69  CB  PHE A   8     -85.310  67.414  -9.087  1.00 26.57           C
ANISOU   69  CB  PHE A   8     1595   3020   5482     -9   -194     -2       C
ATOM     70  CG  PHE A   8     -86.160  68.436  -9.794  1.00 37.77           C
ANISOU   70  CG  PHE A   8     2817   4496   7039    -66    -67    -54       C
ATOM     71  CD1 PHE A   8     -87.541  68.353  -9.760  1.00 39.06           C
ANISOU   71  CD1 PHE A   8     2900   4712   7229   -252    -44   -126       C
ATOM     72  CD2 PHE A   8     -85.578  69.485 -10.489  1.00 40.93           C
ANISOU   72  CD2 PHE A   8     3110   4886   7555     55     58    -48       C
ATOM     73  CE1 PHE A   8     -88.325  69.291 -10.408  1.00 38.02           C
ANISOU   73  CE1 PHE A   8     2573   4642   7230   -328     94   -183       C
ATOM     74  CE2 PHE A   8     -86.355  70.421 -11.143  1.00 41.01           C
ANISOU   74  CE2 PHE A   8     2921   4958   7705     -1    203   -112       C
ATOM     75  CZ  PHE A   8     -87.729  70.327 -11.099  1.00 40.28           C
ANISOU   75  CZ  PHE A   8     2735   4938   7630   -198    218   -176       C
ATOM     76  N   ASN A   9     -83.010  67.155 -11.189  1.00 29.15           N
ANISOU   76  N   ASN A   9     2228   3113   5737    146     69     22       N
ATOM     77  CA  ASN A   9     -82.334  67.672 -12.374  1.00 31.72           C
ANISOU   77  CA  ASN A   9     2599   3371   6082    178    253    -20       C
ATOM     78  C   ASN A   9     -82.147  66.585 -13.422  1.00 27.90           C
ANISOU   78  C   ASN A   9     2335   2842   5426     73    319    -39       C
ATOM     79  O   ASN A   9     -82.263  66.848 -14.624  1.00 33.74           O
ANISOU   79  O   ASN A   9     3119   3572   6128      6    486    -89       O
ATOM     80  CB  ASN A   9     -80.986  68.278 -11.986  1.00 31.80           C
ANISOU   80  CB  ASN A   9     2610   3312   6161    338    254      5       C
ATOM     81  CG  ASN A   9     -81.123  69.631 -11.317  1.00 31.70           C
ANISOU   81  CG  ASN A   9     2356   3343   6346    481    230     46       C
ATOM     82  OD1 ASN A   9     -80.984  70.669 -11.962  1.00 34.08           O
ANISOU   82  OD1 ASN A   9     2549   3607   6794    555    396      2       O
ATOM     83  ND2 ASN A   9     -81.394  69.626 -10.017  1.00 34.15           N
ANISOU   83  ND2 ASN A   9     2572   3743   6658    521     25    130       N
ATOM     84  N   VAL A  10     -81.863  65.358 -12.987  1.00 23.18           N
ANISOU   84  N   VAL A  10     1863   2230   4713     56    189      3       N
ATOM     85  CA  VAL A  10     -81.623  64.278 -13.937  1.00 27.76           C
ANISOU   85  CA  VAL A  10     2618   2796   5132    -21    212     10       C
ATOM     86  C   VAL A  10     -82.895  63.952 -14.709  1.00 30.23           C
ANISOU   86  C   VAL A  10     2965   3122   5400   -132    272     38       C
ATOM     87  O   VAL A  10     -82.866  63.780 -15.933  1.00 34.51           O
ANISOU   87  O   VAL A  10     3615   3675   5822   -205    371     40       O
ATOM     88  CB  VAL A  10     -81.064  63.043 -13.209  1.00 28.33           C
ANISOU   88  CB  VAL A  10     2771   2861   5133      5     62     48       C
ATOM     89  CG1 VAL A  10     -80.969  61.864 -14.163  1.00 30.18           C
ANISOU   89  CG1 VAL A  10     3138   3112   5217    -58     50     79       C
ATOM     90  CG2 VAL A  10     -79.700  63.355 -12.612  1.00 26.78           C
ANISOU   90  CG2 VAL A  10     2580   2636   4960     84     42     26       C
ATOM     91  N   VAL A  11     -84.032  63.879 -14.015  1.00 32.63           N
ANISOU   91  N   VAL A  11     3190   3422   5785   -165    222     58       N
ATOM     92  CA  VAL A  11     -85.264  63.475 -14.681  1.00 35.02           C
ANISOU   92  CA  VAL A  11     3554   3694   6058   -282    294     98       C
ATOM     93  C   VAL A  11     -85.825  64.600 -15.544  1.00 41.84           C
ANISOU   93  C   VAL A  11     4345   4588   6966   -364    482     52       C
ATOM     94  O   VAL A  11     -86.539  64.337 -16.517  1.00 45.71           O
ANISOU   94  O   VAL A  11     4939   5053   7375   -476    594     96       O
ATOM     95  CB  VAL A  11     -86.303  62.989 -13.654  1.00 36.03           C
ANISOU   95  CB  VAL A  11     3640   3780   6268   -322    212    104       C
ATOM     96  CG1 VAL A  11     -85.744  61.837 -12.836  1.00 36.54           C
ANISOU   96  CG1 VAL A  11     3779   3814   6292   -244     66    130       C
ATOM     97  CG2 VAL A  11     -86.736  64.123 -12.747  1.00 42.72           C
ANISOU   97  CG2 VAL A  11     4276   4701   7254   -336    195     25       C
ATOM     98  N   ASN A  12     -85.516  65.855 -15.223  1.00 26.45           N
ANISOU   98  N   ASN A  12     2214   2689   5145   -306    530    -24       N
ATOM     99  CA  ASN A  12     -86.055  66.983 -15.971  1.00 35.54           C
ANISOU   99  CA  ASN A  12     3249   3877   6376   -374    730    -89       C
ATOM    100  C   ASN A  12     -85.075  67.575 -16.972  1.00 36.46           C
ANISOU  100  C   ASN A  12     3418   3993   6443   -338    892   -150       C
ATOM    101  O   ASN A  12     -85.504  68.064 -18.022  1.00 39.47           O
ANISOU  101  O   ASN A  12     3812   4391   6792   -443   1102   -198       O
ATOM    102  CB  ASN A  12     -86.515  68.090 -15.015  1.00 42.27           C
ANISOU  102  CB  ASN A  12     3814   4803   7443   -330    697   -140       C
ATOM    103  CG  ASN A  12     -87.710  67.679 -14.179  1.00 48.37           C
ANISOU  103  CG  ASN A  12     4524   5596   8257   -437    590   -130       C
ATOM    104  OD1 ASN A  12     -88.844  67.660 -14.660  1.00 52.49           O
ANISOU  104  OD1 ASN A  12     5044   6105   8793   -601    708   -148       O
ATOM    105  ND2 ASN A  12     -87.464  67.360 -12.915  1.00 50.76           N
ANISOU  105  ND2 ASN A  12     4789   5926   8573   -364    384   -112       N
ATOM    106  N   LYS A  13     -83.775  67.548 -16.678  1.00 34.55           N
ANISOU  106  N   LYS A  13     3217   3721   6189   -213    825   -165       N
ATOM    107  CA  LYS A  13     -82.775  68.161 -17.540  1.00 33.39           C
ANISOU  107  CA  LYS A  13     3125   3545   6016   -189    999   -259       C
ATOM    108  C   LYS A  13     -81.778  67.168 -18.118  1.00 32.36           C
ANISOU  108  C   LYS A  13     3231   3400   5663   -232    956   -257       C
ATOM    109  O   LYS A  13     -80.857  67.584 -18.830  1.00 36.03           O
ANISOU  109  O   LYS A  13     3770   3837   6081   -244   1102   -362       O
ATOM    110  CB  LYS A  13     -82.015  69.255 -16.775  1.00 31.68           C
ANISOU  110  CB  LYS A  13     2737   3281   6021     -7   1010   -299       C
ATOM    111  CG  LYS A  13     -82.877  70.431 -16.349  1.00 38.11           C
ANISOU  111  CG  LYS A  13     3264   4147   7069     50   1064   -312       C
ATOM    112  CD  LYS A  13     -83.356  71.230 -17.550  1.00 44.29           C
ANISOU  112  CD  LYS A  13     3992   4949   7887    -42   1353   -423       C
ATOM    113  CE  LYS A  13     -84.135  72.465 -17.123  1.00 50.29           C
ANISOU  113  CE  LYS A  13     4413   5781   8916     24   1414   -450       C
ATOM    114  NZ  LYS A  13     -84.534  73.303 -18.288  1.00 51.04           N
ANISOU  114  NZ  LYS A  13     4434   5892   9067    -64   1738   -579       N
ATOM    115  N   GLY A  14     -81.933  65.873 -17.848  1.00 33.40           N
ANISOU  115  N   GLY A  14     3470   3553   5667   -262    770   -156       N
ATOM    116  CA  GLY A  14     -80.987  64.881 -18.312  1.00 30.51           C
ANISOU  116  CA  GLY A  14     3278   3211   5106   -299    696   -149       C
ATOM    117  C   GLY A  14     -79.669  64.857 -17.576  1.00 31.15           C
ANISOU  117  C   GLY A  14     3352   3242   5242   -205    623   -195       C
ATOM    118  O   GLY A  14     -78.893  63.913 -17.764  1.00 27.14           O
ANISOU  118  O   GLY A  14     2953   2768   4591   -245    532   -192       O
ATOM    119  N   HIS A  15     -79.390  65.856 -16.748  1.00 32.39           N
ANISOU  119  N   HIS A  15     3378   3324   5603    -84    658   -225       N
ATOM    120  CA  HIS A  15     -78.175  65.941 -15.945  1.00 30.53           C
ANISOU  120  CA  HIS A  15     3151   3010   5439     12    606   -239       C
ATOM    121  C   HIS A  15     -78.405  67.043 -14.919  1.00 30.80           C
ANISOU  121  C   HIS A  15     3007   2992   5703    165    599   -198       C
ATOM    122  O   HIS A  15     -79.460  67.684 -14.899  1.00 34.54           O
ANISOU  122  O   HIS A  15     3336   3514   6275    179    629   -183       O
ATOM    123  CB  HIS A  15     -76.944  66.228 -16.806  1.00 30.97           C
ANISOU  123  CB  HIS A  15     3330   3003   5435    -41    770   -371       C
ATOM    124  CG  HIS A  15     -76.878  67.636 -17.307  1.00 32.88           C
ANISOU  124  CG  HIS A  15     3509   3159   5825      8   1008   -471       C
ATOM    125  ND1 HIS A  15     -77.923  68.238 -17.975  1.00 33.27           N
ANISOU  125  ND1 HIS A  15     3477   3266   5898    -30   1134   -496       N
ATOM    126  CD2 HIS A  15     -75.894  68.563 -17.234  1.00 29.40           C
ANISOU  126  CD2 HIS A  15     3070   2563   5539     99   1166   -555       C
ATOM    127  CE1 HIS A  15     -77.584  69.475 -18.293  1.00 35.39           C
ANISOU  127  CE1 HIS A  15     3676   3436   6333     41   1361   -603       C
ATOM    128  NE2 HIS A  15     -76.358  69.697 -17.855  1.00 35.91           N
ANISOU  128  NE2 HIS A  15     3796   3359   6489    132   1384   -636       N
ATOM    129  N   PHE A  16     -77.410  67.268 -14.068  1.00 30.88           N
ANISOU  129  N   PHE A  16     3024   2915   5796    274    555   -170       N
ATOM    130  CA  PHE A  16     -77.510  68.357 -13.105  1.00 33.38           C
ANISOU  130  CA  PHE A  16     3173   3195   6317    442    526    -96       C
ATOM    131  C   PHE A  16     -77.355  69.690 -13.825  1.00 40.24           C
ANISOU  131  C   PHE A  16     3952   3980   7356    523    751   -173       C
ATOM    132  O   PHE A  16     -76.327  69.945 -14.461  1.00 47.25           O
ANISOU  132  O   PHE A  16     4960   4734   8258    522    924   -268       O
ATOM    133  CB  PHE A  16     -76.458  68.214 -12.009  1.00 29.40           C
ANISOU  133  CB  PHE A  16     2731   2606   5834    536    426    -12       C
ATOM    134  CG  PHE A  16     -76.600  69.228 -10.909  1.00 29.87           C
ANISOU  134  CG  PHE A  16     2625   2660   6064    718    342    114       C
ATOM    135  CD1 PHE A  16     -77.506  69.029  -9.879  1.00 27.72           C
ANISOU  135  CD1 PHE A  16     2237   2537   5759    720    135    206       C
ATOM    136  CD2 PHE A  16     -75.840  70.387 -10.911  1.00 32.94           C
ANISOU  136  CD2 PHE A  16     2972   2898   6645    886    468    140       C
ATOM    137  CE1 PHE A  16     -77.646  69.961  -8.867  1.00 32.02           C
ANISOU  137  CE1 PHE A  16     2625   3130   6412    868     23    331       C
ATOM    138  CE2 PHE A  16     -75.975  71.325  -9.902  1.00 36.71           C
ANISOU  138  CE2 PHE A  16     3333   3441   7176   1024    348    284       C
ATOM    139  CZ  PHE A  16     -76.879  71.111  -8.878  1.00 39.33           C
ANISOU  139  CZ  PHE A  16     3548   3960   7434   1012    117    380       C
ATOM    140  N   ASP A  17     -78.380  70.537 -13.728  1.00 35.96           N
ANISOU  140  N   ASP A  17     3191   3516   6956    580    765   -153       N
ATOM    141  CA  ASP A  17     -78.376  71.844 -14.371  1.00 33.43           C
ANISOU  141  CA  ASP A  17     2732   3133   6836    672    994   -232       C
ATOM    142  C   ASP A  17     -78.544  72.979 -13.368  1.00 37.00           C
ANISOU  142  C   ASP A  17     2952   3610   7496    873    898   -114       C
ATOM    143  O   ASP A  17     -78.720  74.133 -13.776  1.00 40.64           O
ANISOU  143  O   ASP A  17     3289   4069   8082    939   1037   -155       O
ATOM    144  CB  ASP A  17     -79.477  71.912 -15.435  1.00 43.04           C
ANISOU  144  CB  ASP A  17     3897   4458   7998    515   1137   -332       C
ATOM    145  CG  ASP A  17     -79.215  72.977 -16.481  1.00 56.60           C
ANISOU  145  CG  ASP A  17     5566   6092   9849    544   1456   -479       C
ATOM    146  OD1 ASP A  17     -78.041  73.368 -16.651  1.00 63.42           O
ANISOU  146  OD1 ASP A  17     6522   6785  10790    639   1591   -539       O
ATOM    147  OD2 ASP A  17     -80.184  73.430 -17.127  1.00 61.43           O
ANISOU  147  OD2 ASP A  17     6050   6794  10496    462   1596   -546       O
ATOM    148  N   GLY A  18     -78.496  72.684 -12.072  1.00 35.84           N
ANISOU  148  N   GLY A  18     2802   3528   7287    928    637     37       N
ATOM    149  CA  GLY A  18     -78.646  73.715 -11.064  1.00 34.96           C
ANISOU  149  CA  GLY A  18     2542   3505   7238   1073    494    167       C
ATOM    150  C   GLY A  18     -80.060  74.206 -10.862  1.00 35.96           C
ANISOU  150  C   GLY A  18     2418   3845   7401   1031    408    163       C
ATOM    151  O   GLY A  18     -80.255  75.345 -10.428  1.00 46.31           O
ANISOU  151  O   GLY A  18     3552   5239   8805   1160    362    223       O
ATOM    152  N   GLN A  19     -81.056  73.379 -11.160  1.00 37.43           N
ANISOU  152  N   GLN A  19     2580   4121   7519    850    388     92       N
ATOM    153  CA  GLN A  19     -82.452  73.771 -11.046  1.00 39.71           C
ANISOU  153  CA  GLN A  19     2651   4600   7838    758    337     61       C
ATOM    154  C   GLN A  19     -83.013  73.384  -9.683  1.00 42.17           C
ANISOU  154  C   GLN A  19     2911   5075   8038    718     55    147       C
ATOM    155  O   GLN A  19     -82.570  72.417  -9.057  1.00 46.46           O
ANISOU  155  O   GLN A  19     3614   5580   8460    695    -73    200       O
ATOM    156  CB  GLN A  19     -83.285  73.120 -12.152  1.00 41.04           C
ANISOU  156  CB  GLN A  19     2837   4761   7995    554    506    -66       C
ATOM    157  CG  GLN A  19     -82.721  73.303 -13.553  1.00 46.18           C
ANISOU  157  CG  GLN A  19     3576   5270   8699    551    807   -175       C
ATOM    158  CD  GLN A  19     -82.752  74.746 -14.018  1.00 52.43           C
ANISOU  158  CD  GLN A  19     4214   6069   9637    645    974   -228       C
ATOM    159  OE1 GLN A  19     -83.597  75.531 -13.589  1.00 56.41           O
ANISOU  159  OE1 GLN A  19     4498   6724  10210    657    900   -209       O
ATOM    160  NE2 GLN A  19     -81.827  75.102 -14.902  1.00 55.19           N
ANISOU  160  NE2 GLN A  19     4675   6263  10033    704   1208   -311       N
ATOM    161  N   GLN A  20     -83.997  74.156  -9.228  1.00 44.50           N
ANISOU  161  N   GLN A  20     2974   5568   8367    695    -31    144       N
ATOM    162  CA  GLN A  20     -84.679  73.863  -7.976  1.00 46.28           C
ANISOU  162  CA  GLN A  20     3128   5983   8472    616   -279    186       C
ATOM    163  C   GLN A  20     -85.765  72.816  -8.189  1.00 43.02           C
ANISOU  163  C   GLN A  20     2761   5592   7994    361   -268     78       C
ATOM    164  O   GLN A  20     -86.414  72.768  -9.237  1.00 46.09           O
ANISOU  164  O   GLN A  20     3125   5933   8453    240    -81    -22       O
ATOM    165  CB  GLN A  20     -85.302  75.129  -7.388  1.00 54.62           C
ANISOU  165  CB  GLN A  20     3895   7276   9582    680   -382    214       C
ATOM    166  CG  GLN A  20     -84.313  76.103  -6.779  1.00 70.11           C
ANISOU  166  CG  GLN A  20     5804   9249  11584    948   -467    359       C
ATOM    167  CD  GLN A  20     -84.999  77.319  -6.189  1.00 89.11           C
ANISOU  167  CD  GLN A  20     7888  11928  14040   1019   -592    386       C
ATOM    168  OE1 GLN A  20     -86.099  77.686  -6.603  1.00 92.82           O
ANISOU  168  OE1 GLN A  20     8153  12544  14571    886   -531    276       O
ATOM    169  NE2 GLN A  20     -84.355  77.947  -5.212  1.00 98.18           N
ANISOU  169  NE2 GLN A  20     8989  13155  15160   1225   -770    537       N
ATOM    170  N   GLY A  21     -85.965  71.987  -7.181  1.00 36.47           N
ANISOU  170  N   GLY A  21     2007   4823   7026    274   -452     96       N
ATOM    171  CA  GLY A  21     -86.983  70.953  -7.211  1.00 33.55           C
ANISOU  171  CA  GLY A  21     1701   4447   6598     36   -448     -8       C
ATOM    172  C   GLY A  21     -86.482  69.678  -6.562  1.00 40.06           C
ANISOU  172  C   GLY A  21     2734   5188   7301     10   -556     17       C
ATOM    173  O   GLY A  21     -85.283  69.440  -6.426  1.00 41.41           O
ANISOU  173  O   GLY A  21     3030   5266   7440    158   -583    107       O
ATOM    174  N   GLU A  22     -87.429  68.839  -6.146  1.00 39.34           N
ANISOU  174  N   GLU A  22     2684   5119   7145   -193   -600    -75       N
ATOM    175  CA  GLU A  22     -87.116  67.567  -5.511  1.00 39.83           C
ANISOU  175  CA  GLU A  22     2975   5101   7056   -236   -667    -82       C
ATOM    176  C   GLU A  22     -88.086  66.502  -5.996  1.00 42.20           C
ANISOU  176  C   GLU A  22     3426   5273   7336   -422   -542   -189       C
ATOM    177  O   GLU A  22     -89.278  66.770  -6.170  1.00 44.84           O
ANISOU  177  O   GLU A  22     3649   5648   7742   -590   -487   -281       O
ATOM    178  CB  GLU A  22     -87.184  67.662  -3.979  1.00 46.88           C
ANISOU  178  CB  GLU A  22     3804   6180   7829   -275   -888    -79       C
ATOM    179  CG  GLU A  22     -86.020  68.397  -3.331  1.00 58.49           C
ANISOU  179  CG  GLU A  22     5217   7736   9272    -67  -1030     82       C
ATOM    180  CD  GLU A  22     -86.210  69.901  -3.309  1.00 70.41           C
ANISOU  180  CD  GLU A  22     6501   9416  10835     34  -1065    142       C
ATOM    181  OE1 GLU A  22     -87.323  70.367  -3.634  1.00 74.79           O
ANISOU  181  OE1 GLU A  22     6896  10072  11448    -92  -1016     42       O
ATOM    182  OE2 GLU A  22     -85.246  70.617  -2.965  1.00 75.02           O
ANISOU  182  OE2 GLU A  22     7068  10024  11411    238  -1130    289       O
ATOM    183  N   VAL A  23     -87.567  65.297  -6.213  1.00 41.19           N
ANISOU  183  N   VAL A  23     3542   4985   7125   -389   -492   -169       N
ATOM    184  CA  VAL A  23     -88.394  64.136  -6.536  1.00 40.99           C
ANISOU  184  CA  VAL A  23     3678   4809   7088   -520   -390   -236       C
ATOM    185  C   VAL A  23     -88.113  63.058  -5.495  1.00 34.45           C
ANISOU  185  C   VAL A  23     2989   3951   6149   -528   -466   -273       C
ATOM    186  O   VAL A  23     -87.004  63.009  -4.944  1.00 31.70           O
ANISOU  186  O   VAL A  23     2674   3653   5719   -410   -555   -213       O
ATOM    187  CB  VAL A  23     -88.127  63.630  -7.964  1.00 25.43           C
ANISOU  187  CB  VAL A  23     1848   2678   5137   -463   -241   -166       C
ATOM    188  CG1 VAL A  23     -88.413  64.725  -8.981  1.00 26.40           C
ANISOU  188  CG1 VAL A  23     1843   2838   5349   -478   -130   -152       C
ATOM    189  CG2 VAL A  23     -86.703  63.139  -8.100  1.00 23.75           C
ANISOU  189  CG2 VAL A  23     1751   2429   4846   -301   -277    -85       C
ATOM    190  N   PRO A  24     -89.077  62.195  -5.176  1.00 34.92           N
ANISOU  190  N   PRO A  24     3139   3916   6212   -671   -409   -378       N
ATOM    191  CA  PRO A  24     -88.829  61.165  -4.158  1.00 30.62           C
ANISOU  191  CA  PRO A  24     2720   3338   5574   -682   -445   -442       C
ATOM    192  C   PRO A  24     -87.855  60.111  -4.659  1.00 32.21           C
ANISOU  192  C   PRO A  24     3072   3405   5762   -526   -396   -355       C
ATOM    193  O   PRO A  24     -87.934  59.655  -5.803  1.00 26.60           O
ANISOU  193  O   PRO A  24     2430   2557   5121   -473   -301   -285       O
ATOM    194  CB  PRO A  24     -90.220  60.573  -3.902  1.00 33.62           C
ANISOU  194  CB  PRO A  24     3159   3605   6011   -878   -345   -593       C
ATOM    195  CG  PRO A  24     -90.985  60.859  -5.151  1.00 36.51           C
ANISOU  195  CG  PRO A  24     3509   3859   6507   -921   -220   -549       C
ATOM    196  CD  PRO A  24     -90.467  62.171  -5.663  1.00 32.88           C
ANISOU  196  CD  PRO A  24     2873   3565   6055   -845   -286   -457       C
ATOM    197  N   VAL A  25     -86.934  59.716  -3.782  1.00 31.92           N
ANISOU  197  N   VAL A  25     3080   3426   5622   -466   -464   -357       N
ATOM    198  CA  VAL A  25     -85.843  58.816  -4.130  1.00 27.47           C
ANISOU  198  CA  VAL A  25     2614   2784   5041   -331   -434   -286       C
ATOM    199  C   VAL A  25     -85.784  57.682  -3.117  1.00 28.15           C
ANISOU  199  C   VAL A  25     2788   2832   5076   -364   -403   -387       C
ATOM    200  O   VAL A  25     -85.931  57.904  -1.910  1.00 29.96           O
ANISOU  200  O   VAL A  25     3011   3170   5202   -461   -454   -478       O
ATOM    201  CB  VAL A  25     -84.493  59.564  -4.182  1.00 29.34           C
ANISOU  201  CB  VAL A  25     2811   3122   5216   -220   -510   -181       C
ATOM    202  CG1 VAL A  25     -83.347  58.593  -4.409  1.00 30.15           C
ANISOU  202  CG1 VAL A  25     3002   3163   5290   -128   -476   -142       C
ATOM    203  CG2 VAL A  25     -84.517  60.623  -5.268  1.00 25.68           C
ANISOU  203  CG2 VAL A  25     2263   2669   4824   -176   -496   -106       C
ATOM    204  N   SER A  26     -85.575  56.464  -3.611  1.00 29.62           N
ANISOU  204  N   SER A  26     3047   2878   5329   -283   -318   -372       N
ATOM    205  CA  SER A  26     -85.280  55.310  -2.776  1.00 30.37           C
ANISOU  205  CA  SER A  26     3202   2930   5405   -275   -259   -462       C
ATOM    206  C   SER A  26     -83.967  54.691  -3.233  1.00 31.62           C
ANISOU  206  C   SER A  26     3357   3099   5559   -141   -264   -372       C
ATOM    207  O   SER A  26     -83.724  54.542  -4.435  1.00 33.24           O
ANISOU  207  O   SER A  26     3547   3259   5826    -51   -270   -263       O
ATOM    208  CB  SER A  26     -86.403  54.271  -2.835  1.00 34.36           C
ANISOU  208  CB  SER A  26     3770   3239   6046   -301   -127   -553       C
ATOM    209  OG  SER A  26     -86.542  53.742  -4.141  1.00 44.33           O
ANISOU  209  OG  SER A  26     5043   4365   7435   -182    -91   -424       O
ATOM    210  N   ILE A  27     -83.116  54.342  -2.275  1.00 27.57           N
ANISOU  210  N   ILE A  27     2860   2660   4954   -152   -257   -425       N
ATOM    211  CA  ILE A  27     -81.803  53.776  -2.556  1.00 25.53           C
ANISOU  211  CA  ILE A  27     2584   2430   4686    -66   -250   -368       C
ATOM    212  C   ILE A  27     -81.770  52.355  -2.018  1.00 30.84           C
ANISOU  212  C   ILE A  27     3257   3041   5420    -45   -136   -472       C
ATOM    213  O   ILE A  27     -81.988  52.133  -0.820  1.00 37.01           O
ANISOU  213  O   ILE A  27     4084   3844   6133   -135    -71   -601       O
ATOM    214  CB  ILE A  27     -80.672  54.618  -1.948  1.00 27.57           C
ANISOU  214  CB  ILE A  27     2859   2815   4800    -98   -310   -323       C
ATOM    215  CG1 ILE A  27     -80.535  55.942  -2.703  1.00 22.55           C
ANISOU  215  CG1 ILE A  27     2197   2211   4161    -68   -397   -208       C
ATOM    216  CG2 ILE A  27     -79.363  53.843  -1.964  1.00 24.70           C
ANISOU  216  CG2 ILE A  27     2489   2470   4427    -64   -259   -315       C
ATOM    217  CD1 ILE A  27     -79.379  56.789  -2.238  1.00 27.68           C
ANISOU  217  CD1 ILE A  27     2872   2935   4711    -63   -441   -133       C
ATOM    218  N  AILE A  28     -81.464  51.405  -2.897  0.52 31.75           N
ANISOU  218  N  AILE A  28     3311   3098   5655     71   -112   -418       N
ATOM    219  N  BILE A  28     -81.539  51.390  -2.902  0.48 31.95           N
ANISOU  219  N  BILE A  28     3338   3116   5686     72   -109   -420       N
ATOM    220  CA AILE A  28     -81.350  49.998  -2.532  0.52 34.28           C
ANISOU  220  CA AILE A  28     3581   3361   6082    133      0   -500       C
ATOM    221  CA BILE A  28     -81.473  49.992  -2.500  0.48 34.33           C
ANISOU  221  CA BILE A  28     3594   3357   6095    131      6   -507       C
ATOM    222  C  AILE A  28     -80.501  49.307  -3.592  0.52 34.71           C
ANISOU  222  C  AILE A  28     3523   3455   6210    254    -48   -393       C
ATOM    223  C  BILE A  28     -80.459  49.297  -3.395  0.48 34.81           C
ANISOU  223  C  BILE A  28     3540   3472   6213    241    -34   -414       C
ATOM    224  O  AILE A  28     -80.577  49.637  -4.779  0.52 34.83           O
ANISOU  224  O  AILE A  28     3528   3473   6233    305   -144   -262       O
ATOM    225  O  BILE A  28     -80.283  49.661  -4.561  0.48 33.58           O
ANISOU  225  O  BILE A  28     3363   3344   6050    286   -138   -283       O
ATOM    226  CB AILE A  28     -82.748  49.346  -2.387  0.52 36.24           C
ANISOU  226  CB AILE A  28     3866   3425   6480    160    104   -578       C
ATOM    227  CB BILE A  28     -82.865  49.313  -2.548  0.48 36.20           C
ANISOU  227  CB BILE A  28     3860   3400   6495    175    101   -562       C
ATOM    228  CG1AILE A  28     -82.630  47.890  -1.934  0.52 36.66           C
ANISOU  228  CG1AILE A  28     3852   3398   6677    249    251   -677       C
ATOM    229  CG1BILE A  28     -82.812  47.921  -1.915  0.48 36.80           C
ANISOU  229  CG1BILE A  28     3884   3396   6702    244    258   -684       C
ATOM    230  CG2AILE A  28     -83.532  49.449  -3.687  0.52 36.41           C
ANISOU  230  CG2AILE A  28     3894   3334   6607    245     48   -432       C
ATOM    231  CG2BILE A  28     -83.391  49.242  -3.967  0.48 36.80           C
ANISOU  231  CG2BILE A  28     3919   3381   6680    287     37   -396       C
ATOM    232  CD1AILE A  28     -83.965  47.200  -1.752  0.52 39.24           C
ANISOU  232  CD1AILE A  28     4232   3493   7184    288    393   -766       C
ATOM    233  CD1BILE A  28     -84.156  47.236  -1.843  0.48 39.25           C
ANISOU  233  CD1BILE A  28     4245   3467   7200    290    393   -758       C
ATOM    234  N  AASN A  29     -79.662  48.368  -3.145  0.52 37.36           N
ANISOU  234  N  AASN A  29     3768   3847   6581    277     22   -460       N
ATOM    235  N  BASN A  29     -79.784  48.303  -2.830  0.48 38.03           N
ANISOU  235  N  BASN A  29     3866   3917   6666    262     55   -498       N
ATOM    236  CA AASN A  29     -78.869  47.512  -4.035  0.52 40.71           C
ANISOU  236  CA AASN A  29     4039   4341   7089    380    -25   -387       C
ATOM    237  CA BASN A  29     -78.591  47.694  -3.436  0.48 39.75           C
ANISOU  237  CA BASN A  29     3945   4246   6911    315     16   -447       C
ATOM    238  C  AASN A  29     -77.884  48.319  -4.882  0.52 37.52           C
ANISOU  238  C  AASN A  29     3635   4065   6556    323   -150   -293       C
ATOM    239  C  BASN A  29     -77.596  48.837  -3.664  0.48 37.64           C
ANISOU  239  C  BASN A  29     3736   4092   6472    207    -71   -392       C
ATOM    240  O  AASN A  29     -77.715  48.059  -6.075  0.52 32.27           O
ANISOU  240  O  AASN A  29     2896   3448   5916    391   -249   -188       O
ATOM    241  O  BASN A  29     -77.416  49.684  -2.776  0.48 35.29           O
ANISOU  241  O  BASN A  29     3549   3814   6047     99    -45   -432       O
ATOM    242  CB AASN A  29     -79.771  46.662  -4.936  0.52 43.88           C
ANISOU  242  CB AASN A  29     4374   4629   7668    552    -51   -288       C
ATOM    243  CB BASN A  29     -78.972  46.905  -4.677  0.48 42.49           C
ANISOU  243  CB BASN A  29     4182   4554   7407    478    -57   -326       C
ATOM    244  CG AASN A  29     -80.835  45.910  -4.161  0.52 47.27           C
ANISOU  244  CG AASN A  29     4828   4872   8260    614    105   -390       C
ATOM    245  CG BASN A  29     -80.237  46.089  -4.484  0.48 45.73           C
ANISOU  245  CG BASN A  29     4597   4774   8005    598     39   -348       C
ATOM    246  OD1AASN A  29     -82.014  45.936  -4.519  0.52 47.98           O
ANISOU  246  OD1AASN A  29     4999   4791   8439    669    120   -336       O
ATOM    247  OD1BASN A  29     -81.217  46.262  -5.209  0.48 47.37           O
ANISOU  247  OD1BASN A  29     4872   4861   8266    662     -6   -239       O
ATOM    248  ND2AASN A  29     -80.424  45.232  -3.096  0.52 48.16           N
ANISOU  248  ND2AASN A  29     4882   5003   8414    590    249   -552       N
ATOM    249  ND2BASN A  29     -80.222  45.195  -3.502  0.48 47.79           N
ANISOU  249  ND2BASN A  29     4798   4990   8372    620    198   -496       N
ATOM    250  N  AASN A  30     -77.221  49.298  -4.261  0.52 34.88           N
ANISOU  250  N  AASN A  30     3393   3783   6078    195   -138   -330       N
ATOM    251  N  BASN A  30     -76.943  48.895  -4.821  0.48 34.58           N
ANISOU  251  N  BASN A  30     3284   3778   6076    233   -169   -300       N
ATOM    252  CA AASN A  30     -76.245  50.160  -4.938  0.52 31.35           C
ANISOU  252  CA AASN A  30     2972   3412   5527    132   -211   -267       C
ATOM    253  CA BASN A  30     -76.128  50.042  -5.214  0.48 31.93           C
ANISOU  253  CA BASN A  30     3022   3500   5608    142   -227   -255       C
ATOM    254  C  AASN A  30     -76.843  50.827  -6.177  0.52 26.23           C
ANISOU  254  C  AASN A  30     2359   2737   4868    175   -310   -160       C
ATOM    255  C  BASN A  30     -76.837  50.878  -6.267  0.48 26.49           C
ANISOU  255  C  BASN A  30     2394   2771   4898    175   -316   -154       C
ATOM    256  O  AASN A  30     -76.142  51.102  -7.153  0.52 25.30           O
ANISOU  256  O  AASN A  30     2228   2688   4699    150   -366   -117       O
ATOM    257  O  BASN A  30     -76.210  51.336  -7.227  0.48 25.51           O
ANISOU  257  O  BASN A  30     2274   2705   4714    145   -371   -107       O
ATOM    258  CB AASN A  30     -74.975  49.382  -5.300  0.52 34.68           C
ANISOU  258  CB AASN A  30     3268   3947   5961    102   -205   -296       C
ATOM    259  CB BASN A  30     -74.769  49.575  -5.731  0.48 34.57           C
ANISOU  259  CB BASN A  30     3255   3955   5927     92   -240   -271       C
ATOM    260  CG AASN A  30     -73.708  50.170  -5.022  0.52 35.76           C
ANISOU  260  CG AASN A  30     3479   4122   5984    -34   -170   -320       C
ATOM    261  CG BASN A  30     -73.610  50.114  -4.915  0.48 35.84           C
ANISOU  261  CG BASN A  30     3487   4137   5994    -44   -158   -330       C
ATOM    262  OD1AASN A  30     -73.720  51.141  -4.264  0.52 35.06           O
ANISOU  262  OD1AASN A  30     3528   3976   5815    -83   -137   -309       O
ATOM    263  OD1BASN A  30     -73.731  51.133  -4.234  0.48 35.08           O
ANISOU  263  OD1BASN A  30     3532   3978   5818    -83   -135   -310       O
ATOM    264  ND2AASN A  30     -72.605  49.752  -5.632  0.52 37.61           N
ANISOU  264  ND2AASN A  30     3620   4453   6216    -99   -177   -348       N
ATOM    265  ND2BASN A  30     -72.472  49.433  -4.988  0.48 37.92           N
ANISOU  265  ND2BASN A  30     3645   4494   6269   -118   -116   -391       N
ATOM    266  N   THR A  31     -78.147  51.085  -6.132  1.00 27.41           N
ANISOU  266  N   THR A  31     2564   2789   5061    216   -311   -135       N
ATOM    267  CA  THR A  31     -78.914  51.687  -7.211  1.00 30.22           C
ANISOU  267  CA  THR A  31     2964   3106   5414    241   -368    -39       C
ATOM    268  C   THR A  31     -79.789  52.803  -6.661  1.00 25.92           C
ANISOU  268  C   THR A  31     2502   2500   4847    187   -349    -59       C
ATOM    269  O   THR A  31     -80.291  52.714  -5.537  1.00 26.73           O
ANISOU  269  O   THR A  31     2626   2565   4965    154   -302   -141       O
ATOM    270  CB  THR A  31     -79.784  50.630  -7.919  1.00 32.35           C
ANISOU  270  CB  THR A  31     3193   3307   5793    351   -383     37       C
ATOM    271  OG1 THR A  31     -78.974  49.502  -8.271  1.00 35.43           O
ANISOU  271  OG1 THR A  31     3458   3787   6218    417   -420     56       O
ATOM    272  CG2 THR A  31     -80.420  51.197  -9.181  1.00 30.14           C
ANISOU  272  CG2 THR A  31     2974   3006   5474    357   -434    158       C
ATOM    273  N   VAL A  32     -79.960  53.854  -7.455  1.00 24.15           N
ANISOU  273  N   VAL A  32     2310   2284   4581    164   -381      1       N
ATOM    274  CA  VAL A  32     -80.832  54.970  -7.116  1.00 18.83           C
ANISOU  274  CA  VAL A  32     1668   1581   3907    115   -374    -10       C
ATOM    275  C   VAL A  32     -82.124  54.825  -7.905  1.00 25.50           C
ANISOU  275  C   VAL A  32     2534   2337   4820    122   -352     38       C
ATOM    276  O   VAL A  32     -82.096  54.636  -9.128  1.00 23.88           O
ANISOU  276  O   VAL A  32     2342   2130   4602    154   -362    127       O
ATOM    277  CB  VAL A  32     -80.153  56.318  -7.414  1.00 27.04           C
ANISOU  277  CB  VAL A  32     2710   2678   4888     94   -392     18       C
ATOM    278  CG1 VAL A  32     -81.061  57.468  -7.013  1.00 28.82           C
ANISOU  278  CG1 VAL A  32     2913   2903   5134     56   -400     10       C
ATOM    279  CG2 VAL A  32     -78.819  56.409  -6.695  1.00 25.71           C
ANISOU  279  CG2 VAL A  32     2551   2555   4661     87   -395     -4       C
ATOM    280  N   TYR A  33     -83.255  54.904  -7.208  1.00 21.30           N
ANISOU  280  N   TYR A  33     2017   1733   4344     71   -314    -21       N
ATOM    281  CA  TYR A  33     -84.567  54.813  -7.826  1.00 25.58           C
ANISOU  281  CA  TYR A  33     2598   2155   4965     48   -261     15       C
ATOM    282  C   TYR A  33     -85.368  56.074  -7.538  1.00 23.30           C
ANISOU  282  C   TYR A  33     2285   1893   4674    -68   -250    -38       C
ATOM    283  O   TYR A  33     -85.132  56.767  -6.545  1.00 26.41           O
ANISOU  283  O   TYR A  33     2631   2386   5020   -118   -295   -113       O
ATOM    284  CB  TYR A  33     -85.350  53.596  -7.316  1.00 28.39           C
ANISOU  284  CB  TYR A  33     2994   2361   5433     74   -190    -33       C
ATOM    285  CG  TYR A  33     -84.738  52.258  -7.653  1.00 29.04           C
ANISOU  285  CG  TYR A  33     3057   2413   5563    213   -198     31       C
ATOM    286  CD1 TYR A  33     -83.767  51.694  -6.838  1.00 22.21           C
ANISOU  286  CD1 TYR A  33     2135   1625   4679    246   -207    -47       C
ATOM    287  CD2 TYR A  33     -85.144  51.550  -8.776  1.00 26.45           C
ANISOU  287  CD2 TYR A  33     2758   1993   5300    310   -198    180       C
ATOM    288  CE1 TYR A  33     -83.211  50.471  -7.138  1.00 25.23           C
ANISOU  288  CE1 TYR A  33     2454   2006   5127    371   -213      0       C
ATOM    289  CE2 TYR A  33     -84.592  50.323  -9.083  1.00 28.27           C
ANISOU  289  CE2 TYR A  33     2930   2227   5584    454   -233    254       C
ATOM    290  CZ  TYR A  33     -83.625  49.787  -8.260  1.00 31.79           C
ANISOU  290  CZ  TYR A  33     3283   2764   6033    484   -239    152       C
ATOM    291  OH  TYR A  33     -83.070  48.564  -8.558  1.00 36.42           O
ANISOU  291  OH  TYR A  33     3766   3379   6693    624   -273    215       O
ATOM    292  N   THR A  34     -86.325  56.360  -8.416  1.00 25.21           N
ANISOU  292  N   THR A  34     2555   2059   4966   -113   -192     14       N
ATOM    293  CA  THR A  34     -87.289  57.426  -8.198  1.00 29.19           C
ANISOU  293  CA  THR A  34     3008   2582   5501   -245   -160    -50       C
ATOM    294  C   THR A  34     -88.685  56.899  -8.494  1.00 30.50           C
ANISOU  294  C   THR A  34     3254   2564   5769   -325    -48    -55       C
ATOM    295  O   THR A  34     -88.872  56.042  -9.362  1.00 32.80           O
ANISOU  295  O   THR A  34     3644   2723   6095   -254      2     61       O
ATOM    296  CB  THR A  34     -86.993  58.662  -9.066  1.00 31.12           C
ANISOU  296  CB  THR A  34     3185   2928   5712   -252   -160      6       C
ATOM    297  OG1 THR A  34     -87.903  59.714  -8.726  1.00 28.26           O
ANISOU  297  OG1 THR A  34     2722   2616   5401   -377   -136    -70       O
ATOM    298  CG2 THR A  34     -87.134  58.335 -10.549  1.00 29.53           C
ANISOU  298  CG2 THR A  34     3072   2654   5494   -229    -88    126       C
ATOM    299  N   LYS A  35     -89.664  57.405  -7.751  1.00 33.12           N
ANISOU  299  N   LYS A  35     3547   2890   6148   -480    -12   -184       N
ATOM    300  CA  LYS A  35     -91.049  56.985  -7.914  1.00 37.85           C
ANISOU  300  CA  LYS A  35     4233   3286   6860   -598    124   -220       C
ATOM    301  C   LYS A  35     -91.694  57.820  -9.014  1.00 36.49           C
ANISOU  301  C   LYS A  35     4046   3108   6712   -688    202   -145       C
ATOM    302  O   LYS A  35     -91.763  59.049  -8.907  1.00 32.38           O
ANISOU  302  O   LYS A  35     3380   2754   6170   -781    172   -205       O
ATOM    303  CB  LYS A  35     -91.822  57.128  -6.603  1.00 44.08           C
ANISOU  303  CB  LYS A  35     4990   4084   7675   -772    142   -431       C
ATOM    304  CG  LYS A  35     -93.219  56.523  -6.638  1.00 47.28           C
ANISOU  304  CG  LYS A  35     5517   4229   8219   -908    315   -505       C
ATOM    305  CD  LYS A  35     -94.086  57.058  -5.506  1.00 54.48           C
ANISOU  305  CD  LYS A  35     6366   5209   9125  -1157    331   -744       C
ATOM    306  CE  LYS A  35     -93.657  56.515  -4.152  1.00 58.23           C
ANISOU  306  CE  LYS A  35     6855   5746   9524  -1159    278   -901       C
ATOM    307  NZ  LYS A  35     -94.552  55.421  -3.682  1.00 62.02           N
ANISOU  307  NZ  LYS A  35     7506   6011  10047  -1202    446  -1016       N
ATOM    308  N   VAL A  36     -92.153  57.154 -10.070  1.00 36.82           N
ANISOU  308  N   VAL A  36     4230   2963   6796   -653    304     -3       N
ATOM    309  CA  VAL A  36     -92.808  57.801 -11.201  1.00 36.77           C
ANISOU  309  CA  VAL A  36     4250   2927   6791   -754    414     85       C
ATOM    310  C   VAL A  36     -94.212  57.223 -11.302  1.00 45.31           C
ANISOU  310  C   VAL A  36     5477   3735   8004   -881    584     87       C
ATOM    311  O   VAL A  36     -94.387  56.076 -11.733  1.00 49.78           O
ANISOU  311  O   VAL A  36     6212   4088   8616   -769    631    228       O
ATOM    312  CB  VAL A  36     -92.035  57.600 -12.510  1.00 34.40           C
ANISOU  312  CB  VAL A  36     4025   2669   6377   -618    390    284       C
ATOM    313  CG1 VAL A  36     -92.808  58.190 -13.678  1.00 38.46           C
ANISOU  313  CG1 VAL A  36     4602   3141   6871   -748    539    373       C
ATOM    314  CG2 VAL A  36     -90.654  58.223 -12.411  1.00 27.19           C
ANISOU  314  CG2 VAL A  36     2984   1991   5354   -521    259    254       C
ATOM    315  N   ASP A  37     -95.210  58.015 -10.905  1.00 50.20           N
ANISOU  315  N   ASP A  37     6023   4360   8690  -1111    675    -66       N
ATOM    316  CA  ASP A  37     -96.611  57.592 -10.928  1.00 52.30           C
ANISOU  316  CA  ASP A  37     6441   4445   8988  -1234    829    -97       C
ATOM    317  C   ASP A  37     -96.821  56.315 -10.119  1.00 44.47           C
ANISOU  317  C   ASP A  37     5577   3279   8043  -1142    837   -150       C
ATOM    318  O   ASP A  37     -97.558  55.413 -10.522  1.00 45.43           O
ANISOU  318  O   ASP A  37     5886   3168   8209  -1100    950    -54       O
ATOM    319  CB  ASP A  37     -97.116  57.422 -12.363  1.00 68.87           C
ANISOU  319  CB  ASP A  37     8703   6399  11066  -1234    960    118       C
ATOM    320  CG  ASP A  37     -97.551  58.735 -12.984  1.00 87.72           C
ANISOU  320  CG  ASP A  37    10981   8926  13421  -1425   1047     88       C
ATOM    321  OD1 ASP A  37     -98.421  59.412 -12.396  1.00 94.59           O
ANISOU  321  OD1 ASP A  37    11752   9868  14322  -1618   1095    -93       O
ATOM    322  OD2 ASP A  37     -97.015  59.097 -14.053  1.00 93.48           O
ANISOU  322  OD2 ASP A  37    11717   9711  14089  -1386   1072    236       O
ATOM    323  N   GLY A  38     -96.160  56.234  -8.967  1.00 38.70           N
ANISOU  323  N   GLY A  38     4743   2662   7300  -1108    724   -299       N
ATOM    324  CA  GLY A  38     -96.365  55.140  -8.045  1.00 45.81           C
ANISOU  324  CA  GLY A  38     5738   3430   8238  -1054    760   -402       C
ATOM    325  C   GLY A  38     -95.455  53.945  -8.225  1.00 49.99           C
ANISOU  325  C   GLY A  38     6330   3866   8799   -786    715   -265       C
ATOM    326  O   GLY A  38     -95.551  52.996  -7.436  1.00 55.35           O
ANISOU  326  O   GLY A  38     7065   4445   9522   -724    762   -360       O
ATOM    327  N   VAL A  39     -94.581  53.948  -9.229  1.00 46.14           N
ANISOU  327  N   VAL A  39     5821   3424   8285   -631    630    -54       N
ATOM    328  CA  VAL A  39     -93.660  52.840  -9.447  1.00 42.26           C
ANISOU  328  CA  VAL A  39     5350   2899   7806   -377    556     82       C
ATOM    329  C   VAL A  39     -92.236  53.373  -9.462  1.00 34.68           C
ANISOU  329  C   VAL A  39     4247   2175   6756   -305    386    104       C
ATOM    330  O   VAL A  39     -91.980  54.516  -9.854  1.00 36.94           O
ANISOU  330  O   VAL A  39     4456   2650   6930   -389    330    111       O
ATOM    331  CB  VAL A  39     -93.970  52.064 -10.748  1.00 41.34           C
ANISOU  331  CB  VAL A  39     5372   2637   7698   -233    592    351       C
ATOM    332  CG1 VAL A  39     -95.376  51.493 -10.703  1.00 42.72           C
ANISOU  332  CG1 VAL A  39     5707   2571   7955   -291    760    336       C
ATOM    333  CG2 VAL A  39     -93.784  52.953 -11.968  1.00 40.17           C
ANISOU  333  CG2 VAL A  39     5226   2574   7461   -289    561    515       C
ATOM    334  N   ASP A  40     -91.305  52.530  -9.026  1.00 34.71           N
ANISOU  334  N   ASP A  40     4209   2224   6755   -138    310    102       N
ATOM    335  CA  ASP A  40     -89.903  52.914  -8.947  1.00 38.02           C
ANISOU  335  CA  ASP A  40     4508   2913   7023    -69    154    107       C
ATOM    336  C   ASP A  40     -89.218  52.703 -10.292  1.00 33.31           C
ANISOU  336  C   ASP A  40     3921   2388   6347     61     73    326       C
ATOM    337  O   ASP A  40     -89.394  51.663 -10.935  1.00 36.09           O
ANISOU  337  O   ASP A  40     4337   2610   6767    196     84    483       O
ATOM    338  CB  ASP A  40     -89.193  52.110  -7.860  1.00 41.79           C
ANISOU  338  CB  ASP A  40     4936   3421   7522     14    132     -9       C
ATOM    339  CG  ASP A  40     -89.832  52.284  -6.497  1.00 52.40           C
ANISOU  339  CG  ASP A  40     6290   4722   8897   -139    212   -243       C
ATOM    340  OD1 ASP A  40     -90.292  53.405  -6.195  1.00 55.69           O
ANISOU  340  OD1 ASP A  40     6679   5233   9249   -315    197   -332       O
ATOM    341  OD2 ASP A  40     -89.880  51.299  -5.731  1.00 58.50           O
ANISOU  341  OD2 ASP A  40     7087   5383   9756    -91    293   -347       O
ATOM    342  N   VAL A  41     -88.439  53.695 -10.713  1.00 27.72           N
ANISOU  342  N   VAL A  41     3149   1891   5493     21     -7    336       N
ATOM    343  CA  VAL A  41     -87.691  53.648 -11.962  1.00 31.48           C
ANISOU  343  CA  VAL A  41     3637   2477   5848     95    -81    496       C
ATOM    344  C   VAL A  41     -86.218  53.845 -11.639  1.00 27.29           C
ANISOU  344  C   VAL A  41     3004   2146   5218    138   -188    430       C
ATOM    345  O   VAL A  41     -85.852  54.807 -10.954  1.00 31.30           O
ANISOU  345  O   VAL A  41     3450   2748   5696     66   -195    307       O
ATOM    346  CB  VAL A  41     -88.182  54.713 -12.960  1.00 31.62           C
ANISOU  346  CB  VAL A  41     3701   2526   5785    -23    -20    554       C
ATOM    347  CG1 VAL A  41     -87.326  54.700 -14.217  1.00 34.18           C
ANISOU  347  CG1 VAL A  41     4052   2993   5941     23    -88    685       C
ATOM    348  CG2 VAL A  41     -89.646  54.481 -13.303  1.00 33.08           C
ANISOU  348  CG2 VAL A  41     4007   2493   6070    -90    110    630       C
ATOM    349  N   GLU A  42     -85.380  52.931 -12.123  1.00 24.85           N
ANISOU  349  N   GLU A  42     2675   1903   4865    252   -272    519       N
ATOM    350  CA  GLU A  42     -83.948  53.021 -11.876  1.00 25.06           C
ANISOU  350  CA  GLU A  42     2614   2102   4804    268   -352    451       C
ATOM    351  C   GLU A  42     -83.362  54.235 -12.584  1.00 30.14           C
ANISOU  351  C   GLU A  42     3269   2872   5312    180   -356    437       C
ATOM    352  O   GLU A  42     -83.593  54.443 -13.778  1.00 31.52           O
ANISOU  352  O   GLU A  42     3507   3072   5397    151   -347    536       O
ATOM    353  CB  GLU A  42     -83.245  51.750 -12.347  1.00 23.46           C
ANISOU  353  CB  GLU A  42     2360   1965   4590    386   -443    542       C
ATOM    354  CG  GLU A  42     -81.741  51.906 -12.475  1.00 45.31           C
ANISOU  354  CG  GLU A  42     5052   4924   7239    356   -517    482       C
ATOM    355  CD  GLU A  42     -81.069  50.672 -13.034  1.00 45.73           C
ANISOU  355  CD  GLU A  42     5016   5087   7272    447   -625    567       C
ATOM    356  OE1 GLU A  42     -81.554  49.554 -12.764  1.00 49.09           O
ANISOU  356  OE1 GLU A  42     5389   5428   7834    576   -634    631       O
ATOM    357  OE2 GLU A  42     -80.057  50.823 -13.750  1.00 47.31           O
ANISOU  357  OE2 GLU A  42     5187   5461   7328    387   -697    562       O
ATOM    358  N   LEU A  43     -82.601  55.038 -11.843  1.00 30.83           N
ANISOU  358  N   LEU A  43     3304   3026   5383    140   -354    319       N
ATOM    359  CA  LEU A  43     -81.915  56.191 -12.404  1.00 29.59           C
ANISOU  359  CA  LEU A  43     3149   2956   5137     82   -332    288       C
ATOM    360  C   LEU A  43     -80.419  55.993 -12.565  1.00 27.68           C
ANISOU  360  C   LEU A  43     2887   2816   4812     87   -377    251       C
ATOM    361  O   LEU A  43     -79.827  56.582 -13.472  1.00 28.38           O
ANISOU  361  O   LEU A  43     3008   2968   4806     35   -349    238       O
ATOM    362  CB  LEU A  43     -82.147  57.432 -11.533  1.00 27.83           C
ANISOU  362  CB  LEU A  43     2880   2718   4976     44   -289    206       C
ATOM    363  CG  LEU A  43     -83.558  58.016 -11.491  1.00 27.13           C
ANISOU  363  CG  LEU A  43     2782   2565   4960    -14   -229    206       C
ATOM    364  CD1 LEU A  43     -83.563  59.307 -10.688  1.00 21.65           C
ANISOU  364  CD1 LEU A  43     1994   1918   4313    -40   -224    132       C
ATOM    365  CD2 LEU A  43     -84.085  58.248 -12.898  1.00 30.38           C
ANISOU  365  CD2 LEU A  43     3256   2967   5322    -61   -155    280       C
ATOM    366  N   PHE A  44     -79.795  55.175 -11.721  1.00 26.57           N
ANISOU  366  N   PHE A  44     2698   2692   4706    126   -423    214       N
ATOM    367  CA  PHE A  44     -78.342  55.083 -11.697  1.00 26.21           C
ANISOU  367  CA  PHE A  44     2629   2732   4599     96   -441    154       C
ATOM    368  C   PHE A  44     -77.936  53.825 -10.948  1.00 25.37           C
ANISOU  368  C   PHE A  44     2449   2650   4541    139   -482    134       C
ATOM    369  O   PHE A  44     -78.353  53.622  -9.804  1.00 22.17           O
ANISOU  369  O   PHE A  44     2029   2180   4215    168   -455     99       O
ATOM    370  CB  PHE A  44     -77.741  56.327 -11.032  1.00 27.91           C
ANISOU  370  CB  PHE A  44     2865   2915   4826     63   -380     85       C
ATOM    371  CG  PHE A  44     -76.247  56.283 -10.883  1.00 26.12           C
ANISOU  371  CG  PHE A  44     2642   2726   4556     16   -363     21       C
ATOM    372  CD1 PHE A  44     -75.422  56.612 -11.945  1.00 20.58           C
ANISOU  372  CD1 PHE A  44     1978   2066   3774    -55   -330    -19       C
ATOM    373  CD2 PHE A  44     -75.667  55.938  -9.673  1.00 23.72           C
ANISOU  373  CD2 PHE A  44     2320   2408   4283     17   -359    -13       C
ATOM    374  CE1 PHE A  44     -74.047  56.582 -11.809  1.00 24.81           C
ANISOU  374  CE1 PHE A  44     2530   2614   4283   -129   -291    -98       C
ATOM    375  CE2 PHE A  44     -74.293  55.908  -9.530  1.00 24.50           C
ANISOU  375  CE2 PHE A  44     2437   2522   4351    -50   -318    -70       C
ATOM    376  CZ  PHE A  44     -73.482  56.229 -10.600  1.00 24.82           C
ANISOU  376  CZ  PHE A  44     2512   2587   4334   -125   -283   -116       C
ATOM    377  N   GLU A  45     -77.130  52.987 -11.593  1.00 28.14           N
ANISOU  377  N   GLU A  45     2742   3111   4839    130   -540    141       N
ATOM    378  CA  GLU A  45     -76.543  51.815 -10.958  1.00 25.69           C
ANISOU  378  CA  GLU A  45     2320   2853   4586    161   -564    103       C
ATOM    379  C   GLU A  45     -75.080  52.114 -10.660  1.00 25.07           C
ANISOU  379  C   GLU A  45     2232   2841   4453     50   -526     -4       C
ATOM    380  O   GLU A  45     -74.285  52.319 -11.583  1.00 29.06           O
ANISOU  380  O   GLU A  45     2744   3438   4860    -38   -549    -29       O
ATOM    381  CB  GLU A  45     -76.670  50.579 -11.847  1.00 25.97           C
ANISOU  381  CB  GLU A  45     2254   2989   4624    234   -669    195       C
ATOM    382  CG  GLU A  45     -76.069  49.325 -11.228  1.00 40.16           C
ANISOU  382  CG  GLU A  45     3886   4857   6515    281   -685    148       C
ATOM    383  CD  GLU A  45     -75.981  48.169 -12.205  1.00 51.96           C
ANISOU  383  CD  GLU A  45     5235   6499   8006    360   -822    253       C
ATOM    384  OE1 GLU A  45     -76.362  48.353 -13.380  1.00 57.41           O
ANISOU  384  OE1 GLU A  45     5985   7244   8586    364   -913    373       O
ATOM    385  OE2 GLU A  45     -75.529  47.077 -11.798  1.00 56.31           O
ANISOU  385  OE2 GLU A  45     5606   7129   8662    417   -840    222       O
ATOM    386  N   ASN A  46     -74.732  52.139  -9.377  1.00 21.52           N
ANISOU  386  N   ASN A  46     1784   2339   4054     35   -454    -70       N
ATOM    387  CA  ASN A  46     -73.380  52.494  -8.956  1.00 24.26           C
ANISOU  387  CA  ASN A  46     2155   2704   4359    -78   -388   -152       C
ATOM    388  C   ASN A  46     -72.412  51.380  -9.335  1.00 29.19           C
ANISOU  388  C   ASN A  46     2644   3470   4978   -142   -415   -211       C
ATOM    389  O   ASN A  46     -72.480  50.273  -8.791  1.00 31.15           O
ANISOU  389  O   ASN A  46     2766   3766   5303    -96   -415   -230       O
ATOM    390  CB  ASN A  46     -73.352  52.757  -7.453  1.00 22.65           C
ANISOU  390  CB  ASN A  46     2004   2420   4182    -81   -308   -178       C
ATOM    391  CG  ASN A  46     -71.982  53.165  -6.958  1.00 24.05           C
ANISOU  391  CG  ASN A  46     2242   2580   4317   -195   -221   -230       C
ATOM    392  OD1 ASN A  46     -71.152  53.651  -7.724  1.00 29.64           O
ANISOU  392  OD1 ASN A  46     2988   3285   4989   -271   -201   -255       O
ATOM    393  ND2 ASN A  46     -71.737  52.969  -5.668  1.00 29.78           N
ANISOU  393  ND2 ASN A  46     2994   3282   5038   -223   -150   -251       N
ATOM    394  N   LYS A  47     -71.509  51.670 -10.270  1.00 22.01           N
ANISOU  394  N   LYS A  47     1747   2633   3981   -258   -427   -257       N
ATOM    395  CA  LYS A  47     -70.448  50.749 -10.652  1.00 24.50           C
ANISOU  395  CA  LYS A  47     1921   3113   4273   -369   -457   -340       C
ATOM    396  C   LYS A  47     -69.089  51.175 -10.114  1.00 31.35           C
ANISOU  396  C   LYS A  47     2851   3933   5127   -542   -322   -459       C
ATOM    397  O   LYS A  47     -68.065  50.647 -10.560  1.00 31.56           O
ANISOU  397  O   LYS A  47     2782   4091   5118   -693   -326   -561       O
ATOM    398  CB  LYS A  47     -70.387  50.614 -12.176  1.00 33.94           C
ANISOU  398  CB  LYS A  47     3080   4464   5350   -419   -578   -325       C
ATOM    399  CG  LYS A  47     -71.654  50.056 -12.808  1.00 45.54           C
ANISOU  399  CG  LYS A  47     4495   5985   6822   -254   -714   -173       C
ATOM    400  CD  LYS A  47     -72.029  48.710 -12.202  1.00 57.39           C
ANISOU  400  CD  LYS A  47     5805   7534   8466   -116   -766   -124       C
ATOM    401  CE  LYS A  47     -71.053  47.610 -12.601  1.00 71.32           C
ANISOU  401  CE  LYS A  47     7341   9539  10220   -190   -858   -180       C
ATOM    402  NZ  LYS A  47     -71.266  47.140 -13.999  1.00 79.79           N
ANISOU  402  NZ  LYS A  47     8334  10811  11171   -167  -1054    -71       N
ATOM    403  N   THR A  48     -69.056  52.113  -9.170  1.00 30.83           N
ANISOU  403  N   THR A  48     2942   3685   5085   -530   -208   -442       N
ATOM    404  CA  THR A  48     -67.818  52.646  -8.629  1.00 27.72           C
ANISOU  404  CA  THR A  48     2655   3193   4684   -675    -62   -513       C
ATOM    405  C   THR A  48     -67.560  52.077  -7.236  1.00 26.56           C
ANISOU  405  C   THR A  48     2482   3028   4582   -690     23   -519       C
ATOM    406  O   THR A  48     -68.371  51.341  -6.669  1.00 28.75           O
ANISOU  406  O   THR A  48     2664   3360   4900   -584    -19   -489       O
ATOM    407  CB  THR A  48     -67.868  54.175  -8.581  1.00 30.63           C
ANISOU  407  CB  THR A  48     3226   3365   5047   -638      8   -458       C
ATOM    408  OG1 THR A  48     -68.540  54.594  -7.386  1.00 30.37           O
ANISOU  408  OG1 THR A  48     3257   3238   5044   -517     18   -353       O
ATOM    409  CG2 THR A  48     -68.616  54.722  -9.786  1.00 26.49           C
ANISOU  409  CG2 THR A  48     2716   2862   4488   -573    -68   -434       C
ATOM    410  N   THR A  49     -66.405  52.430  -6.679  1.00 31.92           N
ANISOU  410  N   THR A  49     3266   3614   5250   -836    168   -566       N
ATOM    411  CA  THR A  49     -66.045  52.068  -5.316  1.00 30.76           C
ANISOU  411  CA  THR A  49     3146   3434   5108   -884    285   -562       C
ATOM    412  C   THR A  49     -66.487  53.111  -4.299  1.00 33.50           C
ANISOU  412  C   THR A  49     3691   3622   5416   -788    317   -428       C
ATOM    413  O   THR A  49     -66.156  52.983  -3.116  1.00 25.19           O
ANISOU  413  O   THR A  49     2713   2537   4323   -842    418   -403       O
ATOM    414  CB  THR A  49     -64.532  51.857  -5.208  1.00 33.67           C
ANISOU  414  CB  THR A  49     3536   3782   5476  -1117    442   -668       C
ATOM    415  OG1 THR A  49     -63.852  53.058  -5.595  1.00 35.08           O
ANISOU  415  OG1 THR A  49     3916   3771   5641  -1181    519   -650       O
ATOM    416  CG2 THR A  49     -64.090  50.717  -6.112  1.00 31.77           C
ANISOU  416  CG2 THR A  49     3048   3758   5266  -1232    387   -813       C
ATOM    417  N   LEU A  50     -67.215  54.132  -4.732  1.00 23.39           N
ANISOU  417  N   LEU A  50     2488   2264   4136   -657    232   -339       N
ATOM    418  CA  LEU A  50     -67.727  55.199  -3.889  1.00 24.88           C
ANISOU  418  CA  LEU A  50     2820   2341   4294   -549    219   -200       C
ATOM    419  C   LEU A  50     -69.127  54.861  -3.398  1.00 23.32           C
ANISOU  419  C   LEU A  50     2547   2236   4079   -432    111   -170       C
ATOM    420  O   LEU A  50     -69.796  53.984  -3.953  1.00 23.16           O
ANISOU  420  O   LEU A  50     2384   2317   4100   -396     46   -235       O
ATOM    421  CB  LEU A  50     -67.749  56.511  -4.670  1.00 30.46           C
ANISOU  421  CB  LEU A  50     3611   2921   5041   -473    203   -141       C
ATOM    422  CG  LEU A  50     -66.399  57.047  -5.147  1.00 39.06           C
ANISOU  422  CG  LEU A  50     4815   3860   6166   -585    344   -182       C
ATOM    423  CD1 LEU A  50     -66.589  58.280  -6.015  1.00 38.88           C
ANISOU  423  CD1 LEU A  50     4851   3715   6207   -489    347   -153       C
ATOM    424  CD2 LEU A  50     -65.502  57.360  -3.960  1.00 44.01           C
ANISOU  424  CD2 LEU A  50     5602   4350   6770   -643    468    -93       C
ATOM    425  N   PRO A  51     -69.595  55.526  -2.340  1.00 22.84           N
ANISOU  425  N   PRO A  51     2584   2142   3954   -376     89    -70       N
ATOM    426  CA  PRO A  51     -70.990  55.346  -1.924  1.00 21.43           C
ANISOU  426  CA  PRO A  51     2347   2039   3756   -294     -7    -67       C
ATOM    427  C   PRO A  51     -71.946  55.695  -3.055  1.00 26.35           C
ANISOU  427  C   PRO A  51     2890   2662   4459   -193   -108    -62       C
ATOM    428  O   PRO A  51     -71.648  56.524  -3.918  1.00 27.57           O
ANISOU  428  O   PRO A  51     3068   2752   4654   -164   -115    -25       O
ATOM    429  CB  PRO A  51     -71.136  56.311  -0.743  1.00 22.18           C
ANISOU  429  CB  PRO A  51     2570   2114   3743   -274    -35     55       C
ATOM    430  CG  PRO A  51     -69.759  56.420  -0.189  1.00 23.50           C
ANISOU  430  CG  PRO A  51     2866   2210   3853   -368     84    105       C
ATOM    431  CD  PRO A  51     -68.834  56.340  -1.375  1.00 24.43           C
ANISOU  431  CD  PRO A  51     2956   2245   4081   -408    156     46       C
ATOM    432  N   VAL A  52     -73.109  55.043  -3.039  1.00 28.56           N
ANISOU  432  N   VAL A  52     3087   3000   4764   -150   -160   -107       N
ATOM    433  CA  VAL A  52     -74.034  55.133  -4.168  1.00 28.65           C
ANISOU  433  CA  VAL A  52     3029   3010   4849    -77   -232   -101       C
ATOM    434  C   VAL A  52     -74.495  56.573  -4.376  1.00 29.74           C
ANISOU  434  C   VAL A  52     3209   3101   4988    -24   -283    -19       C
ATOM    435  O   VAL A  52     -74.492  57.086  -5.502  1.00 32.36           O
ANISOU  435  O   VAL A  52     3528   3405   5363      4   -289     -3       O
ATOM    436  CB  VAL A  52     -75.221  54.173  -3.963  1.00 25.95           C
ANISOU  436  CB  VAL A  52     2618   2692   4551    -41   -251   -152       C
ATOM    437  CG1 VAL A  52     -75.797  54.314  -2.560  1.00 23.38           C
ANISOU  437  CG1 VAL A  52     2346   2378   4160    -73   -238   -179       C
ATOM    438  CG2 VAL A  52     -76.291  54.409  -5.017  1.00 18.60           C
ANISOU  438  CG2 VAL A  52     1651   1732   3683     25   -314   -114       C
ATOM    439  N   ASN A  53     -74.880  57.253  -3.293  1.00 27.00           N
ANISOU  439  N   ASN A  53     2904   2767   4589    -14   -318     29       N
ATOM    440  CA  ASN A  53     -75.387  58.616  -3.422  1.00 23.61           C
ANISOU  440  CA  ASN A  53     2463   2322   4184     51   -380    110       C
ATOM    441  C   ASN A  53     -74.288  59.588  -3.823  1.00 29.69           C
ANISOU  441  C   ASN A  53     3287   3005   4989     92   -334    184       C
ATOM    442  O   ASN A  53     -74.561  60.589  -4.496  1.00 32.13           O
ANISOU  442  O   ASN A  53     3556   3277   5375    163   -341    220       O
ATOM    443  CB  ASN A  53     -76.036  59.061  -2.113  1.00 23.32           C
ANISOU  443  CB  ASN A  53     2435   2363   4063     40   -458    148       C
ATOM    444  CG  ASN A  53     -75.039  59.175  -0.980  1.00 25.64           C
ANISOU  444  CG  ASN A  53     2835   2667   4240      9   -442    218       C
ATOM    445  OD1 ASN A  53     -74.523  58.171  -0.487  1.00 27.53           O
ANISOU  445  OD1 ASN A  53     3129   2917   4415    -71   -366    156       O
ATOM    446  ND2 ASN A  53     -74.766  60.403  -0.555  1.00 28.52           N
ANISOU  446  ND2 ASN A  53     3226   3028   4583     76   -505    360       N
ATOM    447  N   VAL A  54     -73.048  59.315  -3.421  1.00 29.38           N
ANISOU  447  N   VAL A  54     3339   2916   4910     43   -259    195       N
ATOM    448  CA  VAL A  54     -71.936  60.174  -3.810  1.00 27.65           C
ANISOU  448  CA  VAL A  54     3197   2565   4745     70   -178    250       C
ATOM    449  C   VAL A  54     -71.639  60.015  -5.294  1.00 29.52           C
ANISOU  449  C   VAL A  54     3406   2760   5049     39   -110    149       C
ATOM    450  O   VAL A  54     -71.532  61.001  -6.033  1.00 28.78           O
ANISOU  450  O   VAL A  54     3320   2580   5034     98    -65    162       O
ATOM    451  CB  VAL A  54     -70.700  59.865  -2.949  1.00 26.05           C
ANISOU  451  CB  VAL A  54     3119   2301   4476     -8    -93    285       C
ATOM    452  CG1 VAL A  54     -69.522  60.694  -3.409  1.00 23.34           C
ANISOU  452  CG1 VAL A  54     2880   1773   4214      7     25    328       C
ATOM    453  CG2 VAL A  54     -71.006  60.121  -1.483  1.00 23.65           C
ANISOU  453  CG2 VAL A  54     2868   2060   4058     13   -166    404       C
ATOM    454  N   ALA A  55     -71.503  58.768  -5.753  1.00 27.04           N
ANISOU  454  N   ALA A  55     3053   2523   4701    -56   -101     44       N
ATOM    455  CA  ALA A  55     -71.227  58.523  -7.166  1.00 25.02           C
ANISOU  455  CA  ALA A  55     2769   2278   4459   -108    -67    -48       C
ATOM    456  C   ALA A  55     -72.362  59.030  -8.044  1.00 24.28           C
ANISOU  456  C   ALA A  55     2620   2213   4394    -36   -116    -34       C
ATOM    457  O   ALA A  55     -72.127  59.547  -9.142  1.00 22.80           O
ANISOU  457  O   ALA A  55     2454   1991   4216    -56    -56    -80       O
ATOM    458  CB  ALA A  55     -70.989  57.032  -7.403  1.00 23.53           C
ANISOU  458  CB  ALA A  55     2506   2208   4226   -201    -90   -132       C
ATOM    459  N   PHE A  56     -73.603  58.888  -7.572  1.00 27.03           N
ANISOU  459  N   PHE A  56     2905   2618   4748     25   -203     12       N
ATOM    460  CA  PHE A  56     -74.749  59.399  -8.316  1.00 23.57           C
ANISOU  460  CA  PHE A  56     2416   2197   4343     72   -230     28       C
ATOM    461  C   PHE A  56     -74.635  60.901  -8.534  1.00 27.63           C
ANISOU  461  C   PHE A  56     2939   2632   4927    134   -170     60       C
ATOM    462  O   PHE A  56     -74.924  61.405  -9.626  1.00 28.29           O
ANISOU  462  O   PHE A  56     3009   2705   5033    133   -113     28       O
ATOM    463  CB  PHE A  56     -76.036  59.055  -7.567  1.00 24.83           C
ANISOU  463  CB  PHE A  56     2518   2405   4509    100   -311     56       C
ATOM    464  CG  PHE A  56     -77.264  59.705  -8.131  1.00 26.63           C
ANISOU  464  CG  PHE A  56     2694   2639   4784    125   -322     74       C
ATOM    465  CD1 PHE A  56     -77.689  59.417  -9.416  1.00 26.62           C
ANISOU  465  CD1 PHE A  56     2694   2646   4774    100   -294     62       C
ATOM    466  CD2 PHE A  56     -78.009  60.587  -7.366  1.00 29.28           C
ANISOU  466  CD2 PHE A  56     2972   2990   5161    157   -362    106       C
ATOM    467  CE1 PHE A  56     -78.825  60.008  -9.935  1.00 20.61           C
ANISOU  467  CE1 PHE A  56     1895   1883   4052    100   -274     78       C
ATOM    468  CE2 PHE A  56     -79.149  61.178  -7.877  1.00 24.77           C
ANISOU  468  CE2 PHE A  56     2331   2434   4646    153   -356    106       C
ATOM    469  CZ  PHE A  56     -79.556  60.890  -9.164  1.00 21.07           C
ANISOU  469  CZ  PHE A  56     1880   1948   4177    121   -296     90       C
ATOM    470  N   GLU A  57     -74.199  61.630  -7.506  1.00 24.89           N
ANISOU  470  N   GLU A  57     2613   2229   4616    195   -174    130       N
ATOM    471  CA  GLU A  57     -74.065  63.076  -7.625  1.00 25.23           C
ANISOU  471  CA  GLU A  57     2637   2185   4764    297   -120    184       C
ATOM    472  C   GLU A  57     -72.953  63.449  -8.597  1.00 27.52           C
ANISOU  472  C   GLU A  57     3013   2347   5098    273     37    114       C
ATOM    473  O   GLU A  57     -73.114  64.365  -9.412  1.00 29.36           O
ANISOU  473  O   GLU A  57     3214   2524   5417    321    129     82       O
ATOM    474  CB  GLU A  57     -73.811  63.684  -6.247  1.00 32.31           C
ANISOU  474  CB  GLU A  57     3542   3061   5673    383   -185    315       C
ATOM    475  CG  GLU A  57     -73.642  65.190  -6.242  1.00 41.64           C
ANISOU  475  CG  GLU A  57     4676   4150   6995    534   -148    409       C
ATOM    476  CD  GLU A  57     -73.521  65.752  -4.839  1.00 51.82           C
ANISOU  476  CD  GLU A  57     5962   5461   8268    631   -261    582       C
ATOM    477  OE1 GLU A  57     -73.999  65.093  -3.892  1.00 56.95           O
ANISOU  477  OE1 GLU A  57     6612   6246   8780    564   -386    604       O
ATOM    478  OE2 GLU A  57     -72.944  66.849  -4.683  1.00 56.91           O
ANISOU  478  OE2 GLU A  57     6608   5983   9031    776   -220    700       O
ATOM    479  N   LEU A  58     -71.822  62.743  -8.533  1.00 24.91           N
ANISOU  479  N   LEU A  58     2786   1968   4710    177     89     66       N
ATOM    480  CA  LEU A  58     -70.704  63.054  -9.418  1.00 24.89           C
ANISOU  480  CA  LEU A  58     2881   1837   4739    112    252    -35       C
ATOM    481  C   LEU A  58     -71.052  62.764 -10.873  1.00 23.61           C
ANISOU  481  C   LEU A  58     2698   1760   4511     18    288   -165       C
ATOM    482  O   LEU A  58     -70.719  63.553 -11.766  1.00 24.40           O
ANISOU  482  O   LEU A  58     2843   1769   4660      8    434   -249       O
ATOM    483  CB  LEU A  58     -69.467  62.265  -8.992  1.00 23.23           C
ANISOU  483  CB  LEU A  58     2772   1582   4474    -12    297    -74       C
ATOM    484  CG  LEU A  58     -68.957  62.558  -7.581  1.00 28.12           C
ANISOU  484  CG  LEU A  58     3460   2101   5125     53    293     66       C
ATOM    485  CD1 LEU A  58     -67.829  61.613  -7.202  1.00 31.38           C
ANISOU  485  CD1 LEU A  58     3960   2493   5470   -109    355      9       C
ATOM    486  CD2 LEU A  58     -68.504  64.004  -7.473  1.00 29.14           C
ANISOU  486  CD2 LEU A  58     3656   2013   5404    193    402    156       C
ATOM    487  N   TRP A  59     -71.719  61.638 -11.130  1.00 23.68           N
ANISOU  487  N   TRP A  59     2648   1940   4408    -47    168   -177       N
ATOM    488  CA  TRP A  59     -72.115  61.316 -12.496  1.00 24.08           C
ANISOU  488  CA  TRP A  59     2692   2094   4363   -131    176   -256       C
ATOM    489  C   TRP A  59     -73.106  62.336 -13.038  1.00 30.96           C
ANISOU  489  C   TRP A  59     3524   2947   5292    -56    231   -236       C
ATOM    490  O   TRP A  59     -73.034  62.720 -14.210  1.00 33.28           O
ANISOU  490  O   TRP A  59     3862   3246   5537   -124    342   -327       O
ATOM    491  CB  TRP A  59     -72.710  59.912 -12.555  1.00 24.62           C
ANISOU  491  CB  TRP A  59     2697   2327   4329   -170     25   -223       C
ATOM    492  CG  TRP A  59     -73.359  59.603 -13.866  1.00 25.73           C
ANISOU  492  CG  TRP A  59     2836   2582   4359   -226      2   -239       C
ATOM    493  CD1 TRP A  59     -72.735  59.282 -15.037  1.00 26.62           C
ANISOU  493  CD1 TRP A  59     2998   2784   4331   -362     28   -332       C
ATOM    494  CD2 TRP A  59     -74.762  59.586 -14.140  1.00 23.38           C
ANISOU  494  CD2 TRP A  59     2498   2327   4060   -168    -49   -152       C
ATOM    495  NE1 TRP A  59     -73.666  59.067 -16.025  1.00 24.25           N
ANISOU  495  NE1 TRP A  59     2700   2590   3922   -379    -14   -284       N
ATOM    496  CE2 TRP A  59     -74.918  59.247 -15.499  1.00 25.55           C
ANISOU  496  CE2 TRP A  59     2816   2709   4183   -260    -49   -170       C
ATOM    497  CE3 TRP A  59     -75.903  59.826 -13.369  1.00 24.08           C
ANISOU  497  CE3 TRP A  59     2525   2376   4247    -71    -90    -66       C
ATOM    498  CZ2 TRP A  59     -76.169  59.141 -16.102  1.00 35.18           C
ANISOU  498  CZ2 TRP A  59     4036   3972   5358   -244    -74    -82       C
ATOM    499  CZ3 TRP A  59     -77.142  59.719 -13.968  1.00 32.27           C
ANISOU  499  CZ3 TRP A  59     3551   3449   5260    -70   -106     -8       C
ATOM    500  CH2 TRP A  59     -77.266  59.380 -15.321  1.00 36.28           C
ANISOU  500  CH2 TRP A  59     4119   4039   5627   -150    -91     -4       C
ATOM    501  N   ALA A  60     -74.042  62.784 -12.199  1.00 29.04           N
ANISOU  501  N   ALA A  60     3193   2699   5143     64    164   -132       N
ATOM    502  CA  ALA A  60     -74.985  63.807 -12.635  1.00 25.76           C
ANISOU  502  CA  ALA A  60     2703   2277   4808    125    226   -121       C
ATOM    503  C   ALA A  60     -74.277  65.111 -12.971  1.00 27.17           C
ANISOU  503  C   ALA A  60     2899   2316   5110    185    403   -176       C
ATOM    504  O   ALA A  60     -74.702  65.833 -13.880  1.00 27.27           O
ANISOU  504  O   ALA A  60     2882   2324   5157    180    531   -239       O
ATOM    505  CB  ALA A  60     -76.044  64.037 -11.558  1.00 26.48           C
ANISOU  505  CB  ALA A  60     2674   2411   4976    216    106    -16       C
ATOM    506  N   LYS A  61     -73.195  65.423 -12.259  1.00 31.83           N
ANISOU  506  N   LYS A  61     3177   3435   5481   -794     73   -317       N
ATOM    507  CA  LYS A  61     -72.429  66.639 -12.487  1.00 32.74           C
ANISOU  507  CA  LYS A  61     3110   3555   5776   -704    -34   -377       C
ATOM    508  C   LYS A  61     -71.243  66.424 -13.422  1.00 30.06           C
ANISOU  508  C   LYS A  61     2774   3157   5488   -611     -3   -360       C
ATOM    509  O   LYS A  61     -70.332  67.260 -13.451  1.00 30.50           O
ANISOU  509  O   LYS A  61     2721   3185   5684   -516   -111   -377       O
ATOM    510  CB  LYS A  61     -71.945  67.213 -11.155  1.00 28.23           C
ANISOU  510  CB  LYS A  61     2507   2966   5253   -647   -240   -307       C
ATOM    511  CG  LYS A  61     -73.061  67.576 -10.192  1.00 29.21           C
ANISOU  511  CG  LYS A  61     2608   3154   5336   -731   -304   -338       C
ATOM    512  CD  LYS A  61     -72.507  68.112  -8.884  1.00 30.07           C
ANISOU  512  CD  LYS A  61     2716   3237   5473   -662   -526   -258       C
ATOM    513  CE  LYS A  61     -73.622  68.555  -7.952  1.00 31.28           C
ANISOU  513  CE  LYS A  61     2833   3462   5589   -743   -611   -306       C
ATOM    514  NZ  LYS A  61     -73.091  69.127  -6.686  1.00 32.36           N
ANISOU  514  NZ  LYS A  61     2986   3572   5739   -667   -848   -228       N
ATOM    515  N   ARG A  62     -71.233  65.329 -14.179  1.00 25.73           N
ANISOU  515  N   ARG A  62     2356   2587   4833   -631    130   -332       N
ATOM    516  CA  ARG A  62     -70.143  65.065 -15.106  1.00 27.04           C
ANISOU  516  CA  ARG A  62     2528   2705   5039   -552    155   -327       C
ATOM    517  C   ARG A  62     -70.079  66.144 -16.183  1.00 28.05           C
ANISOU  517  C   ARG A  62     2505   2857   5296   -527    192   -468       C
ATOM    518  O   ARG A  62     -71.056  66.842 -16.466  1.00 31.70           O
ANISOU  518  O   ARG A  62     2877   3382   5786   -593    255   -580       O
ATOM    519  CB  ARG A  62     -70.315  63.694 -15.758  1.00 28.86           C
ANISOU  519  CB  ARG A  62     2922   2920   5122   -576    280   -288       C
ATOM    520  CG  ARG A  62     -71.453  63.638 -16.765  1.00 27.48           C
ANISOU  520  CG  ARG A  62     2785   2782   4874   -654    435   -384       C
ATOM    521  CD  ARG A  62     -71.838  62.207 -17.099  1.00 24.50           C
ANISOU  521  CD  ARG A  62     2606   2378   4326   -673    530   -325       C
ATOM    522  NE  ARG A  62     -72.996  62.154 -17.985  1.00 28.20           N
ANISOU  522  NE  ARG A  62     3150   2861   4702   -760    678   -405       N
ATOM    523  CZ  ARG A  62     -74.256  62.260 -17.575  1.00 30.97           C
ANISOU  523  CZ  ARG A  62     3543   3234   4989   -871    740   -432       C
ATOM    524  NH1 ARG A  62     -74.528  62.431 -16.288  1.00 30.90           N
ANISOU  524  NH1 ARG A  62     3500   3244   4998   -900    655   -390       N
ATOM    525  NH2 ARG A  62     -75.247  62.199 -18.453  1.00 35.06           N
ANISOU  525  NH2 ARG A  62     4150   3751   5419   -962    888   -504       N
ATOM    526  N   ASN A  63     -68.902  66.277 -16.788  1.00 31.37           N
ANISOU  526  N   ASN A  63     2895   3227   5796   -439    161   -473       N
ATOM    527  CA  ASN A  63     -68.722  67.236 -17.868  1.00 30.49           C
ANISOU  527  CA  ASN A  63     2653   3130   5802   -405    206   -612       C
ATOM    528  C   ASN A  63     -69.406  66.726 -19.131  1.00 29.41           C
ANISOU  528  C   ASN A  63     2593   3025   5556   -475    390   -686       C
ATOM    529  O   ASN A  63     -69.136  65.612 -19.589  1.00 31.71           O
ANISOU  529  O   ASN A  63     3034   3284   5730   -472    441   -623       O
ATOM    530  CB  ASN A  63     -67.234  67.470 -18.124  1.00 30.42           C
ANISOU  530  CB  ASN A  63     2616   3043   5900   -294    118   -594       C
ATOM    531  CG  ASN A  63     -66.965  68.766 -18.859  1.00 35.74           C
ANISOU  531  CG  ASN A  63     3122   3722   6736   -234    116   -741       C
ATOM    532  OD1 ASN A  63     -67.268  68.897 -20.045  1.00 38.48           O
ANISOU  532  OD1 ASN A  63     3448   4101   7070   -262    250   -855       O
ATOM    533  ND2 ASN A  63     -66.385  69.732 -18.157  1.00 37.48           N
ANISOU  533  ND2 ASN A  63     3233   3904   7105   -147    -37   -741       N
ATOM    534  N   ILE A  64     -70.297  67.539 -19.692  1.00 27.53           N
ANISOU  534  N   ILE A  64     2257   2850   5355   -539    490   -823       N
ATOM    535  CA  ILE A  64     -71.067  67.156 -20.868  1.00 27.64           C
ANISOU  535  CA  ILE A  64     2365   2888   5250   -626    679   -897       C
ATOM    536  C   ILE A  64     -70.565  67.873 -22.121  1.00 35.88           C
ANISOU  536  C   ILE A  64     3326   3933   6374   -588    752  -1029       C
ATOM    537  O   ILE A  64     -71.266  67.925 -23.130  1.00 35.15           O
ANISOU  537  O   ILE A  64     3278   3871   6206   -672    919  -1126       O
ATOM    538  CB  ILE A  64     -72.570  67.395 -20.653  1.00 30.80           C
ANISOU  538  CB  ILE A  64     2753   3353   5595   -767    783   -959       C
ATOM    539  CG1 ILE A  64     -72.848  68.883 -20.433  1.00 33.30           C
ANISOU  539  CG1 ILE A  64     2817   3741   6095   -776    754  -1100       C
ATOM    540  CG2 ILE A  64     -73.077  66.569 -19.477  1.00 29.55           C
ANISOU  540  CG2 ILE A  64     2710   3183   5334   -807    721   -831       C
ATOM    541  CD1 ILE A  64     -74.317  69.234 -20.429  1.00 34.70           C
ANISOU  541  CD1 ILE A  64     2952   3994   6237   -937    883  -1200       C
ATOM    542  N   LYS A  65     -69.365  68.429 -22.066  1.00 35.07           N
ANISOU  542  N   LYS A  65     3119   3791   6415   -470    634  -1037       N
ATOM    543  CA  LYS A  65     -68.707  69.044 -23.205  1.00 31.64           C
ANISOU  543  CA  LYS A  65     2620   3342   6059   -416    687  -1157       C
ATOM    544  C   LYS A  65     -67.592  68.138 -23.711  1.00 31.38           C
ANISOU  544  C   LYS A  65     2726   3235   5961   -350    649  -1080       C
ATOM    545  O   LYS A  65     -67.160  67.221 -23.004  1.00 32.06           O
ANISOU  545  O   LYS A  65     2909   3281   5990   -326    556   -937       O
ATOM    546  CB  LYS A  65     -68.138  70.415 -22.813  1.00 35.96           C
ANISOU  546  CB  LYS A  65     2944   3887   6832   -320    576  -1242       C
ATOM    547  CG  LYS A  65     -69.202  71.460 -22.520  1.00 44.99           C
ANISOU  547  CG  LYS A  65     3904   5122   8068   -377    616  -1365       C
ATOM    548  CD  LYS A  65     -68.639  72.625 -21.720  1.00 57.59           C
ANISOU  548  CD  LYS A  65     5297   6705   9878   -255    437  -1402       C
ATOM    549  CE  LYS A  65     -68.223  72.183 -20.325  1.00 62.78           C
ANISOU  549  CE  LYS A  65     6025   7308  10521   -206    242  -1222       C
ATOM    550  NZ  LYS A  65     -67.769  73.326 -19.484  1.00 64.93           N
ANISOU  550  NZ  LYS A  65     6129   7559  10984    -84     50  -1248       N
ATOM    551  N   PRO A  66     -67.119  68.341 -24.943  1.00 32.77           N
ANISOU  551  N   PRO A  66     2914   3397   6140   -326    725  -1180       N
ATOM    552  CA  PRO A  66     -65.977  67.550 -25.427  1.00 28.08           C
ANISOU  552  CA  PRO A  66     2431   2736   5501   -261    670  -1124       C
ATOM    553  C   PRO A  66     -64.770  67.737 -24.522  1.00 28.41           C
ANISOU  553  C   PRO A  66     2403   2708   5685   -167    492  -1045       C
ATOM    554  O   PRO A  66     -64.316  68.858 -24.284  1.00 32.82           O
ANISOU  554  O   PRO A  66     2816   3241   6414   -104    427  -1110       O
ATOM    555  CB  PRO A  66     -65.730  68.108 -26.833  1.00 29.11           C
ANISOU  555  CB  PRO A  66     2550   2868   5642   -253    777  -1279       C
ATOM    556  CG  PRO A  66     -67.044  68.658 -27.251  1.00 30.34           C
ANISOU  556  CG  PRO A  66     2674   3101   5753   -353    944  -1387       C
ATOM    557  CD  PRO A  66     -67.678  69.201 -26.002  1.00 31.61           C
ANISOU  557  CD  PRO A  66     2696   3300   6013   -374    883  -1357       C
ATOM    558  N   VAL A  67     -64.261  66.625 -24.003  1.00 30.32           N
ANISOU  558  N   VAL A  67     2752   2914   5853   -159    417   -907       N
ATOM    559  CA  VAL A  67     -63.141  66.656 -23.065  1.00 31.36           C
ANISOU  559  CA  VAL A  67     2851   2972   6091    -97    265   -815       C
ATOM    560  C   VAL A  67     -62.063  65.706 -23.566  1.00 30.67           C
ANISOU  560  C   VAL A  67     2857   2836   5959    -76    237   -777       C
ATOM    561  O   VAL A  67     -62.338  64.790 -24.357  1.00 31.24           O
ANISOU  561  O   VAL A  67     3033   2943   5893   -104    310   -786       O
ATOM    562  CB  VAL A  67     -63.588  66.285 -21.631  1.00 30.71           C
ANISOU  562  CB  VAL A  67     2789   2901   5977   -127    198   -682       C
ATOM    563  CG1 VAL A  67     -64.482  67.370 -21.058  1.00 31.46           C
ANISOU  563  CG1 VAL A  67     2767   3040   6147   -139    188   -731       C
ATOM    564  CG2 VAL A  67     -64.303  64.948 -21.630  1.00 24.84           C
ANISOU  564  CG2 VAL A  67     2184   2203   5050   -191    270   -609       C
ATOM    565  N   PRO A  68     -60.815  65.912 -23.141  1.00 32.75           N
ANISOU  565  N   PRO A  68     3091   3015   6338    -27    127   -740       N
ATOM    566  CA  PRO A  68     -59.756  64.960 -23.490  1.00 32.19           C
ANISOU  566  CA  PRO A  68     3092   2904   6235    -25     95   -706       C
ATOM    567  C   PRO A  68     -60.075  63.567 -22.973  1.00 33.60           C
ANISOU  567  C   PRO A  68     3360   3127   6279    -70    104   -592       C
ATOM    568  O   PRO A  68     -60.732  63.396 -21.944  1.00 33.07           O
ANISOU  568  O   PRO A  68     3304   3086   6176    -98     96   -504       O
ATOM    569  CB  PRO A  68     -58.517  65.539 -22.800  1.00 27.98           C
ANISOU  569  CB  PRO A  68     2516   2261   5855     14    -21   -668       C
ATOM    570  CG  PRO A  68     -58.805  66.990 -22.673  1.00 28.09           C
ANISOU  570  CG  PRO A  68     2428   2252   5994     67    -43   -741       C
ATOM    571  CD  PRO A  68     -60.281  67.095 -22.441  1.00 27.72           C
ANISOU  571  CD  PRO A  68     2354   2307   5870     31     27   -746       C
ATOM    572  N   GLU A  69     -59.605  62.563 -23.707  1.00 31.29           N
ANISOU  572  N   GLU A  69     3131   2847   5912    -71    115   -605       N
ATOM    573  CA  GLU A  69     -59.768  61.189 -23.262  1.00 28.67           C
ANISOU  573  CA  GLU A  69     2867   2556   5470    -94    114   -513       C
ATOM    574  C   GLU A  69     -58.922  60.937 -22.019  1.00 28.33           C
ANISOU  574  C   GLU A  69     2798   2466   5502   -114     40   -409       C
ATOM    575  O   GLU A  69     -57.851  61.521 -21.841  1.00 28.92           O
ANISOU  575  O   GLU A  69     2828   2461   5699   -108    -22   -415       O
ATOM    576  CB  GLU A  69     -59.395  60.218 -24.381  1.00 31.19           C
ANISOU  576  CB  GLU A  69     3243   2902   5706    -74    121   -567       C
ATOM    577  CG  GLU A  69     -60.438  60.154 -25.489  1.00 35.31           C
ANISOU  577  CG  GLU A  69     3849   3474   6094    -66    205   -639       C
ATOM    578  CD  GLU A  69     -60.072  59.183 -26.593  1.00 41.81           C
ANISOU  578  CD  GLU A  69     4748   4320   6818    -34    188   -688       C
ATOM    579  OE1 GLU A  69     -59.089  59.445 -27.318  1.00 48.02           O
ANISOU  579  OE1 GLU A  69     5504   5076   7666    -17    146   -767       O
ATOM    580  OE2 GLU A  69     -60.766  58.154 -26.734  1.00 45.40           O
ANISOU  580  OE2 GLU A  69     5300   4818   7132    -19    205   -651       O
ATOM    581  N   VAL A  70     -59.428  60.057 -21.151  1.00 31.46           N
ANISOU  581  N   VAL A  70     3237   2903   5814   -141     55   -315       N
ATOM    582  CA  VAL A  70     -58.826  59.864 -19.833  1.00 31.45           C
ANISOU  582  CA  VAL A  70     3230   2862   5859   -176      8   -210       C
ATOM    583  C   VAL A  70     -57.367  59.444 -19.959  1.00 32.01           C
ANISOU  583  C   VAL A  70     3274   2882   6005   -192    -34   -214       C
ATOM    584  O   VAL A  70     -56.514  59.870 -19.169  1.00 39.74           O
ANISOU  584  O   VAL A  70     4246   3782   7073   -223    -82   -160       O
ATOM    585  CB  VAL A  70     -59.644  58.842 -19.021  1.00 31.65           C
ANISOU  585  CB  VAL A  70     3312   2948   5763   -203     51   -127       C
ATOM    586  CG1 VAL A  70     -58.993  58.583 -17.673  1.00 35.27           C
ANISOU  586  CG1 VAL A  70     3779   3369   6252   -251     20    -24       C
ATOM    587  CG2 VAL A  70     -61.070  59.338 -18.837  1.00 26.71           C
ANISOU  587  CG2 VAL A  70     2717   2360   5071   -206     92   -127       C
ATOM    588  N   LYS A  71     -57.053  58.614 -20.958  1.00 27.98           N
ANISOU  588  N   LYS A  71     2759   2413   5457   -176    -22   -282       N
ATOM    589  CA  LYS A  71     -55.671  58.190 -21.160  1.00 27.96           C
ANISOU  589  CA  LYS A  71     2718   2374   5532   -204    -62   -308       C
ATOM    590  C   LYS A  71     -54.753  59.388 -21.374  1.00 31.93           C
ANISOU  590  C   LYS A  71     3196   2768   6169   -206   -111   -350       C
ATOM    591  O   LYS A  71     -53.613  59.399 -20.895  1.00 32.62           O
ANISOU  591  O   LYS A  71     3272   2778   6344   -258   -146   -322       O
ATOM    592  CB  LYS A  71     -55.584  57.223 -22.342  1.00 27.81           C
ANISOU  592  CB  LYS A  71     2694   2425   5448   -171    -61   -395       C
ATOM    593  CG  LYS A  71     -56.105  57.784 -23.655  1.00 26.78           C
ANISOU  593  CG  LYS A  71     2596   2307   5273   -116    -50   -495       C
ATOM    594  CD  LYS A  71     -55.975  56.775 -24.782  1.00 26.18           C
ANISOU  594  CD  LYS A  71     2540   2294   5113    -78    -71   -572       C
ATOM    595  CE  LYS A  71     -56.546  57.324 -26.080  1.00 27.54           C
ANISOU  595  CE  LYS A  71     2777   2474   5213    -34    -46   -666       C
ATOM    596  NZ  LYS A  71     -56.517  56.314 -27.173  1.00 30.94           N
ANISOU  596  NZ  LYS A  71     3260   2964   5533     13    -82   -733       N
ATOM    597  N   ILE A  72     -55.238  60.414 -22.076  1.00 30.45           N
ANISOU  597  N   ILE A  72     3004   2565   6000   -154   -106   -421       N
ATOM    598  CA  ILE A  72     -54.447  61.626 -22.268  1.00 31.69           C
ANISOU  598  CA  ILE A  72     3136   2612   6292   -135   -153   -471       C
ATOM    599  C   ILE A  72     -54.202  62.311 -20.930  1.00 32.40           C
ANISOU  599  C   ILE A  72     3237   2615   6458   -151   -202   -368       C
ATOM    600  O   ILE A  72     -53.070  62.685 -20.600  1.00 34.83           O
ANISOU  600  O   ILE A  72     3559   2807   6868   -172   -257   -349       O
ATOM    601  CB  ILE A  72     -55.146  62.569 -23.263  1.00 30.32           C
ANISOU  601  CB  ILE A  72     2944   2457   6119    -73   -120   -582       C
ATOM    602  CG1 ILE A  72     -55.250  61.914 -24.640  1.00 27.72           C
ANISOU  602  CG1 ILE A  72     2638   2195   5698    -63    -79   -684       C
ATOM    603  CG2 ILE A  72     -54.403  63.890 -23.353  1.00 27.03           C
ANISOU  603  CG2 ILE A  72     2492   1923   5854    -34   -170   -639       C
ATOM    604  CD1 ILE A  72     -53.917  61.723 -25.322  1.00 27.64           C
ANISOU  604  CD1 ILE A  72     2621   2128   5753    -74   -127   -756       C
ATOM    605  N   LEU A  73     -55.263  62.478 -20.137  1.00 33.23           N
ANISOU  605  N   LEU A  73     3352   2766   6506   -143   -189   -298       N
ATOM    606  CA  LEU A  73     -55.122  63.128 -18.838  1.00 29.28           C
ANISOU  606  CA  LEU A  73     2879   2189   6058   -151   -253   -196       C
ATOM    607  C   LEU A  73     -54.223  62.319 -17.913  1.00 27.05           C
ANISOU  607  C   LEU A  73     2656   1858   5763   -232   -263    -91       C
ATOM    608  O   LEU A  73     -53.451  62.888 -17.133  1.00 33.68           O
ANISOU  608  O   LEU A  73     3545   2578   6673   -248   -327    -25       O
ATOM    609  CB  LEU A  73     -56.497  63.335 -18.205  1.00 30.41           C
ANISOU  609  CB  LEU A  73     3021   2409   6126   -138   -237   -153       C
ATOM    610  CG  LEU A  73     -57.509  64.129 -19.035  1.00 31.76           C
ANISOU  610  CG  LEU A  73     3125   2638   6303    -83   -204   -262       C
ATOM    611  CD1 LEU A  73     -58.830  64.256 -18.295  1.00 32.41           C
ANISOU  611  CD1 LEU A  73     3207   2794   6313    -96   -188   -218       C
ATOM    612  CD2 LEU A  73     -56.958  65.500 -19.388  1.00 34.46           C
ANISOU  612  CD2 LEU A  73     3407   2891   6796    -12   -268   -341       C
ATOM    613  N   ASN A  74     -54.306  60.990 -17.986  1.00 29.06           N
ANISOU  613  N   ASN A  74     2912   2201   5928   -283   -198    -78       N
ATOM    614  CA  ASN A  74     -53.443  60.150 -17.163  1.00 28.69           C
ANISOU  614  CA  ASN A  74     2901   2124   5875   -373   -184      1       C
ATOM    615  C   ASN A  74     -51.985  60.292 -17.578  1.00 27.01           C
ANISOU  615  C   ASN A  74     2682   1809   5773   -414   -214    -43       C
ATOM    616  O   ASN A  74     -51.098  60.430 -16.728  1.00 29.05           O
ANISOU  616  O   ASN A  74     3001   1960   6075   -485   -232     32       O
ATOM    617  CB  ASN A  74     -53.887  58.691 -17.253  1.00 32.07           C
ANISOU  617  CB  ASN A  74     3305   2681   6198   -399   -109     -3       C
ATOM    618  CG  ASN A  74     -55.284  58.473 -16.715  1.00 36.24           C
ANISOU  618  CG  ASN A  74     3865   3293   6612   -373    -73     48       C
ATOM    619  OD1 ASN A  74     -55.801  59.289 -15.953  1.00 40.72           O
ANISOU  619  OD1 ASN A  74     4474   3825   7173   -365   -103    109       O
ATOM    620  ND2 ASN A  74     -55.903  57.366 -17.106  1.00 39.66           N
ANISOU  620  ND2 ASN A  74     4283   3833   6953   -356    -16     19       N
ATOM    621  N   ASN A  75     -51.721  60.262 -18.886  1.00 29.85           N
ANISOU  621  N   ASN A  75     2984   2190   6168   -378   -216   -166       N
ATOM    622  CA  ASN A  75     -50.348  60.362 -19.367  1.00 28.09           C
ANISOU  622  CA  ASN A  75     2754   1870   6048   -425   -244   -225       C
ATOM    623  C   ASN A  75     -49.710  61.687 -18.980  1.00 31.44           C
ANISOU  623  C   ASN A  75     3242   2123   6582   -408   -311   -197       C
ATOM    624  O   ASN A  75     -48.487  61.762 -18.815  1.00 40.15           O
ANISOU  624  O   ASN A  75     4386   3105   7765   -479   -332   -191       O
ATOM    625  CB  ASN A  75     -50.311  60.183 -20.882  1.00 30.24           C
ANISOU  625  CB  ASN A  75     2968   2201   6322   -378   -245   -370       C
ATOM    626  CG  ASN A  75     -50.770  58.809 -21.316  1.00 27.34           C
ANISOU  626  CG  ASN A  75     2553   1985   5851   -384   -204   -400       C
ATOM    627  OD1 ASN A  75     -50.739  57.856 -20.539  1.00 29.24           O
ANISOU  627  OD1 ASN A  75     2782   2277   6052   -442   -170   -333       O
ATOM    628  ND2 ASN A  75     -51.205  58.699 -22.564  1.00 27.09           N
ANISOU  628  ND2 ASN A  75     2501   2022   5770   -317   -206   -505       N
ATOM    629  N   LEU A  76     -50.512  62.736 -18.832  1.00 32.01           N
ANISOU  629  N   LEU A  76     3321   2178   6664   -314   -349   -186       N
ATOM    630  CA  LEU A  76     -50.021  64.030 -18.384  1.00 32.27           C
ANISOU  630  CA  LEU A  76     3410   2049   6800   -268   -432   -159       C
ATOM    631  C   LEU A  76     -49.955  64.142 -16.868  1.00 35.57           C
ANISOU  631  C   LEU A  76     3928   2395   7190   -310   -470     -2       C
ATOM    632  O   LEU A  76     -49.537  65.185 -16.356  1.00 38.17           O
ANISOU  632  O   LEU A  76     4330   2585   7589   -264   -557     40       O
ATOM    633  CB  LEU A  76     -50.901  65.148 -18.950  1.00 35.75           C
ANISOU  633  CB  LEU A  76     3790   2514   7280   -140   -462   -240       C
ATOM    634  CG  LEU A  76     -50.829  65.304 -20.469  1.00 38.64           C
ANISOU  634  CG  LEU A  76     4086   2915   7681    -95   -427   -403       C
ATOM    635  CD1 LEU A  76     -51.887  66.271 -20.970  1.00 40.53           C
ANISOU  635  CD1 LEU A  76     4253   3210   7935     10   -420   -487       C
ATOM    636  CD2 LEU A  76     -49.443  65.767 -20.882  1.00 41.06           C
ANISOU  636  CD2 LEU A  76     4431   3063   8108   -101   -473   -461       C
ATOM    637  N   GLY A  77     -50.352  63.099 -16.143  1.00 37.06           N
ANISOU  637  N   GLY A  77     4134   2679   7267   -390   -408     81       N
ATOM    638  CA  GLY A  77     -50.276  63.120 -14.697  1.00 37.49           C
ANISOU  638  CA  GLY A  77     4304   2671   7271   -445   -430    228       C
ATOM    639  C   GLY A  77     -51.333  63.949 -14.011  1.00 34.66           C
ANISOU  639  C   GLY A  77     3967   2327   6876   -358   -500    284       C
ATOM    640  O   GLY A  77     -51.106  64.411 -12.889  1.00 36.11           O
ANISOU  640  O   GLY A  77     4268   2408   7042   -372   -568    397       O
ATOM    641  N   VAL A  78     -52.485  64.155 -14.648  1.00 35.39           N
ANISOU  641  N   VAL A  78     3955   2542   6950   -277   -488    204       N
ATOM    642  CA  VAL A  78     -53.551  64.941 -14.041  1.00 35.39           C
ANISOU  642  CA  VAL A  78     3950   2573   6924   -206   -553    236       C
ATOM    643  C   VAL A  78     -54.110  64.193 -12.839  1.00 38.82           C
ANISOU  643  C   VAL A  78     4462   3067   7220   -281   -523    356       C
ATOM    644  O   VAL A  78     -54.417  62.996 -12.919  1.00 40.74           O
ANISOU  644  O   VAL A  78     4692   3417   7372   -348   -416    358       O
ATOM    645  CB  VAL A  78     -54.651  65.244 -15.068  1.00 38.20           C
ANISOU  645  CB  VAL A  78     4175   3052   7288   -132   -516    110       C
ATOM    646  CG1 VAL A  78     -55.829  65.931 -14.398  1.00 34.19           C
ANISOU  646  CG1 VAL A  78     3644   2598   6751    -84   -570    132       C
ATOM    647  CG2 VAL A  78     -54.100  66.104 -16.196  1.00 28.96           C
ANISOU  647  CG2 VAL A  78     2936   1816   6252    -54   -543    -16       C
ATOM    648  N   ASP A  79     -54.238  64.897 -11.715  1.00 38.04           N
ANISOU  648  N   ASP A  79     4452   2897   7104   -261   -623    450       N
ATOM    649  CA  ASP A  79     -54.748  64.311 -10.483  1.00 39.46           C
ANISOU  649  CA  ASP A  79     4729   3120   7143   -332   -605    565       C
ATOM    650  C   ASP A  79     -56.175  64.716 -10.157  1.00 38.11           C
ANISOU  650  C   ASP A  79     4512   3052   6915   -280   -644    552       C
ATOM    651  O   ASP A  79     -56.877  63.959  -9.483  1.00 40.11           O
ANISOU  651  O   ASP A  79     4811   3390   7038   -343   -587    605       O
ATOM    652  CB  ASP A  79     -53.851  64.695  -9.298  1.00 43.08           C
ANISOU  652  CB  ASP A  79     5363   3420   7584   -370   -691    697       C
ATOM    653  CG  ASP A  79     -52.407  64.290  -9.501  1.00 46.80           C
ANISOU  653  CG  ASP A  79     5900   3775   8107   -451   -641    716       C
ATOM    654  OD1 ASP A  79     -52.161  63.181 -10.023  1.00 50.23           O
ANISOU  654  OD1 ASP A  79     6274   4288   8523   -531   -510    672       O
ATOM    655  OD2 ASP A  79     -51.515  65.085  -9.137  1.00 51.85           O
ANISOU  655  OD2 ASP A  79     6653   4240   8806   -433   -739    770       O
ATOM    656  N   ILE A  80     -56.622  65.882 -10.623  1.00 32.73           N
ANISOU  656  N   ILE A  80     3734   2369   6332   -172   -735    470       N
ATOM    657  CA  ILE A  80     -57.912  66.428 -10.218  1.00 31.94           C
ANISOU  657  CA  ILE A  80     3581   2357   6196   -132   -790    451       C
ATOM    658  C   ILE A  80     -58.318  67.486 -11.232  1.00 31.30           C
ANISOU  658  C   ILE A  80     3337   2304   6252    -27   -825    307       C
ATOM    659  O   ILE A  80     -57.469  68.086 -11.895  1.00 36.76           O
ANISOU  659  O   ILE A  80     3991   2905   7070     38   -861    251       O
ATOM    660  CB  ILE A  80     -57.832  67.000  -8.780  1.00 37.70           C
ANISOU  660  CB  ILE A  80     4440   3007   6879   -121   -937    571       C
ATOM    661  CG1 ILE A  80     -59.224  67.153  -8.165  1.00 43.80           C
ANISOU  661  CG1 ILE A  80     5181   3894   7566   -124   -971    565       C
ATOM    662  CG2 ILE A  80     -57.088  68.325  -8.768  1.00 39.03           C
ANISOU  662  CG2 ILE A  80     4609   3033   7188     -4  -1102    561       C
ATOM    663  CD1 ILE A  80     -59.187  67.425  -6.674  1.00 31.75           C
ANISOU  663  CD1 ILE A  80     3814   2304   5945   -137  -1103    694       C
ATOM    664  N   ALA A  81     -59.623  67.705 -11.364  1.00 32.63           N
ANISOU  664  N   ALA A  81     3407   2597   6393    -20   -804    237       N
ATOM    665  CA  ALA A  81     -60.162  68.691 -12.287  1.00 29.64           C
ANISOU  665  CA  ALA A  81     2860   2268   6136     59   -811     86       C
ATOM    666  C   ALA A  81     -60.684  69.897 -11.518  1.00 36.71           C
ANISOU  666  C   ALA A  81     3693   3161   7094    136   -972     72       C
ATOM    667  O   ALA A  81     -61.131  69.781 -10.373  1.00 33.60           O
ANISOU  667  O   ALA A  81     3378   2783   6607    102  -1045    163       O
ATOM    668  CB  ALA A  81     -61.280  68.092 -13.145  1.00 28.43           C
ANISOU  668  CB  ALA A  81     2632   2257   5913     -2   -652     -6       C
ATOM    669  N   ALA A  82     -60.626  71.059 -12.165  1.00 39.25           N
ANISOU  669  N   ALA A  82     3869   3468   7577    244  -1030    -54       N
ATOM    670  CA  ALA A  82     -61.026  72.319 -11.548  1.00 41.45           C
ANISOU  670  CA  ALA A  82     4054   3745   7952    346  -1203    -94       C
ATOM    671  C   ALA A  82     -62.512  72.557 -11.795  1.00 42.52           C
ANISOU  671  C   ALA A  82     4027   4050   8079    306  -1139   -214       C
ATOM    672  O   ALA A  82     -62.918  72.886 -12.915  1.00 43.09           O
ANISOU  672  O   ALA A  82     3947   4194   8230    314  -1028   -367       O
ATOM    673  CB  ALA A  82     -60.190  73.474 -12.093  1.00 40.58           C
ANISOU  673  CB  ALA A  82     3856   3529   8034    495  -1299   -184       C
ATOM    674  N   ASN A  83     -63.321  72.381 -10.747  1.00 42.19           N
ANISOU  674  N   ASN A  83     4028   4069   7933    250  -1201   -149       N
ATOM    675  CA  ASN A  83     -64.739  72.750 -10.757  1.00 45.39           C
ANISOU  675  CA  ASN A  83     4283   4624   8339    206  -1175   -261       C
ATOM    676  C   ASN A  83     -65.519  71.996 -11.832  1.00 46.49           C
ANISOU  676  C   ASN A  83     4383   4869   8414     91   -937   -345       C
ATOM    677  O   ASN A  83     -66.428  72.540 -12.463  1.00 48.03           O
ANISOU  677  O   ASN A  83     4410   5167   8672     70   -865   -497       O
ATOM    678  CB  ASN A  83     -64.908  74.263 -10.920  1.00 53.48           C
ANISOU  678  CB  ASN A  83     5091   5670   9560    336  -1308   -407       C
ATOM    679  CG  ASN A  83     -64.106  75.050  -9.901  1.00 61.67           C
ANISOU  679  CG  ASN A  83     6186   6584  10662    476  -1567   -323       C
ATOM    680  OD1 ASN A  83     -63.016  75.540 -10.196  1.00 68.69           O
ANISOU  680  OD1 ASN A  83     7092   7346  11662    593  -1636   -319       O
ATOM    681  ND2 ASN A  83     -64.639  75.167  -8.689  1.00 61.43           N
ANISOU  681  ND2 ASN A  83     6207   6582  10553    462  -1715   -253       N
ATOM    682  N   THR A  84     -65.168  70.729 -12.037  1.00 44.69           N
ANISOU  682  N   THR A  84     4313   4612   8054     15   -814   -250       N
ATOM    683  CA  THR A  84     -65.892  69.869 -12.963  1.00 40.39           C
ANISOU  683  CA  THR A  84     3778   4149   7417    -86   -606   -304       C
ATOM    684  C   THR A  84     -65.567  68.422 -12.621  1.00 37.07           C
ANISOU  684  C   THR A  84     3552   3697   6836   -156   -538   -164       C
ATOM    685  O   THR A  84     -64.681  68.139 -11.811  1.00 40.41           O
ANISOU  685  O   THR A  84     4086   4036   7234   -134   -627    -40       O
ATOM    686  CB  THR A  84     -65.542  70.179 -14.423  1.00 37.35           C
ANISOU  686  CB  THR A  84     3298   3763   7129    -48   -500   -431       C
ATOM    687  OG1 THR A  84     -66.417  69.451 -15.294  1.00 37.08           O
ANISOU  687  OG1 THR A  84     3287   3811   6991   -147   -310   -489       O
ATOM    688  CG2 THR A  84     -64.106  69.785 -14.722  1.00 33.23           C
ANISOU  688  CG2 THR A  84     2868   3126   6631      8   -519   -362       C
ATOM    689  N   VAL A  85     -66.300  67.508 -13.251  1.00 33.10           N
ANISOU  689  N   VAL A  85     3094   3260   6222   -240   -374   -190       N
ATOM    690  CA  VAL A  85     -66.102  66.074 -13.075  1.00 27.66           C
ANISOU  690  CA  VAL A  85     2565   2556   5389   -294   -294    -84       C
ATOM    691  C   VAL A  85     -65.881  65.454 -14.445  1.00 26.51           C
ANISOU  691  C   VAL A  85     2428   2417   5228   -294   -160   -143       C
ATOM    692  O   VAL A  85     -66.774  65.489 -15.301  1.00 27.41           O
ANISOU  692  O   VAL A  85     2508   2594   5314   -331    -50   -239       O
ATOM    693  CB  VAL A  85     -67.291  65.407 -12.366  1.00 29.18           C
ANISOU  693  CB  VAL A  85     2841   2811   5435   -385   -244    -46       C
ATOM    694  CG1 VAL A  85     -67.152  63.894 -12.420  1.00 24.36           C
ANISOU  694  CG1 VAL A  85     2376   2193   4688   -423   -140     32       C
ATOM    695  CG2 VAL A  85     -67.375  65.874 -10.929  1.00 33.59           C
ANISOU  695  CG2 VAL A  85     3424   3357   5982   -387   -390     28       C
ATOM    696  N   ILE A  86     -64.697  64.889 -14.652  1.00 25.89           N
ANISOU  696  N   ILE A  86     2402   2273   5161   -260   -168    -89       N
ATOM    697  CA  ILE A  86     -64.407  64.107 -15.847  1.00 27.96           C
ANISOU  697  CA  ILE A  86     2693   2543   5387   -259    -62   -131       C
ATOM    698  C   ILE A  86     -64.875  62.682 -15.578  1.00 30.31           C
ANISOU  698  C   ILE A  86     3114   2875   5528   -312     16    -60       C
ATOM    699  O   ILE A  86     -64.331  61.992 -14.711  1.00 30.94           O
ANISOU  699  O   ILE A  86     3261   2926   5567   -323    -16     40       O
ATOM    700  CB  ILE A  86     -62.918  64.147 -16.201  1.00 27.81           C
ANISOU  700  CB  ILE A  86     2664   2443   5462   -205   -113   -121       C
ATOM    701  CG1 ILE A  86     -62.417  65.592 -16.242  1.00 30.27           C
ANISOU  701  CG1 ILE A  86     2869   2698   5934   -137   -211   -180       C
ATOM    702  CG2 ILE A  86     -62.673  63.454 -17.532  1.00 31.08           C
ANISOU  702  CG2 ILE A  86     3093   2874   5840   -199    -20   -188       C
ATOM    703  CD1 ILE A  86     -63.138  66.461 -17.248  1.00 25.82           C
ANISOU  703  CD1 ILE A  86     2193   2188   5429   -117   -152   -328       C
ATOM    704  N   TRP A  87     -65.890  62.240 -16.312  1.00 28.20           N
ANISOU  704  N   TRP A  87     2883   2663   5168   -343    124   -116       N
ATOM    705  CA  TRP A  87     -66.448  60.909 -16.119  1.00 30.61           C
ANISOU  705  CA  TRP A  87     3312   2994   5325   -375    196    -61       C
ATOM    706  C   TRP A  87     -65.714  59.914 -17.010  1.00 29.36           C
ANISOU  706  C   TRP A  87     3194   2824   5136   -332    232    -67       C
ATOM    707  O   TRP A  87     -65.636  60.104 -18.228  1.00 30.55           O
ANISOU  707  O   TRP A  87     3327   2978   5302   -307    269   -149       O
ATOM    708  CB  TRP A  87     -67.945  60.891 -16.422  1.00 30.37           C
ANISOU  708  CB  TRP A  87     3331   3010   5198   -433    290   -112       C
ATOM    709  CG  TRP A  87     -68.583  59.610 -16.015  1.00 27.26           C
ANISOU  709  CG  TRP A  87     3077   2625   4656   -458    348    -50       C
ATOM    710  CD1 TRP A  87     -68.922  58.568 -16.825  1.00 24.76           C
ANISOU  710  CD1 TRP A  87     2868   2308   4232   -440    429    -62       C
ATOM    711  CD2 TRP A  87     -68.932  59.217 -14.685  1.00 21.50           C
ANISOU  711  CD2 TRP A  87     2405   1897   3866   -494    322     30       C
ATOM    712  NE1 TRP A  87     -69.475  57.554 -16.082  1.00 26.04           N
ANISOU  712  NE1 TRP A  87     3142   2469   4281   -454    458      1       N
ATOM    713  CE2 TRP A  87     -69.491  57.928 -14.764  1.00 21.10           C
ANISOU  713  CE2 TRP A  87     2488   1848   3681   -494    401     56       C
ATOM    714  CE3 TRP A  87     -68.831  59.834 -13.435  1.00 21.87           C
ANISOU  714  CE3 TRP A  87     2417   1941   3953   -521    234     80       C
ATOM    715  CZ2 TRP A  87     -69.950  57.244 -13.642  1.00 26.53           C
ANISOU  715  CZ2 TRP A  87     3265   2535   4279   -524    410    121       C
ATOM    716  CZ3 TRP A  87     -69.286  59.154 -12.322  1.00 22.81           C
ANISOU  716  CZ3 TRP A  87     2635   2063   3968   -561    240    150       C
ATOM    717  CH2 TRP A  87     -69.837  57.872 -12.432  1.00 21.36           C
ANISOU  717  CH2 TRP A  87     2575   1883   3658   -564    335    167       C
ATOM    718  N   ASP A  88     -65.176  58.860 -16.401  1.00 27.42           N
ANISOU  718  N   ASP A  88     3001   2570   4847   -325    220     12       N
ATOM    719  CA  ASP A  88     -64.506  57.790 -17.136  1.00 27.21           C
ANISOU  719  CA  ASP A  88     2998   2547   4794   -281    241      1       C
ATOM    720  C   ASP A  88     -65.570  56.778 -17.539  1.00 26.67           C
ANISOU  720  C   ASP A  88     3040   2514   4581   -272    320     -9       C
ATOM    721  O   ASP A  88     -66.034  55.985 -16.717  1.00 24.20           O
ANISOU  721  O   ASP A  88     2794   2212   4188   -285    345     49       O
ATOM    722  CB  ASP A  88     -63.410  57.152 -16.290  1.00 29.56           C
ANISOU  722  CB  ASP A  88     3280   2825   5127   -285    202     73       C
ATOM    723  CG  ASP A  88     -62.521  56.211 -17.086  1.00 35.77           C
ANISOU  723  CG  ASP A  88     4045   3622   5925   -243    204     39       C
ATOM    724  OD1 ASP A  88     -62.941  55.744 -18.167  1.00 38.29           O
ANISOU  724  OD1 ASP A  88     4397   3968   6182   -198    234    -22       O
ATOM    725  OD2 ASP A  88     -61.396  55.933 -16.623  1.00 40.77           O
ANISOU  725  OD2 ASP A  88     4634   4234   6624   -260    173     71       O
ATOM    726  N   TYR A  89     -65.961  56.809 -18.814  1.00 29.36           N
ANISOU  726  N   TYR A  89     3414   2861   4879   -248    361    -83       N
ATOM    727  CA  TYR A  89     -66.975  55.883 -19.300  1.00 29.57           C
ANISOU  727  CA  TYR A  89     3578   2899   4757   -232    430    -90       C
ATOM    728  C   TYR A  89     -66.428  54.477 -19.496  1.00 34.78           C
ANISOU  728  C   TYR A  89     4276   3568   5369   -155    407    -70       C
ATOM    729  O   TYR A  89     -67.213  53.525 -19.559  1.00 36.58           O
ANISOU  729  O   TYR A  89     4624   3797   5477   -123    445    -55       O
ATOM    730  CB  TYR A  89     -67.574  56.404 -20.605  1.00 28.98           C
ANISOU  730  CB  TYR A  89     3554   2821   4637   -241    487   -174       C
ATOM    731  CG  TYR A  89     -68.502  57.584 -20.423  1.00 31.59           C
ANISOU  731  CG  TYR A  89     3860   3157   4986   -326    541   -210       C
ATOM    732  CD1 TYR A  89     -69.880  57.414 -20.443  1.00 32.09           C
ANISOU  732  CD1 TYR A  89     4046   3218   4929   -386    630   -214       C
ATOM    733  CD2 TYR A  89     -68.003  58.866 -20.226  1.00 29.81           C
ANISOU  733  CD2 TYR A  89     3486   2936   4905   -347    500   -247       C
ATOM    734  CE1 TYR A  89     -70.736  58.486 -20.278  1.00 30.91           C
ANISOU  734  CE1 TYR A  89     3853   3085   4806   -479    684   -264       C
ATOM    735  CE2 TYR A  89     -68.853  59.945 -20.061  1.00 30.25           C
ANISOU  735  CE2 TYR A  89     3490   3010   4993   -418    541   -297       C
ATOM    736  CZ  TYR A  89     -70.218  59.748 -20.087  1.00 33.19           C
ANISOU  736  CZ  TYR A  89     3967   3395   5249   -491    636   -309       C
ATOM    737  OH  TYR A  89     -71.073  60.814 -19.922  1.00 30.60           O
ANISOU  737  OH  TYR A  89     3569   3097   4962   -577    682   -375       O
ATOM    738  N   LYS A  90     -65.106  54.323 -19.598  1.00 36.27           N
ANISOU  738  N   LYS A  90     4364   3762   5655   -123    343    -78       N
ATOM    739  CA  LYS A  90     -64.525  52.988 -19.685  1.00 35.12           C
ANISOU  739  CA  LYS A  90     4216   3641   5486    -56    316    -73       C
ATOM    740  C   LYS A  90     -64.700  52.229 -18.376  1.00 32.68           C
ANISOU  740  C   LYS A  90     3917   3347   5152    -69    340     -3       C
ATOM    741  O   LYS A  90     -65.021  51.035 -18.381  1.00 35.14           O
ANISOU  741  O   LYS A  90     4284   3679   5386     -5    356     -1       O
ATOM    742  CB  LYS A  90     -63.046  53.084 -20.060  1.00 36.30           C
ANISOU  742  CB  LYS A  90     4242   3794   5757    -45    250   -109       C
ATOM    743  CG  LYS A  90     -62.800  53.733 -21.410  1.00 41.70           C
ANISOU  743  CG  LYS A  90     4924   4463   6456    -24    226   -191       C
ATOM    744  CD  LYS A  90     -63.294  52.848 -22.541  1.00 45.49           C
ANISOU  744  CD  LYS A  90     5511   4964   6810     55    224   -238       C
ATOM    745  CE  LYS A  90     -63.438  53.634 -23.832  1.00 51.80           C
ANISOU  745  CE  LYS A  90     6359   5744   7580     56    234   -314       C
ATOM    746  NZ  LYS A  90     -62.198  54.383 -24.168  1.00 54.36           N
ANISOU  746  NZ  LYS A  90     6561   6054   8039     36    183   -368       N
ATOM    747  N   ARG A  91     -64.499  52.905 -17.245  1.00 29.06           N
ANISOU  747  N   ARG A  91     3412   2874   4754   -144    340     52       N
ATOM    748  CA  ARG A  91     -64.691  52.301 -15.936  1.00 29.40           C
ANISOU  748  CA  ARG A  91     3482   2928   4759   -173    373    118       C
ATOM    749  C   ARG A  91     -66.057  52.600 -15.335  1.00 28.04           C
ANISOU  749  C   ARG A  91     3418   2745   4493   -214    418    149       C
ATOM    750  O   ARG A  91     -66.372  52.062 -14.267  1.00 29.68           O
ANISOU  750  O   ARG A  91     3672   2959   4647   -236    452    197       O
ATOM    751  CB  ARG A  91     -63.603  52.777 -14.964  1.00 29.64           C
ANISOU  751  CB  ARG A  91     3430   2942   4890   -238    342    168       C
ATOM    752  CG  ARG A  91     -62.183  52.508 -15.427  1.00 28.91           C
ANISOU  752  CG  ARG A  91     3232   2853   4901   -226    305    136       C
ATOM    753  CD  ARG A  91     -61.160  52.988 -14.401  1.00 30.47           C
ANISOU  753  CD  ARG A  91     3385   3012   5181   -308    287    195       C
ATOM    754  NE  ARG A  91     -61.361  54.386 -14.028  1.00 34.54           N
ANISOU  754  NE  ARG A  91     3922   3472   5731   -347    241    231       N
ATOM    755  CZ  ARG A  91     -61.748  54.794 -12.823  1.00 31.58           C
ANISOU  755  CZ  ARG A  91     3607   3076   5317   -400    240    306       C
ATOM    756  NH1 ARG A  91     -61.968  53.911 -11.859  1.00 30.90           N
ANISOU  756  NH1 ARG A  91     3575   3016   5149   -431    298    354       N
ATOM    757  NH2 ARG A  91     -61.907  56.088 -12.577  1.00 32.06           N
ANISOU  757  NH2 ARG A  91     3670   3091   5420   -416    175    325       N
ATOM    758  N   ASP A  92     -66.870  53.430 -15.991  1.00 25.78           N
ANISOU  758  N   ASP A  92     3169   2442   4183   -233    428    113       N
ATOM    759  CA  ASP A  92     -68.155  53.879 -15.452  1.00 27.88           C
ANISOU  759  CA  ASP A  92     3519   2700   4376   -295    470    127       C
ATOM    760  C   ASP A  92     -67.976  54.463 -14.053  1.00 26.81           C
ANISOU  760  C   ASP A  92     3344   2563   4280   -363    436    187       C
ATOM    761  O   ASP A  92     -68.714  54.154 -13.116  1.00 26.95           O
ANISOU  761  O   ASP A  92     3441   2582   4216   -402    466    224       O
ATOM    762  CB  ASP A  92     -69.182  52.745 -15.453  1.00 33.59           C
ANISOU  762  CB  ASP A  92     4388   3416   4959   -265    537    132       C
ATOM    763  CG  ASP A  92     -69.600  52.338 -16.853  1.00 44.79           C
ANISOU  763  CG  ASP A  92     5890   4817   6310   -203    563     78       C
ATOM    764  OD1 ASP A  92     -69.685  53.223 -17.731  1.00 48.05           O
ANISOU  764  OD1 ASP A  92     6281   5225   6750   -230    565     30       O
ATOM    765  OD2 ASP A  92     -69.843  51.133 -17.077  1.00 48.84           O
ANISOU  765  OD2 ASP A  92     6498   5321   6739   -123    580     80       O
ATOM    766  N   ALA A  93     -66.969  55.319 -13.920  1.00 23.81           N
ANISOU  766  N   ALA A  93     2856   2172   4018   -375    366    197       N
ATOM    767  CA  ALA A  93     -66.587  55.895 -12.641  1.00 22.04           C
ANISOU  767  CA  ALA A  93     2611   1933   3832   -426    311    262       C
ATOM    768  C   ALA A  93     -65.941  57.243 -12.901  1.00 21.80           C
ANISOU  768  C   ALA A  93     2479   1874   3931   -426    228    242       C
ATOM    769  O   ALA A  93     -65.500  57.515 -14.024  1.00 22.65           O
ANISOU  769  O   ALA A  93     2524   1976   4107   -386    224    180       O
ATOM    770  CB  ALA A  93     -65.624  54.972 -11.880  1.00 23.01           C
ANISOU  770  CB  ALA A  93     2742   2052   3950   -426    320    322       C
ATOM    771  N   PRO A  94     -65.881  58.119 -11.898  1.00 25.50           N
ANISOU  771  N   PRO A  94     2936   2321   4433   -463    154    287       N
ATOM    772  CA  PRO A  94     -65.161  59.383 -12.081  1.00 25.62           C
ANISOU  772  CA  PRO A  94     2858   2296   4582   -440     60    268       C
ATOM    773  C   PRO A  94     -63.678  59.131 -12.307  1.00 30.92           C
ANISOU  773  C   PRO A  94     3499   2917   5331   -414     36    292       C
ATOM    774  O   PRO A  94     -63.087  58.221 -11.723  1.00 32.52           O
ANISOU  774  O   PRO A  94     3752   3112   5493   -438     64    354       O
ATOM    775  CB  PRO A  94     -65.417  60.134 -10.770  1.00 25.21           C
ANISOU  775  CB  PRO A  94     2832   2227   4520   -475    -29    328       C
ATOM    776  CG  PRO A  94     -65.764  59.072  -9.784  1.00 27.44           C
ANISOU  776  CG  PRO A  94     3232   2528   4668   -525     24    400       C
ATOM    777  CD  PRO A  94     -66.506  58.034 -10.566  1.00 26.83           C
ANISOU  777  CD  PRO A  94     3186   2496   4511   -518    142    350       C
ATOM    778  N   ALA A  95     -63.079  59.950 -13.172  1.00 33.90           N
ANISOU  778  N   ALA A  95     3792   3263   5827   -372     -7    231       N
ATOM    779  CA  ALA A  95     -61.681  59.754 -13.530  1.00 22.57           C
ANISOU  779  CA  ALA A  95     2330   1774   4473   -355    -27    236       C
ATOM    780  C   ALA A  95     -60.729  60.102 -12.393  1.00 24.86           C
ANISOU  780  C   ALA A  95     2659   1984   4804   -385   -102    330       C
ATOM    781  O   ALA A  95     -59.584  59.639 -12.401  1.00 24.75           O
ANISOU  781  O   ALA A  95     2651   1924   4827   -406    -94    354       O
ATOM    782  CB  ALA A  95     -61.334  60.582 -14.769  1.00 22.76           C
ANISOU  782  CB  ALA A  95     2267   1776   4606   -302    -50    136       C
ATOM    783  N   HIS A  96     -61.166  60.896 -11.418  1.00 24.84           N
ANISOU  783  N   HIS A  96     2691   1959   4788   -394   -176    381       N
ATOM    784  CA  HIS A  96     -60.294  61.350 -10.346  1.00 25.05           C
ANISOU  784  CA  HIS A  96     2787   1892   4839   -415   -264    477       C
ATOM    785  C   HIS A  96     -60.968  61.144  -8.997  1.00 28.45           C
ANISOU  785  C   HIS A  96     3322   2344   5145   -467   -277    564       C
ATOM    786  O   HIS A  96     -62.194  61.195  -8.880  1.00 31.50           O
ANISOU  786  O   HIS A  96     3701   2803   5466   -468   -265    535       O
ATOM    787  CB  HIS A  96     -59.914  62.822 -10.529  1.00 27.94           C
ANISOU  787  CB  HIS A  96     3100   2179   5336   -346   -392    448       C
ATOM    788  CG  HIS A  96     -59.379  63.135 -11.891  1.00 26.08           C
ANISOU  788  CG  HIS A  96     2764   1927   5220   -292   -376    345       C
ATOM    789  ND1 HIS A  96     -60.076  63.891 -12.808  1.00 26.43           N
ANISOU  789  ND1 HIS A  96     2699   2016   5326   -233   -378    232       N
ATOM    790  CD2 HIS A  96     -58.223  62.778 -12.498  1.00 25.64           C
ANISOU  790  CD2 HIS A  96     2702   1814   5225   -299   -349    329       C
ATOM    791  CE1 HIS A  96     -59.368  63.995 -13.919  1.00 30.94           C
ANISOU  791  CE1 HIS A  96     3214   2558   5984   -198   -354    154       C
ATOM    792  NE2 HIS A  96     -58.240  63.327 -13.757  1.00 25.55           N
ANISOU  792  NE2 HIS A  96     2592   1813   5305   -236   -344    210       N
ATOM    793  N   ILE A  97     -60.143  60.917  -7.977  1.00 36.64           N
ANISOU  793  N   ILE A  97     4469   3312   6142   -520   -297    667       N
ATOM    794  CA  ILE A  97     -60.621  60.617  -6.631  1.00 41.90           C
ANISOU  794  CA  ILE A  97     5263   3989   6669   -581   -300    756       C
ATOM    795  C   ILE A  97     -61.397  61.802  -6.068  1.00 42.58           C
ANISOU  795  C   ILE A  97     5359   4068   6751   -542   -441    763       C
ATOM    796  O   ILE A  97     -62.611  61.721  -5.845  1.00 41.71           O
ANISOU  796  O   ILE A  97     5244   4040   6565   -553   -428    734       O
ATOM    797  CB  ILE A  97     -59.445  60.250  -5.706  1.00 47.84           C
ANISOU  797  CB  ILE A  97     6144   4652   7380   -655   -287    863       C
ATOM    798  CG1 ILE A  97     -58.545  59.202  -6.364  1.00 51.44           C
ANISOU  798  CG1 ILE A  97     6550   5117   7877   -695   -159    832       C
ATOM    799  CG2 ILE A  97     -59.956  59.760  -4.360  1.00 49.19           C
ANISOU  799  CG2 ILE A  97     6460   4845   7383   -729   -258    946       C
ATOM    800  CD1 ILE A  97     -57.274  58.923  -5.585  1.00 53.12           C
ANISOU  800  CD1 ILE A  97     6874   5234   8073   -788   -130    921       C
ATOM    801  N   SER A  98     -60.700  62.905  -5.826  1.00 41.14           N
ANISOU  801  N   SER A  98     5192   3785   6653   -493   -584    797       N
ATOM    802  CA  SER A  98     -61.291  64.060  -5.173  1.00 37.33           C
ANISOU  802  CA  SER A  98     4719   3290   6174   -443   -748    807       C
ATOM    803  C   SER A  98     -61.803  65.061  -6.204  1.00 35.03           C
ANISOU  803  C   SER A  98     4242   3037   6029   -349   -806    679       C
ATOM    804  O   SER A  98     -61.573  64.932  -7.408  1.00 34.07           O
ANISOU  804  O   SER A  98     4012   2933   6000   -323   -724    594       O
ATOM    805  CB  SER A  98     -60.273  64.718  -4.243  1.00 38.99           C
ANISOU  805  CB  SER A  98     5072   3358   6385   -428   -889    919       C
ATOM    806  OG  SER A  98     -59.784  63.791  -3.289  1.00 35.53           O
ANISOU  806  OG  SER A  98     4814   2884   5802   -534   -812   1033       O
ATOM    807  N   THR A  99     -62.512  66.071  -5.710  1.00 34.28           N
ANISOU  807  N   THR A  99     4110   2962   5952   -302   -949    656       N
ATOM    808  CA  THR A  99     -63.072  67.126  -6.538  1.00 36.34           C
ANISOU  808  CA  THR A  99     4181   3272   6356   -219  -1007    523       C
ATOM    809  C   THR A  99     -62.760  68.478  -5.911  1.00 37.66           C
ANISOU  809  C   THR A  99     4338   3362   6610   -116  -1232    538       C
ATOM    810  O   THR A  99     -62.303  68.572  -4.768  1.00 38.00           O
ANISOU  810  O   THR A  99     4544   3322   6573   -118  -1349    660       O
ATOM    811  CB  THR A  99     -64.588  66.959  -6.716  1.00 35.50           C
ANISOU  811  CB  THR A  99     3989   3306   6194   -271   -935    434       C
ATOM    812  OG1 THR A  99     -65.208  66.792  -5.434  1.00 38.24           O
ANISOU  812  OG1 THR A  99     4451   3677   6403   -327  -1002    507       O
ATOM    813  CG2 THR A  99     -64.894  65.748  -7.585  1.00 29.79           C
ANISOU  813  CG2 THR A  99     3267   2644   5410   -340   -725    400       C
ATOM    814  N   ILE A 100     -63.008  69.535  -6.681  1.00 36.70           N
ANISOU  814  N   ILE A 100     4028   3266   6650    -21  -1292    408       N
ATOM    815  CA  ILE A 100     -62.796  70.910  -6.242  1.00 37.55           C
ANISOU  815  CA  ILE A 100     4082   3312   6872    108  -1517    390       C
ATOM    816  C   ILE A 100     -64.071  71.684  -6.541  1.00 39.10           C
ANISOU  816  C   ILE A 100     4064   3646   7145    134  -1550    236       C
ATOM    817  O   ILE A 100     -64.408  71.901  -7.711  1.00 37.09           O
ANISOU  817  O   ILE A 100     3633   3460   6998    145  -1438     95       O
ATOM    818  CB  ILE A 100     -61.590  71.564  -6.929  1.00 42.39           C
ANISOU  818  CB  ILE A 100     4663   3797   7647    222  -1566    365       C
ATOM    819  CG1 ILE A 100     -60.298  70.839  -6.550  1.00 42.10           C
ANISOU  819  CG1 ILE A 100     4846   3615   7535    176  -1537    515       C
ATOM    820  CG2 ILE A 100     -61.504  73.037  -6.559  1.00 43.01           C
ANISOU  820  CG2 ILE A 100     4662   3820   7860    380  -1805    321       C
ATOM    821  CD1 ILE A 100     -59.076  71.336  -7.293  1.00 41.53           C
ANISOU  821  CD1 ILE A 100     4761   3406   7612    262  -1560    488       C
ATOM    822  N   GLY A 101     -64.777  72.097  -5.493  1.00 41.89           N
ANISOU  822  N   GLY A 101     4434   4044   7440    134  -1699    256       N
ATOM    823  CA  GLY A 101     -65.988  72.886  -5.665  1.00 44.45           C
ANISOU  823  CA  GLY A 101     4541   4504   7844    147  -1746    102       C
ATOM    824  C   GLY A 101     -67.072  72.193  -6.460  1.00 46.00           C
ANISOU  824  C   GLY A 101     4647   4835   7996     15  -1517      2       C
ATOM    825  O   GLY A 101     -67.730  72.829  -7.292  1.00 47.49           O
ANISOU  825  O   GLY A 101     4620   5116   8309     26  -1467   -163       O
ATOM    826  N   VAL A 102     -67.274  70.897  -6.224  1.00 44.48           N
ANISOU  826  N   VAL A 102     4623   4652   7625   -110  -1372     96       N
ATOM    827  CA  VAL A 102     -68.270  70.126  -6.961  1.00 41.64           C
ANISOU  827  CA  VAL A 102     4223   4396   7202   -230  -1157     20       C
ATOM    828  C   VAL A 102     -69.211  69.425  -5.991  1.00 38.89           C
ANISOU  828  C   VAL A 102     4000   4102   6674   -346  -1141     75       C
ATOM    829  O   VAL A 102     -70.410  69.722  -5.947  1.00 41.04           O
ANISOU  829  O   VAL A 102     4176   4476   6941   -412  -1131    -26       O
ATOM    830  CB  VAL A 102     -67.601  69.105  -7.901  1.00 42.22           C
ANISOU  830  CB  VAL A 102     4372   4425   7245   -254   -969     55       C
ATOM    831  CG1 VAL A 102     -68.652  68.209  -8.530  1.00 42.31           C
ANISOU  831  CG1 VAL A 102     4393   4525   7159   -369   -765     -1       C
ATOM    832  CG2 VAL A 102     -66.791  69.817  -8.973  1.00 44.20           C
ANISOU  832  CG2 VAL A 102     4494   4631   7671   -151   -969    -25       C
ATOM    833  N   CYS A 103     -68.676  68.488  -5.212  1.00 37.72           N
ANISOU  833  N   CYS A 103     4066   3887   6378   -381  -1128    226       N
ATOM    834  CA  CYS A 103     -69.464  67.680  -4.292  1.00 38.30           C
ANISOU  834  CA  CYS A 103     4286   4000   6266   -491  -1091    283       C
ATOM    835  C   CYS A 103     -68.868  67.783  -2.898  1.00 38.90           C
ANISOU  835  C   CYS A 103     4531   4003   6246   -469  -1259    418       C
ATOM    836  O   CYS A 103     -67.678  67.513  -2.710  1.00 43.73           O
ANISOU  836  O   CYS A 103     5257   4511   6846   -429  -1271    528       O
ATOM    837  CB  CYS A 103     -69.507  66.217  -4.741  1.00 40.15           C
ANISOU  837  CB  CYS A 103     4635   4234   6387   -569   -867    322       C
ATOM    838  SG  CYS A 103     -70.119  65.072  -3.489  1.00 44.80           S
ANISOU  838  SG  CYS A 103     5446   4835   6740   -681   -816    416       S
ATOM    839  N   SER A 104     -69.703  68.153  -1.923  1.00 37.57           N
ANISOU  839  N   SER A 104     4390   3885   6000   -506  -1384    409       N
ATOM    840  CA  SER A 104     -69.214  68.381  -0.566  1.00 46.93           C
ANISOU  840  CA  SER A 104     5751   5002   7080   -482  -1569    532       C
ATOM    841  C   SER A 104     -68.567  67.136   0.026  1.00 50.05           C
ANISOU  841  C   SER A 104     6392   5326   7299   -552  -1448    678       C
ATOM    842  O   SER A 104     -67.652  67.246   0.850  1.00 57.34           O
ANISOU  842  O   SER A 104     7479   6150   8159   -521  -1555    803       O
ATOM    843  CB  SER A 104     -70.357  68.854   0.331  1.00 57.72           C
ANISOU  843  CB  SER A 104     7110   6451   8371   -528  -1709    482       C
ATOM    844  OG  SER A 104     -70.940  70.043  -0.171  1.00 70.33           O
ANISOU  844  OG  SER A 104     8454   8126  10144   -467  -1824    331       O
ATOM    845  N   MET A 105     -69.020  65.949  -0.378  1.00 44.95           N
ANISOU  845  N   MET A 105     5780   4725   6574   -644  -1225    662       N
ATOM    846  CA  MET A 105     -68.461  64.723   0.177  1.00 46.70           C
ANISOU  846  CA  MET A 105     6207   4897   6641   -709  -1097    778       C
ATOM    847  C   MET A 105     -67.084  64.407  -0.396  1.00 40.99           C
ANISOU  847  C   MET A 105     5493   4086   5994   -664  -1026    839       C
ATOM    848  O   MET A 105     -66.251  63.818   0.301  1.00 41.18           O
ANISOU  848  O   MET A 105     5690   4039   5918   -700   -992    953       O
ATOM    849  CB  MET A 105     -69.419  63.554  -0.061  1.00 56.46           C
ANISOU  849  CB  MET A 105     7471   6206   7776   -802   -894    730       C
ATOM    850  CG  MET A 105     -69.003  62.269   0.634  1.00 66.54           C
ANISOU  850  CG  MET A 105     8946   7449   8887   -868   -761    828       C
ATOM    851  SD  MET A 105     -68.803  62.469   2.416  1.00 69.89           S
ANISOU  851  SD  MET A 105     9606   7825   9124   -916   -904    946       S
ATOM    852  CE  MET A 105     -70.506  62.498   2.954  1.00 62.19           C
ANISOU  852  CE  MET A 105     8648   6946   8035   -992   -933    859       C
ATOM    853  N   THR A 106     -66.821  64.790  -1.647  1.00 37.86           N
ANISOU  853  N   THR A 106     4919   3693   5771   -597   -995    759       N
ATOM    854  CA  THR A 106     -65.534  64.533  -2.278  1.00 34.82           C
ANISOU  854  CA  THR A 106     4532   3228   5470   -559   -934    799       C
ATOM    855  C   THR A 106     -64.670  65.775  -2.434  1.00 37.30           C
ANISOU  855  C   THR A 106     4788   3453   5932   -452  -1107    805       C
ATOM    856  O   THR A 106     -63.507  65.649  -2.833  1.00 35.73           O
ANISOU  856  O   THR A 106     4611   3166   5799   -426  -1075    846       O
ATOM    857  CB  THR A 106     -65.732  63.893  -3.660  1.00 33.21           C
ANISOU  857  CB  THR A 106     4199   3081   5340   -560   -756    704       C
ATOM    858  OG1 THR A 106     -66.523  64.759  -4.482  1.00 35.82           O
ANISOU  858  OG1 THR A 106     4350   3474   5786   -516   -794    577       O
ATOM    859  CG2 THR A 106     -66.427  62.551  -3.530  1.00 27.66           C
ANISOU  859  CG2 THR A 106     3576   2441   4493   -646   -585    707       C
ATOM    860  N   ASP A 107     -65.197  66.961  -2.137  1.00 41.21           N
ANISOU  860  N   ASP A 107     5206   3966   6486   -386  -1291    758       N
ATOM    861  CA  ASP A 107     -64.414  68.181  -2.280  1.00 37.88           C
ANISOU  861  CA  ASP A 107     4725   3454   6214   -259  -1470    754       C
ATOM    862  C   ASP A 107     -63.288  68.219  -1.258  1.00 38.94           C
ANISOU  862  C   ASP A 107     5088   3442   6267   -250  -1577    913       C
ATOM    863  O   ASP A 107     -63.516  68.048  -0.056  1.00 41.90           O
ANISOU  863  O   ASP A 107     5636   3806   6479   -301  -1648   1004       O
ATOM    864  CB  ASP A 107     -65.300  69.416  -2.116  1.00 37.58           C
ANISOU  864  CB  ASP A 107     4537   3482   6259   -184  -1655    655       C
ATOM    865  CG  ASP A 107     -65.972  69.829  -3.409  1.00 40.45           C
ANISOU  865  CG  ASP A 107     4642   3946   6782   -156  -1572    481       C
ATOM    866  OD1 ASP A 107     -65.689  69.209  -4.455  1.00 40.24           O
ANISOU  866  OD1 ASP A 107     4569   3923   6795   -182  -1389    446       O
ATOM    867  OD2 ASP A 107     -66.787  70.774  -3.375  1.00 43.78           O
ANISOU  867  OD2 ASP A 107     4906   4444   7284   -113  -1689    373       O
ATOM    868  N   ILE A 108     -62.063  68.436  -1.744  1.00 38.77           N
ANISOU  868  N   ILE A 108     5082   3300   6350   -194  -1582    944       N
ATOM    869  CA  ILE A 108     -60.958  68.807  -0.867  1.00 44.71           C
ANISOU  869  CA  ILE A 108     6046   3885   7058   -164  -1718   1083       C
ATOM    870  C   ILE A 108     -60.795  70.315  -0.780  1.00 46.72           C
ANISOU  870  C   ILE A 108     6242   4064   7445      1  -1977   1054       C
ATOM    871  O   ILE A 108     -60.099  70.804   0.123  1.00 44.41           O
ANISOU  871  O   ILE A 108     6148   3629   7096     46  -2145   1173       O
ATOM    872  CB  ILE A 108     -59.630  68.179  -1.334  1.00 46.41           C
ANISOU  872  CB  ILE A 108     6342   3987   7305   -210  -1582   1141       C
ATOM    873  CG1 ILE A 108     -59.305  68.620  -2.761  1.00 40.88           C
ANISOU  873  CG1 ILE A 108     5431   3284   6815   -123  -1547   1017       C
ATOM    874  CG2 ILE A 108     -59.692  66.663  -1.238  1.00 47.72           C
ANISOU  874  CG2 ILE A 108     6577   4222   7333   -365  -1347   1177       C
ATOM    875  CD1 ILE A 108     -57.974  68.119  -3.257  1.00 37.54           C
ANISOU  875  CD1 ILE A 108     5077   2747   6439   -164  -1438   1058       C
ATOM    876  N   ALA A 109     -61.419  71.066  -1.685  1.00 49.91           N
ANISOU  876  N   ALA A 109     6386   4556   8021     95  -2013    896       N
ATOM    877  CA  ALA A 109     -61.347  72.520  -1.693  1.00 50.86           C
ANISOU  877  CA  ALA A 109     6403   4626   8296    270  -2253    836       C
ATOM    878  C   ALA A 109     -62.507  73.050  -2.524  1.00 45.83           C
ANISOU  878  C   ALA A 109     5460   4158   7794    310  -2232    641       C
ATOM    879  O   ALA A 109     -63.166  72.306  -3.252  1.00 39.14           O
ANISOU  879  O   ALA A 109     4506   3433   6931    207  -2021    564       O
ATOM    880  CB  ALA A 109     -60.004  73.012  -2.244  1.00 41.51           C
ANISOU  880  CB  ALA A 109     5252   3269   7250    372  -2292    856       C
ATOM    881  N   LYS A 110     -62.749  74.355  -2.404  1.00 51.48           N
ANISOU  881  N   LYS A 110     6041   4876   8643    461  -2455    558       N
ATOM    882  CA  LYS A 110     -63.792  75.007  -3.186  1.00 56.34           C
ANISOU  882  CA  LYS A 110     6347   5650   9411    500  -2439    356       C
ATOM    883  C   LYS A 110     -63.247  75.635  -4.463  1.00 54.03           C
ANISOU  883  C   LYS A 110     5868   5323   9338    610  -2388    229       C
ATOM    884  O   LYS A 110     -63.905  75.582  -5.508  1.00 48.59           O
ANISOU  884  O   LYS A 110     4969   4759   8734    567  -2221     78       O
ATOM    885  CB  LYS A 110     -64.498  76.072  -2.344  1.00 68.23           C
ANISOU  885  CB  LYS A 110     7765   7211  10949    597  -2708    303       C
ATOM    886  CG  LYS A 110     -65.277  75.519  -1.161  1.00 78.01           C
ANISOU  886  CG  LYS A 110     9154   8516  11971    478  -2755    389       C
ATOM    887  CD  LYS A 110     -65.996  76.631  -0.412  1.00 89.95           C
ANISOU  887  CD  LYS A 110    10552  10095  13531    580  -3038    313       C
ATOM    888  CE  LYS A 110     -66.837  76.082   0.731  1.00 94.03           C
ANISOU  888  CE  LYS A 110    11216  10686  13825    451  -3082    382       C
ATOM    889  NZ  LYS A 110     -67.561  77.165   1.455  1.00 96.93           N
ANISOU  889  NZ  LYS A 110    11461  11130  14238    546  -3374    296       N
ATOM    890  N   LYS A 111     -62.061  76.230  -4.400  1.00 56.70           N
ANISOU  890  N   LYS A 111     6296   5486   9763    746  -2523    287       N
ATOM    891  CA  LYS A 111     -61.417  76.845  -5.548  1.00 55.91           C
ANISOU  891  CA  LYS A 111     6049   5327   9867    860  -2485    172       C
ATOM    892  C   LYS A 111     -60.002  76.308  -5.699  1.00 56.25           C
ANISOU  892  C   LYS A 111     6314   5182   9878    844  -2422    301       C
ATOM    893  O   LYS A 111     -59.379  75.903  -4.712  1.00 56.87           O
ANISOU  893  O   LYS A 111     6657   5137   9813    804  -2495    481       O
ATOM    894  CB  LYS A 111     -61.388  78.375  -5.412  1.00 57.74           C
ANISOU  894  CB  LYS A 111     6128   5522  10289   1080  -2744     69       C
ATOM    895  CG  LYS A 111     -62.636  79.053  -5.958  1.00 59.25           C
ANISOU  895  CG  LYS A 111     5982   5916  10614   1105  -2727   -152       C
ATOM    896  CD  LYS A 111     -62.637  80.547  -5.690  1.00 66.46           C
ANISOU  896  CD  LYS A 111     6781   6830  11642   1284  -2931   -265       C
ATOM    897  CE  LYS A 111     -62.901  80.846  -4.224  1.00 72.19           C
ANISOU  897  CE  LYS A 111     7643   7539  12245   1321  -3185   -158       C
ATOM    898  NZ  LYS A 111     -63.026  82.310  -3.971  1.00 76.32           N
ANISOU  898  NZ  LYS A 111     8047   8092  12858   1482  -3358   -287       N
ATOM    899  N   PRO A 112     -59.473  76.282  -6.927  1.00 56.93           N
ANISOU  899  N   PRO A 112     6303   5241  10086    861  -2278    208       N
ATOM    900  CA  PRO A 112     -58.148  75.673  -7.141  1.00 56.41           C
ANISOU  900  CA  PRO A 112     6435   5009   9990    818  -2197    315       C
ATOM    901  C   PRO A 112     -57.011  76.409  -6.456  1.00 62.10           C
ANISOU  901  C   PRO A 112     7344   5499  10753    946  -2412    421       C
ATOM    902  O   PRO A 112     -55.948  75.810  -6.251  1.00 66.07           O
ANISOU  902  O   PRO A 112     8070   5857  11176    871  -2358    550       O
ATOM    903  CB  PRO A 112     -57.985  75.707  -8.669  1.00 52.48           C
ANISOU  903  CB  PRO A 112     5756   4551   9633    832  -2028    154       C
ATOM    904  CG  PRO A 112     -59.372  75.876  -9.207  1.00 54.36           C
ANISOU  904  CG  PRO A 112     5745   5004   9905    810  -1945     -4       C
ATOM    905  CD  PRO A 112     -60.098  76.699  -8.192  1.00 55.89           C
ANISOU  905  CD  PRO A 112     5886   5241  10107    893  -2158     -4       C
ATOM    906  N   THR A 113     -57.192  77.677  -6.093  1.00 61.69           N
ANISOU  906  N   THR A 113     7219   5446  10773   1105  -2614    355       N
ATOM    907  CA  THR A 113     -56.127  78.461  -5.480  1.00 63.49           C
ANISOU  907  CA  THR A 113     7644   5518  10962   1196  -2762    425       C
ATOM    908  C   THR A 113     -55.877  78.103  -4.021  1.00 62.83           C
ANISOU  908  C   THR A 113     7856   5344  10670   1136  -2879    631       C
ATOM    909  O   THR A 113     -54.967  78.675  -3.412  1.00 68.98           O
ANISOU  909  O   THR A 113     8836   5983  11389   1199  -2994    708       O
ATOM    910  CB  THR A 113     -56.445  79.955  -5.586  1.00 67.34           C
ANISOU  910  CB  THR A 113     7952   6053  11580   1383  -2924    269       C
ATOM    911  OG1 THR A 113     -57.792  80.191  -5.158  1.00 67.10           O
ANISOU  911  OG1 THR A 113     7751   6188  11556   1400  -3014    205       O
ATOM    912  CG2 THR A 113     -56.275  80.434  -7.018  1.00 67.95           C
ANISOU  912  CG2 THR A 113     7809   6171  11837   1441  -2794     77       C
ATOM    913  N   GLU A 114     -56.648  77.184  -3.448  1.00 56.58           N
ANISOU  913  N   GLU A 114     7111   4627   9760   1015  -2845    720       N
ATOM    914  CA  GLU A 114     -56.466  76.832  -2.049  1.00 61.12           C
ANISOU  914  CA  GLU A 114     7978   5130  10114    943  -2938    907       C
ATOM    915  C   GLU A 114     -55.170  76.047  -1.849  1.00 63.18           C
ANISOU  915  C   GLU A 114     8516   5245  10246    813  -2795   1050       C
ATOM    916  O   GLU A 114     -54.573  75.521  -2.793  1.00 62.57           O
ANISOU  916  O   GLU A 114     8391   5143  10241    749  -2611   1012       O
ATOM    917  CB  GLU A 114     -57.668  76.038  -1.536  1.00 63.51           C
ANISOU  917  CB  GLU A 114     8255   5563  10314    837  -2921    953       C
ATOM    918  CG  GLU A 114     -58.821  76.923  -1.079  1.00 70.28           C
ANISOU  918  CG  GLU A 114     8946   6550  11206    948  -3131    861       C
ATOM    919  CD  GLU A 114     -60.093  76.146  -0.799  1.00 72.39           C
ANISOU  919  CD  GLU A 114     9138   7030  11335    790  -3008    832       C
ATOM    920  OE1 GLU A 114     -61.033  76.226  -1.618  1.00 71.36           O
ANISOU  920  OE1 GLU A 114     8724   7078  11312    778  -2906    662       O
ATOM    921  OE2 GLU A 114     -60.151  75.450   0.237  1.00 73.14           O
ANISOU  921  OE2 GLU A 114     9472   7110  11210    673  -3006    977       O
ATOM    922  N   THR A 115     -54.741  75.977  -0.587  1.00 64.39           N
ANISOU  922  N   THR A 115     8957   5310  10198    766  -2876   1204       N
ATOM    923  CA  THR A 115     -53.433  75.415  -0.263  1.00 63.57           C
ANISOU  923  CA  THR A 115     9122   5067   9965    649  -2749   1329       C
ATOM    924  C   THR A 115     -53.366  73.925  -0.576  1.00 63.57           C
ANISOU  924  C   THR A 115     9140   5119   9895    440  -2484   1372       C
ATOM    925  O   THR A 115     -52.339  73.433  -1.059  1.00 63.68           O
ANISOU  925  O   THR A 115     9214   5062   9918    355  -2320   1383       O
ATOM    926  CB  THR A 115     -53.113  75.667   1.211  1.00 65.96           C
ANISOU  926  CB  THR A 115     9727   5281  10054    640  -2882   1475       C
ATOM    927  OG1 THR A 115     -53.020  77.078   1.446  1.00 72.68           O
ANISOU  927  OG1 THR A 115    10567   6070  10979    844  -3128   1429       O
ATOM    928  CG2 THR A 115     -51.800  75.004   1.605  1.00 65.92           C
ANISOU  928  CG2 THR A 115     9997   5144   9906    494  -2720   1600       C
ATOM    929  N   ILE A 116     -54.453  73.193  -0.320  1.00 59.44           N
ANISOU  929  N   ILE A 116     8558   4722   9302    355  -2440   1389       N
ATOM    930  CA  ILE A 116     -54.441  71.744  -0.482  1.00 55.19           C
ANISOU  930  CA  ILE A 116     8049   4243   8677    156  -2189   1431       C
ATOM    931  C   ILE A 116     -54.206  71.336  -1.931  1.00 52.42           C
ANISOU  931  C   ILE A 116     7489   3925   8503    139  -2022   1314       C
ATOM    932  O   ILE A 116     -53.790  70.202  -2.194  1.00 51.83           O
ANISOU  932  O   ILE A 116     7444   3877   8373    -15  -1806   1335       O
ATOM    933  CB  ILE A 116     -55.757  71.145   0.061  1.00 52.90           C
ANISOU  933  CB  ILE A 116     7729   4092   8277     84  -2182   1455       C
ATOM    934  CG1 ILE A 116     -55.599  69.647   0.332  1.00 51.14           C
ANISOU  934  CG1 ILE A 116     7617   3923   7892   -129  -1928   1524       C
ATOM    935  CG2 ILE A 116     -56.904  71.398  -0.905  1.00 50.02           C
ANISOU  935  CG2 ILE A 116     7033   3925   8049    156  -2154   1271       C
ATOM    936  CD1 ILE A 116     -54.550  69.324   1.375  1.00 52.95           C
ANISOU  936  CD1 ILE A 116     8140   4050   7927   -230  -1872   1653       C
ATOM    937  N   CYS A 117     -54.443  72.237  -2.881  1.00 52.94           N
ANISOU  937  N   CYS A 117     7336   4000   8777    296  -2111   1179       N
ATOM    938  CA  CYS A 117     -54.278  71.934  -4.296  1.00 54.49           C
ANISOU  938  CA  CYS A 117     7333   4243   9129    288  -1956   1049       C
ATOM    939  C   CYS A 117     -52.857  72.155  -4.794  1.00 58.35           C
ANISOU  939  C   CYS A 117     7898   4605   9667    295  -1907   1035       C
ATOM    940  O   CYS A 117     -52.596  71.938  -5.982  1.00 58.94           O
ANISOU  940  O   CYS A 117     7826   4704   9863    290  -1789    926       O
ATOM    941  CB  CYS A 117     -55.243  72.781  -5.131  1.00 56.75           C
ANISOU  941  CB  CYS A 117     7331   4662   9569    430  -2014    870       C
ATOM    942  SG  CYS A 117     -56.967  72.662  -4.622  1.00 58.61           S
ANISOU  942  SG  CYS A 117     7437   5128   9703    404  -2029    827       S
ATOM    943  N   ALA A 118     -51.940  72.576  -3.925  1.00 59.65           N
ANISOU  943  N   ALA A 118     8295   4639   9730    302  -1989   1138       N
ATOM    944  CA  ALA A 118     -50.589  72.904  -4.377  1.00 55.22           C
ANISOU  944  CA  ALA A 118     7816   3945   9221    316  -1953   1121       C
ATOM    945  C   ALA A 118     -49.835  71.699  -4.930  1.00 52.15           C
ANISOU  945  C   ALA A 118     7448   3562   8803    140  -1718   1122       C
ATOM    946  O   ALA A 118     -49.315  71.796  -6.056  1.00 51.74           O
ANISOU  946  O   ALA A 118     7282   3493   8883    164  -1654   1014       O
ATOM    947  CB  ALA A 118     -49.819  73.586  -3.240  1.00 55.59           C
ANISOU  947  CB  ALA A 118     8130   3840   9152    356  -2086   1241       C
ATOM    948  N   PRO A 119     -49.729  70.561  -4.238  1.00 54.11           N
ANISOU  948  N   PRO A 119     7826   3844   8890    -36  -1581   1224       N
ATOM    949  CA  PRO A 119     -48.966  69.436  -4.793  1.00 58.12           C
ANISOU  949  CA  PRO A 119     8328   4369   9387   -196  -1363   1202       C
ATOM    950  C   PRO A 119     -49.678  68.683  -5.906  1.00 56.62           C
ANISOU  950  C   PRO A 119     7891   4333   9291   -225  -1247   1086       C
ATOM    951  O   PRO A 119     -49.117  67.712  -6.427  1.00 54.35           O
ANISOU  951  O   PRO A 119     7571   4081   8999   -348  -1079   1053       O
ATOM    952  CB  PRO A 119     -48.753  68.519  -3.572  1.00 62.79           C
ANISOU  952  CB  PRO A 119     9122   4963   9771   -363  -1255   1336       C
ATOM    953  CG  PRO A 119     -49.189  69.317  -2.375  1.00 63.64           C
ANISOU  953  CG  PRO A 119     9387   5021   9773   -281  -1434   1438       C
ATOM    954  CD  PRO A 119     -50.234  70.238  -2.892  1.00 57.23           C
ANISOU  954  CD  PRO A 119     8384   4264   9098   -101  -1612   1352       C
ATOM    955  N   LEU A 120     -50.884  69.095  -6.287  1.00 56.02           N
ANISOU  955  N   LEU A 120     7639   4348   9299   -116  -1330   1019       N
ATOM    956  CA  LEU A 120     -51.698  68.357  -7.242  1.00 48.81           C
ANISOU  956  CA  LEU A 120     6515   3578   8451   -146  -1213    920       C
ATOM    957  C   LEU A 120     -51.631  69.001  -8.619  1.00 41.42           C
ANISOU  957  C   LEU A 120     5395   2643   7700    -32  -1228    763       C
ATOM    958  O   LEU A 120     -51.556  70.226  -8.743  1.00 40.40           O
ANISOU  958  O   LEU A 120     5240   2444   7668    114  -1370    717       O
ATOM    959  CB  LEU A 120     -53.153  68.291  -6.775  1.00 45.33           C
ANISOU  959  CB  LEU A 120     6003   3277   7943   -123  -1246    927       C
ATOM    960  CG  LEU A 120     -53.406  67.621  -5.426  1.00 47.06           C
ANISOU  960  CG  LEU A 120     6400   3514   7968   -235  -1226   1069       C
ATOM    961  CD1 LEU A 120     -54.867  67.749  -5.042  1.00 46.52           C
ANISOU  961  CD1 LEU A 120     6247   3603   7825   -194  -1271   1043       C
ATOM    962  CD2 LEU A 120     -52.987  66.160  -5.467  1.00 47.41           C
ANISOU  962  CD2 LEU A 120     6477   3611   7925   -406  -1015   1095       C
ATOM    963  N   THR A 121     -51.665  68.162  -9.652  1.00 38.00           N
ANISOU  963  N   THR A 121     4835   2299   7306    -96  -1079    673       N
ATOM    964  CA  THR A 121     -51.729  68.624 -11.036  1.00 38.10           C
ANISOU  964  CA  THR A 121     4671   2345   7458     -5  -1061    510       C
ATOM    965  C   THR A 121     -53.199  68.809 -11.391  1.00 38.07           C
ANISOU  965  C   THR A 121     4497   2529   7439     60  -1046    421       C
ATOM    966  O   THR A 121     -53.903  67.846 -11.703  1.00 38.78           O
ANISOU  966  O   THR A 121     4521   2774   7440    -15   -918    394       O
ATOM    967  CB  THR A 121     -51.043  67.634 -11.972  1.00 38.12           C
ANISOU  967  CB  THR A 121     4636   2379   7470   -106   -912    448       C
ATOM    968  OG1 THR A 121     -49.667  67.494 -11.595  1.00 41.62           O
ANISOU  968  OG1 THR A 121     5231   2713   7870   -182   -900    511       O
ATOM    969  CG2 THR A 121     -51.121  68.121 -13.412  1.00 33.94           C
ANISOU  969  CG2 THR A 121     3948   1881   7066    -16   -894    277       C
ATOM    970  N   VAL A 122     -53.664  70.050 -11.335  1.00 38.06           N
ANISOU  970  N   VAL A 122     4426   2508   7527    199  -1179    370       N
ATOM    971  CA  VAL A 122     -55.065  70.382 -11.563  1.00 34.79           C
ANISOU  971  CA  VAL A 122     3849   2261   7109    250  -1174    280       C
ATOM    972  C   VAL A 122     -55.301  70.559 -13.055  1.00 35.91           C
ANISOU  972  C   VAL A 122     3817   2480   7346    291  -1074    105       C
ATOM    973  O   VAL A 122     -54.491  71.171 -13.758  1.00 38.78           O
ANISOU  973  O   VAL A 122     4156   2740   7839    364  -1102     29       O
ATOM    974  CB  VAL A 122     -55.453  71.653 -10.783  1.00 35.75           C
ANISOU  974  CB  VAL A 122     3955   2336   7291    379  -1369    291       C
ATOM    975  CG1 VAL A 122     -56.923  71.984 -10.988  1.00 35.21           C
ANISOU  975  CG1 VAL A 122     3704   2450   7223    409  -1354    186       C
ATOM    976  CG2 VAL A 122     -55.137  71.486  -9.305  1.00 36.54           C
ANISOU  976  CG2 VAL A 122     4267   2343   7274    338  -1476    472       C
ATOM    977  N   PHE A 123     -56.413  70.024 -13.547  1.00 35.32           N
ANISOU  977  N   PHE A 123     3640   2580   7200    241   -955     39       N
ATOM    978  CA  PHE A 123     -56.785  70.177 -14.947  1.00 36.31           C
ANISOU  978  CA  PHE A 123     3621   2789   7386    267   -850   -125       C
ATOM    979  C   PHE A 123     -57.648  71.423 -15.107  1.00 38.77           C
ANISOU  979  C   PHE A 123     3774   3156   7799    370   -909   -243       C
ATOM    980  O   PHE A 123     -58.679  71.560 -14.439  1.00 39.10           O
ANISOU  980  O   PHE A 123     3777   3291   7790    357   -940   -223       O
ATOM    981  CB  PHE A 123     -57.529  68.945 -15.452  1.00 35.57           C
ANISOU  981  CB  PHE A 123     3523   2840   7154    159   -687   -136       C
ATOM    982  CG  PHE A 123     -58.099  69.112 -16.827  1.00 37.84           C
ANISOU  982  CG  PHE A 123     3689   3218   7469    176   -576   -296       C
ATOM    983  CD1 PHE A 123     -57.272  69.118 -17.937  1.00 35.65           C
ANISOU  983  CD1 PHE A 123     3399   2890   7255    198   -530   -383       C
ATOM    984  CD2 PHE A 123     -59.462  69.265 -17.011  1.00 43.80           C
ANISOU  984  CD2 PHE A 123     4357   4106   8179    159   -512   -363       C
ATOM    985  CE1 PHE A 123     -57.793  69.273 -19.204  1.00 35.63           C
ANISOU  985  CE1 PHE A 123     3310   2969   7258    208   -422   -530       C
ATOM    986  CE2 PHE A 123     -59.990  69.419 -18.277  1.00 42.98           C
ANISOU  986  CE2 PHE A 123     4167   4080   8085    158   -393   -508       C
ATOM    987  CZ  PHE A 123     -59.153  69.423 -19.374  1.00 39.77           C
ANISOU  987  CZ  PHE A 123     3760   3623   7730    186   -348   -589       C
ATOM    988  N   PHE A 124     -57.230  72.322 -15.993  1.00 41.36           N
ANISOU  988  N   PHE A 124     4005   3434   8275    469   -921   -376       N
ATOM    989  CA  PHE A 124     -57.942  73.562 -16.260  1.00 37.77           C
ANISOU  989  CA  PHE A 124     3370   3035   7946    575   -965   -518       C
ATOM    990  C   PHE A 124     -58.476  73.558 -17.685  1.00 35.67           C
ANISOU  990  C   PHE A 124     2979   2880   7696    551   -791   -691       C
ATOM    991  O   PHE A 124     -57.829  73.040 -18.601  1.00 33.70           O
ANISOU  991  O   PHE A 124     2780   2596   7427    518   -696   -724       O
ATOM    992  CB  PHE A 124     -57.035  74.777 -16.047  1.00 39.45           C
ANISOU  992  CB  PHE A 124     3569   3088   8333    734  -1132   -548       C
ATOM    993  CG  PHE A 124     -56.510  74.906 -14.645  1.00 37.61           C
ANISOU  993  CG  PHE A 124     3486   2728   8077    768  -1317   -377       C
ATOM    994  CD1 PHE A 124     -57.226  75.599 -13.682  1.00 38.67           C
ANISOU  994  CD1 PHE A 124     3566   2900   8227    836  -1464   -354       C
ATOM    995  CD2 PHE A 124     -55.295  74.342 -14.293  1.00 41.82           C
ANISOU  995  CD2 PHE A 124     4221   3103   8566    724  -1343   -244       C
ATOM    996  CE1 PHE A 124     -56.742  75.721 -12.391  1.00 39.63           C
ANISOU  996  CE1 PHE A 124     3855   2897   8304    868  -1642   -193       C
ATOM    997  CE2 PHE A 124     -54.805  74.461 -13.006  1.00 38.51           C
ANISOU  997  CE2 PHE A 124     3970   2557   8107    742  -1499    -83       C
ATOM    998  CZ  PHE A 124     -55.529  75.151 -12.053  1.00 39.55           C
ANISOU  998  CZ  PHE A 124     4068   2721   8239    818  -1653    -52       C
ATOM    999  N   ASP A 125     -59.659  74.141 -17.865  1.00 38.34           N
ANISOU  999  N   ASP A 125     3157   3349   8063    558   -749   -804       N
ATOM   1000  CA  ASP A 125     -60.338  74.201 -19.156  1.00 41.62           C
ANISOU 1000  CA  ASP A 125     3461   3877   8475    517   -568   -971       C
ATOM   1001  C   ASP A 125     -60.434  75.662 -19.574  1.00 41.58           C
ANISOU 1001  C   ASP A 125     3258   3877   8665    644   -604  -1153       C
ATOM   1002  O   ASP A 125     -61.217  76.425 -19.000  1.00 46.55           O
ANISOU 1002  O   ASP A 125     3747   4576   9365    684   -674  -1203       O
ATOM   1003  CB  ASP A 125     -61.722  73.556 -19.072  1.00 44.49           C
ANISOU 1003  CB  ASP A 125     3813   4396   8695    388   -452   -962       C
ATOM   1004  CG  ASP A 125     -62.403  73.438 -20.427  1.00 43.90           C
ANISOU 1004  CG  ASP A 125     3682   4424   8576    319   -245  -1111       C
ATOM   1005  OD1 ASP A 125     -61.848  73.929 -21.432  1.00 45.63           O
ANISOU 1005  OD1 ASP A 125     3851   4606   8880    376   -191  -1235       O
ATOM   1006  OD2 ASP A 125     -63.500  72.845 -20.484  1.00 41.88           O
ANISOU 1006  OD2 ASP A 125     3448   4276   8191    204   -133  -1104       O
ATOM   1007  N   GLY A 126     -59.647  76.044 -20.582  1.00 43.25           N
ANISOU 1007  N   GLY A 126     3450   4018   8966    709   -554  -1265       N
ATOM   1008  CA  GLY A 126     -59.642  77.420 -21.049  1.00 43.60           C
ANISOU 1008  CA  GLY A 126     3355   4079   9132    802   -570  -1431       C
ATOM   1009  C   GLY A 126     -60.977  77.901 -21.577  1.00 46.08           C
ANISOU 1009  C   GLY A 126     3498   4568   9442    745   -431  -1591       C
ATOM   1010  O   GLY A 126     -61.198  79.114 -21.667  1.00 50.33           O
ANISOU 1010  O   GLY A 126     3910   5146  10067    810   -464  -1716       O
ATOM   1011  N   ARG A 127     -61.874  76.979 -21.929  1.00 46.86           N
ANISOU 1011  N   ARG A 127     3597   4772   9437    617   -269  -1592       N
ATOM   1012  CA  ARG A 127     -63.204  77.349 -22.395  1.00 46.99           C
ANISOU 1012  CA  ARG A 127     3480   4951   9423    527   -117  -1732       C
ATOM   1013  C   ARG A 127     -64.081  77.912 -21.286  1.00 50.31           C
ANISOU 1013  C   ARG A 127     3790   5448   9876    528   -229  -1717       C
ATOM   1014  O   ARG A 127     -65.125  78.501 -21.586  1.00 54.28           O
ANISOU 1014  O   ARG A 127     4168   6077  10377    465   -128  -1851       O
ATOM   1015  CB  ARG A 127     -63.883  76.136 -23.031  1.00 46.90           C
ANISOU 1015  CB  ARG A 127     3569   5014   9236    368     81  -1706       C
ATOM   1016  CG  ARG A 127     -63.082  75.509 -24.160  1.00 48.97           C
ANISOU 1016  CG  ARG A 127     3977   5212   9416    353    183  -1716       C
ATOM   1017  CD  ARG A 127     -63.689  74.192 -24.609  1.00 45.51           C
ANISOU 1017  CD  ARG A 127     3714   4832   8744    200    326  -1637       C
ATOM   1018  NE  ARG A 127     -63.674  73.192 -23.546  1.00 42.21           N
ANISOU 1018  NE  ARG A 127     3430   4389   8220    161    221  -1431       N
ATOM   1019  CZ  ARG A 127     -64.051  71.928 -23.708  1.00 39.34           C
ANISOU 1019  CZ  ARG A 127     3233   4054   7662     57    300  -1333       C
ATOM   1020  NH1 ARG A 127     -64.471  71.508 -24.893  1.00 37.03           N
ANISOU 1020  NH1 ARG A 127     3013   3807   7249    -17    472  -1410       N
ATOM   1021  NH2 ARG A 127     -64.005  71.083 -22.687  1.00 40.89           N
ANISOU 1021  NH2 ARG A 127     3532   4228   7778     32    208  -1160       N
ATOM   1022  N   VAL A 128     -63.689  77.748 -20.027  1.00 48.09           N
ANISOU 1022  N   VAL A 128     3562   5092   9616    591   -433  -1560       N
ATOM   1023  CA  VAL A 128     -64.421  78.291 -18.889  1.00 48.41           C
ANISOU 1023  CA  VAL A 128     3515   5195   9682    607   -574  -1538       C
ATOM   1024  C   VAL A 128     -63.750  79.586 -18.457  1.00 52.93           C
ANISOU 1024  C   VAL A 128     4037   5692  10382    774   -766  -1577       C
ATOM   1025  O   VAL A 128     -62.516  79.683 -18.441  1.00 55.82           O
ANISOU 1025  O   VAL A 128     4508   5909  10791    875   -864  -1513       O
ATOM   1026  CB  VAL A 128     -64.478  77.275 -17.732  1.00 46.04           C
ANISOU 1026  CB  VAL A 128     3339   4865   9290    557   -680  -1333       C
ATOM   1027  CG1 VAL A 128     -65.352  77.796 -16.603  1.00 48.98           C
ANISOU 1027  CG1 VAL A 128     3608   5316   9685    560   -821  -1328       C
ATOM   1028  CG2 VAL A 128     -64.983  75.931 -18.232  1.00 45.42           C
ANISOU 1028  CG2 VAL A 128     3415   4841   9000    378   -479  -1266       C
ATOM   1029  N   ASP A 129     -64.561  80.584 -18.111  1.00 54.67           N
ANISOU 1029  N   ASP A 129     4101   6012  10657    799   -818  -1685       N
ATOM   1030  CA  ASP A 129     -64.037  81.899 -17.764  1.00 59.54           C
ANISOU 1030  CA  ASP A 129     4649   6575  11399    964   -994  -1746       C
ATOM   1031  C   ASP A 129     -63.115  81.818 -16.554  1.00 57.40           C
ANISOU 1031  C   ASP A 129     4525   6153  11132   1076  -1247  -1559       C
ATOM   1032  O   ASP A 129     -63.440  81.178 -15.550  1.00 53.40           O
ANISOU 1032  O   ASP A 129     4088   5651  10553   1032  -1342  -1419       O
ATOM   1033  CB  ASP A 129     -65.185  82.869 -17.481  1.00 70.18           C
ANISOU 1033  CB  ASP A 129     5797   8071  12798    962  -1014  -1888       C
ATOM   1034  CG  ASP A 129     -65.983  83.210 -18.724  1.00 79.00           C
ANISOU 1034  CG  ASP A 129     6773   9319  13925    864   -767  -2092       C
ATOM   1035  OD1 ASP A 129     -65.422  83.116 -19.836  1.00 81.89           O
ANISOU 1035  OD1 ASP A 129     7176   9642  14297    857   -626  -2154       O
ATOM   1036  OD2 ASP A 129     -67.170  83.577 -18.589  1.00 83.11           O
ANISOU 1036  OD2 ASP A 129     7153   9984  14442    786   -712  -2193       O
ATOM   1037  N   GLY A 130     -61.956  82.469 -16.660  1.00 60.54           N
ANISOU 1037  N   GLY A 130     4984   6413  11606   1212  -1352  -1557       N
ATOM   1038  CA  GLY A 130     -61.023  82.575 -15.559  1.00 57.21           C
ANISOU 1038  CA  GLY A 130     4722   5833  11183   1322  -1590  -1391       C
ATOM   1039  C   GLY A 130     -60.126  81.378 -15.338  1.00 51.23           C
ANISOU 1039  C   GLY A 130     4192   4936  10336   1268  -1589  -1198       C
ATOM   1040  O   GLY A 130     -59.209  81.462 -14.512  1.00 56.98           O
ANISOU 1040  O   GLY A 130     5089   5512  11051   1346  -1764  -1056       O
ATOM   1041  N   GLN A 131     -60.348  80.267 -16.042  1.00 45.13           N
ANISOU 1041  N   GLN A 131     3442   4209   9497   1136  -1394  -1186       N
ATOM   1042  CA  GLN A 131     -59.525  79.084 -15.821  1.00 42.69           C
ANISOU 1042  CA  GLN A 131     3339   3775   9108   1080  -1388  -1008       C
ATOM   1043  C   GLN A 131     -58.137  79.226 -16.430  1.00 49.19           C
ANISOU 1043  C   GLN A 131     4281   4446   9963   1131  -1381  -1005       C
ATOM   1044  O   GLN A 131     -57.188  78.599 -15.946  1.00 47.15           O
ANISOU 1044  O   GLN A 131     4220   4045   9651   1114  -1442   -846       O
ATOM   1045  CB  GLN A 131     -60.225  77.848 -16.380  1.00 41.59           C
ANISOU 1045  CB  GLN A 131     3180   3735   8888    933  -1188  -1004       C
ATOM   1046  CG  GLN A 131     -61.554  77.554 -15.712  1.00 48.84           C
ANISOU 1046  CG  GLN A 131     4022   4802   9732    845  -1183   -983       C
ATOM   1047  CD  GLN A 131     -61.569  76.214 -15.005  1.00 52.77           C
ANISOU 1047  CD  GLN A 131     4741   5292  10018    704  -1155   -781       C
ATOM   1048  OE1 GLN A 131     -61.129  75.204 -15.553  1.00 46.60           O
ANISOU 1048  OE1 GLN A 131     4089   4484   9134    615  -1021   -724       O
ATOM   1049  NE2 GLN A 131     -62.075  76.201 -13.778  1.00 58.16           N
ANISOU 1049  NE2 GLN A 131     5464   6000  10635    689  -1287   -682       N
ATOM   1050  N   VAL A 132     -57.997  80.032 -17.483  1.00 49.88           N
ANISOU 1050  N   VAL A 132     4259   4563  10130   1180  -1300  -1181       N
ATOM   1051  CA  VAL A 132     -56.672  80.319 -18.023  1.00 47.92           C
ANISOU 1051  CA  VAL A 132     4116   4173   9919   1238  -1313  -1189       C
ATOM   1052  C   VAL A 132     -55.845  81.093 -17.005  1.00 51.68           C
ANISOU 1052  C   VAL A 132     4702   4503  10430   1365  -1539  -1094       C
ATOM   1053  O   VAL A 132     -54.677  80.774 -16.755  1.00 56.10           O
ANISOU 1053  O   VAL A 132     5455   4903  10956   1367  -1595   -973       O
ATOM   1054  CB  VAL A 132     -56.786  81.083 -19.354  1.00 46.59           C
ANISOU 1054  CB  VAL A 132     3800   4075   9826   1268  -1180  -1407       C
ATOM   1055  CG1 VAL A 132     -55.407  81.485 -19.855  1.00 47.23           C
ANISOU 1055  CG1 VAL A 132     3986   4006   9952   1340  -1211  -1421       C
ATOM   1056  CG2 VAL A 132     -57.506  80.240 -20.390  1.00 44.30           C
ANISOU 1056  CG2 VAL A 132     3449   3910   9471   1133   -949  -1487       C
ATOM   1057  N   ASP A 133     -56.444  82.119 -16.395  1.00 49.58           N
ANISOU 1057  N   ASP A 133     4322   4291  10225   1467  -1670  -1148       N
ATOM   1058  CA  ASP A 133     -55.728  82.903 -15.395  1.00 56.39           C
ANISOU 1058  CA  ASP A 133     5299   5017  11110   1600  -1898  -1059       C
ATOM   1059  C   ASP A 133     -55.446  82.078 -14.146  1.00 53.71           C
ANISOU 1059  C   ASP A 133     5173   4584  10652   1548  -2014   -828       C
ATOM   1060  O   ASP A 133     -54.387  82.227 -13.524  1.00 55.05           O
ANISOU 1060  O   ASP A 133     5545   4583  10790   1600  -2139   -704       O
ATOM   1061  CB  ASP A 133     -56.526  84.159 -15.048  1.00 69.60           C
ANISOU 1061  CB  ASP A 133     6787   6787  12872   1721  -2014  -1183       C
ATOM   1062  CG  ASP A 133     -55.783  85.076 -14.098  1.00 84.43           C
ANISOU 1062  CG  ASP A 133     8781   8522  14777   1881  -2256  -1110       C
ATOM   1063  OD1 ASP A 133     -54.759  85.661 -14.512  1.00 89.63           O
ANISOU 1063  OD1 ASP A 133     9507   9054  15493   1975  -2282  -1141       O
ATOM   1064  OD2 ASP A 133     -56.222  85.211 -12.937  1.00 89.24           O
ANISOU 1064  OD2 ASP A 133     9424   9142  15342   1915  -2423  -1020       O
ATOM   1065  N   LEU A 134     -56.382  81.205 -13.760  1.00 56.09           N
ANISOU 1065  N   LEU A 134     5443   4990  10879   1438  -1964   -768       N
ATOM   1066  CA  LEU A 134     -56.133  80.300 -12.642  1.00 56.89           C
ANISOU 1066  CA  LEU A 134     5754   5005  10855   1368  -2046   -549       C
ATOM   1067  C   LEU A 134     -54.964  79.369 -12.930  1.00 54.91           C
ANISOU 1067  C   LEU A 134     5706   4616  10541   1279  -1955   -437       C
ATOM   1068  O   LEU A 134     -54.213  79.013 -12.015  1.00 54.15           O
ANISOU 1068  O   LEU A 134     5839   4385  10352   1253  -2045   -260       O
ATOM   1069  CB  LEU A 134     -57.390  79.486 -12.329  1.00 54.58           C
ANISOU 1069  CB  LEU A 134     5376   4859  10504   1263  -1986   -523       C
ATOM   1070  CG  LEU A 134     -58.527  80.199 -11.592  1.00 56.17           C
ANISOU 1070  CG  LEU A 134     5434   5184  10722   1318  -2116   -575       C
ATOM   1071  CD1 LEU A 134     -59.743  79.292 -11.492  1.00 52.70           C
ANISOU 1071  CD1 LEU A 134     4903   4897  10224   1190  -2017   -565       C
ATOM   1072  CD2 LEU A 134     -58.071  80.639 -10.213  1.00 58.66           C
ANISOU 1072  CD2 LEU A 134     5929   5382  10977   1401  -2362   -427       C
ATOM   1073  N   PHE A 135     -54.795  78.970 -14.192  1.00 50.60           N
ANISOU 1073  N   PHE A 135     5087   4108  10031   1221  -1770   -542       N
ATOM   1074  CA  PHE A 135     -53.674  78.113 -14.554  1.00 47.37           C
ANISOU 1074  CA  PHE A 135     4850   3583   9566   1131  -1681   -461       C
ATOM   1075  C   PHE A 135     -52.346  78.850 -14.440  1.00 48.54           C
ANISOU 1075  C   PHE A 135     5142   3560   9742   1215  -1781   -434       C
ATOM   1076  O   PHE A 135     -51.328  78.241 -14.093  1.00 53.06           O
ANISOU 1076  O   PHE A 135     5923   4001  10238   1141  -1778   -302       O
ATOM   1077  CB  PHE A 135     -53.870  77.569 -15.969  1.00 48.88           C
ANISOU 1077  CB  PHE A 135     4924   3866   9782   1059  -1473   -596       C
ATOM   1078  CG  PHE A 135     -52.675  76.843 -16.513  1.00 50.33           C
ANISOU 1078  CG  PHE A 135     5254   3944   9924    978  -1389   -553       C
ATOM   1079  CD1 PHE A 135     -52.361  75.568 -16.074  1.00 47.67           C
ANISOU 1079  CD1 PHE A 135     5062   3570   9480    843  -1340   -406       C
ATOM   1080  CD2 PHE A 135     -51.868  77.432 -17.473  1.00 51.53           C
ANISOU 1080  CD2 PHE A 135     5392   4042  10144   1029  -1354   -670       C
ATOM   1081  CE1 PHE A 135     -51.262  74.897 -16.577  1.00 47.69           C
ANISOU 1081  CE1 PHE A 135     5181   3495   9446    756  -1261   -383       C
ATOM   1082  CE2 PHE A 135     -50.769  76.766 -17.980  1.00 50.16           C
ANISOU 1082  CE2 PHE A 135     5346   3780   9933    948  -1283   -641       C
ATOM   1083  CZ  PHE A 135     -50.467  75.495 -17.533  1.00 48.25           C
ANISOU 1083  CZ  PHE A 135     5235   3512   9586    808  -1237   -500       C
ATOM   1084  N  AARG A 136     -52.334  80.153 -14.735  0.49 49.82           N
ANISOU 1084  N  AARG A 136     5198   3721  10012   1362  -1858   -563       N
ATOM   1085  N  BARG A 136     -52.337  80.157 -14.718  0.51 49.88           N
ANISOU 1085  N  BARG A 136     5206   3728  10019   1363  -1861   -562       N
ATOM   1086  CA AARG A 136     -51.101  80.924 -14.618  0.49 50.27           C
ANISOU 1086  CA AARG A 136     5396   3604  10101   1460  -1960   -541       C
ATOM   1087  CA BARG A 136     -51.099  80.922 -14.621  0.51 50.24           C
ANISOU 1087  CA BARG A 136     5393   3600  10098   1460  -1959   -542       C
ATOM   1088  C  AARG A 136     -50.621  80.996 -13.175  0.49 51.88           C
ANISOU 1088  C  AARG A 136     5822   3672  10216   1484  -2134   -349       C
ATOM   1089  C  BARG A 136     -50.626  81.050 -13.179  0.51 51.94           C
ANISOU 1089  C  BARG A 136     5826   3680  10228   1491  -2139   -354       C
ATOM   1090  O  AARG A 136     -49.412  81.045 -12.925  0.49 53.36           O
ANISOU 1090  O  AARG A 136     6221   3685  10368   1486  -2173   -259       O
ATOM   1091  O  BARG A 136     -49.422  81.187 -12.935  0.51 53.48           O
ANISOU 1091  O  BARG A 136     6226   3700  10395   1505  -2185   -271       O
ATOM   1092  CB AARG A 136     -51.302  82.335 -15.170  0.49 53.11           C
ANISOU 1092  CB AARG A 136     5584   3999  10597   1625  -2012   -724       C
ATOM   1093  CB BARG A 136     -51.284  82.307 -15.238  0.51 52.26           C
ANISOU 1093  CB BARG A 136     5473   3892  10490   1620  -2002   -729       C
ATOM   1094  CG AARG A 136     -51.699  82.406 -16.634  0.49 51.60           C
ANISOU 1094  CG AARG A 136     5192   3931  10482   1602  -1831   -925       C
ATOM   1095  CG BARG A 136     -51.814  82.292 -16.659  0.51 55.71           C
ANISOU 1095  CG BARG A 136     5702   4470  10997   1587  -1816   -925       C
ATOM   1096  CD AARG A 136     -51.737  83.855 -17.096  0.49 61.64           C
ANISOU 1096  CD AARG A 136     6320   5216  11886   1766  -1885  -1098       C
ATOM   1097  CD BARG A 136     -51.789  83.684 -17.261  0.51 61.20           C
ANISOU 1097  CD BARG A 136     6254   5177  11823   1741  -1849  -1106       C
ATOM   1098  NE AARG A 136     -52.265  84.005 -18.449  0.49 61.82           N
ANISOU 1098  NE AARG A 136     6145   5374  11970   1739  -1704  -1299       N
ATOM   1099  NE BARG A 136     -50.827  83.784 -18.353  0.51 62.56           N
ANISOU 1099  NE BARG A 136     6468   5268  12033   1745  -1749  -1190       N
ATOM   1100  CZ AARG A 136     -51.522  83.980 -19.550  0.49 62.63           C
ANISOU 1100  CZ AARG A 136     6273   5427  12096   1724  -1588  -1384       C
ATOM   1101  CZ BARG A 136     -51.161  83.854 -19.637  0.51 62.60           C
ANISOU 1101  CZ BARG A 136     6322   5380  12083   1715  -1582  -1365       C
ATOM   1102  NH1AARG A 136     -52.091  84.131 -20.738  0.49 62.54           N
ANISOU 1102  NH1AARG A 136     6093   5546  12123   1694  -1422  -1566       N
ATOM   1103  NH1BARG A 136     -50.217  83.939 -20.564  0.51 62.51           N
ANISOU 1103  NH1BARG A 136     6373   5283  12097   1720  -1508  -1433       N
ATOM   1104  NH2AARG A 136     -50.210  83.802 -19.466  0.49 62.38           N
ANISOU 1104  NH2AARG A 136     6446   5214  12042   1731  -1634  -1291       N
ATOM   1105  NH2BARG A 136     -52.438  83.850 -19.995  0.51 61.51           N
ANISOU 1105  NH2BARG A 136     5984   5431  11957   1674  -1485  -1475       N
ATOM   1106  N   ASN A 137     -51.547  81.007 -12.219  1.00 53.23           N
ANISOU 1106  N   ASN A 137     5964   3919  10341   1495  -2236   -286       N
ATOM   1107  CA  ASN A 137     -51.213  81.120 -10.807  1.00 60.73           C
ANISOU 1107  CA  ASN A 137     7132   4755  11187   1519  -2409   -108       C
ATOM   1108  C   ASN A 137     -51.122  79.773 -10.107  1.00 59.09           C
ANISOU 1108  C   ASN A 137     7106   4524  10821   1343  -2345     76       C
ATOM   1109  O   ASN A 137     -50.873  79.734  -8.899  1.00 61.56           O
ANISOU 1109  O   ASN A 137     7624   4749  11018   1334  -2465    234       O
ATOM   1110  CB  ASN A 137     -52.245  82.001 -10.095  1.00 69.18           C
ANISOU 1110  CB  ASN A 137     8077   5919  12288   1641  -2581   -151       C
ATOM   1111  CG  ASN A 137     -52.326  83.394 -10.686  1.00 74.71           C
ANISOU 1111  CG  ASN A 137     8596   6647  13145   1819  -2649   -337       C
ATOM   1112  OD1 ASN A 137     -51.583  84.292 -10.291  1.00 81.65           O
ANISOU 1112  OD1 ASN A 137     9586   7390  14045   1951  -2796   -315       O
ATOM   1113  ND2 ASN A 137     -53.231  83.582 -11.640  1.00 71.12           N
ANISOU 1113  ND2 ASN A 137     7865   6363  12792   1819  -2534   -523       N
ATOM   1114  N   ALA A 138     -51.321  78.674 -10.826  1.00 56.28           N
ANISOU 1114  N   ALA A 138     6687   4246  10451   1202  -2156     56       N
ATOM   1115  CA  ALA A 138     -51.250  77.346 -10.239  1.00 61.86           C
ANISOU 1115  CA  ALA A 138     7548   4944  11015   1028  -2073    214       C
ATOM   1116  C   ALA A 138     -49.822  76.820 -10.281  1.00 59.06           C
ANISOU 1116  C   ALA A 138     7410   4437  10594    930  -1996    303       C
ATOM   1117  O   ALA A 138     -49.065  77.090 -11.218  1.00 57.32           O
ANISOU 1117  O   ALA A 138     7163   4162  10455    956  -1936    209       O
ATOM   1118  CB  ALA A 138     -52.184  76.380 -10.970  1.00 68.09           C
ANISOU 1118  CB  ALA A 138     8164   5891  11817    926  -1907    147       C
ATOM   1119  N   ARG A 139     -49.458  76.062  -9.246  1.00 57.59           N
ANISOU 1119  N   ARG A 139     7442   4186  10252    809  -1990    480       N
ATOM   1120  CA  ARG A 139     -48.119  75.483  -9.184  1.00 55.77           C
ANISOU 1120  CA  ARG A 139     7421   3822   9947    688  -1897    564       C
ATOM   1121  C   ARG A 139     -47.964  74.360 -10.205  1.00 52.15           C
ANISOU 1121  C   ARG A 139     6868   3441   9507    547  -1694    500       C
ATOM   1122  O   ARG A 139     -47.077  74.401 -11.065  1.00 48.84           O
ANISOU 1122  O   ARG A 139     6449   2959   9150    535  -1625    425       O
ATOM   1123  CB  ARG A 139     -47.833  74.979  -7.767  1.00 61.16           C
ANISOU 1123  CB  ARG A 139     8359   4433  10448    584  -1922    759       C
ATOM   1124  CG  ARG A 139     -46.402  74.521  -7.552  1.00 71.13           C
ANISOU 1124  CG  ARG A 139     9854   5543  11630    459  -1827    846       C
ATOM   1125  CD  ARG A 139     -45.931  74.792  -6.132  1.00 80.65           C
ANISOU 1125  CD  ARG A 139    11339   6617  12686    448  -1921   1012       C
ATOM   1126  NE  ARG A 139     -46.367  73.769  -5.186  1.00 82.60           N
ANISOU 1126  NE  ARG A 139    11682   6936  12766    295  -1847   1134       N
ATOM   1127  CZ  ARG A 139     -46.167  73.838  -3.874  1.00 86.88           C
ANISOU 1127  CZ  ARG A 139    12462   7401  13149    262  -1909   1282       C
ATOM   1128  NH1 ARG A 139     -45.544  74.886  -3.351  1.00 88.64           N
ANISOU 1128  NH1 ARG A 139    12852   7464  13362    377  -2058   1331       N
ATOM   1129  NH2 ARG A 139     -46.592  72.862  -3.083  1.00 87.60           N
ANISOU 1129  NH2 ARG A 139    12627   7571  13085    116  -1819   1376       N
ATOM   1130  N   ASN A 140     -48.824  73.349 -10.125  1.00 50.83           N
ANISOU 1130  N   ASN A 140     6623   3409   9281    443  -1601    524       N
ATOM   1131  CA  ASN A 140     -48.852  72.250 -11.079  1.00 47.02           C
ANISOU 1131  CA  ASN A 140     6033   3023   8810    323  -1421    456       C
ATOM   1132  C   ASN A 140     -50.235  72.191 -11.710  1.00 47.72           C
ANISOU 1132  C   ASN A 140     5891   3273   8966    374  -1393    350       C
ATOM   1133  O   ASN A 140     -51.243  72.194 -10.997  1.00 49.82           O
ANISOU 1133  O   ASN A 140     6133   3603   9194    392  -1451    402       O
ATOM   1134  CB  ASN A 140     -48.520  70.919 -10.400  1.00 47.33           C
ANISOU 1134  CB  ASN A 140     6209   3074   8699    130  -1304    583       C
ATOM   1135  CG  ASN A 140     -47.341  71.027  -9.456  1.00 50.76           C
ANISOU 1135  CG  ASN A 140     6900   3348   9039     70  -1332    709       C
ATOM   1136  OD1 ASN A 140     -46.186  70.958  -9.875  1.00 54.95           O
ANISOU 1136  OD1 ASN A 140     7506   3781   9591     18  -1274    686       O
ATOM   1137  ND2 ASN A 140     -47.628  71.195  -8.170  1.00 50.72           N
ANISOU 1137  ND2 ASN A 140     7042   3310   8921     71  -1417    841       N
ATOM   1138  N   GLY A 141     -50.284  72.142 -13.036  1.00 38.62           N
ANISOU 1138  N   GLY A 141     4584   2183   7908    392  -1301    199       N
ATOM   1139  CA  GLY A 141     -51.564  72.140 -13.715  1.00 37.31           C
ANISOU 1139  CA  GLY A 141     4214   2161   7803    438  -1253     84       C
ATOM   1140  C   GLY A 141     -51.430  71.815 -15.184  1.00 40.18           C
ANISOU 1140  C   GLY A 141     4460   2585   8222    418  -1119    -66       C
ATOM   1141  O   GLY A 141     -50.343  71.895 -15.767  1.00 40.92           O
ANISOU 1141  O   GLY A 141     4603   2604   8339    406  -1096   -106       O
ATOM   1142  N   VAL A 142     -52.565  71.445 -15.776  1.00 36.75           N
ANISOU 1142  N   VAL A 142     3883   2302   7778    408  -1027   -148       N
ATOM   1143  CA  VAL A 142     -52.682  71.177 -17.204  1.00 38.75           C
ANISOU 1143  CA  VAL A 142     4028   2643   8051    394   -897   -300       C
ATOM   1144  C   VAL A 142     -53.848  71.993 -17.742  1.00 37.44           C
ANISOU 1144  C   VAL A 142     3688   2601   7935    485   -877   -436       C
ATOM   1145  O   VAL A 142     -54.936  71.989 -17.156  1.00 35.24           O
ANISOU 1145  O   VAL A 142     3359   2436   7594    475   -884   -403       O
ATOM   1146  CB  VAL A 142     -52.889  69.677 -17.492  1.00 41.45           C
ANISOU 1146  CB  VAL A 142     4396   3108   8246    250   -759   -264       C
ATOM   1147  CG1 VAL A 142     -53.199  69.455 -18.965  1.00 41.07           C
ANISOU 1147  CG1 VAL A 142     4248   3161   8195    250   -641   -420       C
ATOM   1148  CG2 VAL A 142     -51.658  68.884 -17.079  1.00 40.29           C
ANISOU 1148  CG2 VAL A 142     4388   2848   8072    151   -760   -162       C
ATOM   1149  N   LEU A 143     -53.622  72.692 -18.852  1.00 37.79           N
ANISOU 1149  N   LEU A 143     3641   2624   8092    563   -845   -598       N
ATOM   1150  CA  LEU A 143     -54.614  73.578 -19.442  1.00 38.60           C
ANISOU 1150  CA  LEU A 143     3567   2835   8263    645   -809   -753       C
ATOM   1151  C   LEU A 143     -54.890  73.172 -20.882  1.00 40.03           C
ANISOU 1151  C   LEU A 143     3690   3118   8400    594   -638   -894       C
ATOM   1152  O   LEU A 143     -53.972  72.800 -21.619  1.00 42.15           O
ANISOU 1152  O   LEU A 143     4026   3316   8672    569   -599   -929       O
ATOM   1153  CB  LEU A 143     -54.142  75.037 -19.393  1.00 40.75           C
ANISOU 1153  CB  LEU A 143     3789   3035   8659    781   -924   -826       C
ATOM   1154  CG  LEU A 143     -55.027  76.084 -20.074  1.00 44.33           C
ANISOU 1154  CG  LEU A 143     4047   3607   9189    857   -877  -1011       C
ATOM   1155  CD1 LEU A 143     -56.390  76.166 -19.402  1.00 45.51           C
ANISOU 1155  CD1 LEU A 143     4080   3878   9334    857   -892  -1002       C
ATOM   1156  CD2 LEU A 143     -54.346  77.444 -20.083  1.00 46.03           C
ANISOU 1156  CD2 LEU A 143     4241   3745   9505    983   -988  -1079       C
ATOM   1157  N   ILE A 144     -56.159  73.242 -21.279  1.00 42.12           N
ANISOU 1157  N   ILE A 144     3842   3546   8616    571   -537   -977       N
ATOM   1158  CA  ILE A 144     -56.568  73.035 -22.661  1.00 40.38           C
ANISOU 1158  CA  ILE A 144     3575   3422   8345    530   -372  -1122       C
ATOM   1159  C   ILE A 144     -57.316  74.274 -23.133  1.00 38.95           C
ANISOU 1159  C   ILE A 144     3216   3306   8278    610   -329  -1298       C
ATOM   1160  O   ILE A 144     -58.073  74.883 -22.369  1.00 37.12           O
ANISOU 1160  O   ILE A 144     2881   3126   8097    645   -388  -1292       O
ATOM   1161  CB  ILE A 144     -57.440  71.772 -22.833  1.00 36.97           C
ANISOU 1161  CB  ILE A 144     3205   3126   7716    397   -254  -1061       C
ATOM   1162  CG1 ILE A 144     -58.744  71.894 -22.041  1.00 38.79           C
ANISOU 1162  CG1 ILE A 144     3370   3466   7901    367   -250  -1020       C
ATOM   1163  CG2 ILE A 144     -56.670  70.532 -22.407  1.00 32.65           C
ANISOU 1163  CG2 ILE A 144     2806   2527   7073    326   -290   -910       C
ATOM   1164  CD1 ILE A 144     -59.815  70.922 -22.483  1.00 33.71           C
ANISOU 1164  CD1 ILE A 144     2771   2956   7079    252   -106  -1013       C
ATOM   1165  N   THR A 145     -57.083  74.659 -24.386  1.00 39.79           N
ANISOU 1165  N   THR A 145     3281   3413   8426    636   -226  -1464       N
ATOM   1166  CA  THR A 145     -57.766  75.793 -24.991  1.00 43.67           C
ANISOU 1166  CA  THR A 145     3619   4000   8974    670   -151  -1637       C
ATOM   1167  C   THR A 145     -58.092  75.470 -26.441  1.00 45.26           C
ANISOU 1167  C   THR A 145     3833   4278   9087    600     49  -1776       C
ATOM   1168  O   THR A 145     -57.542  74.538 -27.033  1.00 41.91           O
ANISOU 1168  O   THR A 145     3540   3812   8574    554     94  -1751       O
ATOM   1169  CB  THR A 145     -56.927  77.082 -24.940  1.00 46.65           C
ANISOU 1169  CB  THR A 145     3955   4296   9474    783   -266  -1693       C
ATOM   1170  OG1 THR A 145     -55.656  76.852 -25.558  1.00 52.55           O
ANISOU 1170  OG1 THR A 145     4823   4932  10210    791   -276  -1692       O
ATOM   1171  CG2 THR A 145     -56.721  77.552 -23.507  1.00 40.14           C
ANISOU 1171  CG2 THR A 145     3128   3399   8723    861   -468  -1568       C
ATOM   1172  N   GLU A 146     -59.002  76.259 -27.008  1.00 52.86           N
ANISOU 1172  N   GLU A 146     4665   5356  10063    586    167  -1928       N
ATOM   1173  CA  GLU A 146     -59.312  76.177 -28.428  1.00 54.13           C
ANISOU 1173  CA  GLU A 146     4846   5586  10134    520    364  -2076       C
ATOM   1174  C   GLU A 146     -58.449  77.103 -29.271  1.00 55.65           C
ANISOU 1174  C   GLU A 146     5023   5730  10391    584    365  -2200       C
ATOM   1175  O   GLU A 146     -58.274  76.848 -30.468  1.00 58.96           O
ANISOU 1175  O   GLU A 146     5518   6165  10720    538    494  -2293       O
ATOM   1176  CB  GLU A 146     -60.787  76.509 -28.673  1.00 56.56           C
ANISOU 1176  CB  GLU A 146     5038   6047  10404    439    524  -2181       C
ATOM   1177  CG  GLU A 146     -61.769  75.641 -27.907  1.00 59.69           C
ANISOU 1177  CG  GLU A 146     5450   6510  10718    358    544  -2068       C
ATOM   1178  CD  GLU A 146     -63.212  76.011 -28.197  1.00 67.36           C
ANISOU 1178  CD  GLU A 146     6312   7630  11652    256    718  -2183       C
ATOM   1179  OE1 GLU A 146     -63.441  76.885 -29.060  1.00 71.79           O
ANISOU 1179  OE1 GLU A 146     6805   8244  12230    237    828  -2345       O
ATOM   1180  OE2 GLU A 146     -64.118  75.431 -27.563  1.00 67.27           O
ANISOU 1180  OE2 GLU A 146     6336   7686  11535    159    725  -2078       O
ATOM   1181  N   GLY A 147     -57.908  78.164 -28.678  1.00 52.74           N
ANISOU 1181  N   GLY A 147     4572   5299  10168    694    221  -2204       N
ATOM   1182  CA  GLY A 147     -57.087  79.108 -29.407  1.00 54.86           C
ANISOU 1182  CA  GLY A 147     4820   5514  10509    769    216  -2324       C
ATOM   1183  C   GLY A 147     -55.786  79.439 -28.706  1.00 55.72           C
ANISOU 1183  C   GLY A 147     4991   5464  10715    878     16  -2228       C
ATOM   1184  O   GLY A 147     -55.340  78.698 -27.824  1.00 54.23           O
ANISOU 1184  O   GLY A 147     4901   5196  10508    871   -101  -2060       O
ATOM   1185  N   SER A 148     -55.175  80.557 -29.084  1.00 58.36           N
ANISOU 1185  N   SER A 148     5276   5749  11150    975    -16  -2336       N
ATOM   1186  CA  SER A 148     -53.864  80.916 -28.568  1.00 61.50           C
ANISOU 1186  CA  SER A 148     5759   5981  11628   1076   -187  -2259       C
ATOM   1187  C   SER A 148     -53.961  81.483 -27.159  1.00 63.30           C
ANISOU 1187  C   SER A 148     5939   6164  11948   1166   -371  -2157       C
ATOM   1188  O   SER A 148     -54.972  82.072 -26.767  1.00 67.21           O
ANISOU 1188  O   SER A 148     6287   6761  12489   1188   -373  -2207       O
ATOM   1189  CB  SER A 148     -53.186  81.935 -29.484  1.00 66.59           C
ANISOU 1189  CB  SER A 148     6376   6579  12344   1158   -153  -2416       C
ATOM   1190  OG  SER A 148     -52.840  81.350 -30.723  1.00 72.53           O
ANISOU 1190  OG  SER A 148     7217   7342  12998   1081    -14  -2490       O
ATOM   1191  N   VAL A 149     -52.888  81.302 -26.397  1.00 63.99           N
ANISOU 1191  N   VAL A 149     6163   6096  12053   1212   -527  -2014       N
ATOM   1192  CA  VAL A 149     -52.746  81.887 -25.072  1.00 66.27           C
ANISOU 1192  CA  VAL A 149     6455   6310  12416   1311   -720  -1907       C
ATOM   1193  C   VAL A 149     -51.492  82.747 -25.089  1.00 68.89           C
ANISOU 1193  C   VAL A 149     6864   6480  12832   1433   -828  -1923       C
ATOM   1194  O   VAL A 149     -50.394  82.247 -25.363  1.00 67.79           O
ANISOU 1194  O   VAL A 149     6881   6219  12656   1401   -831  -1868       O
ATOM   1195  CB  VAL A 149     -52.675  80.816 -23.973  1.00 65.42           C
ANISOU 1195  CB  VAL A 149     6472   6153  12230   1240   -806  -1695       C
ATOM   1196  CG1 VAL A 149     -52.430  81.459 -22.618  1.00 65.07           C
ANISOU 1196  CG1 VAL A 149     6465   6016  12243   1346  -1013  -1581       C
ATOM   1197  CG2 VAL A 149     -53.960  80.013 -23.948  1.00 67.88           C
ANISOU 1197  CG2 VAL A 149     6707   6620  12464   1133   -699  -1686       C
ATOM   1198  N   LYS A 150     -51.662  84.036 -24.811  1.00 73.04           N
ANISOU 1198  N   LYS A 150     7280   7003  13469   1572   -916  -2006       N
ATOM   1199  CA  LYS A 150     -50.559  84.984 -24.893  1.00 77.56           C
ANISOU 1199  CA  LYS A 150     7915   7424  14131   1709  -1011  -2044       C
ATOM   1200  C   LYS A 150     -49.452  84.623 -23.911  1.00 71.87           C
ANISOU 1200  C   LYS A 150     7414   6511  13380   1727  -1169  -1847       C
ATOM   1201  O   LYS A 150     -49.704  84.388 -22.726  1.00 69.22           O
ANISOU 1201  O   LYS A 150     7125   6158  13016   1727  -1290  -1699       O
ATOM   1202  CB  LYS A 150     -51.081  86.397 -24.629  1.00 89.40           C
ANISOU 1202  CB  LYS A 150     9244   8969  15757   1862  -1092  -2161       C
ATOM   1203  CG  LYS A 150     -50.109  87.335 -23.933  1.00 97.70           C
ANISOU 1203  CG  LYS A 150    10387   9841  16893   2034  -1287  -2112       C
ATOM   1204  CD  LYS A 150     -50.766  88.687 -23.692  1.00105.00           C
ANISOU 1204  CD  LYS A 150    11116  10837  17943   2186  -1366  -2243       C
ATOM   1205  CE  LYS A 150     -50.049  89.485 -22.616  1.00110.90           C
ANISOU 1205  CE  LYS A 150    11966  11419  18754   2358  -1603  -2148       C
ATOM   1206  NZ  LYS A 150     -50.750  90.770 -22.335  1.00113.44           N
ANISOU 1206  NZ  LYS A 150    12081  11821  19198   2512  -1695  -2279       N
ATOM   1207  N   GLY A 151     -48.221  84.569 -24.414  1.00 69.59           N
ANISOU 1207  N   GLY A 151     7272   6078  13092   1732  -1158  -1847       N
ATOM   1208  CA  GLY A 151     -47.069  84.291 -23.583  1.00 72.20           C
ANISOU 1208  CA  GLY A 151     7829   6212  13393   1737  -1285  -1675       C
ATOM   1209  C   GLY A 151     -46.824  82.833 -23.279  1.00 73.27           C
ANISOU 1209  C   GLY A 151     8101   6333  13406   1566  -1245  -1521       C
ATOM   1210  O   GLY A 151     -46.027  82.531 -22.383  1.00 78.27           O
ANISOU 1210  O   GLY A 151     8919   6818  14000   1547  -1346  -1359       O
ATOM   1211  N   LEU A 152     -47.475  81.916 -23.991  1.00 66.94           N
ANISOU 1211  N   LEU A 152     7221   5676  12537   1438  -1096  -1567       N
ATOM   1212  CA  LEU A 152     -47.315  80.489 -23.749  1.00 58.07           C
ANISOU 1212  CA  LEU A 152     6206   4555  11302   1278  -1052  -1434       C
ATOM   1213  C   LEU A 152     -47.270  79.749 -25.076  1.00 57.28           C
ANISOU 1213  C   LEU A 152     6083   4532  11146   1174   -888  -1542       C
ATOM   1214  O   LEU A 152     -48.150  79.930 -25.923  1.00 55.36           O
ANISOU 1214  O   LEU A 152     5696   4433  10906   1177   -776  -1683       O
ATOM   1215  CB  LEU A 152     -48.453  79.946 -22.877  1.00 55.38           C
ANISOU 1215  CB  LEU A 152     5800   4331  10912   1230  -1071  -1335       C
ATOM   1216  CG  LEU A 152     -48.454  80.398 -21.417  1.00 57.38           C
ANISOU 1216  CG  LEU A 152     6116   4503  11181   1305  -1246  -1192       C
ATOM   1217  CD1 LEU A 152     -49.670  79.851 -20.691  1.00 52.42           C
ANISOU 1217  CD1 LEU A 152     5411   4005  10502   1252  -1249  -1118       C
ATOM   1218  CD2 LEU A 152     -47.171  79.961 -20.726  1.00 59.92           C
ANISOU 1218  CD2 LEU A 152     6677   4638  11454   1259  -1323  -1031       C
ATOM   1219  N   GLN A 153     -46.247  78.920 -25.249  1.00 58.73           N
ANISOU 1219  N   GLN A 153     6420   4622  11275   1077   -873  -1480       N
ATOM   1220  CA  GLN A 153     -46.112  78.129 -26.465  1.00 56.68           C
ANISOU 1220  CA  GLN A 153     6159   4427  10948    976   -739  -1575       C
ATOM   1221  C   GLN A 153     -47.020  76.906 -26.387  1.00 50.27           C
ANISOU 1221  C   GLN A 153     5305   3758  10039    860   -666  -1517       C
ATOM   1222  O   GLN A 153     -46.982  76.176 -25.392  1.00 44.58           O
ANISOU 1222  O   GLN A 153     4652   3011   9277    795   -722  -1358       O
ATOM   1223  CB  GLN A 153     -44.661  77.700 -26.663  1.00 65.11           C
ANISOU 1223  CB  GLN A 153     7396   5344  11998    910   -760  -1541       C
ATOM   1224  CG  GLN A 153     -44.320  77.270 -28.079  1.00 74.28           C
ANISOU 1224  CG  GLN A 153     8562   6548  13114    846   -648  -1682       C
ATOM   1225  CD  GLN A 153     -44.165  78.442 -29.030  1.00 84.59           C
ANISOU 1225  CD  GLN A 153     9819   7833  14487    957   -611  -1858       C
ATOM   1226  OE1 GLN A 153     -44.410  79.594 -28.669  1.00 86.42           O
ANISOU 1226  OE1 GLN A 153     9988   8036  14810   1090   -664  -1887       O
ATOM   1227  NE2 GLN A 153     -43.747  78.151 -30.256  1.00 89.44           N
ANISOU 1227  NE2 GLN A 153    10465   8464  15055    906   -524  -1982       N
ATOM   1228  N   PRO A 154     -47.846  76.657 -27.399  1.00 49.91           N
ANISOU 1228  N   PRO A 154     5163   3856   9945    829   -538  -1640       N
ATOM   1229  CA  PRO A 154     -48.841  75.587 -27.308  1.00 48.55           C
ANISOU 1229  CA  PRO A 154     4954   3814   9678    738   -468  -1590       C
ATOM   1230  C   PRO A 154     -48.335  74.246 -27.823  1.00 50.28           C
ANISOU 1230  C   PRO A 154     5269   4040   9794    614   -420  -1565       C
ATOM   1231  O   PRO A 154     -47.322  74.146 -28.518  1.00 53.51           O
ANISOU 1231  O   PRO A 154     5753   4380  10197    589   -416  -1622       O
ATOM   1232  CB  PRO A 154     -49.975  76.109 -28.199  1.00 48.43           C
ANISOU 1232  CB  PRO A 154     4804   3941   9655    770   -346  -1750       C
ATOM   1233  CG  PRO A 154     -49.257  76.873 -29.262  1.00 49.71           C
ANISOU 1233  CG  PRO A 154     4975   4056   9855    821   -309  -1899       C
ATOM   1234  CD  PRO A 154     -48.031  77.480 -28.607  1.00 52.77           C
ANISOU 1234  CD  PRO A 154     5445   4269  10335    889   -447  -1833       C
ATOM   1235  N   SER A 155     -49.080  73.204 -27.458  1.00 45.87           N
ANISOU 1235  N   SER A 155     4704   3567   9156    538   -388  -1483       N
ATOM   1236  CA  SER A 155     -48.877  71.857 -27.976  1.00 42.70           C
ANISOU 1236  CA  SER A 155     4368   3208   8649    427   -339  -1473       C
ATOM   1237  C   SER A 155     -50.205  71.363 -28.524  1.00 36.25           C
ANISOU 1237  C   SER A 155     3495   2538   7739    405   -229  -1531       C
ATOM   1238  O   SER A 155     -51.207  71.343 -27.802  1.00 40.78           O
ANISOU 1238  O   SER A 155     4014   3167   8312    415   -221  -1466       O
ATOM   1239  CB  SER A 155     -48.355  70.912 -26.891  1.00 42.30           C
ANISOU 1239  CB  SER A 155     4391   3100   8580    345   -412  -1302       C
ATOM   1240  OG  SER A 155     -48.221  69.592 -27.387  1.00 42.70           O
ANISOU 1240  OG  SER A 155     4480   3207   8537    243   -370  -1305       O
ATOM   1241  N   VAL A 156     -50.216  70.975 -29.794  1.00 36.29           N
ANISOU 1241  N   VAL A 156     3529   2600   7658    372   -146  -1653       N
ATOM   1242  CA  VAL A 156     -51.446  70.545 -30.450  1.00 45.88           C
ANISOU 1242  CA  VAL A 156     4726   3943   8761    349    -29  -1719       C
ATOM   1243  C   VAL A 156     -51.764  69.117 -30.030  1.00 46.39           C
ANISOU 1243  C   VAL A 156     4846   4054   8726    269    -43  -1606       C
ATOM   1244  O   VAL A 156     -50.905  68.230 -30.095  1.00 50.40           O
ANISOU 1244  O   VAL A 156     5419   4529   9201    211   -100  -1567       O
ATOM   1245  CB  VAL A 156     -51.318  70.665 -31.976  1.00 42.98           C
ANISOU 1245  CB  VAL A 156     4402   3616   8311    343     60  -1887       C
ATOM   1246  CG1 VAL A 156     -52.631  70.302 -32.648  1.00 39.72           C
ANISOU 1246  CG1 VAL A 156     4001   3329   7764    313    194  -1953       C
ATOM   1247  CG2 VAL A 156     -50.889  72.073 -32.359  1.00 43.60           C
ANISOU 1247  CG2 VAL A 156     4427   3648   8490    421     71  -1993       C
ATOM   1248  N   GLY A 157     -53.003  68.890 -29.599  1.00 45.05           N
ANISOU 1248  N   GLY A 157     4646   4001   8470    253     10  -1535       N
ATOM   1249  CA  GLY A 157     -53.423  67.592 -29.127  1.00 37.58           C
ANISOU 1249  CA  GLY A 157     3751   3140   7387    181      0  -1399       C
ATOM   1250  C   GLY A 157     -54.028  66.737 -30.221  1.00 38.41           C
ANISOU 1250  C   GLY A 157     3932   3358   7303    141     82  -1452       C
ATOM   1251  O   GLY A 157     -53.882  67.016 -31.415  1.00 43.05           O
ANISOU 1251  O   GLY A 157     4555   3948   7853    152    136  -1593       O
ATOM   1252  N   PRO A 158     -54.717  65.668 -29.830  1.00 36.17           N
ANISOU 1252  N   PRO A 158     3691   3164   6889     98     88  -1341       N
ATOM   1253  CA  PRO A 158     -55.350  64.794 -30.823  1.00 32.34           C
ANISOU 1253  CA  PRO A 158     3304   2774   6210     72    150  -1377       C
ATOM   1254  C   PRO A 158     -56.516  65.489 -31.508  1.00 32.76           C
ANISOU 1254  C   PRO A 158     3373   2886   6187     74    285  -1466       C
ATOM   1255  O   PRO A 158     -57.077  66.469 -31.012  1.00 33.91           O
ANISOU 1255  O   PRO A 158     3430   3030   6424     87    333  -1479       O
ATOM   1256  CB  PRO A 158     -55.834  63.597 -29.995  1.00 29.10           C
ANISOU 1256  CB  PRO A 158     2923   2425   5707     42    118  -1227       C
ATOM   1257  CG  PRO A 158     -55.114  63.702 -28.680  1.00 29.35           C
ANISOU 1257  CG  PRO A 158     2879   2388   5884     35     33  -1123       C
ATOM   1258  CD  PRO A 158     -54.887  65.160 -28.460  1.00 30.58           C
ANISOU 1258  CD  PRO A 158     2960   2462   6198     74     34  -1179       C
ATOM   1259  N   LYS A 159     -56.878  64.958 -32.677  1.00 32.89           N
ANISOU 1259  N   LYS A 159     3509   2956   6031     56    346  -1534       N
ATOM   1260  CA  LYS A 159     -58.047  65.471 -33.381  1.00 30.95           C
ANISOU 1260  CA  LYS A 159     3311   2768   5680     31    498  -1614       C
ATOM   1261  C   LYS A 159     -59.335  65.141 -32.641  1.00 37.38           C
ANISOU 1261  C   LYS A 159     4137   3647   6419     -8    552  -1507       C
ATOM   1262  O   LYS A 159     -60.306  65.903 -32.720  1.00 43.01           O
ANISOU 1262  O   LYS A 159     4820   4397   7127    -41    676  -1560       O
ATOM   1263  CB  LYS A 159     -58.107  64.906 -34.800  1.00 36.85           C
ANISOU 1263  CB  LYS A 159     4225   3545   6231     15    543  -1699       C
ATOM   1264  CG  LYS A 159     -57.132  65.535 -35.779  1.00 40.28           C
ANISOU 1264  CG  LYS A 159     4663   3926   6716     39    543  -1855       C
ATOM   1265  CD  LYS A 159     -57.397  65.037 -37.192  1.00 46.95           C
ANISOU 1265  CD  LYS A 159     5697   4809   7333     17    601  -1940       C
ATOM   1266  CE  LYS A 159     -56.544  65.771 -38.213  1.00 55.31           C
ANISOU 1266  CE  LYS A 159     6770   5818   8428     33    624  -2114       C
ATOM   1267  NZ  LYS A 159     -55.089  65.555 -37.982  1.00 59.73           N
ANISOU 1267  NZ  LYS A 159     7267   6305   9123     68    464  -2117       N
ATOM   1268  N   GLN A 160     -59.362  64.028 -31.917  1.00 32.52           N
ANISOU 1268  N   GLN A 160     3559   3047   5750    -11    469  -1367       N
ATOM   1269  CA  GLN A 160     -60.581  63.518 -31.311  1.00 34.20           C
ANISOU 1269  CA  GLN A 160     3818   3314   5861    -48    518  -1266       C
ATOM   1270  C   GLN A 160     -60.646  63.858 -29.826  1.00 33.68           C
ANISOU 1270  C   GLN A 160     3624   3235   5937    -49    466  -1168       C
ATOM   1271  O   GLN A 160     -59.629  64.073 -29.162  1.00 32.15           O
ANISOU 1271  O   GLN A 160     3340   2986   5891    -17    363  -1135       O
ATOM   1272  CB  GLN A 160     -60.685  62.002 -31.500  1.00 29.87           C
ANISOU 1272  CB  GLN A 160     3411   2794   5145    -40    464  -1184       C
ATOM   1273  CG  GLN A 160     -59.682  61.189 -30.688  1.00 33.57           C
ANISOU 1273  CG  GLN A 160     3818   3243   5695     -8    322  -1092       C
ATOM   1274  CD  GLN A 160     -58.303  61.139 -31.319  1.00 40.55           C
ANISOU 1274  CD  GLN A 160     4675   4087   6645     20    236  -1168       C
ATOM   1275  OE1 GLN A 160     -58.041  61.797 -32.325  1.00 47.82           O
ANISOU 1275  OE1 GLN A 160     5620   4988   7560     24    274  -1290       O
ATOM   1276  NE2 GLN A 160     -57.413  60.350 -30.728  1.00 42.63           N
ANISOU 1276  NE2 GLN A 160     4888   4340   6969     30    126  -1104       N
ATOM   1277  N   ALA A 161     -61.874  63.901 -29.313  1.00 33.13           N
ANISOU 1277  N   ALA A 161     3565   3212   5810    -93    538  -1121       N
ATOM   1278  CA  ALA A 161     -62.133  64.106 -27.897  1.00 30.42           C
ANISOU 1278  CA  ALA A 161     3129   2867   5560   -101    489  -1022       C
ATOM   1279  C   ALA A 161     -63.348  63.279 -27.507  1.00 31.36           C
ANISOU 1279  C   ALA A 161     3350   3038   5529   -152    543   -936       C
ATOM   1280  O   ALA A 161     -64.059  62.742 -28.360  1.00 34.43           O
ANISOU 1280  O   ALA A 161     3875   3453   5752   -180    629   -962       O
ATOM   1281  CB  ALA A 161     -62.352  65.587 -27.567  1.00 32.08           C
ANISOU 1281  CB  ALA A 161     3189   3073   5926    -97    516  -1098       C
ATOM   1282  N   SER A 162     -63.586  63.180 -26.203  1.00 34.15           N
ANISOU 1282  N   SER A 162     3653   3394   5930   -163    491   -834       N
ATOM   1283  CA  SER A 162     -64.685  62.389 -25.665  1.00 30.79           C
ANISOU 1283  CA  SER A 162     3321   3004   5372   -209    532   -749       C
ATOM   1284  C   SER A 162     -65.860  63.302 -25.340  1.00 29.73           C
ANISOU 1284  C   SER A 162     3134   2906   5256   -276    618   -790       C
ATOM   1285  O   SER A 162     -65.719  64.250 -24.562  1.00 33.79           O
ANISOU 1285  O   SER A 162     3506   3418   5916   -270    567   -799       O
ATOM   1286  CB  SER A 162     -64.248  61.621 -24.419  1.00 32.85           C
ANISOU 1286  CB  SER A 162     3573   3250   5656   -190    432   -617       C
ATOM   1287  OG  SER A 162     -65.351  60.967 -23.817  1.00 34.51           O
ANISOU 1287  OG  SER A 162     3870   3491   5752   -232    475   -546       O
ATOM   1288  N   LEU A 163     -67.015  63.010 -25.933  1.00 30.77           N
ANISOU 1288  N   LEU A 163     3385   3067   5239   -342    742   -819       N
ATOM   1289  CA  LEU A 163     -68.255  63.729 -25.658  1.00 29.77           C
ANISOU 1289  CA  LEU A 163     3220   2981   5110   -433    842   -865       C
ATOM   1290  C   LEU A 163     -69.284  62.723 -25.162  1.00 29.80           C
ANISOU 1290  C   LEU A 163     3376   2988   4959   -488    878   -771       C
ATOM   1291  O   LEU A 163     -69.805  61.924 -25.949  1.00 29.54           O
ANISOU 1291  O   LEU A 163     3529   2941   4755   -509    956   -765       O
ATOM   1292  CB  LEU A 163     -68.758  64.462 -26.900  1.00 30.78           C
ANISOU 1292  CB  LEU A 163     3358   3133   5205   -490    992  -1010       C
ATOM   1293  CG  LEU A 163     -70.100  65.175 -26.734  1.00 32.13           C
ANISOU 1293  CG  LEU A 163     3485   3354   5369   -610   1123  -1079       C
ATOM   1294  CD1 LEU A 163     -70.022  66.197 -25.613  1.00 32.80           C
ANISOU 1294  CD1 LEU A 163     3341   3471   5652   -596   1037  -1096       C
ATOM   1295  CD2 LEU A 163     -70.524  65.834 -28.034  1.00 30.92           C
ANISOU 1295  CD2 LEU A 163     3352   3224   5172   -678   1296  -1230       C
ATOM   1296  N   ASN A 164     -69.572  62.763 -23.860  1.00 29.46           N
ANISOU 1296  N   ASN A 164     3270   2957   4968   -505    817   -699       N
ATOM   1297  CA  ASN A 164     -70.525  61.848 -23.230  1.00 34.83           C
ANISOU 1297  CA  ASN A 164     4087   3632   5513   -554    844   -612       C
ATOM   1298  C   ASN A 164     -70.133  60.392 -23.471  1.00 36.52           C
ANISOU 1298  C   ASN A 164     4463   3810   5603   -484    808   -526       C
ATOM   1299  O   ASN A 164     -70.978  59.539 -23.747  1.00 38.68           O
ANISOU 1299  O   ASN A 164     4917   4064   5716   -509    876   -497       O
ATOM   1300  CB  ASN A 164     -71.952  62.112 -23.714  1.00 37.95           C
ANISOU 1300  CB  ASN A 164     4568   4046   5806   -676   1002   -681       C
ATOM   1301  CG  ASN A 164     -72.338  63.573 -23.617  1.00 36.05           C
ANISOU 1301  CG  ASN A 164     4137   3858   5701   -748   1048   -797       C
ATOM   1302  OD1 ASN A 164     -72.808  64.168 -24.588  1.00 36.51           O
ANISOU 1302  OD1 ASN A 164     4193   3937   5740   -816   1180   -912       O
ATOM   1303  ND2 ASN A 164     -72.137  64.161 -22.444  1.00 31.03           N
ANISOU 1303  ND2 ASN A 164     3341   3247   5201   -731    938   -773       N
ATOM   1304  N   GLY A 165     -68.837  60.108 -23.368  1.00 35.33           N
ANISOU 1304  N   GLY A 165     4248   3646   5532   -393    698   -492       N
ATOM   1305  CA  GLY A 165     -68.339  58.774 -23.624  1.00 32.10           C
ANISOU 1305  CA  GLY A 165     3948   3217   5032   -318    651   -433       C
ATOM   1306  C   GLY A 165     -68.232  58.401 -25.082  1.00 29.94           C
ANISOU 1306  C   GLY A 165     3788   2931   4656   -284    688   -493       C
ATOM   1307  O   GLY A 165     -67.950  57.237 -25.387  1.00 32.70           O
ANISOU 1307  O   GLY A 165     4239   3268   4916   -214    641   -454       O
ATOM   1308  N   VAL A 166     -68.452  59.344 -25.991  1.00 29.48           N
ANISOU 1308  N   VAL A 166     3718   2878   4606   -329    769   -594       N
ATOM   1309  CA  VAL A 166     -68.354  59.103 -27.424  1.00 30.85           C
ANISOU 1309  CA  VAL A 166     4018   3038   4667   -307    811   -660       C
ATOM   1310  C   VAL A 166     -67.119  59.835 -27.925  1.00 26.97           C
ANISOU 1310  C   VAL A 166     3388   2550   4311   -265    757   -738       C
ATOM   1311  O   VAL A 166     -67.076  61.072 -27.929  1.00 31.07           O
ANISOU 1311  O   VAL A 166     3776   3080   4948   -305    802   -816       O
ATOM   1312  CB  VAL A 166     -69.612  59.562 -28.172  1.00 32.66           C
ANISOU 1312  CB  VAL A 166     4374   3263   4771   -407    974   -726       C
ATOM   1313  CG1 VAL A 166     -69.489  59.244 -29.653  1.00 34.22           C
ANISOU 1313  CG1 VAL A 166     4740   3438   4823   -384   1014   -785       C
ATOM   1314  CG2 VAL A 166     -70.848  58.905 -27.580  1.00 31.16           C
ANISOU 1314  CG2 VAL A 166     4326   3056   4460   -461   1029   -650       C
ATOM   1315  N   THR A 167     -66.109  59.075 -28.336  1.00 30.34           N
ANISOU 1315  N   THR A 167     3837   2964   4726   -183    657   -727       N
ATOM   1316  CA  THR A 167     -64.903  59.661 -28.901  1.00 33.31           C
ANISOU 1316  CA  THR A 167     4110   3332   5216   -147    604   -806       C
ATOM   1317  C   THR A 167     -65.126  59.949 -30.380  1.00 37.74           C
ANISOU 1317  C   THR A 167     4789   3889   5661   -162    688   -915       C
ATOM   1318  O   THR A 167     -65.526  59.062 -31.140  1.00 38.31           O
ANISOU 1318  O   THR A 167     5050   3956   5549   -143    699   -904       O
ATOM   1319  CB  THR A 167     -63.711  58.723 -28.711  1.00 31.92           C
ANISOU 1319  CB  THR A 167     3900   3147   5079    -71    464   -761       C
ATOM   1320  OG1 THR A 167     -63.497  58.498 -27.312  1.00 33.69           O
ANISOU 1320  OG1 THR A 167     4025   3373   5404    -73    407   -663       O
ATOM   1321  CG2 THR A 167     -62.456  59.329 -29.317  1.00 25.67           C
ANISOU 1321  CG2 THR A 167     3016   2334   4402    -47    411   -850       C
ATOM   1322  N   LEU A 168     -64.872  61.191 -30.787  1.00 38.64           N
ANISOU 1322  N   LEU A 168     4802   4002   5877   -191    748  -1023       N
ATOM   1323  CA  LEU A 168     -65.175  61.607 -32.147  1.00 36.71           C
ANISOU 1323  CA  LEU A 168     4668   3758   5520   -224    861  -1140       C
ATOM   1324  C   LEU A 168     -64.331  62.818 -32.509  1.00 38.63           C
ANISOU 1324  C   LEU A 168     4760   3993   5926   -213    871  -1264       C
ATOM   1325  O   LEU A 168     -63.851  63.550 -31.638  1.00 41.40           O
ANISOU 1325  O   LEU A 168     4921   4335   6475   -194    819  -1260       O
ATOM   1326  CB  LEU A 168     -66.667  61.923 -32.309  1.00 39.04           C
ANISOU 1326  CB  LEU A 168     5062   4072   5699   -326   1031  -1158       C
ATOM   1327  CG  LEU A 168     -67.274  62.938 -31.330  1.00 41.10           C
ANISOU 1327  CG  LEU A 168     5145   4362   6109   -391   1094  -1170       C
ATOM   1328  CD1 LEU A 168     -67.193  64.364 -31.864  1.00 36.42           C
ANISOU 1328  CD1 LEU A 168     4416   3791   5631   -428   1199  -1327       C
ATOM   1329  CD2 LEU A 168     -68.711  62.574 -30.994  1.00 45.86           C
ANISOU 1329  CD2 LEU A 168     5869   4975   6582   -483   1197  -1115       C
ATOM   1330  N   ILE A 169     -64.163  63.019 -33.812  1.00 37.89           N
ANISOU 1330  N   ILE A 169     4767   3894   5737   -219    936  -1375       N
ATOM   1331  CA  ILE A 169     -63.551  64.229 -34.347  1.00 37.92           C
ANISOU 1331  CA  ILE A 169     4654   3887   5868   -215    985  -1520       C
ATOM   1332  C   ILE A 169     -64.683  65.198 -34.669  1.00 44.86           C
ANISOU 1332  C   ILE A 169     5519   4802   6722   -307   1185  -1617       C
ATOM   1333  O   ILE A 169     -65.469  64.966 -35.592  1.00 47.23           O
ANISOU 1333  O   ILE A 169     6005   5116   6823   -375   1317  -1657       O
ATOM   1334  CB  ILE A 169     -62.693  63.934 -35.582  1.00 35.12           C
ANISOU 1334  CB  ILE A 169     4413   3508   5422   -176    950  -1603       C
ATOM   1335  CG1 ILE A 169     -61.555  62.979 -35.215  1.00 36.58           C
ANISOU 1335  CG1 ILE A 169     4580   3666   5651    -99    752  -1522       C
ATOM   1336  CG2 ILE A 169     -62.140  65.225 -36.165  1.00 35.01           C
ANISOU 1336  CG2 ILE A 169     4291   3478   5534   -174   1021  -1768       C
ATOM   1337  CD1 ILE A 169     -60.638  62.645 -36.369  1.00 39.25           C
ANISOU 1337  CD1 ILE A 169     5017   3985   5911    -62    689  -1608       C
ATOM   1338  N   GLY A 170     -64.763  66.284 -33.907  1.00 45.64           N
ANISOU 1338  N   GLY A 170     5400   4917   7024   -312   1207  -1659       N
ATOM   1339  CA  GLY A 170     -65.932  67.141 -33.967  1.00 32.88           C
ANISOU 1339  CA  GLY A 170     3730   3353   5411   -409   1387  -1745       C
ATOM   1340  C   GLY A 170     -66.055  67.864 -35.298  1.00 39.15           C
ANISOU 1340  C   GLY A 170     4570   4162   6142   -457   1561  -1924       C
ATOM   1341  O   GLY A 170     -65.067  68.293 -35.896  1.00 40.52           O
ANISOU 1341  O   GLY A 170     4703   4307   6386   -392   1531  -2020       O
ATOM   1342  N   GLU A 171     -67.293  67.991 -35.761  1.00 40.65           N
ANISOU 1342  N   GLU A 171     4858   4394   6194   -583   1756  -1972       N
ATOM   1343  CA  GLU A 171     -67.641  68.777 -36.937  1.00 46.01           C
ANISOU 1343  CA  GLU A 171     5573   5100   6808   -663   1970  -2153       C
ATOM   1344  C   GLU A 171     -68.553  69.946 -36.608  1.00 47.13           C
ANISOU 1344  C   GLU A 171     5512   5314   7082   -758   2137  -2273       C
ATOM   1345  O   GLU A 171     -68.337  71.052 -37.110  1.00 53.03           O
ANISOU 1345  O   GLU A 171     6110   6092   7948   -757   2246  -2454       O
ATOM   1346  CB  GLU A 171     -68.309  67.884 -37.991  1.00 55.34           C
ANISOU 1346  CB  GLU A 171     7091   6263   7672   -753   2085  -2124       C
ATOM   1347  CG  GLU A 171     -67.451  66.709 -38.431  1.00 64.17           C
ANISOU 1347  CG  GLU A 171     8411   7322   8650   -654   1913  -2026       C
ATOM   1348  CD  GLU A 171     -68.172  65.784 -39.391  1.00 71.85           C
ANISOU 1348  CD  GLU A 171     9734   8267   9300   -724   1997  -1982       C
ATOM   1349  OE1 GLU A 171     -69.373  66.011 -39.651  1.00 75.29           O
ANISOU 1349  OE1 GLU A 171    10274   8717   9614   -863   2198  -2013       O
ATOM   1350  OE2 GLU A 171     -67.537  64.830 -39.887  1.00 73.41           O
ANISOU 1350  OE2 GLU A 171    10105   8423   9363   -641   1857  -1921       O
ATOM   1351  N   ALA A 172     -69.571  69.727 -35.780  1.00 43.95           N
ANISOU 1351  N   ALA A 172     5092   4942   6666   -838   2159  -2190       N
ATOM   1352  CA  ALA A 172     -70.385  70.801 -35.232  1.00 45.71           C
ANISOU 1352  CA  ALA A 172     5078   5242   7049   -920   2272  -2296       C
ATOM   1353  C   ALA A 172     -69.845  71.318 -33.906  1.00 46.22           C
ANISOU 1353  C   ALA A 172     4864   5316   7379   -802   2072  -2254       C
ATOM   1354  O   ALA A 172     -70.454  72.210 -33.307  1.00 47.53           O
ANISOU 1354  O   ALA A 172     4808   5551   7701   -846   2118  -2337       O
ATOM   1355  CB  ALA A 172     -71.831  70.332 -35.050  1.00 42.14           C
ANISOU 1355  CB  ALA A 172     4764   4814   6435  -1089   2408  -2240       C
ATOM   1356  N   VAL A 173     -68.722  70.772 -33.436  1.00 45.67           N
ANISOU 1356  N   VAL A 173     4811   5180   7361   -660   1850  -2132       N
ATOM   1357  CA  VAL A 173     -68.092  71.196 -32.193  1.00 45.06           C
ANISOU 1357  CA  VAL A 173     4518   5090   7512   -545   1651  -2075       C
ATOM   1358  C   VAL A 173     -66.592  70.984 -32.343  1.00 45.40           C
ANISOU 1358  C   VAL A 173     4581   5050   7619   -403   1490  -2039       C
ATOM   1359  O   VAL A 173     -66.134  70.221 -33.195  1.00 46.24           O
ANISOU 1359  O   VAL A 173     4882   5117   7572   -398   1498  -2016       O
ATOM   1360  CB  VAL A 173     -68.653  70.427 -30.970  1.00 43.84           C
ANISOU 1360  CB  VAL A 173     4402   4938   7317   -573   1545  -1896       C
ATOM   1361  CG1 VAL A 173     -68.075  69.021 -30.904  1.00 38.41           C
ANISOU 1361  CG1 VAL A 173     3930   4182   6481   -525   1423  -1723       C
ATOM   1362  CG2 VAL A 173     -68.399  71.197 -29.678  1.00 49.01           C
ANISOU 1362  CG2 VAL A 173     4812   5604   8204   -495   1391  -1879       C
ATOM   1363  N   LYS A 174     -65.818  71.680 -31.514  1.00 44.22           N
ANISOU 1363  N   LYS A 174     4237   4869   7694   -289   1337  -2038       N
ATOM   1364  CA  LYS A 174     -64.364  71.676 -31.608  1.00 43.44           C
ANISOU 1364  CA  LYS A 174     4138   4680   7688   -164   1192  -2024       C
ATOM   1365  C   LYS A 174     -63.797  70.667 -30.615  1.00 40.72           C
ANISOU 1365  C   LYS A 174     3870   4280   7323   -123   1003  -1819       C
ATOM   1366  O   LYS A 174     -64.069  70.754 -29.413  1.00 39.11           O
ANISOU 1366  O   LYS A 174     3578   4084   7198   -112    909  -1725       O
ATOM   1367  CB  LYS A 174     -63.808  73.074 -31.343  1.00 50.16           C
ANISOU 1367  CB  LYS A 174     4754   5509   8796    -59   1142  -2152       C
ATOM   1368  CG  LYS A 174     -62.487  73.362 -32.034  1.00 60.79           C
ANISOU 1368  CG  LYS A 174     6116   6764  10216     41   1092  -2230       C
ATOM   1369  CD  LYS A 174     -62.344  74.847 -32.327  1.00 66.56           C
ANISOU 1369  CD  LYS A 174     6639   7499  11151    117   1148  -2435       C
ATOM   1370  CE  LYS A 174     -63.487  75.342 -33.203  1.00 69.63           C
ANISOU 1370  CE  LYS A 174     6999   8006  11450     -2   1380  -2582       C
ATOM   1371  NZ  LYS A 174     -63.371  76.794 -33.517  1.00 71.44           N
ANISOU 1371  NZ  LYS A 174     7056   8268  11820     37   1394  -2725       N
ATOM   1372  N   THR A 175     -63.009  69.714 -31.120  1.00 37.00           N
ANISOU 1372  N   THR A 175     3558   3756   6743   -103    948  -1758       N
ATOM   1373  CA  THR A 175     -62.448  68.652 -30.296  1.00 35.14           C
ANISOU 1373  CA  THR A 175     3396   3479   6478    -77    793  -1580       C
ATOM   1374  C   THR A 175     -60.926  68.648 -30.230  1.00 34.58           C
ANISOU 1374  C   THR A 175     3306   3313   6520     10    652  -1567       C
ATOM   1375  O   THR A 175     -60.368  67.918 -29.402  1.00 32.66           O
ANISOU 1375  O   THR A 175     3090   3031   6288     26    525  -1429       O
ATOM   1376  CB  THR A 175     -62.924  67.277 -30.794  1.00 33.63           C
ANISOU 1376  CB  THR A 175     3413   3317   6049   -137    835  -1501       C
ATOM   1377  OG1 THR A 175     -62.661  67.151 -32.196  1.00 38.14           O
ANISOU 1377  OG1 THR A 175     4099   3883   6509   -144    912  -1607       O
ATOM   1378  CG2 THR A 175     -64.414  67.104 -30.546  1.00 33.92           C
ANISOU 1378  CG2 THR A 175     3494   3421   5971   -230    949  -1470       C
ATOM   1379  N   GLN A 176     -60.240  69.425 -31.063  1.00 34.35           N
ANISOU 1379  N   GLN A 176     3235   3242   6574     56    678  -1711       N
ATOM   1380  CA  GLN A 176     -58.784  69.499 -31.046  1.00 35.36           C
ANISOU 1380  CA  GLN A 176     3354   3265   6816    128    552  -1713       C
ATOM   1381  C   GLN A 176     -58.366  70.713 -30.227  1.00 39.38           C
ANISOU 1381  C   GLN A 176     3699   3707   7556    212    473  -1739       C
ATOM   1382  O   GLN A 176     -58.735  71.845 -30.557  1.00 47.62           O
ANISOU 1382  O   GLN A 176     4627   4770   8696    246    551  -1881       O
ATOM   1383  CB  GLN A 176     -58.225  69.578 -32.466  1.00 40.42           C
ANISOU 1383  CB  GLN A 176     4072   3885   7400    133    618  -1859       C
ATOM   1384  CG  GLN A 176     -56.716  69.398 -32.553  1.00 41.62           C
ANISOU 1384  CG  GLN A 176     4250   3927   7635    182    489  -1858       C
ATOM   1385  CD  GLN A 176     -56.238  69.173 -33.975  1.00 46.88           C
ANISOU 1385  CD  GLN A 176     5029   4588   8195    170    542  -1987       C
ATOM   1386  OE1 GLN A 176     -56.896  69.575 -34.935  1.00 52.22           O
ANISOU 1386  OE1 GLN A 176     5739   5319   8782    146    686  -2113       O
ATOM   1387  NE2 GLN A 176     -55.091  68.519 -34.117  1.00 47.91           N
ANISOU 1387  NE2 GLN A 176     5222   4652   8327    175    428  -1961       N
ATOM   1388  N   PHE A 177     -57.601  70.480 -29.165  1.00 36.71           N
ANISOU 1388  N   PHE A 177     3354   3289   7303    246    320  -1608       N
ATOM   1389  CA  PHE A 177     -57.247  71.520 -28.212  1.00 42.84           C
ANISOU 1389  CA  PHE A 177     4010   3989   8278    331    215  -1597       C
ATOM   1390  C   PHE A 177     -55.755  71.825 -28.263  1.00 44.34           C
ANISOU 1390  C   PHE A 177     4224   4028   8594    400    108  -1615       C
ATOM   1391  O   PHE A 177     -54.952  71.074 -28.823  1.00 43.35           O
ANISOU 1391  O   PHE A 177     4204   3862   8404    365     98  -1609       O
ATOM   1392  CB  PHE A 177     -57.637  71.110 -26.786  1.00 40.78           C
ANISOU 1392  CB  PHE A 177     3746   3742   8005    309    122  -1419       C
ATOM   1393  CG  PHE A 177     -59.007  70.508 -26.677  1.00 43.11           C
ANISOU 1393  CG  PHE A 177     4060   4170   8149    222    218  -1375       C
ATOM   1394  CD1 PHE A 177     -60.138  71.274 -26.909  1.00 46.32           C
ANISOU 1394  CD1 PHE A 177     4363   4667   8570    208    321  -1481       C
ATOM   1395  CD2 PHE A 177     -59.165  69.177 -26.326  1.00 43.19           C
ANISOU 1395  CD2 PHE A 177     4190   4211   8008    151    208  -1236       C
ATOM   1396  CE1 PHE A 177     -61.402  70.719 -26.805  1.00 46.21           C
ANISOU 1396  CE1 PHE A 177     4385   4760   8414    113    415  -1442       C
ATOM   1397  CE2 PHE A 177     -60.425  68.617 -26.219  1.00 39.82           C
ANISOU 1397  CE2 PHE A 177     3801   3889   7441     76    294  -1196       C
ATOM   1398  CZ  PHE A 177     -61.545  69.388 -26.458  1.00 41.19           C
ANISOU 1398  CZ  PHE A 177     3890   4138   7622     52    398  -1295       C
ATOM   1399  N   ASN A 178     -55.397  72.954 -27.659  1.00 35.25           N
ANISOU 1399  N   ASN A 178     2976   2789   7627    502     20  -1642       N
ATOM   1400  CA  ASN A 178     -54.013  73.285 -27.355  1.00 36.05           C
ANISOU 1400  CA  ASN A 178     3131   2760   7806    546   -112  -1590       C
ATOM   1401  C   ASN A 178     -53.726  72.883 -25.915  1.00 40.43           C
ANISOU 1401  C   ASN A 178     3732   3239   8390    540   -246  -1402       C
ATOM   1402  O   ASN A 178     -54.523  73.174 -25.017  1.00 35.20           O
ANISOU 1402  O   ASN A 178     3002   2610   7763    568   -283  -1346       O
ATOM   1403  CB  ASN A 178     -53.744  74.777 -27.551  1.00 40.31           C
ANISOU 1403  CB  ASN A 178     3579   3274   8464    645   -142  -1697       C
ATOM   1404  CG  ASN A 178     -53.846  75.202 -29.002  1.00 45.76           C
ANISOU 1404  CG  ASN A 178     4242   4025   9122    643     -6  -1883       C
ATOM   1405  OD1 ASN A 178     -53.623  74.403 -29.911  1.00 50.96           O
ANISOU 1405  OD1 ASN A 178     4992   4700   9671    577     73  -1921       O
ATOM   1406  ND2 ASN A 178     -54.180  76.467 -29.225  1.00 48.54           N
ANISOU 1406  ND2 ASN A 178     4471   4411   9561    714     19  -2003       N
ATOM   1407  N   TYR A 179     -52.596  72.218 -25.696  1.00 38.74           N
ANISOU 1407  N   TYR A 179     3634   2927   8156    496   -313  -1310       N
ATOM   1408  CA  TYR A 179     -52.247  71.686 -24.388  1.00 38.82           C
ANISOU 1408  CA  TYR A 179     3716   2866   8166    462   -415  -1128       C
ATOM   1409  C   TYR A 179     -51.112  72.487 -23.765  1.00 36.03           C
ANISOU 1409  C   TYR A 179     3417   2374   7898    517   -541  -1072       C
ATOM   1410  O   TYR A 179     -50.197  72.937 -24.462  1.00 44.99           O
ANISOU 1410  O   TYR A 179     4581   3445   9070    542   -546  -1153       O
ATOM   1411  CB  TYR A 179     -51.856  70.210 -24.485  1.00 38.35           C
ANISOU 1411  CB  TYR A 179     3752   2815   8003    345   -383  -1055       C
ATOM   1412  CG  TYR A 179     -53.042  69.275 -24.552  1.00 35.02           C
ANISOU 1412  CG  TYR A 179     3317   2572   7415    275   -294  -1014       C
ATOM   1413  CD1 TYR A 179     -53.507  68.631 -23.412  1.00 30.83           C
ANISOU 1413  CD1 TYR A 179     2816   2087   6812    224   -321   -858       C
ATOM   1414  CD2 TYR A 179     -53.703  69.044 -25.751  1.00 34.12           C
ANISOU 1414  CD2 TYR A 179     3182   2571   7209    261   -180  -1132       C
ATOM   1415  CE1 TYR A 179     -54.593  67.778 -23.467  1.00 33.00           C
ANISOU 1415  CE1 TYR A 179     3093   2509   6938    167   -240   -824       C
ATOM   1416  CE2 TYR A 179     -54.790  68.195 -25.815  1.00 34.42           C
ANISOU 1416  CE2 TYR A 179     3236   2750   7090    201   -102  -1089       C
ATOM   1417  CZ  TYR A 179     -55.230  67.564 -24.670  1.00 34.17           C
ANISOU 1417  CZ  TYR A 179     3227   2755   7000    158   -135   -938       C
ATOM   1418  OH  TYR A 179     -56.311  66.717 -24.732  1.00 35.69           O
ANISOU 1418  OH  TYR A 179     3448   3073   7039    106    -59   -900       O
ATOM   1419  N   TYR A 180     -51.188  72.663 -22.448  1.00 36.15           N
ANISOU 1419  N   TYR A 180     3464   2337   7934    535   -644   -934       N
ATOM   1420  CA  TYR A 180     -50.192  73.397 -21.683  1.00 41.60           C
ANISOU 1420  CA  TYR A 180     4239   2883   8682    588   -773   -859       C
ATOM   1421  C   TYR A 180     -50.020  72.708 -20.338  1.00 44.57           C
ANISOU 1421  C   TYR A 180     4731   3206   8999    518   -840   -664       C
ATOM   1422  O   TYR A 180     -50.987  72.180 -19.781  1.00 49.75           O
ANISOU 1422  O   TYR A 180     5354   3941   9606    484   -824   -600       O
ATOM   1423  CB  TYR A 180     -50.605  74.861 -21.476  1.00 39.24           C
ANISOU 1423  CB  TYR A 180     3847   2580   8482    732   -852   -927       C
ATOM   1424  CG  TYR A 180     -51.079  75.563 -22.731  1.00 45.13           C
ANISOU 1424  CG  TYR A 180     4453   3416   9278    791   -760  -1128       C
ATOM   1425  CD1 TYR A 180     -52.409  75.491 -23.131  1.00 46.37           C
ANISOU 1425  CD1 TYR A 180     4475   3728   9417    780   -660  -1213       C
ATOM   1426  CD2 TYR A 180     -50.202  76.306 -23.509  1.00 44.58           C
ANISOU 1426  CD2 TYR A 180     4398   3274   9268    850   -761  -1235       C
ATOM   1427  CE1 TYR A 180     -52.847  76.132 -24.275  1.00 44.95           C
ANISOU 1427  CE1 TYR A 180     4180   3633   9265    815   -555  -1398       C
ATOM   1428  CE2 TYR A 180     -50.633  76.953 -24.652  1.00 44.09           C
ANISOU 1428  CE2 TYR A 180     4216   3295   9239    895   -664  -1420       C
ATOM   1429  CZ  TYR A 180     -51.955  76.861 -25.031  1.00 49.12           C
ANISOU 1429  CZ  TYR A 180     4723   4092   9849    872   -557  -1500       C
ATOM   1430  OH  TYR A 180     -52.386  77.503 -26.170  1.00 55.04           O
ANISOU 1430  OH  TYR A 180     5367   4927  10619    899   -442  -1685       O
ATOM   1431  N   LYS A 181     -48.794  72.715 -19.816  1.00 46.02           N
ANISOU 1431  N   LYS A 181     5059   3251   9176    488   -906   -574       N
ATOM   1432  CA  LYS A 181     -48.504  72.046 -18.556  1.00 44.08           C
ANISOU 1432  CA  LYS A 181     4946   2949   8852    401   -949   -391       C
ATOM   1433  C   LYS A 181     -47.496  72.854 -17.754  1.00 43.80           C
ANISOU 1433  C   LYS A 181     5059   2744   8838    449  -1067   -308       C
ATOM   1434  O   LYS A 181     -46.543  73.404 -18.311  1.00 41.23           O
ANISOU 1434  O   LYS A 181     4779   2319   8566    485  -1080   -375       O
ATOM   1435  CB  LYS A 181     -47.971  70.625 -18.786  1.00 40.37           C
ANISOU 1435  CB  LYS A 181     4532   2506   8300    241   -848   -352       C
ATOM   1436  CG  LYS A 181     -47.815  69.809 -17.511  1.00 37.43           C
ANISOU 1436  CG  LYS A 181     4280   2111   7832    131   -856   -176       C
ATOM   1437  CD  LYS A 181     -47.348  68.393 -17.806  1.00 37.56           C
ANISOU 1437  CD  LYS A 181     4311   2182   7777    -24   -748   -165       C
ATOM   1438  CE  LYS A 181     -47.204  67.586 -16.525  1.00 42.44           C
ANISOU 1438  CE  LYS A 181     5039   2791   8293   -141   -733     -2       C
ATOM   1439  NZ  LYS A 181     -46.717  66.202 -16.785  1.00 47.74           N
ANISOU 1439  NZ  LYS A 181     5701   3530   8907   -289   -626     -6       N
ATOM   1440  N   LYS A 182     -47.717  72.917 -16.442  1.00 41.57           N
ANISOU 1440  N   LYS A 182     4870   2422   8504    448  -1152   -162       N
ATOM   1441  CA  LYS A 182     -46.812  73.576 -15.512  1.00 42.20           C
ANISOU 1441  CA  LYS A 182     5132   2333   8569    484  -1265    -57       C
ATOM   1442  C   LYS A 182     -46.437  72.605 -14.405  1.00 41.91           C
ANISOU 1442  C   LYS A 182     5268   2256   8402    335  -1240    118       C
ATOM   1443  O   LYS A 182     -47.287  71.859 -13.909  1.00 54.22           O
ANISOU 1443  O   LYS A 182     6791   3922   9890    270  -1204    182       O
ATOM   1444  CB  LYS A 182     -47.444  74.834 -14.905  1.00 43.49           C
ANISOU 1444  CB  LYS A 182     5259   2480   8785    652  -1417    -57       C
ATOM   1445  CG  LYS A 182     -47.509  76.017 -15.851  1.00 69.87           C
ANISOU 1445  CG  LYS A 182     8463   5826  12258    806  -1450   -229       C
ATOM   1446  CD  LYS A 182     -48.224  77.196 -15.211  1.00 63.48           C
ANISOU 1446  CD  LYS A 182     7589   5030  11502    967  -1602   -240       C
ATOM   1447  CE  LYS A 182     -47.484  77.693 -13.981  1.00 58.94           C
ANISOU 1447  CE  LYS A 182     7233   4288  10875   1011  -1751    -92       C
ATOM   1448  NZ  LYS A 182     -48.234  78.775 -13.287  1.00 58.06           N
ANISOU 1448  NZ  LYS A 182     7055   4202  10804   1168  -1918   -101       N
ATOM   1449  N   VAL A 183     -45.163  72.615 -14.024  1.00 45.28           N
ANISOU 1449  N   VAL A 183     5886   2526   8791    274  -1246    188       N
ATOM   1450  CA  VAL A 183     -44.653  71.771 -12.949  1.00 48.69           C
ANISOU 1450  CA  VAL A 183     6503   2906   9091    120  -1203    346       C
ATOM   1451  C   VAL A 183     -43.903  72.659 -11.968  1.00 54.41           C
ANISOU 1451  C   VAL A 183     7451   3441   9782    176  -1316    452       C
ATOM   1452  O   VAL A 183     -42.926  73.317 -12.345  1.00 54.37           O
ANISOU 1452  O   VAL A 183     7529   3294   9835    222  -1343    410       O
ATOM   1453  CB  VAL A 183     -43.738  70.651 -13.473  1.00 50.84           C
ANISOU 1453  CB  VAL A 183     6804   3179   9334    -58  -1055    322       C
ATOM   1454  CG1 VAL A 183     -43.040  69.957 -12.316  1.00 51.96           C
ANISOU 1454  CG1 VAL A 183     7153   3243   9346   -219  -1000    472       C
ATOM   1455  CG2 VAL A 183     -44.542  69.648 -14.285  1.00 40.85           C
ANISOU 1455  CG2 VAL A 183     5337   2108   8076   -113   -951    238       C
ATOM   1456  N   ASP A 184     -44.362  72.677 -10.715  1.00 53.62           N
ANISOU 1456  N   ASP A 184     6232   4780   9360    763  -1865    843       N
ATOM   1457  CA  ASP A 184     -43.750  73.477  -9.653  1.00 61.30           C
ANISOU 1457  CA  ASP A 184     7245   5704  10343    818  -2031   1003       C
ATOM   1458  C   ASP A 184     -43.625  74.942 -10.065  1.00 59.79           C
ANISOU 1458  C   ASP A 184     7016   5340  10361    930  -2156    906       C
ATOM   1459  O   ASP A 184     -42.605  75.593  -9.831  1.00 62.52           O
ANISOU 1459  O   ASP A 184     7419   5568  10767    935  -2257   1013       O
ATOM   1460  CB  ASP A 184     -42.394  72.901  -9.242  1.00 71.85           C
ANISOU 1460  CB  ASP A 184     8677   6985  11640    726  -2060   1249       C
ATOM   1461  CG  ASP A 184     -42.523  71.564  -8.535  1.00 81.52           C
ANISOU 1461  CG  ASP A 184     9926   8412  12636    633  -1958   1362       C
ATOM   1462  OD1 ASP A 184     -43.537  71.357  -7.835  1.00 84.76           O
ANISOU 1462  OD1 ASP A 184    10300   9004  12900    669  -1934   1310       O
ATOM   1463  OD2 ASP A 184     -41.613  70.720  -8.680  1.00 83.68           O
ANISOU 1463  OD2 ASP A 184    10248   8664  12881    526  -1904   1494       O
ATOM   1464  N   GLY A 185     -44.681  75.463 -10.688  1.00 56.74           N
ANISOU 1464  N   GLY A 185     6533   4981  10044    997  -2113    679       N
ATOM   1465  CA  GLY A 185     -44.714  76.838 -11.134  1.00 55.94           C
ANISOU 1465  CA  GLY A 185     6382   4795  10078   1078  -2172    534       C
ATOM   1466  C   GLY A 185     -44.031  77.107 -12.455  1.00 54.03           C
ANISOU 1466  C   GLY A 185     6147   4434   9947   1042  -2107    428       C
ATOM   1467  O   GLY A 185     -44.182  78.210 -12.997  1.00 55.53           O
ANISOU 1467  O   GLY A 185     6279   4583  10237   1105  -2128    271       O
ATOM   1468  N   VAL A 186     -43.291  76.145 -12.997  1.00 52.98           N
ANISOU 1468  N   VAL A 186     6077   4256   9795    944  -2032    501       N
ATOM   1469  CA  VAL A 186     -42.543  76.326 -14.235  1.00 53.70           C
ANISOU 1469  CA  VAL A 186     6181   4247   9974    908  -1981    406       C
ATOM   1470  C   VAL A 186     -43.329  75.704 -15.380  1.00 48.90           C
ANISOU 1470  C   VAL A 186     5520   3701   9358    879  -1825    239       C
ATOM   1471  O   VAL A 186     -43.708  74.528 -15.317  1.00 45.25           O
ANISOU 1471  O   VAL A 186     5073   3305   8813    821  -1742    291       O
ATOM   1472  CB  VAL A 186     -41.140  75.705 -14.133  1.00 54.51           C
ANISOU 1472  CB  VAL A 186     6384   4261  10066    813  -2007    588       C
ATOM   1473  CG1 VAL A 186     -40.408  75.830 -15.461  1.00 54.76           C
ANISOU 1473  CG1 VAL A 186     6420   4204  10181    780  -1960    470       C
ATOM   1474  CG2 VAL A 186     -40.348  76.365 -13.015  1.00 55.69           C
ANISOU 1474  CG2 VAL A 186     6591   4346  10224    834  -2159    763       C
ATOM   1475  N   VAL A 187     -43.573  76.495 -16.426  1.00 46.19           N
ANISOU 1475  N   VAL A 187     5115   3340   9096    921  -1785     42       N
ATOM   1476  CA  VAL A 187     -44.224  75.979 -17.623  1.00 42.81           C
ANISOU 1476  CA  VAL A 187     4644   2969   8653    889  -1635   -111       C
ATOM   1477  C   VAL A 187     -43.322  74.947 -18.283  1.00 47.76           C
ANISOU 1477  C   VAL A 187     5349   3553   9246    794  -1574    -46       C
ATOM   1478  O   VAL A 187     -42.099  75.124 -18.368  1.00 58.88           O
ANISOU 1478  O   VAL A 187     6814   4862  10694    771  -1642     24       O
ATOM   1479  CB  VAL A 187     -44.555  77.128 -18.590  1.00 46.97           C
ANISOU 1479  CB  VAL A 187     5086   3492   9266    955  -1613   -320       C
ATOM   1480  CG1 VAL A 187     -45.299  76.605 -19.810  1.00 46.99           C
ANISOU 1480  CG1 VAL A 187     5046   3569   9240    920  -1452   -465       C
ATOM   1481  CG2 VAL A 187     -45.365  78.202 -17.881  1.00 50.61           C
ANISOU 1481  CG2 VAL A 187     5463   3995   9770   1047  -1685   -381       C
ATOM   1482  N   GLN A 188     -43.921  73.858 -18.749  1.00 45.93           N
ANISOU 1482  N   GLN A 188     5117   3392   8942    737  -1451    -72       N
ATOM   1483  CA  GLN A 188     -43.187  72.778 -19.386  1.00 49.31           C
ANISOU 1483  CA  GLN A 188     5611   3799   9327    646  -1387    -20       C
ATOM   1484  C   GLN A 188     -43.362  72.832 -20.898  1.00 51.44           C
ANISOU 1484  C   GLN A 188     5853   4084   9608    642  -1286   -198       C
ATOM   1485  O   GLN A 188     -44.382  73.301 -21.407  1.00 58.46           O
ANISOU 1485  O   GLN A 188     6671   5034  10507    687  -1220   -346       O
ATOM   1486  CB  GLN A 188     -43.655  71.419 -18.863  1.00 55.04           C
ANISOU 1486  CB  GLN A 188     6363   4594   9956    583  -1325     86       C
ATOM   1487  CG  GLN A 188     -43.583  71.286 -17.356  1.00 61.49           C
ANISOU 1487  CG  GLN A 188     7202   5420  10741    593  -1420    267       C
ATOM   1488  CD  GLN A 188     -42.178  71.480 -16.826  1.00 66.94           C
ANISOU 1488  CD  GLN A 188     7959   6020  11456    559  -1525    432       C
ATOM   1489  OE1 GLN A 188     -41.301  70.643 -17.039  1.00 69.65           O
ANISOU 1489  OE1 GLN A 188     8355   6333  11775    470  -1501    526       O
ATOM   1490  NE2 GLN A 188     -41.954  72.592 -16.134  1.00 68.05           N
ANISOU 1490  NE2 GLN A 188     8094   6116  11646    625  -1644    467       N
ATOM   1491  N   GLN A 189     -42.351  72.346 -21.611  1.00 49.46           N
ANISOU 1491  N   GLN A 189     5656   3783   9352    587  -1275   -180       N
ATOM   1492  CA  GLN A 189     -42.422  72.177 -23.057  1.00 53.49           C
ANISOU 1492  CA  GLN A 189     6158   4317   9849    577  -1181   -328       C
ATOM   1493  C   GLN A 189     -42.762  70.719 -23.340  1.00 48.75           C
ANISOU 1493  C   GLN A 189     5594   3782   9148    496  -1077   -287       C
ATOM   1494  O   GLN A 189     -41.968  69.820 -23.045  1.00 51.13           O
ANISOU 1494  O   GLN A 189     5952   4057   9417    426  -1098   -159       O
ATOM   1495  CB  GLN A 189     -41.111  72.577 -23.729  1.00 62.58           C
ANISOU 1495  CB  GLN A 189     7341   5375  11062    578  -1245   -354       C
ATOM   1496  CG  GLN A 189     -41.106  72.339 -25.233  1.00 72.01           C
ANISOU 1496  CG  GLN A 189     8532   6596  12231    573  -1157   -502       C
ATOM   1497  CD  GLN A 189     -39.874  72.900 -25.913  1.00 82.96           C
ANISOU 1497  CD  GLN A 189     9940   7889  13694    594  -1233   -556       C
ATOM   1498  OE1 GLN A 189     -39.028  73.526 -25.275  1.00 85.53           O
ANISOU 1498  OE1 GLN A 189    10279   8119  14099    611  -1353   -486       O
ATOM   1499  NE2 GLN A 189     -39.768  72.679 -27.218  1.00 86.41           N
ANISOU 1499  NE2 GLN A 189    10381   8347  14105    594  -1170   -683       N
ATOM   1500  N   LEU A 190     -43.943  70.488 -23.901  1.00 44.30           N
ANISOU 1500  N   LEU A 190     4991   3302   8537    503   -967   -392       N
ATOM   1501  CA  LEU A 190     -44.385  69.127 -24.154  1.00 39.71           C
ANISOU 1501  CA  LEU A 190     4444   2782   7862    432   -873   -360       C
ATOM   1502  C   LEU A 190     -43.619  68.535 -25.335  1.00 38.60           C
ANISOU 1502  C   LEU A 190     4350   2626   7689    389   -836   -398       C
ATOM   1503  O   LEU A 190     -43.359  69.231 -26.322  1.00 41.07           O
ANISOU 1503  O   LEU A 190     4648   2918   8038    428   -831   -521       O
ATOM   1504  CB  LEU A 190     -45.889  69.096 -24.421  1.00 40.70           C
ANISOU 1504  CB  LEU A 190     4517   2992   7955    448   -771   -459       C
ATOM   1505  CG  LEU A 190     -46.749  69.546 -23.237  1.00 39.23           C
ANISOU 1505  CG  LEU A 190     4278   2830   7798    490   -808   -430       C
ATOM   1506  CD1 LEU A 190     -48.228  69.505 -23.581  1.00 36.54           C
ANISOU 1506  CD1 LEU A 190     3880   2595   7409    486   -700   -533       C
ATOM   1507  CD2 LEU A 190     -46.460  68.694 -22.009  1.00 37.34           C
ANISOU 1507  CD2 LEU A 190     4083   2618   7485    446   -856   -259       C
ATOM   1508  N   PRO A 191     -43.244  67.262 -25.268  1.00 40.42           N
ANISOU 1508  N   PRO A 191     4632   2869   7855    315   -816   -304       N
ATOM   1509  CA  PRO A 191     -42.391  66.676 -26.304  1.00 44.15           C
ANISOU 1509  CA  PRO A 191     5148   3321   8304    275   -803   -333       C
ATOM   1510  C   PRO A 191     -43.180  66.326 -27.558  1.00 41.96           C
ANISOU 1510  C   PRO A 191     4871   3106   7964    278   -695   -463       C
ATOM   1511  O   PRO A 191     -44.411  66.327 -27.580  1.00 41.16           O
ANISOU 1511  O   PRO A 191     4742   3068   7831    292   -618   -511       O
ATOM   1512  CB  PRO A 191     -41.846  65.415 -25.628  1.00 42.83           C
ANISOU 1512  CB  PRO A 191     5021   3158   8096    194   -819   -179       C
ATOM   1513  CG  PRO A 191     -42.946  65.009 -24.705  1.00 37.83           C
ANISOU 1513  CG  PRO A 191     4367   2587   7420    192   -779   -123       C
ATOM   1514  CD  PRO A 191     -43.560  66.293 -24.202  1.00 36.65           C
ANISOU 1514  CD  PRO A 191     4170   2427   7330    268   -811   -170       C
ATOM   1515  N   GLU A 192     -42.432  66.029 -28.621  1.00 42.33           N
ANISOU 1515  N   GLU A 192     4954   3132   7999    263   -694   -518       N
ATOM   1516  CA  GLU A 192     -43.035  65.460 -29.817  1.00 38.00           C
ANISOU 1516  CA  GLU A 192     4424   2638   7377    255   -600   -617       C
ATOM   1517  C   GLU A 192     -43.693  64.133 -29.471  1.00 34.38           C
ANISOU 1517  C   GLU A 192     3990   2239   6835    194   -543   -533       C
ATOM   1518  O   GLU A 192     -43.092  63.284 -28.809  1.00 40.01           O
ANISOU 1518  O   GLU A 192     4725   2942   7536    143   -584   -415       O
ATOM   1519  CB  GLU A 192     -41.982  65.250 -30.905  1.00 34.33           C
ANISOU 1519  CB  GLU A 192     3998   2133   6913    248   -631   -678       C
ATOM   1520  CG  GLU A 192     -41.518  66.513 -31.602  1.00 35.20           C
ANISOU 1520  CG  GLU A 192     4085   2197   7094    320   -669   -809       C
ATOM   1521  CD  GLU A 192     -40.706  66.211 -32.847  1.00 42.44           C
ANISOU 1521  CD  GLU A 192     5041   3089   7994    319   -684   -900       C
ATOM   1522  OE1 GLU A 192     -40.588  65.020 -33.203  1.00 40.43           O
ANISOU 1522  OE1 GLU A 192     4832   2857   7673    263   -663   -864       O
ATOM   1523  OE2 GLU A 192     -40.187  67.162 -33.469  1.00 50.01           O
ANISOU 1523  OE2 GLU A 192     5984   4007   9010    380   -725  -1016       O
ATOM   1524  N   THR A 193     -44.933  63.955 -29.917  1.00 30.31           N
ANISOU 1524  N   THR A 193     3466   1783   6267    200   -448   -597       N
ATOM   1525  CA  THR A 193     -45.676  62.753 -29.576  1.00 32.05           C
ANISOU 1525  CA  THR A 193     3707   2055   6414    151   -397   -528       C
ATOM   1526  C   THR A 193     -46.576  62.347 -30.731  1.00 35.66           C
ANISOU 1526  C   THR A 193     4187   2588   6774    141   -297   -606       C
ATOM   1527  O   THR A 193     -47.111  63.198 -31.448  1.00 32.60           O
ANISOU 1527  O   THR A 193     3775   2217   6395    175   -244   -712       O
ATOM   1528  CB  THR A 193     -46.519  62.951 -28.309  1.00 29.76           C
ANISOU 1528  CB  THR A 193     3374   1816   6116    156   -393   -462       C
ATOM   1529  OG1 THR A 193     -47.332  61.793 -28.088  1.00 32.45           O
ANISOU 1529  OG1 THR A 193     3734   2247   6348    114   -336   -411       O
ATOM   1530  CG2 THR A 193     -47.411  64.172 -28.441  1.00 29.02           C
ANISOU 1530  CG2 THR A 193     3224   1737   6065    206   -355   -559       C
ATOM   1531  N   TYR A 194     -46.718  61.038 -30.913  1.00 35.76           N
ANISOU 1531  N   TYR A 194     4245   2649   6694     95   -273   -551       N
ATOM   1532  CA  TYR A 194     -47.792  60.505 -31.727  1.00 31.33           C
ANISOU 1532  CA  TYR A 194     3711   2164   6028     79   -182   -586       C
ATOM   1533  C   TYR A 194     -49.071  60.440 -30.899  1.00 31.58           C
ANISOU 1533  C   TYR A 194     3712   2253   6033     68   -138   -545       C
ATOM   1534  O   TYR A 194     -49.061  60.608 -29.677  1.00 32.56           O
ANISOU 1534  O   TYR A 194     3800   2372   6199     74   -180   -487       O
ATOM   1535  CB  TYR A 194     -47.434  59.118 -32.260  1.00 28.68           C
ANISOU 1535  CB  TYR A 194     3437   1849   5612     44   -190   -547       C
ATOM   1536  CG  TYR A 194     -46.272  59.093 -33.228  1.00 31.40           C
ANISOU 1536  CG  TYR A 194     3814   2143   5972     51   -235   -604       C
ATOM   1537  CD1 TYR A 194     -46.456  59.393 -34.572  1.00 30.99           C
ANISOU 1537  CD1 TYR A 194     3792   2113   5868     70   -189   -706       C
ATOM   1538  CD2 TYR A 194     -44.995  58.751 -32.802  1.00 31.82           C
ANISOU 1538  CD2 TYR A 194     3866   2133   6091     34   -325   -555       C
ATOM   1539  CE1 TYR A 194     -45.398  59.365 -35.463  1.00 34.07           C
ANISOU 1539  CE1 TYR A 194     4213   2462   6270     83   -239   -774       C
ATOM   1540  CE2 TYR A 194     -43.930  58.719 -33.686  1.00 34.07           C
ANISOU 1540  CE2 TYR A 194     4178   2363   6404     37   -378   -616       C
ATOM   1541  CZ  TYR A 194     -44.137  59.026 -35.015  1.00 35.64           C
ANISOU 1541  CZ  TYR A 194     4408   2583   6549     67   -338   -734       C
ATOM   1542  OH  TYR A 194     -43.081  58.996 -35.897  1.00 35.89           O
ANISOU 1542  OH  TYR A 194     4468   2565   6606     77   -400   -811       O
ATOM   1543  N   PHE A 195     -50.186  60.191 -31.576  1.00 30.85           N
ANISOU 1543  N   PHE A 195     3636   2214   5869     50    -55   -574       N
ATOM   1544  CA  PHE A 195     -51.470  60.058 -30.906  1.00 28.36           C
ANISOU 1544  CA  PHE A 195     3297   1943   5537     32    -16   -545       C
ATOM   1545  C   PHE A 195     -52.189  58.817 -31.404  1.00 32.07           C
ANISOU 1545  C   PHE A 195     3827   2449   5910     -4     24   -510       C
ATOM   1546  O   PHE A 195     -52.208  58.539 -32.607  1.00 29.84           O
ANISOU 1546  O   PHE A 195     3595   2177   5567    -17     64   -536       O
ATOM   1547  CB  PHE A 195     -52.350  61.294 -31.121  1.00 28.12           C
ANISOU 1547  CB  PHE A 195     3205   1930   5549     43     45   -620       C
ATOM   1548  CG  PHE A 195     -51.842  62.523 -30.430  1.00 29.70           C
ANISOU 1548  CG  PHE A 195     3336   2094   5855     90     -7   -654       C
ATOM   1549  CD1 PHE A 195     -51.711  62.550 -29.052  1.00 26.74           C
ANISOU 1549  CD1 PHE A 195     2931   1707   5522    104    -78   -592       C
ATOM   1550  CD2 PHE A 195     -51.502  63.653 -31.155  1.00 27.84           C
ANISOU 1550  CD2 PHE A 195     3064   1842   5672    127     11   -750       C
ATOM   1551  CE1 PHE A 195     -51.243  63.680 -28.409  1.00 27.27           C
ANISOU 1551  CE1 PHE A 195     2941   1736   5685    152   -137   -613       C
ATOM   1552  CE2 PHE A 195     -51.034  64.788 -30.518  1.00 28.37           C
ANISOU 1552  CE2 PHE A 195     3067   1865   5847    181    -50   -784       C
ATOM   1553  CZ  PHE A 195     -50.905  64.802 -29.144  1.00 32.02           C
ANISOU 1553  CZ  PHE A 195     3507   2306   6353    192   -128   -709       C
ATOM   1554  N   THR A 196     -52.769  58.070 -30.470  1.00 33.67           N
ANISOU 1554  N   THR A 196     4027   2670   6098    -15      5   -452       N
ATOM   1555  CA  THR A 196     -53.618  56.951 -30.838  1.00 31.20           C
ANISOU 1555  CA  THR A 196     3766   2378   5711    -42     33   -423       C
ATOM   1556  C   THR A 196     -54.933  57.464 -31.418  1.00 30.26           C
ANISOU 1556  C   THR A 196     3642   2268   5588    -71    113   -456       C
ATOM   1557  O   THR A 196     -55.376  58.580 -31.135  1.00 29.33           O
ANISOU 1557  O   THR A 196     3459   2153   5530    -70    140   -498       O
ATOM   1558  CB  THR A 196     -53.879  56.050 -29.630  1.00 31.28           C
ANISOU 1558  CB  THR A 196     3765   2406   5713    -34    -14   -371       C
ATOM   1559  OG1 THR A 196     -54.309  56.847 -28.520  1.00 31.28           O
ANISOU 1559  OG1 THR A 196     3699   2415   5772    -21    -27   -382       O
ATOM   1560  CG2 THR A 196     -52.616  55.299 -29.247  1.00 24.15           C
ANISOU 1560  CG2 THR A 196     2870   1510   4795    -20    -77   -326       C
ATOM   1561  N   GLN A 197     -55.557  56.630 -32.247  1.00 30.07           N
ANISOU 1561  N   GLN A 197     3685   2248   5492   -100    147   -432       N
ATOM   1562  CA  GLN A 197     -56.738  57.037 -32.995  1.00 29.59           C
ANISOU 1562  CA  GLN A 197     3631   2196   5416   -144    230   -444       C
ATOM   1563  C   GLN A 197     -58.046  56.769 -32.261  1.00 29.26           C
ANISOU 1563  C   GLN A 197     3571   2138   5411   -173    233   -420       C
ATOM   1564  O   GLN A 197     -59.082  57.302 -32.671  1.00 33.58           O
ANISOU 1564  O   GLN A 197     4100   2686   5974   -221    301   -429       O
ATOM   1565  CB  GLN A 197     -56.758  56.337 -34.356  1.00 32.58           C
ANISOU 1565  CB  GLN A 197     4101   2585   5694   -165    263   -419       C
ATOM   1566  CG  GLN A 197     -55.563  56.678 -35.228  1.00 32.13           C
ANISOU 1566  CG  GLN A 197     4062   2548   5598   -137    263   -464       C
ATOM   1567  CD  GLN A 197     -55.481  58.158 -35.547  1.00 38.64           C
ANISOU 1567  CD  GLN A 197     4820   3399   6463   -132    323   -543       C
ATOM   1568  OE1 GLN A 197     -56.480  58.785 -35.899  1.00 44.46           O
ANISOU 1568  OE1 GLN A 197     5528   4165   7199   -169    406   -556       O
ATOM   1569  NE2 GLN A 197     -54.289  58.727 -35.416  1.00 40.66           N
ANISOU 1569  NE2 GLN A 197     5044   3642   6764    -86    278   -596       N
ATOM   1570  N   SER A 198     -58.024  55.956 -31.202  1.00 26.63           N
ANISOU 1570  N   SER A 198     3237   1791   5091   -147    161   -394       N
ATOM   1571  CA  SER A 198     -59.193  55.726 -30.349  1.00 28.17           C
ANISOU 1571  CA  SER A 198     3407   1966   5329   -162    145   -392       C
ATOM   1572  C   SER A 198     -60.371  55.151 -31.135  1.00 34.41           C
ANISOU 1572  C   SER A 198     4259   2719   6098   -214    184   -359       C
ATOM   1573  O   SER A 198     -61.529  55.497 -30.892  1.00 38.20           O
ANISOU 1573  O   SER A 198     4707   3172   6634   -256    207   -369       O
ATOM   1574  CB  SER A 198     -59.607  57.009 -29.625  1.00 27.95           C
ANISOU 1574  CB  SER A 198     3283   1951   5387   -166    158   -442       C
ATOM   1575  OG  SER A 198     -58.524  57.561 -28.899  1.00 30.69           O
ANISOU 1575  OG  SER A 198     3582   2323   5756   -115    113   -459       O
ATOM   1576  N   ARG A 199     -60.081  54.264 -32.080  1.00 35.40           N
ANISOU 1576  N   ARG A 199     4471   2835   6143   -216    184   -316       N
ATOM   1577  CA  ARG A 199     -61.126  53.600 -32.843  1.00 37.23           C
ANISOU 1577  CA  ARG A 199     4777   3021   6346   -262    207   -265       C
ATOM   1578  C   ARG A 199     -61.487  52.262 -32.197  1.00 42.38           C
ANISOU 1578  C   ARG A 199     5469   3627   7004   -228    122   -243       C
ATOM   1579  O   ARG A 199     -60.851  51.812 -31.241  1.00 44.07           O
ANISOU 1579  O   ARG A 199     5651   3865   7228   -169     57   -268       O
ATOM   1580  CB  ARG A 199     -60.684  53.407 -34.295  1.00 33.58           C
ANISOU 1580  CB  ARG A 199     4395   2581   5785   -277    249   -229       C
ATOM   1581  CG  ARG A 199     -60.568  54.710 -35.072  1.00 33.14           C
ANISOU 1581  CG  ARG A 199     4301   2576   5715   -312    344   -261       C
ATOM   1582  CD  ARG A 199     -59.902  54.516 -36.425  1.00 34.63           C
ANISOU 1582  CD  ARG A 199     4565   2805   5790   -308    374   -247       C
ATOM   1583  NE  ARG A 199     -58.472  54.247 -36.301  1.00 33.60           N
ANISOU 1583  NE  ARG A 199     4435   2694   5639   -242    309   -282       N
ATOM   1584  CZ  ARG A 199     -57.613  54.291 -37.314  1.00 32.25           C
ANISOU 1584  CZ  ARG A 199     4305   2561   5386   -225    319   -303       C
ATOM   1585  NH1 ARG A 199     -58.036  54.597 -38.533  1.00 30.15           N
ANISOU 1585  NH1 ARG A 199     4085   2335   5034   -261    396   -292       N
ATOM   1586  NH2 ARG A 199     -56.329  54.030 -37.109  1.00 32.77           N
ANISOU 1586  NH2 ARG A 199     4364   2630   5456   -173    250   -336       N
ATOM   1587  N   ASN A 200     -62.535  51.629 -32.722  1.00 42.80           N
ANISOU 1587  N   ASN A 200     5591   3617   7055   -266    122   -195       N
ATOM   1588  CA  ASN A 200     -62.974  50.330 -32.236  1.00 43.76           C
ANISOU 1588  CA  ASN A 200     5756   3681   7189   -227     36   -182       C
ATOM   1589  C   ASN A 200     -63.197  49.386 -33.411  1.00 41.15           C
ANISOU 1589  C   ASN A 200     5539   3304   6790   -238     24   -107       C
ATOM   1590  O   ASN A 200     -63.292  49.808 -34.566  1.00 39.24           O
ANISOU 1590  O   ASN A 200     5346   3073   6492   -292     92    -58       O
ATOM   1591  CB  ASN A 200     -64.253  50.436 -31.390  1.00 47.55           C
ANISOU 1591  CB  ASN A 200     6200   4096   7770   -252     14   -208       C
ATOM   1592  CG  ASN A 200     -65.417  51.015 -32.162  1.00 54.08           C
ANISOU 1592  CG  ASN A 200     7051   4864   8634   -352     82   -161       C
ATOM   1593  OD1 ASN A 200     -66.044  50.330 -32.969  1.00 58.52           O
ANISOU 1593  OD1 ASN A 200     7704   5356   9174   -386     76    -89       O
ATOM   1594  ND2 ASN A 200     -65.721  52.283 -31.911  1.00 55.64           N
ANISOU 1594  ND2 ASN A 200     7162   5092   8888   -402    146   -197       N
ATOM   1595  N   LEU A 201     -63.291  48.094 -33.090  1.00 45.22           N
ANISOU 1595  N   LEU A 201     6097   3777   7307   -180    -67   -103       N
ATOM   1596  CA  LEU A 201     -63.336  47.055 -34.117  1.00 46.88           C
ANISOU 1596  CA  LEU A 201     6415   3947   7450   -167   -105    -36       C
ATOM   1597  C   LEU A 201     -64.598  47.153 -34.965  1.00 51.74           C
ANISOU 1597  C   LEU A 201     7110   4474   8075   -248    -71     46       C
ATOM   1598  O   LEU A 201     -64.529  47.220 -36.198  1.00 58.75           O
ANISOU 1598  O   LEU A 201     8073   5375   8875   -287    -27    118       O
ATOM   1599  CB  LEU A 201     -63.242  45.675 -33.467  1.00 44.77           C
ANISOU 1599  CB  LEU A 201     6158   3651   7200    -77   -217    -63       C
ATOM   1600  CG  LEU A 201     -61.857  45.220 -33.018  1.00 42.58           C
ANISOU 1600  CG  LEU A 201     5828   3468   6881     -1   -255   -111       C
ATOM   1601  CD1 LEU A 201     -61.914  43.793 -32.510  1.00 41.70           C
ANISOU 1601  CD1 LEU A 201     5725   3335   6785     86   -359   -138       C
ATOM   1602  CD2 LEU A 201     -60.884  45.341 -34.171  1.00 44.41           C
ANISOU 1602  CD2 LEU A 201     6102   3752   7019    -12   -226    -74       C
ATOM   1603  N   GLN A 202     -65.765  47.140 -34.316  1.00 48.38           N
ANISOU 1603  N   GLN A 202     6669   3959   7752   -277    -94     39       N
ATOM   1604  CA  GLN A 202     -67.027  47.107 -35.048  1.00 59.20           C
ANISOU 1604  CA  GLN A 202     8117   5226   9151   -363    -74    130       C
ATOM   1605  C   GLN A 202     -67.164  48.298 -35.986  1.00 59.73           C
ANISOU 1605  C   GLN A 202     8178   5347   9168   -467     57    183       C
ATOM   1606  O   GLN A 202     -67.636  48.157 -37.119  1.00 62.36           O
ANISOU 1606  O   GLN A 202     8603   5650   9439   -529     93    288       O
ATOM   1607  CB  GLN A 202     -68.196  47.069 -34.064  1.00 72.93           C
ANISOU 1607  CB  GLN A 202     9818   6861  11032   -384   -122     91       C
ATOM   1608  CG  GLN A 202     -68.349  45.751 -33.327  1.00 84.29           C
ANISOU 1608  CG  GLN A 202    11282   8225  12519   -284   -257     45       C
ATOM   1609  CD  GLN A 202     -69.042  44.695 -34.166  1.00 92.77           C
ANISOU 1609  CD  GLN A 202    12486   9172  13592   -289   -325    142       C
ATOM   1610  OE1 GLN A 202     -69.623  44.997 -35.209  1.00 96.49           O
ANISOU 1610  OE1 GLN A 202    13031   9595  14037   -385   -269    255       O
ATOM   1611  NE2 GLN A 202     -68.987  43.449 -33.712  1.00 93.19           N
ANISOU 1611  NE2 GLN A 202    12567   9173  13670   -182   -447     98       N
ATOM   1612  N   GLU A 203     -66.745  49.478 -35.535  1.00 57.04           N
ANISOU 1612  N   GLU A 203     7730   5094   8849   -482    129    112       N
ATOM   1613  CA  GLU A 203     -66.948  50.720 -36.268  1.00 57.91           C
ANISOU 1613  CA  GLU A 203     7806   5265   8932   -573    258    136       C
ATOM   1614  C   GLU A 203     -65.636  51.312 -36.772  1.00 49.15           C
ANISOU 1614  C   GLU A 203     6671   4281   7721   -534    312     95       C
ATOM   1615  O   GLU A 203     -65.487  52.534 -36.838  1.00 51.88           O
ANISOU 1615  O   GLU A 203     6936   4700   8077   -569    401     52       O
ATOM   1616  CB  GLU A 203     -67.684  51.728 -35.388  1.00 71.03           C
ANISOU 1616  CB  GLU A 203     9353   6915  10722   -626    294     77       C
ATOM   1617  CG  GLU A 203     -68.992  51.207 -34.811  1.00 84.82           C
ANISOU 1617  CG  GLU A 203    11114   8527  12587   -666    230     98       C
ATOM   1618  CD  GLU A 203     -69.252  51.707 -33.402  1.00 93.09           C
ANISOU 1618  CD  GLU A 203    12046   9568  13758   -643    190    -12       C
ATOM   1619  OE1 GLU A 203     -68.707  51.112 -32.448  1.00 95.24           O
ANISOU 1619  OE1 GLU A 203    12302   9847  14039   -542     99    -82       O
ATOM   1620  OE2 GLU A 203     -69.994  52.699 -33.248  1.00 95.63           O
ANISOU 1620  OE2 GLU A 203    12287   9887  14162   -726    250    -28       O
ATOM   1621  N   PHE A 204     -64.677  50.462 -37.130  1.00 42.47           N
ANISOU 1621  N   PHE A 204     5889   3459   6787   -460    253    101       N
ATOM   1622  CA  PHE A 204     -63.387  50.953 -37.594  1.00 39.96           C
ANISOU 1622  CA  PHE A 204     5551   3246   6387   -421    286     54       C
ATOM   1623  C   PHE A 204     -63.530  51.601 -38.964  1.00 39.37           C
ANISOU 1623  C   PHE A 204     5517   3233   6208   -485    392     99       C
ATOM   1624  O   PHE A 204     -64.142  51.033 -39.873  1.00 45.62           O
ANISOU 1624  O   PHE A 204     6410   3996   6926   -526    400    196       O
ATOM   1625  CB  PHE A 204     -62.370  49.815 -37.654  1.00 44.39           C
ANISOU 1625  CB  PHE A 204     6165   3814   6888   -334    189     49       C
ATOM   1626  CG  PHE A 204     -60.950  50.280 -37.821  1.00 47.77           C
ANISOU 1626  CG  PHE A 204     6552   4329   7268   -289    198    -18       C
ATOM   1627  CD1 PHE A 204     -60.443  50.578 -39.077  1.00 48.02           C
ANISOU 1627  CD1 PHE A 204     6633   4423   7187   -300    246     -9       C
ATOM   1628  CD2 PHE A 204     -60.122  50.421 -36.720  1.00 46.13           C
ANISOU 1628  CD2 PHE A 204     6260   4141   7128   -237    154    -88       C
ATOM   1629  CE1 PHE A 204     -59.140  51.009 -39.229  1.00 45.42           C
ANISOU 1629  CE1 PHE A 204     6268   4159   6830   -257    242    -82       C
ATOM   1630  CE2 PHE A 204     -58.817  50.849 -36.868  1.00 44.18           C
ANISOU 1630  CE2 PHE A 204     5978   3953   6854   -203    153   -141       C
ATOM   1631  CZ  PHE A 204     -58.326  51.143 -38.123  1.00 44.75           C
ANISOU 1631  CZ  PHE A 204     6099   4073   6830   -212    193   -144       C
ATOM   1632  N   LYS A 205     -62.959  52.796 -39.110  1.00 36.34           N
ANISOU 1632  N   LYS A 205     5056   2938   5815   -490    471     29       N
ATOM   1633  CA  LYS A 205     -62.993  53.527 -40.365  1.00 45.22           C
ANISOU 1633  CA  LYS A 205     6200   4148   6834   -538    582     45       C
ATOM   1634  C   LYS A 205     -61.571  53.970 -40.708  1.00 39.79           C
ANISOU 1634  C   LYS A 205     5487   3546   6084   -468    581    -47       C
ATOM   1635  O   LYS A 205     -60.866  54.508 -39.837  1.00 36.39           O
ANISOU 1635  O   LYS A 205     4967   3120   5740   -421    553   -135       O
ATOM   1636  CB  LYS A 205     -63.929  54.741 -40.281  1.00 54.07           C
ANISOU 1636  CB  LYS A 205     7229   5295   8020   -624    696     35       C
ATOM   1637  CG  LYS A 205     -65.240  54.468 -39.558  1.00 59.99           C
ANISOU 1637  CG  LYS A 205     7966   5941   8886   -689    676     92       C
ATOM   1638  CD  LYS A 205     -66.420  55.086 -40.286  1.00 66.84           C
ANISOU 1638  CD  LYS A 205     8825   6827   9742   -812    797    165       C
ATOM   1639  CE  LYS A 205     -66.677  54.377 -41.605  1.00 70.07           C
ANISOU 1639  CE  LYS A 205     9373   7247  10003   -853    823    288       C
ATOM   1640  NZ  LYS A 205     -66.911  52.919 -41.406  1.00 67.96           N
ANISOU 1640  NZ  LYS A 205     9222   6856   9744   -821    694    367       N
ATOM   1641  N   PRO A 206     -61.120  53.763 -41.941  1.00 39.02           N
ANISOU 1641  N   PRO A 206     5470   3514   5843   -459    602    -30       N
ATOM   1642  CA  PRO A 206     -59.758  54.173 -42.300  1.00 39.71           C
ANISOU 1642  CA  PRO A 206     5535   3671   5880   -392    590   -131       C
ATOM   1643  C   PRO A 206     -59.637  55.685 -42.389  1.00 44.41           C
ANISOU 1643  C   PRO A 206     6026   4342   6504   -404    692   -224       C
ATOM   1644  O   PRO A 206     -60.565  56.384 -42.802  1.00 46.49           O
ANISOU 1644  O   PRO A 206     6262   4653   6750   -474    804   -200       O
ATOM   1645  CB  PRO A 206     -59.541  53.514 -43.667  1.00 33.29           C
ANISOU 1645  CB  PRO A 206     4844   2911   4895   -385    586    -83       C
ATOM   1646  CG  PRO A 206     -60.916  53.401 -44.238  1.00 43.44           C
ANISOU 1646  CG  PRO A 206     6187   4194   6124   -474    662     36       C
ATOM   1647  CD  PRO A 206     -61.831  53.141 -43.071  1.00 40.42           C
ANISOU 1647  CD  PRO A 206     5765   3699   5892   -509    631     83       C
ATOM   1648  N   ARG A 207     -58.467  56.189 -41.993  1.00 42.22           N
ANISOU 1648  N   ARG A 207     5687   4076   6280   -335    650   -332       N
ATOM   1649  CA  ARG A 207     -58.206  57.624 -41.978  1.00 38.17           C
ANISOU 1649  CA  ARG A 207     5068   3620   5814   -324    723   -438       C
ATOM   1650  C   ARG A 207     -57.027  58.008 -42.867  1.00 37.71           C
ANISOU 1650  C   ARG A 207     5023   3630   5675   -263    720   -539       C
ATOM   1651  O   ARG A 207     -56.482  59.107 -42.727  1.00 38.86           O
ANISOU 1651  O   ARG A 207     5081   3803   5883   -224    742   -650       O
ATOM   1652  CB  ARG A 207     -57.981  58.107 -40.544  1.00 37.69           C
ANISOU 1652  CB  ARG A 207     4905   3496   5920   -296    670   -483       C
ATOM   1653  CG  ARG A 207     -59.223  57.999 -39.672  1.00 42.20           C
ANISOU 1653  CG  ARG A 207     5442   4016   6578   -355    683   -415       C
ATOM   1654  CD  ARG A 207     -58.944  58.372 -38.225  1.00 43.63           C
ANISOU 1654  CD  ARG A 207     5533   4143   6903   -318    616   -457       C
ATOM   1655  NE  ARG A 207     -60.158  58.310 -37.414  1.00 45.20           N
ANISOU 1655  NE  ARG A 207     5694   4298   7182   -370    624   -411       N
ATOM   1656  CZ  ARG A 207     -60.186  58.443 -36.092  1.00 45.15           C
ANISOU 1656  CZ  ARG A 207     5623   4247   7286   -346    560   -431       C
ATOM   1657  NH1 ARG A 207     -59.062  58.641 -35.418  1.00 46.41           N
ANISOU 1657  NH1 ARG A 207     5748   4398   7486   -276    489   -479       N
ATOM   1658  NH2 ARG A 207     -61.339  58.372 -35.442  1.00 45.08           N
ANISOU 1658  NH2 ARG A 207     5583   4200   7345   -394    563   -401       N
ATOM   1659  N   SER A 208     -56.625  57.126 -43.779  1.00 33.21           N
ANISOU 1659  N   SER A 208     4561   3084   4973   -247    682   -510       N
ATOM   1660  CA  SER A 208     -55.577  57.435 -44.741  1.00 33.91           C
ANISOU 1660  CA  SER A 208     4671   3243   4970   -190    675   -613       C
ATOM   1661  C   SER A 208     -55.701  56.473 -45.911  1.00 34.76           C
ANISOU 1661  C   SER A 208     4908   3402   4898   -200    668   -547       C
ATOM   1662  O   SER A 208     -56.263  55.382 -45.782  1.00 46.43           O
ANISOU 1662  O   SER A 208     6460   4828   6352   -230    624   -426       O
ATOM   1663  CB  SER A 208     -54.181  57.342 -44.117  1.00 35.61           C
ANISOU 1663  CB  SER A 208     4856   3388   5284   -119    553   -693       C
ATOM   1664  OG  SER A 208     -53.791  55.991 -43.934  1.00 39.04           O
ANISOU 1664  OG  SER A 208     5366   3764   5704   -108    444   -624       O
ATOM   1665  N   GLN A 209     -55.165  56.894 -47.060  1.00 35.96           N
ANISOU 1665  N   GLN A 209     5085   3657   4920   -167    703   -634       N
ATOM   1666  CA  GLN A 209     -55.180  56.033 -48.239  1.00 36.95           C
ANISOU 1666  CA  GLN A 209     5337   3847   4855   -166    687   -581       C
ATOM   1667  C   GLN A 209     -54.419  54.738 -47.990  1.00 43.93           C
ANISOU 1667  C   GLN A 209     6288   4647   5757   -124    530   -550       C
ATOM   1668  O   GLN A 209     -54.784  53.689 -48.533  1.00 45.29           O
ANISOU 1668  O   GLN A 209     6566   4824   5818   -136    491   -449       O
ATOM   1669  CB  GLN A 209     -54.593  56.773 -49.442  1.00 42.04           C
ANISOU 1669  CB  GLN A 209     5988   4627   5358   -122    741   -709       C
ATOM   1670  CG  GLN A 209     -54.645  55.988 -50.745  1.00 44.71           C
ANISOU 1670  CG  GLN A 209     6459   5058   5473   -118    731   -659       C
ATOM   1671  CD  GLN A 209     -56.059  55.812 -51.268  1.00 48.64           C
ANISOU 1671  CD  GLN A 209     7017   5617   5846   -207    844   -501       C
ATOM   1672  OE1 GLN A 209     -56.862  56.745 -51.246  1.00 50.37           O
ANISOU 1672  OE1 GLN A 209     7166   5895   6076   -264    983   -493       O
ATOM   1673  NE2 GLN A 209     -56.371  54.611 -51.741  1.00 49.33           N
ANISOU 1673  NE2 GLN A 209     7234   5688   5823   -221    780   -372       N
ATOM   1674  N   MET A 210     -53.367  54.790 -47.170  1.00 34.91           N
ANISOU 1674  N   MET A 210     5081   3427   4755    -76    437   -631       N
ATOM   1675  CA  MET A 210     -52.657  53.570 -46.806  1.00 42.83           C
ANISOU 1675  CA  MET A 210     6123   4354   5794    -45    296   -600       C
ATOM   1676  C   MET A 210     -53.562  52.621 -46.031  1.00 46.89           C
ANISOU 1676  C   MET A 210     6662   4795   6359    -83    271   -460       C
ATOM   1677  O   MET A 210     -53.578  51.412 -46.292  1.00 46.50           O
ANISOU 1677  O   MET A 210     6690   4726   6250    -71    191   -392       O
ATOM   1678  CB  MET A 210     -51.410  53.915 -45.992  1.00 39.74           C
ANISOU 1678  CB  MET A 210     5647   3895   5557     -4    215   -700       C
ATOM   1679  CG  MET A 210     -50.578  52.710 -45.591  1.00 43.58           C
ANISOU 1679  CG  MET A 210     6152   4316   6090     20     77   -675       C
ATOM   1680  SD  MET A 210     -49.203  53.144 -44.509  1.00 48.54           S
ANISOU 1680  SD  MET A 210     6675   4856   6911     45     -7   -758       S
ATOM   1681  CE  MET A 210     -48.254  54.221 -45.580  1.00 47.48           C
ANISOU 1681  CE  MET A 210     6536   4769   6735     91     -2   -927       C
ATOM   1682  N   GLU A 211     -54.330  53.153 -45.075  1.00 51.26           N
ANISOU 1682  N   GLU A 211     7145   5306   7025   -123    331   -426       N
ATOM   1683  CA  GLU A 211     -55.280  52.320 -44.346  1.00 32.03           C
ANISOU 1683  CA  GLU A 211     4730   2798   4640   -157    309   -309       C
ATOM   1684  C   GLU A 211     -56.389  51.822 -45.261  1.00 41.53           C
ANISOU 1684  C   GLU A 211     6038   4030   5712   -202    355   -200       C
ATOM   1685  O   GLU A 211     -56.836  50.676 -45.136  1.00 43.93           O
ANISOU 1685  O   GLU A 211     6408   4276   6007   -202    286   -107       O
ATOM   1686  CB  GLU A 211     -55.867  53.096 -43.168  1.00 31.30           C
ANISOU 1686  CB  GLU A 211     4537   2662   4692   -189    361   -311       C
ATOM   1687  CG  GLU A 211     -54.860  53.456 -42.094  1.00 39.02           C
ANISOU 1687  CG  GLU A 211     5423   3599   5805   -148    302   -388       C
ATOM   1688  CD  GLU A 211     -55.520  53.943 -40.821  1.00 41.42           C
ANISOU 1688  CD  GLU A 211     5643   3856   6241   -173    326   -371       C
ATOM   1689  OE1 GLU A 211     -56.686  54.384 -40.885  1.00 44.27           O
ANISOU 1689  OE1 GLU A 211     5994   4226   6600   -225    410   -334       O
ATOM   1690  OE2 GLU A 211     -54.876  53.875 -39.753  1.00 43.91           O
ANISOU 1690  OE2 GLU A 211     5899   4127   6658   -143    260   -393       O
ATOM   1691  N   ILE A 212     -56.851  52.671 -46.182  1.00 39.25           N
ANISOU 1691  N   ILE A 212     5762   3831   5320   -239    471   -207       N
ATOM   1692  CA  ILE A 212     -57.849  52.241 -47.155  1.00 39.18           C
ANISOU 1692  CA  ILE A 212     5859   3859   5167   -291    521    -88       C
ATOM   1693  C   ILE A 212     -57.299  51.106 -48.006  1.00 40.00           C
ANISOU 1693  C   ILE A 212     6080   3981   5138   -241    418    -58       C
ATOM   1694  O   ILE A 212     -57.978  50.098 -48.239  1.00 42.50           O
ANISOU 1694  O   ILE A 212     6492   4251   5405   -257    370     65       O
ATOM   1695  CB  ILE A 212     -58.300  53.432 -48.022  1.00 47.34           C
ANISOU 1695  CB  ILE A 212     6871   5016   6099   -340    675   -112       C
ATOM   1696  CG1 ILE A 212     -58.999  54.487 -47.163  1.00 48.48           C
ANISOU 1696  CG1 ILE A 212     6894   5140   6386   -395    772   -131       C
ATOM   1697  CG2 ILE A 212     -59.218  52.964 -49.141  1.00 48.78           C
ANISOU 1697  CG2 ILE A 212     7175   5254   6107   -397    727     24       C
ATOM   1698  CD1 ILE A 212     -59.413  55.724 -47.931  1.00 48.94           C
ANISOU 1698  CD1 ILE A 212     6902   5330   6363   -440    930   -171       C
ATOM   1699  N   ASP A 213     -56.057  51.244 -48.474  1.00 41.63           N
ANISOU 1699  N   ASP A 213     6279   4246   5293   -175    371   -176       N
ATOM   1700  CA  ASP A 213     -55.441  50.175 -49.251  1.00 41.79           C
ANISOU 1700  CA  ASP A 213     6398   4286   5196   -122    258   -165       C
ATOM   1701  C   ASP A 213     -55.164  48.947 -48.395  1.00 40.32           C
ANISOU 1701  C   ASP A 213     6211   3988   5120    -86    120   -128       C
ATOM   1702  O   ASP A 213     -55.229  47.819 -48.896  1.00 40.85           O
ANISOU 1702  O   ASP A 213     6371   4043   5105    -59     29    -60       O
ATOM   1703  CB  ASP A 213     -54.152  50.672 -49.903  1.00 44.00           C
ANISOU 1703  CB  ASP A 213     6657   4647   5414    -63    233   -318       C
ATOM   1704  CG  ASP A 213     -54.405  51.726 -50.963  1.00 49.82           C
ANISOU 1704  CG  ASP A 213     7408   5521   6000    -81    363   -365       C
ATOM   1705  OD1 ASP A 213     -55.587  52.007 -51.252  1.00 50.74           O
ANISOU 1705  OD1 ASP A 213     7554   5676   6048   -149    476   -262       O
ATOM   1706  OD2 ASP A 213     -53.423  52.273 -51.507  1.00 52.08           O
ANISOU 1706  OD2 ASP A 213     7672   5877   6238    -29    352   -510       O
ATOM   1707  N   PHE A 214     -54.858  49.139 -47.109  1.00 38.77           N
ANISOU 1707  N   PHE A 214     5909   3717   5104    -82    100   -171       N
ATOM   1708  CA  PHE A 214     -54.608  47.997 -46.236  1.00 38.85           C
ANISOU 1708  CA  PHE A 214     5905   3642   5215    -48    -18   -142       C
ATOM   1709  C   PHE A 214     -55.843  47.115 -46.118  1.00 41.96           C
ANISOU 1709  C   PHE A 214     6370   3974   5601    -70    -36     -9       C
ATOM   1710  O   PHE A 214     -55.743  45.883 -46.158  1.00 47.85           O
ANISOU 1710  O   PHE A 214     7165   4682   6334    -26   -147     32       O
ATOM   1711  CB  PHE A 214     -54.161  48.475 -44.855  1.00 35.81           C
ANISOU 1711  CB  PHE A 214     5394   3205   5007    -47    -18   -201       C
ATOM   1712  CG  PHE A 214     -54.000  47.365 -43.854  1.00 34.14           C
ANISOU 1712  CG  PHE A 214     5152   2925   4895    -17   -119   -172       C
ATOM   1713  CD1 PHE A 214     -52.827  46.634 -43.793  1.00 32.20           C
ANISOU 1713  CD1 PHE A 214     4884   2683   4667     32   -225   -221       C
ATOM   1714  CD2 PHE A 214     -55.025  47.052 -42.976  1.00 34.76           C
ANISOU 1714  CD2 PHE A 214     5217   2939   5050    -37   -108   -103       C
ATOM   1715  CE1 PHE A 214     -52.679  45.612 -42.875  1.00 34.81           C
ANISOU 1715  CE1 PHE A 214     5173   2971   5083     60   -308   -199       C
ATOM   1716  CE2 PHE A 214     -54.884  46.032 -42.057  1.00 33.95           C
ANISOU 1716  CE2 PHE A 214     5081   2790   5030      0   -196    -91       C
ATOM   1717  CZ  PHE A 214     -53.709  45.311 -42.006  1.00 34.57           C
ANISOU 1717  CZ  PHE A 214     5131   2888   5117     49   -291   -137       C
ATOM   1718  N   LEU A 215     -57.017  47.727 -45.972  1.00 41.98           N
ANISOU 1718  N   LEU A 215     6373   3957   5619   -136     67     56       N
ATOM   1719  CA  LEU A 215     -58.246  46.959 -45.827  1.00 43.63           C
ANISOU 1719  CA  LEU A 215     6650   4085   5842   -165     47    182       C
ATOM   1720  C   LEU A 215     -58.730  46.395 -47.156  1.00 46.01           C
ANISOU 1720  C   LEU A 215     7093   4417   5972   -175     34    284       C
ATOM   1721  O   LEU A 215     -59.300  45.299 -47.186  1.00 47.56           O
ANISOU 1721  O   LEU A 215     7368   4536   6167   -159    -52    378       O
ATOM   1722  CB  LEU A 215     -59.330  47.833 -45.196  1.00 44.22           C
ANISOU 1722  CB  LEU A 215     6670   4124   6009   -243    155    214       C
ATOM   1723  CG  LEU A 215     -58.986  48.377 -43.807  1.00 44.59           C
ANISOU 1723  CG  LEU A 215     6583   4138   6222   -232    159    126       C
ATOM   1724  CD1 LEU A 215     -59.986  49.440 -43.378  1.00 44.90           C
ANISOU 1724  CD1 LEU A 215     6562   4166   6334   -310    273    140       C
ATOM   1725  CD2 LEU A 215     -58.936  47.241 -42.796  1.00 40.74           C
ANISOU 1725  CD2 LEU A 215     6080   3564   5835   -180     42    134       C
ATOM   1726  N   GLU A 216     -58.510  47.116 -48.256  1.00 49.28           N
ANISOU 1726  N   GLU A 216     7542   4944   6237   -196    114    266       N
ATOM   1727  CA  GLU A 216     -58.992  46.654 -49.552  1.00 56.58           C
ANISOU 1727  CA  GLU A 216     8607   5916   6975   -210    111    374       C
ATOM   1728  C   GLU A 216     -58.073  45.595 -50.149  1.00 57.54           C
ANISOU 1728  C   GLU A 216     8798   6060   7005   -120    -33    349       C
ATOM   1729  O   GLU A 216     -58.538  44.540 -50.595  1.00 60.96           O
ANISOU 1729  O   GLU A 216     9341   6450   7373   -101   -121    458       O
ATOM   1730  CB  GLU A 216     -59.135  47.836 -50.513  1.00 66.00           C
ANISOU 1730  CB  GLU A 216     9808   7246   8025   -265    260    359       C
ATOM   1731  CG  GLU A 216     -60.267  48.791 -50.176  1.00 77.08           C
ANISOU 1731  CG  GLU A 216    11158   8638   9489   -368    407    416       C
ATOM   1732  CD  GLU A 216     -60.394  49.922 -51.181  1.00 86.35           C
ANISOU 1732  CD  GLU A 216    12328   9970  10510   -417    561    396       C
ATOM   1733  OE1 GLU A 216     -59.408  50.200 -51.897  1.00 87.88           O
ANISOU 1733  OE1 GLU A 216    12527  10279  10586   -358    556    288       O
ATOM   1734  OE2 GLU A 216     -61.483  50.531 -51.259  1.00 88.42           O
ANISOU 1734  OE2 GLU A 216    12577  10246  10774   -516    686    482       O
ATOM   1735  N   LEU A 217     -56.770  45.856 -50.164  1.00 55.03           N
ANISOU 1735  N   LEU A 217     8415   5803   6690    -64    -68    204       N
ATOM   1736  CA  LEU A 217     -55.830  44.969 -50.830  1.00 54.43           C
ANISOU 1736  CA  LEU A 217     8394   5765   6524     15   -201    163       C
ATOM   1737  C   LEU A 217     -55.529  43.746 -49.968  1.00 54.71           C
ANISOU 1737  C   LEU A 217     8398   5698   6692     72   -345    166       C
ATOM   1738  O   LEU A 217     -55.867  43.680 -48.782  1.00 55.11           O
ANISOU 1738  O   LEU A 217     8373   5661   6907     57   -338    174       O
ATOM   1739  CB  LEU A 217     -54.534  45.708 -51.157  1.00 51.38           C
ANISOU 1739  CB  LEU A 217     7944   5469   6108     48   -193     -1       C
ATOM   1740  CG  LEU A 217     -54.659  46.992 -51.976  1.00 49.23           C
ANISOU 1740  CG  LEU A 217     7679   5316   5710     10    -51    -46       C
ATOM   1741  CD1 LEU A 217     -53.297  47.645 -52.145  1.00 44.27           C
ANISOU 1741  CD1 LEU A 217     6978   4748   5094     58    -71   -229       C
ATOM   1742  CD2 LEU A 217     -55.296  46.707 -53.327  1.00 51.53           C
ANISOU 1742  CD2 LEU A 217     8114   5699   5767     -1    -30     56       C
ATOM   1743  N   ALA A 218     -54.880  42.764 -50.589  1.00 55.21           N
ANISOU 1743  N   ALA A 218     8516   5785   6677    141   -478    151       N
ATOM   1744  CA  ALA A 218     -54.415  41.583 -49.885  1.00 55.72           C
ANISOU 1744  CA  ALA A 218     8535   5779   6856    206   -619    131       C
ATOM   1745  C   ALA A 218     -53.063  41.858 -49.229  1.00 58.08           C
ANISOU 1745  C   ALA A 218     8701   6099   7270    227   -645    -15       C
ATOM   1746  O   ALA A 218     -52.432  42.894 -49.451  1.00 63.35           O
ANISOU 1746  O   ALA A 218     9326   6824   7918    204   -577   -105       O
ATOM   1747  CB  ALA A 218     -54.318  40.392 -50.838  1.00 55.15           C
ANISOU 1747  CB  ALA A 218     8571   5725   6659    273   -759    179       C
ATOM   1748  N   MET A 219     -52.614  40.902 -48.413  1.00 54.61           N
ANISOU 1748  N   MET A 219     8190   5607   6952    272   -749    -39       N
ATOM   1749  CA  MET A 219     -51.383  41.092 -47.651  1.00 51.22           C
ANISOU 1749  CA  MET A 219     7627   5187   6649    279   -773   -154       C
ATOM   1750  C   MET A 219     -50.175  41.217 -48.572  1.00 50.08           C
ANISOU 1750  C   MET A 219     7486   5115   6426    303   -833   -255       C
ATOM   1751  O   MET A 219     -49.411  42.184 -48.482  1.00 48.86           O
ANISOU 1751  O   MET A 219     7271   4985   6311    276   -783   -347       O
ATOM   1752  CB  MET A 219     -51.194  39.939 -46.667  1.00 51.25           C
ANISOU 1752  CB  MET A 219     7553   5141   6779    321   -868   -150       C
ATOM   1753  CG  MET A 219     -49.911  40.024 -45.861  1.00 54.03           C
ANISOU 1753  CG  MET A 219     7764   5507   7258    317   -895   -248       C
ATOM   1754  SD  MET A 219     -49.804  38.748 -44.594  1.00 55.54           S
ANISOU 1754  SD  MET A 219     7847   5668   7590    360   -976   -241       S
ATOM   1755  CE  MET A 219     -49.724  37.274 -45.607  1.00 57.67           C
ANISOU 1755  CE  MET A 219     8188   5957   7769    445  -1136   -230       C
ATOM   1756  N   ASP A 220     -49.985  40.242 -49.464  1.00 55.46           N
ANISOU 1756  N   ASP A 220     8241   5829   7002    360   -952   -246       N
ATOM   1757  CA  ASP A 220     -48.835  40.273 -50.362  1.00 60.38           C
ANISOU 1757  CA  ASP A 220     8868   6523   7551    389  -1028   -354       C
ATOM   1758  C   ASP A 220     -48.883  41.485 -51.282  1.00 61.85           C
ANISOU 1758  C   ASP A 220     9120   6780   7602    361   -930   -394       C
ATOM   1759  O   ASP A 220     -47.846  42.087 -51.585  1.00 62.57           O
ANISOU 1759  O   ASP A 220     9166   6909   7698    363   -942   -521       O
ATOM   1760  CB  ASP A 220     -48.772  38.983 -51.179  1.00 67.76           C
ANISOU 1760  CB  ASP A 220     9878   7484   8385    460  -1179   -328       C
ATOM   1761  CG  ASP A 220     -48.422  37.774 -50.335  1.00 72.76           C
ANISOU 1761  CG  ASP A 220    10418   8068   9159    500  -1292   -331       C
ATOM   1762  OD1 ASP A 220     -47.984  37.959 -49.180  1.00 72.50           O
ANISOU 1762  OD1 ASP A 220    10255   7998   9292    469  -1257   -369       O
ATOM   1763  OD2 ASP A 220     -48.588  36.639 -50.828  1.00 75.34           O
ANISOU 1763  OD2 ASP A 220    10799   8401   9427    566  -1416   -295       O
ATOM   1764  N   GLU A 221     -50.080  41.861 -51.735  1.00 62.34           N
ANISOU 1764  N   GLU A 221     9280   6860   7546    334   -833   -291       N
ATOM   1765  CA  GLU A 221     -50.203  43.002 -52.636  1.00 63.60           C
ANISOU 1765  CA  GLU A 221     9494   7109   7562    308   -725   -328       C
ATOM   1766  C   GLU A 221     -49.953  44.314 -51.902  1.00 55.90           C
ANISOU 1766  C   GLU A 221     8413   6117   6709    260   -604   -407       C
ATOM   1767  O   GLU A 221     -49.377  45.249 -52.470  1.00 54.26           O
ANISOU 1767  O   GLU A 221     8194   5978   6445    263   -560   -518       O
ATOM   1768  CB  GLU A 221     -51.584  43.000 -53.290  1.00 72.95           C
ANISOU 1768  CB  GLU A 221    10805   8321   8590    279   -649   -179       C
ATOM   1769  CG  GLU A 221     -51.749  44.005 -54.415  1.00 83.21           C
ANISOU 1769  CG  GLU A 221    12172   9746   9696    258   -542   -207       C
ATOM   1770  CD  GLU A 221     -53.102  43.897 -55.091  1.00 91.62           C
ANISOU 1770  CD  GLU A 221    13367  10844  10602    218   -470    -36       C
ATOM   1771  OE1 GLU A 221     -53.946  43.115 -54.606  1.00 93.54           O
ANISOU 1771  OE1 GLU A 221    13644  10988  10908    204   -505    101       O
ATOM   1772  OE2 GLU A 221     -53.321  44.591 -56.106  1.00 95.72           O
ANISOU 1772  OE2 GLU A 221    13950  11487  10930    200   -380    -38       O
ATOM   1773  N   PHE A 222     -50.372  44.399 -50.638  1.00 51.77           N
ANISOU 1773  N   PHE A 222     7810   5505   6354    224   -558   -358       N
ATOM   1774  CA  PHE A 222     -50.175  45.627 -49.873  1.00 51.18           C
ANISOU 1774  CA  PHE A 222     7635   5409   6402    183   -455   -423       C
ATOM   1775  C   PHE A 222     -48.710  45.818 -49.499  1.00 51.84           C
ANISOU 1775  C   PHE A 222     7621   5473   6602    205   -528   -558       C
ATOM   1776  O   PHE A 222     -48.178  46.930 -49.601  1.00 51.85           O
ANISOU 1776  O   PHE A 222     7579   5495   6627    198   -474   -659       O
ATOM   1777  CB  PHE A 222     -51.051  45.610 -48.621  1.00 49.51           C
ANISOU 1777  CB  PHE A 222     7372   5113   6327    143   -399   -333       C
ATOM   1778  CG  PHE A 222     -50.876  46.814 -47.742  1.00 50.72           C
ANISOU 1778  CG  PHE A 222     7419   5241   6610    107   -307   -391       C
ATOM   1779  CD1 PHE A 222     -51.539  47.996 -48.025  1.00 53.40           C
ANISOU 1779  CD1 PHE A 222     7763   5621   6904     68   -173   -394       C
ATOM   1780  CD2 PHE A 222     -50.053  46.764 -46.628  1.00 50.00           C
ANISOU 1780  CD2 PHE A 222     7221   5091   6686    112   -356   -438       C
ATOM   1781  CE1 PHE A 222     -51.383  49.106 -47.217  1.00 52.74           C
ANISOU 1781  CE1 PHE A 222     7580   5513   6946     44   -100   -452       C
ATOM   1782  CE2 PHE A 222     -49.891  47.871 -45.818  1.00 49.29           C
ANISOU 1782  CE2 PHE A 222     7041   4974   6712     84   -284   -483       C
ATOM   1783  CZ  PHE A 222     -50.557  49.044 -46.112  1.00 48.97           C
ANISOU 1783  CZ  PHE A 222     7007   4967   6631     55   -161   -494       C
ATOM   1784  N   ILE A 223     -48.045  44.748 -49.058  1.00 48.26           N
ANISOU 1784  N   ILE A 223     7128   4978   6230    231   -653   -560       N
ATOM   1785  CA  ILE A 223     -46.641  44.851 -48.671  1.00 44.26           C
ANISOU 1785  CA  ILE A 223     6525   4444   5848    237   -728   -672       C
ATOM   1786  C   ILE A 223     -45.775  45.208 -49.872  1.00 44.36           C
ANISOU 1786  C   ILE A 223     6576   4518   5759    269   -778   -797       C
ATOM   1787  O   ILE A 223     -44.787  45.941 -49.741  1.00 46.24           O
ANISOU 1787  O   ILE A 223     6748   4733   6087    262   -791   -910       O
ATOM   1788  CB  ILE A 223     -46.186  43.540 -47.999  1.00 40.82           C
ANISOU 1788  CB  ILE A 223     6032   3969   5510    253   -844   -640       C
ATOM   1789  CG1 ILE A 223     -46.986  43.301 -46.716  1.00 37.54           C
ANISOU 1789  CG1 ILE A 223     5565   3498   5200    228   -790   -541       C
ATOM   1790  CG2 ILE A 223     -44.696  43.571 -47.695  1.00 38.54           C
ANISOU 1790  CG2 ILE A 223     5642   3654   5346    246   -927   -744       C
ATOM   1791  CD1 ILE A 223     -46.643  42.011 -46.009  1.00 34.77           C
ANISOU 1791  CD1 ILE A 223     5148   3126   4937    250   -889   -514       C
ATOM   1792  N   GLU A 224     -46.136  44.720 -51.061  1.00 49.01           N
ANISOU 1792  N   GLU A 224     7278   5185   6160    305   -813   -781       N
ATOM   1793  CA  GLU A 224     -45.376  45.062 -52.258  1.00 52.88           C
ANISOU 1793  CA  GLU A 224     7812   5752   6530    343   -861   -911       C
ATOM   1794  C   GLU A 224     -45.590  46.517 -52.654  1.00 52.66           C
ANISOU 1794  C   GLU A 224     7793   5773   6441    331   -730   -980       C
ATOM   1795  O   GLU A 224     -44.640  47.205 -53.046  1.00 53.59           O
ANISOU 1795  O   GLU A 224     7880   5907   6575    352   -757  -1132       O
ATOM   1796  CB  GLU A 224     -45.762  44.134 -53.410  1.00 57.23           C
ANISOU 1796  CB  GLU A 224     8486   6384   6876    390   -935   -864       C
ATOM   1797  CG  GLU A 224     -45.125  44.502 -54.740  1.00 65.88           C
ANISOU 1797  CG  GLU A 224     9643   7582   7806    436   -979   -997       C
ATOM   1798  CD  GLU A 224     -45.673  43.686 -55.894  1.00 77.38           C
ANISOU 1798  CD  GLU A 224    11237   9134   9031    480  -1036   -929       C
ATOM   1799  OE1 GLU A 224     -46.525  42.806 -55.649  1.00 80.17           O
ANISOU 1799  OE1 GLU A 224    11637   9456   9369    476  -1052   -776       O
ATOM   1800  OE2 GLU A 224     -45.254  43.927 -57.046  1.00 81.60           O
ANISOU 1800  OE2 GLU A 224    11836   9774   9396    523  -1072  -1030       O
ATOM   1801  N   ARG A 225     -46.829  47.004 -52.554  1.00 53.21           N
ANISOU 1801  N   ARG A 225     7899   5866   6451    297   -591   -878       N
ATOM   1802  CA  ARG A 225     -47.131  48.361 -52.999  1.00 57.13           C
ANISOU 1802  CA  ARG A 225     8398   6433   6877    286   -456   -942       C
ATOM   1803  C   ARG A 225     -46.390  49.400 -52.168  1.00 54.65           C
ANISOU 1803  C   ARG A 225     7963   6047   6753    276   -430  -1052       C
ATOM   1804  O   ARG A 225     -45.856  50.375 -52.710  1.00 57.25           O
ANISOU 1804  O   ARG A 225     8275   6423   7054    303   -402  -1193       O
ATOM   1805  CB  ARG A 225     -48.639  48.609 -52.943  1.00 61.13           C
ANISOU 1805  CB  ARG A 225     8950   6968   7307    237   -314   -796       C
ATOM   1806  CG  ARG A 225     -49.037  50.051 -53.214  1.00 66.63           C
ANISOU 1806  CG  ARG A 225     9619   7737   7958    216   -158   -855       C
ATOM   1807  CD  ARG A 225     -50.527  50.172 -53.470  1.00 71.22           C
ANISOU 1807  CD  ARG A 225    10262   8373   8424    160    -26   -706       C
ATOM   1808  NE  ARG A 225     -50.949  49.314 -54.572  1.00 80.02           N
ANISOU 1808  NE  ARG A 225    11513   9569   9324    173    -64   -619       N
ATOM   1809  CZ  ARG A 225     -52.182  49.282 -55.066  1.00 87.33           C
ANISOU 1809  CZ  ARG A 225    12520  10553  10110    124     34   -476       C
ATOM   1810  NH1 ARG A 225     -53.123  50.065 -54.558  1.00 87.71           N
ANISOU 1810  NH1 ARG A 225    12518  10588  10219     54    178   -413       N
ATOM   1811  NH2 ARG A 225     -52.473  48.466 -56.070  1.00 90.91           N
ANISOU 1811  NH2 ARG A 225    13103  11074  10364    141    -18   -391       N
ATOM   1812  N   TYR A 226     -46.342  49.211 -50.852  1.00 49.89           N
ANISOU 1812  N   TYR A 226     7278   5333   6344    242   -442   -991       N
ATOM   1813  CA  TYR A 226     -45.693  50.159 -49.958  1.00 48.12           C
ANISOU 1813  CA  TYR A 226     6946   5031   6306    229   -424  -1067       C
ATOM   1814  C   TYR A 226     -44.279  49.734 -49.581  1.00 52.18           C
ANISOU 1814  C   TYR A 226     7399   5466   6961    240   -566  -1144       C
ATOM   1815  O   TYR A 226     -43.704  50.297 -48.644  1.00 54.31           O
ANISOU 1815  O   TYR A 226     7579   5648   7408    220   -571  -1171       O
ATOM   1816  CB  TYR A 226     -46.549  50.368 -48.708  1.00 45.26           C
ANISOU 1816  CB  TYR A 226     6528   4607   6060    180   -340   -952       C
ATOM   1817  CG  TYR A 226     -47.838  51.109 -48.996  1.00 43.49           C
ANISOU 1817  CG  TYR A 226     6335   4448   5739    156   -190   -900       C
ATOM   1818  CD1 TYR A 226     -47.920  52.487 -48.838  1.00 40.80           C
ANISOU 1818  CD1 TYR A 226     5934   4120   5449    152    -93   -975       C
ATOM   1819  CD2 TYR A 226     -48.966  50.434 -49.444  1.00 43.22           C
ANISOU 1819  CD2 TYR A 226     6389   4462   5570    136   -151   -777       C
ATOM   1820  CE1 TYR A 226     -49.092  53.169 -49.107  1.00 41.45           C
ANISOU 1820  CE1 TYR A 226     6029   4271   5449    122     48   -931       C
ATOM   1821  CE2 TYR A 226     -50.142  51.108 -49.717  1.00 42.60           C
ANISOU 1821  CE2 TYR A 226     6334   4441   5411     99    -12   -720       C
ATOM   1822  CZ  TYR A 226     -50.199  52.475 -49.546  1.00 43.73           C
ANISOU 1822  CZ  TYR A 226     6404   4607   5605     89     92   -800       C
ATOM   1823  OH  TYR A 226     -51.367  53.148 -49.816  1.00 52.51           O
ANISOU 1823  OH  TYR A 226     7523   5786   6644     45    235   -746       O
ATOM   1824  N   LYS A 227     -43.711  48.758 -50.294  1.00 55.84           N
ANISOU 1824  N   LYS A 227     7907   5958   7351    269   -684  -1174       N
ATOM   1825  CA  LYS A 227     -42.300  48.388 -50.166  1.00 56.81           C
ANISOU 1825  CA  LYS A 227     7972   6018   7596    276   -825  -1266       C
ATOM   1826  C   LYS A 227     -41.946  48.028 -48.724  1.00 50.47           C
ANISOU 1826  C   LYS A 227     7067   5109   6999    226   -852  -1188       C
ATOM   1827  O   LYS A 227     -40.951  48.496 -48.166  1.00 51.21           O
ANISOU 1827  O   LYS A 227     7082   5120   7254    205   -897  -1249       O
ATOM   1828  CB  LYS A 227     -41.397  49.509 -50.689  1.00 66.11           C
ANISOU 1828  CB  LYS A 227     9129   7184   8805    302   -841  -1441       C
ATOM   1829  CG  LYS A 227     -41.817  50.062 -52.043  1.00 76.41           C
ANISOU 1829  CG  LYS A 227    10523   8614   9895    354   -786  -1530       C
ATOM   1830  CD  LYS A 227     -41.716  49.005 -53.130  1.00 85.66           C
ANISOU 1830  CD  LYS A 227    11782   9873  10893    392   -882  -1542       C
ATOM   1831  CE  LYS A 227     -42.259  49.520 -54.454  1.00 92.82           C
ANISOU 1831  CE  LYS A 227    12785  10927  11554    439   -811  -1605       C
ATOM   1832  NZ  LYS A 227     -43.726  49.773 -54.396  1.00 95.10           N
ANISOU 1832  NZ  LYS A 227    13121  11281  11731    410   -651  -1462       N
ATOM   1833  N   LEU A 228     -42.775  47.179 -48.119  1.00 46.74           N
ANISOU 1833  N   LEU A 228     6600   4643   6518    209   -828  -1049       N
ATOM   1834  CA  LEU A 228     -42.636  46.819 -46.715  1.00 46.53           C
ANISOU 1834  CA  LEU A 228     6479   4544   6656    167   -833   -966       C
ATOM   1835  C   LEU A 228     -41.953  45.471 -46.514  1.00 46.59           C
ANISOU 1835  C   LEU A 228     6445   4544   6714    166   -957   -946       C
ATOM   1836  O   LEU A 228     -42.109  44.858 -45.453  1.00 49.70           O
ANISOU 1836  O   LEU A 228     6774   4915   7196    141   -954   -858       O
ATOM   1837  CB  LEU A 228     -44.006  46.823 -46.036  1.00 47.40           C
ANISOU 1837  CB  LEU A 228     6606   4663   6743    153   -724   -842       C
ATOM   1838  CG  LEU A 228     -44.643  48.199 -45.839  1.00 46.84           C
ANISOU 1838  CG  LEU A 228     6534   4586   6678    138   -597   -850       C
ATOM   1839  CD1 LEU A 228     -46.110  48.066 -45.467  1.00 50.17           C
ANISOU 1839  CD1 LEU A 228     6990   5026   7047    124   -503   -734       C
ATOM   1840  CD2 LEU A 228     -43.889  48.974 -44.772  1.00 45.10           C
ANISOU 1840  CD2 LEU A 228     6212   4286   6636    109   -596   -877       C
ATOM   1841  N   GLU A 229     -41.200  44.998 -47.505  1.00 47.18           N
ANISOU 1841  N   GLU A 229     6546   4647   6732    194  -1065  -1035       N
ATOM   1842  CA  GLU A 229     -40.483  43.738 -47.359  1.00 51.32           C
ANISOU 1842  CA  GLU A 229     7015   5170   7316    192  -1190  -1030       C
ATOM   1843  C   GLU A 229     -39.404  43.867 -46.289  1.00 47.37           C
ANISOU 1843  C   GLU A 229     6385   4592   7022    131  -1222  -1037       C
ATOM   1844  O   GLU A 229     -38.656  44.849 -46.260  1.00 48.01           O
ANISOU 1844  O   GLU A 229     6439   4612   7190    105  -1223  -1112       O
ATOM   1845  CB  GLU A 229     -39.859  43.316 -48.689  1.00 59.24           C
ANISOU 1845  CB  GLU A 229     8071   6220   8218    236  -1308  -1139       C
ATOM   1846  CG  GLU A 229     -40.854  43.025 -49.803  1.00 67.81           C
ANISOU 1846  CG  GLU A 229     9290   7396   9080    297  -1293  -1116       C
ATOM   1847  CD  GLU A 229     -41.075  44.215 -50.718  1.00 78.00           C
ANISOU 1847  CD  GLU A 229    10663   8727  10246    318  -1222  -1196       C
ATOM   1848  OE1 GLU A 229     -41.631  45.230 -50.254  1.00 80.09           O
ANISOU 1848  OE1 GLU A 229    10923   8970  10536    293  -1093  -1168       O
ATOM   1849  OE2 GLU A 229     -40.681  44.137 -51.901  1.00 83.96           O
ANISOU 1849  OE2 GLU A 229    11482   9544  10876    363  -1296  -1296       O
ATOM   1850  N   GLY A 230     -39.328  42.873 -45.409  1.00 42.46           N
ANISOU 1850  N   GLY A 230     5683   3972   6479    107  -1250   -957       N
ATOM   1851  CA  GLY A 230     -38.326  42.852 -44.365  1.00 44.04           C
ANISOU 1851  CA  GLY A 230     5756   4116   6862     39  -1276   -940       C
ATOM   1852  C   GLY A 230     -38.723  43.512 -43.065  1.00 45.54           C
ANISOU 1852  C   GLY A 230     5900   4269   7136     -1  -1167   -850       C
ATOM   1853  O   GLY A 230     -37.872  43.653 -42.178  1.00 51.75           O
ANISOU 1853  O   GLY A 230     6589   5006   8067    -64  -1182   -824       O
ATOM   1854  N   TYR A 231     -39.982  43.922 -42.919  1.00 41.39           N
ANISOU 1854  N   TYR A 231     5440   3765   6522     28  -1063   -796       N
ATOM   1855  CA  TYR A 231     -40.456  44.566 -41.703  1.00 38.80           C
ANISOU 1855  CA  TYR A 231     5071   3408   6262     -3   -965   -717       C
ATOM   1856  C   TYR A 231     -41.451  43.716 -40.925  1.00 39.20           C
ANISOU 1856  C   TYR A 231     5106   3509   6279     14   -921   -620       C
ATOM   1857  O   TYR A 231     -41.989  44.187 -39.917  1.00 38.93           O
ANISOU 1857  O   TYR A 231     5044   3463   6284     -4   -841   -559       O
ATOM   1858  CB  TYR A 231     -41.077  45.928 -42.037  1.00 38.97           C
ANISOU 1858  CB  TYR A 231     5163   3406   6238     12   -877   -748       C
ATOM   1859  CG  TYR A 231     -40.080  46.925 -42.585  1.00 44.48           C
ANISOU 1859  CG  TYR A 231     5860   4044   6995      3   -915   -854       C
ATOM   1860  CD1 TYR A 231     -39.293  47.690 -41.733  1.00 43.96           C
ANISOU 1860  CD1 TYR A 231     5723   3897   7081    -43   -920   -848       C
ATOM   1861  CD2 TYR A 231     -39.920  47.098 -43.954  1.00 51.08           C
ANISOU 1861  CD2 TYR A 231     6771   4905   7732     44   -954   -961       C
ATOM   1862  CE1 TYR A 231     -38.377  48.601 -42.228  1.00 43.43           C
ANISOU 1862  CE1 TYR A 231     5658   3758   7086    -44   -968   -952       C
ATOM   1863  CE2 TYR A 231     -39.006  48.007 -44.460  1.00 51.92           C
ANISOU 1863  CE2 TYR A 231     6876   4956   7897     46   -996  -1078       C
ATOM   1864  CZ  TYR A 231     -38.238  48.756 -43.592  1.00 48.01           C
ANISOU 1864  CZ  TYR A 231     6307   4363   7571      3  -1006  -1076       C
ATOM   1865  OH  TYR A 231     -37.327  49.662 -44.088  1.00 44.74           O
ANISOU 1865  OH  TYR A 231     5893   3876   7231     11  -1061  -1199       O
ATOM   1866  N   ALA A 232     -41.715  42.485 -41.372  1.00 39.40           N
ANISOU 1866  N   ALA A 232     5149   3587   6236     54   -980   -614       N
ATOM   1867  CA  ALA A 232     -42.514  41.509 -40.625  1.00 39.84           C
ANISOU 1867  CA  ALA A 232     5176   3684   6279     79   -963   -541       C
ATOM   1868  C   ALA A 232     -43.939  42.000 -40.377  1.00 39.72           C
ANISOU 1868  C   ALA A 232     5231   3660   6200    100   -865   -488       C
ATOM   1869  O   ALA A 232     -44.508  41.790 -39.304  1.00 39.07           O
ANISOU 1869  O   ALA A 232     5103   3587   6155     99   -819   -431       O
ATOM   1870  CB  ALA A 232     -41.834  41.133 -39.306  1.00 35.92           C
ANISOU 1870  CB  ALA A 232     4542   3201   5903     34   -964   -500       C
ATOM   1871  N   PHE A 233     -44.531  42.651 -41.381  1.00 41.32           N
ANISOU 1871  N   PHE A 233     5542   3851   6305    117   -832   -509       N
ATOM   1872  CA  PHE A 233     -45.915  43.094 -41.243  1.00 40.38           C
ANISOU 1872  CA  PHE A 233     5489   3724   6131    126   -740   -456       C
ATOM   1873  C   PHE A 233     -46.883  41.921 -41.252  1.00 42.20           C
ANISOU 1873  C   PHE A 233     5759   3970   6305    172   -769   -399       C
ATOM   1874  O   PHE A 233     -47.960  42.005 -40.651  1.00 43.74           O
ANISOU 1874  O   PHE A 233     5968   4147   6504    174   -708   -345       O
ATOM   1875  CB  PHE A 233     -46.266  44.085 -42.350  1.00 42.47           C
ANISOU 1875  CB  PHE A 233     5849   3988   6300    126   -689   -491       C
ATOM   1876  CG  PHE A 233     -46.159  45.518 -41.927  1.00 45.14           C
ANISOU 1876  CG  PHE A 233     6155   4297   6700     89   -605   -517       C
ATOM   1877  CD1 PHE A 233     -45.081  45.950 -41.172  1.00 48.19           C
ANISOU 1877  CD1 PHE A 233     6449   4649   7210     59   -626   -546       C
ATOM   1878  CD2 PHE A 233     -47.133  46.434 -42.282  1.00 48.54           C
ANISOU 1878  CD2 PHE A 233     6644   4732   7069     83   -508   -508       C
ATOM   1879  CE1 PHE A 233     -44.978  47.269 -40.777  1.00 51.99           C
ANISOU 1879  CE1 PHE A 233     6904   5095   7756     36   -563   -570       C
ATOM   1880  CE2 PHE A 233     -47.035  47.756 -41.892  1.00 51.33           C
ANISOU 1880  CE2 PHE A 233     6957   5061   7486     59   -438   -542       C
ATOM   1881  CZ  PHE A 233     -45.956  48.174 -41.138  1.00 53.10           C
ANISOU 1881  CZ  PHE A 233     7096   5245   7836     41   -471   -574       C
ATOM   1882  N   GLU A 234     -46.521  40.828 -41.927  1.00 44.47           N
ANISOU 1882  N   GLU A 234     6064   4286   6548    213   -870   -416       N
ATOM   1883  CA  GLU A 234     -47.326  39.613 -41.859  1.00 49.14           C
ANISOU 1883  CA  GLU A 234     6681   4883   7108    268   -919   -369       C
ATOM   1884  C   GLU A 234     -47.501  39.154 -40.418  1.00 51.27           C
ANISOU 1884  C   GLU A 234     6846   5156   7479    271   -901   -344       C
ATOM   1885  O   GLU A 234     -48.572  38.672 -40.034  1.00 59.37           O
ANISOU 1885  O   GLU A 234     7899   6162   8496    306   -891   -301       O
ATOM   1886  CB  GLU A 234     -46.680  38.503 -42.690  1.00 53.94           C
ANISOU 1886  CB  GLU A 234     7295   5526   7674    316  -1047   -405       C
ATOM   1887  CG  GLU A 234     -46.267  38.912 -44.095  1.00 59.66           C
ANISOU 1887  CG  GLU A 234     8109   6266   8292    318  -1081   -450       C
ATOM   1888  CD  GLU A 234     -44.878  39.520 -44.150  1.00 64.33           C
ANISOU 1888  CD  GLU A 234     8628   6866   8950    274  -1100   -534       C
ATOM   1889  OE1 GLU A 234     -44.286  39.760 -43.076  1.00 66.04           O
ANISOU 1889  OE1 GLU A 234     8732   7068   9293    230  -1071   -539       O
ATOM   1890  OE2 GLU A 234     -44.377  39.753 -45.269  1.00 66.32           O
ANISOU 1890  OE2 GLU A 234     8938   7137   9124    284  -1147   -596       O
ATOM   1891  N   HIS A 235     -46.456  39.299 -39.605  1.00 44.61           N
ANISOU 1891  N   HIS A 235     5884   4337   6730    233   -898   -371       N
ATOM   1892  CA  HIS A 235     -46.535  38.884 -38.211  1.00 34.68           C
ANISOU 1892  CA  HIS A 235     4520   3106   5552    234   -875   -348       C
ATOM   1893  C   HIS A 235     -47.097  40.002 -37.339  1.00 35.52           C
ANISOU 1893  C   HIS A 235     4623   3184   5690    195   -769   -317       C
ATOM   1894  O   HIS A 235     -48.072  39.801 -36.606  1.00 36.04           O
ANISOU 1894  O   HIS A 235     4686   3246   5759    220   -736   -290       O
ATOM   1895  CB  HIS A 235     -45.147  38.447 -37.731  1.00 30.54           C
ANISOU 1895  CB  HIS A 235     3865   2632   5108    204   -920   -375       C
ATOM   1896  CG  HIS A 235     -45.073  38.143 -36.268  1.00 31.99           C
ANISOU 1896  CG  HIS A 235     3930   2866   5359    193   -881   -349       C
ATOM   1897  ND1 HIS A 235     -45.221  36.870 -35.761  1.00 31.95           N
ANISOU 1897  ND1 HIS A 235     3850   2927   5364    247   -923   -357       N
ATOM   1898  CD2 HIS A 235     -44.848  38.948 -35.203  1.00 32.28           C
ANISOU 1898  CD2 HIS A 235     3907   2907   5449    140   -807   -317       C
ATOM   1899  CE1 HIS A 235     -45.101  36.905 -34.446  1.00 34.69           C
ANISOU 1899  CE1 HIS A 235     4096   3328   5759    225   -867   -335       C
ATOM   1900  NE2 HIS A 235     -44.874  38.155 -34.082  1.00 32.47           N
ANISOU 1900  NE2 HIS A 235     3826   3009   5501    158   -799   -304       N
ATOM   1901  N   ILE A 236     -46.515  41.198 -37.439  1.00 36.41           N
ANISOU 1901  N   ILE A 236     4736   3272   5828    140   -725   -329       N
ATOM   1902  CA  ILE A 236     -46.841  42.282 -36.514  1.00 36.00           C
ANISOU 1902  CA  ILE A 236     4658   3198   5821    104   -639   -304       C
ATOM   1903  C   ILE A 236     -48.267  42.777 -36.730  1.00 36.35           C
ANISOU 1903  C   ILE A 236     4791   3207   5813    118   -577   -284       C
ATOM   1904  O   ILE A 236     -49.026  42.971 -35.772  1.00 33.95           O
ANISOU 1904  O   ILE A 236     4462   2900   5537    120   -530   -258       O
ATOM   1905  CB  ILE A 236     -45.825  43.428 -36.666  1.00 38.13           C
ANISOU 1905  CB  ILE A 236     4909   3439   6141     51   -623   -330       C
ATOM   1906  CG1 ILE A 236     -44.414  42.930 -36.352  1.00 27.27           C
ANISOU 1906  CG1 ILE A 236     3439   2086   4837     20   -687   -338       C
ATOM   1907  CG2 ILE A 236     -46.198  44.599 -35.774  1.00 35.01           C
ANISOU 1907  CG2 ILE A 236     4493   3019   5792     23   -544   -306       C
ATOM   1908  CD1 ILE A 236     -43.333  43.896 -36.758  1.00 38.92           C
ANISOU 1908  CD1 ILE A 236     4910   3510   6369    -26   -703   -375       C
ATOM   1909  N   VAL A 237     -48.648  43.005 -37.981  1.00 36.47           N
ANISOU 1909  N   VAL A 237     4908   3201   5750    125   -576   -294       N
ATOM   1910  CA  VAL A 237     -49.917  43.652 -38.304  1.00 34.78           C
ANISOU 1910  CA  VAL A 237     4772   2953   5488    118   -505   -267       C
ATOM   1911  C   VAL A 237     -50.993  42.636 -38.661  1.00 32.10           C
ANISOU 1911  C   VAL A 237     4506   2598   5091    159   -538   -225       C
ATOM   1912  O   VAL A 237     -52.101  42.684 -38.129  1.00 35.49           O
ANISOU 1912  O   VAL A 237     4950   2997   5540    159   -501   -191       O
ATOM   1913  CB  VAL A 237     -49.717  44.679 -39.440  1.00 39.59           C
ANISOU 1913  CB  VAL A 237     5445   3560   6038     94   -465   -299       C
ATOM   1914  CG1 VAL A 237     -51.001  45.449 -39.690  1.00 38.90           C
ANISOU 1914  CG1 VAL A 237     5418   3451   5909     72   -375   -267       C
ATOM   1915  CG2 VAL A 237     -48.578  45.625 -39.099  1.00 42.49           C
ANISOU 1915  CG2 VAL A 237     5741   3924   6479     64   -453   -350       C
ATOM   1916  N   TYR A 238     -50.684  41.708 -39.569  1.00 32.34           N
ANISOU 1916  N   TYR A 238     4585   2644   5060    196   -619   -229       N
ATOM   1917  CA  TYR A 238     -51.687  40.749 -40.016  1.00 33.66           C
ANISOU 1917  CA  TYR A 238     4834   2783   5173    240   -666   -182       C
ATOM   1918  C   TYR A 238     -51.904  39.628 -39.008  1.00 36.90           C
ANISOU 1918  C   TYR A 238     5177   3192   5651    292   -723   -182       C
ATOM   1919  O   TYR A 238     -53.010  39.081 -38.928  1.00 38.05           O
ANISOU 1919  O   TYR A 238     5376   3289   5793    324   -742   -144       O
ATOM   1920  CB  TYR A 238     -51.289  40.169 -41.374  1.00 33.61           C
ANISOU 1920  CB  TYR A 238     4907   2798   5066    270   -743   -186       C
ATOM   1921  CG  TYR A 238     -51.290  41.184 -42.496  1.00 34.89           C
ANISOU 1921  CG  TYR A 238     5152   2973   5131    232   -685   -188       C
ATOM   1922  CD1 TYR A 238     -52.435  41.418 -43.244  1.00 41.08           C
ANISOU 1922  CD1 TYR A 238     6051   3735   5824    218   -641   -121       C
ATOM   1923  CD2 TYR A 238     -50.146  41.906 -42.806  1.00 37.01           C
ANISOU 1923  CD2 TYR A 238     5381   3278   5401    208   -676   -260       C
ATOM   1924  CE1 TYR A 238     -52.441  42.344 -44.271  1.00 42.15           C
ANISOU 1924  CE1 TYR A 238     6253   3905   5857    184   -577   -128       C
ATOM   1925  CE2 TYR A 238     -50.142  42.835 -43.830  1.00 38.12           C
ANISOU 1925  CE2 TYR A 238     5591   3444   5449    185   -622   -282       C
ATOM   1926  CZ  TYR A 238     -51.291  43.048 -44.559  1.00 41.74           C
ANISOU 1926  CZ  TYR A 238     6156   3901   5803    174   -568   -216       C
ATOM   1927  OH  TYR A 238     -51.294  43.971 -45.580  1.00 45.43           O
ANISOU 1927  OH  TYR A 238     6684   4415   6164    152   -504   -241       O
ATOM   1928  N   GLY A 239     -50.879  39.273 -38.239  1.00 35.49           N
ANISOU 1928  N   GLY A 239     4882   3066   5536    299   -751   -224       N
ATOM   1929  CA  GLY A 239     -51.013  38.230 -37.241  1.00 32.67           C
ANISOU 1929  CA  GLY A 239     4444   2733   5235    352   -795   -237       C
ATOM   1930  C   GLY A 239     -50.790  36.833 -37.782  1.00 35.75           C
ANISOU 1930  C   GLY A 239     4838   3143   5604    424   -909   -254       C
ATOM   1931  O   GLY A 239     -51.172  36.528 -38.916  1.00 38.00           O
ANISOU 1931  O   GLY A 239     5231   3391   5817    449   -960   -230       O
ATOM   1932  N   ASP A 240     -50.172  35.974 -36.976  1.00 39.65           N
ANISOU 1932  N   ASP A 240     5209   3703   6153    458   -950   -293       N
ATOM   1933  CA  ASP A 240     -49.885  34.594 -37.346  1.00 42.67           C
ANISOU 1933  CA  ASP A 240     5564   4118   6532    535  -1062   -323       C
ATOM   1934  C   ASP A 240     -50.850  33.680 -36.603  1.00 43.85           C
ANISOU 1934  C   ASP A 240     5691   4254   6714    617  -1095   -336       C
ATOM   1935  O   ASP A 240     -50.861  33.657 -35.367  1.00 43.75           O
ANISOU 1935  O   ASP A 240     5576   4290   6755    620  -1048   -363       O
ATOM   1936  CB  ASP A 240     -48.434  34.235 -37.021  1.00 46.73           C
ANISOU 1936  CB  ASP A 240     5937   4726   7093    513  -1088   -368       C
ATOM   1937  CG  ASP A 240     -48.028  32.875 -37.562  1.00 50.58           C
ANISOU 1937  CG  ASP A 240     6387   5254   7578    588  -1210   -408       C
ATOM   1938  OD1 ASP A 240     -48.848  32.228 -38.246  1.00 52.06           O
ANISOU 1938  OD1 ASP A 240     6670   5391   7721    662  -1284   -398       O
ATOM   1939  OD2 ASP A 240     -46.881  32.454 -37.302  1.00 53.18           O
ANISOU 1939  OD2 ASP A 240     6588   5663   7954    569  -1237   -447       O
ATOM   1940  N   PHE A 241     -51.652  32.927 -37.355  1.00 41.98           N
ANISOU 1940  N   PHE A 241     5552   3953   6444    688  -1180   -320       N
ATOM   1941  CA  PHE A 241     -52.674  32.057 -36.788  1.00 40.08           C
ANISOU 1941  CA  PHE A 241     5313   3672   6244    777  -1229   -337       C
ATOM   1942  C   PHE A 241     -52.401  30.581 -37.046  1.00 41.57           C
ANISOU 1942  C   PHE A 241     5453   3893   6448    884  -1360   -386       C
ATOM   1943  O   PHE A 241     -53.258  29.743 -36.750  1.00 42.75           O
ANISOU 1943  O   PHE A 241     5615   3996   6633    977  -1426   -408       O
ATOM   1944  CB  PHE A 241     -54.050  32.430 -37.343  1.00 38.10           C
ANISOU 1944  CB  PHE A 241     5223   3289   5964    772  -1225   -268       C
ATOM   1945  CG  PHE A 241     -54.416  33.872 -37.143  1.00 35.49           C
ANISOU 1945  CG  PHE A 241     4933   2927   5624    670  -1099   -225       C
ATOM   1946  CD1 PHE A 241     -54.057  34.829 -38.078  1.00 37.68           C
ANISOU 1946  CD1 PHE A 241     5283   3203   5832    592  -1047   -180       C
ATOM   1947  CD2 PHE A 241     -55.122  34.269 -36.022  1.00 34.31           C
ANISOU 1947  CD2 PHE A 241     4744   2757   5534    659  -1038   -242       C
ATOM   1948  CE1 PHE A 241     -54.393  36.157 -37.896  1.00 34.07           C
ANISOU 1948  CE1 PHE A 241     4849   2723   5372    507   -933   -151       C
ATOM   1949  CE2 PHE A 241     -55.462  35.596 -35.834  1.00 33.28           C
ANISOU 1949  CE2 PHE A 241     4642   2601   5402    570   -930   -208       C
ATOM   1950  CZ  PHE A 241     -55.097  36.541 -36.773  1.00 32.80           C
ANISOU 1950  CZ  PHE A 241     4646   2539   5279    494   -876   -163       C
ATOM   1951  N   SER A 242     -51.231  30.241 -37.588  1.00 41.86           N
ANISOU 1951  N   SER A 242     5433   4006   6468    879  -1408   -411       N
ATOM   1952  CA  SER A 242     -50.947  28.858 -37.952  1.00 41.82           C
ANISOU 1952  CA  SER A 242     5380   4036   6476    982  -1542   -460       C
ATOM   1953  C   SER A 242     -50.599  27.986 -36.753  1.00 41.20           C
ANISOU 1953  C   SER A 242     5117   4059   6476   1043  -1550   -546       C
ATOM   1954  O   SER A 242     -50.681  26.758 -36.857  1.00 45.92           O
ANISOU 1954  O   SER A 242     5669   4676   7102   1154  -1662   -600       O
ATOM   1955  CB  SER A 242     -49.805  28.808 -38.968  1.00 44.63           C
ANISOU 1955  CB  SER A 242     5729   4440   6790    952  -1598   -467       C
ATOM   1956  OG  SER A 242     -48.622  29.372 -38.429  1.00 50.00           O
ANISOU 1956  OG  SER A 242     6282   5211   7505    862  -1520   -494       O
ATOM   1957  N   HIS A 243     -50.219  28.581 -35.628  1.00 39.80           N
ANISOU 1957  N   HIS A 243     4832   3957   6332    978  -1435   -561       N
ATOM   1958  CA  HIS A 243     -49.788  27.838 -34.455  1.00 41.95           C
ANISOU 1958  CA  HIS A 243     4921   4358   6662   1022  -1422   -638       C
ATOM   1959  C   HIS A 243     -50.759  28.069 -33.304  1.00 42.50           C
ANISOU 1959  C   HIS A 243     4983   4415   6750   1048  -1354   -656       C
ATOM   1960  O   HIS A 243     -51.638  28.933 -33.365  1.00 43.67           O
ANISOU 1960  O   HIS A 243     5257   4457   6880   1011  -1308   -604       O
ATOM   1961  CB  HIS A 243     -48.365  28.238 -34.048  1.00 46.33           C
ANISOU 1961  CB  HIS A 243     5337   5034   7232    919  -1351   -637       C
ATOM   1962  CG  HIS A 243     -47.382  28.187 -35.176  1.00 57.26           C
ANISOU 1962  CG  HIS A 243     6734   6419   8605    878  -1416   -626       C
ATOM   1963  ND1 HIS A 243     -46.927  27.003 -35.714  1.00 62.14           N
ANISOU 1963  ND1 HIS A 243     7284   7086   9241    952  -1535   -682       N
ATOM   1964  CD2 HIS A 243     -46.772  29.175 -35.872  1.00 60.55           C
ANISOU 1964  CD2 HIS A 243     7218   6794   8994    776  -1386   -578       C
ATOM   1965  CE1 HIS A 243     -46.077  27.263 -36.691  1.00 63.70           C
ANISOU 1965  CE1 HIS A 243     7510   7272   9422    894  -1578   -668       C
ATOM   1966  NE2 HIS A 243     -45.965  28.574 -36.807  1.00 61.78           N
ANISOU 1966  NE2 HIS A 243     7350   6974   9150    789  -1488   -608       N
ATOM   1967  N   SER A 244     -50.591  27.275 -32.243  1.00 42.26           N
ANISOU 1967  N   SER A 244     4796   4504   6756   1113  -1349   -737       N
ATOM   1968  CA  SER A 244     -51.482  27.381 -31.092  1.00 41.82           C
ANISOU 1968  CA  SER A 244     4721   4456   6714   1155  -1297   -778       C
ATOM   1969  C   SER A 244     -51.362  28.745 -30.427  1.00 39.15           C
ANISOU 1969  C   SER A 244     4394   4131   6351   1035  -1165   -719       C
ATOM   1970  O   SER A 244     -52.365  29.320 -29.989  1.00 42.43           O
ANISOU 1970  O   SER A 244     4884   4472   6767   1037  -1130   -713       O
ATOM   1971  CB  SER A 244     -51.181  26.269 -30.087  1.00 43.89           C
ANISOU 1971  CB  SER A 244     4795   4876   7003   1248  -1310   -887       C
ATOM   1972  OG  SER A 244     -49.944  26.496 -29.434  1.00 47.86           O
ANISOU 1972  OG  SER A 244     5146   5545   7494   1162  -1219   -877       O
ATOM   1973  N   GLN A 245     -50.147  29.275 -30.341  1.00 36.93           N
ANISOU 1973  N   GLN A 245     4037   3937   6059    932  -1100   -677       N
ATOM   1974  CA  GLN A 245     -49.921  30.610 -29.805  1.00 35.51           C
ANISOU 1974  CA  GLN A 245     3872   3760   5861    819   -988   -614       C
ATOM   1975  C   GLN A 245     -50.058  31.628 -30.928  1.00 36.71           C
ANISOU 1975  C   GLN A 245     4180   3773   5995    745   -984   -538       C
ATOM   1976  O   GLN A 245     -49.354  31.543 -31.941  1.00 38.02           O
ANISOU 1976  O   GLN A 245     4372   3920   6156    715  -1029   -517       O
ATOM   1977  CB  GLN A 245     -48.544  30.710 -29.151  1.00 37.56           C
ANISOU 1977  CB  GLN A 245     3979   4168   6125    741   -925   -596       C
ATOM   1978  CG  GLN A 245     -48.525  30.250 -27.708  1.00 46.19           C
ANISOU 1978  CG  GLN A 245     4926   5416   7208    779   -871   -646       C
ATOM   1979  CD  GLN A 245     -49.452  31.071 -26.835  1.00 55.21           C
ANISOU 1979  CD  GLN A 245     6123   6530   8324    778   -807   -640       C
ATOM   1980  OE1 GLN A 245     -49.418  32.302 -26.863  1.00 56.84           O
ANISOU 1980  OE1 GLN A 245     6404   6671   8522    689   -751   -568       O
ATOM   1981  NE2 GLN A 245     -50.294  30.394 -26.063  1.00 57.11           N
ANISOU 1981  NE2 GLN A 245     6324   6818   8556    885   -822   -728       N
ATOM   1982  N   LEU A 246     -50.970  32.579 -30.753  1.00 33.22           N
ANISOU 1982  N   LEU A 246     3837   3243   5543    717   -933   -507       N
ATOM   1983  CA  LEU A 246     -51.149  33.631 -31.741  1.00 32.86           C
ANISOU 1983  CA  LEU A 246     3926   3083   5475    644   -912   -440       C
ATOM   1984  C   LEU A 246     -49.898  34.496 -31.810  1.00 32.17           C
ANISOU 1984  C   LEU A 246     3794   3040   5387    541   -856   -401       C
ATOM   1985  O   LEU A 246     -49.336  34.888 -30.784  1.00 34.12           O
ANISOU 1985  O   LEU A 246     3944   3368   5651    498   -792   -395       O
ATOM   1986  CB  LEU A 246     -52.373  34.479 -31.395  1.00 33.85           C
ANISOU 1986  CB  LEU A 246     4138   3121   5602    631   -861   -421       C
ATOM   1987  CG  LEU A 246     -52.981  35.333 -32.511  1.00 38.49           C
ANISOU 1987  CG  LEU A 246     4878   3584   6165    581   -848   -362       C
ATOM   1988  CD1 LEU A 246     -54.471  35.499 -32.279  1.00 42.49           C
ANISOU 1988  CD1 LEU A 246     5463   3992   6690    606   -844   -359       C
ATOM   1989  CD2 LEU A 246     -52.309  36.695 -32.607  1.00 37.98           C
ANISOU 1989  CD2 LEU A 246     4815   3526   6089    478   -764   -321       C
ATOM   1990  N   GLY A 247     -49.458  34.786 -33.031  1.00 34.38           N
ANISOU 1990  N   GLY A 247     4150   3266   5647    505   -885   -376       N
ATOM   1991  CA  GLY A 247     -48.237  35.533 -33.264  1.00 35.25           C
ANISOU 1991  CA  GLY A 247     4226   3398   5768    416   -855   -353       C
ATOM   1992  C   GLY A 247     -48.542  36.952 -33.731  1.00 35.75           C
ANISOU 1992  C   GLY A 247     4395   3375   5812    352   -794   -315       C
ATOM   1993  O   GLY A 247     -49.310  37.151 -34.673  1.00 36.75           O
ANISOU 1993  O   GLY A 247     4644   3424   5895    367   -808   -303       O
ATOM   1994  N   GLY A 248     -47.929  37.917 -33.051  1.00 33.51           N
ANISOU 1994  N   GLY A 248     4059   3111   5561    281   -728   -293       N
ATOM   1995  CA  GLY A 248     -48.033  39.302 -33.481  1.00 32.26           C
ANISOU 1995  CA  GLY A 248     3979   2880   5397    224   -674   -270       C
ATOM   1996  C   GLY A 248     -49.431  39.858 -33.296  1.00 34.56           C
ANISOU 1996  C   GLY A 248     4346   3116   5668    240   -624   -257       C
ATOM   1997  O   GLY A 248     -50.075  39.665 -32.258  1.00 34.32           O
ANISOU 1997  O   GLY A 248     4276   3111   5654    267   -602   -260       O
ATOM   1998  N   LEU A 249     -49.905  40.567 -34.324  1.00 33.80           N
ANISOU 1998  N   LEU A 249     4358   2949   5536    222   -606   -247       N
ATOM   1999  CA  LEU A 249     -51.217  41.213 -34.336  1.00 33.31           C
ANISOU 1999  CA  LEU A 249     4371   2827   5460    218   -553   -229       C
ATOM   2000  C   LEU A 249     -51.319  42.244 -33.205  1.00 36.85           C
ANISOU 2000  C   LEU A 249     4760   3285   5957    182   -483   -224       C
ATOM   2001  O   LEU A 249     -52.010  42.058 -32.202  1.00 36.16           O
ANISOU 2001  O   LEU A 249     4637   3209   5892    206   -472   -229       O
ATOM   2002  CB  LEU A 249     -52.337  40.169 -34.250  1.00 37.07           C
ANISOU 2002  CB  LEU A 249     4883   3278   5924    281   -597   -227       C
ATOM   2003  CG  LEU A 249     -53.748  40.623 -34.623  1.00 36.15           C
ANISOU 2003  CG  LEU A 249     4866   3078   5793    271   -563   -198       C
ATOM   2004  CD1 LEU A 249     -53.875  40.828 -36.126  1.00 37.84           C
ANISOU 2004  CD1 LEU A 249     5193   3251   5935    250   -567   -165       C
ATOM   2005  CD2 LEU A 249     -54.775  39.621 -34.124  1.00 34.18           C
ANISOU 2005  CD2 LEU A 249     4626   2795   5567    335   -614   -206       C
ATOM   2006  N   HIS A 250     -50.603  43.352 -33.406  1.00 37.54           N
ANISOU 2006  N   HIS A 250     4840   3364   6061    130   -445   -223       N
ATOM   2007  CA  HIS A 250     -50.475  44.385 -32.388  1.00 32.66           C
ANISOU 2007  CA  HIS A 250     4163   2754   5492     98   -394   -216       C
ATOM   2008  C   HIS A 250     -51.076  45.726 -32.790  1.00 32.13           C
ANISOU 2008  C   HIS A 250     4146   2633   5429     66   -332   -220       C
ATOM   2009  O   HIS A 250     -51.112  46.641 -31.960  1.00 32.79           O
ANISOU 2009  O   HIS A 250     4184   2718   5556     47   -295   -217       O
ATOM   2010  CB  HIS A 250     -48.996  44.578 -32.017  1.00 28.35           C
ANISOU 2010  CB  HIS A 250     3542   2242   4986     65   -412   -208       C
ATOM   2011  CG  HIS A 250     -48.337  43.333 -31.508  1.00 30.41           C
ANISOU 2011  CG  HIS A 250     3729   2574   5251     84   -460   -201       C
ATOM   2012  ND1 HIS A 250     -48.580  42.822 -30.251  1.00 29.39           N
ANISOU 2012  ND1 HIS A 250     3526   2514   5126    107   -452   -190       N
ATOM   2013  CD2 HIS A 250     -47.445  42.494 -32.088  1.00 31.04           C
ANISOU 2013  CD2 HIS A 250     3787   2678   5328     85   -517   -212       C
ATOM   2014  CE1 HIS A 250     -47.867  41.723 -30.078  1.00 29.17           C
ANISOU 2014  CE1 HIS A 250     3430   2555   5097    120   -493   -192       C
ATOM   2015  NE2 HIS A 250     -47.169  41.502 -31.178  1.00 29.36           N
ANISOU 2015  NE2 HIS A 250     3482   2550   5125    105   -535   -204       N
ATOM   2016  N   LEU A 251     -51.546  45.876 -34.025  1.00 33.75           N
ANISOU 2016  N   LEU A 251     4438   2802   5586     61   -318   -225       N
ATOM   2017  CA  LEU A 251     -52.203  47.097 -34.472  1.00 31.55           C
ANISOU 2017  CA  LEU A 251     4197   2488   5303     30   -248   -232       C
ATOM   2018  C   LEU A 251     -53.698  46.855 -34.614  1.00 35.22           C
ANISOU 2018  C   LEU A 251     4718   2920   5745     32   -224   -209       C
ATOM   2019  O   LEU A 251     -54.119  45.841 -35.180  1.00 42.79           O
ANISOU 2019  O   LEU A 251     5736   3864   6657     55   -263   -187       O
ATOM   2020  CB  LEU A 251     -51.633  47.587 -35.806  1.00 34.39           C
ANISOU 2020  CB  LEU A 251     4609   2843   5614     15   -238   -258       C
ATOM   2021  CG  LEU A 251     -50.410  48.504 -35.752  1.00 37.49           C
ANISOU 2021  CG  LEU A 251     4953   3237   6056     -1   -239   -297       C
ATOM   2022  CD1 LEU A 251     -50.127  49.071 -37.132  1.00 44.17           C
ANISOU 2022  CD1 LEU A 251     5858   4081   6844     -6   -221   -343       C
ATOM   2023  CD2 LEU A 251     -50.613  49.624 -34.743  1.00 32.76           C
ANISOU 2023  CD2 LEU A 251     4291   2625   5531    -17   -193   -299       C
ATOM   2024  N   LEU A 252     -54.494  47.800 -34.108  1.00 32.83           N
ANISOU 2024  N   LEU A 252     4392   2598   5483      5   -165   -212       N
ATOM   2025  CA  LEU A 252     -55.946  47.644 -34.128  1.00 35.41           C
ANISOU 2025  CA  LEU A 252     4762   2881   5811     -6   -144   -188       C
ATOM   2026  C   LEU A 252     -56.482  47.474 -35.544  1.00 34.33           C
ANISOU 2026  C   LEU A 252     4726   2718   5600    -28   -123   -154       C
ATOM   2027  O   LEU A 252     -57.466  46.754 -35.751  1.00 38.68           O
ANISOU 2027  O   LEU A 252     5336   3222   6138    -25   -144   -114       O
ATOM   2028  CB  LEU A 252     -56.614  48.842 -33.455  1.00 37.62           C
ANISOU 2028  CB  LEU A 252     4990   3150   6153    -40    -83   -206       C
ATOM   2029  CG  LEU A 252     -58.141  48.784 -33.380  1.00 39.82           C
ANISOU 2029  CG  LEU A 252     5299   3375   6457    -65    -62   -186       C
ATOM   2030  CD1 LEU A 252     -58.586  47.644 -32.479  1.00 39.34           C
ANISOU 2030  CD1 LEU A 252     5230   3293   6423    -18   -134   -189       C
ATOM   2031  CD2 LEU A 252     -58.721  50.103 -32.906  1.00 39.84           C
ANISOU 2031  CD2 LEU A 252     5243   3374   6522   -106      1   -211       C
ATOM   2032  N   ILE A 253     -55.855  48.122 -36.528  1.00 34.40           N
ANISOU 2032  N   ILE A 253     4758   2755   5556    -47    -87   -167       N
ATOM   2033  CA  ILE A 253     -56.324  47.981 -37.902  1.00 33.86           C
ANISOU 2033  CA  ILE A 253     4789   2683   5393    -68    -63   -131       C
ATOM   2034  C   ILE A 253     -56.136  46.549 -38.389  1.00 32.57           C
ANISOU 2034  C   ILE A 253     4693   2511   5172    -23   -153    -98       C
ATOM   2035  O   ILE A 253     -56.918  46.057 -39.211  1.00 37.67           O
ANISOU 2035  O   ILE A 253     5431   3129   5752    -32   -158    -40       O
ATOM   2036  CB  ILE A 253     -55.615  48.999 -38.817  1.00 33.07           C
ANISOU 2036  CB  ILE A 253     4692   2633   5240    -86     -7   -174       C
ATOM   2037  CG1 ILE A 253     -56.209  48.958 -40.226  1.00 35.73           C
ANISOU 2037  CG1 ILE A 253     5130   2988   5458   -111     34   -132       C
ATOM   2038  CG2 ILE A 253     -54.115  48.749 -38.847  1.00 32.49           C
ANISOU 2038  CG2 ILE A 253     4589   2588   5167    -46    -73   -225       C
ATOM   2039  CD1 ILE A 253     -55.656  50.012 -41.152  1.00 37.59           C
ANISOU 2039  CD1 ILE A 253     5365   3288   5629   -124    100   -188       C
ATOM   2040  N   GLY A 254     -55.115  45.853 -37.886  1.00 33.27           N
ANISOU 2040  N   GLY A 254     4733   2622   5287     23   -227   -130       N
ATOM   2041  CA  GLY A 254     -54.958  44.449 -38.226  1.00 29.23           C
ANISOU 2041  CA  GLY A 254     4265   2106   4736     73   -320   -110       C
ATOM   2042  C   GLY A 254     -56.058  43.591 -37.634  1.00 30.49           C
ANISOU 2042  C   GLY A 254     4442   2210   4934     99   -358    -75       C
ATOM   2043  O   GLY A 254     -56.516  42.632 -38.260  1.00 36.56           O
ANISOU 2043  O   GLY A 254     5288   2944   5657    130   -418    -35       O
ATOM   2044  N   LEU A 255     -56.498  43.925 -36.418  1.00 28.41           N
ANISOU 2044  N   LEU A 255     4107   1932   4754     93   -332    -94       N
ATOM   2045  CA  LEU A 255     -57.635  43.228 -35.828  1.00 30.61           C
ANISOU 2045  CA  LEU A 255     4401   2149   5079    118   -368    -78       C
ATOM   2046  C   LEU A 255     -58.923  43.555 -36.572  1.00 35.38           C
ANISOU 2046  C   LEU A 255     5100   2678   5666     67   -330    -15       C
ATOM   2047  O   LEU A 255     -59.794  42.691 -36.728  1.00 39.77           O
ANISOU 2047  O   LEU A 255     5720   3160   6231     90   -387     24       O
ATOM   2048  CB  LEU A 255     -57.771  43.590 -34.347  1.00 31.00           C
ANISOU 2048  CB  LEU A 255     4350   2214   5213    123   -351   -125       C
ATOM   2049  CG  LEU A 255     -56.816  42.994 -33.308  1.00 34.59           C
ANISOU 2049  CG  LEU A 255     4707   2741   5692    177   -396   -173       C
ATOM   2050  CD1 LEU A 255     -55.435  43.621 -33.382  1.00 33.47           C
ANISOU 2050  CD1 LEU A 255     4514   2669   5536    152   -368   -185       C
ATOM   2051  CD2 LEU A 255     -57.397  43.158 -31.912  1.00 37.07           C
ANISOU 2051  CD2 LEU A 255     4952   3062   6071    192   -389   -210       C
ATOM   2052  N   ALA A 256     -59.062  44.800 -37.036  1.00 35.69           N
ANISOU 2052  N   ALA A 256     5144   2733   5685     -3   -234     -2       N
ATOM   2053  CA  ALA A 256     -60.267  45.193 -37.758  1.00 34.36           C
ANISOU 2053  CA  ALA A 256     5053   2507   5496    -68   -180     66       C
ATOM   2054  C   ALA A 256     -60.396  44.433 -39.071  1.00 36.08           C
ANISOU 2054  C   ALA A 256     5393   2708   5610    -60   -218    140       C
ATOM   2055  O   ALA A 256     -61.485  43.958 -39.415  1.00 41.38           O
ANISOU 2055  O   ALA A 256     6145   3296   6282    -81   -240    216       O
ATOM   2056  CB  ALA A 256     -60.262  46.701 -38.006  1.00 30.31           C
ANISOU 2056  CB  ALA A 256     4500   2039   4976   -138    -63     51       C
ATOM   2057  N   LYS A 257     -59.296  44.309 -39.816  1.00 37.41           N
ANISOU 2057  N   LYS A 257     5577   2947   5688    -32   -236    121       N
ATOM   2058  CA  LYS A 257     -59.331  43.561 -41.068  1.00 40.32           C
ANISOU 2058  CA  LYS A 257     6063   3313   5944    -15   -285    186       C
ATOM   2059  C   LYS A 257     -59.687  42.100 -40.823  1.00 44.78           C
ANISOU 2059  C   LYS A 257     6669   3806   6541     54   -409    214       C
ATOM   2060  O   LYS A 257     -60.487  41.514 -41.562  1.00 46.36           O
ANISOU 2060  O   LYS A 257     6979   3942   6693     51   -449    304       O
ATOM   2061  CB  LYS A 257     -57.983  43.680 -41.780  1.00 34.64           C
ANISOU 2061  CB  LYS A 257     5338   2688   5137     12   -296    134       C
ATOM   2062  CG  LYS A 257     -57.950  43.069 -43.170  1.00 34.14           C
ANISOU 2062  CG  LYS A 257     5395   2643   4933     29   -343    192       C
ATOM   2063  CD  LYS A 257     -56.562  43.187 -43.780  1.00 34.88           C
ANISOU 2063  CD  LYS A 257     5470   2828   4954     61   -368    117       C
ATOM   2064  CE  LYS A 257     -56.538  42.677 -45.212  1.00 41.00           C
ANISOU 2064  CE  LYS A 257     6369   3638   5570     80   -413    168       C
ATOM   2065  NZ  LYS A 257     -57.423  43.482 -46.098  1.00 47.33           N
ANISOU 2065  NZ  LYS A 257     7254   4462   6266     10   -306    242       N
ATOM   2066  N   ARG A 258     -59.108  41.499 -39.781  1.00 43.73           N
ANISOU 2066  N   ARG A 258     6445   3682   6487    119   -473    141       N
ATOM   2067  CA  ARG A 258     -59.417  40.111 -39.453  1.00 40.10           C
ANISOU 2067  CA  ARG A 258     6004   3164   6068    199   -592    145       C
ATOM   2068  C   ARG A 258     -60.857  39.960 -38.982  1.00 44.39           C
ANISOU 2068  C   ARG A 258     6583   3590   6691    182   -600    187       C
ATOM   2069  O   ARG A 258     -61.513  38.956 -39.285  1.00 46.51           O
ANISOU 2069  O   ARG A 258     6931   3773   6967    227   -693    235       O
ATOM   2070  CB  ARG A 258     -58.447  39.606 -38.384  1.00 39.67           C
ANISOU 2070  CB  ARG A 258     5825   3171   6076    264   -639     50       C
ATOM   2071  CG  ARG A 258     -58.769  38.226 -37.828  1.00 44.86           C
ANISOU 2071  CG  ARG A 258     6470   3785   6790    357   -752     27       C
ATOM   2072  CD  ARG A 258     -58.350  37.122 -38.784  1.00 49.38           C
ANISOU 2072  CD  ARG A 258     7105   4362   7296    422   -858     48       C
ATOM   2073  NE  ARG A 258     -58.510  35.798 -38.189  1.00 49.91           N
ANISOU 2073  NE  ARG A 258     7135   4403   7427    525   -971      5       N
ATOM   2074  CZ  ARG A 258     -58.125  34.667 -38.771  1.00 52.26           C
ANISOU 2074  CZ  ARG A 258     7457   4708   7692    605  -1084      2       C
ATOM   2075  NH1 ARG A 258     -57.553  34.698 -39.967  1.00 58.25           N
ANISOU 2075  NH1 ARG A 258     8283   5501   8350    591  -1103     43       N
ATOM   2076  NH2 ARG A 258     -58.309  33.505 -38.159  1.00 49.23           N
ANISOU 2076  NH2 ARG A 258     7024   4304   7376    706  -1182    -52       N
ATOM   2077  N   PHE A 259     -61.370  40.951 -38.249  1.00 45.07           N
ANISOU 2077  N   PHE A 259     6613   3665   6846    121   -514    168       N
ATOM   2078  CA  PHE A 259     -62.703  40.829 -37.668  1.00 44.08           C
ANISOU 2078  CA  PHE A 259     6505   3425   6817    104   -531    188       C
ATOM   2079  C   PHE A 259     -63.789  40.809 -38.734  1.00 48.28           C
ANISOU 2079  C   PHE A 259     7170   3860   7315     41   -525    311       C
ATOM   2080  O   PHE A 259     -64.832  40.173 -38.540  1.00 54.12           O
ANISOU 2080  O   PHE A 259     7962   4473   8128     52   -593    347       O
ATOM   2081  CB  PHE A 259     -62.948  41.968 -36.681  1.00 47.47           C
ANISOU 2081  CB  PHE A 259     6838   3876   7324     49   -443    134       C
ATOM   2082  CG  PHE A 259     -64.163  41.774 -35.827  1.00 54.66           C
ANISOU 2082  CG  PHE A 259     7739   4680   8351     47   -478    118       C
ATOM   2083  CD1 PHE A 259     -64.137  40.895 -34.757  1.00 56.14           C
ANISOU 2083  CD1 PHE A 259     7870   4855   8607    140   -567     35       C
ATOM   2084  CD2 PHE A 259     -65.329  42.471 -36.089  1.00 59.24           C
ANISOU 2084  CD2 PHE A 259     8359   5176   8974    -49   -423    179       C
ATOM   2085  CE1 PHE A 259     -65.252  40.711 -33.966  1.00 58.54           C
ANISOU 2085  CE1 PHE A 259     8165   5058   9019    146   -610      2       C
ATOM   2086  CE2 PHE A 259     -66.448  42.292 -35.301  1.00 65.37           C
ANISOU 2086  CE2 PHE A 259     9124   5842   9871    -54   -466    156       C
ATOM   2087  CZ  PHE A 259     -66.410  41.411 -34.238  1.00 64.52           C
ANISOU 2087  CZ  PHE A 259     8967   5717   9831     48   -565     62       C
ATOM   2088  N   LYS A 260     -63.571  41.494 -39.858  1.00 50.59           N
ANISOU 2088  N   LYS A 260     7518   4208   7495    -25   -445    376       N
ATOM   2089  CA  LYS A 260     -64.553  41.467 -40.935  1.00 55.36           C
ANISOU 2089  CA  LYS A 260     8252   4739   8043    -93   -431    510       C
ATOM   2090  C   LYS A 260     -64.633  40.089 -41.579  1.00 59.71           C
ANISOU 2090  C   LYS A 260     8914   5224   8549    -18   -566    574       C
ATOM   2091  O   LYS A 260     -65.703  39.687 -42.051  1.00 61.68           O
ANISOU 2091  O   LYS A 260     9271   5355   8809    -50   -605    686       O
ATOM   2092  CB  LYS A 260     -64.213  42.528 -41.982  1.00 59.11           C
ANISOU 2092  CB  LYS A 260     8751   5320   8389   -172   -308    552       C
ATOM   2093  CG  LYS A 260     -65.406  43.351 -42.441  1.00 65.14           C
ANISOU 2093  CG  LYS A 260     9558   6040   9152   -297   -204    653       C
ATOM   2094  CD  LYS A 260     -65.017  44.328 -43.541  1.00 67.49           C
ANISOU 2094  CD  LYS A 260     9875   6467   9303   -361    -80    682       C
ATOM   2095  CE  LYS A 260     -66.202  45.181 -43.968  1.00 65.17           C
ANISOU 2095  CE  LYS A 260     9604   6149   9008   -494     38    782       C
ATOM   2096  NZ  LYS A 260     -65.869  46.062 -45.122  1.00 61.54           N
ANISOU 2096  NZ  LYS A 260     9166   5831   8386   -550    163    811       N
ATOM   2097  N   GLU A 261     -63.523  39.352 -41.598  1.00 64.53           N
ANISOU 2097  N   GLU A 261     9497   5904   9116     81   -645    508       N
ATOM   2098  CA  GLU A 261     -63.513  38.018 -42.188  1.00 70.45           C
ANISOU 2098  CA  GLU A 261    10339   6601   9826    168   -786    554       C
ATOM   2099  C   GLU A 261     -64.017  36.976 -41.197  1.00 66.49           C
ANISOU 2099  C   GLU A 261     9808   5992   9464    254   -904    505       C
ATOM   2100  O   GLU A 261     -64.996  36.270 -41.461  1.00 67.66           O
ANISOU 2100  O   GLU A 261    10055   6003   9651    270   -990    584       O
ATOM   2101  CB  GLU A 261     -62.100  37.664 -42.657  1.00 84.47           C
ANISOU 2101  CB  GLU A 261    12088   8504  11504    235   -825    494       C
ATOM   2102  CG  GLU A 261     -61.320  38.830 -43.234  1.00 97.41           C
ANISOU 2102  CG  GLU A 261    13702  10270  13038    168   -704    476       C
ATOM   2103  CD  GLU A 261     -59.869  38.480 -43.498  1.00107.36           C
ANISOU 2103  CD  GLU A 261    14914  11641  14237    234   -756    394       C
ATOM   2104  OE1 GLU A 261     -59.300  38.996 -44.483  1.00110.57           O
ANISOU 2104  OE1 GLU A 261    15361  12132  14517    206   -713    403       O
ATOM   2105  OE2 GLU A 261     -59.297  37.685 -42.721  1.00110.30           O
ANISOU 2105  OE2 GLU A 261    15203  12020  14687    314   -838    314       O
ATOM   2106  N   SER A 262     -63.354  36.867 -40.047  1.00 61.42           N
ANISOU 2106  N   SER A 262     9029   5411   8897    313   -911    372       N
ATOM   2107  CA  SER A 262     -63.666  35.862 -39.048  1.00 61.65           C
ANISOU 2107  CA  SER A 262     9007   5373   9044    412  -1018    296       C
ATOM   2108  C   SER A 262     -63.777  36.506 -37.673  1.00 54.80           C
ANISOU 2108  C   SER A 262     8014   4532   8275    393   -950    197       C
ATOM   2109  O   SER A 262     -63.025  37.435 -37.359  1.00 58.06           O
ANISOU 2109  O   SER A 262     8344   5059   8659    346   -849    154       O
ATOM   2110  CB  SER A 262     -62.591  34.767 -39.024  1.00 68.21           C
ANISOU 2110  CB  SER A 262     9785   6284   9847    532  -1119    223       C
ATOM   2111  OG  SER A 262     -62.856  33.816 -38.009  1.00 78.61           O
ANISOU 2111  OG  SER A 262    11036   7559  11274    636  -1212    132       O
ATOM   2112  N   PRO A 263     -64.698  36.039 -36.838  1.00 53.38           N
ANISOU 2112  N   PRO A 263     7822   4247   8213    433  -1013    155       N
ATOM   2113  CA  PRO A 263     -64.825  36.593 -35.488  1.00 50.76           C
ANISOU 2113  CA  PRO A 263     7372   3949   7966    426   -962     52       C
ATOM   2114  C   PRO A 263     -63.787  36.010 -34.540  1.00 47.04           C
ANISOU 2114  C   PRO A 263     6772   3606   7497    527   -993    -73       C
ATOM   2115  O   PRO A 263     -63.152  34.989 -34.813  1.00 51.73           O
ANISOU 2115  O   PRO A 263     7360   4237   8058    616  -1074    -94       O
ATOM   2116  CB  PRO A 263     -66.240  36.176 -35.076  1.00 57.26           C
ANISOU 2116  CB  PRO A 263     8241   4611   8905    438  -1033     51       C
ATOM   2117  CG  PRO A 263     -66.453  34.885 -35.803  1.00 60.14           C
ANISOU 2117  CG  PRO A 263     8692   4913   9247    517  -1153     97       C
ATOM   2118  CD  PRO A 263     -65.726  35.022 -37.120  1.00 56.56           C
ANISOU 2118  CD  PRO A 263     8326   4484   8679    486  -1141    202       C
ATOM   2119  N   PHE A 264     -63.624  36.686 -33.407  1.00 38.01           N
ANISOU 2119  N   PHE A 264     5518   2534   6388    510   -927   -153       N
ATOM   2120  CA  PHE A 264     -62.709  36.234 -32.367  1.00 37.48           C
ANISOU 2120  CA  PHE A 264     5320   2600   6320    592   -940   -263       C
ATOM   2121  C   PHE A 264     -63.121  36.874 -31.050  1.00 40.34           C
ANISOU 2121  C   PHE A 264     5597   2988   6742    579   -895   -342       C
ATOM   2122  O   PHE A 264     -63.920  37.812 -31.014  1.00 42.42           O
ANISOU 2122  O   PHE A 264     5891   3181   7044    497   -844   -311       O
ATOM   2123  CB  PHE A 264     -61.253  36.565 -32.709  1.00 40.62           C
ANISOU 2123  CB  PHE A 264     5666   3140   6629    567   -881   -248       C
ATOM   2124  CG  PHE A 264     -61.048  37.969 -33.194  1.00 47.33           C
ANISOU 2124  CG  PHE A 264     6538   4007   7437    450   -768   -184       C
ATOM   2125  CD1 PHE A 264     -60.905  39.016 -32.298  1.00 49.76           C
ANISOU 2125  CD1 PHE A 264     6764   4373   7767    402   -685   -220       C
ATOM   2126  CD2 PHE A 264     -60.998  38.242 -34.550  1.00 52.67           C
ANISOU 2126  CD2 PHE A 264     7316   4650   8047    396   -749    -94       C
ATOM   2127  CE1 PHE A 264     -60.719  40.310 -32.747  1.00 52.18           C
ANISOU 2127  CE1 PHE A 264     7084   4696   8045    306   -588   -174       C
ATOM   2128  CE2 PHE A 264     -60.810  39.531 -35.005  1.00 55.73           C
ANISOU 2128  CE2 PHE A 264     7716   5065   8395    299   -643    -51       C
ATOM   2129  CZ  PHE A 264     -60.671  40.567 -34.104  1.00 55.00           C
ANISOU 2129  CZ  PHE A 264     7535   5022   8340    256   -564    -95       C
ATOM   2130  N   GLU A 265     -62.559  36.355 -29.963  1.00 39.72           N
ANISOU 2130  N   GLU A 265     5404   3021   6666    661   -916   -445       N
ATOM   2131  CA  GLU A 265     -62.899  36.804 -28.621  1.00 39.63           C
ANISOU 2131  CA  GLU A 265     5307   3056   6695    670   -890   -532       C
ATOM   2132  C   GLU A 265     -61.788  37.693 -28.080  1.00 41.22           C
ANISOU 2132  C   GLU A 265     5416   3413   6835    622   -792   -531       C
ATOM   2133  O   GLU A 265     -60.607  37.345 -28.174  1.00 43.16           O
ANISOU 2133  O   GLU A 265     5608   3769   7021    641   -780   -524       O
ATOM   2134  CB  GLU A 265     -63.122  35.614 -27.688  1.00 46.29           C
ANISOU 2134  CB  GLU A 265     6086   3928   7573    802   -980   -655       C
ATOM   2135  CG  GLU A 265     -64.016  35.927 -26.501  1.00 57.26           C
ANISOU 2135  CG  GLU A 265     7432   5300   9024    823   -989   -752       C
ATOM   2136  CD  GLU A 265     -65.464  36.145 -26.904  1.00 67.67           C
ANISOU 2136  CD  GLU A 265     8852   6434  10426    775  -1028   -721       C
ATOM   2137  OE1 GLU A 265     -65.958  35.404 -27.781  1.00 69.45           O
ANISOU 2137  OE1 GLU A 265     9164   6568  10656    785  -1087   -664       O
ATOM   2138  OE2 GLU A 265     -66.105  37.061 -26.349  1.00 73.11           O
ANISOU 2138  OE2 GLU A 265     9525   7107  11146    712   -986   -737       O
ATOM   2139  N   LEU A 266     -62.171  38.836 -27.517  1.00 43.14           N
ANISOU 2139  N   LEU A 266     5637   3656   7100    557   -730   -535       N
ATOM   2140  CA  LEU A 266     -61.238  39.768 -26.894  1.00 41.73           C
ANISOU 2140  CA  LEU A 266     5375   3606   6875    514   -649   -532       C
ATOM   2141  C   LEU A 266     -61.620  39.932 -25.431  1.00 42.27           C
ANISOU 2141  C   LEU A 266     5361   3738   6964    555   -656   -625       C
ATOM   2142  O   LEU A 266     -62.700  40.446 -25.122  1.00 46.80           O
ANISOU 2142  O   LEU A 266     5956   4229   7598    533   -664   -654       O
ATOM   2143  CB  LEU A 266     -61.242  41.122 -27.607  1.00 40.69           C
ANISOU 2143  CB  LEU A 266     5288   3431   6743    403   -569   -452       C
ATOM   2144  CG  LEU A 266     -60.405  41.250 -28.883  1.00 44.89           C
ANISOU 2144  CG  LEU A 266     5871   3964   7220    358   -537   -370       C
ATOM   2145  CD1 LEU A 266     -60.426  42.684 -29.377  1.00 47.83           C
ANISOU 2145  CD1 LEU A 266     6265   4316   7592    260   -452   -319       C
ATOM   2146  CD2 LEU A 266     -58.973  40.789 -28.655  1.00 43.04           C
ANISOU 2146  CD2 LEU A 266     5565   3856   6932    392   -540   -379       C
ATOM   2147  N   GLU A 267     -60.739  39.494 -24.538  1.00 38.96           N
ANISOU 2147  N   GLU A 267     4844   3470   6489    611   -653   -671       N
ATOM   2148  CA  GLU A 267     -60.960  39.586 -23.100  1.00 40.14           C
ANISOU 2148  CA  GLU A 267     4909   3715   6627    660   -657   -760       C
ATOM   2149  C   GLU A 267     -60.213  40.812 -22.588  1.00 34.71           C
ANISOU 2149  C   GLU A 267     4171   3120   5897    591   -580   -712       C
ATOM   2150  O   GLU A 267     -58.982  40.805 -22.499  1.00 34.08           O
ANISOU 2150  O   GLU A 267     4040   3151   5757    576   -542   -665       O
ATOM   2151  CB  GLU A 267     -60.492  38.315 -22.396  1.00 48.35           C
ANISOU 2151  CB  GLU A 267     5869   4882   7621    767   -697   -839       C
ATOM   2152  CG  GLU A 267     -61.492  37.715 -21.423  1.00 62.86           C
ANISOU 2152  CG  GLU A 267     7676   6721   9486    865   -763   -975       C
ATOM   2153  CD  GLU A 267     -61.135  37.990 -19.977  1.00 75.66           C
ANISOU 2153  CD  GLU A 267     9192   8522  11034    897   -731  -1038       C
ATOM   2154  OE1 GLU A 267     -61.905  38.706 -19.305  1.00 79.07           O
ANISOU 2154  OE1 GLU A 267     9625   8930  11488    888   -739  -1086       O
ATOM   2155  OE2 GLU A 267     -60.084  37.495 -19.515  1.00 80.03           O
ANISOU 2155  OE2 GLU A 267     9658   9244  11504    927   -699  -1035       O
ATOM   2156  N   ASP A 268     -60.960  41.863 -22.259  1.00 32.47           N
ANISOU 2156  N   ASP A 268     3899   2784   5653    547   -564   -722       N
ATOM   2157  CA  ASP A 268     -60.384  43.119 -21.781  1.00 31.40           C
ANISOU 2157  CA  ASP A 268     3722   2717   5491    488   -505   -679       C
ATOM   2158  C   ASP A 268     -60.205  43.033 -20.264  1.00 32.35           C
ANISOU 2158  C   ASP A 268     3752   2985   5553    548   -517   -746       C
ATOM   2159  O   ASP A 268     -60.961  43.601 -19.476  1.00 37.47           O
ANISOU 2159  O   ASP A 268     4382   3635   6221    558   -536   -806       O
ATOM   2160  CB  ASP A 268     -61.275  44.286 -22.191  1.00 35.06           C
ANISOU 2160  CB  ASP A 268     4231   3062   6028    416   -485   -663       C
ATOM   2161  CG  ASP A 268     -60.666  45.632 -21.871  1.00 38.98           C
ANISOU 2161  CG  ASP A 268     4688   3613   6510    360   -431   -618       C
ATOM   2162  OD1 ASP A 268     -59.492  45.675 -21.444  1.00 40.84           O
ANISOU 2162  OD1 ASP A 268     4876   3962   6682    368   -410   -581       O
ATOM   2163  OD2 ASP A 268     -61.367  46.651 -22.048  1.00 42.32           O
ANISOU 2163  OD2 ASP A 268     5124   3963   6993    308   -413   -618       O
ATOM   2164  N   PHE A 269     -59.166  42.297 -19.861  1.00 32.89           N
ANISOU 2164  N   PHE A 269     3761   3192   5544    587   -507   -735       N
ATOM   2165  CA  PHE A 269     -59.002  41.977 -18.447  1.00 36.30           C
ANISOU 2165  CA  PHE A 269     4106   3787   5899    654   -516   -800       C
ATOM   2166  C   PHE A 269     -58.489  43.150 -17.622  1.00 34.58           C
ANISOU 2166  C   PHE A 269     3848   3658   5633    610   -477   -750       C
ATOM   2167  O   PHE A 269     -58.477  43.056 -16.389  1.00 35.66           O
ANISOU 2167  O   PHE A 269     3920   3934   5694    661   -485   -800       O
ATOM   2168  CB  PHE A 269     -58.087  40.758 -18.276  1.00 38.69           C
ANISOU 2168  CB  PHE A 269     4345   4222   6133    705   -510   -804       C
ATOM   2169  CG  PHE A 269     -56.717  40.915 -18.881  1.00 39.43           C
ANISOU 2169  CG  PHE A 269     4428   4350   6205    633   -459   -684       C
ATOM   2170  CD1 PHE A 269     -55.649  41.331 -18.105  1.00 37.75           C
ANISOU 2170  CD1 PHE A 269     4145   4279   5919    599   -412   -617       C
ATOM   2171  CD2 PHE A 269     -56.489  40.612 -20.216  1.00 38.77           C
ANISOU 2171  CD2 PHE A 269     4402   4156   6172    601   -466   -638       C
ATOM   2172  CE1 PHE A 269     -54.385  41.464 -18.649  1.00 37.79           C
ANISOU 2172  CE1 PHE A 269     4138   4300   5922    528   -376   -510       C
ATOM   2173  CE2 PHE A 269     -55.225  40.742 -20.767  1.00 35.25           C
ANISOU 2173  CE2 PHE A 269     3942   3738   5713    538   -430   -544       C
ATOM   2174  CZ  PHE A 269     -54.172  41.169 -19.981  1.00 37.19           C
ANISOU 2174  CZ  PHE A 269     4116   4110   5903    500   -387   -482       C
ATOM   2175  N   ILE A 270     -58.070  44.240 -18.255  1.00 33.32           N
ANISOU 2175  N   ILE A 270     3723   3425   5511    524   -440   -656       N
ATOM   2176  CA  ILE A 270     -57.829  45.492 -17.542  1.00 29.59           C
ANISOU 2176  CA  ILE A 270     3225   2997   5020    489   -423   -617       C
ATOM   2177  C   ILE A 270     -58.741  46.545 -18.160  1.00 30.90           C
ANISOU 2177  C   ILE A 270     3444   3013   5284    442   -426   -627       C
ATOM   2178  O   ILE A 270     -58.286  47.351 -18.985  1.00 32.27           O
ANISOU 2178  O   ILE A 270     3647   3114   5498    374   -391   -553       O
ATOM   2179  CB  ILE A 270     -56.354  45.914 -17.604  1.00 34.69           C
ANISOU 2179  CB  ILE A 270     3848   3706   5628    434   -379   -497       C
ATOM   2180  CG1 ILE A 270     -55.446  44.752 -17.201  1.00 38.49           C
ANISOU 2180  CG1 ILE A 270     4270   4327   6026    464   -367   -479       C
ATOM   2181  CG2 ILE A 270     -56.105  47.098 -16.683  1.00 35.34           C
ANISOU 2181  CG2 ILE A 270     3900   3844   5682    416   -378   -458       C
ATOM   2182  CD1 ILE A 270     -53.973  45.094 -17.223  1.00 40.72           C
ANISOU 2182  CD1 ILE A 270     4526   4665   6282    400   -330   -355       C
ATOM   2183  N   PRO A 271     -60.030  46.568 -17.805  1.00 29.87           N
ANISOU 2183  N   PRO A 271     3321   2833   5197    473   -469   -724       N
ATOM   2184  CA  PRO A 271     -60.963  47.490 -18.467  1.00 30.52           C
ANISOU 2184  CA  PRO A 271     3444   2770   5381    416   -467   -732       C
ATOM   2185  C   PRO A 271     -60.758  48.939 -18.054  1.00 32.47           C
ANISOU 2185  C   PRO A 271     3658   3039   5641    377   -450   -701       C
ATOM   2186  O   PRO A 271     -61.371  49.421 -17.096  1.00 39.00           O
ANISOU 2186  O   PRO A 271     4446   3904   6470    403   -489   -767       O
ATOM   2187  CB  PRO A 271     -62.337  46.968 -18.029  1.00 27.24           C
ANISOU 2187  CB  PRO A 271     3032   2306   5012    464   -530   -851       C
ATOM   2188  CG  PRO A 271     -62.081  46.313 -16.717  1.00 27.78           C
ANISOU 2188  CG  PRO A 271     3040   2530   4983    553   -565   -919       C
ATOM   2189  CD  PRO A 271     -60.701  45.719 -16.805  1.00 29.48           C
ANISOU 2189  CD  PRO A 271     3236   2856   5109    561   -523   -839       C
ATOM   2190  N   MET A 272     -59.898  49.642 -18.783  1.00 29.87           N
ANISOU 2190  N   MET A 272     3343   2683   5323    320   -402   -610       N
ATOM   2191  CA  MET A 272     -59.625  51.044 -18.510  1.00 29.86           C
ANISOU 2191  CA  MET A 272     3311   2689   5347    289   -391   -579       C
ATOM   2192  C   MET A 272     -59.142  51.698 -19.793  1.00 30.79           C
ANISOU 2192  C   MET A 272     3464   2718   5517    223   -338   -514       C
ATOM   2193  O   MET A 272     -58.765  51.020 -20.752  1.00 35.22           O
ANISOU 2193  O   MET A 272     4072   3241   6070    205   -311   -479       O
ATOM   2194  CB  MET A 272     -58.582  51.213 -17.401  1.00 28.02           C
ANISOU 2194  CB  MET A 272     3030   2590   5025    320   -406   -532       C
ATOM   2195  CG  MET A 272     -57.235  50.597 -17.739  1.00 31.06           C
ANISOU 2195  CG  MET A 272     3425   3021   5356    306   -376   -442       C
ATOM   2196  SD  MET A 272     -55.970  50.958 -16.511  1.00 39.43           S
ANISOU 2196  SD  MET A 272     4433   4224   6324    318   -387   -355       S
ATOM   2197  CE  MET A 272     -55.773  52.726 -16.723  1.00 40.39           C
ANISOU 2197  CE  MET A 272     4557   4262   6529    278   -393   -312       C
ATOM   2198  N   ASP A 273     -59.160  53.026 -19.796  1.00 34.61           N
ANISOU 2198  N   ASP A 273     3922   3175   6052    196   -328   -507       N
ATOM   2199  CA  ASP A 273     -58.637  53.791 -20.919  1.00 34.77           C
ANISOU 2199  CA  ASP A 273     3964   3128   6118    145   -279   -461       C
ATOM   2200  C   ASP A 273     -57.122  53.881 -20.792  1.00 35.66           C
ANISOU 2200  C   ASP A 273     4072   3289   6188    150   -280   -383       C
ATOM   2201  O   ASP A 273     -56.607  54.434 -19.813  1.00 35.20           O
ANISOU 2201  O   ASP A 273     3974   3291   6111    173   -312   -358       O
ATOM   2202  CB  ASP A 273     -59.263  55.183 -20.957  1.00 33.85           C
ANISOU 2202  CB  ASP A 273     3808   2970   6083    122   -270   -498       C
ATOM   2203  CG  ASP A 273     -59.197  55.815 -22.334  1.00 34.23           C
ANISOU 2203  CG  ASP A 273     3880   2942   6184     69   -206   -484       C
ATOM   2204  OD1 ASP A 273     -59.073  55.066 -23.326  1.00 32.70           O
ANISOU 2204  OD1 ASP A 273     3746   2712   5965     46   -172   -458       O
ATOM   2205  OD2 ASP A 273     -59.262  57.059 -22.425  1.00 32.85           O
ANISOU 2205  OD2 ASP A 273     3661   2751   6069     56   -193   -504       O
ATOM   2206  N   SER A 274     -56.408  53.326 -21.768  1.00 24.18           N
ANISOU 2206  N   SER A 274     2662   1806   4720    127   -251   -342       N
ATOM   2207  CA  SER A 274     -54.956  53.383 -21.769  1.00 27.31           C
ANISOU 2207  CA  SER A 274     3054   2228   5094    120   -256   -270       C
ATOM   2208  C   SER A 274     -54.463  53.407 -23.207  1.00 26.58           C
ANISOU 2208  C   SER A 274     3009   2061   5028     83   -220   -256       C
ATOM   2209  O   SER A 274     -55.146  52.938 -24.121  1.00 25.34           O
ANISOU 2209  O   SER A 274     2896   1861   4872     70   -193   -286       O
ATOM   2210  CB  SER A 274     -54.339  52.202 -21.008  1.00 32.18           C
ANISOU 2210  CB  SER A 274     3655   2940   5631    144   -278   -233       C
ATOM   2211  OG  SER A 274     -54.706  50.968 -21.595  1.00 45.60           O
ANISOU 2211  OG  SER A 274     5387   4634   7305    152   -269   -260       O
ATOM   2212  N   THR A 275     -53.266  53.968 -23.395  1.00 31.18           N
ANISOU 2212  N   THR A 275     3587   2629   5632     68   -227   -210       N
ATOM   2213  CA  THR A 275     -52.697  54.076 -24.735  1.00 31.93           C
ANISOU 2213  CA  THR A 275     3723   2659   5749     40   -203   -211       C
ATOM   2214  C   THR A 275     -52.454  52.700 -25.342  1.00 30.80           C
ANISOU 2214  C   THR A 275     3619   2530   5554     34   -202   -198       C
ATOM   2215  O   THR A 275     -52.751  52.472 -26.521  1.00 34.01           O
ANISOU 2215  O   THR A 275     4075   2893   5954     21   -175   -224       O
ATOM   2216  CB  THR A 275     -51.400  54.884 -24.687  1.00 35.33           C
ANISOU 2216  CB  THR A 275     4138   3063   6225     30   -229   -171       C
ATOM   2217  OG1 THR A 275     -51.685  56.218 -24.247  1.00 38.43           O
ANISOU 2217  OG1 THR A 275     4496   3432   6675     45   -237   -192       O
ATOM   2218  CG2 THR A 275     -50.749  54.937 -26.060  1.00 36.78           C
ANISOU 2218  CG2 THR A 275     4363   3184   6428      8   -214   -189       C
ATOM   2219  N   VAL A 276     -51.922  51.770 -24.555  1.00 29.47           N
ANISOU 2219  N   VAL A 276     3424   2432   5342     47   -230   -158       N
ATOM   2220  CA  VAL A 276     -51.734  50.385 -24.972  1.00 29.06           C
ANISOU 2220  CA  VAL A 276     3391   2408   5244     52   -238   -154       C
ATOM   2221  C   VAL A 276     -52.746  49.524 -24.230  1.00 26.60           C
ANISOU 2221  C   VAL A 276     3065   2152   4890     94   -246   -187       C
ATOM   2222  O   VAL A 276     -52.826  49.572 -22.997  1.00 27.20           O
ANISOU 2222  O   VAL A 276     3091   2300   4944    116   -259   -181       O
ATOM   2223  CB  VAL A 276     -50.299  49.899 -24.704  1.00 31.08           C
ANISOU 2223  CB  VAL A 276     3612   2708   5489     33   -262    -93       C
ATOM   2224  CG1 VAL A 276     -50.190  48.404 -24.962  1.00 33.54           C
ANISOU 2224  CG1 VAL A 276     3921   3068   5754     48   -274   -100       C
ATOM   2225  CG2 VAL A 276     -49.313  50.660 -25.572  1.00 26.02           C
ANISOU 2225  CG2 VAL A 276     2992   1991   4902     -5   -268    -77       C
ATOM   2226  N   LYS A 277     -53.519  48.746 -24.980  1.00 29.45           N
ANISOU 2226  N   LYS A 277     3472   2477   5239    108   -244   -224       N
ATOM   2227  CA  LYS A 277     -54.492  47.828 -24.408  1.00 32.56           C
ANISOU 2227  CA  LYS A 277     3860   2903   5608    154   -264   -267       C
ATOM   2228  C   LYS A 277     -53.962  46.403 -24.476  1.00 33.25           C
ANISOU 2228  C   LYS A 277     3935   3046   5652    186   -291   -264       C
ATOM   2229  O   LYS A 277     -53.323  46.011 -25.457  1.00 33.17           O
ANISOU 2229  O   LYS A 277     3954   3008   5639    168   -295   -241       O
ATOM   2230  CB  LYS A 277     -55.833  47.924 -25.138  1.00 35.77           C
ANISOU 2230  CB  LYS A 277     4328   3217   6046    150   -255   -307       C
ATOM   2231  CG  LYS A 277     -56.573  49.232 -24.912  1.00 36.53           C
ANISOU 2231  CG  LYS A 277     4414   3272   6191    123   -229   -326       C
ATOM   2232  CD  LYS A 277     -56.951  49.407 -23.449  1.00 35.89           C
ANISOU 2232  CD  LYS A 277     4272   3257   6108    158   -255   -360       C
ATOM   2233  CE  LYS A 277     -57.879  48.298 -22.978  1.00 34.29           C
ANISOU 2233  CE  LYS A 277     4073   3064   5890    208   -294   -416       C
ATOM   2234  NZ  LYS A 277     -58.219  48.438 -21.535  1.00 37.30           N
ANISOU 2234  NZ  LYS A 277     4393   3525   6254    250   -324   -463       N
ATOM   2235  N   ASN A 278     -54.225  45.633 -23.425  1.00 33.32           N
ANISOU 2235  N   ASN A 278     3893   3140   5625    237   -313   -296       N
ATOM   2236  CA  ASN A 278     -53.812  44.238 -23.338  1.00 30.87           C
ANISOU 2236  CA  ASN A 278     3551   2903   5276    279   -338   -308       C
ATOM   2237  C   ASN A 278     -55.057  43.362 -23.319  1.00 32.31           C
ANISOU 2237  C   ASN A 278     3759   3056   5462    345   -374   -386       C
ATOM   2238  O   ASN A 278     -55.938  43.547 -22.472  1.00 27.94           O
ANISOU 2238  O   ASN A 278     3190   2515   4910    377   -383   -438       O
ATOM   2239  CB  ASN A 278     -52.957  43.993 -22.095  1.00 34.91           C
ANISOU 2239  CB  ASN A 278     3967   3561   5735    289   -330   -285       C
ATOM   2240  CG  ASN A 278     -51.619  44.701 -22.161  1.00 46.98           C
ANISOU 2240  CG  ASN A 278     5474   5104   7274    219   -308   -195       C
ATOM   2241  OD1 ASN A 278     -51.065  44.908 -23.242  1.00 49.43           O
ANISOU 2241  OD1 ASN A 278     5824   5335   7622    177   -308   -166       O
ATOM   2242  ND2 ASN A 278     -51.089  45.076 -21.002  1.00 52.59           N
ANISOU 2242  ND2 ASN A 278     6123   5912   7948    208   -294   -151       N
ATOM   2243  N   TYR A 279     -55.125  42.413 -24.249  1.00 36.10           N
ANISOU 2243  N   TYR A 279     4279   3490   5947    367   -404   -395       N
ATOM   2244  CA  TYR A 279     -56.287  41.551 -24.402  1.00 34.81           C
ANISOU 2244  CA  TYR A 279     4155   3269   5803    430   -452   -460       C
ATOM   2245  C   TYR A 279     -55.874  40.088 -24.369  1.00 35.73           C
ANISOU 2245  C   TYR A 279     4228   3456   5893    500   -497   -494       C
ATOM   2246  O   TYR A 279     -54.805  39.720 -24.865  1.00 36.10           O
ANISOU 2246  O   TYR A 279     4252   3545   5920    482   -494   -454       O
ATOM   2247  CB  TYR A 279     -57.025  41.828 -25.718  1.00 32.38           C
ANISOU 2247  CB  TYR A 279     3956   2811   5534    395   -458   -433       C
ATOM   2248  CG  TYR A 279     -57.583  43.226 -25.854  1.00 33.89           C
ANISOU 2248  CG  TYR A 279     4183   2933   5760    328   -411   -410       C
ATOM   2249  CD1 TYR A 279     -58.632  43.657 -25.053  1.00 37.27           C
ANISOU 2249  CD1 TYR A 279     4599   3338   6224    338   -415   -459       C
ATOM   2250  CD2 TYR A 279     -57.079  44.106 -26.802  1.00 32.39           C
ANISOU 2250  CD2 TYR A 279     4032   2704   5570    259   -366   -352       C
ATOM   2251  CE1 TYR A 279     -59.151  44.932 -25.180  1.00 39.21           C
ANISOU 2251  CE1 TYR A 279     4862   3526   6509    276   -374   -444       C
ATOM   2252  CE2 TYR A 279     -57.593  45.381 -26.939  1.00 32.49           C
ANISOU 2252  CE2 TYR A 279     4063   2664   5617    204   -320   -341       C
ATOM   2253  CZ  TYR A 279     -58.628  45.789 -26.126  1.00 37.17           C
ANISOU 2253  CZ  TYR A 279     4636   3238   6251    210   -323   -384       C
ATOM   2254  OH  TYR A 279     -59.144  47.059 -26.257  1.00 43.48           O
ANISOU 2254  OH  TYR A 279     5438   3992   7092    154   -278   -379       O
ATOM   2255  N   PHE A 280     -56.732  39.261 -23.777  1.00 36.16           N
ANISOU 2255  N   PHE A 280     4266   3520   5954    584   -543   -578       N
ATOM   2256  CA  PHE A 280     -56.669  37.813 -23.938  1.00 32.71           C
ANISOU 2256  CA  PHE A 280     3803   3115   5511    669   -602   -631       C
ATOM   2257  C   PHE A 280     -57.520  37.475 -25.157  1.00 32.59           C
ANISOU 2257  C   PHE A 280     3903   2933   5546    679   -657   -621       C
ATOM   2258  O   PHE A 280     -58.748  37.597 -25.118  1.00 36.72           O
ANISOU 2258  O   PHE A 280     4486   3348   6116    696   -688   -655       O
ATOM   2259  CB  PHE A 280     -57.165  37.107 -22.677  1.00 30.14           C
ANISOU 2259  CB  PHE A 280     3399   2885   5169    765   -629   -740       C
ATOM   2260  CG  PHE A 280     -56.793  35.645 -22.590  1.00 33.38           C
ANISOU 2260  CG  PHE A 280     3738   3384   5561    858   -676   -804       C
ATOM   2261  CD1 PHE A 280     -56.641  34.868 -23.728  1.00 38.97           C
ANISOU 2261  CD1 PHE A 280     4491   4018   6298    879   -728   -785       C
ATOM   2262  CD2 PHE A 280     -56.603  35.047 -21.354  1.00 35.19           C
ANISOU 2262  CD2 PHE A 280     3851   3782   5739    931   -667   -887       C
ATOM   2263  CE1 PHE A 280     -56.306  33.528 -23.637  1.00 38.16           C
ANISOU 2263  CE1 PHE A 280     4311   4000   6188    972   -778   -853       C
ATOM   2264  CE2 PHE A 280     -56.267  33.708 -21.256  1.00 36.93           C
ANISOU 2264  CE2 PHE A 280     3988   4097   5946   1023   -705   -958       C
ATOM   2265  CZ  PHE A 280     -56.119  32.948 -22.399  1.00 36.52           C
ANISOU 2265  CZ  PHE A 280     3976   3962   5938   1044   -763   -942       C
ATOM   2266  N   ILE A 281     -56.868  37.064 -26.239  1.00 34.50           N
ANISOU 2266  N   ILE A 281     4178   3153   5778    664   -675   -570       N
ATOM   2267  CA  ILE A 281     -57.518  36.887 -27.531  1.00 35.55           C
ANISOU 2267  CA  ILE A 281     4432   3137   5937    657   -720   -532       C
ATOM   2268  C   ILE A 281     -57.597  35.402 -27.856  1.00 35.19           C
ANISOU 2268  C   ILE A 281     4384   3086   5900    757   -813   -578       C
ATOM   2269  O   ILE A 281     -56.641  34.653 -27.628  1.00 37.05           O
ANISOU 2269  O   ILE A 281     4527   3440   6110    798   -827   -606       O
ATOM   2270  CB  ILE A 281     -56.771  37.660 -28.637  1.00 35.01           C
ANISOU 2270  CB  ILE A 281     4418   3044   5840    566   -676   -442       C
ATOM   2271  CG1 ILE A 281     -57.352  37.334 -30.014  1.00 41.49           C
ANISOU 2271  CG1 ILE A 281     5364   3739   6662    566   -724   -397       C
ATOM   2272  CG2 ILE A 281     -55.278  37.368 -28.584  1.00 38.28           C
ANISOU 2272  CG2 ILE A 281     4744   3581   6219    558   -664   -433       C
ATOM   2273  CD1 ILE A 281     -56.740  38.137 -31.137  1.00 48.34           C
ANISOU 2273  CD1 ILE A 281     6291   4587   7488    484   -680   -323       C
ATOM   2274  N   THR A 282     -58.749  34.979 -28.376  1.00 33.89           N
ANISOU 2274  N   THR A 282     4316   2779   5779    796   -882   -583       N
ATOM   2275  CA  THR A 282     -58.956  33.617 -28.853  1.00 31.45           C
ANISOU 2275  CA  THR A 282     4029   2430   5491    897   -989   -618       C
ATOM   2276  C   THR A 282     -59.598  33.687 -30.229  1.00 35.14           C
ANISOU 2276  C   THR A 282     4649   2737   5966    863  -1030   -528       C
ATOM   2277  O   THR A 282     -60.706  34.216 -30.371  1.00 39.84           O
ANISOU 2277  O   THR A 282     5332   3203   6601    823  -1026   -497       O
ATOM   2278  CB  THR A 282     -59.838  32.813 -27.892  1.00 34.64           C
ANISOU 2278  CB  THR A 282     4392   2819   5950   1008  -1056   -732       C
ATOM   2279  OG1 THR A 282     -59.212  32.742 -26.606  1.00 38.74           O
ANISOU 2279  OG1 THR A 282     4766   3515   6439   1040  -1009   -813       O
ATOM   2280  CG2 THR A 282     -60.050  31.403 -28.423  1.00 32.94           C
ANISOU 2280  CG2 THR A 282     4198   2550   5766   1123  -1179   -771       C
ATOM   2281  N   ASP A 283     -58.906  33.162 -31.237  1.00 31.98           N
ANISOU 2281  N   ASP A 283     4277   2348   5524    874  -1071   -485       N
ATOM   2282  CA  ASP A 283     -59.430  33.159 -32.596  1.00 34.27           C
ANISOU 2282  CA  ASP A 283     4717   2506   5798    846  -1114   -392       C
ATOM   2283  C   ASP A 283     -60.398  31.995 -32.773  1.00 40.19           C
ANISOU 2283  C   ASP A 283     5528   3136   6604    951  -1243   -415       C
ATOM   2284  O   ASP A 283     -60.046  30.839 -32.518  1.00 44.27           O
ANISOU 2284  O   ASP A 283     5976   3705   7139   1062  -1327   -491       O
ATOM   2285  CB  ASP A 283     -58.289  33.066 -33.608  1.00 36.02           C
ANISOU 2285  CB  ASP A 283     4948   2794   5945    823  -1117   -344       C
ATOM   2286  CG  ASP A 283     -58.779  33.117 -35.041  1.00 39.63           C
ANISOU 2286  CG  ASP A 283     5563   3139   6358    793  -1155   -243       C
ATOM   2287  OD1 ASP A 283     -59.225  34.198 -35.480  1.00 40.48           O
ANISOU 2287  OD1 ASP A 283     5749   3193   6440    695  -1077   -171       O
ATOM   2288  OD2 ASP A 283     -58.719  32.076 -35.730  1.00 42.18           O
ANISOU 2288  OD2 ASP A 283     5927   3434   6666    869  -1264   -235       O
ATOM   2289  N   ALA A 284     -61.618  32.304 -33.217  1.00 38.71           N
ANISOU 2289  N   ALA A 284     5468   2788   6454    914  -1260   -350       N
ATOM   2290  CA  ALA A 284     -62.654  31.282 -33.317  1.00 36.99           C
ANISOU 2290  CA  ALA A 284     5318   2425   6311   1007  -1391   -366       C
ATOM   2291  C   ALA A 284     -62.458  30.367 -34.519  1.00 35.78           C
ANISOU 2291  C   ALA A 284     5252   2223   6120   1063  -1498   -303       C
ATOM   2292  O   ALA A 284     -62.847  29.195 -34.467  1.00 45.08           O
ANISOU 2292  O   ALA A 284     6430   3362   7338   1170  -1613   -349       O
ATOM   2293  CB  ALA A 284     -64.034  31.937 -33.380  1.00 38.25           C
ANISOU 2293  CB  ALA A 284     5574   2442   6516    924  -1363   -303       C
ATOM   2294  N   GLN A 285     -61.864  30.870 -35.601  1.00 35.44           N
ANISOU 2294  N   GLN A 285     5273   2215   5979    985  -1452   -203       N
ATOM   2295  CA  GLN A 285     -61.730  30.058 -36.805  1.00 41.62           C
ANISOU 2295  CA  GLN A 285     6152   2952   6711   1035  -1560   -135       C
ATOM   2296  C   GLN A 285     -60.644  28.999 -36.658  1.00 41.71           C
ANISOU 2296  C   GLN A 285     6050   3087   6712   1147  -1638   -229       C
ATOM   2297  O   GLN A 285     -60.846  27.842 -37.044  1.00 45.96           O
ANISOU 2297  O   GLN A 285     6621   3566   7275   1259  -1779   -241       O
ATOM   2298  CB  GLN A 285     -61.440  30.950 -38.013  1.00 41.19           C
ANISOU 2298  CB  GLN A 285     6199   2911   6540    921  -1486    -11       C
ATOM   2299  CG  GLN A 285     -61.399  30.205 -39.338  1.00 48.05           C
ANISOU 2299  CG  GLN A 285     7189   3733   7336    965  -1598     74       C
ATOM   2300  CD  GLN A 285     -62.729  29.562 -39.686  1.00 57.57           C
ANISOU 2300  CD  GLN A 285     8529   4747   8597   1007  -1710    151       C
ATOM   2301  OE1 GLN A 285     -63.697  30.249 -40.013  1.00 59.95           O
ANISOU 2301  OE1 GLN A 285     8939   4939   8900    912  -1659    256       O
ATOM   2302  NE2 GLN A 285     -62.783  28.237 -39.614  1.00 58.58           N
ANISOU 2302  NE2 GLN A 285     8646   4830   8780   1148  -1866     98       N
ATOM   2303  N   THR A 286     -59.492  29.370 -36.103  1.00 43.42           N
ANISOU 2303  N   THR A 286     6128   3470   6899   1117  -1552   -293       N
ATOM   2304  CA  THR A 286     -58.337  28.484 -36.055  1.00 42.26           C
ANISOU 2304  CA  THR A 286     5863   3455   6739   1195  -1608   -369       C
ATOM   2305  C   THR A 286     -58.057  27.903 -34.679  1.00 41.59           C
ANISOU 2305  C   THR A 286     5606   3475   6723   1274  -1605   -505       C
ATOM   2306  O   THR A 286     -57.516  26.799 -34.591  1.00 44.63           O
ANISOU 2306  O   THR A 286     5897   3933   7126   1377  -1690   -581       O
ATOM   2307  CB  THR A 286     -57.082  29.223 -36.534  1.00 38.48           C
ANISOU 2307  CB  THR A 286     5348   3096   6178   1099  -1525   -339       C
ATOM   2308  OG1 THR A 286     -56.745  30.253 -35.597  1.00 36.61           O
ANISOU 2308  OG1 THR A 286     5025   2935   5951   1014  -1388   -362       O
ATOM   2309  CG2 THR A 286     -57.325  29.849 -37.897  1.00 38.91           C
ANISOU 2309  CG2 THR A 286     5568   3072   6146   1025  -1517   -218       C
ATOM   2310  N   GLY A 287     -58.408  28.610 -33.610  1.00 40.26           N
ANISOU 2310  N   GLY A 287     5386   3326   6586   1230  -1509   -540       N
ATOM   2311  CA  GLY A 287     -58.062  28.184 -32.273  1.00 37.20           C
ANISOU 2311  CA  GLY A 287     4831   3068   6235   1294  -1487   -664       C
ATOM   2312  C   GLY A 287     -56.776  28.769 -31.735  1.00 36.58           C
ANISOU 2312  C   GLY A 287     4622   3167   6109   1216  -1373   -674       C
ATOM   2313  O   GLY A 287     -56.384  28.433 -30.610  1.00 36.96           O
ANISOU 2313  O   GLY A 287     4524   3349   6172   1259  -1342   -765       O
ATOM   2314  N   SER A 288     -56.103  29.623 -32.501  1.00 32.90           N
ANISOU 2314  N   SER A 288     4204   2709   5587   1106  -1314   -585       N
ATOM   2315  CA  SER A 288     -54.900  30.280 -32.017  1.00 35.10           C
ANISOU 2315  CA  SER A 288     4373   3130   5836   1022  -1212   -583       C
ATOM   2316  C   SER A 288     -55.267  31.335 -30.980  1.00 36.51           C
ANISOU 2316  C   SER A 288     4529   3322   6021    959  -1105   -583       C
ATOM   2317  O   SER A 288     -56.247  32.067 -31.138  1.00 30.84           O
ANISOU 2317  O   SER A 288     3918   2487   5313    921  -1081   -542       O
ATOM   2318  CB  SER A 288     -54.144  30.916 -33.182  1.00 34.00           C
ANISOU 2318  CB  SER A 288     4300   2974   5643    932  -1194   -500       C
ATOM   2319  OG  SER A 288     -52.787  31.138 -32.849  1.00 43.33           O
ANISOU 2319  OG  SER A 288     5360   4289   6814    876  -1141   -512       O
ATOM   2320  N   SER A 289     -54.480  31.408 -29.908  1.00 35.48           N
ANISOU 2320  N   SER A 289     4255   3342   5886    946  -1041   -625       N
ATOM   2321  CA  SER A 289     -54.802  32.294 -28.799  1.00 35.72           C
ANISOU 2321  CA  SER A 289     4252   3403   5915    904   -953   -634       C
ATOM   2322  C   SER A 289     -53.517  32.809 -28.164  1.00 33.20           C
ANISOU 2322  C   SER A 289     3817   3232   5566    828   -868   -611       C
ATOM   2323  O   SER A 289     -52.427  32.279 -28.391  1.00 34.32           O
ANISOU 2323  O   SER A 289     3878   3463   5699    822   -881   -609       O
ATOM   2324  CB  SER A 289     -55.677  31.582 -27.760  1.00 30.88           C
ANISOU 2324  CB  SER A 289     3588   2813   5332   1011   -989   -737       C
ATOM   2325  OG  SER A 289     -55.022  30.442 -27.236  1.00 31.67           O
ANISOU 2325  OG  SER A 289     3549   3058   5427   1094  -1019   -817       O
ATOM   2326  N   LYS A 290     -53.665  33.860 -27.358  1.00 28.96           N
ANISOU 2326  N   LYS A 290     3272   2714   5019    769   -787   -591       N
ATOM   2327  CA  LYS A 290     -52.544  34.453 -26.637  1.00 31.83           C
ANISOU 2327  CA  LYS A 290     3536   3203   5356    695   -709   -555       C
ATOM   2328  C   LYS A 290     -53.083  35.187 -25.418  1.00 28.28           C
ANISOU 2328  C   LYS A 290     3062   2791   4892    687   -650   -571       C
ATOM   2329  O   LYS A 290     -54.036  35.963 -25.534  1.00 27.86           O
ANISOU 2329  O   LYS A 290     3102   2626   4856    670   -642   -562       O
ATOM   2330  CB  LYS A 290     -51.747  35.407 -27.536  1.00 29.34           C
ANISOU 2330  CB  LYS A 290     3276   2831   5041    588   -678   -468       C
ATOM   2331  CG  LYS A 290     -50.561  36.067 -26.847  1.00 28.97           C
ANISOU 2331  CG  LYS A 290     3138   2885   4984    505   -610   -418       C
ATOM   2332  CD  LYS A 290     -49.537  36.573 -27.853  1.00 31.04           C
ANISOU 2332  CD  LYS A 290     3431   3102   5262    423   -612   -359       C
ATOM   2333  CE  LYS A 290     -50.147  37.569 -28.824  1.00 33.77           C
ANISOU 2333  CE  LYS A 290     3916   3303   5611    388   -606   -330       C
ATOM   2334  NZ  LYS A 290     -49.137  38.098 -29.783  1.00 34.00           N
ANISOU 2334  NZ  LYS A 290     3973   3295   5651    318   -610   -292       N
ATOM   2335  N   CYS A 291     -52.470  34.942 -24.258  1.00 29.34           N
ANISOU 2335  N   CYS A 291     3068   3089   4989    697   -610   -592       N
ATOM   2336  CA  CYS A 291     -52.981  35.501 -23.009  1.00 28.60           C
ANISOU 2336  CA  CYS A 291     2944   3056   4865    706   -565   -619       C
ATOM   2337  C   CYS A 291     -52.855  37.018 -22.983  1.00 27.71           C
ANISOU 2337  C   CYS A 291     2888   2884   4755    606   -510   -535       C
ATOM   2338  O   CYS A 291     -53.789  37.721 -22.581  1.00 34.03           O
ANISOU 2338  O   CYS A 291     3739   3629   5563    611   -503   -556       O
ATOM   2339  CB  CYS A 291     -52.243  34.891 -21.818  1.00 38.02           C
ANISOU 2339  CB  CYS A 291     3986   4462   5999    733   -528   -647       C
ATOM   2340  SG  CYS A 291     -52.536  33.133 -21.576  1.00 45.76           S
ANISOU 2340  SG  CYS A 291     4872   5540   6973    876   -588   -779       S
ATOM   2341  N   VAL A 292     -51.703  37.541 -23.386  1.00 34.99           N
ANISOU 2341  N   VAL A 292     3798   3817   5680    517   -478   -447       N
ATOM   2342  CA  VAL A 292     -51.434  38.974 -23.347  1.00 31.94           C
ANISOU 2342  CA  VAL A 292     3453   3379   5303    429   -432   -372       C
ATOM   2343  C   VAL A 292     -51.065  39.400 -24.760  1.00 36.60           C
ANISOU 2343  C   VAL A 292     4127   3844   5935    372   -446   -326       C
ATOM   2344  O   VAL A 292     -49.931  39.191 -25.208  1.00 40.22           O
ANISOU 2344  O   VAL A 292     4550   4329   6403    329   -450   -286       O
ATOM   2345  CB  VAL A 292     -50.324  39.332 -22.355  1.00 32.79           C
ANISOU 2345  CB  VAL A 292     3465   3618   5376    374   -382   -308       C
ATOM   2346  CG1 VAL A 292     -50.200  40.840 -22.234  1.00 32.58           C
ANISOU 2346  CG1 VAL A 292     3486   3524   5367    303   -350   -241       C
ATOM   2347  CG2 VAL A 292     -50.597  38.704 -21.004  1.00 34.03           C
ANISOU 2347  CG2 VAL A 292     3528   3935   5467    439   -366   -360       C
ATOM   2348  N   CYS A 293     -52.014  40.001 -25.466  1.00 37.31           N
ANISOU 2348  N   CYS A 293     4324   3803   6050    369   -452   -334       N
ATOM   2349  CA  CYS A 293     -51.780  40.544 -26.799  1.00 38.79           C
ANISOU 2349  CA  CYS A 293     4596   3882   6259    318   -456   -296       C
ATOM   2350  C   CYS A 293     -51.850  42.063 -26.692  1.00 36.51           C
ANISOU 2350  C   CYS A 293     4340   3542   5991    256   -405   -260       C
ATOM   2351  O   CYS A 293     -52.937  42.638 -26.586  1.00 30.56           O
ANISOU 2351  O   CYS A 293     3633   2729   5249    262   -390   -279       O
ATOM   2352  CB  CYS A 293     -52.794  39.998 -27.800  1.00 45.54           C
ANISOU 2352  CB  CYS A 293     5547   4639   7118    361   -499   -325       C
ATOM   2353  SG  CYS A 293     -52.364  40.321 -29.523  1.00 54.38           S
ANISOU 2353  SG  CYS A 293     6764   5668   8232    313   -512   -285       S
ATOM   2354  N   SER A 294     -50.686  42.707 -26.705  1.00 38.23           N
ANISOU 2354  N   SER A 294     4526   3778   6221    196   -386   -211       N
ATOM   2355  CA  SER A 294     -50.625  44.161 -26.624  1.00 35.11           C
ANISOU 2355  CA  SER A 294     4155   3333   5854    145   -348   -182       C
ATOM   2356  C   SER A 294     -51.069  44.769 -27.949  1.00 31.85           C
ANISOU 2356  C   SER A 294     3836   2809   5455    125   -340   -193       C
ATOM   2357  O   SER A 294     -50.501  44.465 -29.003  1.00 33.83           O
ANISOU 2357  O   SER A 294     4121   3032   5700    113   -362   -191       O
ATOM   2358  CB  SER A 294     -49.212  44.613 -26.270  1.00 37.29           C
ANISOU 2358  CB  SER A 294     4372   3646   6151     91   -343   -126       C
ATOM   2359  OG  SER A 294     -48.821  44.117 -25.001  1.00 39.28           O
ANISOU 2359  OG  SER A 294     4534   4015   6376     99   -338   -101       O
ATOM   2360  N   VAL A 295     -52.086  45.623 -27.894  1.00 31.83           N
ANISOU 2360  N   VAL A 295     3872   2755   5468    122   -309   -208       N
ATOM   2361  CA  VAL A 295     -52.669  46.236 -29.080  1.00 32.59           C
ANISOU 2361  CA  VAL A 295     4050   2764   5567     99   -285   -216       C
ATOM   2362  C   VAL A 295     -52.648  47.747 -28.907  1.00 31.48           C
ANISOU 2362  C   VAL A 295     3899   2596   5466     62   -241   -214       C
ATOM   2363  O   VAL A 295     -52.919  48.262 -27.816  1.00 30.70           O
ANISOU 2363  O   VAL A 295     3751   2523   5390     67   -232   -215       O
ATOM   2364  CB  VAL A 295     -54.108  45.734 -29.329  1.00 33.14           C
ANISOU 2364  CB  VAL A 295     4177   2789   5627    126   -290   -237       C
ATOM   2365  CG1 VAL A 295     -54.686  46.353 -30.593  1.00 32.54           C
ANISOU 2365  CG1 VAL A 295     4185   2638   5543     90   -255   -229       C
ATOM   2366  CG2 VAL A 295     -54.132  44.215 -29.416  1.00 30.99           C
ANISOU 2366  CG2 VAL A 295     3909   2539   5326    178   -347   -247       C
ATOM   2367  N   ILE A 296     -52.315  48.456 -29.982  1.00 29.63           N
ANISOU 2367  N   ILE A 296     3707   2316   5235     32   -219   -218       N
ATOM   2368  CA  ILE A 296     -52.318  49.913 -29.997  1.00 32.17           C
ANISOU 2368  CA  ILE A 296     4017   2608   5599      6   -179   -231       C
ATOM   2369  C   ILE A 296     -52.977  50.371 -31.292  1.00 32.85           C
ANISOU 2369  C   ILE A 296     4170   2649   5662    -12   -134   -254       C
ATOM   2370  O   ILE A 296     -52.832  49.726 -32.336  1.00 33.54           O
ANISOU 2370  O   ILE A 296     4316   2729   5699    -11   -145   -253       O
ATOM   2371  CB  ILE A 296     -50.890  50.483 -29.849  1.00 31.74           C
ANISOU 2371  CB  ILE A 296     3924   2555   5582     -9   -200   -219       C
ATOM   2372  CG1 ILE A 296     -50.929  51.998 -29.644  1.00 28.38           C
ANISOU 2372  CG1 ILE A 296     3474   2097   5212    -19   -172   -238       C
ATOM   2373  CG2 ILE A 296     -50.027  50.120 -31.050  1.00 29.48           C
ANISOU 2373  CG2 ILE A 296     3678   2248   5274    -18   -222   -231       C
ATOM   2374  CD1 ILE A 296     -49.582  52.597 -29.333  1.00 24.79           C
ANISOU 2374  CD1 ILE A 296     2983   1625   4812    -30   -207   -219       C
ATOM   2375  N   ASP A 297     -53.726  51.471 -31.218  1.00 31.03           N
ANISOU 2375  N   ASP A 297     3927   2398   5465    -29    -84   -275       N
ATOM   2376  CA  ASP A 297     -54.437  52.000 -32.380  1.00 32.21           C
ANISOU 2376  CA  ASP A 297     4127   2524   5589    -56    -25   -293       C
ATOM   2377  C   ASP A 297     -53.689  53.225 -32.896  1.00 35.77           C
ANISOU 2377  C   ASP A 297     4556   2973   6063    -63      5   -334       C
ATOM   2378  O   ASP A 297     -54.046  54.372 -32.629  1.00 37.89           O
ANISOU 2378  O   ASP A 297     4778   3237   6382    -71     44   -364       O
ATOM   2379  CB  ASP A 297     -55.883  52.330 -32.030  1.00 30.89           C
ANISOU 2379  CB  ASP A 297     3950   2339   5449    -77     15   -294       C
ATOM   2380  CG  ASP A 297     -56.670  52.834 -33.226  1.00 36.76           C
ANISOU 2380  CG  ASP A 297     4739   3067   6161   -118     88   -296       C
ATOM   2381  OD1 ASP A 297     -56.205  52.655 -34.373  1.00 37.29           O
ANISOU 2381  OD1 ASP A 297     4863   3144   6161   -122    101   -293       O
ATOM   2382  OD2 ASP A 297     -57.756  53.413 -33.019  1.00 43.34           O
ANISOU 2382  OD2 ASP A 297     5549   3886   7034   -150    132   -302       O
ATOM   2383  N   LEU A 298     -52.633  52.964 -33.655  1.00 32.85           N
ANISOU 2383  N   LEU A 298     4216   2604   5661    -55    -23   -345       N
ATOM   2384  CA  LEU A 298     -51.893  54.007 -34.344  1.00 29.92           C
ANISOU 2384  CA  LEU A 298     3837   2226   5307    -52     -5   -401       C
ATOM   2385  C   LEU A 298     -52.366  54.106 -35.786  1.00 32.82           C
ANISOU 2385  C   LEU A 298     4269   2612   5590    -64     52   -429       C
ATOM   2386  O   LEU A 298     -52.816  53.122 -36.380  1.00 35.79           O
ANISOU 2386  O   LEU A 298     4711   2999   5888    -71     48   -392       O
ATOM   2387  CB  LEU A 298     -50.389  53.727 -34.317  1.00 29.61           C
ANISOU 2387  CB  LEU A 298     3788   2171   5293    -38    -77   -407       C
ATOM   2388  CG  LEU A 298     -49.645  53.896 -32.993  1.00 31.08           C
ANISOU 2388  CG  LEU A 298     3906   2340   5562    -35   -128   -374       C
ATOM   2389  CD1 LEU A 298     -48.227  53.361 -33.117  1.00 29.35           C
ANISOU 2389  CD1 LEU A 298     3686   2104   5362    -39   -199   -365       C
ATOM   2390  CD2 LEU A 298     -49.632  55.356 -32.571  1.00 31.49           C
ANISOU 2390  CD2 LEU A 298     3908   2365   5692    -26   -109   -409       C
ATOM   2391  N   LEU A 299     -52.273  55.311 -36.343  1.00 35.04           N
ANISOU 2391  N   LEU A 299     4527   2902   5883    -62    103   -494       N
ATOM   2392  CA  LEU A 299     -52.432  55.463 -37.780  1.00 33.22           C
ANISOU 2392  CA  LEU A 299     4356   2712   5557    -68    156   -531       C
ATOM   2393  C   LEU A 299     -51.370  54.628 -38.479  1.00 35.85           C
ANISOU 2393  C   LEU A 299     4745   3044   5833    -46     85   -543       C
ATOM   2394  O   LEU A 299     -50.200  54.641 -38.087  1.00 38.73           O
ANISOU 2394  O   LEU A 299     5078   3375   6262    -26     14   -569       O
ATOM   2395  CB  LEU A 299     -52.311  56.932 -38.180  1.00 30.73           C
ANISOU 2395  CB  LEU A 299     3989   2416   5271    -56    215   -621       C
ATOM   2396  CG  LEU A 299     -52.543  57.245 -39.659  1.00 31.71           C
ANISOU 2396  CG  LEU A 299     4161   2608   5282    -59    289   -672       C
ATOM   2397  CD1 LEU A 299     -53.997  57.014 -40.031  1.00 29.95           C
ANISOU 2397  CD1 LEU A 299     3970   2424   4984   -113    376   -604       C
ATOM   2398  CD2 LEU A 299     -52.123  58.668 -39.985  1.00 32.77           C
ANISOU 2398  CD2 LEU A 299     4230   2763   5457    -27    329   -788       C
ATOM   2399  N   LEU A 300     -51.786  53.878 -39.502  1.00 37.77           N
ANISOU 2399  N   LEU A 300     5070   3322   5959    -54     98   -518       N
ATOM   2400  CA  LEU A 300     -50.868  52.947 -40.152  1.00 37.87           C
ANISOU 2400  CA  LEU A 300     5136   3340   5913    -32     19   -528       C
ATOM   2401  C   LEU A 300     -49.640  53.668 -40.694  1.00 38.96           C
ANISOU 2401  C   LEU A 300     5255   3476   6070     -4    -10   -630       C
ATOM   2402  O   LEU A 300     -48.521  53.148 -40.616  1.00 40.91           O
ANISOU 2402  O   LEU A 300     5498   3695   6353     11   -100   -649       O
ATOM   2403  CB  LEU A 300     -51.588  52.194 -41.268  1.00 37.21           C
ANISOU 2403  CB  LEU A 300     5150   3299   5688    -39     40   -486       C
ATOM   2404  CG  LEU A 300     -50.817  51.031 -41.890  1.00 35.17           C
ANISOU 2404  CG  LEU A 300     4949   3048   5364    -12    -56   -485       C
ATOM   2405  CD1 LEU A 300     -50.421  50.027 -40.820  1.00 32.46           C
ANISOU 2405  CD1 LEU A 300     4566   2661   5105     -3   -141   -440       C
ATOM   2406  CD2 LEU A 300     -51.647  50.364 -42.972  1.00 38.21           C
ANISOU 2406  CD2 LEU A 300     5440   3475   5604    -16    -38   -431       C
ATOM   2407  N   ASP A 301     -49.828  54.874 -41.234  1.00 36.60           N
ANISOU 2407  N   ASP A 301     4940   3209   5758      3     64   -705       N
ATOM   2408  CA  ASP A 301     -48.694  55.649 -41.723  1.00 36.35           C
ANISOU 2408  CA  ASP A 301     4887   3168   5758     40     31   -822       C
ATOM   2409  C   ASP A 301     -47.734  55.990 -40.591  1.00 35.65           C
ANISOU 2409  C   ASP A 301     4724   2991   5830     49    -43   -831       C
ATOM   2410  O   ASP A 301     -46.511  55.975 -40.777  1.00 39.93           O
ANISOU 2410  O   ASP A 301     5262   3489   6420     69   -126   -889       O
ATOM   2411  CB  ASP A 301     -49.189  56.923 -42.407  1.00 42.29           C
ANISOU 2411  CB  ASP A 301     5618   3978   6471     53    134   -906       C
ATOM   2412  CG  ASP A 301     -50.324  56.660 -43.375  1.00 49.11           C
ANISOU 2412  CG  ASP A 301     6548   4936   7176     26    228   -866       C
ATOM   2413  OD1 ASP A 301     -51.374  56.142 -42.936  1.00 50.67           O
ANISOU 2413  OD1 ASP A 301     6760   5131   7362    -18    264   -757       O
ATOM   2414  OD2 ASP A 301     -50.170  56.974 -44.574  1.00 51.30           O
ANISOU 2414  OD2 ASP A 301     6863   5290   7340     48    264   -944       O
ATOM   2415  N   ASP A 302     -48.271  56.298 -39.408  1.00 33.15           N
ANISOU 2415  N   ASP A 302     4351   2648   5598     31    -20   -770       N
ATOM   2416  CA  ASP A 302     -47.415  56.620 -38.271  1.00 35.07           C
ANISOU 2416  CA  ASP A 302     4530   2814   5980     36    -90   -757       C
ATOM   2417  C   ASP A 302     -46.621  55.403 -37.817  1.00 33.12           C
ANISOU 2417  C   ASP A 302     4294   2539   5751     18   -180   -691       C
ATOM   2418  O   ASP A 302     -45.430  55.515 -37.503  1.00 31.37           O
ANISOU 2418  O   ASP A 302     4044   2256   5619     18   -258   -705       O
ATOM   2419  CB  ASP A 302     -48.255  57.171 -37.119  1.00 36.81           C
ANISOU 2419  CB  ASP A 302     4692   3029   6264     25    -47   -706       C
ATOM   2420  CG  ASP A 302     -48.733  58.587 -37.372  1.00 41.33           C
ANISOU 2420  CG  ASP A 302     5220   3617   6866     48     23   -786       C
ATOM   2421  OD1 ASP A 302     -48.233  59.223 -38.324  1.00 44.39           O
ANISOU 2421  OD1 ASP A 302     5615   4012   7239     79     31   -889       O
ATOM   2422  OD2 ASP A 302     -49.609  59.063 -36.619  1.00 42.55           O
ANISOU 2422  OD2 ASP A 302     5327   3782   7059     38     67   -757       O
ATOM   2423  N   PHE A 303     -47.261  54.233 -37.775  1.00 32.71           N
ANISOU 2423  N   PHE A 303     4278   2528   5624      0   -172   -618       N
ATOM   2424  CA  PHE A 303     -46.549  53.023 -37.376  1.00 35.68           C
ANISOU 2424  CA  PHE A 303     4650   2894   6012    -14   -252   -564       C
ATOM   2425  C   PHE A 303     -45.458  52.671 -38.379  1.00 35.35           C
ANISOU 2425  C   PHE A 303     4640   2841   5951     -5   -321   -627       C
ATOM   2426  O   PHE A 303     -44.389  52.181 -37.995  1.00 36.83           O
ANISOU 2426  O   PHE A 303     4794   2994   6206    -22   -401   -612       O
ATOM   2427  CB  PHE A 303     -47.527  51.861 -37.217  1.00 39.01           C
ANISOU 2427  CB  PHE A 303     5103   3361   6358    -20   -235   -491       C
ATOM   2428  CG  PHE A 303     -46.864  50.561 -36.862  1.00 41.02           C
ANISOU 2428  CG  PHE A 303     5343   3623   6619    -24   -312   -448       C
ATOM   2429  CD1 PHE A 303     -46.415  50.329 -35.573  1.00 39.09           C
ANISOU 2429  CD1 PHE A 303     5026   3370   6454    -41   -341   -394       C
ATOM   2430  CD2 PHE A 303     -46.686  49.573 -37.817  1.00 41.08           C
ANISOU 2430  CD2 PHE A 303     5403   3656   6550    -12   -356   -461       C
ATOM   2431  CE1 PHE A 303     -45.801  49.137 -35.242  1.00 37.59           C
ANISOU 2431  CE1 PHE A 303     4808   3205   6271    -48   -401   -357       C
ATOM   2432  CE2 PHE A 303     -46.074  48.378 -37.493  1.00 39.58           C
ANISOU 2432  CE2 PHE A 303     5184   3480   6374    -14   -428   -430       C
ATOM   2433  CZ  PHE A 303     -45.631  48.159 -36.204  1.00 41.46           C
ANISOU 2433  CZ  PHE A 303     5340   3717   6696    -34   -445   -380       C
ATOM   2434  N   VAL A 304     -45.708  52.914 -39.667  1.00 37.01           N
ANISOU 2434  N   VAL A 304     4911   3087   6066     17   -293   -699       N
ATOM   2435  CA  VAL A 304     -44.683  52.675 -40.679  1.00 35.37           C
ANISOU 2435  CA  VAL A 304     4733   2873   5831     34   -365   -780       C
ATOM   2436  C   VAL A 304     -43.500  53.610 -40.466  1.00 36.16           C
ANISOU 2436  C   VAL A 304     4785   2894   6061     39   -418   -854       C
ATOM   2437  O   VAL A 304     -42.338  53.197 -40.566  1.00 41.85           O
ANISOU 2437  O   VAL A 304     5492   3569   6841     28   -514   -881       O
ATOM   2438  CB  VAL A 304     -45.280  52.826 -42.090  1.00 34.16           C
ANISOU 2438  CB  VAL A 304     4659   2792   5528     61   -314   -843       C
ATOM   2439  CG1 VAL A 304     -44.179  52.833 -43.137  1.00 34.18           C
ANISOU 2439  CG1 VAL A 304     4689   2793   5507     89   -391   -956       C
ATOM   2440  CG2 VAL A 304     -46.266  51.705 -42.365  1.00 31.18           C
ANISOU 2440  CG2 VAL A 304     4343   2472   5033     54   -293   -756       C
ATOM   2441  N   GLU A 305     -43.776  54.880 -40.159  1.00 36.21           N
ANISOU 2441  N   GLU A 305     4759   2877   6123     54   -364   -890       N
ATOM   2442  CA  GLU A 305     -42.698  55.835 -39.918  1.00 38.76           C
ANISOU 2442  CA  GLU A 305     5037   3107   6582     68   -424   -959       C
ATOM   2443  C   GLU A 305     -41.844  55.414 -38.729  1.00 37.08           C
ANISOU 2443  C   GLU A 305     4773   2817   6498     24   -503   -867       C
ATOM   2444  O   GLU A 305     -40.620  55.586 -38.743  1.00 39.54           O
ANISOU 2444  O   GLU A 305     5065   3043   6914     16   -594   -905       O
ATOM   2445  CB  GLU A 305     -43.274  57.233 -39.692  1.00 39.59           C
ANISOU 2445  CB  GLU A 305     5107   3206   6727     99   -352  -1005       C
ATOM   2446  CG  GLU A 305     -42.216  58.320 -39.556  1.00 42.15           C
ANISOU 2446  CG  GLU A 305     5392   3427   7196    130   -421  -1092       C
ATOM   2447  CD  GLU A 305     -42.801  59.666 -39.170  1.00 43.73           C
ANISOU 2447  CD  GLU A 305     5544   3622   7451    167   -360  -1130       C
ATOM   2448  OE1 GLU A 305     -43.458  59.750 -38.111  1.00 44.50           O
ANISOU 2448  OE1 GLU A 305     5605   3724   7578    146   -325  -1031       O
ATOM   2449  OE2 GLU A 305     -42.606  60.639 -39.928  1.00 47.48           O
ANISOU 2449  OE2 GLU A 305     6010   4092   7937    223   -351  -1269       O
ATOM   2450  N   ILE A 306     -42.472  54.855 -37.694  1.00 35.57           N
ANISOU 2450  N   ILE A 306     4558   2658   6300     -6   -470   -746       N
ATOM   2451  CA  ILE A 306     -41.733  54.450 -36.503  1.00 28.66           C
ANISOU 2451  CA  ILE A 306     3629   1736   5526    -50   -528   -648       C
ATOM   2452  C   ILE A 306     -40.824  53.268 -36.815  1.00 31.04           C
ANISOU 2452  C   ILE A 306     3930   2036   5827    -84   -606   -634       C
ATOM   2453  O   ILE A 306     -39.622  53.295 -36.526  1.00 34.46           O
ANISOU 2453  O   ILE A 306     4328   2393   6371   -119   -687   -624       O
ATOM   2454  CB  ILE A 306     -42.705  54.121 -35.356  1.00 35.97           C
ANISOU 2454  CB  ILE A 306     4527   2716   6423    -64   -470   -540       C
ATOM   2455  CG1 ILE A 306     -43.500  55.364 -34.950  1.00 30.02           C
ANISOU 2455  CG1 ILE A 306     3757   1955   5692    -35   -408   -556       C
ATOM   2456  CG2 ILE A 306     -41.948  53.546 -34.166  1.00 31.88           C
ANISOU 2456  CG2 ILE A 306     3954   2182   5978   -111   -522   -434       C
ATOM   2457  CD1 ILE A 306     -44.589  55.083 -33.933  1.00 26.70           C
ANISOU 2457  CD1 ILE A 306     3315   1593   5236    -42   -353   -472       C
ATOM   2458  N   ILE A 307     -41.384  52.215 -37.414  1.00 28.72           N
ANISOU 2458  N   ILE A 307     3674   1823   5416    -76   -589   -632       N
ATOM   2459  CA  ILE A 307     -40.615  50.994 -37.632  1.00 31.76           C
ANISOU 2459  CA  ILE A 307     4046   2221   5800   -103   -664   -617       C
ATOM   2460  C   ILE A 307     -39.540  51.206 -38.692  1.00 36.25           C
ANISOU 2460  C   ILE A 307     4635   2735   6405    -98   -747   -727       C
ATOM   2461  O   ILE A 307     -38.505  50.527 -38.679  1.00 38.91           O
ANISOU 2461  O   ILE A 307     4935   3043   6806   -137   -833   -722       O
ATOM   2462  CB  ILE A 307     -41.560  49.830 -37.989  1.00 33.01           C
ANISOU 2462  CB  ILE A 307     4241   2474   5827    -82   -635   -588       C
ATOM   2463  CG1 ILE A 307     -40.832  48.490 -37.874  1.00 33.09           C
ANISOU 2463  CG1 ILE A 307     4210   2509   5853   -110   -711   -555       C
ATOM   2464  CG2 ILE A 307     -42.146  50.012 -39.383  1.00 29.01           C
ANISOU 2464  CG2 ILE A 307     3821   2001   5199    -37   -611   -673       C
ATOM   2465  CD1 ILE A 307     -41.736  47.288 -38.039  1.00 37.36           C
ANISOU 2465  CD1 ILE A 307     4776   3134   6285    -81   -696   -520       C
ATOM   2466  N   LYS A 308     -39.747  52.149 -39.613  1.00 36.59           N
ANISOU 2466  N   LYS A 308     4728   2766   6408    -52   -725   -836       N
ATOM   2467  CA  LYS A 308     -38.718  52.469 -40.593  1.00 35.71           C
ANISOU 2467  CA  LYS A 308     4635   2600   6334    -36   -808   -963       C
ATOM   2468  C   LYS A 308     -37.654  53.410 -40.048  1.00 35.26           C
ANISOU 2468  C   LYS A 308     4530   2412   6455    -57   -871   -986       C
ATOM   2469  O   LYS A 308     -36.680  53.694 -40.753  1.00 39.91           O
ANISOU 2469  O   LYS A 308     5126   2931   7106    -48   -958  -1096       O
ATOM   2470  CB  LYS A 308     -39.345  53.088 -41.844  1.00 38.51           C
ANISOU 2470  CB  LYS A 308     5059   3011   6562     29   -757  -1083       C
ATOM   2471  CG  LYS A 308     -40.075  52.100 -42.734  1.00 44.39           C
ANISOU 2471  CG  LYS A 308     5869   3867   7129     49   -734  -1078       C
ATOM   2472  CD  LYS A 308     -40.542  52.769 -44.015  1.00 50.35           C
ANISOU 2472  CD  LYS A 308     6692   4686   7751    107   -685  -1195       C
ATOM   2473  CE  LYS A 308     -41.138  51.760 -44.981  1.00 55.05           C
ANISOU 2473  CE  LYS A 308     7364   5386   8166    125   -681  -1183       C
ATOM   2474  NZ  LYS A 308     -41.613  52.407 -46.236  1.00 61.54           N
ANISOU 2474  NZ  LYS A 308     8254   6291   8836    176   -623  -1285       N
ATOM   2475  N   SER A 309     -37.811  53.896 -38.817  1.00 32.35           N
ANISOU 2475  N   SER A 309     4116   2004   6171    -82   -838   -886       N
ATOM   2476  CA  SER A 309     -36.881  54.843 -38.222  1.00 32.41           C
ANISOU 2476  CA  SER A 309     4084   1894   6334    -98   -895   -881       C
ATOM   2477  C   SER A 309     -35.967  54.194 -37.190  1.00 36.55           C
ANISOU 2477  C   SER A 309     4547   2394   6945   -180   -950   -743       C
ATOM   2478  O   SER A 309     -35.350  54.901 -36.386  1.00 37.08           O
ANISOU 2478  O   SER A 309     4578   2418   7093   -199   -970   -674       O
ATOM   2479  CB  SER A 309     -37.652  56.001 -37.588  1.00 39.54           C
ANISOU 2479  CB  SER A 309     4977   2807   7238    -60   -817   -856       C
ATOM   2480  OG  SER A 309     -38.511  56.618 -38.531  1.00 39.77           O
ANISOU 2480  OG  SER A 309     5050   2866   7194      8   -755   -983       O
ATOM   2481  N   GLN A 310     -35.860  52.870 -37.198  1.00 38.75           N
ANISOU 2481  N   GLN A 310     4766   3076   6880    379   -561  -1731       N
ATOM   2482  CA  GLN A 310     -35.101  52.145 -36.192  1.00 34.64           C
ANISOU 2482  CA  GLN A 310     4135   2330   6698    253   -617  -1552       C
ATOM   2483  C   GLN A 310     -33.889  51.464 -36.814  1.00 37.86           C
ANISOU 2483  C   GLN A 310     4484   2644   7260    190   -863  -1697       C
ATOM   2484  O   GLN A 310     -33.834  51.216 -38.022  1.00 39.39           O
ANISOU 2484  O   GLN A 310     4741   2936   7288    233  -1022  -1954       O
ATOM   2485  CB  GLN A 310     -35.979  51.102 -35.491  1.00 32.41           C
ANISOU 2485  CB  GLN A 310     3812   2147   6354    190   -503  -1267       C
ATOM   2486  CG  GLN A 310     -37.297  51.650 -34.970  1.00 34.28           C
ANISOU 2486  CG  GLN A 310     4105   2519   6401    237   -291  -1121       C
ATOM   2487  CD  GLN A 310     -37.113  52.806 -34.005  1.00 36.16           C
ANISOU 2487  CD  GLN A 310     4326   2640   6774    240   -185  -1065       C
ATOM   2488  OE1 GLN A 310     -36.168  52.829 -33.216  1.00 36.68           O
ANISOU 2488  OE1 GLN A 310     4301   2615   7021    158   -218   -953       O
ATOM   2489  NE2 GLN A 310     -38.017  53.777 -34.069  1.00 32.52           N
ANISOU 2489  NE2 GLN A 310     3926   2284   6147    317    -63  -1062       N
ATOM   2490  N   ASP A 311     -32.912  51.166 -35.962  1.00 40.98           N
ANISOU 2490  N   ASP A 311     4738   2899   7933     82   -900  -1507       N
ATOM   2491  CA  ASP A 311     -31.730  50.413 -36.359  1.00 47.74           C
ANISOU 2491  CA  ASP A 311     5490   3642   9006      2  -1132  -1572       C
ATOM   2492  C   ASP A 311     -31.998  48.927 -36.159  1.00 45.99           C
ANISOU 2492  C   ASP A 311     5178   3446   8848    -84  -1162  -1408       C
ATOM   2493  O   ASP A 311     -32.445  48.510 -35.086  1.00 37.53           O
ANISOU 2493  O   ASP A 311     4029   2400   7830   -126   -982  -1148       O
ATOM   2494  CB  ASP A 311     -30.512  50.863 -35.549  1.00 41.40           C
ANISOU 2494  CB  ASP A 311     4543   2663   8524    -67  -1169  -1426       C
ATOM   2495  CG  ASP A 311     -29.233  50.164 -35.971  1.00 44.38           C
ANISOU 2495  CG  ASP A 311     4793   2900   9170   -145  -1422  -1485       C
ATOM   2496  OD1 ASP A 311     -29.113  48.942 -35.750  1.00 60.34           O
ANISOU 2496  OD1 ASP A 311     6703   4929  11296   -236  -1466  -1330       O
ATOM   2497  OD2 ASP A 311     -28.345  50.839 -36.530  1.00 61.76           O
ANISOU 2497  OD2 ASP A 311     6989   4976  11501   -110  -1582  -1692       O
ATOM   2498  N   LEU A 312     -31.719  48.131 -37.191  1.00 48.66           N
ANISOU 2498  N   LEU A 312     5513   3792   9186   -108  -1400  -1579       N
ATOM   2499  CA  LEU A 312     -32.059  46.713 -37.205  1.00 46.58           C
ANISOU 2499  CA  LEU A 312     5146   3590   8963   -171  -1452  -1420       C
ATOM   2500  C   LEU A 312     -30.823  45.817 -37.171  1.00 49.73           C
ANISOU 2500  C   LEU A 312     5345   3844   9708   -294  -1663  -1365       C
ATOM   2501  O   LEU A 312     -30.846  44.702 -37.696  1.00 55.96           O
ANISOU 2501  O   LEU A 312     6045   4687  10530   -340  -1829  -1337       O
ATOM   2502  CB  LEU A 312     -32.910  46.385 -38.431  1.00 45.21           C
ANISOU 2502  CB  LEU A 312     5091   3696   8389    -95  -1537  -1508       C
ATOM   2503  CG  LEU A 312     -34.078  47.323 -38.742  1.00 43.40           C
ANISOU 2503  CG  LEU A 312     5043   3681   7767     27  -1352  -1548       C
ATOM   2504  CD1 LEU A 312     -34.813  46.857 -39.990  1.00 43.84           C
ANISOU 2504  CD1 LEU A 312     5167   4047   7444     64  -1466  -1550       C
ATOM   2505  CD2 LEU A 312     -35.030  47.424 -37.561  1.00 40.67           C
ANISOU 2505  CD2 LEU A 312     4683   3326   7445     48  -1062  -1293       C
ATOM   2506  N   SER A 313     -29.740  46.284 -36.552  1.00 53.11           N
ANISOU 2506  N   SER A 313     5678   4147  10356   -332  -1648  -1282       N
ATOM   2507  CA  SER A 313     -28.492  45.535 -36.503  1.00 57.28           C
ANISOU 2507  CA  SER A 313     6005   4552  11206   -433  -1833  -1189       C
ATOM   2508  C   SER A 313     -28.281  44.819 -35.174  1.00 58.69           C
ANISOU 2508  C   SER A 313     5955   4716  11627   -519  -1657   -825       C
ATOM   2509  O   SER A 313     -27.198  44.272 -34.943  1.00 61.53           O
ANISOU 2509  O   SER A 313     6122   4975  12282   -606  -1771   -686       O
ATOM   2510  CB  SER A 313     -27.308  46.463 -36.786  1.00 59.71           C
ANISOU 2510  CB  SER A 313     6325   4699  11664   -425  -1984  -1339       C
ATOM   2511  OG  SER A 313     -27.188  47.455 -35.782  1.00 61.98           O
ANISOU 2511  OG  SER A 313     6597   4924  12029   -411  -1798  -1184       O
ATOM   2512  N   VAL A 314     -29.285  44.804 -34.302  1.00 57.75           N
ANISOU 2512  N   VAL A 314     5847   4708  11387   -495  -1381   -677       N
ATOM   2513  CA  VAL A 314     -29.179  44.201 -32.979  1.00 62.39           C
ANISOU 2513  CA  VAL A 314     6218   5338  12151   -571  -1173   -370       C
ATOM   2514  C   VAL A 314     -30.277  43.158 -32.830  1.00 57.24           C
ANISOU 2514  C   VAL A 314     5498   4810  11441   -546  -1035   -339       C
ATOM   2515  O   VAL A 314     -31.385  43.332 -33.351  1.00 57.14           O
ANISOU 2515  O   VAL A 314     5674   4876  11161   -439  -1001   -481       O
ATOM   2516  CB  VAL A 314     -29.263  45.272 -31.869  1.00 74.74           C
ANISOU 2516  CB  VAL A 314     7821   6919  13656   -578   -961   -225       C
ATOM   2517  CG1 VAL A 314     -29.443  44.639 -30.496  1.00 80.57           C
ANISOU 2517  CG1 VAL A 314     8352   7789  14473   -659   -703     65       C
ATOM   2518  CG2 VAL A 314     -28.014  46.142 -31.886  1.00 79.62           C
ANISOU 2518  CG2 VAL A 314     8417   7377  14458   -613  -1120   -193       C
ATOM   2519  N   VAL A 315     -29.958  42.065 -32.131  1.00 53.54           N
ANISOU 2519  N   VAL A 315     4748   4403  11192   -612   -944   -137       N
ATOM   2520  CA  VAL A 315     -30.921  40.983 -31.930  1.00 56.10           C
ANISOU 2520  CA  VAL A 315     4974   4898  11441   -521   -788   -115       C
ATOM   2521  C   VAL A 315     -32.189  41.512 -31.268  1.00 51.08           C
ANISOU 2521  C   VAL A 315     4514   4417  10477   -399   -511   -156       C
ATOM   2522  O   VAL A 315     -33.299  41.334 -31.782  1.00 51.17           O
ANISOU 2522  O   VAL A 315     4665   4480  10296   -275   -506   -271       O
ATOM   2523  CB  VAL A 315     -30.291  39.847 -31.106  1.00 63.13           C
ANISOU 2523  CB  VAL A 315     5491   5874  12621   -594   -674     99       C
ATOM   2524  CG1 VAL A 315     -31.328  38.776 -30.803  1.00 65.27           C
ANISOU 2524  CG1 VAL A 315     5657   6323  12818   -444   -482     71       C
ATOM   2525  CG2 VAL A 315     -29.105  39.250 -31.848  1.00 68.07           C
ANISOU 2525  CG2 VAL A 315     5994   6366  13502   -672   -968    149       C
ATOM   2526  N   SER A 316     -32.045  42.167 -30.118  1.00 46.71           N
ANISOU 2526  N   SER A 316     3939   3940   9868   -449   -299    -35       N
ATOM   2527  CA  SER A 316     -33.202  42.695 -29.410  1.00 45.97           C
ANISOU 2527  CA  SER A 316     3997   4001   9468   -354    -61    -81       C
ATOM   2528  C   SER A 316     -32.796  43.913 -28.597  1.00 49.00           C
ANISOU 2528  C   SER A 316     4437   4394   9787   -441     24     47       C
ATOM   2529  O   SER A 316     -31.683  43.983 -28.069  1.00 55.48           O
ANISOU 2529  O   SER A 316     5075   5184  10820   -581      8    257       O
ATOM   2530  CB  SER A 316     -33.832  41.649 -28.485  1.00 49.57           C
ANISOU 2530  CB  SER A 316     4271   4678   9885   -281    189    -68       C
ATOM   2531  OG  SER A 316     -33.069  41.496 -27.301  1.00 53.67           O
ANISOU 2531  OG  SER A 316     4556   5371  10464   -386    370    131       O
ATOM   2532  N   LYS A 317     -33.714  44.871 -28.503  1.00 44.19           N
ANISOU 2532  N   LYS A 317     4056   3820   8916   -367     97    -42       N
ATOM   2533  CA  LYS A 317     -33.518  46.044 -27.663  1.00 41.04           C
ANISOU 2533  CA  LYS A 317     3704   3450   8441   -434    178     97       C
ATOM   2534  C   LYS A 317     -34.875  46.678 -27.394  1.00 37.69           C
ANISOU 2534  C   LYS A 317     3478   3145   7698   -330    306    -14       C
ATOM   2535  O   LYS A 317     -35.891  46.293 -27.977  1.00 33.46           O
ANISOU 2535  O   LYS A 317     3049   2621   7043   -218    306   -191       O
ATOM   2536  CB  LYS A 317     -32.560  47.051 -28.307  1.00 41.16           C
ANISOU 2536  CB  LYS A 317     3781   3188   8670   -497    -44    110       C
ATOM   2537  CG  LYS A 317     -33.155  47.844 -29.458  1.00 36.83           C
ANISOU 2537  CG  LYS A 317     3485   2516   7994   -378   -166   -146       C
ATOM   2538  CD  LYS A 317     -32.234  48.989 -29.845  1.00 42.27           C
ANISOU 2538  CD  LYS A 317     4220   3037   8804   -387   -335   -170       C
ATOM   2539  CE  LYS A 317     -32.873  49.895 -30.883  1.00 49.43           C
ANISOU 2539  CE  LYS A 317     5350   3955   9476   -249   -390   -423       C
ATOM   2540  NZ  LYS A 317     -32.032  51.095 -31.154  1.00 54.87           N
ANISOU 2540  NZ  LYS A 317     6058   4527  10264   -229   -513   -475       N
ATOM   2541  N   VAL A 318     -34.875  47.662 -26.501  1.00 43.17           N
ANISOU 2541  N   VAL A 318     4199   3918   8286   -384    392    126       N
ATOM   2542  CA  VAL A 318     -36.081  48.381 -26.112  1.00 30.86           C
ANISOU 2542  CA  VAL A 318     2802   2474   6451   -315    492     52       C
ATOM   2543  C   VAL A 318     -36.129  49.699 -26.871  1.00 35.68           C
ANISOU 2543  C   VAL A 318     3583   2886   7087   -280    359      4       C
ATOM   2544  O   VAL A 318     -35.153  50.461 -26.873  1.00 37.34           O
ANISOU 2544  O   VAL A 318     3753   2942   7491   -346    258    128       O
ATOM   2545  CB  VAL A 318     -36.124  48.617 -24.593  1.00 34.50           C
ANISOU 2545  CB  VAL A 318     3166   3208   6735   -397    662    238       C
ATOM   2546  CG1 VAL A 318     -37.275  49.540 -24.230  1.00 30.63           C
ANISOU 2546  CG1 VAL A 318     2842   2804   5994   -348    707    169       C
ATOM   2547  CG2 VAL A 318     -36.247  47.292 -23.858  1.00 34.79           C
ANISOU 2547  CG2 VAL A 318     3026   3506   6687   -393    838    204       C
ATOM   2548  N   VAL A 319     -37.261  49.968 -27.516  1.00 35.81           N
ANISOU 2548  N   VAL A 319     3764   2901   6941   -172    359   -168       N
ATOM   2549  CA  VAL A 319     -37.485  51.198 -28.267  1.00 31.95           C
ANISOU 2549  CA  VAL A 319     3417   2292   6430   -112    278   -239       C
ATOM   2550  C   VAL A 319     -38.543  52.017 -27.541  1.00 33.36           C
ANISOU 2550  C   VAL A 319     3665   2596   6414    -96    383   -190       C
ATOM   2551  O   VAL A 319     -39.641  51.519 -27.265  1.00 36.70           O
ANISOU 2551  O   VAL A 319     4121   3147   6677    -67    465   -251       O
ATOM   2552  CB  VAL A 319     -37.914  50.902 -29.715  1.00 33.00           C
ANISOU 2552  CB  VAL A 319     3652   2372   6513    -17    185   -432       C
ATOM   2553  CG1 VAL A 319     -38.277  52.190 -30.433  1.00 33.74           C
ANISOU 2553  CG1 VAL A 319     3868   2429   6523     61    156   -519       C
ATOM   2554  CG2 VAL A 319     -36.808  50.165 -30.454  1.00 34.73           C
ANISOU 2554  CG2 VAL A 319     3800   2474   6921    -45     35   -493       C
ATOM   2555  N   LYS A 320     -38.211  53.268 -27.233  1.00 33.21           N
ANISOU 2555  N   LYS A 320     3651   2516   6452   -116    356    -84       N
ATOM   2556  CA  LYS A 320     -39.119  54.184 -26.556  1.00 33.29           C
ANISOU 2556  CA  LYS A 320     3705   2635   6307   -113    419    -10       C
ATOM   2557  C   LYS A 320     -39.742  55.126 -27.576  1.00 33.06           C
ANISOU 2557  C   LYS A 320     3778   2522   6259     -4    385   -132       C
ATOM   2558  O   LYS A 320     -39.026  55.774 -28.347  1.00 33.38           O
ANISOU 2558  O   LYS A 320     3821   2402   6460     52    307   -198       O
ATOM   2559  CB  LYS A 320     -38.385  54.992 -25.485  1.00 34.59           C
ANISOU 2559  CB  LYS A 320     3769   2810   6562   -209    400    246       C
ATOM   2560  CG  LYS A 320     -37.491  54.170 -24.574  1.00 40.81           C
ANISOU 2560  CG  LYS A 320     4412   3707   7388   -334    434    430       C
ATOM   2561  CD  LYS A 320     -38.102  54.005 -23.193  1.00 45.23           C
ANISOU 2561  CD  LYS A 320     4927   4599   7661   -413    553    553       C
ATOM   2562  CE  LYS A 320     -37.017  53.778 -22.151  1.00 56.11           C
ANISOU 2562  CE  LYS A 320     6118   6127   9074   -562    577    868       C
ATOM   2563  NZ  LYS A 320     -37.566  53.673 -20.772  1.00 62.83           N
ANISOU 2563  NZ  LYS A 320     6917   7387   9567   -642    696    979       N
ATOM   2564  N   VAL A 321     -41.071  55.201 -27.579  1.00 32.39           N
ANISOU 2564  N   VAL A 321     3758   2554   5996     27    444   -172       N
ATOM   2565  CA  VAL A 321     -41.812  56.070 -28.484  1.00 29.17           C
ANISOU 2565  CA  VAL A 321     3411   2134   5540    116    444   -236       C
ATOM   2566  C   VAL A 321     -42.795  56.891 -27.663  1.00 27.00           C
ANISOU 2566  C   VAL A 321     3125   1952   5182     85    481   -124       C
ATOM   2567  O   VAL A 321     -43.578  56.333 -26.887  1.00 29.59           O
ANISOU 2567  O   VAL A 321     3458   2385   5402     23    507   -109       O
ATOM   2568  CB  VAL A 321     -42.556  55.273 -29.572  1.00 29.31           C
ANISOU 2568  CB  VAL A 321     3488   2194   5455    168    443   -348       C
ATOM   2569  CG1 VAL A 321     -43.247  56.221 -30.541  1.00 31.34           C
ANISOU 2569  CG1 VAL A 321     3774   2504   5631    250    465   -370       C
ATOM   2570  CG2 VAL A 321     -41.597  54.352 -30.311  1.00 31.65           C
ANISOU 2570  CG2 VAL A 321     3783   2423   5820    182    374   -449       C
ATOM   2571  N   THR A 322     -42.756  58.210 -27.835  1.00 30.30           N
ANISOU 2571  N   THR A 322     3513   2328   5673    134    471    -71       N
ATOM   2572  CA  THR A 322     -43.661  59.103 -27.119  1.00 29.34           C
ANISOU 2572  CA  THR A 322     3355   2289   5502    100    478     56       C
ATOM   2573  C   THR A 322     -45.006  59.115 -27.834  1.00 33.36           C
ANISOU 2573  C   THR A 322     3895   2871   5910    135    517      8       C
ATOM   2574  O   THR A 322     -45.122  59.637 -28.948  1.00 35.41           O
ANISOU 2574  O   THR A 322     4145   3129   6179    232    554    -44       O
ATOM   2575  CB  THR A 322     -43.073  60.508 -27.025  1.00 31.21           C
ANISOU 2575  CB  THR A 322     3506   2434   5920    148    443    158       C
ATOM   2576  OG1 THR A 322     -41.782  60.446 -26.408  1.00 37.45           O
ANISOU 2576  OG1 THR A 322     4244   3119   6865     97    379    257       O
ATOM   2577  CG2 THR A 322     -43.976  61.403 -26.191  1.00 32.36           C
ANISOU 2577  CG2 THR A 322     3590   2678   6026     96    422    324       C
ATOM   2578  N   ILE A 323     -46.019  58.531 -27.202  1.00 28.24           N
ANISOU 2578  N   ILE A 323     3266   2295   5170     54    504     20       N
ATOM   2579  CA  ILE A 323     -47.365  58.460 -27.754  1.00 27.19           C
ANISOU 2579  CA  ILE A 323     3133   2188   5008     53    505     26       C
ATOM   2580  C   ILE A 323     -48.333  58.954 -26.691  1.00 29.29           C
ANISOU 2580  C   ILE A 323     3358   2506   5264    -40    448    100       C
ATOM   2581  O   ILE A 323     -48.238  58.548 -25.528  1.00 30.56           O
ANISOU 2581  O   ILE A 323     3533   2719   5360   -115    411     58       O
ATOM   2582  CB  ILE A 323     -47.731  57.030 -28.194  1.00 23.18           C
ANISOU 2582  CB  ILE A 323     2675   1643   4488     48    492    -69       C
ATOM   2583  CG1 ILE A 323     -46.649  56.463 -29.114  1.00 28.65           C
ANISOU 2583  CG1 ILE A 323     3404   2305   5179    119    511   -144       C
ATOM   2584  CG2 ILE A 323     -49.081  57.017 -28.893  1.00 23.62           C
ANISOU 2584  CG2 ILE A 323     2703   1695   4576     34    468      9       C
ATOM   2585  CD1 ILE A 323     -46.830  55.003 -29.443  1.00 26.70           C
ANISOU 2585  CD1 ILE A 323     3178   2013   4954    115    477   -212       C
ATOM   2586  N   ASP A 324     -49.256  59.832 -27.089  1.00 29.96           N
ANISOU 2586  N   ASP A 324     3375   2610   5397    -40    441    207       N
ATOM   2587  CA  ASP A 324     -50.250  60.396 -26.175  1.00 30.86           C
ANISOU 2587  CA  ASP A 324     3430   2761   5534   -141    351    282       C
ATOM   2588  C   ASP A 324     -49.582  61.065 -24.975  1.00 33.06           C
ANISOU 2588  C   ASP A 324     3683   3114   5764   -186    301    343       C
ATOM   2589  O   ASP A 324     -50.078  60.994 -23.849  1.00 26.67           O
ANISOU 2589  O   ASP A 324     2872   2386   4877   -293    204    326       O
ATOM   2590  CB  ASP A 324     -51.248  59.332 -25.712  1.00 31.58           C
ANISOU 2590  CB  ASP A 324     3561   2806   5633   -226    267    162       C
ATOM   2591  CG  ASP A 324     -52.055  58.751 -26.852  1.00 35.61           C
ANISOU 2591  CG  ASP A 324     4057   3219   6253   -207    272    192       C
ATOM   2592  OD1 ASP A 324     -52.181  59.424 -27.895  1.00 38.49           O
ANISOU 2592  OD1 ASP A 324     4359   3626   6640   -160    336    349       O
ATOM   2593  OD2 ASP A 324     -52.570  57.623 -26.702  1.00 37.32           O
ANISOU 2593  OD2 ASP A 324     4306   3332   6540   -236    210     70       O
ATOM   2594  N   TYR A 325     -48.439  61.708 -25.223  1.00 27.06           N
ANISOU 2594  N   TYR A 325     2893   2328   5060   -107    350    414       N
ATOM   2595  CA  TYR A 325     -47.648  62.417 -24.219  1.00 31.71           C
ANISOU 2595  CA  TYR A 325     3425   2958   5664   -148    287    555       C
ATOM   2596  C   TYR A 325     -47.044  61.493 -23.169  1.00 34.85           C
ANISOU 2596  C   TYR A 325     3882   3455   5905   -239    263    524       C
ATOM   2597  O   TYR A 325     -46.740  61.940 -22.058  1.00 39.99           O
ANISOU 2597  O   TYR A 325     4480   4231   6486   -328    184    681       O
ATOM   2598  CB  TYR A 325     -48.462  63.512 -23.520  1.00 31.61           C
ANISOU 2598  CB  TYR A 325     3305   3024   5681   -219    180    719       C
ATOM   2599  CG  TYR A 325     -48.971  64.594 -24.439  1.00 33.12           C
ANISOU 2599  CG  TYR A 325     3377   3156   6050   -127    221    798       C
ATOM   2600  CD1 TYR A 325     -48.116  65.570 -24.933  1.00 32.86           C
ANISOU 2600  CD1 TYR A 325     3245   3036   6206      3    268    869       C
ATOM   2601  CD2 TYR A 325     -50.309  64.649 -24.800  1.00 34.61           C
ANISOU 2601  CD2 TYR A 325     3526   3375   6249   -167    211    800       C
ATOM   2602  CE1 TYR A 325     -48.579  66.566 -25.771  1.00 37.24           C
ANISOU 2602  CE1 TYR A 325     3660   3583   6906    110    340    909       C
ATOM   2603  CE2 TYR A 325     -50.782  65.642 -25.637  1.00 37.77           C
ANISOU 2603  CE2 TYR A 325     3780   3778   6795    -89    276    905       C
ATOM   2604  CZ  TYR A 325     -49.913  66.598 -26.119  1.00 39.41           C
ANISOU 2604  CZ  TYR A 325     3886   3947   7140     60    357    944       C
ATOM   2605  OH  TYR A 325     -50.381  67.587 -26.953  1.00 41.11           O
ANISOU 2605  OH  TYR A 325     3927   4209   7483    161    455   1016       O
ATOM   2606  N   THR A 326     -46.856  60.214 -23.482  1.00 30.49           N
ANISOU 2606  N   THR A 326     3415   2883   5286   -221    332    348       N
ATOM   2607  CA  THR A 326     -46.203  59.296 -22.562  1.00 31.74           C
ANISOU 2607  CA  THR A 326     3593   3168   5300   -290    350    315       C
ATOM   2608  C   THR A 326     -45.230  58.420 -23.339  1.00 32.72           C
ANISOU 2608  C   THR A 326     3747   3176   5510   -221    428    234       C
ATOM   2609  O   THR A 326     -45.406  58.178 -24.536  1.00 35.79           O
ANISOU 2609  O   THR A 326     4178   3426   5996   -131    457    128       O
ATOM   2610  CB  THR A 326     -47.221  58.431 -21.795  1.00 29.21           C
ANISOU 2610  CB  THR A 326     3311   2993   4795   -356    335    125       C
ATOM   2611  OG1 THR A 326     -46.602  57.880 -20.625  1.00 35.35           O
ANISOU 2611  OG1 THR A 326     4064   4004   5363   -432    363    129       O
ATOM   2612  CG2 THR A 326     -47.736  57.294 -22.660  1.00 27.58           C
ANISOU 2612  CG2 THR A 326     3164   2648   4669   -284    385    -94       C
ATOM   2613  N   GLU A 327     -44.186  57.963 -22.650  1.00 29.00           N
ANISOU 2613  N   GLU A 327     3235   2789   4995   -277    450    312       N
ATOM   2614  CA  GLU A 327     -43.180  57.108 -23.267  1.00 36.49           C
ANISOU 2614  CA  GLU A 327     4182   3630   6054   -237    498    257       C
ATOM   2615  C   GLU A 327     -43.664  55.663 -23.270  1.00 32.40           C
ANISOU 2615  C   GLU A 327     3697   3179   5433   -223    566     42       C
ATOM   2616  O   GLU A 327     -43.847  55.061 -22.207  1.00 33.00           O
ANISOU 2616  O   GLU A 327     3738   3468   5332   -285    613     -2       O
ATOM   2617  CB  GLU A 327     -41.847  57.223 -22.532  1.00 46.17           C
ANISOU 2617  CB  GLU A 327     5305   4902   7334   -321    483    486       C
ATOM   2618  CG  GLU A 327     -40.834  58.134 -23.208  1.00 57.46           C
ANISOU 2618  CG  GLU A 327     6690   6076   9067   -276    403    611       C
ATOM   2619  CD  GLU A 327     -39.423  57.916 -22.692  1.00 69.36           C
ANISOU 2619  CD  GLU A 327     8077   7553  10724   -369    368    835       C
ATOM   2620  OE1 GLU A 327     -39.214  56.955 -21.922  1.00 73.03           O
ANISOU 2620  OE1 GLU A 327     8491   8237  11020   -461    440    891       O
ATOM   2621  OE2 GLU A 327     -38.524  58.704 -23.056  1.00 72.55           O
ANISOU 2621  OE2 GLU A 327     8416   7710  11440   -348    267    954       O
ATOM   2622  N   ILE A 328     -43.866  55.109 -24.462  1.00 29.30           N
ANISOU 2622  N   ILE A 328     3356   2626   5150   -136    568    -96       N
ATOM   2623  CA  ILE A 328     -44.268  53.719 -24.631  1.00 29.52           C
ANISOU 2623  CA  ILE A 328     3388   2655   5172   -104    606   -277       C
ATOM   2624  C   ILE A 328     -43.040  52.905 -25.012  1.00 29.68           C
ANISOU 2624  C   ILE A 328     3355   2623   5298    -93    626   -268       C
ATOM   2625  O   ILE A 328     -42.342  53.233 -25.980  1.00 27.00           O
ANISOU 2625  O   ILE A 328     3034   2140   5084    -58    571   -229       O
ATOM   2626  CB  ILE A 328     -45.373  53.579 -25.691  1.00 31.25           C
ANISOU 2626  CB  ILE A 328     3670   2743   5462    -38    560   -366       C
ATOM   2627  CG1 ILE A 328     -46.603  54.396 -25.292  1.00 29.03           C
ANISOU 2627  CG1 ILE A 328     3409   2494   5126    -71    522   -348       C
ATOM   2628  CG2 ILE A 328     -45.752  52.118 -25.871  1.00 30.81           C
ANISOU 2628  CG2 ILE A 328     3590   2639   5477      2    568   -521       C
ATOM   2629  CD1 ILE A 328     -47.263  53.916 -24.020  1.00 26.35           C
ANISOU 2629  CD1 ILE A 328     3048   2278   4686   -125    525   -485       C
ATOM   2630  N   SER A 329     -42.774  51.846 -24.253  1.00 34.74           N
ANISOU 2630  N   SER A 329     3913   3394   5893   -119    702   -326       N
ATOM   2631  CA  SER A 329     -41.631  50.980 -24.504  1.00 32.47           C
ANISOU 2631  CA  SER A 329     3532   3076   5731   -125    722   -295       C
ATOM   2632  C   SER A 329     -42.036  49.865 -25.460  1.00 33.80           C
ANISOU 2632  C   SER A 329     3706   3115   6022    -36    691   -458       C
ATOM   2633  O   SER A 329     -42.971  49.107 -25.179  1.00 35.56           O
ANISOU 2633  O   SER A 329     3912   3372   6226     11    730   -615       O
ATOM   2634  CB  SER A 329     -41.096  50.399 -23.196  1.00 38.98           C
ANISOU 2634  CB  SER A 329     4215   4158   6437   -198    843   -237       C
ATOM   2635  OG  SER A 329     -40.573  51.419 -22.363  1.00 48.06           O
ANISOU 2635  OG  SER A 329     5336   5439   7486   -302    840     -1       O
ATOM   2636  N   PHE A 330     -41.339  49.774 -26.587  1.00 35.23           N
ANISOU 2636  N   PHE A 330     3899   3140   6347    -15    598   -427       N
ATOM   2637  CA  PHE A 330     -41.521  48.700 -27.549  1.00 30.98           C
ANISOU 2637  CA  PHE A 330     3342   2502   5928     50    533   -519       C
ATOM   2638  C   PHE A 330     -40.344  47.739 -27.472  1.00 36.31           C
ANISOU 2638  C   PHE A 330     3869   3179   6749     19    533   -490       C
ATOM   2639  O   PHE A 330     -39.237  48.116 -27.078  1.00 39.00           O
ANISOU 2639  O   PHE A 330     4146   3537   7134    -60    539   -370       O
ATOM   2640  CB  PHE A 330     -41.639  49.241 -28.976  1.00 32.99           C
ANISOU 2640  CB  PHE A 330     3707   2642   6186     90    406   -514       C
ATOM   2641  CG  PHE A 330     -42.917  49.982 -29.248  1.00 30.07           C
ANISOU 2641  CG  PHE A 330     3438   2282   5704    122    408   -511       C
ATOM   2642  CD1 PHE A 330     -43.090  51.282 -28.805  1.00 28.75           C
ANISOU 2642  CD1 PHE A 330     3325   2157   5442    100    450   -458       C
ATOM   2643  CD2 PHE A 330     -43.937  49.383 -29.969  1.00 32.04           C
ANISOU 2643  CD2 PHE A 330     3701   2490   5984    166    350   -518       C
ATOM   2644  CE1 PHE A 330     -44.264  51.967 -29.064  1.00 25.75           C
ANISOU 2644  CE1 PHE A 330     3004   1792   4988    118    449   -431       C
ATOM   2645  CE2 PHE A 330     -45.111  50.063 -30.232  1.00 31.75           C
ANISOU 2645  CE2 PHE A 330     3723   2459   5880    172    343   -463       C
ATOM   2646  CZ  PHE A 330     -45.275  51.355 -29.778  1.00 25.87           C
ANISOU 2646  CZ  PHE A 330     3027   1772   5032    147    399   -428       C
ATOM   2647  N   MET A 331     -40.589  46.491 -27.856  1.00 39.29           N
ANISOU 2647  N   MET A 331     4164   3519   7247     76    509   -570       N
ATOM   2648  CA  MET A 331     -39.546  45.478 -27.929  1.00 39.28           C
ANISOU 2648  CA  MET A 331     3990   3510   7425     52    490   -536       C
ATOM   2649  C   MET A 331     -39.310  45.142 -29.394  1.00 37.42           C
ANISOU 2649  C   MET A 331     3789   3122   7306     77    288   -539       C
ATOM   2650  O   MET A 331     -40.220  44.661 -30.078  1.00 38.13           O
ANISOU 2650  O   MET A 331     3915   3158   7413    150    216   -583       O
ATOM   2651  CB  MET A 331     -39.931  44.230 -27.136  1.00 44.24           C
ANISOU 2651  CB  MET A 331     4445   4242   8124    111    625   -634       C
ATOM   2652  CG  MET A 331     -38.738  43.423 -26.660  1.00 55.39           C
ANISOU 2652  CG  MET A 331     5623   5752   9671     58    695   -550       C
ATOM   2653  SD  MET A 331     -37.661  44.386 -25.582  1.00 58.60           S
ANISOU 2653  SD  MET A 331     5983   6338   9945    -96    802   -336       S
ATOM   2654  CE  MET A 331     -36.350  43.207 -25.260  1.00 57.12           C
ANISOU 2654  CE  MET A 331     5467   6247   9988   -166    861   -192       C
ATOM   2655  N   LEU A 332     -38.099  45.407 -29.874  1.00 37.08           N
ANISOU 2655  N   LEU A 332     3726   3012   7350      8    174   -485       N
ATOM   2656  CA  LEU A 332     -37.735  45.194 -31.268  1.00 35.64           C
ANISOU 2656  CA  LEU A 332     3584   2732   7226     18    -44   -523       C
ATOM   2657  C   LEU A 332     -36.795  44.001 -31.363  1.00 35.56           C
ANISOU 2657  C   LEU A 332     3366   2683   7464    -26   -131   -482       C
ATOM   2658  O   LEU A 332     -35.749  43.978 -30.706  1.00 34.84           O
ANISOU 2658  O   LEU A 332     3139   2580   7518   -116    -96   -402       O
ATOM   2659  CB  LEU A 332     -37.075  46.439 -31.858  1.00 34.63           C
ANISOU 2659  CB  LEU A 332     3586   2534   7036    -14   -147   -570       C
ATOM   2660  CG  LEU A 332     -36.557  46.292 -33.290  1.00 36.23           C
ANISOU 2660  CG  LEU A 332     3832   2684   7248     -8   -384   -674       C
ATOM   2661  CD1 LEU A 332     -37.704  45.993 -34.244  1.00 35.32           C
ANISOU 2661  CD1 LEU A 332     3808   2677   6934     69   -437   -686       C
ATOM   2662  CD2 LEU A 332     -35.805  47.541 -33.721  1.00 38.75           C
ANISOU 2662  CD2 LEU A 332     4252   2918   7554    -19   -469   -797       C
ATOM   2663  N   TRP A 333     -37.166  43.020 -32.180  1.00 32.45           N
ANISOU 2663  N   TRP A 333     2921   2269   7139     25   -259   -497       N
ATOM   2664  CA  TRP A 333     -36.348  41.842 -32.425  1.00 34.25           C
ANISOU 2664  CA  TRP A 333     2932   2456   7625    -11   -380   -449       C
ATOM   2665  C   TRP A 333     -35.963  41.805 -33.895  1.00 35.21           C
ANISOU 2665  C   TRP A 333     3125   2529   7725    -35   -678   -485       C
ATOM   2666  O   TRP A 333     -36.825  41.930 -34.770  1.00 41.06           O
ANISOU 2666  O   TRP A 333     4003   3318   8281     24   -768   -499       O
ATOM   2667  CB  TRP A 333     -37.089  40.563 -32.034  1.00 44.08           C
ANISOU 2667  CB  TRP A 333     3998   3726   9023     81   -292   -430       C
ATOM   2668  CG  TRP A 333     -37.322  40.450 -30.565  1.00 47.16           C
ANISOU 2668  CG  TRP A 333     4282   4222   9417    108     -1   -457       C
ATOM   2669  CD1 TRP A 333     -38.300  41.066 -29.841  1.00 47.14           C
ANISOU 2669  CD1 TRP A 333     4406   4286   9219    160    173   -535       C
ATOM   2670  CD2 TRP A 333     -36.560  39.674 -29.633  1.00 51.96           C
ANISOU 2670  CD2 TRP A 333     4614   4929  10200     79    148   -409       C
ATOM   2671  NE1 TRP A 333     -38.195  40.721 -28.516  1.00 49.61           N
ANISOU 2671  NE1 TRP A 333     4559   4755   9535    169    414   -569       N
ATOM   2672  CE2 TRP A 333     -37.135  39.867 -28.362  1.00 53.64           C
ANISOU 2672  CE2 TRP A 333     4814   5309  10259    123    423   -482       C
ATOM   2673  CE3 TRP A 333     -35.450  38.833 -29.751  1.00 55.04           C
ANISOU 2673  CE3 TRP A 333     4748   5309  10856     12     73   -303       C
ATOM   2674  CZ2 TRP A 333     -36.637  39.252 -27.216  1.00 57.39           C
ANISOU 2674  CZ2 TRP A 333     5030   5991  10784    111    651   -457       C
ATOM   2675  CZ3 TRP A 333     -34.956  38.223 -28.612  1.00 56.18           C
ANISOU 2675  CZ3 TRP A 333     4616   5628  11101     -5    305   -244       C
ATOM   2676  CH2 TRP A 333     -35.549  38.435 -27.362  1.00 57.37           C
ANISOU 2676  CH2 TRP A 333     4762   5994  11043     49    604   -322       C
ATOM   2677  N   CYS A 334     -34.671  41.640 -34.161  1.00 37.05           N
ANISOU 2677  N   CYS A 334     3253   2685   8138   -133   -841   -490       N
ATOM   2678  CA  CYS A 334     -34.156  41.619 -35.520  1.00 39.05           C
ANISOU 2678  CA  CYS A 334     3566   2915   8354   -170  -1154   -580       C
ATOM   2679  C   CYS A 334     -33.220  40.436 -35.702  1.00 43.28           C
ANISOU 2679  C   CYS A 334     3845   3385   9214   -249  -1342   -507       C
ATOM   2680  O   CYS A 334     -32.553  39.998 -34.761  1.00 51.15           O
ANISOU 2680  O   CYS A 334     4623   4326  10486   -311  -1232   -402       O
ATOM   2681  CB  CYS A 334     -33.413  42.915 -35.862  1.00 38.58           C
ANISOU 2681  CB  CYS A 334     3670   2785   8204   -216  -1239   -748       C
ATOM   2682  SG  CYS A 334     -34.382  44.407 -35.609  1.00 42.89           S
ANISOU 2682  SG  CYS A 334     4472   3404   8422   -125  -1016   -821       S
ATOM   2683  N   LYS A 335     -33.182  39.924 -36.928  1.00 44.51           N
ANISOU 2683  N   LYS A 335     4009   3581   9320   -255  -1634   -540       N
ATOM   2684  CA  LYS A 335     -32.247  38.875 -37.304  1.00 49.55           C
ANISOU 2684  CA  LYS A 335     4408   4157  10262   -345  -1887   -483       C
ATOM   2685  C   LYS A 335     -31.786  39.133 -38.728  1.00 53.24           C
ANISOU 2685  C   LYS A 335     5006   4673  10551   -398  -2255   -650       C
ATOM   2686  O   LYS A 335     -32.612  39.370 -39.613  1.00 52.29           O
ANISOU 2686  O   LYS A 335     5067   4727  10074   -331  -2329   -687       O
ATOM   2687  CB  LYS A 335     -32.882  37.483 -37.191  1.00 54.11           C
ANISOU 2687  CB  LYS A 335     4758   4774  11028   -275  -1869   -294       C
ATOM   2688  CG  LYS A 335     -31.947  36.350 -37.589  1.00 63.92           C
ANISOU 2688  CG  LYS A 335     5712   5959  12614   -365  -2141   -206       C
ATOM   2689  CD  LYS A 335     -31.934  35.242 -36.547  1.00 69.67           C
ANISOU 2689  CD  LYS A 335     6094   6654  13722   -323  -1932    -42       C
ATOM   2690  CE  LYS A 335     -30.805  34.255 -36.810  1.00 78.58           C
ANISOU 2690  CE  LYS A 335     6974   7724  15160   -414  -2140     66       C
ATOM   2691  NZ  LYS A 335     -30.705  33.219 -35.745  1.00 81.89           N
ANISOU 2691  NZ  LYS A 335     7120   8154  15840   -349  -1854    214       N
ATOM   2692  N   ASP A 336     -30.468  39.104 -38.934  1.00 55.28           N
ANISOU 2692  N   ASP A 336     5159   4794  11050   -527  -2489   -750       N
ATOM   2693  CA  ASP A 336     -29.867  39.279 -40.257  1.00 59.18           C
ANISOU 2693  CA  ASP A 336     5751   5334  11401   -589  -2880   -978       C
ATOM   2694  C   ASP A 336     -30.308  40.590 -40.906  1.00 59.08           C
ANISOU 2694  C   ASP A 336     6066   5454  10927   -508  -2849  -1246       C
ATOM   2695  O   ASP A 336     -30.523  40.664 -42.118  1.00 61.56           O
ANISOU 2695  O   ASP A 336     6511   5991  10887   -489  -3074  -1393       O
ATOM   2696  CB  ASP A 336     -30.180  38.088 -41.166  1.00 64.27           C
ANISOU 2696  CB  ASP A 336     6279   6142  11999   -596  -3151   -845       C
ATOM   2697  CG  ASP A 336     -29.647  36.779 -40.614  1.00 72.64           C
ANISOU 2697  CG  ASP A 336     6984   7073  13544   -659  -3192   -603       C
ATOM   2698  OD1 ASP A 336     -28.582  36.795 -39.960  1.00 73.99           O
ANISOU 2698  OD1 ASP A 336     7068   7075  13969   -711  -3098   -581       O
ATOM   2699  OD2 ASP A 336     -30.296  35.735 -40.831  1.00 76.79           O
ANISOU 2699  OD2 ASP A 336     7351   7689  14136   -612  -3254   -391       O
ATOM   2700  N   GLY A 337     -30.453  41.632 -40.091  1.00 56.20           N
ANISOU 2700  N   GLY A 337     5813   4989  10552   -459  -2564  -1296       N
ATOM   2701  CA  GLY A 337     -30.751  42.954 -40.601  1.00 55.50           C
ANISOU 2701  CA  GLY A 337     5988   4996  10104   -374  -2511  -1562       C
ATOM   2702  C   GLY A 337     -32.201  43.224 -40.934  1.00 57.19           C
ANISOU 2702  C   GLY A 337     6368   5496   9867   -251  -2322  -1472       C
ATOM   2703  O   GLY A 337     -32.502  44.297 -41.467  1.00 61.40           O
ANISOU 2703  O   GLY A 337     7096   6169  10065   -173  -2270  -1684       O
ATOM   2704  N   HIS A 338     -33.108  42.295 -40.648  1.00 54.42           N
ANISOU 2704  N   HIS A 338     5922   5224   9529   -227  -2223  -1167       N
ATOM   2705  CA  HIS A 338     -34.527  42.505 -40.887  1.00 50.70           C
ANISOU 2705  CA  HIS A 338     5574   4970   8722   -132  -2062  -1026       C
ATOM   2706  C   HIS A 338     -35.300  42.321 -39.589  1.00 41.49           C
ANISOU 2706  C   HIS A 338     4336   3675   7753    -86  -1751   -816       C
ATOM   2707  O   HIS A 338     -34.814  41.716 -38.630  1.00 41.04           O
ANISOU 2707  O   HIS A 338     4103   3439   8051   -122  -1676   -739       O
ATOM   2708  CB  HIS A 338     -35.064  41.555 -41.968  1.00 55.70           C
ANISOU 2708  CB  HIS A 338     6159   5829   9177   -142  -2299   -853       C
ATOM   2709  CG  HIS A 338     -34.885  40.103 -41.648  1.00 67.20           C
ANISOU 2709  CG  HIS A 338     7360   7147  11025   -185  -2418   -630       C
ATOM   2710  ND1 HIS A 338     -35.574  39.471 -40.634  1.00 68.45           N
ANISOU 2710  ND1 HIS A 338     7380   7160  11468   -130  -2199   -415       N
ATOM   2711  CD2 HIS A 338     -34.102  39.156 -42.217  1.00 72.21           C
ANISOU 2711  CD2 HIS A 338     7832   7776  11828   -267  -2737   -608       C
ATOM   2712  CE1 HIS A 338     -35.219  38.200 -40.589  1.00 69.09           C
ANISOU 2712  CE1 HIS A 338     7212   7152  11888   -160  -2353   -274       C
ATOM   2713  NE2 HIS A 338     -34.326  37.983 -41.538  1.00 72.13           N
ANISOU 2713  NE2 HIS A 338     7572   7614  12218   -252  -2687   -361       N
ATOM   2714  N   VAL A 339     -36.520  42.855 -39.572  1.00 39.89           N
ANISOU 2714  N   VAL A 339     4260   3593   7305     -9  -1572   -732       N
ATOM   2715  CA  VAL A 339     -37.333  42.822 -38.363  1.00 37.42           C
ANISOU 2715  CA  VAL A 339     3908   3172   7140     38  -1295   -599       C
ATOM   2716  C   VAL A 339     -37.892  41.422 -38.154  1.00 47.61           C
ANISOU 2716  C   VAL A 339     5007   4403   8678     59  -1332   -392       C
ATOM   2717  O   VAL A 339     -38.525  40.847 -39.048  1.00 47.81           O
ANISOU 2717  O   VAL A 339     5012   4529   8626     72  -1500   -239       O
ATOM   2718  CB  VAL A 339     -38.463  43.858 -38.447  1.00 40.04           C
ANISOU 2718  CB  VAL A 339     4412   3626   7174    100  -1128   -577       C
ATOM   2719  CG1 VAL A 339     -39.352  43.774 -37.219  1.00 38.89           C
ANISOU 2719  CG1 VAL A 339     4224   3367   7185    139   -887   -471       C
ATOM   2720  CG2 VAL A 339     -37.888  45.256 -38.597  1.00 35.73           C
ANISOU 2720  CG2 VAL A 339     4018   3120   6440    107  -1074   -803       C
ATOM   2721  N   GLU A 340     -37.650  40.862 -36.967  1.00 48.93           N
ANISOU 2721  N   GLU A 340     5014   4423   9156     66  -1176   -378       N
ATOM   2722  CA  GLU A 340     -38.333  39.637 -36.564  1.00 54.00           C
ANISOU 2722  CA  GLU A 340     5461   4988  10069    130  -1144   -243       C
ATOM   2723  C   GLU A 340     -39.723  39.955 -36.026  1.00 50.21           C
ANISOU 2723  C   GLU A 340     5062   4487   9530    212   -952   -210       C
ATOM   2724  O   GLU A 340     -40.732  39.460 -36.541  1.00 49.06           O
ANISOU 2724  O   GLU A 340     4888   4316   9435    259  -1049    -65       O
ATOM   2725  CB  GLU A 340     -37.506  38.888 -35.514  1.00 60.28           C
ANISOU 2725  CB  GLU A 340     6018   5694  11191    117  -1028   -272       C
ATOM   2726  CG  GLU A 340     -36.373  38.038 -36.071  1.00 66.66           C
ANISOU 2726  CG  GLU A 340     6635   6475  12218     42  -1268   -228       C
ATOM   2727  CD  GLU A 340     -36.836  36.663 -36.520  1.00 75.91           C
ANISOU 2727  CD  GLU A 340     7591   7604  13646    106  -1425    -81       C
ATOM   2728  OE1 GLU A 340     -37.517  36.570 -37.562  1.00 80.18           O
ANISOU 2728  OE1 GLU A 340     8219   8193  14054    123  -1631     26       O
ATOM   2729  OE2 GLU A 340     -36.524  35.675 -35.822  1.00 79.30           O
ANISOU 2729  OE2 GLU A 340     7740   7968  14421    140  -1340    -52       O
ATOM   2730  N   THR A 341     -39.792  40.787 -34.989  1.00 46.70           N
ANISOU 2730  N   THR A 341     4702   4040   9003    216   -707   -322       N
ATOM   2731  CA  THR A 341     -41.063  41.252 -34.455  1.00 41.85           C
ANISOU 2731  CA  THR A 341     4178   3408   8316    273   -549   -324       C
ATOM   2732  C   THR A 341     -40.853  42.616 -33.813  1.00 41.19           C
ANISOU 2732  C   THR A 341     4255   3390   8005    236   -377   -422       C
ATOM   2733  O   THR A 341     -39.723  43.076 -33.627  1.00 39.88           O
ANISOU 2733  O   THR A 341     4100   3247   7806    176   -364   -481       O
ATOM   2734  CB  THR A 341     -41.655  40.266 -33.442  1.00 42.46           C
ANISOU 2734  CB  THR A 341     4073   3375   8684    357   -421   -372       C
ATOM   2735  OG1 THR A 341     -42.993  40.663 -33.118  1.00 41.84           O
ANISOU 2735  OG1 THR A 341     4083   3242   8573    405   -343   -386       O
ATOM   2736  CG2 THR A 341     -40.823  40.246 -32.171  1.00 43.12           C
ANISOU 2736  CG2 THR A 341     4058   3516   8809    342   -207   -502       C
ATOM   2737  N   PHE A 342     -41.969  43.257 -33.468  1.00 43.66           N
ANISOU 2737  N   PHE A 342     4672   3708   8210    266   -269   -420       N
ATOM   2738  CA  PHE A 342     -41.948  44.614 -32.927  1.00 38.40           C
ANISOU 2738  CA  PHE A 342     4148   3105   7337    236   -130   -478       C
ATOM   2739  C   PHE A 342     -43.309  44.860 -32.293  1.00 42.01           C
ANISOU 2739  C   PHE A 342     4640   3534   7789    270    -26   -478       C
ATOM   2740  O   PHE A 342     -44.318  44.918 -33.004  1.00 44.77           O
ANISOU 2740  O   PHE A 342     5031   3860   8120    286   -109   -372       O
ATOM   2741  CB  PHE A 342     -41.647  45.625 -34.029  1.00 33.98           C
ANISOU 2741  CB  PHE A 342     3733   2633   6545    214   -225   -464       C
ATOM   2742  CG  PHE A 342     -41.579  47.045 -33.554  1.00 37.20           C
ANISOU 2742  CG  PHE A 342     4256   3082   6798    202    -99   -519       C
ATOM   2743  CD1 PHE A 342     -40.618  47.438 -32.640  1.00 38.65           C
ANISOU 2743  CD1 PHE A 342     4408   3224   7051    162    -18   -574       C
ATOM   2744  CD2 PHE A 342     -42.462  47.994 -34.042  1.00 40.05           C
ANISOU 2744  CD2 PHE A 342     4724   3527   6967    224    -70   -474       C
ATOM   2745  CE1 PHE A 342     -40.549  48.747 -32.210  1.00 36.04           C
ANISOU 2745  CE1 PHE A 342     4159   2910   6625    153     69   -589       C
ATOM   2746  CE2 PHE A 342     -42.397  49.306 -33.614  1.00 36.95           C
ANISOU 2746  CE2 PHE A 342     4406   3162   6473    225     37   -517       C
ATOM   2747  CZ  PHE A 342     -41.440  49.683 -32.697  1.00 36.43           C
ANISOU 2747  CZ  PHE A 342     4314   3027   6500    194     96   -577       C
ATOM   2748  N   TYR A 343     -43.342  44.994 -30.970  1.00 40.73           N
ANISOU 2748  N   TYR A 343     4447   3388   7641    269    140   -582       N
ATOM   2749  CA  TYR A 343     -44.606  45.040 -30.251  1.00 38.57           C
ANISOU 2749  CA  TYR A 343     4181   3081   7392    298    209   -644       C
ATOM   2750  C   TYR A 343     -44.474  45.938 -29.039  1.00 38.94           C
ANISOU 2750  C   TYR A 343     4278   3238   7278    258    365   -724       C
ATOM   2751  O   TYR A 343     -43.368  46.102 -28.502  1.00 35.37           O
ANISOU 2751  O   TYR A 343     3790   2889   6761    216    443   -722       O
ATOM   2752  CB  TYR A 343     -45.047  43.635 -29.815  1.00 35.95           C
ANISOU 2752  CB  TYR A 343     3686   2700   7271    359    207   -735       C
ATOM   2753  CG  TYR A 343     -44.040  42.914 -28.949  1.00 36.66           C
ANISOU 2753  CG  TYR A 343     3622   2841   7467    388    340   -864       C
ATOM   2754  CD1 TYR A 343     -43.049  42.125 -29.518  1.00 36.61           C
ANISOU 2754  CD1 TYR A 343     3490   2804   7616    395    272   -798       C
ATOM   2755  CD2 TYR A 343     -44.082  43.017 -27.564  1.00 38.80           C
ANISOU 2755  CD2 TYR A 343     3848   3236   7659    401    532  -1036       C
ATOM   2756  CE1 TYR A 343     -42.127  41.462 -28.734  1.00 34.87           C
ANISOU 2756  CE1 TYR A 343     3091   2691   7466    396    400   -858       C
ATOM   2757  CE2 TYR A 343     -43.163  42.358 -26.771  1.00 39.19           C
ANISOU 2757  CE2 TYR A 343     3726   3442   7722    405    677  -1098       C
ATOM   2758  CZ  TYR A 343     -42.188  41.581 -27.362  1.00 39.39           C
ANISOU 2758  CZ  TYR A 343     3612   3434   7919    402    617   -995       C
ATOM   2759  OH  TYR A 343     -41.269  40.921 -26.580  1.00 45.64           O
ANISOU 2759  OH  TYR A 343     4195   4398   8747    393    770  -1014       O
ATOM   2760  N   PRO A 344     -45.568  46.535 -28.571  1.00 43.40           N
ANISOU 2760  N   PRO A 344     4908   3795   7786    253    391   -764       N
ATOM   2761  CA  PRO A 344     -45.525  47.304 -27.330  1.00 44.67           C
ANISOU 2761  CA  PRO A 344     5100   4099   7775    207    512   -832       C
ATOM   2762  C   PRO A 344     -45.497  46.387 -26.118  1.00 48.64           C
ANISOU 2762  C   PRO A 344     5479   4699   8304    239    629  -1031       C
ATOM   2763  O   PRO A 344     -46.047  45.284 -26.129  1.00 50.32           O
ANISOU 2763  O   PRO A 344     5595   4804   8721    322    612  -1178       O
ATOM   2764  CB  PRO A 344     -46.825  48.121 -27.366  1.00 45.15           C
ANISOU 2764  CB  PRO A 344     5248   4102   7805    188    459   -815       C
ATOM   2765  CG  PRO A 344     -47.420  47.896 -28.737  1.00 41.11           C
ANISOU 2765  CG  PRO A 344     4752   3467   7402    209    323   -672       C
ATOM   2766  CD  PRO A 344     -46.898  46.584 -29.201  1.00 40.02           C
ANISOU 2766  CD  PRO A 344     4517   3292   7397    257    275   -683       C
ATOM   2767  N   LYS A 345     -44.849  46.865 -25.061  1.00 55.65           N
ANISOU 2767  N   LYS A 345     6351   5809   8986    178    750  -1028       N
ATOM   2768  CA  LYS A 345     -44.751  46.105 -23.828  1.00 62.63           C
ANISOU 2768  CA  LYS A 345     7104   6899   9795    201    899  -1213       C
ATOM   2769  C   LYS A 345     -45.945  46.413 -22.925  1.00 68.67           C
ANISOU 2769  C   LYS A 345     7917   7738  10436    208    911  -1429       C
ATOM   2770  O   LYS A 345     -46.851  47.170 -23.281  1.00 65.52           O
ANISOU 2770  O   LYS A 345     7637   7196  10062    186    792  -1401       O
ATOM   2771  CB  LYS A 345     -43.424  46.399 -23.129  1.00 60.52           C
ANISOU 2771  CB  LYS A 345     6761   6884   9349    109   1014  -1045       C
ATOM   2772  CG  LYS A 345     -42.206  46.027 -23.963  1.00 57.45           C
ANISOU 2772  CG  LYS A 345     6300   6391   9138     89    972   -864       C
ATOM   2773  CD  LYS A 345     -40.909  46.358 -23.247  1.00 59.04           C
ANISOU 2773  CD  LYS A 345     6399   6798   9236    -27   1057   -648       C
ATOM   2774  CE  LYS A 345     -40.780  45.585 -21.946  1.00 62.14           C
ANISOU 2774  CE  LYS A 345     6607   7534   9468    -29   1264   -734       C
ATOM   2775  NZ  LYS A 345     -39.468  45.834 -21.286  1.00 63.43           N
ANISOU 2775  NZ  LYS A 345     6627   7920   9552   -168   1342   -434       N
ATOM   2776  N   LEU A 346     -45.949  45.810 -21.738  1.00 77.78           N
ANISOU 2776  N   LEU A 346     8960   9144  11450    238   1055  -1659       N
ATOM   2777  CA  LEU A 346     -47.041  45.973 -20.784  1.00 86.34           C
ANISOU 2777  CA  LEU A 346    10075  10333  12398    251   1054  -1950       C
ATOM   2778  C   LEU A 346     -47.203  47.423 -20.347  1.00 91.22           C
ANISOU 2778  C   LEU A 346    10825  11088  12746    119    992  -1784       C
ATOM   2779  O   LEU A 346     -48.209  48.066 -20.665  1.00 89.01           O
ANISOU 2779  O   LEU A 346    10650  10614  12555     98    843  -1801       O
ATOM   2780  CB  LEU A 346     -46.809  45.083 -19.560  1.00 90.26           C
ANISOU 2780  CB  LEU A 346    10410  11180  12706    311   1253  -2245       C
ATOM   2781  CG  LEU A 346     -46.833  43.576 -19.811  1.00 92.22           C
ANISOU 2781  CG  LEU A 346    10480  11300  13259    476   1326  -2492       C
ATOM   2782  CD1 LEU A 346     -46.525  42.813 -18.531  1.00 95.14           C
ANISOU 2782  CD1 LEU A 346    10663  12107  13377    541   1570  -2790       C
ATOM   2783  CD2 LEU A 346     -48.183  43.172 -20.369  1.00 92.86           C
ANISOU 2783  CD2 LEU A 346    10616  10983  13683    559   1118  -2675       C
ATOM   2784  N   GLN A 347     -46.222  47.941 -19.617  1.00100.87           N
ANISOU 2784  N   GLN A 347    12016  12640  13672     21   1093  -1587       N
ATOM   2785  CA  GLN A 347     -46.288  49.303 -19.107  1.00107.15           C
ANISOU 2785  CA  GLN A 347    12900  13583  14228   -104   1022  -1393       C
ATOM   2786  C   GLN A 347     -44.892  49.889 -18.924  1.00113.23           C
ANISOU 2786  C   GLN A 347    13620  14528  14874   -208   1078  -1006       C
ATOM   2787  O   GLN A 347     -44.627  51.022 -19.323  1.00114.82           O
ANISOU 2787  O   GLN A 347    13892  14609  15124   -274    975   -731       O
ATOM   2788  CB  GLN A 347     -47.052  49.339 -17.782  1.00110.46           C
ANISOU 2788  CB  GLN A 347    13309  14324  14336   -131   1041  -1671       C
ATOM   2789  CG  GLN A 347     -47.124  50.710 -17.140  1.00111.09           C
ANISOU 2789  CG  GLN A 347    13456  14604  14151   -272    945  -1451       C
ATOM   2790  CD  GLN A 347     -47.705  50.662 -15.742  1.00115.71           C
ANISOU 2790  CD  GLN A 347    14015  15606  14345   -315    960  -1728       C
ATOM   2791  OE1 GLN A 347     -47.922  51.696 -15.109  1.00116.93           O
ANISOU 2791  OE1 GLN A 347    14211  15957  14261   -434    851  -1589       O
ATOM   2792  NE2 GLN A 347     -47.956  49.455 -15.249  1.00118.06           N
ANISOU 2792  NE2 GLN A 347    14228  16058  14572   -210   1090  -2143       N
TER    2793      GLN A 347
ATOM   2794  N   ALA B   0     -43.924  40.844   1.138  1.00 82.01           N
ANISOU 2794  N   ALA B   0    11458   8087  11616  -1627   -886   -922       N
ATOM   2795  CA  ALA B   0     -45.003  40.033   0.591  1.00 77.20           C
ANISOU 2795  CA  ALA B   0    10599   7827  10905  -1528   -978   -868       C
ATOM   2796  C   ALA B   0     -46.309  40.295   1.334  1.00 72.65           C
ANISOU 2796  C   ALA B   0     9823   7412  10369  -1183   -734   -735       C
ATOM   2797  O   ALA B   0     -46.851  39.398   1.981  1.00 72.98           O
ANISOU 2797  O   ALA B   0     9505   7676  10549  -1156   -727   -572       O
ATOM   2798  CB  ALA B   0     -44.649  38.557   0.651  1.00 74.38           C
ANISOU 2798  CB  ALA B   0     9866   7699  10697  -1803  -1215   -729       C
ATOM   2799  N  AMET B   1     -46.816  41.523   1.238  0.56 70.10           N
ANISOU 2799  N  AMET B   1     9734   6976   9924   -919   -535   -802       N
ATOM   2800  N  BMET B   1     -46.792  41.533   1.245  0.44 70.09           N
ANISOU 2800  N  BMET B   1     9738   6970   9925   -922   -535   -803       N
ATOM   2801  CA AMET B   1     -48.058  41.881   1.913  0.56 65.53           C
ANISOU 2801  CA AMET B   1     8978   6545   9375   -638   -338   -674       C
ATOM   2802  CA BMET B   1     -48.064  41.890   1.857  0.44 65.52           C
ANISOU 2802  CA BMET B   1     8986   6544   9366   -637   -341   -680       C
ATOM   2803  C  AMET B   1     -49.248  41.261   1.189  0.56 60.74           C
ANISOU 2803  C  AMET B   1     8225   6194   8658   -547   -409   -639       C
ATOM   2804  C  BMET B   1     -49.201  41.154   1.158  0.44 60.86           C
ANISOU 2804  C  BMET B   1     8231   6217   8677   -568   -428   -639       C
ATOM   2805  O  AMET B   1     -49.382  41.388  -0.032  0.56 60.98           O
ANISOU 2805  O  AMET B   1     8440   6249   8479   -536   -488   -740       O
ATOM   2806  O  BMET B   1     -49.235  41.064  -0.074  0.44 61.43           O
ANISOU 2806  O  BMET B   1     8460   6327   8554   -601   -549   -736       O
ATOM   2807  CB AMET B   1     -48.206  43.401   1.979  0.56 66.51           C
ANISOU 2807  CB AMET B   1     9347   6502   9422   -393   -117   -713       C
ATOM   2808  CB BMET B   1     -48.261  43.410   1.797  0.44 66.66           C
ANISOU 2808  CB BMET B   1     9387   6528   9411   -386   -126   -730       C
ATOM   2809  CG AMET B   1     -49.250  43.892   2.972  0.56 63.96           C
ANISOU 2809  CG AMET B   1     8820   6309   9173   -168     61   -549       C
ATOM   2810  CG BMET B   1     -49.608  43.892   1.262  0.44 66.64           C
ANISOU 2810  CG BMET B   1     9354   6705   9263   -133    -19   -695       C
ATOM   2811  SD AMET B   1     -48.823  43.459   4.670  0.56 59.97           S
ANISOU 2811  SD AMET B   1     8087   5807   8893   -269     99   -393       S
ATOM   2812  SD BMET B   1     -49.598  44.164  -0.524  0.44 71.40           S
ANISOU 2812  SD BMET B   1    10281   7299   9550    -97    -72   -879       S
ATOM   2813  CE AMET B   1     -47.261  44.317   4.866  0.56 60.86           C
ANISOU 2813  CE AMET B   1     8496   5557   9070   -347    154   -434       C
ATOM   2814  CE BMET B   1     -51.188  44.954  -0.770  0.44 69.92           C
ANISOU 2814  CE BMET B   1     9984   7322   9261    222    140   -744       C
ATOM   2815  N   SER B   2     -50.118  40.598   1.948  1.00 51.76           N
ANISOU 2815  N   SER B   2     6787   5232   7647   -477   -371   -494       N
ATOM   2816  CA  SER B   2     -51.231  39.856   1.375  1.00 42.81           C
ANISOU 2816  CA  SER B   2     5504   4300   6462   -403   -443   -427       C
ATOM   2817  C   SER B   2     -52.334  39.699   2.406  1.00 36.59           C
ANISOU 2817  C   SER B   2     4510   3597   5796   -258   -312   -307       C
ATOM   2818  O   SER B   2     -52.097  39.760   3.615  1.00 36.84           O
ANISOU 2818  O   SER B   2     4454   3590   5954   -259   -213   -268       O
ATOM   2819  CB  SER B   2     -50.790  38.479   0.873  1.00 45.84           C
ANISOU 2819  CB  SER B   2     5723   4804   6889   -586   -674   -393       C
ATOM   2820  OG  SER B   2     -50.775  37.528   1.925  1.00 44.71           O
ANISOU 2820  OG  SER B   2     5280   4740   6969   -611   -651   -271       O
ATOM   2821  N   LEU B   3     -53.549  39.478   1.899  1.00 29.13           N
ANISOU 2821  N   LEU B   3     3512   2761   4794   -147   -320   -246       N
ATOM   2822  CA  LEU B   3     -54.693  39.241   2.771  1.00 30.67           C
ANISOU 2822  CA  LEU B   3     3556   3004   5095    -41   -229   -156       C
ATOM   2823  C   LEU B   3     -54.509  37.973   3.596  1.00 32.74           C
ANISOU 2823  C   LEU B   3     3609   3305   5527    -80   -255   -110       C
ATOM   2824  O   LEU B   3     -54.793  37.958   4.800  1.00 33.99           O
ANISOU 2824  O   LEU B   3     3701   3446   5766    -33   -139    -95       O
ATOM   2825  CB  LEU B   3     -55.968  39.152   1.934  1.00 33.64           C
ANISOU 2825  CB  LEU B   3     3934   3452   5396     48   -253    -82       C
ATOM   2826  CG  LEU B   3     -57.216  38.606   2.623  1.00 35.68           C
ANISOU 2826  CG  LEU B   3     4066   3717   5775    118   -212      3       C
ATOM   2827  CD1 LEU B   3     -57.708  39.567   3.694  1.00 38.69           C
ANISOU 2827  CD1 LEU B   3     4467   4055   6177    150    -84     -4       C
ATOM   2828  CD2 LEU B   3     -58.307  38.323   1.601  1.00 34.22           C
ANISOU 2828  CD2 LEU B   3     3889   3577   5536    168   -268    107       C
ATOM   2829  N   GLU B   4     -54.046  36.895   2.961  1.00 32.19           N
ANISOU 2829  N   GLU B   4     3426   3310   5495   -156   -402    -76       N
ATOM   2830  CA  GLU B   4     -53.855  35.639   3.677  1.00 28.54           C
ANISOU 2830  CA  GLU B   4     2718   2917   5209   -155   -398      1       C
ATOM   2831  C   GLU B   4     -52.764  35.756   4.732  1.00 26.80           C
ANISOU 2831  C   GLU B   4     2444   2665   5074   -257   -310    -15       C
ATOM   2832  O   GLU B   4     -52.838  35.097   5.775  1.00 28.48           O
ANISOU 2832  O   GLU B   4     2497   2923   5402   -195   -191     40       O
ATOM   2833  CB  GLU B   4     -53.526  34.517   2.691  1.00 34.88           C
ANISOU 2833  CB  GLU B   4     3365   3847   6043   -219   -599     87       C
ATOM   2834  CG  GLU B   4     -54.707  34.050   1.842  1.00 41.10           C
ANISOU 2834  CG  GLU B   4     4143   4684   6788    -83   -669    174       C
ATOM   2835  CD  GLU B   4     -55.104  35.046   0.763  1.00 46.79           C
ANISOU 2835  CD  GLU B   4     5114   5379   7283    -94   -719    121       C
ATOM   2836  OE1 GLU B   4     -54.395  36.059   0.585  1.00 46.94           O
ANISOU 2836  OE1 GLU B   4     5320   5339   7176   -189   -705     -2       O
ATOM   2837  OE2 GLU B   4     -56.129  34.812   0.090  1.00 48.70           O
ANISOU 2837  OE2 GLU B   4     5371   5654   7476      8   -752    216       O
ATOM   2838  N   ASN B   5     -51.750  36.587   4.486  1.00 29.62           N
ANISOU 2838  N   ASN B   5     2956   2930   5367   -401   -349    -84       N
ATOM   2839  CA  ASN B   5     -50.699  36.770   5.480  1.00 30.86           C
ANISOU 2839  CA  ASN B   5     3084   3028   5613   -512   -262    -65       C
ATOM   2840  C   ASN B   5     -51.195  37.595   6.659  1.00 28.17           C
ANISOU 2840  C   ASN B   5     2823   2633   5246   -380    -63    -65       C
ATOM   2841  O   ASN B   5     -50.843  37.317   7.811  1.00 35.78           O
ANISOU 2841  O   ASN B   5     3682   3630   6284   -390     57      2       O
ATOM   2842  CB  ASN B   5     -49.474  37.424   4.843  1.00 26.82           C
ANISOU 2842  CB  ASN B   5     2762   2372   5054   -711   -369   -141       C
ATOM   2843  CG  ASN B   5     -48.412  37.786   5.862  1.00 41.63           C
ANISOU 2843  CG  ASN B   5     4652   4135   7031   -829   -267    -96       C
ATOM   2844  OD1 ASN B   5     -48.215  38.958   6.180  1.00 38.89           O
ANISOU 2844  OD1 ASN B   5     4526   3623   6630   -779   -165   -137       O
ATOM   2845  ND2 ASN B   5     -47.728  36.776   6.388  1.00 40.49           N
ANISOU 2845  ND2 ASN B   5     4252   4091   7041   -973   -282     22       N
ATOM   2846  N   VAL B   6     -52.009  38.618   6.391  1.00 25.39           N
ANISOU 2846  N   VAL B   6     2643   2227   4776   -262    -29   -117       N
ATOM   2847  CA  VAL B   6     -52.593  39.401   7.475  1.00 26.46           C
ANISOU 2847  CA  VAL B   6     2824   2353   4876   -154    113    -94       C
ATOM   2848  C   VAL B   6     -53.437  38.507   8.373  1.00 28.78           C
ANISOU 2848  C   VAL B   6     2979   2747   5210    -78    179    -66       C
ATOM   2849  O   VAL B   6     -53.373  38.596   9.605  1.00 33.34           O
ANISOU 2849  O   VAL B   6     3541   3350   5775    -58    292    -37       O
ATOM   2850  CB  VAL B   6     -53.411  40.576   6.906  1.00 31.60           C
ANISOU 2850  CB  VAL B   6     3618   2974   5416    -49    121   -116       C
ATOM   2851  CG1 VAL B   6     -54.191  41.266   8.008  1.00 31.09           C
ANISOU 2851  CG1 VAL B   6     3546   2949   5319     36    214    -65       C
ATOM   2852  CG2 VAL B   6     -52.497  41.571   6.207  1.00 33.91           C
ANISOU 2852  CG2 VAL B   6     4093   3137   5653    -69    120   -159       C
ATOM   2853  N   ALA B   7     -54.223  37.614   7.768  1.00 30.82           N
ANISOU 2853  N   ALA B   7     3158   3051   5502    -22    117    -72       N
ATOM   2854  CA  ALA B   7     -55.047  36.704   8.551  1.00 26.15           C
ANISOU 2854  CA  ALA B   7     2481   2500   4956     82    197    -69       C
ATOM   2855  C   ALA B   7     -54.199  35.712   9.335  1.00 30.84           C
ANISOU 2855  C   ALA B   7     2905   3171   5642     72    293    -20       C
ATOM   2856  O   ALA B   7     -54.576  35.320  10.445  1.00 33.74           O
ANISOU 2856  O   ALA B   7     3262   3566   5991    164    437    -34       O
ATOM   2857  CB  ALA B   7     -56.026  35.968   7.637  1.00 24.75           C
ANISOU 2857  CB  ALA B   7     2269   2315   4821    162    113    -56       C
ATOM   2858  N   PHE B   8     -53.058  35.297   8.778  1.00 31.46           N
ANISOU 2858  N   PHE B   8     2853   3292   5807    -50    216     43       N
ATOM   2859  CA  PHE B   8     -52.166  34.401   9.506  1.00 31.11           C
ANISOU 2859  CA  PHE B   8     2595   3352   5874    -89    315    138       C
ATOM   2860  C   PHE B   8     -51.662  35.054  10.785  1.00 36.78           C
ANISOU 2860  C   PHE B   8     3390   4060   6525   -123    476    155       C
ATOM   2861  O   PHE B   8     -51.636  34.421  11.846  1.00 43.69           O
ANISOU 2861  O   PHE B   8     4163   5032   7406    -42    656    204       O
ATOM   2862  CB  PHE B   8     -50.994  33.985   8.617  1.00 29.40           C
ANISOU 2862  CB  PHE B   8     2227   3180   5765   -287    152    215       C
ATOM   2863  CG  PHE B   8     -49.939  33.188   9.335  1.00 32.38           C
ANISOU 2863  CG  PHE B   8     2344   3680   6280   -384    246    359       C
ATOM   2864  CD1 PHE B   8     -50.020  31.807   9.403  1.00 35.60           C
ANISOU 2864  CD1 PHE B   8     2436   4262   6826   -286    293    481       C
ATOM   2865  CD2 PHE B   8     -48.861  33.819   9.939  1.00 37.24           C
ANISOU 2865  CD2 PHE B   8     3013   4238   6900   -561    302    405       C
ATOM   2866  CE1 PHE B   8     -49.052  31.070  10.063  1.00 37.37           C
ANISOU 2866  CE1 PHE B   8     2372   4640   7188   -370    406    651       C
ATOM   2867  CE2 PHE B   8     -47.894  33.090  10.604  1.00 41.98           C
ANISOU 2867  CE2 PHE B   8     3352   4964   7633   -674    402    575       C
ATOM   2868  CZ  PHE B   8     -47.987  31.713  10.664  1.00 40.16           C
ANISOU 2868  CZ  PHE B   8     2776   4945   7537   -583    459    702       C
ATOM   2869  N   ASN B   9     -51.247  36.320  10.700  1.00 34.23           N
ANISOU 2869  N   ASN B   9     3254   3624   6126   -219    430    131       N
ATOM   2870  CA  ASN B   9     -50.759  37.016  11.885  1.00 30.80           C
ANISOU 2870  CA  ASN B   9     2900   3180   5625   -243    565    189       C
ATOM   2871  C   ASN B   9     -51.860  37.169  12.924  1.00 27.86           C
ANISOU 2871  C   ASN B   9     2612   2869   5106    -85    680    142       C
ATOM   2872  O   ASN B   9     -51.613  37.027  14.126  1.00 33.66           O
ANISOU 2872  O   ASN B   9     3333   3688   5768    -62    834    202       O
ATOM   2873  CB  ASN B   9     -50.195  38.382  11.496  1.00 30.02           C
ANISOU 2873  CB  ASN B   9     2995   2920   5490   -325    492    185       C
ATOM   2874  CG  ASN B   9     -48.823  38.289  10.863  1.00 25.78           C
ANISOU 2874  CG  ASN B   9     2439   2280   5076   -531    408    228       C
ATOM   2875  OD1 ASN B   9     -47.807  38.485  11.529  1.00 41.71           O
ANISOU 2875  OD1 ASN B   9     4458   4245   7146   -647    480    340       O
ATOM   2876  ND2 ASN B   9     -48.786  37.989   9.571  1.00 27.48           N
ANISOU 2876  ND2 ASN B   9     2654   2460   5326   -598    240    148       N
ATOM   2877  N   VAL B  10     -53.084  37.448  12.477  1.00 22.60           N
ANISOU 2877  N   VAL B  10     2045   2164   4379      5    601     39       N
ATOM   2878  CA  VAL B  10     -54.181  37.671  13.413  1.00 28.61           C
ANISOU 2878  CA  VAL B  10     2921   2957   4993     99    660    -25       C
ATOM   2879  C   VAL B  10     -54.482  36.402  14.200  1.00 33.62           C
ANISOU 2879  C   VAL B  10     3492   3666   5616    206    811    -63       C
ATOM   2880  O   VAL B  10     -54.674  36.442  15.421  1.00 37.34           O
ANISOU 2880  O   VAL B  10     4054   4204   5931    249    933    -85       O
ATOM   2881  CB  VAL B  10     -55.424  38.183  12.663  1.00 28.17           C
ANISOU 2881  CB  VAL B  10     2962   2831   4912    128    529   -101       C
ATOM   2882  CG1 VAL B  10     -56.635  38.182  13.579  1.00 29.56           C
ANISOU 2882  CG1 VAL B  10     3258   3019   4957    177    553   -185       C
ATOM   2883  CG2 VAL B  10     -55.169  39.578  12.118  1.00 20.05           C
ANISOU 2883  CG2 VAL B  10     1999   1762   3857     75    443    -49       C
ATOM   2884  N   VAL B  11     -54.514  35.255  13.521  1.00 33.93           N
ANISOU 2884  N   VAL B  11     3379   3706   5806    270    815    -61       N
ATOM   2885  CA  VAL B  11     -54.884  34.022  14.208  1.00 34.26           C
ANISOU 2885  CA  VAL B  11     3359   3802   5855    436    993    -93       C
ATOM   2886  C   VAL B  11     -53.744  33.512  15.084  1.00 34.81           C
ANISOU 2886  C   VAL B  11     3268   4027   5932    430   1190     27       C
ATOM   2887  O   VAL B  11     -53.989  32.867  16.109  1.00 37.71           O
ANISOU 2887  O   VAL B  11     3659   4468   6200    578   1406     -6       O
ATOM   2888  CB  VAL B  11     -55.340  32.956  13.196  1.00 40.29           C
ANISOU 2888  CB  VAL B  11     3986   4524   6798    547    938    -84       C
ATOM   2889  CG1 VAL B  11     -56.561  33.441  12.429  1.00 42.03           C
ANISOU 2889  CG1 VAL B  11     4383   4590   6998    551    774   -176       C
ATOM   2890  CG2 VAL B  11     -54.220  32.603  12.237  1.00 46.80           C
ANISOU 2890  CG2 VAL B  11     4555   5432   7796    434    832     62       C
ATOM   2891  N   ASN B  12     -52.495  33.795  14.719  1.00 34.81           N
ANISOU 2891  N   ASN B  12     3123   4069   6034    256   1131    169       N
ATOM   2892  CA  ASN B  12     -51.350  33.293  15.469  1.00 37.54           C
ANISOU 2892  CA  ASN B  12     3278   4563   6422    205   1310    332       C
ATOM   2893  C   ASN B  12     -50.804  34.286  16.482  1.00 40.75           C
ANISOU 2893  C   ASN B  12     3836   4985   6662    110   1387    395       C
ATOM   2894  O   ASN B  12     -50.281  33.867  17.520  1.00 46.02           O
ANISOU 2894  O   ASN B  12     4424   5798   7262    138   1610    507       O
ATOM   2895  CB  ASN B  12     -50.218  32.892  14.514  1.00 40.90           C
ANISOU 2895  CB  ASN B  12     3442   5015   7083     22   1185    479       C
ATOM   2896  CG  ASN B  12     -50.538  31.643  13.719  1.00 44.27           C
ANISOU 2896  CG  ASN B  12     3625   5514   7681    130   1142    503       C
ATOM   2897  OD1 ASN B  12     -50.330  30.523  14.188  1.00 49.34           O
ANISOU 2897  OD1 ASN B  12     4011   6323   8414    251   1329    618       O
ATOM   2898  ND2 ASN B  12     -51.038  31.829  12.504  1.00 41.21           N
ANISOU 2898  ND2 ASN B  12     3303   5021   7336    106    907    422       N
ATOM   2899  N   LYS B  13     -50.906  35.587  16.211  1.00 35.78           N
ANISOU 2899  N   LYS B  13     3408   4225   5962     17   1225    354       N
ATOM   2900  CA  LYS B  13     -50.338  36.602  17.086  1.00 33.36           C
ANISOU 2900  CA  LYS B  13     3232   3923   5522    -59   1274    459       C
ATOM   2901  C   LYS B  13     -51.375  37.545  17.677  1.00 32.87           C
ANISOU 2901  C   LYS B  13     3409   3855   5224     23   1225    361       C
ATOM   2902  O   LYS B  13     -51.001  38.465  18.412  1.00 35.43           O
ANISOU 2902  O   LYS B  13     3840   4202   5420    -18   1240    472       O
ATOM   2903  CB  LYS B  13     -49.280  37.419  16.333  1.00 35.64           C
ANISOU 2903  CB  LYS B  13     3529   4056   5957   -241   1138    558       C
ATOM   2904  CG  LYS B  13     -48.111  36.595  15.818  1.00 42.66           C
ANISOU 2904  CG  LYS B  13     4191   4946   7070   -406   1140    674       C
ATOM   2905  CD  LYS B  13     -47.321  35.982  16.963  1.00 49.15           C
ANISOU 2905  CD  LYS B  13     4858   5932   7886   -446   1370    873       C
ATOM   2906  CE  LYS B  13     -46.141  35.173  16.451  1.00 52.07           C
ANISOU 2906  CE  LYS B  13     4950   6324   8508   -658   1349   1028       C
ATOM   2907  NZ  LYS B  13     -45.312  34.637  17.567  1.00 55.06           N
ANISOU 2907  NZ  LYS B  13     5147   6879   8894   -716   1597   1272       N
ATOM   2908  N   GLY B  14     -52.661  37.345  17.389  1.00 33.28           N
ANISOU 2908  N   GLY B  14     3543   3878   5223    122   1153    182       N
ATOM   2909  CA  GLY B  14     -53.695  38.243  17.854  1.00 30.36           C
ANISOU 2909  CA  GLY B  14     3375   3508   4654    143   1058     98       C
ATOM   2910  C   GLY B  14     -53.791  39.549  17.099  1.00 32.31           C
ANISOU 2910  C   GLY B  14     3666   3661   4952     78    869    140       C
ATOM   2911  O   GLY B  14     -54.762  40.290  17.298  1.00 34.26           O
ANISOU 2911  O   GLY B  14     4020   3923   5073     81    758     93       O
ATOM   2912  N   HIS B  15     -52.826  39.851  16.243  1.00 31.34           N
ANISOU 2912  N   HIS B  15     3465   3441   5002     16    832    228       N
ATOM   2913  CA  HIS B  15     -52.781  41.075  15.448  1.00 24.45           C
ANISOU 2913  CA  HIS B  15     2648   2462   4181      0    705    266       C
ATOM   2914  C   HIS B  15     -51.690  40.881  14.401  1.00 23.00           C
ANISOU 2914  C   HIS B  15     2410   2142   4185    -75    686    288       C
ATOM   2915  O   HIS B  15     -51.093  39.803  14.301  1.00 26.25           O
ANISOU 2915  O   HIS B  15     2704   2572   4696   -137    736    290       O
ATOM   2916  CB  HIS B  15     -52.513  42.301  16.320  1.00 26.07           C
ANISOU 2916  CB  HIS B  15     2936   2706   4265     12    711    415       C
ATOM   2917  CG  HIS B  15     -51.122  42.351  16.869  1.00 30.32           C
ANISOU 2917  CG  HIS B  15     3470   3207   4842    -43    821    578       C
ATOM   2918  ND1 HIS B  15     -50.306  43.453  16.729  1.00 32.40           N
ANISOU 2918  ND1 HIS B  15     3803   3339   5170    -41    809    726       N
ATOM   2919  CD2 HIS B  15     -50.399  41.430  17.549  1.00 30.95           C
ANISOU 2919  CD2 HIS B  15     3483   3355   4921   -101    960    640       C
ATOM   2920  CE1 HIS B  15     -49.140  43.209  17.301  1.00 34.73           C
ANISOU 2920  CE1 HIS B  15     4092   3595   5508   -123    917    871       C
ATOM   2921  NE2 HIS B  15     -49.172  41.990  17.809  1.00 34.10           N
ANISOU 2921  NE2 HIS B  15     3911   3658   5387   -170   1012    833       N
ATOM   2922  N   PHE B  16     -51.412  41.926  13.628  1.00 29.38           N
ANISOU 2922  N   PHE B  16     3306   2820   5038    -71    615    308       N
ATOM   2923  CA  PHE B  16     -50.333  41.862  12.652  1.00 32.98           C
ANISOU 2923  CA  PHE B  16     3786   3113   5632   -165    578    296       C
ATOM   2924  C   PHE B  16     -48.997  42.026  13.367  1.00 36.14           C
ANISOU 2924  C   PHE B  16     4212   3429   6090   -266    661    442       C
ATOM   2925  O   PHE B  16     -48.739  43.066  13.983  1.00 38.80           O
ANISOU 2925  O   PHE B  16     4653   3711   6379   -208    710    562       O
ATOM   2926  CB  PHE B  16     -50.504  42.928  11.575  1.00 22.57           C
ANISOU 2926  CB  PHE B  16     2602   1664   4309    -94    510    244       C
ATOM   2927  CG  PHE B  16     -49.492  42.829  10.469  1.00 31.46           C
ANISOU 2927  CG  PHE B  16     3821   2606   5527   -201    450    175       C
ATOM   2928  CD1 PHE B  16     -49.660  41.917   9.440  1.00 31.10           C
ANISOU 2928  CD1 PHE B  16     3716   2593   5506   -275    342     62       C
ATOM   2929  CD2 PHE B  16     -48.367  43.638  10.463  1.00 28.58           C
ANISOU 2929  CD2 PHE B  16     3623   2021   5214   -236    487    227       C
ATOM   2930  CE1 PHE B  16     -48.728  41.816   8.423  1.00 30.59           C
ANISOU 2930  CE1 PHE B  16     3759   2377   5486   -410    247    -16       C
ATOM   2931  CE2 PHE B  16     -47.432  43.543   9.449  1.00 32.60           C
ANISOU 2931  CE2 PHE B  16     4273   2328   5787   -369    410    127       C
ATOM   2932  CZ  PHE B  16     -47.614  42.630   8.427  1.00 35.15           C
ANISOU 2932  CZ  PHE B  16     4536   2716   6102   -471    277     -2       C
ATOM   2933  N   ASP B  17     -48.152  41.000  13.287  1.00 36.66           N
ANISOU 2933  N   ASP B  17     4164   3494   6272   -423    672    466       N
ATOM   2934  CA  ASP B  17     -46.851  41.005  13.944  1.00 36.11           C
ANISOU 2934  CA  ASP B  17     4089   3344   6286   -569    754    634       C
ATOM   2935  C   ASP B  17     -45.706  40.844  12.951  1.00 39.33           C
ANISOU 2935  C   ASP B  17     4538   3540   6865   -784    646    609       C
ATOM   2936  O   ASP B  17     -44.567  40.599  13.365  1.00 45.12           O
ANISOU 2936  O   ASP B  17     5231   4198   7714   -974    689    754       O
ATOM   2937  CB  ASP B  17     -46.795  39.903  15.008  1.00 45.68           C
ANISOU 2937  CB  ASP B  17     5094   4785   7477   -596    895    741       C
ATOM   2938  CG  ASP B  17     -45.704  40.133  16.038  1.00 57.26           C
ANISOU 2938  CG  ASP B  17     6567   6226   8964   -702   1028    974       C
ATOM   2939  OD1 ASP B  17     -45.744  41.173  16.726  1.00 60.04           O
ANISOU 2939  OD1 ASP B  17     7076   6534   9202   -612   1074   1073       O
ATOM   2940  OD2 ASP B  17     -44.810  39.268  16.162  1.00 62.03           O
ANISOU 2940  OD2 ASP B  17     6997   6868   9702   -879   1084   1092       O
ATOM   2941  N   GLY B  18     -45.976  40.975  11.654  1.00 36.28           N
ANISOU 2941  N   GLY B  18     4244   3058   6482   -780    501    433       N
ATOM   2942  CA  GLY B  18     -44.937  40.848  10.654  1.00 35.54           C
ANISOU 2942  CA  GLY B  18     4243   2760   6500  -1005    363    369       C
ATOM   2943  C   GLY B  18     -44.434  39.444  10.416  1.00 39.69           C
ANISOU 2943  C   GLY B  18     4506   3424   7151  -1236    269    408       C
ATOM   2944  O   GLY B  18     -43.388  39.277   9.782  1.00 47.16           O
ANISOU 2944  O   GLY B  18     5510   4219   8191  -1495    130    391       O
ATOM   2945  N   GLN B  19     -45.139  38.428  10.904  1.00 38.67           N
ANISOU 2945  N   GLN B  19     4096   3581   7017  -1143    336    463       N
ATOM   2946  CA  GLN B  19     -44.722  37.052  10.698  1.00 33.63           C
ANISOU 2946  CA  GLN B  19     3144   3117   6516  -1310    269    543       C
ATOM   2947  C   GLN B  19     -45.131  36.572   9.309  1.00 39.01           C
ANISOU 2947  C   GLN B  19     3801   3837   7185  -1333     44    402       C
ATOM   2948  O   GLN B  19     -46.073  37.082   8.697  1.00 38.81           O
ANISOU 2948  O   GLN B  19     3946   3777   7023  -1153      2    253       O
ATOM   2949  CB  GLN B  19     -45.327  36.141  11.766  1.00 37.48           C
ANISOU 2949  CB  GLN B  19     3360   3883   6998  -1142    471    659       C
ATOM   2950  CG  GLN B  19     -45.141  36.643  13.190  1.00 42.79           C
ANISOU 2950  CG  GLN B  19     4090   4568   7599  -1075    702    790       C
ATOM   2951  CD  GLN B  19     -43.685  36.698  13.609  1.00 51.94           C
ANISOU 2951  CD  GLN B  19     5200   5634   8899  -1349    738    992       C
ATOM   2952  OE1 GLN B  19     -42.854  35.935  13.116  1.00 56.73           O
ANISOU 2952  OE1 GLN B  19     5657   6301   9597  -1552    614   1037       O
ATOM   2953  NE2 GLN B  19     -43.368  37.607  14.523  1.00 55.72           N
ANISOU 2953  NE2 GLN B  19     5858   6008   9303  -1321    871   1098       N
ATOM   2954  N   GLN B  20     -44.404  35.577   8.811  1.00 41.55           N
ANISOU 2954  N   GLN B  20     3886   4254   7646  -1571   -109    481       N
ATOM   2955  CA  GLN B  20     -44.701  34.986   7.516  1.00 47.83           C
ANISOU 2955  CA  GLN B  20     4619   5134   8418  -1618   -352    393       C
ATOM   2956  C   GLN B  20     -45.610  33.773   7.674  1.00 45.96           C
ANISOU 2956  C   GLN B  20     4041   5192   8231  -1411   -295    488       C
ATOM   2957  O   GLN B  20     -45.526  33.031   8.655  1.00 44.98           O
ANISOU 2957  O   GLN B  20     3650   5239   8201  -1340   -111    648       O
ATOM   2958  CB  GLN B  20     -43.418  34.578   6.790  1.00 56.13           C
ANISOU 2958  CB  GLN B  20     5674   6191   9462  -1940   -574    403       C
ATOM   2959  CG  GLN B  20     -42.717  35.719   6.077  1.00 67.57           C
ANISOU 2959  CG  GLN B  20     7559   7321  10793  -2106   -692    216       C
ATOM   2960  CD  GLN B  20     -41.640  35.233   5.128  1.00 87.16           C
ANISOU 2960  CD  GLN B  20    10059   9815  13241  -2425   -941    167       C
ATOM   2961  OE1 GLN B  20     -41.235  34.071   5.173  1.00 95.64           O
ANISOU 2961  OE1 GLN B  20    10787  11141  14411  -2550  -1019    317       O
ATOM   2962  NE2 GLN B  20     -41.175  36.120   4.256  1.00 92.62           N
ANISOU 2962  NE2 GLN B  20    11158  10237  13795  -2535  -1054    -51       N
ATOM   2963  N   GLY B  21     -46.472  33.579   6.692  1.00 44.12           N
ANISOU 2963  N   GLY B  21     3849   5009   7905  -1285   -433    394       N
ATOM   2964  CA  GLY B  21     -47.427  32.486   6.687  1.00 44.90           C
ANISOU 2964  CA  GLY B  21     3681   5326   8055  -1057   -392    478       C
ATOM   2965  C   GLY B  21     -48.742  32.933   6.079  1.00 39.35           C
ANISOU 2965  C   GLY B  21     3202   4558   7190   -826   -410    340       C
ATOM   2966  O   GLY B  21     -49.068  34.118   6.026  1.00 35.40           O
ANISOU 2966  O   GLY B  21     3019   3888   6544   -781   -368    201       O
ATOM   2967  N   GLU B  22     -49.514  31.958   5.604  1.00 40.81           N
ANISOU 2967  N   GLU B  22     3198   4889   7417   -671   -469    414       N
ATOM   2968  CA  GLU B  22     -50.805  32.226   4.989  1.00 40.32           C
ANISOU 2968  CA  GLU B  22     3316   4774   7231   -470   -490    333       C
ATOM   2969  C   GLU B  22     -51.831  31.230   5.505  1.00 40.76           C
ANISOU 2969  C   GLU B  22     3187   4907   7392   -191   -344    424       C
ATOM   2970  O   GLU B  22     -51.506  30.078   5.805  1.00 46.42           O
ANISOU 2970  O   GLU B  22     3580   5780   8277   -143   -308    579       O
ATOM   2971  CB  GLU B  22     -50.740  32.149   3.455  1.00 47.27           C
ANISOU 2971  CB  GLU B  22     4253   5699   8008   -583   -778    326       C
ATOM   2972  CG  GLU B  22     -50.003  33.299   2.786  1.00 52.50           C
ANISOU 2972  CG  GLU B  22     5228   6223   8498   -797   -899    169       C
ATOM   2973  CD  GLU B  22     -48.500  33.106   2.770  1.00 65.55           C
ANISOU 2973  CD  GLU B  22     6796   7880  10230  -1115  -1042    190       C
ATOM   2974  OE1 GLU B  22     -48.035  32.007   3.138  1.00 72.24           O
ANISOU 2974  OE1 GLU B  22     7280   8899  11269  -1189  -1078    363       O
ATOM   2975  OE2 GLU B  22     -47.784  34.055   2.387  1.00 69.31           O
ANISOU 2975  OE2 GLU B  22     7568   8179  10588  -1291  -1111     43       O
ATOM   2976  N   VAL B  23     -53.075  31.688   5.608  1.00 35.38           N
ANISOU 2976  N   VAL B  23     2715   4106   6620     -7   -252    335       N
ATOM   2977  CA  VAL B  23     -54.203  30.828   5.959  1.00 35.92           C
ANISOU 2977  CA  VAL B  23     2707   4166   6773    259   -129    385       C
ATOM   2978  C   VAL B  23     -55.327  31.091   4.963  1.00 38.38           C
ANISOU 2978  C   VAL B  23     3192   4390   7000    334   -246    371       C
ATOM   2979  O   VAL B  23     -55.452  32.216   4.457  1.00 37.15           O
ANISOU 2979  O   VAL B  23     3263   4163   6688    226   -316    280       O
ATOM   2980  CB  VAL B  23     -54.666  31.061   7.407  1.00 32.33           C
ANISOU 2980  CB  VAL B  23     2360   3624   6300    387    135    291       C
ATOM   2981  CG1 VAL B  23     -53.584  30.639   8.390  1.00 34.86           C
ANISOU 2981  CG1 VAL B  23     2480   4068   6699    340    283    356       C
ATOM   2982  CG2 VAL B  23     -55.041  32.512   7.620  1.00 30.48           C
ANISOU 2982  CG2 VAL B  23     2430   3256   5894    304    143    147       C
ATOM   2983  N   PRO B  24     -56.157  30.097   4.645  1.00 42.19           N
ANISOU 2983  N   PRO B  24     3573   4871   7586    531   -252    482       N
ATOM   2984  CA  PRO B  24     -57.224  30.320   3.663  1.00 40.46           C
ANISOU 2984  CA  PRO B  24     3515   4566   7293    585   -362    513       C
ATOM   2985  C   PRO B  24     -58.284  31.273   4.196  1.00 35.15           C
ANISOU 2985  C   PRO B  24     3122   3697   6534    612   -236    379       C
ATOM   2986  O   PRO B  24     -58.675  31.208   5.364  1.00 35.02           O
ANISOU 2986  O   PRO B  24     3163   3579   6565    702    -57    290       O
ATOM   2987  CB  PRO B  24     -57.791  28.915   3.432  1.00 43.37           C
ANISOU 2987  CB  PRO B  24     3690   4950   7839    818   -363    694       C
ATOM   2988  CG  PRO B  24     -57.462  28.167   4.681  1.00 44.58           C
ANISOU 2988  CG  PRO B  24     3696   5124   8118    949   -142    677       C
ATOM   2989  CD  PRO B  24     -56.141  28.711   5.143  1.00 44.47           C
ANISOU 2989  CD  PRO B  24     3586   5237   8075    734   -142    614       C
ATOM   2990  N   VAL B  25     -58.748  32.165   3.322  1.00 30.30           N
ANISOU 2990  N   VAL B  25     2679   3055   5780    525   -335    374       N
ATOM   2991  CA  VAL B  25     -59.652  33.246   3.696  1.00 29.35           C
ANISOU 2991  CA  VAL B  25     2775   2800   5575    496   -252    284       C
ATOM   2992  C   VAL B  25     -60.843  33.256   2.749  1.00 31.96           C
ANISOU 2992  C   VAL B  25     3198   3060   5887    537   -321    401       C
ATOM   2993  O   VAL B  25     -60.687  33.077   1.536  1.00 32.43           O
ANISOU 2993  O   VAL B  25     3224   3223   5876    521   -456    518       O
ATOM   2994  CB  VAL B  25     -58.933  34.613   3.673  1.00 31.13           C
ANISOU 2994  CB  VAL B  25     3101   3083   5646    343   -254    188       C
ATOM   2995  CG1 VAL B  25     -59.917  35.746   3.921  1.00 28.47           C
ANISOU 2995  CG1 VAL B  25     2922   2662   5234    319   -190    156       C
ATOM   2996  CG2 VAL B  25     -57.816  34.642   4.702  1.00 27.93           C
ANISOU 2996  CG2 VAL B  25     2626   2713   5273    292   -174    104       C
ATOM   2997  N   SER B  26     -62.034  33.461   3.308  1.00 33.86           N
ANISOU 2997  N   SER B  26     3566   3123   6176    567   -240    377       N
ATOM   2998  CA  SER B  26     -63.257  33.649   2.539  1.00 32.24           C
ANISOU 2998  CA  SER B  26     3463   2819   5966    559   -287    504       C
ATOM   2999  C   SER B  26     -63.843  35.015   2.861  1.00 30.85           C
ANISOU 2999  C   SER B  26     3408   2614   5699    417   -244    449       C
ATOM   3000  O   SER B  26     -64.008  35.362   4.035  1.00 31.22           O
ANISOU 3000  O   SER B  26     3512   2584   5766    375   -172    316       O
ATOM   3001  CB  SER B  26     -64.283  32.555   2.842  1.00 33.28           C
ANISOU 3001  CB  SER B  26     3640   2721   6283    703   -250    565       C
ATOM   3002  OG  SER B  26     -63.881  31.313   2.298  1.00 46.35           O
ANISOU 3002  OG  SER B  26     5142   4432   8037    867   -302    697       O
ATOM   3003  N   ILE B  27     -64.156  35.784   1.823  1.00 29.32           N
ANISOU 3003  N   ILE B  27     3240   2509   5392    348   -286    570       N
ATOM   3004  CA  ILE B  27     -64.778  37.095   1.962  1.00 25.18           C
ANISOU 3004  CA  ILE B  27     2767   2003   4799    228   -240    586       C
ATOM   3005  C   ILE B  27     -66.217  36.997   1.482  1.00 31.79           C
ANISOU 3005  C   ILE B  27     3658   2711   5711    177   -264    763       C
ATOM   3006  O   ILE B  27     -66.473  36.572   0.348  1.00 35.28           O
ANISOU 3006  O   ILE B  27     4098   3184   6125    224   -308    937       O
ATOM   3007  CB  ILE B  27     -64.014  38.172   1.174  1.00 29.26           C
ANISOU 3007  CB  ILE B  27     3266   2729   5125    209   -217    602       C
ATOM   3008  CG1 ILE B  27     -62.585  38.309   1.701  1.00 35.69           C
ANISOU 3008  CG1 ILE B  27     4060   3609   5891    229   -199    430       C
ATOM   3009  CG2 ILE B  27     -64.746  39.501   1.252  1.00 22.86           C
ANISOU 3009  CG2 ILE B  27     2449   1968   4269    123   -148    678       C
ATOM   3010  CD1 ILE B  27     -62.510  38.697   3.155  1.00 38.60           C
ANISOU 3010  CD1 ILE B  27     4422   3918   6326    191   -137    312       C
ATOM   3011  N   ILE B  28     -67.155  37.390   2.341  1.00 25.36           N
ANISOU 3011  N   ILE B  28     2900   1753   4982     58   -252    734       N
ATOM   3012  CA  ILE B  28     -68.568  37.403   1.986  1.00 36.57           C
ANISOU 3012  CA  ILE B  28     4381   3017   6499    -53   -285    909       C
ATOM   3013  C   ILE B  28     -69.284  38.316   2.971  1.00 34.12           C
ANISOU 3013  C   ILE B  28     4092   2654   6219   -257   -300    854       C
ATOM   3014  O   ILE B  28     -68.944  38.357   4.157  1.00 33.16           O
ANISOU 3014  O   ILE B  28     4012   2498   6089   -272   -300    648       O
ATOM   3015  CB  ILE B  28     -69.159  35.970   1.969  1.00 39.90           C
ANISOU 3015  CB  ILE B  28     4915   3155   7091     50   -316    940       C
ATOM   3016  CG1 ILE B  28     -70.594  35.973   1.437  1.00 38.60           C
ANISOU 3016  CG1 ILE B  28     4835   2806   7026    -77   -353   1156       C
ATOM   3017  CG2 ILE B  28     -69.091  35.330   3.343  1.00 39.69           C
ANISOU 3017  CG2 ILE B  28     4995   2932   7153    102   -286    694       C
ATOM   3018  CD1 ILE B  28     -71.232  34.604   1.403  1.00 47.55           C
ANISOU 3018  CD1 ILE B  28     6109   3715   8242     49   -353   1152       C
ATOM   3019  N  AASN B  29     -70.229  39.105   2.462  0.50 39.86           N
ANISOU 3019  N  AASN B  29     4765   3418   6960   -425   -318   1061       N
ATOM   3020  N  BASN B  29     -70.315  38.993   2.479  0.50 40.33           N
ANISOU 3020  N  BASN B  29     4842   3447   7037   -427   -324   1062       N
ATOM   3021  CA AASN B  29     -71.108  39.935   3.295  0.50 43.39           C
ANISOU 3021  CA AASN B  29     5199   3824   7462   -675   -381   1068       C
ATOM   3022  CA BASN B  29     -70.979  40.113   3.156  0.50 43.15           C
ANISOU 3022  CA BASN B  29     5133   3856   7406   -662   -366   1091       C
ATOM   3023  C  AASN B  29     -70.330  40.847   4.251  0.50 41.40           C
ANISOU 3023  C  AASN B  29     4857   3773   7100   -687   -372    918       C
ATOM   3024  C  BASN B  29     -69.896  41.175   3.352  0.50 41.16           C
ANISOU 3024  C  BASN B  29     4727   3912   7000   -586   -298   1034       C
ATOM   3025  O  AASN B  29     -70.643  40.946   5.439  0.50 40.01           O
ANISOU 3025  O  AASN B  29     4755   3504   6942   -822   -454    775       O
ATOM   3026  O  BASN B  29     -69.070  41.386   2.451  0.50 38.87           O
ANISOU 3026  O  BASN B  29     4371   3806   6594   -423   -206   1087       O
ATOM   3027  CB AASN B  29     -72.092  39.062   4.078  0.50 50.12           C
ANISOU 3027  CB AASN B  29     6275   4324   8444   -783   -466    948       C
ATOM   3028  CB BASN B  29     -71.674  39.639   4.424  0.50 45.86           C
ANISOU 3028  CB BASN B  29     5658   3913   7856   -807   -465    909       C
ATOM   3029  CG AASN B  29     -72.917  38.162   3.183  0.50 55.02           C
ANISOU 3029  CG AASN B  29     7002   4773   9131   -734   -457   1090       C
ATOM   3030  CG BASN B  29     -72.614  38.472   4.174  0.50 53.33           C
ANISOU 3030  CG BASN B  29     6808   4573   8884   -785   -481    909       C
ATOM   3031  OD1AASN B  29     -72.966  36.948   3.381  0.50 57.15           O
ANISOU 3031  OD1AASN B  29     7443   4828   9442   -581   -436    969       O
ATOM   3032  OD1BASN B  29     -73.404  38.485   3.230  0.50 56.27           O
ANISOU 3032  OD1BASN B  29     7156   4928   9295   -849   -484   1135       O
ATOM   3033  ND2AASN B  29     -73.574  38.753   2.192  0.50 58.59           N
ANISOU 3033  ND2AASN B  29     7341   5334   9587   -850   -454   1371       N
ATOM   3034  ND2BASN B  29     -72.523  37.447   5.017  0.50 53.44           N
ANISOU 3034  ND2BASN B  29     7025   4376   8904   -670   -463    666       N
ATOM   3035  N  AASN B  30     -69.306  41.525   3.722  0.50 36.06           N
ANISOU 3035  N  AASN B  30     4045   3363   6294   -542   -276    953       N
ATOM   3036  N  BASN B  30     -69.862  41.856   4.491  0.50 36.88           N
ANISOU 3036  N  BASN B  30     4150   3423   6441   -696   -346    932       N
ATOM   3037  CA AASN B  30     -68.539  42.531   4.470  0.50 33.27           C
ANISOU 3037  CA AASN B  30     3591   3204   5847   -524   -248    876       C
ATOM   3038  CA BASN B  30     -68.723  42.689   4.859  0.50 32.90           C
ANISOU 3038  CA BASN B  30     3539   3150   5812   -584   -279    862       C
ATOM   3039  C  AASN B  30     -67.939  41.962   5.757  0.50 29.19           C
ANISOU 3039  C  AASN B  30     3195   2582   5316   -493   -284    620       C
ATOM   3040  C  BASN B  30     -67.846  41.980   5.877  0.50 29.14           C
ANISOU 3040  C  BASN B  30     3190   2580   5301   -488   -284    601       C
ATOM   3041  O  AASN B  30     -67.749  42.677   6.744  0.50 28.06           O
ANISOU 3041  O  AASN B  30     3010   2534   5119   -559   -318    568       O
ATOM   3042  O  BASN B  30     -67.349  42.610   6.815  0.50 27.78           O
ANISOU 3042  O  BASN B  30     2981   2514   5059   -503   -292    526       O
ATOM   3043  CB AASN B  30     -69.396  43.764   4.775  0.50 37.18           C
ANISOU 3043  CB AASN B  30     3920   3839   6370   -724   -299   1053       C
ATOM   3044  CB BASN B  30     -69.198  44.034   5.401  0.50 37.07           C
ANISOU 3044  CB BASN B  30     3892   3860   6334   -746   -327    992       C
ATOM   3045  CG AASN B  30     -68.650  45.067   4.550  0.50 36.92           C
ANISOU 3045  CG AASN B  30     3692   4099   6238   -601   -186   1158       C
ATOM   3046  CG BASN B  30     -68.730  45.206   4.560  0.50 37.17           C
ANISOU 3046  CG BASN B  30     3698   4151   6272   -616   -188   1183       C
ATOM   3047  OD1AASN B  30     -67.610  45.096   3.891  0.50 34.81           O
ANISOU 3047  OD1AASN B  30     3451   3903   5874   -382    -58   1112       O
ATOM   3048  OD1BASN B  30     -67.686  45.144   3.910  0.50 35.40           O
ANISOU 3048  OD1BASN B  30     3515   3982   5953   -395    -63   1124       O
ATOM   3049  ND2AASN B  30     -69.184  46.155   5.092  0.50 39.95           N
ANISOU 3049  ND2AASN B  30     3885   4645   6650   -743   -240   1306       N
ATOM   3050  ND2BASN B  30     -69.503  46.287   4.573  0.50 40.79           N
ANISOU 3050  ND2BASN B  30     3937   4787   6773   -756   -207   1416       N
ATOM   3051  N   THR B  31     -67.642  40.668   5.740  1.00 29.63           N
ANISOU 3051  N   THR B  31     3382   2463   5411   -379   -269    490       N
ATOM   3052  CA  THR B  31     -67.021  39.924   6.825  1.00 28.05           C
ANISOU 3052  CA  THR B  31     3288   2175   5195   -304   -251    268       C
ATOM   3053  C   THR B  31     -65.871  39.088   6.284  1.00 28.14           C
ANISOU 3053  C   THR B  31     3272   2217   5202   -103   -175    223       C
ATOM   3054  O   THR B  31     -65.930  38.589   5.157  1.00 30.29           O
ANISOU 3054  O   THR B  31     3520   2474   5513    -32   -180    330       O
ATOM   3055  CB  THR B  31     -68.053  39.024   7.527  1.00 30.83           C
ANISOU 3055  CB  THR B  31     3834   2248   5634   -376   -304    158       C
ATOM   3056  OG1 THR B  31     -69.198  39.806   7.892  1.00 33.63           O
ANISOU 3056  OG1 THR B  31     4215   2563   5999   -630   -421    217       O
ATOM   3057  CG2 THR B  31     -67.463  38.396   8.782  1.00 30.68           C
ANISOU 3057  CG2 THR B  31     3931   2174   5551   -288   -247    -73       C
ATOM   3058  N   VAL B  32     -64.819  38.955   7.089  1.00 27.18           N
ANISOU 3058  N   VAL B  32     3144   2157   5026    -32   -121     89       N
ATOM   3059  CA  VAL B  32     -63.663  38.133   6.756  1.00 27.00           C
ANISOU 3059  CA  VAL B  32     3068   2173   5018    110    -69     51       C
ATOM   3060  C   VAL B  32     -63.755  36.833   7.541  1.00 29.11           C
ANISOU 3060  C   VAL B  32     3397   2300   5363    205    -17    -62       C
ATOM   3061  O   VAL B  32     -63.892  36.849   8.771  1.00 26.90           O
ANISOU 3061  O   VAL B  32     3208   1977   5037    181     27   -187       O
ATOM   3062  CB  VAL B  32     -62.346  38.866   7.065  1.00 29.56           C
ANISOU 3062  CB  VAL B  32     3329   2651   5250    117    -23     14       C
ATOM   3063  CG1 VAL B  32     -61.159  38.043   6.589  1.00 30.92           C
ANISOU 3063  CG1 VAL B  32     3433   2864   5452    199     -5     -3       C
ATOM   3064  CG2 VAL B  32     -62.339  40.245   6.429  1.00 27.59           C
ANISOU 3064  CG2 VAL B  32     3044   2516   4923     72    -32    115       C
ATOM   3065  N   TYR B  33     -63.682  35.708   6.834  1.00 28.37           N
ANISOU 3065  N   TYR B  33     3256   2151   5373    331    -16     -6       N
ATOM   3066  CA  TYR B  33     -63.717  34.391   7.448  1.00 24.34           C
ANISOU 3066  CA  TYR B  33     2766   1519   4962    488     70    -77       C
ATOM   3067  C   TYR B  33     -62.422  33.646   7.160  1.00 26.15           C
ANISOU 3067  C   TYR B  33     2798   1904   5233    598    103    -32       C
ATOM   3068  O   TYR B  33     -61.692  33.961   6.217  1.00 24.29           O
ANISOU 3068  O   TYR B  33     2451   1816   4964    542     16     57       O
ATOM   3069  CB  TYR B  33     -64.901  33.559   6.938  1.00 26.28           C
ANISOU 3069  CB  TYR B  33     3105   1536   5344    572     45     -5       C
ATOM   3070  CG  TYR B  33     -66.258  34.151   7.231  1.00 27.10           C
ANISOU 3070  CG  TYR B  33     3412   1446   5437    420     -6    -38       C
ATOM   3071  CD1 TYR B  33     -66.838  35.065   6.364  1.00 31.88           C
ANISOU 3071  CD1 TYR B  33     3999   2090   6023    258   -112    109       C
ATOM   3072  CD2 TYR B  33     -66.967  33.783   8.367  1.00 28.91           C
ANISOU 3072  CD2 TYR B  33     3860   1494   5632    420     51   -208       C
ATOM   3073  CE1 TYR B  33     -68.080  35.605   6.624  1.00 36.42           C
ANISOU 3073  CE1 TYR B  33     4718   2502   6618     74   -176    115       C
ATOM   3074  CE2 TYR B  33     -68.213  34.318   8.635  1.00 49.12           C
ANISOU 3074  CE2 TYR B  33     6615   3876   8172    225    -35   -240       C
ATOM   3075  CZ  TYR B  33     -68.765  35.228   7.759  1.00 43.82           C
ANISOU 3075  CZ  TYR B  33     5873   3241   7537     38   -157    -65       C
ATOM   3076  OH  TYR B  33     -70.006  35.766   8.018  1.00 42.56           O
ANISOU 3076  OH  TYR B  33     5866   2937   7369   -196   -254    -64       O
ATOM   3077  N   THR B  34     -62.148  32.643   7.989  1.00 26.90           N
ANISOU 3077  N   THR B  34     2856   1969   5397    748    233    -94       N
ATOM   3078  CA  THR B  34     -61.047  31.724   7.752  1.00 33.70           C
ANISOU 3078  CA  THR B  34     3476   2982   6347    853    266     -8       C
ATOM   3079  C   THR B  34     -61.493  30.324   8.142  1.00 31.14           C
ANISOU 3079  C   THR B  34     3140   2577   6114   1081    391      6       C
ATOM   3080  O   THR B  34     -62.364  30.148   8.998  1.00 30.84           O
ANISOU 3080  O   THR B  34     3322   2375   6020   1149    497   -121       O
ATOM   3081  CB  THR B  34     -59.780  32.119   8.530  1.00 39.51           C
ANISOU 3081  CB  THR B  34     4120   3889   7005    767    340    -62       C
ATOM   3082  OG1 THR B  34     -58.664  31.363   8.043  1.00 37.26           O
ANISOU 3082  OG1 THR B  34     3567   3770   6819    789    312     62       O
ATOM   3083  CG2 THR B  34     -59.951  31.852  10.019  1.00 42.06           C
ANISOU 3083  CG2 THR B  34     4542   4161   7276    860    541   -192       C
ATOM   3084  N   LYS B  35     -60.900  29.328   7.493  1.00 33.96           N
ANISOU 3084  N   LYS B  35     3261   3074   6571   1184    360    165       N
ATOM   3085  CA  LYS B  35     -61.275  27.939   7.712  1.00 38.10           C
ANISOU 3085  CA  LYS B  35     3752   3570   7154   1419    469    220       C
ATOM   3086  C   LYS B  35     -60.433  27.367   8.846  1.00 43.01           C
ANISOU 3086  C   LYS B  35     4246   4328   7769   1520    671    173       C
ATOM   3087  O   LYS B  35     -59.200  27.364   8.772  1.00 45.55           O
ANISOU 3087  O   LYS B  35     4306   4871   8132   1434    653    262       O
ATOM   3088  CB  LYS B  35     -61.099  27.123   6.431  1.00 45.16           C
ANISOU 3088  CB  LYS B  35     4433   4577   8150   1483    321    449       C
ATOM   3089  CG  LYS B  35     -62.154  26.042   6.247  1.00 53.36           C
ANISOU 3089  CG  LYS B  35     5567   5462   9246   1712    367    516       C
ATOM   3090  CD  LYS B  35     -62.256  25.571   4.800  1.00 59.86           C
ANISOU 3090  CD  LYS B  35     6249   6362  10134   1732    172    754       C
ATOM   3091  CE  LYS B  35     -61.131  24.619   4.430  1.00 67.22           C
ANISOU 3091  CE  LYS B  35     6814   7583  11142   1794    119    931       C
ATOM   3092  NZ  LYS B  35     -61.346  24.007   3.088  1.00 69.43           N
ANISOU 3092  NZ  LYS B  35     6976   7943  11462   1842    -77   1171       N
ATOM   3093  N   VAL B  36     -61.097  26.899   9.894  1.00 48.23           N
ANISOU 3093  N   VAL B  36     5104   4854   8367   1687    858     35       N
ATOM   3094  CA  VAL B  36     -60.437  26.270  11.035  1.00 50.63           C
ANISOU 3094  CA  VAL B  36     5314   5289   8634   1823   1089     -8       C
ATOM   3095  C   VAL B  36     -60.996  24.855  11.129  1.00 59.02           C
ANISOU 3095  C   VAL B  36     6373   6290   9763   2119   1203     29       C
ATOM   3096  O   VAL B  36     -62.052  24.624  11.725  1.00 63.93           O
ANISOU 3096  O   VAL B  36     7298   6673  10319   2255   1294   -137       O
ATOM   3097  CB  VAL B  36     -60.645  27.045  12.337  1.00 45.53           C
ANISOU 3097  CB  VAL B  36     4931   4557   7811   1771   1231   -235       C
ATOM   3098  CG1 VAL B  36     -59.925  26.351  13.481  1.00 47.90           C
ANISOU 3098  CG1 VAL B  36     5127   5027   8047   1922   1490   -252       C
ATOM   3099  CG2 VAL B  36     -60.152  28.470  12.184  1.00 34.75           C
ANISOU 3099  CG2 VAL B  36     3562   3235   6406   1498   1110   -257       C
ATOM   3100  N   ASP B  37     -60.283  23.899  10.530  1.00 63.53           N
ANISOU 3100  N   ASP B  37     6600   7068  10472   2211   1182    247       N
ATOM   3101  CA  ASP B  37     -60.675  22.490  10.531  1.00 68.39           C
ANISOU 3101  CA  ASP B  37     7140   7657  11187   2512   1290    326       C
ATOM   3102  C   ASP B  37     -62.070  22.301   9.936  1.00 63.14           C
ANISOU 3102  C   ASP B  37     6744   6688  10560   2616   1196    294       C
ATOM   3103  O   ASP B  37     -62.962  21.717  10.554  1.00 66.98           O
ANISOU 3103  O   ASP B  37     7463   6947  11038   2831   1336    163       O
ATOM   3104  CB  ASP B  37     -60.592  21.892  11.938  1.00 81.33           C
ANISOU 3104  CB  ASP B  37     8838   9310  12754   2716   1593    193       C
ATOM   3105  CG  ASP B  37     -59.167  21.587  12.359  1.00 92.05           C
ANISOU 3105  CG  ASP B  37     9829  11011  14134   2676   1709    333       C
ATOM   3106  OD1 ASP B  37     -58.399  21.057  11.528  1.00 95.92           O
ANISOU 3106  OD1 ASP B  37     9955  11719  14771   2634   1589    578       O
ATOM   3107  OD2 ASP B  37     -58.813  21.881  13.520  1.00 94.95           O
ANISOU 3107  OD2 ASP B  37    10277  11436  14364   2666   1907    208       O
ATOM   3108  N   GLY B  38     -62.256  22.813   8.719  1.00 58.11           N
ANISOU 3108  N   GLY B  38     6084   6035   9962   2453    954    418       N
ATOM   3109  CA  GLY B  38     -63.432  22.548   7.927  1.00 66.10           C
ANISOU 3109  CA  GLY B  38     7276   6808  11032   2533    845    475       C
ATOM   3110  C   GLY B  38     -64.448  23.675   7.876  1.00 69.11           C
ANISOU 3110  C   GLY B  38     8020   6922  11318   2345    753    329       C
ATOM   3111  O   GLY B  38     -65.082  23.870   6.833  1.00 72.48           O
ANISOU 3111  O   GLY B  38     8507   7251  11784   2277    590    454       O
ATOM   3112  N   VAL B  39     -64.626  24.415   8.968  1.00 49.82           N
ANISOU 3112  N   VAL B  39     5586   6061   7282   1355    524    700       N
ATOM   3113  CA  VAL B  39     -65.690  25.409   9.063  1.00 41.25           C
ANISOU 3113  CA  VAL B  39     4681   4868   6125   1299    459    602       C
ATOM   3114  C   VAL B  39     -65.094  26.809   9.040  1.00 35.28           C
ANISOU 3114  C   VAL B  39     3899   4116   5391   1144    418    558       C
ATOM   3115  O   VAL B  39     -63.940  27.029   9.424  1.00 31.98           O
ANISOU 3115  O   VAL B  39     3374   3760   5017   1112    464    591       O
ATOM   3116  CB  VAL B  39     -66.549  25.204  10.328  1.00 41.56           C
ANISOU 3116  CB  VAL B  39     4908   4818   6065   1435    515    570       C
ATOM   3117  CG1 VAL B  39     -67.329  23.902  10.232  1.00 46.22           C
ANISOU 3117  CG1 VAL B  39     5555   5380   6625   1590    540    601       C
ATOM   3118  CG2 VAL B  39     -65.675  25.219  11.571  1.00 38.45           C
ANISOU 3118  CG2 VAL B  39     4491   4466   5654   1500    625    602       C
ATOM   3119  N   ASP B  40     -65.904  27.763   8.585  1.00 34.60           N
ANISOU 3119  N   ASP B  40     3909   3960   5278   1052    333    490       N
ATOM   3120  CA  ASP B  40     -65.492  29.157   8.529  1.00 34.39           C
ANISOU 3120  CA  ASP B  40     3872   3928   5266    916    294    446       C
ATOM   3121  C   ASP B  40     -65.722  29.823   9.880  1.00 34.80           C
ANISOU 3121  C   ASP B  40     4043   3917   5262    940    328    409       C
ATOM   3122  O   ASP B  40     -66.799  29.695  10.471  1.00 33.00           O
ANISOU 3122  O   ASP B  40     3968   3602   4968   1008    317    379       O
ATOM   3123  CB  ASP B  40     -66.264  29.898   7.438  1.00 36.45           C
ANISOU 3123  CB  ASP B  40     4172   4151   5528    817    200    408       C
ATOM   3124  CG  ASP B  40     -66.017  29.325   6.059  1.00 44.56           C
ANISOU 3124  CG  ASP B  40     5096   5241   6595    792    158    441       C
ATOM   3125  OD1 ASP B  40     -64.879  28.882   5.795  1.00 48.39           O
ANISOU 3125  OD1 ASP B  40     5446   5807   7131    784    176    480       O
ATOM   3126  OD2 ASP B  40     -66.959  29.314   5.239  1.00 49.33           O
ANISOU 3126  OD2 ASP B  40     5753   5810   7180    777    102    434       O
ATOM   3127  N   VAL B  41     -64.705  30.527  10.367  1.00 31.48           N
ANISOU 3127  N   VAL B  41     3560   3534   4868    884    359    412       N
ATOM   3128  CA  VAL B  41     -64.780  31.276  11.614  1.00 28.86           C
ANISOU 3128  CA  VAL B  41     3330   3151   4483    895    385    381       C
ATOM   3129  C   VAL B  41     -64.618  32.751  11.283  1.00 29.02           C
ANISOU 3129  C   VAL B  41     3340   3154   4531    751    320    338       C
ATOM   3130  O   VAL B  41     -63.674  33.133  10.582  1.00 25.63           O
ANISOU 3130  O   VAL B  41     2787   2785   4168    665    310    352       O
ATOM   3131  CB  VAL B  41     -63.708  30.819  12.621  1.00 29.92           C
ANISOU 3131  CB  VAL B  41     3403   3345   4619    971    493    436       C
ATOM   3132  CG1 VAL B  41     -63.873  31.550  13.944  1.00 25.58           C
ANISOU 3132  CG1 VAL B  41     2983   2738   3996    997    517    403       C
ATOM   3133  CG2 VAL B  41     -63.782  29.317  12.824  1.00 26.71           C
ANISOU 3133  CG2 VAL B  41     2980   2973   4197   1123    571    495       C
ATOM   3134  N   GLU B  42     -65.542  33.573  11.776  1.00 35.18           N
ANISOU 3134  N   GLU B  42     4254   3848   5264    728    270    291       N
ATOM   3135  CA  GLU B  42     -65.483  35.005  11.519  1.00 32.61           C
ANISOU 3135  CA  GLU B  42     3918   3504   4967    604    214    260       C
ATOM   3136  C   GLU B  42     -64.299  35.629  12.245  1.00 35.54           C
ANISOU 3136  C   GLU B  42     4234   3912   5356    577    263    269       C
ATOM   3137  O   GLU B  42     -64.124  35.437  13.451  1.00 36.65           O
ANISOU 3137  O   GLU B  42     4436   4040   5450    650    315    277       O
ATOM   3138  CB  GLU B  42     -66.780  35.681  11.959  1.00 34.66           C
ANISOU 3138  CB  GLU B  42     4325   3661   5185    587    141    223       C
ATOM   3139  CG  GLU B  42     -66.658  37.190  12.105  1.00 42.25           C
ANISOU 3139  CG  GLU B  42     5280   4602   6170    482     99    204       C
ATOM   3140  CD  GLU B  42     -67.910  37.830  12.668  1.00 50.29           C
ANISOU 3140  CD  GLU B  42     6434   5516   7157    462     16    181       C
ATOM   3141  OE1 GLU B  42     -69.021  37.379  12.319  1.00 53.95           O
ANISOU 3141  OE1 GLU B  42     6968   5922   7610    478    -38    180       O
ATOM   3142  OE2 GLU B  42     -67.780  38.782  13.467  1.00 52.87           O
ANISOU 3142  OE2 GLU B  42     6797   5814   7476    427     -5    168       O
ATOM   3143  N   LEU B  43     -63.485  36.381  11.506  1.00 35.33           N
ANISOU 3143  N   LEU B  43     4103   3929   5392    478    246    269       N
ATOM   3144  CA  LEU B  43     -62.356  37.097  12.080  1.00 36.03           C
ANISOU 3144  CA  LEU B  43     4138   4041   5509    437    280    278       C
ATOM   3145  C   LEU B  43     -62.587  38.591  12.216  1.00 37.30           C
ANISOU 3145  C   LEU B  43     4343   4156   5672    355    231    242       C
ATOM   3146  O   LEU B  43     -62.010  39.211  13.111  1.00 39.58           O
ANISOU 3146  O   LEU B  43     4642   4438   5958    346    256    246       O
ATOM   3147  CB  LEU B  43     -61.096  36.878  11.234  1.00 37.39           C
ANISOU 3147  CB  LEU B  43     4164   4285   5757    386    291    305       C
ATOM   3148  CG  LEU B  43     -60.561  35.452  11.120  1.00 37.84           C
ANISOU 3148  CG  LEU B  43     4135   4402   5840    454    339    363       C
ATOM   3149  CD1 LEU B  43     -59.284  35.444  10.297  1.00 36.60           C
ANISOU 3149  CD1 LEU B  43     3837   4299   5768    378    319    388       C
ATOM   3150  CD2 LEU B  43     -60.323  34.860  12.499  1.00 39.54           C
ANISOU 3150  CD2 LEU B  43     4376   4626   6022    553    430    408       C
ATOM   3151  N   PHE B  44     -63.421  39.181  11.362  1.00 31.69           N
ANISOU 3151  N   PHE B  44     3654   3418   4969    301    166    218       N
ATOM   3152  CA  PHE B  44     -63.556  40.629  11.321  1.00 28.85           C
ANISOU 3152  CA  PHE B  44     3305   3029   4628    223    126    200       C
ATOM   3153  C   PHE B  44     -64.840  40.991  10.592  1.00 27.70           C
ANISOU 3153  C   PHE B  44     3201   2845   4480    192     63    194       C
ATOM   3154  O   PHE B  44     -65.060  40.543   9.463  1.00 24.69           O
ANISOU 3154  O   PHE B  44     2780   2491   4109    187     54    201       O
ATOM   3155  CB  PHE B  44     -62.345  41.258  10.626  1.00 27.93           C
ANISOU 3155  CB  PHE B  44     3086   2960   4565    161    140    197       C
ATOM   3156  CG  PHE B  44     -62.454  42.742  10.425  1.00 25.34           C
ANISOU 3156  CG  PHE B  44     2761   2609   4260     95    109    183       C
ATOM   3157  CD1 PHE B  44     -62.216  43.616  11.472  1.00 20.29           C
ANISOU 3157  CD1 PHE B  44     2151   1939   3621     82    113    184       C
ATOM   3158  CD2 PHE B  44     -62.771  43.265   9.182  1.00 25.96           C
ANISOU 3158  CD2 PHE B  44     2810   2700   4354     56     82    177       C
ATOM   3159  CE1 PHE B  44     -62.306  44.982  11.287  1.00 20.12           C
ANISOU 3159  CE1 PHE B  44     2120   1898   3626     29     87    180       C
ATOM   3160  CE2 PHE B  44     -62.861  44.630   8.991  1.00 25.70           C
ANISOU 3160  CE2 PHE B  44     2771   2651   4342     10     68    176       C
ATOM   3161  CZ  PHE B  44     -62.629  45.489  10.045  1.00 22.58           C
ANISOU 3161  CZ  PHE B  44     2396   2224   3958     -4     69    178       C
ATOM   3162  N   GLU B  45     -65.679  41.793  11.240  1.00 24.46           N
ANISOU 3162  N   GLU B  45     2866   2370   4059    170     16    192       N
ATOM   3163  CA  GLU B  45     -66.878  42.349  10.627  1.00 28.45           C
ANISOU 3163  CA  GLU B  45     3393   2833   4582    123    -49    206       C
ATOM   3164  C   GLU B  45     -66.615  43.816  10.322  1.00 30.55           C
ANISOU 3164  C   GLU B  45     3601   3112   4895     51    -58    217       C
ATOM   3165  O   GLU B  45     -66.424  44.620  11.241  1.00 32.10           O
ANISOU 3165  O   GLU B  45     3820   3281   5097     33    -71    215       O
ATOM   3166  CB  GLU B  45     -68.092  42.193  11.541  1.00 31.57           C
ANISOU 3166  CB  GLU B  45     3913   3137   4946    143   -115    205       C
ATOM   3167  CG  GLU B  45     -69.374  42.765  10.956  1.00 43.41           C
ANISOU 3167  CG  GLU B  45     5427   4585   6483     83   -193    238       C
ATOM   3168  CD  GLU B  45     -70.524  42.752  11.943  1.00 55.28           C
ANISOU 3168  CD  GLU B  45     7062   5978   7965     86   -285    236       C
ATOM   3169  OE1 GLU B  45     -70.354  42.197  13.049  1.00 60.42           O
ANISOU 3169  OE1 GLU B  45     7810   6595   8553    153   -281    200       O
ATOM   3170  OE2 GLU B  45     -71.598  43.300  11.613  1.00 59.38           O
ANISOU 3170  OE2 GLU B  45     7590   6442   8530     24   -364    274       O
ATOM   3171  N   ASN B  46     -66.603  44.161   9.037  1.00 28.67           N
ANISOU 3171  N   ASN B  46     3293   2915   4684     19    -48    232       N
ATOM   3172  CA  ASN B  46     -66.257  45.513   8.612  1.00 25.72           C
ANISOU 3172  CA  ASN B  46     2861   2562   4349    -29    -39    245       C
ATOM   3173  C   ASN B  46     -67.367  46.478   9.010  1.00 28.74           C
ANISOU 3173  C   ASN B  46     3266   2889   4763    -71    -95    287       C
ATOM   3174  O   ASN B  46     -68.465  46.442   8.448  1.00 32.16           O
ANISOU 3174  O   ASN B  46     3705   3302   5213    -89   -131    328       O
ATOM   3175  CB  ASN B  46     -66.016  45.548   7.106  1.00 23.27           C
ANISOU 3175  CB  ASN B  46     2490   2310   4041    -32    -10    251       C
ATOM   3176  CG  ASN B  46     -65.626  46.925   6.612  1.00 22.38           C
ANISOU 3176  CG  ASN B  46     2327   2219   3955    -60     13    263       C
ATOM   3177  OD1 ASN B  46     -65.157  47.762   7.383  1.00 28.50           O
ANISOU 3177  OD1 ASN B  46     3098   2977   4754    -75     16    258       O
ATOM   3178  ND2 ASN B  46     -65.821  47.170   5.322  1.00 23.01           N
ANISOU 3178  ND2 ASN B  46     2376   2338   4027    -55     33    283       N
ATOM   3179  N   LYS B  47     -67.081  47.341   9.981  1.00 29.76           N
ANISOU 3179  N   LYS B  47     3405   2992   4909    -90   -110    286       N
ATOM   3180  CA  LYS B  47     -67.996  48.398  10.383  1.00 25.26           C
ANISOU 3180  CA  LYS B  47     2840   2373   4384   -139   -174    335       C
ATOM   3181  C   LYS B  47     -67.619  49.746   9.785  1.00 29.23           C
ANISOU 3181  C   LYS B  47     3251   2915   4938   -167   -140    370       C
ATOM   3182  O   LYS B  47     -68.207  50.765  10.158  1.00 31.59           O
ANISOU 3182  O   LYS B  47     3531   3184   5288   -207   -187    421       O
ATOM   3183  CB  LYS B  47     -68.049  48.501  11.910  1.00 26.43           C
ANISOU 3183  CB  LYS B  47     3070   2459   4512   -136   -228    317       C
ATOM   3184  CG  LYS B  47     -68.468  47.220  12.606  1.00 35.01           C
ANISOU 3184  CG  LYS B  47     4268   3499   5534    -88   -256    282       C
ATOM   3185  CD  LYS B  47     -69.855  46.793  12.158  1.00 47.91           C
ANISOU 3185  CD  LYS B  47     5942   5080   7182   -107   -326    312       C
ATOM   3186  CE  LYS B  47     -70.892  47.846  12.514  1.00 59.97           C
ANISOU 3186  CE  LYS B  47     7478   6539   8768   -178   -430    366       C
ATOM   3187  NZ  LYS B  47     -72.159  47.662  11.753  1.00 65.66           N
ANISOU 3187  NZ  LYS B  47     8193   7221   9533   -218   -488    420       N
ATOM   3188  N   THR B  48     -66.659  49.774   8.867  1.00 30.60           N
ANISOU 3188  N   THR B  48     3373   3153   5100   -144    -66    346       N
ATOM   3189  CA  THR B  48     -66.153  51.009   8.289  1.00 27.08           C
ANISOU 3189  CA  THR B  48     2858   2743   4688   -148    -23    367       C
ATOM   3190  C   THR B  48     -66.753  51.243   6.906  1.00 28.67           C
ANISOU 3190  C   THR B  48     3012   2984   4897   -142      8    415       C
ATOM   3191  O   THR B  48     -67.477  50.409   6.358  1.00 32.70           O
ANISOU 3191  O   THR B  48     3539   3497   5388   -139     -6    429       O
ATOM   3192  CB  THR B  48     -64.624  50.972   8.195  1.00 30.51           C
ANISOU 3192  CB  THR B  48     3285   3208   5098   -121     31    306       C
ATOM   3193  OG1 THR B  48     -64.237  50.326   6.976  1.00 28.81           O
ANISOU 3193  OG1 THR B  48     3060   3039   4849    -95     67    278       O
ATOM   3194  CG2 THR B  48     -64.039  50.202   9.368  1.00 29.54           C
ANISOU 3194  CG2 THR B  48     3213   3060   4953   -115     17    264       C
ATOM   3195  N   THR B  49     -66.437  52.407   6.344  1.00 32.79           N
ANISOU 3195  N   THR B  49     3477   3538   5442   -130     56    445       N
ATOM   3196  CA  THR B  49     -66.837  52.756   4.988  1.00 31.50           C
ANISOU 3196  CA  THR B  49     3270   3425   5272   -103    108    494       C
ATOM   3197  C   THR B  49     -65.799  52.355   3.949  1.00 28.98           C
ANISOU 3197  C   THR B  49     2974   3154   4885    -51    164    427       C
ATOM   3198  O   THR B  49     -65.963  52.681   2.769  1.00 24.53           O
ANISOU 3198  O   THR B  49     2392   2636   4294    -12    216    458       O
ATOM   3199  CB  THR B  49     -67.108  54.262   4.885  1.00 35.41           C
ANISOU 3199  CB  THR B  49     3694   3934   5827   -100    139    574       C
ATOM   3200  OG1 THR B  49     -65.901  54.987   5.145  1.00 40.47           O
ANISOU 3200  OG1 THR B  49     4335   4579   6463    -71    176    525       O
ATOM   3201  CG2 THR B  49     -68.168  54.679   5.891  1.00 37.84           C
ANISOU 3201  CG2 THR B  49     3974   4189   6213   -163     61    649       C
ATOM   3202  N   LEU B  50     -64.743  51.668   4.359  1.00 24.24           N
ANISOU 3202  N   LEU B  50     2413   2542   4256    -49    151    344       N
ATOM   3203  CA  LEU B  50     -63.699  51.173   3.478  1.00 26.72           C
ANISOU 3203  CA  LEU B  50     2752   2887   4514    -14    175    278       C
ATOM   3204  C   LEU B  50     -64.042  49.777   2.983  1.00 27.25           C
ANISOU 3204  C   LEU B  50     2842   2970   4541    -11    149    264       C
ATOM   3205  O   LEU B  50     -64.909  49.101   3.547  1.00 28.99           O
ANISOU 3205  O   LEU B  50     3069   3167   4777    -33    115    291       O
ATOM   3206  CB  LEU B  50     -62.364  51.151   4.218  1.00 28.25           C
ANISOU 3206  CB  LEU B  50     2961   3055   4718    -24    165    213       C
ATOM   3207  CG  LEU B  50     -61.820  52.495   4.701  1.00 30.86           C
ANISOU 3207  CG  LEU B  50     3276   3365   5086    -21    189    218       C
ATOM   3208  CD1 LEU B  50     -60.633  52.282   5.622  1.00 33.70           C
ANISOU 3208  CD1 LEU B  50     3651   3691   5464    -41    171    168       C
ATOM   3209  CD2 LEU B  50     -61.430  53.368   3.521  1.00 31.34           C
ANISOU 3209  CD2 LEU B  50     3340   3451   5117     32    239    211       C
ATOM   3210  N   PRO B  51     -63.394  49.319   1.910  1.00 20.94           N
ANISOU 3210  N   PRO B  51     2063   2206   3688     20    159    222       N
ATOM   3211  CA  PRO B  51     -63.557  47.920   1.502  1.00 19.87           C
ANISOU 3211  CA  PRO B  51     1944   2087   3520     24    127    208       C
ATOM   3212  C   PRO B  51     -63.177  46.972   2.630  1.00 26.57           C
ANISOU 3212  C   PRO B  51     2792   2907   4396      0     93    181       C
ATOM   3213  O   PRO B  51     -62.361  47.294   3.496  1.00 26.51           O
ANISOU 3213  O   PRO B  51     2778   2876   4419    -18     94    155       O
ATOM   3214  CB  PRO B  51     -62.608  47.786   0.307  1.00 23.48           C
ANISOU 3214  CB  PRO B  51     2426   2576   3918     57    128    157       C
ATOM   3215  CG  PRO B  51     -62.552  49.160  -0.263  1.00 20.62           C
ANISOU 3215  CG  PRO B  51     2072   2225   3537     90    178    170       C
ATOM   3216  CD  PRO B  51     -62.634  50.096   0.915  1.00 20.29           C
ANISOU 3216  CD  PRO B  51     1996   2147   3564     62    195    194       C
ATOM   3217  N   VAL B  52     -63.786  45.784   2.606  1.00 32.06           N
ANISOU 3217  N   VAL B  52     3497   3607   5079      7     69    195       N
ATOM   3218  CA  VAL B  52     -63.693  44.870   3.743  1.00 34.89           C
ANISOU 3218  CA  VAL B  52     3861   3939   5458      3     52    186       C
ATOM   3219  C   VAL B  52     -62.249  44.433   3.973  1.00 28.05           C
ANISOU 3219  C   VAL B  52     2970   3086   4602      0     51    143       C
ATOM   3220  O   VAL B  52     -61.758  44.432   5.108  1.00 33.01           O
ANISOU 3220  O   VAL B  52     3593   3692   5259     -8     60    138       O
ATOM   3221  CB  VAL B  52     -64.634  43.666   3.538  1.00 37.26           C
ANISOU 3221  CB  VAL B  52     4180   4238   5737     27     31    211       C
ATOM   3222  CG1 VAL B  52     -64.450  43.058   2.152  1.00 29.91           C
ANISOU 3222  CG1 VAL B  52     3239   3357   4769     48     22    206       C
ATOM   3223  CG2 VAL B  52     -64.418  42.623   4.624  1.00 19.44           C
ANISOU 3223  CG2 VAL B  52     1935   1962   3488     47     26    200       C
ATOM   3224  N   ASN B  53     -61.543  44.067   2.901  1.00 25.30           N
ANISOU 3224  N   ASN B  53     2607   2772   4233      6     35    118       N
ATOM   3225  CA  ASN B  53     -60.168  43.598   3.055  1.00 21.77           C
ANISOU 3225  CA  ASN B  53     2129   2331   3813     -9     17     89       C
ATOM   3226  C   ASN B  53     -59.230  44.727   3.459  1.00 24.78           C
ANISOU 3226  C   ASN B  53     2508   2684   4222    -37     28     64       C
ATOM   3227  O   ASN B  53     -58.223  44.484   4.135  1.00 27.78           O
ANISOU 3227  O   ASN B  53     2859   3052   4646    -59     23     58       O
ATOM   3228  CB  ASN B  53     -59.683  42.951   1.759  1.00 22.09           C
ANISOU 3228  CB  ASN B  53     2164   2406   3825     -3    -28     69       C
ATOM   3229  CG  ASN B  53     -59.703  43.910   0.588  1.00 22.42           C
ANISOU 3229  CG  ASN B  53     2250   2454   3815      8    -31     42       C
ATOM   3230  OD1 ASN B  53     -60.690  44.607   0.360  1.00 27.03           O
ANISOU 3230  OD1 ASN B  53     2859   3040   4371     28      5     67       O
ATOM   3231  ND2 ASN B  53     -58.605  43.958  -0.156  1.00 23.67           N
ANISOU 3231  ND2 ASN B  53     2421   2612   3960     -1    -77     -2       N
ATOM   3232  N   VAL B  54     -59.537  45.959   3.055  1.00 23.09           N
ANISOU 3232  N   VAL B  54     2323   2460   3989    -31     47     57       N
ATOM   3233  CA  VAL B  54     -58.696  47.093   3.422  1.00 23.84           C
ANISOU 3233  CA  VAL B  54     2423   2524   4112    -47     60     35       C
ATOM   3234  C   VAL B  54     -58.846  47.406   4.905  1.00 27.51           C
ANISOU 3234  C   VAL B  54     2875   2959   4620    -64     83     62       C
ATOM   3235  O   VAL B  54     -57.855  47.500   5.640  1.00 25.36           O
ANISOU 3235  O   VAL B  54     2587   2663   4385    -85     82     53       O
ATOM   3236  CB  VAL B  54     -59.036  48.313   2.549  1.00 22.52           C
ANISOU 3236  CB  VAL B  54     2287   2360   3910    -18     86     30       C
ATOM   3237  CG1 VAL B  54     -58.243  49.519   3.003  1.00 24.62           C
ANISOU 3237  CG1 VAL B  54     2560   2588   4207    -24    104     13       C
ATOM   3238  CG2 VAL B  54     -58.762  48.008   1.085  1.00 20.38           C
ANISOU 3238  CG2 VAL B  54     2050   2116   3577     10     62     -3       C
ATOM   3239  N   ALA B  55     -60.088  47.575   5.366  1.00 25.51           N
ANISOU 3239  N   ALA B  55     2631   2701   4359    -56     95    100       N
ATOM   3240  CA  ALA B  55     -60.326  47.841   6.780  1.00 23.07           C
ANISOU 3240  CA  ALA B  55     2329   2360   4077    -67    101    123       C
ATOM   3241  C   ALA B  55     -59.817  46.703   7.653  1.00 24.82           C
ANISOU 3241  C   ALA B  55     2545   2581   4305    -62    102    123       C
ATOM   3242  O   ALA B  55     -59.347  46.939   8.772  1.00 26.42           O
ANISOU 3242  O   ALA B  55     2752   2761   4527    -68    115    131       O
ATOM   3243  CB  ALA B  55     -61.816  48.078   7.026  1.00 23.25           C
ANISOU 3243  CB  ALA B  55     2372   2368   4092    -64     90    163       C
ATOM   3244  N   PHE B  56     -59.903  45.467   7.159  1.00 24.66           N
ANISOU 3244  N   PHE B  56     2514   2590   4268    -45     93    122       N
ATOM   3245  CA  PHE B  56     -59.363  44.333   7.898  1.00 22.73           C
ANISOU 3245  CA  PHE B  56     2248   2355   4033    -28    107    135       C
ATOM   3246  C   PHE B  56     -57.862  44.480   8.103  1.00 24.26           C
ANISOU 3246  C   PHE B  56     2396   2550   4274    -57    113    131       C
ATOM   3247  O   PHE B  56     -57.348  44.220   9.197  1.00 26.35           O
ANISOU 3247  O   PHE B  56     2646   2807   4557    -50    142    157       O
ATOM   3248  CB  PHE B  56     -59.687  43.036   7.158  1.00 25.43           C
ANISOU 3248  CB  PHE B  56     2573   2732   4356     -1     93    142       C
ATOM   3249  CG  PHE B  56     -59.013  41.824   7.730  1.00 26.90           C
ANISOU 3249  CG  PHE B  56     2715   2941   4564     23    113    169       C
ATOM   3250  CD1 PHE B  56     -59.299  41.397   9.015  1.00 26.43           C
ANISOU 3250  CD1 PHE B  56     2682   2869   4491     67    154    196       C
ATOM   3251  CD2 PHE B  56     -58.106  41.099   6.975  1.00 28.69           C
ANISOU 3251  CD2 PHE B  56     2875   3204   4824      9     90    174       C
ATOM   3252  CE1 PHE B  56     -58.686  40.275   9.543  1.00 21.93           C
ANISOU 3252  CE1 PHE B  56     2064   2329   3939    104    190    236       C
ATOM   3253  CE2 PHE B  56     -57.489  39.976   7.495  1.00 26.64           C
ANISOU 3253  CE2 PHE B  56     2553   2971   4597     32    114    218       C
ATOM   3254  CZ  PHE B  56     -57.779  39.563   8.782  1.00 21.66           C
ANISOU 3254  CZ  PHE B  56     1940   2336   3953     85    174    254       C
ATOM   3255  N   GLU B  57     -57.146  44.912   7.063  1.00 27.93           N
ANISOU 3255  N   GLU B  57     2844   3016   4753    -86     84    100       N
ATOM   3256  CA  GLU B  57     -55.705  45.102   7.181  1.00 23.10           C
ANISOU 3256  CA  GLU B  57     2196   2387   4193   -124     72     94       C
ATOM   3257  C   GLU B  57     -55.374  46.240   8.136  1.00 24.06           C
ANISOU 3257  C   GLU B  57     2336   2468   4337   -137     98    100       C
ATOM   3258  O   GLU B  57     -54.445  46.128   8.944  1.00 28.44           O
ANISOU 3258  O   GLU B  57     2860   3009   4937   -156    112    126       O
ATOM   3259  CB  GLU B  57     -55.102  45.359   5.801  1.00 26.14           C
ANISOU 3259  CB  GLU B  57     2589   2769   4576   -145     19     49       C
ATOM   3260  CG  GLU B  57     -53.617  45.683   5.820  1.00 32.57           C
ANISOU 3260  CG  GLU B  57     3383   3544   5449   -192    -15     36       C
ATOM   3261  CD  GLU B  57     -53.027  45.780   4.426  1.00 41.15           C
ANISOU 3261  CD  GLU B  57     4498   4617   6520   -207    -87    -17       C
ATOM   3262  OE1 GLU B  57     -53.732  45.429   3.457  1.00 46.67           O
ANISOU 3262  OE1 GLU B  57     5223   5350   7161   -178   -104    -36       O
ATOM   3263  OE2 GLU B  57     -51.860  46.206   4.298  1.00 45.65           O
ANISOU 3263  OE2 GLU B  57     5074   5137   7132   -246   -131    -40       O
ATOM   3264  N   LEU B  58     -56.124  47.342   8.063  1.00 23.47           N
ANISOU 3264  N   LEU B  58     2305   2377   4236   -126    107     86       N
ATOM   3265  CA  LEU B  58     -55.864  48.471   8.950  1.00 23.79           C
ANISOU 3265  CA  LEU B  58     2361   2380   4298   -135    126     96       C
ATOM   3266  C   LEU B  58     -56.142  48.108  10.401  1.00 21.37           C
ANISOU 3266  C   LEU B  58     2062   2070   3988   -122    152    137       C
ATOM   3267  O   LEU B  58     -55.378  48.485  11.298  1.00 22.15           O
ANISOU 3267  O   LEU B  58     2155   2145   4115   -133    169    157       O
ATOM   3268  CB  LEU B  58     -56.706  49.673   8.529  1.00 25.78           C
ANISOU 3268  CB  LEU B  58     2642   2622   4530   -121    128     88       C
ATOM   3269  CG  LEU B  58     -56.431  50.200   7.123  1.00 28.28           C
ANISOU 3269  CG  LEU B  58     2969   2943   4833   -112    118     50       C
ATOM   3270  CD1 LEU B  58     -57.280  51.423   6.834  1.00 30.16           C
ANISOU 3270  CD1 LEU B  58     3220   3180   5058    -87    140     65       C
ATOM   3271  CD2 LEU B  58     -54.958  50.519   6.966  1.00 31.96           C
ANISOU 3271  CD2 LEU B  58     3437   3373   5334   -133    101     18       C
ATOM   3272  N   TRP B  59     -57.231  47.383  10.652  1.00 18.99           N
ANISOU 3272  N   TRP B  59     1784   1786   3646    -92    155    150       N
ATOM   3273  CA  TRP B  59     -57.533  46.963  12.014  1.00 27.29           C
ANISOU 3273  CA  TRP B  59     2867   2828   4673    -62    177    181       C
ATOM   3274  C   TRP B  59     -56.462  46.023  12.549  1.00 28.63           C
ANISOU 3274  C   TRP B  59     2993   3019   4864    -52    215    212       C
ATOM   3275  O   TRP B  59     -56.075  46.111  13.719  1.00 28.10           O
ANISOU 3275  O   TRP B  59     2941   2940   4794    -36    248    245       O
ATOM   3276  CB  TRP B  59     -58.907  46.299  12.064  1.00 24.15           C
ANISOU 3276  CB  TRP B  59     2517   2433   4224    -26    163    182       C
ATOM   3277  CG  TRP B  59     -59.201  45.658  13.375  1.00 24.75           C
ANISOU 3277  CG  TRP B  59     2648   2497   4257     23    185    205       C
ATOM   3278  CD1 TRP B  59     -59.551  46.284  14.535  1.00 24.03           C
ANISOU 3278  CD1 TRP B  59     2623   2368   4138     35    175    215       C
ATOM   3279  CD2 TRP B  59     -59.172  44.258  13.666  1.00 26.34           C
ANISOU 3279  CD2 TRP B  59     2850   2725   4431     79    221    223       C
ATOM   3280  NE1 TRP B  59     -59.742  45.360  15.533  1.00 28.35           N
ANISOU 3280  NE1 TRP B  59     3229   2915   4629    100    204    232       N
ATOM   3281  CE2 TRP B  59     -59.515  44.108  15.024  1.00 28.36           C
ANISOU 3281  CE2 TRP B  59     3188   2957   4632    133    240    240       C
ATOM   3282  CE3 TRP B  59     -58.888  43.117  12.911  1.00 24.42           C
ANISOU 3282  CE3 TRP B  59     2550   2526   4204     96    237    231       C
ATOM   3283  CZ2 TRP B  59     -59.583  42.863  15.642  1.00 29.90           C
ANISOU 3283  CZ2 TRP B  59     3410   3170   4780    214    290    264       C
ATOM   3284  CZ3 TRP B  59     -58.956  41.883  13.525  1.00 29.04           C
ANISOU 3284  CZ3 TRP B  59     3145   3132   4757    169    283    262       C
ATOM   3285  CH2 TRP B  59     -59.300  41.764  14.877  1.00 34.10           C
ANISOU 3285  CH2 TRP B  59     3871   3748   5337    233    316    278       C
ATOM   3286  N   ALA B  60     -55.964  45.118  11.703  1.00 27.20           N
ANISOU 3286  N   ALA B  60     2755   2871   4709    -60    210    212       N
ATOM   3287  CA  ALA B  60     -54.901  44.218  12.136  1.00 25.18           C
ANISOU 3287  CA  ALA B  60     2433   2639   4495    -58    242    260       C
ATOM   3288  C   ALA B  60     -53.621  44.976  12.452  1.00 24.98           C
ANISOU 3288  C   ALA B  60     2374   2584   4531   -108    244    276       C
ATOM   3289  O   ALA B  60     -52.846  44.554  13.317  1.00 24.03           O
ANISOU 3289  O   ALA B  60     2214   2474   4443   -102    287    337       O
ATOM   3290  CB  ALA B  60     -54.640  43.160  11.065  1.00 25.75           C
ANISOU 3290  CB  ALA B  60     2442   2749   4594    -66    216    261       C
ATOM   3291  N   LYS B  61     -53.385  46.094  11.769  1.00 28.95           N
ANISOU 3291  N   LYS B  61     2896   3051   5053   -150    201    230       N
ATOM   3292  CA  LYS B  61     -52.195  46.904  11.975  1.00 26.09           C
ANISOU 3292  CA  LYS B  61     2516   2647   4751   -196    192    237       C
ATOM   3293  C   LYS B  61     -52.439  48.066  12.929  1.00 27.73           C
ANISOU 3293  C   LYS B  61     2776   2820   4939   -184    215    243       C
ATOM   3294  O   LYS B  61     -51.634  49.001  12.975  1.00 27.32           O
ANISOU 3294  O   LYS B  61     2726   2724   4929   -215    203    239       O
ATOM   3295  CB  LYS B  61     -51.675  47.420  10.634  1.00 23.07           C
ANISOU 3295  CB  LYS B  61     2135   2236   4394   -236    130    180       C
ATOM   3296  CG  LYS B  61     -51.285  46.315   9.668  1.00 22.11           C
ANISOU 3296  CG  LYS B  61     1964   2141   4297   -258     86    176       C
ATOM   3297  CD  LYS B  61     -50.774  46.882   8.357  1.00 24.31           C
ANISOU 3297  CD  LYS B  61     2273   2383   4582   -289     14    110       C
ATOM   3298  CE  LYS B  61     -50.230  45.784   7.455  1.00 25.48           C
ANISOU 3298  CE  LYS B  61     2373   2549   4760   -320    -51    110       C
ATOM   3299  NZ  LYS B  61     -49.638  46.343   6.208  1.00 28.33           N
ANISOU 3299  NZ  LYS B  61     2787   2862   5116   -346   -134     39       N
ATOM   3300  N   ARG B  62     -53.531  48.026  13.689  1.00 20.01           N
ANISOU 3300  N   ARG B  62     1847   1856   3899   -138    239    253       N
ATOM   3301  CA  ARG B  62     -53.827  49.087  14.638  1.00 24.31           C
ANISOU 3301  CA  ARG B  62     2444   2369   4424   -127    245    264       C
ATOM   3302  C   ARG B  62     -52.751  49.156  15.718  1.00 26.66           C
ANISOU 3302  C   ARG B  62     2726   2652   4752   -132    283    320       C
ATOM   3303  O   ARG B  62     -52.059  48.177  16.016  1.00 25.75           O
ANISOU 3303  O   ARG B  62     2564   2562   4659   -128    319    366       O
ATOM   3304  CB  ARG B  62     -55.196  48.866  15.278  1.00 23.52           C
ANISOU 3304  CB  ARG B  62     2409   2277   4250    -81    243    265       C
ATOM   3305  CG  ARG B  62     -55.218  47.733  16.288  1.00 23.53           C
ANISOU 3305  CG  ARG B  62     2431   2303   4207    -29    290    306       C
ATOM   3306  CD  ARG B  62     -56.630  47.256  16.565  1.00 26.11           C
ANISOU 3306  CD  ARG B  62     2834   2628   4457     20    272    289       C
ATOM   3307  NE  ARG B  62     -56.641  46.097  17.452  1.00 31.18           N
ANISOU 3307  NE  ARG B  62     3508   3295   5046     91    326    324       N
ATOM   3308  CZ  ARG B  62     -56.379  44.854  17.061  1.00 26.92           C
ANISOU 3308  CZ  ARG B  62     2916   2797   4515    120    366    342       C
ATOM   3309  NH1 ARG B  62     -56.078  44.601  15.794  1.00 23.44           N
ANISOU 3309  NH1 ARG B  62     2396   2378   4133     74    344    324       N
ATOM   3310  NH2 ARG B  62     -56.415  43.863  17.940  1.00 23.68           N
ANISOU 3310  NH2 ARG B  62     2537   2411   4051    201    428    383       N
ATOM   3311  N   ASN B  63     -52.612  50.340  16.306  1.00 31.71           N
ANISOU 3311  N   ASN B  63     3399   3253   5397   -139    275    326       N
ATOM   3312  CA  ASN B  63     -51.641  50.537  17.373  1.00 26.29           C
ANISOU 3312  CA  ASN B  63     2706   2548   4736   -142    311    386       C
ATOM   3313  C   ASN B  63     -52.146  49.895  18.658  1.00 26.68           C
ANISOU 3313  C   ASN B  63     2804   2625   4710    -81    356    432       C
ATOM   3314  O   ASN B  63     -53.253  50.189  19.120  1.00 32.12           O
ANISOU 3314  O   ASN B  63     3568   3308   5329    -46    332    412       O
ATOM   3315  CB  ASN B  63     -51.385  52.028  17.584  1.00 26.76           C
ANISOU 3315  CB  ASN B  63     2791   2555   4821   -160    286    380       C
ATOM   3316  CG  ASN B  63     -50.134  52.298  18.392  1.00 31.46           C
ANISOU 3316  CG  ASN B  63     3368   3121   5465   -178    314    442       C
ATOM   3317  OD1 ASN B  63     -49.909  51.690  19.438  1.00 34.82           O
ANISOU 3317  OD1 ASN B  63     3798   3569   5862   -151    364    505       O
ATOM   3318  ND2 ASN B  63     -49.304  53.210  17.902  1.00 30.65           N
ANISOU 3318  ND2 ASN B  63     3250   2966   5431   -217    288    428       N
ATOM   3319  N   ILE B  64     -51.334  49.013  19.236  1.00 29.79           N
ANISOU 3319  N   ILE B  64     3157   3045   5116    -66    417    499       N
ATOM   3320  CA  ILE B  64     -51.708  48.273  20.433  1.00 30.71           C
ANISOU 3320  CA  ILE B  64     3326   3193   5149     13    477    548       C
ATOM   3321  C   ILE B  64     -51.001  48.807  21.671  1.00 31.62           C
ANISOU 3321  C   ILE B  64     3467   3292   5254     29    519    618       C
ATOM   3322  O   ILE B  64     -50.983  48.139  22.710  1.00 35.89           O
ANISOU 3322  O   ILE B  64     4042   3864   5729    101    589    678       O
ATOM   3323  CB  ILE B  64     -51.451  46.768  20.257  1.00 31.03           C
ANISOU 3323  CB  ILE B  64     3301   3290   5198     46    537    591       C
ATOM   3324  CG1 ILE B  64     -49.962  46.510  20.027  1.00 32.89           C
ANISOU 3324  CG1 ILE B  64     3418   3533   5547    -12    565    661       C
ATOM   3325  CG2 ILE B  64     -52.275  46.221  19.098  1.00 30.56           C
ANISOU 3325  CG2 ILE B  64     3231   3247   5134     40    492    523       C
ATOM   3326  CD1 ILE B  64     -49.571  45.058  20.146  1.00 32.25           C
ANISOU 3326  CD1 ILE B  64     3255   3514   5485     27    637    740       C
ATOM   3327  N   LYS B  65     -50.413  49.984  21.587  1.00 31.00           N
ANISOU 3327  N   LYS B  65     3378   3166   5235    -26    482    614       N
ATOM   3328  CA  LYS B  65     -49.823  50.651  22.732  1.00 29.05           C
ANISOU 3328  CA  LYS B  65     3164   2896   4977    -13    510    678       C
ATOM   3329  C   LYS B  65     -50.756  51.741  23.237  1.00 27.88           C
ANISOU 3329  C   LYS B  65     3116   2715   4762      8    451    638       C
ATOM   3330  O   LYS B  65     -51.698  52.132  22.543  1.00 29.03           O
ANISOU 3330  O   LYS B  65     3282   2849   4900     -7    386    567       O
ATOM   3331  CB  LYS B  65     -48.462  51.248  22.353  1.00 36.41           C
ANISOU 3331  CB  LYS B  65     4019   3786   6030    -88    503    711       C
ATOM   3332  CG  LYS B  65     -47.431  50.206  21.949  1.00 50.32           C
ANISOU 3332  CG  LYS B  65     5672   5571   7875   -123    545    769       C
ATOM   3333  CD  LYS B  65     -46.036  50.800  21.841  1.00 63.15           C
ANISOU 3333  CD  LYS B  65     7238   7138   9618   -197    531    818       C
ATOM   3334  CE  LYS B  65     -45.955  51.845  20.741  1.00 71.59           C
ANISOU 3334  CE  LYS B  65     8319   8141  10743   -255    442    726       C
ATOM   3335  NZ  LYS B  65     -44.580  52.406  20.617  1.00 78.04           N
ANISOU 3335  NZ  LYS B  65     9094   8883  11672   -324    417    767       N
ATOM   3336  N   PRO B  66     -50.551  52.233  24.461  1.00 29.91           N
ANISOU 3336  N   PRO B  66     3436   2959   4972     43    468    693       N
ATOM   3337  CA  PRO B  66     -51.372  53.355  24.945  1.00 27.05           C
ANISOU 3337  CA  PRO B  66     3160   2560   4560     53    394    664       C
ATOM   3338  C   PRO B  66     -51.249  54.555  24.020  1.00 29.51           C
ANISOU 3338  C   PRO B  66     3418   2829   4966    -14    331    623       C
ATOM   3339  O   PRO B  66     -50.156  55.079  23.793  1.00 34.39           O
ANISOU 3339  O   PRO B  66     3981   3419   5669    -53    347    650       O
ATOM   3340  CB  PRO B  66     -50.793  53.640  26.334  1.00 26.47           C
ANISOU 3340  CB  PRO B  66     3143   2479   4435     95    432    744       C
ATOM   3341  CG  PRO B  66     -50.219  52.342  26.765  1.00 29.04           C
ANISOU 3341  CG  PRO B  66     3449   2855   4729    144    537    808       C
ATOM   3342  CD  PRO B  66     -49.676  51.700  25.521  1.00 28.58           C
ANISOU 3342  CD  PRO B  66     3267   2814   4779     85    558    792       C
ATOM   3343  N   VAL B  67     -52.383  54.981  23.476  1.00 27.79           N
ANISOU 3343  N   VAL B  67     3220   2603   4734    -22    261    563       N
ATOM   3344  CA  VAL B  67     -52.411  56.072  22.504  1.00 28.78           C
ANISOU 3344  CA  VAL B  67     3294   2700   4941    -66    215    528       C
ATOM   3345  C   VAL B  67     -53.377  57.136  22.998  1.00 29.87           C
ANISOU 3345  C   VAL B  67     3481   2815   5054    -57    140    532       C
ATOM   3346  O   VAL B  67     -54.291  56.851  23.791  1.00 27.86           O
ANISOU 3346  O   VAL B  67     3305   2565   4716    -27    101    535       O
ATOM   3347  CB  VAL B  67     -52.808  55.568  21.095  1.00 32.07           C
ANISOU 3347  CB  VAL B  67     3659   3138   5388    -90    211    468       C
ATOM   3348  CG1 VAL B  67     -51.712  54.689  20.520  1.00 32.16           C
ANISOU 3348  CG1 VAL B  67     3611   3163   5446   -112    265    470       C
ATOM   3349  CG2 VAL B  67     -54.124  54.812  21.155  1.00 34.00           C
ANISOU 3349  CG2 VAL B  67     3951   3410   5557    -64    184    442       C
ATOM   3350  N   PRO B  68     -53.195  58.385  22.563  1.00 29.47           N
ANISOU 3350  N   PRO B  68     3388   2735   5075    -79    111    534       N
ATOM   3351  CA  PRO B  68     -54.139  59.439  22.944  1.00 30.02           C
ANISOU 3351  CA  PRO B  68     3479   2787   5141    -76     32    551       C
ATOM   3352  C   PRO B  68     -55.545  59.117  22.464  1.00 31.84           C
ANISOU 3352  C   PRO B  68     3716   3035   5345    -84    -21    518       C
ATOM   3353  O   PRO B  68     -55.742  58.470  21.433  1.00 32.36           O
ANISOU 3353  O   PRO B  68     3745   3126   5424    -95      6    477       O
ATOM   3354  CB  PRO B  68     -53.585  60.685  22.244  1.00 26.61           C
ANISOU 3354  CB  PRO B  68     2978   2328   4803    -88     36    558       C
ATOM   3355  CG  PRO B  68     -52.145  60.392  22.033  1.00 25.59           C
ANISOU 3355  CG  PRO B  68     2829   2183   4712    -94    105    557       C
ATOM   3356  CD  PRO B  68     -52.059  58.917  21.790  1.00 26.11           C
ANISOU 3356  CD  PRO B  68     2899   2284   4738   -102    146    529       C
ATOM   3357  N   GLU B  69     -56.529  59.571  23.232  1.00 29.67           N
ANISOU 3357  N   GLU B  69     3493   2744   5036    -81   -108    542       N
ATOM   3358  CA  GLU B  69     -57.914  59.390  22.829  1.00 29.59           C
ANISOU 3358  CA  GLU B  69     3489   2736   5018   -100   -177    524       C
ATOM   3359  C   GLU B  69     -58.213  60.225  21.590  1.00 29.22           C
ANISOU 3359  C   GLU B  69     3334   2700   5067   -127   -178    530       C
ATOM   3360  O   GLU B  69     -57.625  61.287  21.372  1.00 33.42           O
ANISOU 3360  O   GLU B  69     3808   3226   5666   -124   -159    558       O
ATOM   3361  CB  GLU B  69     -58.856  59.758  23.974  1.00 33.36           C
ANISOU 3361  CB  GLU B  69     4051   3179   5445   -100   -293    553       C
ATOM   3362  CG  GLU B  69     -58.824  58.755  25.119  1.00 37.59           C
ANISOU 3362  CG  GLU B  69     4721   3706   5857    -55   -292    538       C
ATOM   3363  CD  GLU B  69     -59.893  59.014  26.161  1.00 44.31           C
ANISOU 3363  CD  GLU B  69     5684   4511   6642    -52   -428    552       C
ATOM   3364  OE1 GLU B  69     -59.780  60.014  26.901  1.00 48.78           O
ANISOU 3364  OE1 GLU B  69     6264   5053   7218    -56   -491    597       O
ATOM   3365  OE2 GLU B  69     -60.851  58.216  26.236  1.00 49.23           O
ANISOU 3365  OE2 GLU B  69     6387   5116   7204    -45   -480    516       O
ATOM   3366  N   VAL B  70     -59.137  59.722  20.767  1.00 30.95           N
ANISOU 3366  N   VAL B  70     3534   2937   5290   -144   -193    507       N
ATOM   3367  CA  VAL B  70     -59.373  60.314  19.452  1.00 29.81           C
ANISOU 3367  CA  VAL B  70     3290   2814   5221   -156   -167    514       C
ATOM   3368  C   VAL B  70     -59.841  61.758  19.583  1.00 28.74           C
ANISOU 3368  C   VAL B  70     3094   2667   5160   -166   -222    583       C
ATOM   3369  O   VAL B  70     -59.487  62.616  18.764  1.00 29.97           O
ANISOU 3369  O   VAL B  70     3167   2837   5381   -149   -173    603       O
ATOM   3370  CB  VAL B  70     -60.376  59.455  18.658  1.00 34.74           C
ANISOU 3370  CB  VAL B  70     3912   3459   5830   -172   -178    490       C
ATOM   3371  CG1 VAL B  70     -60.657  60.076  17.299  1.00 36.39           C
ANISOU 3371  CG1 VAL B  70     4022   3698   6106   -174   -143    508       C
ATOM   3372  CG2 VAL B  70     -59.841  58.039  18.497  1.00 30.24           C
ANISOU 3372  CG2 VAL B  70     3388   2906   5195   -154   -120    430       C
ATOM   3373  N   LYS B  71     -60.633  62.054  20.617  1.00 28.61           N
ANISOU 3373  N   LYS B  71     3120   2620   5132   -187   -329    623       N
ATOM   3374  CA  LYS B  71     -61.081  63.427  20.823  1.00 28.68           C
ANISOU 3374  CA  LYS B  71     3060   2617   5222   -201   -396    703       C
ATOM   3375  C   LYS B  71     -59.906  64.373  21.029  1.00 29.11           C
ANISOU 3375  C   LYS B  71     3081   2668   5312   -165   -341    725       C
ATOM   3376  O   LYS B  71     -59.953  65.525  20.585  1.00 31.30           O
ANISOU 3376  O   LYS B  71     3263   2954   5674   -153   -333    783       O
ATOM   3377  CB  LYS B  71     -62.046  63.499  22.010  1.00 29.28           C
ANISOU 3377  CB  LYS B  71     3207   2650   5270   -236   -542    738       C
ATOM   3378  CG  LYS B  71     -61.470  63.011  23.329  1.00 30.55           C
ANISOU 3378  CG  LYS B  71     3500   2781   5328   -211   -564    706       C
ATOM   3379  CD  LYS B  71     -62.498  63.123  24.445  1.00 31.79           C
ANISOU 3379  CD  LYS B  71     3746   2887   5446   -239   -726    734       C
ATOM   3380  CE  LYS B  71     -61.954  62.600  25.764  1.00 31.01           C
ANISOU 3380  CE  LYS B  71     3798   2763   5223   -197   -739    704       C
ATOM   3381  NZ  LYS B  71     -62.971  62.667  26.852  1.00 31.97           N
ANISOU 3381  NZ  LYS B  71     4036   2825   5286   -216   -910    718       N
ATOM   3382  N   ILE B  72     -58.841  63.903  21.683  1.00 28.82           N
ANISOU 3382  N   ILE B  72     3120   2617   5215   -143   -299    687       N
ATOM   3383  CA  ILE B  72     -57.639  64.718  21.829  1.00 28.39           C
ANISOU 3383  CA  ILE B  72     3041   2548   5197   -111   -245    705       C
ATOM   3384  C   ILE B  72     -57.012  64.980  20.466  1.00 28.26           C
ANISOU 3384  C   ILE B  72     2952   2549   5236    -86   -146    679       C
ATOM   3385  O   ILE B  72     -56.704  66.123  20.112  1.00 31.30           O
ANISOU 3385  O   ILE B  72     3274   2927   5690    -56   -124    717       O
ATOM   3386  CB  ILE B  72     -56.645  64.037  22.787  1.00 27.58           C
ANISOU 3386  CB  ILE B  72     3031   2427   5022    -98   -216    682       C
ATOM   3387  CG1 ILE B  72     -57.239  63.943  24.194  1.00 28.45           C
ANISOU 3387  CG1 ILE B  72     3232   2517   5062   -103   -314    712       C
ATOM   3388  CG2 ILE B  72     -55.323  64.786  22.802  1.00 23.23           C
ANISOU 3388  CG2 ILE B  72     2455   1852   4518    -72   -156    699       C
ATOM   3389  CD1 ILE B  72     -57.606  65.283  24.792  1.00 24.06           C
ANISOU 3389  CD1 ILE B  72     2647   1938   4557   -107   -404    786       C
ATOM   3390  N   LEU B  73     -56.824  63.920  19.677  1.00 25.17           N
ANISOU 3390  N   LEU B  73     2575   2178   4809    -91    -90    613       N
ATOM   3391  CA  LEU B  73     -56.245  64.079  18.347  1.00 22.75           C
ANISOU 3391  CA  LEU B  73     2223   1883   4537    -64     -9    577       C
ATOM   3392  C   LEU B  73     -57.140  64.929  17.456  1.00 24.45           C
ANISOU 3392  C   LEU B  73     2355   2127   4807    -46     -8    619       C
ATOM   3393  O   LEU B  73     -56.648  65.703  16.627  1.00 28.83           O
ANISOU 3393  O   LEU B  73     2870   2683   5403      3     53    621       O
ATOM   3394  CB  LEU B  73     -56.005  62.710  17.714  1.00 25.17           C
ANISOU 3394  CB  LEU B  73     2562   2209   4792    -79     31    506       C
ATOM   3395  CG  LEU B  73     -55.193  61.717  18.547  1.00 28.34           C
ANISOU 3395  CG  LEU B  73     3028   2595   5145    -94     40    481       C
ATOM   3396  CD1 LEU B  73     -55.004  60.413  17.790  1.00 29.93           C
ANISOU 3396  CD1 LEU B  73     3239   2821   5312   -106     78    423       C
ATOM   3397  CD2 LEU B  73     -53.851  62.313  18.936  1.00 31.58           C
ANISOU 3397  CD2 LEU B  73     3447   2962   5589    -81     70    493       C
ATOM   3398  N   ASN B  74     -58.459  64.796  17.609  1.00 26.61           N
ANISOU 3398  N   ASN B  74     2606   2421   5084    -79    -73    658       N
ATOM   3399  CA  ASN B  74     -59.378  65.619  16.831  1.00 28.10           C
ANISOU 3399  CA  ASN B  74     2697   2641   5338    -67    -72    724       C
ATOM   3400  C   ASN B  74     -59.254  67.087  17.216  1.00 32.33           C
ANISOU 3400  C   ASN B  74     3167   3165   5951    -36    -85    806       C
ATOM   3401  O   ASN B  74     -59.136  67.959  16.348  1.00 35.40           O
ANISOU 3401  O   ASN B  74     3483   3576   6392     20    -16    841       O
ATOM   3402  CB  ASN B  74     -60.816  65.136  17.023  1.00 37.42           C
ANISOU 3402  CB  ASN B  74     3869   3832   6518   -124   -158    759       C
ATOM   3403  CG  ASN B  74     -61.066  63.778  16.397  1.00 39.05           C
ANISOU 3403  CG  ASN B  74     4122   4055   6659   -141   -134    690       C
ATOM   3404  OD1 ASN B  74     -60.313  63.332  15.532  1.00 38.85           O
ANISOU 3404  OD1 ASN B  74     4109   4049   6605   -109    -47    629       O
ATOM   3405  ND2 ASN B  74     -62.133  63.115  16.829  1.00 38.44           N
ANISOU 3405  ND2 ASN B  74     4078   3966   6561   -190   -219    700       N
ATOM   3406  N   ASN B  75     -59.273  67.377  18.519  1.00 32.12           N
ANISOU 3406  N   ASN B  75     3172   3106   5927    -63   -171    841       N
ATOM   3407  CA  ASN B  75     -59.179  68.759  18.973  1.00 30.78           C
ANISOU 3407  CA  ASN B  75     2937   2924   5834    -35   -197    927       C
ATOM   3408  C   ASN B  75     -57.867  69.409  18.562  1.00 32.86           C
ANISOU 3408  C   ASN B  75     3198   3171   6115     38    -97    905       C
ATOM   3409  O   ASN B  75     -57.800  70.638  18.459  1.00 37.67           O
ANISOU 3409  O   ASN B  75     3731   3782   6798     88    -81    977       O
ATOM   3410  CB  ASN B  75     -59.344  68.831  20.491  1.00 31.07           C
ANISOU 3410  CB  ASN B  75     3032   2924   5850    -76   -315    957       C
ATOM   3411  CG  ASN B  75     -60.718  68.387  20.949  1.00 29.49           C
ANISOU 3411  CG  ASN B  75     2843   2721   5639   -144   -439    986       C
ATOM   3412  OD1 ASN B  75     -61.645  68.271  20.147  1.00 33.54           O
ANISOU 3412  OD1 ASN B  75     3289   3262   6191   -167   -442   1012       O
ATOM   3413  ND2 ASN B  75     -60.859  68.141  22.245  1.00 28.07           N
ANISOU 3413  ND2 ASN B  75     2757   2504   5405   -175   -544    985       N
ATOM   3414  N   LEU B  76     -56.828  68.617  18.322  1.00 30.56           N
ANISOU 3414  N   LEU B  76     2988   2860   5763     47    -36    812       N
ATOM   3415  CA  LEU B  76     -55.551  69.135  17.857  1.00 28.58           C
ANISOU 3415  CA  LEU B  76     2753   2577   5528    109     46    780       C
ATOM   3416  C   LEU B  76     -55.460  69.205  16.340  1.00 31.37           C
ANISOU 3416  C   LEU B  76     3080   2954   5884    164    136    742       C
ATOM   3417  O   LEU B  76     -54.462  69.711  15.818  1.00 38.19           O
ANISOU 3417  O   LEU B  76     3969   3782   6758    228    199    710       O
ATOM   3418  CB  LEU B  76     -54.405  68.280  18.404  1.00 28.89           C
ANISOU 3418  CB  LEU B  76     2890   2573   5514     83     53    711       C
ATOM   3419  CG  LEU B  76     -54.243  68.328  19.924  1.00 33.34           C
ANISOU 3419  CG  LEU B  76     3496   3108   6063     52    -15    752       C
ATOM   3420  CD1 LEU B  76     -53.134  67.399  20.390  1.00 30.35           C
ANISOU 3420  CD1 LEU B  76     3199   2697   5634     29     10    701       C
ATOM   3421  CD2 LEU B  76     -53.979  69.754  20.378  1.00 39.85           C
ANISOU 3421  CD2 LEU B  76     4281   3906   6956     97    -31    828       C
ATOM   3422  N   GLY B  77     -56.466  68.711  15.625  1.00 32.12           N
ANISOU 3422  N   GLY B  77     3139   3102   5965    147    140    744       N
ATOM   3423  CA  GLY B  77     -56.475  68.819  14.180  1.00 35.15           C
ANISOU 3423  CA  GLY B  77     3502   3516   6339    209    228    719       C
ATOM   3424  C   GLY B  77     -55.641  67.790  13.455  1.00 34.53           C
ANISOU 3424  C   GLY B  77     3511   3419   6189    208    267    605       C
ATOM   3425  O   GLY B  77     -55.178  68.056  12.341  1.00 39.49           O
ANISOU 3425  O   GLY B  77     4159   4047   6800    278    338    566       O
ATOM   3426  N   VAL B  78     -55.435  66.617  14.052  1.00 32.36           N
ANISOU 3426  N   VAL B  78     3293   3131   5871    135    220    554       N
ATOM   3427  CA  VAL B  78     -54.658  65.570  13.400  1.00 29.46           C
ANISOU 3427  CA  VAL B  78     2994   2750   5449    123    244    459       C
ATOM   3428  C   VAL B  78     -55.471  64.970  12.262  1.00 29.21           C
ANISOU 3428  C   VAL B  78     2944   2774   5379    130    270    439       C
ATOM   3429  O   VAL B  78     -56.644  64.613  12.433  1.00 32.79           O
ANISOU 3429  O   VAL B  78     3358   3270   5831     93    238    481       O
ATOM   3430  CB  VAL B  78     -54.241  64.496  14.413  1.00 28.26           C
ANISOU 3430  CB  VAL B  78     2890   2578   5271     52    198    433       C
ATOM   3431  CG1 VAL B  78     -53.553  63.336  13.706  1.00 25.42           C
ANISOU 3431  CG1 VAL B  78     2578   2213   4869     32    215    351       C
ATOM   3432  CG2 VAL B  78     -53.328  65.095  15.472  1.00 24.30           C
ANISOU 3432  CG2 VAL B  78     2411   2020   4802     52    182    458       C
ATOM   3433  N   ASP B  79     -54.847  64.860  11.088  1.00 30.01           N
ANISOU 3433  N   ASP B  79     3086   2868   5446    177    320    375       N
ATOM   3434  CA  ASP B  79     -55.494  64.291   9.916  1.00 31.44           C
ANISOU 3434  CA  ASP B  79     3264   3102   5580    194    348    353       C
ATOM   3435  C   ASP B  79     -55.016  62.890   9.577  1.00 30.06           C
ANISOU 3435  C   ASP B  79     3148   2921   5351    147    323    271       C
ATOM   3436  O   ASP B  79     -55.746  62.152   8.909  1.00 35.62           O
ANISOU 3436  O   ASP B  79     3844   3673   6016    137    326    263       O
ATOM   3437  CB  ASP B  79     -55.264  65.188   8.691  1.00 39.51           C
ANISOU 3437  CB  ASP B  79     4298   4130   6585    299    424    345       C
ATOM   3438  CG  ASP B  79     -55.479  66.652   8.993  1.00 47.08           C
ANISOU 3438  CG  ASP B  79     5195   5088   7605    363    461    430       C
ATOM   3439  OD1 ASP B  79     -56.558  67.008   9.512  1.00 52.86           O
ANISOU 3439  OD1 ASP B  79     5835   5861   8387    338    444    526       O
ATOM   3440  OD2 ASP B  79     -54.558  67.447   8.716  1.00 51.26           O
ANISOU 3440  OD2 ASP B  79     5769   5569   8137    439    500    403       O
ATOM   3441  N   ILE B  80     -53.819  62.508  10.019  1.00 28.83           N
ANISOU 3441  N   ILE B  80     3044   2709   5201    116    297    220       N
ATOM   3442  CA  ILE B  80     -53.200  61.262   9.589  1.00 24.97           C
ANISOU 3442  CA  ILE B  80     2600   2212   4676     77    272    150       C
ATOM   3443  C   ILE B  80     -52.072  60.937  10.555  1.00 29.34           C
ANISOU 3443  C   ILE B  80     3176   2708   5266     25    239    140       C
ATOM   3444  O   ILE B  80     -51.506  61.828  11.191  1.00 31.97           O
ANISOU 3444  O   ILE B  80     3514   2992   5640     39    242    165       O
ATOM   3445  CB  ILE B  80     -52.698  61.382   8.127  1.00 27.61           C
ANISOU 3445  CB  ILE B  80     2991   2534   4967    134    294     84       C
ATOM   3446  CG1 ILE B  80     -52.342  60.013   7.549  1.00 29.47           C
ANISOU 3446  CG1 ILE B  80     3258   2775   5164     89    255     23       C
ATOM   3447  CG2 ILE B  80     -51.514  62.330   8.043  1.00 33.79           C
ANISOU 3447  CG2 ILE B  80     3829   3235   5773    179    300     53       C
ATOM   3448  CD1 ILE B  80     -52.067  60.046   6.062  1.00 26.16           C
ANISOU 3448  CD1 ILE B  80     2906   2351   4682    148    263    -42       C
ATOM   3449  N   ALA B  81     -51.752  59.651  10.675  1.00 28.59           N
ANISOU 3449  N   ALA B  81     3086   2619   5157    -32    210    116       N
ATOM   3450  CA  ALA B  81     -50.706  59.183  11.571  1.00 27.57           C
ANISOU 3450  CA  ALA B  81     2963   2446   5066    -83    187    124       C
ATOM   3451  C   ALA B  81     -49.489  58.732  10.774  1.00 32.50           C
ANISOU 3451  C   ALA B  81     3624   3020   5705   -104    157     66       C
ATOM   3452  O   ALA B  81     -49.601  58.313   9.618  1.00 37.44           O
ANISOU 3452  O   ALA B  81     4272   3662   6293    -92    144     14       O
ATOM   3453  CB  ALA B  81     -51.207  58.035  12.452  1.00 20.75           C
ANISOU 3453  CB  ALA B  81     2069   1629   4186   -126    180    159       C
ATOM   3454  N   ALA B  82     -48.324  58.819  11.410  1.00 31.11           N
ANISOU 3454  N   ALA B  82     3457   2777   5585   -140    137     81       N
ATOM   3455  CA  ALA B  82     -47.060  58.467  10.774  1.00 29.16           C
ANISOU 3455  CA  ALA B  82     3246   2461   5372   -176     88     36       C
ATOM   3456  C   ALA B  82     -46.745  57.003  11.058  1.00 32.39           C
ANISOU 3456  C   ALA B  82     3605   2899   5802   -248     63     60       C
ATOM   3457  O   ALA B  82     -46.378  56.646  12.183  1.00 35.37           O
ANISOU 3457  O   ALA B  82     3942   3276   6221   -286     76    127       O
ATOM   3458  CB  ALA B  82     -45.937  59.374  11.271  1.00 30.84           C
ANISOU 3458  CB  ALA B  82     3493   2577   5650   -180     74     50       C
ATOM   3459  N   ASN B  83     -46.899  56.158  10.038  1.00 30.13           N
ANISOU 3459  N   ASN B  83     3321   2641   5485   -258     31     14       N
ATOM   3460  CA  ASN B  83     -46.455  54.764  10.078  1.00 33.49           C
ANISOU 3460  CA  ASN B  83     3694   3087   5942   -323     -4     36       C
ATOM   3461  C   ASN B  83     -47.173  53.954  11.155  1.00 30.69           C
ANISOU 3461  C   ASN B  83     3273   2812   5575   -328     50    107       C
ATOM   3462  O   ASN B  83     -46.592  53.048  11.754  1.00 28.09           O
ANISOU 3462  O   ASN B  83     2888   2492   5294   -374     49    163       O
ATOM   3463  CB  ASN B  83     -44.937  54.680  10.265  1.00 36.92           C
ANISOU 3463  CB  ASN B  83     4126   3433   6470   -390    -61     54       C
ATOM   3464  CG  ASN B  83     -44.181  55.518   9.251  1.00 43.08           C
ANISOU 3464  CG  ASN B  83     4999   4115   7256   -378   -125    -25       C
ATOM   3465  OD1 ASN B  83     -43.501  56.480   9.608  1.00 49.42           O
ANISOU 3465  OD1 ASN B  83     5843   4836   8099   -373   -130    -21       O
ATOM   3466  ND2 ASN B  83     -44.302  55.159   7.978  1.00 42.54           N
ANISOU 3466  ND2 ASN B  83     4975   4051   7139   -366   -177    -98       N
ATOM   3467  N   THR B  84     -48.442  54.266  11.402  1.00 32.92           N
ANISOU 3467  N   THR B  84     3564   3150   5796   -277     95    110       N
ATOM   3468  CA  THR B  84     -49.251  53.498  12.339  1.00 31.70           C
ANISOU 3468  CA  THR B  84     3373   3059   5611   -270    134    162       C
ATOM   3469  C   THR B  84     -50.717  53.760  12.032  1.00 29.74           C
ANISOU 3469  C   THR B  84     3145   2858   5295   -223    150    142       C
ATOM   3470  O   THR B  84     -51.056  54.581  11.176  1.00 32.90           O
ANISOU 3470  O   THR B  84     3573   3249   5678   -196    143    102       O
ATOM   3471  CB  THR B  84     -48.927  53.851  13.795  1.00 34.83           C
ANISOU 3471  CB  THR B  84     3764   3438   6031   -272    168    230       C
ATOM   3472  OG1 THR B  84     -49.667  52.993  14.673  1.00 35.39           O
ANISOU 3472  OG1 THR B  84     3821   3568   6057   -253    204    274       O
ATOM   3473  CG2 THR B  84     -49.293  55.296  14.085  1.00 36.66           C
ANISOU 3473  CG2 THR B  84     4036   3640   6253   -239    174    226       C
ATOM   3474  N   VAL B  85     -51.586  53.042  12.740  1.00 25.00           N
ANISOU 3474  N   VAL B  85     2535   2308   4658   -211    172    175       N
ATOM   3475  CA  VAL B  85     -53.030  53.201  12.610  1.00 23.04           C
ANISOU 3475  CA  VAL B  85     2304   2094   4355   -179    174    169       C
ATOM   3476  C   VAL B  85     -53.609  53.406  14.000  1.00 24.82           C
ANISOU 3476  C   VAL B  85     2551   2320   4561   -164    186    216       C
ATOM   3477  O   VAL B  85     -53.434  52.557  14.882  1.00 27.55           O
ANISOU 3477  O   VAL B  85     2898   2679   4890   -161    204    247       O
ATOM   3478  CB  VAL B  85     -53.693  51.993  11.927  1.00 19.50           C
ANISOU 3478  CB  VAL B  85     1844   1694   3870   -173    168    151       C
ATOM   3479  CG1 VAL B  85     -55.205  52.166  11.902  1.00 19.12           C
ANISOU 3479  CG1 VAL B  85     1818   1671   3778   -147    164    156       C
ATOM   3480  CG2 VAL B  85     -53.159  51.822  10.522  1.00 25.67           C
ANISOU 3480  CG2 VAL B  85     2618   2475   4661   -184    144    103       C
ATOM   3481  N   ILE B  86     -54.290  54.530  14.197  1.00 26.56           N
ANISOU 3481  N   ILE B  86     2787   2526   4778   -151    173    225       N
ATOM   3482  CA  ILE B  86     -55.046  54.779  15.417  1.00 27.06           C
ANISOU 3482  CA  ILE B  86     2882   2584   4813   -139    159    265       C
ATOM   3483  C   ILE B  86     -56.466  54.283  15.176  1.00 29.01           C
ANISOU 3483  C   ILE B  86     3146   2858   5018   -130    133    259       C
ATOM   3484  O   ILE B  86     -57.192  54.829  14.341  1.00 29.23           O
ANISOU 3484  O   ILE B  86     3154   2894   5057   -131    117    254       O
ATOM   3485  CB  ILE B  86     -55.029  56.263  15.801  1.00 29.02           C
ANISOU 3485  CB  ILE B  86     3132   2800   5095   -135    143    290       C
ATOM   3486  CG1 ILE B  86     -53.591  56.739  16.007  1.00 29.66           C
ANISOU 3486  CG1 ILE B  86     3205   2844   5221   -143    166    296       C
ATOM   3487  CG2 ILE B  86     -55.858  56.496  17.054  1.00 27.54           C
ANISOU 3487  CG2 ILE B  86     2985   2604   4875   -128    107    331       C
ATOM   3488  CD1 ILE B  86     -52.845  55.972  17.075  1.00 29.34           C
ANISOU 3488  CD1 ILE B  86     3179   2798   5169   -151    187    328       C
ATOM   3489  N   TRP B  87     -56.862  53.240  15.897  1.00 27.74           N
ANISOU 3489  N   TRP B  87     3023   2708   4807   -116    132    266       N
ATOM   3490  CA  TRP B  87     -58.176  52.643  15.712  1.00 24.54           C
ANISOU 3490  CA  TRP B  87     2647   2314   4362   -106    100    259       C
ATOM   3491  C   TRP B  87     -59.192  53.336  16.609  1.00 29.66           C
ANISOU 3491  C   TRP B  87     3348   2931   4993   -106     40    286       C
ATOM   3492  O   TRP B  87     -58.999  53.427  17.825  1.00 31.11           O
ANISOU 3492  O   TRP B  87     3583   3092   5145    -91     30    305       O
ATOM   3493  CB  TRP B  87     -58.138  51.144  16.010  1.00 22.03           C
ANISOU 3493  CB  TRP B  87     2357   2018   3996    -76    126    252       C
ATOM   3494  CG  TRP B  87     -59.389  50.447  15.595  1.00 21.80           C
ANISOU 3494  CG  TRP B  87     2357   1995   3931    -64     96    238       C
ATOM   3495  CD1 TRP B  87     -60.413  50.048  16.401  1.00 19.51           C
ANISOU 3495  CD1 TRP B  87     2150   1679   3586    -37     57    243       C
ATOM   3496  CD2 TRP B  87     -59.762  50.084  14.262  1.00 20.88           C
ANISOU 3496  CD2 TRP B  87     2200   1904   3830    -75     94    218       C
ATOM   3497  NE1 TRP B  87     -61.397  49.450  15.654  1.00 25.98           N
ANISOU 3497  NE1 TRP B  87     2976   2500   4394    -36     31    230       N
ATOM   3498  CE2 TRP B  87     -61.021  49.459  14.336  1.00 22.27           C
ANISOU 3498  CE2 TRP B  87     2427   2068   3966    -58     58    218       C
ATOM   3499  CE3 TRP B  87     -59.149  50.221  13.012  1.00 22.51           C
ANISOU 3499  CE3 TRP B  87     2343   2137   4072    -93    115    198       C
ATOM   3500  CZ2 TRP B  87     -61.680  48.972  13.211  1.00 23.67           C
ANISOU 3500  CZ2 TRP B  87     2584   2264   4145    -62     48    209       C
ATOM   3501  CZ3 TRP B  87     -59.805  49.738  11.896  1.00 22.91           C
ANISOU 3501  CZ3 TRP B  87     2381   2212   4113    -91    106    185       C
ATOM   3502  CH2 TRP B  87     -61.058  49.122  12.002  1.00 26.97           C
ANISOU 3502  CH2 TRP B  87     2935   2718   4593    -77     76    195       C
ATOM   3503  N   ASP B  88     -60.270  53.828  16.002  1.00 25.47           N
ANISOU 3503  N   ASP B  88     2800   2395   4483   -126     -5    295       N
ATOM   3504  CA  ASP B  88     -61.361  54.462  16.738  1.00 25.16           C
ANISOU 3504  CA  ASP B  88     2799   2318   4442   -141    -86    329       C
ATOM   3505  C   ASP B  88     -62.325  53.363  17.164  1.00 27.27           C
ANISOU 3505  C   ASP B  88     3150   2564   4646   -126   -129    314       C
ATOM   3506  O   ASP B  88     -63.153  52.905  16.374  1.00 26.88           O
ANISOU 3506  O   ASP B  88     3090   2520   4603   -137   -146    310       O
ATOM   3507  CB  ASP B  88     -62.051  55.519  15.882  1.00 30.24           C
ANISOU 3507  CB  ASP B  88     3370   2965   5153   -171   -112    366       C
ATOM   3508  CG  ASP B  88     -62.949  56.440  16.692  1.00 37.03           C
ANISOU 3508  CG  ASP B  88     4244   3784   6040   -198   -204    419       C
ATOM   3509  OD1 ASP B  88     -63.416  56.033  17.777  1.00 38.69           O
ANISOU 3509  OD1 ASP B  88     4545   3954   6201   -198   -272    415       O
ATOM   3510  OD2 ASP B  88     -63.190  57.578  16.236  1.00 39.50           O
ANISOU 3510  OD2 ASP B  88     4479   4105   6425   -216   -213    469       O
ATOM   3511  N   TYR B  89     -62.213  52.935  18.422  1.00 28.75           N
ANISOU 3511  N   TYR B  89     3430   2726   4769    -94   -145    308       N
ATOM   3512  CA  TYR B  89     -63.065  51.862  18.918  1.00 28.91           C
ANISOU 3512  CA  TYR B  89     3553   2718   4714    -60   -182    288       C
ATOM   3513  C   TYR B  89     -64.504  52.308  19.134  1.00 33.64           C
ANISOU 3513  C   TYR B  89     4205   3256   5321    -96   -305    304       C
ATOM   3514  O   TYR B  89     -65.403  51.460  19.149  1.00 38.65           O
ANISOU 3514  O   TYR B  89     4914   3857   5913    -80   -348    285       O
ATOM   3515  CB  TYR B  89     -62.487  51.295  20.213  1.00 27.84           C
ANISOU 3515  CB  TYR B  89     3512   2574   4492      2   -152    280       C
ATOM   3516  CG  TYR B  89     -61.272  50.424  19.997  1.00 31.67           C
ANISOU 3516  CG  TYR B  89     3948   3116   4969     41    -35    275       C
ATOM   3517  CD1 TYR B  89     -61.392  49.045  19.914  1.00 34.30           C
ANISOU 3517  CD1 TYR B  89     4314   3468   5250     96     10    258       C
ATOM   3518  CD2 TYR B  89     -60.006  50.982  19.864  1.00 31.51           C
ANISOU 3518  CD2 TYR B  89     3845   3125   5001     20     24    294       C
ATOM   3519  CE1 TYR B  89     -60.287  48.242  19.714  1.00 34.37           C
ANISOU 3519  CE1 TYR B  89     4260   3531   5267    126    109    269       C
ATOM   3520  CE2 TYR B  89     -58.895  50.187  19.665  1.00 28.64           C
ANISOU 3520  CE2 TYR B  89     3430   2806   4647     42    115    301       C
ATOM   3521  CZ  TYR B  89     -59.042  48.818  19.590  1.00 33.15           C
ANISOU 3521  CZ  TYR B  89     4020   3402   5174     92    156    293       C
ATOM   3522  OH  TYR B  89     -57.941  48.017  19.391  1.00 35.50           O
ANISOU 3522  OH  TYR B  89     4247   3746   5494    108    240    314       O
ATOM   3523  N   LYS B  90     -64.747  53.610  19.306  1.00 35.53           N
ANISOU 3523  N   LYS B  90     4405   3475   5620   -145   -369    346       N
ATOM   3524  CA  LYS B  90     -66.120  54.086  19.427  1.00 38.49           C
ANISOU 3524  CA  LYS B  90     4806   3790   6027   -194   -499    379       C
ATOM   3525  C   LYS B  90     -66.838  54.089  18.087  1.00 37.73           C
ANISOU 3525  C   LYS B  90     4618   3713   6003   -235   -495    404       C
ATOM   3526  O   LYS B  90     -68.072  54.057  18.054  1.00 43.69           O
ANISOU 3526  O   LYS B  90     5403   4415   6780   -274   -596    430       O
ATOM   3527  CB  LYS B  90     -66.145  55.484  20.039  1.00 45.94           C
ANISOU 3527  CB  LYS B  90     5721   4712   7024   -233   -571    431       C
ATOM   3528  CG  LYS B  90     -65.693  55.517  21.482  1.00 53.06           C
ANISOU 3528  CG  LYS B  90     6736   5580   7843   -195   -604    415       C
ATOM   3529  CD  LYS B  90     -66.023  56.844  22.132  1.00 58.28           C
ANISOU 3529  CD  LYS B  90     7382   6205   8556   -240   -714    472       C
ATOM   3530  CE  LYS B  90     -65.896  56.746  23.638  1.00 61.83           C
ANISOU 3530  CE  LYS B  90     7985   6607   8902   -201   -780    454       C
ATOM   3531  NZ  LYS B  90     -64.565  56.215  24.043  1.00 63.53           N
ANISOU 3531  NZ  LYS B  90     8229   6868   9041   -128   -647    422       N
ATOM   3532  N   ARG B  91     -66.092  54.131  16.987  1.00 31.83           N
ANISOU 3532  N   ARG B  91     3769   3036   5291   -226   -387    401       N
ATOM   3533  CA  ARG B  91     -66.653  54.033  15.652  1.00 27.64           C
ANISOU 3533  CA  ARG B  91     3160   2534   4809   -248   -364    424       C
ATOM   3534  C   ARG B  91     -66.372  52.694  14.988  1.00 31.26           C
ANISOU 3534  C   ARG B  91     3640   3025   5214   -208   -294    371       C
ATOM   3535  O   ARG B  91     -66.922  52.432  13.912  1.00 36.65           O
ANISOU 3535  O   ARG B  91     4278   3728   5921   -220   -281    388       O
ATOM   3536  CB  ARG B  91     -66.108  55.161  14.763  1.00 28.10           C
ANISOU 3536  CB  ARG B  91     3092   2645   4938   -257   -298    462       C
ATOM   3537  CG  ARG B  91     -66.625  56.544  15.122  1.00 30.95           C
ANISOU 3537  CG  ARG B  91     3398   2984   5378   -298   -366    540       C
ATOM   3538  CD  ARG B  91     -65.879  57.639  14.365  1.00 36.19           C
ANISOU 3538  CD  ARG B  91     3952   3701   6098   -280   -281    572       C
ATOM   3539  NE  ARG B  91     -65.755  57.346  12.939  1.00 40.55           N
ANISOU 3539  NE  ARG B  91     4450   4308   6650   -256   -192    563       N
ATOM   3540  CZ  ARG B  91     -64.616  57.014  12.338  1.00 35.63           C
ANISOU 3540  CZ  ARG B  91     3829   3723   5987   -212   -100    502       C
ATOM   3541  NH1 ARG B  91     -64.599  56.761  11.037  1.00 35.41           N
ANISOU 3541  NH1 ARG B  91     3766   3739   5948   -188    -37    495       N
ATOM   3542  NH2 ARG B  91     -63.491  56.939  13.037  1.00 32.66           N
ANISOU 3542  NH2 ARG B  91     3493   3336   5582   -194    -80    452       N
ATOM   3543  N   ASP B  92     -65.547  51.844  15.603  1.00 31.69           N
ANISOU 3543  N   ASP B  92     3754   3086   5199   -159   -249    320       N
ATOM   3544  CA  ASP B  92     -65.109  50.584  15.005  1.00 33.94           C
ANISOU 3544  CA  ASP B  92     4040   3410   5444   -118   -179    281       C
ATOM   3545  C   ASP B  92     -64.551  50.825  13.604  1.00 30.12           C
ANISOU 3545  C   ASP B  92     3452   2987   5005   -130   -113    282       C
ATOM   3546  O   ASP B  92     -64.886  50.135  12.640  1.00 32.65           O
ANISOU 3546  O   ASP B  92     3754   3332   5320   -124    -96    276       O
ATOM   3547  CB  ASP B  92     -66.245  49.559  14.984  1.00 40.32           C
ANISOU 3547  CB  ASP B  92     4925   4181   6216   -103   -228    272       C
ATOM   3548  CG  ASP B  92     -66.708  49.173  16.377  1.00 50.02           C
ANISOU 3548  CG  ASP B  92     6288   5341   7377    -71   -292    255       C
ATOM   3549  OD1 ASP B  92     -65.857  49.085  17.287  1.00 54.55           O
ANISOU 3549  OD1 ASP B  92     6899   5924   7904    -30   -253    238       O
ATOM   3550  OD2 ASP B  92     -67.925  48.961  16.564  1.00 53.76           O
ANISOU 3550  OD2 ASP B  92     6837   5748   7840    -84   -383    262       O
ATOM   3551  N   ALA B  93     -63.684  51.827  13.503  1.00 24.84           N
ANISOU 3551  N   ALA B  93     2725   2338   4373   -142    -78    290       N
ATOM   3552  CA  ALA B  93     -63.158  52.275  12.223  1.00 23.96           C
ANISOU 3552  CA  ALA B  93     2536   2273   4296   -144    -24    288       C
ATOM   3553  C   ALA B  93     -61.841  52.990  12.473  1.00 23.19           C
ANISOU 3553  C   ALA B  93     2412   2182   4218   -138     17    274       C
ATOM   3554  O   ALA B  93     -61.576  53.429  13.598  1.00 26.09           O
ANISOU 3554  O   ALA B  93     2806   2519   4587   -142     -2    286       O
ATOM   3555  CB  ALA B  93     -64.154  53.206  11.510  1.00 25.98           C
ANISOU 3555  CB  ALA B  93     2741   2531   4598   -168    -47    344       C
ATOM   3556  N   PRO B  94     -60.988  53.111  11.456  1.00 24.71           N
ANISOU 3556  N   PRO B  94     2563   2404   4420   -128     67    249       N
ATOM   3557  CA  PRO B  94     -59.762  53.896  11.627  1.00 23.82           C
ANISOU 3557  CA  PRO B  94     2433   2283   4334   -124     96    237       C
ATOM   3558  C   PRO B  94     -60.096  55.345  11.940  1.00 27.22           C
ANISOU 3558  C   PRO B  94     2840   2695   4808   -127     83    282       C
ATOM   3559  O   PRO B  94     -61.054  55.910  11.410  1.00 31.62           O
ANISOU 3559  O   PRO B  94     3365   3264   5386   -129     73    322       O
ATOM   3560  CB  PRO B  94     -59.057  53.761  10.272  1.00 22.32           C
ANISOU 3560  CB  PRO B  94     2222   2120   4141   -109    133    199       C
ATOM   3561  CG  PRO B  94     -59.637  52.534   9.658  1.00 25.07           C
ANISOU 3561  CG  PRO B  94     2577   2496   4451   -107    125    185       C
ATOM   3562  CD  PRO B  94     -61.056  52.482  10.125  1.00 24.13           C
ANISOU 3562  CD  PRO B  94     2472   2369   4328   -116     90    227       C
ATOM   3563  N   ALA B  95     -59.297  55.946  12.822  1.00 24.57           N
ANISOU 3563  N   ALA B  95     2513   2332   4492   -128     85    287       N
ATOM   3564  CA  ALA B  95     -59.532  57.336  13.184  1.00 21.99           C
ANISOU 3564  CA  ALA B  95     2157   1986   4210   -127     69    336       C
ATOM   3565  C   ALA B  95     -59.213  58.293  12.044  1.00 24.50           C
ANISOU 3565  C   ALA B  95     2427   2320   4560    -96    118    340       C
ATOM   3566  O   ALA B  95     -59.650  59.447  12.083  1.00 26.92           O
ANISOU 3566  O   ALA B  95     2690   2626   4911    -85    115    396       O
ATOM   3567  CB  ALA B  95     -58.713  57.706  14.421  1.00 21.33           C
ANISOU 3567  CB  ALA B  95     2102   1868   4134   -130     59    343       C
ATOM   3568  N   HIS B  96     -58.476  57.844  11.031  1.00 24.59           N
ANISOU 3568  N   HIS B  96     2449   2347   4548    -76    160    286       N
ATOM   3569  CA  HIS B  96     -58.066  58.703   9.933  1.00 28.90           C
ANISOU 3569  CA  HIS B  96     2977   2901   5101    -28    209    277       C
ATOM   3570  C   HIS B  96     -58.291  57.993   8.605  1.00 33.58           C
ANISOU 3570  C   HIS B  96     3580   3532   5648     -9    231    243       C
ATOM   3571  O   HIS B  96     -58.314  56.762   8.525  1.00 38.79           O
ANISOU 3571  O   HIS B  96     4262   4202   6274    -36    210    210       O
ATOM   3572  CB  HIS B  96     -56.598  59.121  10.076  1.00 29.43           C
ANISOU 3572  CB  HIS B  96     3075   2925   5184    -13    225    236       C
ATOM   3573  CG  HIS B  96     -56.281  59.749  11.396  1.00 27.94           C
ANISOU 3573  CG  HIS B  96     2881   2698   5035    -30    204    272       C
ATOM   3574  ND1 HIS B  96     -55.496  59.132  12.346  1.00 25.36           N
ANISOU 3574  ND1 HIS B  96     2584   2342   4708    -64    184    256       N
ATOM   3575  CD2 HIS B  96     -56.662  60.932  11.934  1.00 24.96           C
ANISOU 3575  CD2 HIS B  96     2470   2311   4700    -14    199    332       C
ATOM   3576  CE1 HIS B  96     -55.397  59.912  13.407  1.00 25.30           C
ANISOU 3576  CE1 HIS B  96     2574   2308   4731    -66    168    300       C
ATOM   3577  NE2 HIS B  96     -56.096  61.010  13.183  1.00 28.34           N
ANISOU 3577  NE2 HIS B  96     2920   2702   5145    -39    171    344       N
ATOM   3578  N   ILE B  97     -58.453  58.799   7.555  1.00 37.53           N
ANISOU 3578  N   ILE B  97     4065   4054   6140     46    279    257       N
ATOM   3579  CA  ILE B  97     -58.799  58.264   6.241  1.00 45.87           C
ANISOU 3579  CA  ILE B  97     5135   5151   7141     76    305    237       C
ATOM   3580  C   ILE B  97     -57.598  57.565   5.614  1.00 47.73           C
ANISOU 3580  C   ILE B  97     5437   5369   7331     84    295    146       C
ATOM   3581  O   ILE B  97     -57.630  56.359   5.341  1.00 48.50           O
ANISOU 3581  O   ILE B  97     5551   5481   7396     55    265    114       O
ATOM   3582  CB  ILE B  97     -59.332  59.385   5.331  1.00 54.65           C
ANISOU 3582  CB  ILE B  97     6215   6298   8252    149    371    292       C
ATOM   3583  CG1 ILE B  97     -60.563  60.040   5.960  1.00 59.94           C
ANISOU 3583  CG1 ILE B  97     6802   6986   8988    126    365    400       C
ATOM   3584  CG2 ILE B  97     -59.652  58.844   3.945  1.00 57.73           C
ANISOU 3584  CG2 ILE B  97     6632   6733   8569    190    404    275       C
ATOM   3585  CD1 ILE B  97     -61.706  59.079   6.211  1.00 64.00           C
ANISOU 3585  CD1 ILE B  97     7297   7514   9505     63    314    433       C
ATOM   3586  N   SER B  98     -56.528  58.312   5.372  1.00 39.20           N
ANISOU 3586  N   SER B  98     4394   4249   6252    122    312    106       N
ATOM   3587  CA  SER B  98     -55.350  57.795   4.694  1.00 31.82           C
ANISOU 3587  CA  SER B  98     3529   3281   5280    127    286     21       C
ATOM   3588  C   SER B  98     -54.308  57.326   5.703  1.00 28.20           C
ANISOU 3588  C   SER B  98     3075   2768   4870     61    236     -4       C
ATOM   3589  O   SER B  98     -54.428  57.535   6.913  1.00 25.46           O
ANISOU 3589  O   SER B  98     2690   2410   4573     28    233     40       O
ATOM   3590  CB  SER B  98     -54.758  58.862   3.770  1.00 36.71           C
ANISOU 3590  CB  SER B  98     4209   3874   5865    214    325    -13       C
ATOM   3591  OG  SER B  98     -55.719  59.311   2.833  1.00 38.18           O
ANISOU 3591  OG  SER B  98     4385   4120   6002    288    388     26       O
ATOM   3592  N   THR B  99     -53.269  56.678   5.182  1.00 30.55           N
ANISOU 3592  N   THR B  99     3420   3033   5154     43    191    -69       N
ATOM   3593  CA  THR B  99     -52.168  56.173   5.987  1.00 30.89           C
ANISOU 3593  CA  THR B  99     3460   3025   5252    -22    144    -81       C
ATOM   3594  C   THR B  99     -50.846  56.605   5.366  1.00 30.85           C
ANISOU 3594  C   THR B  99     3527   2943   5252    -10    107   -145       C
ATOM   3595  O   THR B  99     -50.793  57.108   4.240  1.00 34.02           O
ANISOU 3595  O   THR B  99     3997   3334   5596     54    114   -192       O
ATOM   3596  CB  THR B  99     -52.214  54.643   6.115  1.00 30.83           C
ANISOU 3596  CB  THR B  99     3418   3050   5245    -80    106    -78       C
ATOM   3597  OG1 THR B  99     -52.249  54.052   4.810  1.00 34.89           O
ANISOU 3597  OG1 THR B  99     3967   3585   5703    -63     77   -126       O
ATOM   3598  CG2 THR B  99     -53.441  54.205   6.900  1.00 31.13           C
ANISOU 3598  CG2 THR B  99     3404   3145   5280    -89    135    -20       C
ATOM   3599  N   ILE B 100     -49.769  56.403   6.120  1.00 29.42           N
ANISOU 3599  N   ILE B 100     3338   2702   5137    -70     67   -142       N
ATOM   3600  CA  ILE B 100     -48.414  56.696   5.670  1.00 29.77           C
ANISOU 3600  CA  ILE B 100     3453   2652   5205    -79      9   -197       C
ATOM   3601  C   ILE B 100     -47.575  55.452   5.924  1.00 31.77           C
ANISOU 3601  C   ILE B 100     3671   2886   5514   -172    -64   -191       C
ATOM   3602  O   ILE B 100     -47.294  55.117   7.081  1.00 30.93           O
ANISOU 3602  O   ILE B 100     3499   2779   5475   -226    -55   -130       O
ATOM   3603  CB  ILE B 100     -47.808  57.914   6.381  1.00 31.74           C
ANISOU 3603  CB  ILE B 100     3724   2830   5505    -60     31   -181       C
ATOM   3604  CG1 ILE B 100     -48.594  59.180   6.037  1.00 33.12           C
ANISOU 3604  CG1 ILE B 100     3924   3028   5634     42    104   -177       C
ATOM   3605  CG2 ILE B 100     -46.346  58.077   5.997  1.00 27.87           C
ANISOU 3605  CG2 ILE B 100     3311   2226   5051    -84    -46   -236       C
ATOM   3606  CD1 ILE B 100     -48.128  60.412   6.784  1.00 27.01           C
ANISOU 3606  CD1 ILE B 100     3159   2192   4911     71    131   -150       C
ATOM   3607  N   GLY B 101     -47.179  54.771   4.854  1.00 32.65           N
ANISOU 3607  N   GLY B 101     3823   2984   5597   -187   -136   -246       N
ATOM   3608  CA  GLY B 101     -46.347  53.585   4.990  1.00 37.04           C
ANISOU 3608  CA  GLY B 101     4331   3522   6219   -278   -216   -230       C
ATOM   3609  C   GLY B 101     -46.982  52.474   5.796  1.00 38.59           C
ANISOU 3609  C   GLY B 101     4417   3806   6440   -315   -177   -154       C
ATOM   3610  O   GLY B 101     -46.304  51.838   6.614  1.00 39.59           O
ANISOU 3610  O   GLY B 101     4473   3921   6649   -381   -194    -96       O
ATOM   3611  N   VAL B 102     -48.274  52.223   5.588  1.00 38.89           N
ANISOU 3611  N   VAL B 102     4440   3930   6407   -267   -124   -149       N
ATOM   3612  CA  VAL B 102     -48.991  51.202   6.344  1.00 33.22           C
ANISOU 3612  CA  VAL B 102     3637   3287   5697   -283    -85    -85       C
ATOM   3613  C   VAL B 102     -49.655  50.214   5.394  1.00 30.49           C
ANISOU 3613  C   VAL B 102     3286   3003   5298   -270   -109   -104       C
ATOM   3614  O   VAL B 102     -49.325  49.023   5.389  1.00 36.61           O
ANISOU 3614  O   VAL B 102     4003   3799   6106   -312   -148    -78       O
ATOM   3615  CB  VAL B 102     -50.032  51.833   7.286  1.00 36.26           C
ANISOU 3615  CB  VAL B 102     4010   3706   6060   -243     -1    -45       C
ATOM   3616  CG1 VAL B 102     -50.807  50.748   8.011  1.00 38.23           C
ANISOU 3616  CG1 VAL B 102     4201   4023   6302   -248     31      8       C
ATOM   3617  CG2 VAL B 102     -49.358  52.767   8.279  1.00 37.54           C
ANISOU 3617  CG2 VAL B 102     4176   3811   6275   -255     19    -18       C
ATOM   3618  N   CYS B 103     -50.598  50.699   4.588  1.00 28.96           N
ANISOU 3618  N   CYS B 103     3143   2839   5023   -209    -83   -139       N
ATOM   3619  CA  CYS B 103     -51.377  49.857   3.689  1.00 28.83           C
ANISOU 3619  CA  CYS B 103     3126   2882   4944   -188    -97   -150       C
ATOM   3620  C   CYS B 103     -51.351  50.450   2.289  1.00 32.13           C
ANISOU 3620  C   CYS B 103     3636   3285   5286   -138   -124   -216       C
ATOM   3621  O   CYS B 103     -51.625  51.641   2.114  1.00 36.94           O
ANISOU 3621  O   CYS B 103     4296   3880   5861    -83    -75   -232       O
ATOM   3622  CB  CYS B 103     -52.822  49.721   4.176  1.00 31.43           C
ANISOU 3622  CB  CYS B 103     3424   3276   5244   -155    -27   -103       C
ATOM   3623  SG  CYS B 103     -53.952  48.976   2.978  1.00 40.63           S
ANISOU 3623  SG  CYS B 103     4604   4507   6327   -115    -32   -111       S
ATOM   3624  N   SER B 104     -51.046  49.609   1.296  1.00 31.75           N
ANISOU 3624  N   SER B 104     3611   3245   5207   -149   -199   -250       N
ATOM   3625  CA  SER B 104     -50.930  50.083  -0.080  1.00 38.31           C
ANISOU 3625  CA  SER B 104     4550   4058   5947    -93   -233   -319       C
ATOM   3626  C   SER B 104     -52.218  50.730  -0.572  1.00 38.77           C
ANISOU 3626  C   SER B 104     4637   4174   5918     -8   -142   -306       C
ATOM   3627  O   SER B 104     -52.174  51.666  -1.378  1.00 41.50           O
ANISOU 3627  O   SER B 104     5075   4502   6193     64   -121   -348       O
ATOM   3628  CB  SER B 104     -50.546  48.926  -1.000  1.00 46.72           C
ANISOU 3628  CB  SER B 104     5630   5133   6990   -122   -338   -347       C
ATOM   3629  OG  SER B 104     -49.447  48.203  -0.474  1.00 61.37           O
ANISOU 3629  OG  SER B 104     7426   6944   8947   -212   -422   -332       O
ATOM   3630  N   MET B 105     -53.370  50.251  -0.100  1.00 36.64           N
ANISOU 3630  N   MET B 105     4294   3971   5655     -9    -87   -243       N
ATOM   3631  CA  MET B 105     -54.640  50.771  -0.592  1.00 37.06           C
ANISOU 3631  CA  MET B 105     4362   4079   5643     59    -10   -213       C
ATOM   3632  C   MET B 105     -54.947  52.158  -0.040  1.00 35.81           C
ANISOU 3632  C   MET B 105     4197   3905   5503     94     70   -186       C
ATOM   3633  O   MET B 105     -55.595  52.960  -0.721  1.00 40.14           O
ANISOU 3633  O   MET B 105     4777   4481   5995    167    131   -170       O
ATOM   3634  CB  MET B 105     -55.768  49.799  -0.252  1.00 35.86           C
ANISOU 3634  CB  MET B 105     4139   3985   5500     38      8   -153       C
ATOM   3635  CG  MET B 105     -56.127  48.891  -1.406  1.00 37.59           C
ANISOU 3635  CG  MET B 105     4386   4248   5648     61    -29   -164       C
ATOM   3636  SD  MET B 105     -56.539  49.873  -2.859  1.00 44.75           S
ANISOU 3636  SD  MET B 105     5388   5177   6436    160     17   -182       S
ATOM   3637  CE  MET B 105     -56.573  48.618  -4.122  1.00 45.15           C
ANISOU 3637  CE  MET B 105     5484   5266   6405    173    -59   -207       C
ATOM   3638  N   THR B 106     -54.495  52.462   1.176  1.00 31.52           N
ANISOU 3638  N   THR B 106     3611   3322   5041     49     72   -169       N
ATOM   3639  CA  THR B 106     -54.784  53.744   1.803  1.00 32.25           C
ANISOU 3639  CA  THR B 106     3690   3400   5163     77    137   -135       C
ATOM   3640  C   THR B 106     -53.574  54.658   1.917  1.00 33.24           C
ANISOU 3640  C   THR B 106     3866   3452   5312     90    125   -179       C
ATOM   3641  O   THR B 106     -53.730  55.809   2.340  1.00 34.13           O
ANISOU 3641  O   THR B 106     3971   3551   5447    125    179   -151       O
ATOM   3642  CB  THR B 106     -55.378  53.532   3.203  1.00 29.30           C
ANISOU 3642  CB  THR B 106     3238   3038   4856     27    152    -72       C
ATOM   3643  OG1 THR B 106     -54.456  52.785   4.005  1.00 27.44           O
ANISOU 3643  OG1 THR B 106     2984   2770   4674    -36    105    -85       O
ATOM   3644  CG2 THR B 106     -56.689  52.777   3.112  1.00 28.86           C
ANISOU 3644  CG2 THR B 106     3147   3041   4779     23    163    -27       C
ATOM   3645  N   ASP B 107     -52.382  54.188   1.561  1.00 33.98           N
ANISOU 3645  N   ASP B 107     4009   3494   5409     60     49   -242       N
ATOM   3646  CA  ASP B 107     -51.190  55.015   1.684  1.00 29.58           C
ANISOU 3646  CA  ASP B 107     3510   2849   4881     66     25   -284       C
ATOM   3647  C   ASP B 107     -51.225  56.160   0.685  1.00 32.37           C
ANISOU 3647  C   ASP B 107     3958   3186   5155    173     68   -323       C
ATOM   3648  O   ASP B 107     -51.464  55.954  -0.509  1.00 38.30           O
ANISOU 3648  O   ASP B 107     4776   3963   5814    228     61   -360       O
ATOM   3649  CB  ASP B 107     -49.929  54.182   1.466  1.00 32.51           C
ANISOU 3649  CB  ASP B 107     3913   3159   5282     -2    -85   -336       C
ATOM   3650  CG  ASP B 107     -49.425  53.543   2.740  1.00 38.06           C
ANISOU 3650  CG  ASP B 107     4526   3846   6090    -96   -109   -286       C
ATOM   3651  OD1 ASP B 107     -50.062  53.735   3.795  1.00 39.91           O
ANISOU 3651  OD1 ASP B 107     4691   4115   6358   -102    -44   -224       O
ATOM   3652  OD2 ASP B 107     -48.390  52.848   2.682  1.00 40.88           O
ANISOU 3652  OD2 ASP B 107     4882   4155   6496   -162   -197   -304       O
ATOM   3653  N   ILE B 108     -50.996  57.374   1.182  1.00 30.66           N
ANISOU 3653  N   ILE B 108     3750   2928   4970    214    117   -309       N
ATOM   3654  CA  ILE B 108     -50.667  58.492   0.308  1.00 30.58           C
ANISOU 3654  CA  ILE B 108     3846   2879   4893    325    152   -355       C
ATOM   3655  C   ILE B 108     -49.160  58.672   0.188  1.00 35.54           C
ANISOU 3655  C   ILE B 108     4577   3387   5539    310     65   -436       C
ATOM   3656  O   ILE B 108     -48.696  59.373  -0.724  1.00 35.99           O
ANISOU 3656  O   ILE B 108     4761   3392   5521    405     66   -501       O
ATOM   3657  CB  ILE B 108     -51.311  59.795   0.809  1.00 30.23           C
ANISOU 3657  CB  ILE B 108     3752   2858   4874    394    258   -285       C
ATOM   3658  CG1 ILE B 108     -50.804  60.124   2.212  1.00 26.89           C
ANISOU 3658  CG1 ILE B 108     3271   2385   4562    326    242   -251       C
ATOM   3659  CG2 ILE B 108     -52.827  59.677   0.799  1.00 24.71           C
ANISOU 3659  CG2 ILE B 108     2958   2268   4162    407    330   -199       C
ATOM   3660  CD1 ILE B 108     -51.332  61.423   2.753  1.00 27.69           C
ANISOU 3660  CD1 ILE B 108     3321   2501   4698    390    327   -181       C
ATOM   3661  N   ALA B 109     -48.387  58.055   1.079  1.00 35.49           N
ANISOU 3661  N   ALA B 109     4524   3331   5628    197     -9   -430       N
ATOM   3662  CA  ALA B 109     -46.936  58.141   1.072  1.00 33.03           C
ANISOU 3662  CA  ALA B 109     4294   2897   5359    158   -106   -491       C
ATOM   3663  C   ALA B 109     -46.390  57.019   1.940  1.00 34.17           C
ANISOU 3663  C   ALA B 109     4347   3030   5607     20   -181   -454       C
ATOM   3664  O   ALA B 109     -47.099  56.458   2.777  1.00 36.91           O
ANISOU 3664  O   ALA B 109     4575   3455   5993    -26   -136   -381       O
ATOM   3665  CB  ALA B 109     -46.448  59.500   1.583  1.00 31.52           C
ANISOU 3665  CB  ALA B 109     4141   2630   5204    213    -62   -487       C
ATOM   3666  N   LYS B 110     -45.118  56.695   1.724  1.00 39.98           N
ANISOU 3666  N   LYS B 110     5142   3664   6387    -41   -298   -502       N
ATOM   3667  CA  LYS B 110     -44.437  55.730   2.573  1.00 40.20           C
ANISOU 3667  CA  LYS B 110     5074   3673   6529   -170   -364   -450       C
ATOM   3668  C   LYS B 110     -43.689  56.395   3.717  1.00 39.81           C
ANISOU 3668  C   LYS B 110     4997   3548   6580   -207   -350   -404       C
ATOM   3669  O   LYS B 110     -43.464  55.757   4.751  1.00 39.06           O
ANISOU 3669  O   LYS B 110     4792   3472   6576   -292   -349   -326       O
ATOM   3670  CB  LYS B 110     -43.467  54.887   1.741  1.00 44.18           C
ANISOU 3670  CB  LYS B 110     5632   4108   7047   -237   -515   -504       C
ATOM   3671  CG  LYS B 110     -43.781  54.879   0.255  1.00 53.41           C
ANISOU 3671  CG  LYS B 110     6925   5285   8084   -158   -554   -594       C
ATOM   3672  CD  LYS B 110     -43.620  53.493  -0.345  1.00 64.47           C
ANISOU 3672  CD  LYS B 110     8295   6711   9488   -233   -666   -601       C
ATOM   3673  CE  LYS B 110     -44.672  52.537   0.197  1.00 72.58           C
ANISOU 3673  CE  LYS B 110     9170   7876  10531   -258   -588   -516       C
ATOM   3674  NZ  LYS B 110     -44.648  51.222  -0.503  1.00 77.82           N
ANISOU 3674  NZ  LYS B 110     9806   8577  11186   -309   -686   -520       N
ATOM   3675  N   LYS B 111     -43.314  57.662   3.557  1.00 43.20           N
ANISOU 3675  N   LYS B 111     5526   3896   6992   -135   -333   -446       N
ATOM   3676  CA  LYS B 111     -42.606  58.427   4.567  1.00 44.94           C
ANISOU 3676  CA  LYS B 111     5736   4038   7301   -157   -320   -405       C
ATOM   3677  C   LYS B 111     -43.323  59.749   4.805  1.00 40.27           C
ANISOU 3677  C   LYS B 111     5164   3473   6666    -43   -205   -393       C
ATOM   3678  O   LYS B 111     -43.839  60.357   3.858  1.00 39.71           O
ANISOU 3678  O   LYS B 111     5171   3419   6497     66   -165   -447       O
ATOM   3679  CB  LYS B 111     -41.157  58.696   4.139  1.00 52.50           C
ANISOU 3679  CB  LYS B 111     6809   4834   8305   -190   -442   -467       C
ATOM   3680  CG  LYS B 111     -40.341  57.445   3.861  1.00 61.65           C
ANISOU 3680  CG  LYS B 111     7945   5953   9528   -314   -579   -469       C
ATOM   3681  CD  LYS B 111     -40.160  56.612   5.118  1.00 71.02           C
ANISOU 3681  CD  LYS B 111     8967   7184  10832   -426   -563   -351       C
ATOM   3682  CE  LYS B 111     -39.269  55.408   4.858  1.00 78.59           C
ANISOU 3682  CE  LYS B 111     9884   8101  11876   -550   -699   -333       C
ATOM   3683  NZ  LYS B 111     -39.072  54.585   6.084  1.00 80.99           N
ANISOU 3683  NZ  LYS B 111    10021   8456  12295   -645   -666   -203       N
ATOM   3684  N   PRO B 112     -43.375  60.219   6.054  1.00 36.46           N
ANISOU 3684  N   PRO B 112     4606   2996   6252    -61   -149   -314       N
ATOM   3685  CA  PRO B 112     -44.012  61.520   6.321  1.00 37.18           C
ANISOU 3685  CA  PRO B 112     4702   3107   6315     42    -52   -291       C
ATOM   3686  C   PRO B 112     -43.281  62.692   5.691  1.00 43.74           C
ANISOU 3686  C   PRO B 112     5666   3826   7128    134    -63   -355       C
ATOM   3687  O   PRO B 112     -43.886  63.758   5.525  1.00 49.34           O
ANISOU 3687  O   PRO B 112     6392   4561   7794    248     23   -347       O
ATOM   3688  CB  PRO B 112     -43.995  61.616   7.853  1.00 33.09           C
ANISOU 3688  CB  PRO B 112     4087   2602   5882    -16    -21   -194       C
ATOM   3689  CG  PRO B 112     -43.810  60.208   8.330  1.00 33.16           C
ANISOU 3689  CG  PRO B 112     4019   2647   5933   -130    -66   -158       C
ATOM   3690  CD  PRO B 112     -42.968  59.537   7.292  1.00 33.70           C
ANISOU 3690  CD  PRO B 112     4154   2650   5999   -170   -164   -231       C
ATOM   3691  N   THR B 113     -42.006  62.533   5.340  1.00 44.06           N
ANISOU 3691  N   THR B 113     5802   3736   7202     90   -168   -414       N
ATOM   3692  CA  THR B 113     -41.236  63.611   4.738  1.00 45.75           C
ANISOU 3692  CA  THR B 113     6167   3822   7393    182   -190   -486       C
ATOM   3693  C   THR B 113     -41.595  63.859   3.280  1.00 46.28           C
ANISOU 3693  C   THR B 113     6360   3898   7327    304   -179   -580       C
ATOM   3694  O   THR B 113     -41.157  64.868   2.719  1.00 53.20           O
ANISOU 3694  O   THR B 113     7372   4683   8157    419   -170   -640       O
ATOM   3695  CB  THR B 113     -39.740  63.311   4.845  1.00 51.24           C
ANISOU 3695  CB  THR B 113     6934   4360   8176     85   -327   -517       C
ATOM   3696  OG1 THR B 113     -39.485  61.981   4.374  1.00 49.44           O
ANISOU 3696  OG1 THR B 113     6689   4142   7954    -20   -429   -542       O
ATOM   3697  CG2 THR B 113     -39.274  63.439   6.285  1.00 53.02           C
ANISOU 3697  CG2 THR B 113     7061   4557   8527      1   -316   -416       C
ATOM   3698  N   GLU B 114     -42.366  62.971   2.657  1.00 41.70           N
ANISOU 3698  N   GLU B 114     5744   3424   6678    291   -175   -592       N
ATOM   3699  CA  GLU B 114     -42.718  63.145   1.257  1.00 41.36           C
ANISOU 3699  CA  GLU B 114     5823   3396   6495    409   -162   -674       C
ATOM   3700  C   GLU B 114     -43.560  64.404   1.069  1.00 41.86           C
ANISOU 3700  C   GLU B 114     5893   3518   6494    572    -13   -645       C
ATOM   3701  O   GLU B 114     -44.228  64.885   1.990  1.00 42.05           O
ANISOU 3701  O   GLU B 114     5788   3611   6576    575     79   -550       O
ATOM   3702  CB  GLU B 114     -43.462  61.916   0.736  1.00 41.27           C
ANISOU 3702  CB  GLU B 114     5753   3497   6432    358   -180   -672       C
ATOM   3703  CG  GLU B 114     -42.655  60.630   0.840  1.00 50.01           C
ANISOU 3703  CG  GLU B 114     6839   4554   7606    204   -326   -689       C
ATOM   3704  CD  GLU B 114     -43.331  59.452   0.168  1.00 58.99           C
ANISOU 3704  CD  GLU B 114     7938   5793   8682    173   -352   -696       C
ATOM   3705  OE1 GLU B 114     -44.169  59.677  -0.731  1.00 63.75           O
ANISOU 3705  OE1 GLU B 114     8591   6467   9163    281   -286   -722       O
ATOM   3706  OE2 GLU B 114     -43.028  58.299   0.542  1.00 60.01           O
ANISOU 3706  OE2 GLU B 114     7982   5932   8886     43   -433   -666       O
ATOM   3707  N   THR B 115     -43.513  64.939  -0.154  1.00 42.03           N
ANISOU 3707  N   THR B 115     6070   3510   6392    715      8   -724       N
ATOM   3708  CA  THR B 115     -44.146  66.224  -0.442  1.00 46.47           C
ANISOU 3708  CA  THR B 115     6652   4114   6892    891    154   -694       C
ATOM   3709  C   THR B 115     -45.641  66.202  -0.148  1.00 48.97           C
ANISOU 3709  C   THR B 115     6793   4603   7210    902    278   -581       C
ATOM   3710  O   THR B 115     -46.205  67.216   0.284  1.00 48.77           O
ANISOU 3710  O   THR B 115     6693   4624   7215    984    390   -500       O
ATOM   3711  CB  THR B 115     -43.897  66.605  -1.904  1.00 50.81           C
ANISOU 3711  CB  THR B 115     7406   4615   7284   1051    159   -798       C
ATOM   3712  OG1 THR B 115     -42.495  66.533  -2.185  1.00 54.76           O
ANISOU 3712  OG1 THR B 115     8083   4937   7785   1024     13   -910       O
ATOM   3713  CG2 THR B 115     -44.384  68.017  -2.187  1.00 55.89           C
ANISOU 3713  CG2 THR B 115     8077   5289   7870   1252    319   -760       C
ATOM   3714  N   ILE B 116     -46.293  65.056  -0.356  1.00 50.04           N
ANISOU 3714  N   ILE B 116     6859   4831   7324    818    251   -569       N
ATOM   3715  CA  ILE B 116     -47.741  64.979  -0.222  1.00 45.28           C
ANISOU 3715  CA  ILE B 116     6110   4378   6714    829    355   -468       C
ATOM   3716  C   ILE B 116     -48.202  65.201   1.216  1.00 42.61           C
ANISOU 3716  C   ILE B 116     5605   4080   6503    748    385   -362       C
ATOM   3717  O   ILE B 116     -49.344  65.619   1.440  1.00 39.50           O
ANISOU 3717  O   ILE B 116     5099   3786   6121    784    478   -266       O
ATOM   3718  CB  ILE B 116     -48.234  63.621  -0.763  1.00 43.10           C
ANISOU 3718  CB  ILE B 116     5814   4174   6389    754    303   -487       C
ATOM   3719  CG1 ILE B 116     -49.752  63.626  -0.953  1.00 43.21           C
ANISOU 3719  CG1 ILE B 116     5714   4332   6371    794    412   -392       C
ATOM   3720  CG2 ILE B 116     -47.810  62.493   0.158  1.00 38.80           C
ANISOU 3720  CG2 ILE B 116     5192   3608   5943    578    196   -482       C
ATOM   3721  CD1 ILE B 116     -50.224  64.581  -2.026  1.00 50.07           C
ANISOU 3721  CD1 ILE B 116     6652   5241   7133    974    528   -383       C
ATOM   3722  N   CYS B 117     -47.341  64.950   2.200  1.00 40.98           N
ANISOU 3722  N   CYS B 117     5383   3794   6392    640    304   -368       N
ATOM   3723  CA  CYS B 117     -47.739  65.024   3.599  1.00 38.80           C
ANISOU 3723  CA  CYS B 117     4967   3555   6222    559    321   -273       C
ATOM   3724  C   CYS B 117     -47.548  66.403   4.213  1.00 42.80           C
ANISOU 3724  C   CYS B 117     5462   4020   6782    633    377   -224       C
ATOM   3725  O   CYS B 117     -47.937  66.606   5.368  1.00 44.05           O
ANISOU 3725  O   CYS B 117     5509   4210   7019    580    390   -139       O
ATOM   3726  CB  CYS B 117     -46.953  64.001   4.425  1.00 40.70           C
ANISOU 3726  CB  CYS B 117     5184   3744   6534    409    218   -285       C
ATOM   3727  SG  CYS B 117     -47.026  62.312   3.800  1.00 44.96           S
ANISOU 3727  SG  CYS B 117     5724   4325   7031    316    139   -333       S
ATOM   3728  N   ALA B 118     -46.965  67.349   3.476  1.00 44.72           N
ANISOU 3728  N   ALA B 118     5822   4191   6979    761    408   -274       N
ATOM   3729  CA  ALA B 118     -46.635  68.648   4.059  1.00 45.10           C
ANISOU 3729  CA  ALA B 118     5868   4185   7084    837    456   -231       C
ATOM   3730  C   ALA B 118     -47.857  69.428   4.534  1.00 42.47           C
ANISOU 3730  C   ALA B 118     5389   3962   6786    890    558   -106       C
ATOM   3731  O   ALA B 118     -47.844  69.905   5.682  1.00 42.72           O
ANISOU 3731  O   ALA B 118     5339   3983   6909    849    552    -34       O
ATOM   3732  CB  ALA B 118     -45.800  69.460   3.061  1.00 46.73           C
ANISOU 3732  CB  ALA B 118     6247   4288   7219    984    472   -317       C
ATOM   3733  N   PRO B 119     -48.924  69.606   3.744  1.00 41.99           N
ANISOU 3733  N   PRO B 119     5286   4005   6664    974    645    -66       N
ATOM   3734  CA  PRO B 119     -50.071  70.381   4.242  1.00 42.37           C
ANISOU 3734  CA  PRO B 119     5180   4150   6768   1009    727     69       C
ATOM   3735  C   PRO B 119     -50.909  69.660   5.286  1.00 41.44           C
ANISOU 3735  C   PRO B 119     4924   4102   6720    860    677    143       C
ATOM   3736  O   PRO B 119     -51.870  70.250   5.793  1.00 40.21           O
ANISOU 3736  O   PRO B 119     4639   4016   6622    869    718    257       O
ATOM   3737  CB  PRO B 119     -50.890  70.644   2.971  1.00 42.08           C
ANISOU 3737  CB  PRO B 119     5147   4200   6642   1137    832     92       C
ATOM   3738  CG  PRO B 119     -50.582  69.496   2.100  1.00 41.09           C
ANISOU 3738  CG  PRO B 119     5133   4061   6420   1100    777    -18       C
ATOM   3739  CD  PRO B 119     -49.136  69.177   2.348  1.00 42.22           C
ANISOU 3739  CD  PRO B 119     5403   4066   6571   1045    672   -131       C
ATOM   3740  N   LEU B 120     -50.581  68.418   5.630  1.00 42.13           N
ANISOU 3740  N   LEU B 120     5034   4169   6805    730    586     85       N
ATOM   3741  CA  LEU B 120     -51.365  67.631   6.569  1.00 35.37           C
ANISOU 3741  CA  LEU B 120     4072   3373   5994    604    540    143       C
ATOM   3742  C   LEU B 120     -50.713  67.622   7.946  1.00 34.14           C
ANISOU 3742  C   LEU B 120     3900   3157   5915    519    477    160       C
ATOM   3743  O   LEU B 120     -49.486  67.634   8.075  1.00 37.35           O
ANISOU 3743  O   LEU B 120     4390   3468   6334    509    440    100       O
ATOM   3744  CB  LEU B 120     -51.529  66.194   6.070  1.00 30.20           C
ANISOU 3744  CB  LEU B 120     3443   2748   5282    527    495     83       C
ATOM   3745  CG  LEU B 120     -52.265  66.007   4.743  1.00 29.80           C
ANISOU 3745  CG  LEU B 120     3408   2767   5147    598    550     72       C
ATOM   3746  CD1 LEU B 120     -52.208  64.555   4.311  1.00 27.65           C
ANISOU 3746  CD1 LEU B 120     3174   2508   4824    519    488      6       C
ATOM   3747  CD2 LEU B 120     -53.707  66.474   4.855  1.00 26.71           C
ANISOU 3747  CD2 LEU B 120     2892   2473   4784    620    611    190       C
ATOM   3748  N   THR B 121     -51.553  67.596   8.978  1.00 30.95           N
ANISOU 3748  N   THR B 121     3395   2804   5561    457    460    245       N
ATOM   3749  CA  THR B 121     -51.085  67.494  10.358  1.00 29.37           C
ANISOU 3749  CA  THR B 121     3180   2561   5417    378    402    271       C
ATOM   3750  C   THR B 121     -50.834  66.023  10.663  1.00 28.72           C
ANISOU 3750  C   THR B 121     3122   2480   5312    271    345    224       C
ATOM   3751  O   THR B 121     -51.771  65.246  10.861  1.00 29.48           O
ANISOU 3751  O   THR B 121     3171   2642   5388    219    329    247       O
ATOM   3752  CB  THR B 121     -52.101  68.097  11.321  1.00 26.26           C
ANISOU 3752  CB  THR B 121     2685   2217   5074    365    396    380       C
ATOM   3753  OG1 THR B 121     -52.235  69.498  11.056  1.00 29.45           O
ANISOU 3753  OG1 THR B 121     3053   2621   5515    468    452    437       O
ATOM   3754  CG2 THR B 121     -51.650  67.903  12.759  1.00 24.53           C
ANISOU 3754  CG2 THR B 121     2468   1959   4892    289    335    405       C
ATOM   3755  N   VAL B 122     -49.565  65.640  10.697  1.00 30.43           N
ANISOU 3755  N   VAL B 122     3410   2618   5536    240    312    165       N
ATOM   3756  CA  VAL B 122     -49.164  64.251  10.879  1.00 26.32           C
ANISOU 3756  CA  VAL B 122     2903   2095   5003    148    264    128       C
ATOM   3757  C   VAL B 122     -48.917  63.987  12.357  1.00 29.21           C
ANISOU 3757  C   VAL B 122     3238   2449   5413     79    236    186       C
ATOM   3758  O   VAL B 122     -48.273  64.784  13.048  1.00 33.84           O
ANISOU 3758  O   VAL B 122     3835   2976   6045     91    233    218       O
ATOM   3759  CB  VAL B 122     -47.912  63.935  10.040  1.00 28.02           C
ANISOU 3759  CB  VAL B 122     3206   2230   5212    145    232     44       C
ATOM   3760  CG1 VAL B 122     -47.517  62.479  10.200  1.00 23.81           C
ANISOU 3760  CG1 VAL B 122     2665   1703   4681     47    180     23       C
ATOM   3761  CG2 VAL B 122     -48.156  64.268   8.577  1.00 28.77           C
ANISOU 3761  CG2 VAL B 122     3355   2334   5242    232    261    -16       C
ATOM   3762  N   PHE B 123     -49.425  62.861  12.846  1.00 30.70           N
ANISOU 3762  N   PHE B 123     3393   2692   5579     16    218    201       N
ATOM   3763  CA  PHE B 123     -49.227  62.461  14.232  1.00 27.44           C
ANISOU 3763  CA  PHE B 123     2964   2277   5187    -37    201    255       C
ATOM   3764  C   PHE B 123     -47.965  61.617  14.349  1.00 27.56           C
ANISOU 3764  C   PHE B 123     3000   2242   5228    -94    181    236       C
ATOM   3765  O   PHE B 123     -47.815  60.610  13.650  1.00 25.20           O
ANISOU 3765  O   PHE B 123     2703   1960   4913   -124    167    194       O
ATOM   3766  CB  PHE B 123     -50.437  61.683  14.750  1.00 29.28           C
ANISOU 3766  CB  PHE B 123     3162   2587   5376    -62    195    284       C
ATOM   3767  CG  PHE B 123     -50.245  61.111  16.126  1.00 30.38           C
ANISOU 3767  CG  PHE B 123     3304   2729   5511   -101    184    333       C
ATOM   3768  CD1 PHE B 123     -50.307  61.927  17.243  1.00 29.66           C
ANISOU 3768  CD1 PHE B 123     3216   2619   5433    -89    175    393       C
ATOM   3769  CD2 PHE B 123     -50.006  59.759  16.302  1.00 35.62           C
ANISOU 3769  CD2 PHE B 123     3967   3415   6152   -141    187    326       C
ATOM   3770  CE1 PHE B 123     -50.131  61.405  18.510  1.00 33.65           C
ANISOU 3770  CE1 PHE B 123     3739   3128   5917   -112    170    440       C
ATOM   3771  CE2 PHE B 123     -49.830  59.230  17.567  1.00 36.95           C
ANISOU 3771  CE2 PHE B 123     4143   3591   6306   -158    193    378       C
ATOM   3772  CZ  PHE B 123     -49.893  60.055  18.672  1.00 37.34           C
ANISOU 3772  CZ  PHE B 123     4210   3622   6356   -142    186    433       C
ATOM   3773  N   PHE B 124     -47.064  62.031  15.235  1.00 30.91           N
ANISOU 3773  N   PHE B 124     3436   2606   5701   -110    175    279       N
ATOM   3774  CA  PHE B 124     -45.808  61.336  15.470  1.00 26.06           C
ANISOU 3774  CA  PHE B 124     2830   1939   5134   -171    155    287       C
ATOM   3775  C   PHE B 124     -45.778  60.799  16.893  1.00 29.61           C
ANISOU 3775  C   PHE B 124     3250   2417   5584   -204    173    370       C
ATOM   3776  O   PHE B 124     -46.216  61.473  17.832  1.00 30.94           O
ANISOU 3776  O   PHE B 124     3422   2598   5738   -176    185    420       O
ATOM   3777  CB  PHE B 124     -44.608  62.260  15.235  1.00 25.79           C
ANISOU 3777  CB  PHE B 124     2844   1792   5163   -162    133    274       C
ATOM   3778  CG  PHE B 124     -44.538  62.824  13.844  1.00 25.80           C
ANISOU 3778  CG  PHE B 124     2899   1754   5150   -110    120    188       C
ATOM   3779  CD1 PHE B 124     -43.853  62.154  12.843  1.00 26.83           C
ANISOU 3779  CD1 PHE B 124     3065   1842   5286   -144     74    121       C
ATOM   3780  CD2 PHE B 124     -45.151  64.028  13.538  1.00 29.92           C
ANISOU 3780  CD2 PHE B 124     3437   2282   5650    -22    152    179       C
ATOM   3781  CE1 PHE B 124     -43.784  62.673  11.562  1.00 27.76           C
ANISOU 3781  CE1 PHE B 124     3255   1920   5371    -83     60     37       C
ATOM   3782  CE2 PHE B 124     -45.085  64.553  12.259  1.00 29.14           C
ANISOU 3782  CE2 PHE B 124     3396   2151   5524     45    156    106       C
ATOM   3783  CZ  PHE B 124     -44.400  63.874  11.271  1.00 26.53           C
ANISOU 3783  CZ  PHE B 124     3123   1775   5182     19    109     29       C
ATOM   3784  N   ASP B 125     -45.259  59.585  17.046  1.00 35.21           N
ANISOU 3784  N   ASP B 125     3931   3140   6306   -259    173    390       N
ATOM   3785  CA  ASP B 125     -45.128  58.925  18.342  1.00 36.36           C
ANISOU 3785  CA  ASP B 125     4052   3319   6444   -278    205    475       C
ATOM   3786  C   ASP B 125     -43.651  58.935  18.721  1.00 35.38           C
ANISOU 3786  C   ASP B 125     3918   3117   6406   -327    198    531       C
ATOM   3787  O   ASP B 125     -42.861  58.143  18.200  1.00 38.14           O
ANISOU 3787  O   ASP B 125     4236   3443   6810   -383    177    529       O
ATOM   3788  CB  ASP B 125     -45.687  57.505  18.284  1.00 41.70           C
ANISOU 3788  CB  ASP B 125     4694   4077   7075   -290    224    475       C
ATOM   3789  CG  ASP B 125     -45.705  56.823  19.642  1.00 48.04           C
ANISOU 3789  CG  ASP B 125     5484   4924   7846   -283    273    563       C
ATOM   3790  OD1 ASP B 125     -45.226  57.420  20.630  1.00 49.57           O
ANISOU 3790  OD1 ASP B 125     5696   5085   8052   -276    289    628       O
ATOM   3791  OD2 ASP B 125     -46.205  55.681  19.720  1.00 49.95           O
ANISOU 3791  OD2 ASP B 125     5704   5232   8043   -275    299    571       O
ATOM   3792  N   GLY B 126     -43.285  59.828  19.642  1.00 33.36           N
ANISOU 3792  N   GLY B 126     3686   2818   6169   -311    209    588       N
ATOM   3793  CA  GLY B 126     -41.905  59.946  20.084  1.00 33.85           C
ANISOU 3793  CA  GLY B 126     3742   2800   6320   -357    203    655       C
ATOM   3794  C   GLY B 126     -41.342  58.697  20.729  1.00 40.23           C
ANISOU 3794  C   GLY B 126     4491   3643   7153   -406    239    744       C
ATOM   3795  O   GLY B 126     -40.120  58.603  20.893  1.00 49.40           O
ANISOU 3795  O   GLY B 126     5628   4734   8408   -463    226    806       O
ATOM   3796  N   ARG B 127     -42.196  57.742  21.102  1.00 37.79           N
ANISOU 3796  N   ARG B 127     4157   3437   6766   -381    284    759       N
ATOM   3797  CA  ARG B 127     -41.722  56.476  21.644  1.00 37.12           C
ANISOU 3797  CA  ARG B 127     4007   3398   6699   -410    333    850       C
ATOM   3798  C   ARG B 127     -41.109  55.576  20.580  1.00 39.51           C
ANISOU 3798  C   ARG B 127     4245   3686   7081   -478    294    827       C
ATOM   3799  O   ARG B 127     -40.497  54.562  20.930  1.00 46.50           O
ANISOU 3799  O   ARG B 127     5054   4598   8015   -514    327    919       O
ATOM   3800  CB  ARG B 127     -42.870  55.743  22.338  1.00 34.84           C
ANISOU 3800  CB  ARG B 127     3729   3218   6292   -344    393    864       C
ATOM   3801  CG  ARG B 127     -43.476  56.510  23.498  1.00 36.34           C
ANISOU 3801  CG  ARG B 127     3990   3421   6395   -280    416    894       C
ATOM   3802  CD  ARG B 127     -44.743  55.842  23.999  1.00 37.80           C
ANISOU 3802  CD  ARG B 127     4214   3695   6455   -214    448    880       C
ATOM   3803  NE  ARG B 127     -45.790  55.835  22.982  1.00 36.55           N
ANISOU 3803  NE  ARG B 127     4065   3556   6265   -208    401    771       N
ATOM   3804  CZ  ARG B 127     -47.028  55.395  23.187  1.00 34.39           C
ANISOU 3804  CZ  ARG B 127     3833   3340   5893   -159    403    738       C
ATOM   3805  NH1 ARG B 127     -47.377  54.925  24.376  1.00 31.86           N
ANISOU 3805  NH1 ARG B 127     3562   3060   5482   -103    448    794       N
ATOM   3806  NH2 ARG B 127     -47.917  55.427  22.203  1.00 32.66           N
ANISOU 3806  NH2 ARG B 127     3616   3134   5661   -162    359    652       N
ATOM   3807  N   VAL B 128     -41.259  55.916  19.305  1.00 32.98           N
ANISOU 3807  N   VAL B 128     3445   2819   6266   -492    223    716       N
ATOM   3808  CA  VAL B 128     -40.720  55.129  18.203  1.00 31.81           C
ANISOU 3808  CA  VAL B 128     3252   2650   6183   -556    164    682       C
ATOM   3809  C   VAL B 128     -39.471  55.821  17.678  1.00 37.31           C
ANISOU 3809  C   VAL B 128     3976   3214   6987   -618     84    668       C
ATOM   3810  O   VAL B 128     -39.431  57.053  17.566  1.00 38.84           O
ANISOU 3810  O   VAL B 128     4247   3338   7172   -586     63    619       O
ATOM   3811  CB  VAL B 128     -41.768  54.947  17.089  1.00 29.92           C
ANISOU 3811  CB  VAL B 128     3041   2458   5868   -522    137    566       C
ATOM   3812  CG1 VAL B 128     -41.255  53.999  16.018  1.00 29.72           C
ANISOU 3812  CG1 VAL B 128     2971   2422   5899   -584     71    539       C
ATOM   3813  CG2 VAL B 128     -43.080  54.450  17.671  1.00 28.04           C
ANISOU 3813  CG2 VAL B 128     2799   2332   5524   -456    207    575       C
ATOM   3814  N   ASP B 129     -38.448  55.028  17.360  1.00 41.96           N
ANISOU 3814  N   ASP B 129     4500   3761   7681   -706     33    717       N
ATOM   3815  CA  ASP B 129     -37.172  55.574  16.914  1.00 45.29           C
ANISOU 3815  CA  ASP B 129     4963   4078   8168   -756    -62    698       C
ATOM   3816  C   ASP B 129     -37.345  56.418  15.658  1.00 43.10           C
ANISOU 3816  C   ASP B 129     4791   3711   7872   -736   -141    554       C
ATOM   3817  O   ASP B 129     -37.994  55.999  14.695  1.00 41.28           O
ANISOU 3817  O   ASP B 129     4570   3505   7609   -727   -168    472       O
ATOM   3818  CB  ASP B 129     -36.177  54.442  16.650  1.00 57.08           C
ANISOU 3818  CB  ASP B 129     6373   5582   9732   -838   -121    757       C
ATOM   3819  CG  ASP B 129     -35.676  53.793  17.926  1.00 65.75           C
ANISOU 3819  CG  ASP B 129     7373   6745  10865   -852    -44    916       C
ATOM   3820  OD1 ASP B 129     -36.072  54.247  19.020  1.00 68.25           O
ANISOU 3820  OD1 ASP B 129     7699   7090  11143   -799     52    974       O
ATOM   3821  OD2 ASP B 129     -34.885  52.830  17.833  1.00 68.31           O
ANISOU 3821  OD2 ASP B 129     7610   7090  11254   -912    -79    988       O
ATOM   3822  N   GLY B 130     -36.761  57.614  15.676  1.00 42.00           N
ANISOU 3822  N   GLY B 130     4738   3473   7747   -718   -172    526       N
ATOM   3823  CA  GLY B 130     -36.737  58.478  14.516  1.00 41.15           C
ANISOU 3823  CA  GLY B 130     4745   3267   7624   -684   -242    397       C
ATOM   3824  C   GLY B 130     -37.966  59.333  14.306  1.00 36.08           C
ANISOU 3824  C   GLY B 130     4158   2661   6891   -577   -179    325       C
ATOM   3825  O   GLY B 130     -37.976  60.150  13.377  1.00 38.75           O
ANISOU 3825  O   GLY B 130     4595   2932   7194   -522   -217    224       O
ATOM   3826  N   GLN B 131     -39.002  59.184  15.134  1.00 35.14           N
ANISOU 3826  N   GLN B 131     3983   2664   6705   -533    -85    374       N
ATOM   3827  CA  GLN B 131     -40.226  59.950  14.926  1.00 36.22           C
ANISOU 3827  CA  GLN B 131     4159   2863   6740   -434    -35    315       C
ATOM   3828  C   GLN B 131     -40.091  61.394  15.391  1.00 36.40           C
ANISOU 3828  C   GLN B 131     4237   2821   6771   -374    -14    325       C
ATOM   3829  O   GLN B 131     -40.742  62.281  14.829  1.00 37.30           O
ANISOU 3829  O   GLN B 131     4400   2941   6830   -291      2    262       O
ATOM   3830  CB  GLN B 131     -41.396  59.275  15.641  1.00 35.76           C
ANISOU 3830  CB  GLN B 131     4033   2943   6611   -413     37    361       C
ATOM   3831  CG  GLN B 131     -41.703  57.876  15.132  1.00 40.10           C
ANISOU 3831  CG  GLN B 131     4528   3565   7141   -452     27    348       C
ATOM   3832  CD  GLN B 131     -42.851  57.843  14.142  1.00 44.75           C
ANISOU 3832  CD  GLN B 131     5142   4218   7641   -397     30    260       C
ATOM   3833  OE1 GLN B 131     -44.004  58.088  14.502  1.00 46.03           O
ANISOU 3833  OE1 GLN B 131     5300   4455   7735   -343     81    264       O
ATOM   3834  NE2 GLN B 131     -42.543  57.533  12.889  1.00 43.95           N
ANISOU 3834  NE2 GLN B 131     5071   4085   7543   -414    -32    184       N
ATOM   3835  N   VAL B 132     -39.266  61.650  16.409  1.00 36.21           N
ANISOU 3835  N   VAL B 132     4201   2740   6818   -409    -10    414       N
ATOM   3836  CA  VAL B 132     -39.050  63.024  16.856  1.00 34.78           C
ANISOU 3836  CA  VAL B 132     4073   2489   6653   -351      2    430       C
ATOM   3837  C   VAL B 132     -38.364  63.834  15.764  1.00 37.14           C
ANISOU 3837  C   VAL B 132     4469   2660   6981   -321    -58    340       C
ATOM   3838  O   VAL B 132     -38.734  64.985  15.497  1.00 38.74           O
ANISOU 3838  O   VAL B 132     4726   2842   7151   -227    -36    300       O
ATOM   3839  CB  VAL B 132     -38.242  63.041  18.168  1.00 38.32           C
ANISOU 3839  CB  VAL B 132     4490   2899   7170   -399     18    553       C
ATOM   3840  CG1 VAL B 132     -37.865  64.466  18.542  1.00 29.28           C
ANISOU 3840  CG1 VAL B 132     3406   1666   6053   -342     17    569       C
ATOM   3841  CG2 VAL B 132     -39.037  62.388  19.287  1.00 36.20           C
ANISOU 3841  CG2 VAL B 132     4152   2759   6844   -396     87    635       C
ATOM   3842  N   ASP B 133     -37.360  63.244  15.110  1.00 38.86           N
ANISOU 3842  N   ASP B 133     4714   2788   7262   -396   -139    309       N
ATOM   3843  CA  ASP B 133     -36.679  63.933  14.018  1.00 42.72           C
ANISOU 3843  CA  ASP B 133     5322   3142   7766   -364   -212    210       C
ATOM   3844  C   ASP B 133     -37.629  64.203  12.859  1.00 41.19           C
ANISOU 3844  C   ASP B 133     5182   3006   7464   -268   -192     98       C
ATOM   3845  O   ASP B 133     -37.599  65.285  12.261  1.00 45.80           O
ANISOU 3845  O   ASP B 133     5863   3523   8016   -169   -188     33       O
ATOM   3846  CB  ASP B 133     -35.479  63.115  13.544  1.00 53.17           C
ANISOU 3846  CB  ASP B 133     6664   4408   9129   -468   -318    196       C
ATOM   3847  CG  ASP B 133     -34.251  63.336  14.399  1.00 68.20           C
ANISOU 3847  CG  ASP B 133     8565   6255  11093   -527   -347    282       C
ATOM   3848  OD1 ASP B 133     -34.121  62.662  15.442  1.00 74.17           O
ANISOU 3848  OD1 ASP B 133     9214   7088  11880   -589   -309    397       O
ATOM   3849  OD2 ASP B 133     -33.417  64.190  14.029  1.00 75.02           O
ANISOU 3849  OD2 ASP B 133     9539   6996  11970   -504   -404    237       O
ATOM   3850  N   LEU B 134     -38.473  63.225  12.522  1.00 35.82           N
ANISOU 3850  N   LEU B 134     4439   2448   6724   -287   -173     83       N
ATOM   3851  CA  LEU B 134     -39.472  63.435  11.482  1.00 33.69           C
ANISOU 3851  CA  LEU B 134     4207   2246   6349   -196   -142     -4       C
ATOM   3852  C   LEU B 134     -40.426  64.562  11.851  1.00 33.51           C
ANISOU 3852  C   LEU B 134     4172   2283   6278    -87    -51     19       C
ATOM   3853  O   LEU B 134     -40.877  65.308  10.974  1.00 35.23           O
ANISOU 3853  O   LEU B 134     4451   2501   6433     16    -23    -44       O
ATOM   3854  CB  LEU B 134     -40.246  62.140  11.230  1.00 32.67           C
ANISOU 3854  CB  LEU B 134     4000   2239   6173   -242   -136     -5       C
ATOM   3855  CG  LEU B 134     -39.449  60.970  10.649  1.00 34.96           C
ANISOU 3855  CG  LEU B 134     4290   2487   6505   -341   -232    -30       C
ATOM   3856  CD1 LEU B 134     -40.224  59.671  10.792  1.00 35.83           C
ANISOU 3856  CD1 LEU B 134     4296   2731   6587   -386   -206      5       C
ATOM   3857  CD2 LEU B 134     -39.107  61.229   9.193  1.00 35.94           C
ANISOU 3857  CD2 LEU B 134     4541   2531   6583   -298   -307   -151       C
ATOM   3858  N   PHE B 135     -40.740  64.702  13.141  1.00 30.67           N
ANISOU 3858  N   PHE B 135     3734   1973   5946   -106     -4    117       N
ATOM   3859  CA  PHE B 135     -41.576  65.810  13.585  1.00 30.48           C
ANISOU 3859  CA  PHE B 135     3692   1996   5894    -14     63    153       C
ATOM   3860  C   PHE B 135     -40.871  67.145  13.381  1.00 38.73           C
ANISOU 3860  C   PHE B 135     4820   2923   6972     65     60    134       C
ATOM   3861  O   PHE B 135     -41.502  68.134  12.990  1.00 44.16           O
ANISOU 3861  O   PHE B 135     5522   3634   7623    174    110    121       O
ATOM   3862  CB  PHE B 135     -41.960  65.616  15.051  1.00 31.78           C
ANISOU 3862  CB  PHE B 135     3773   2226   6076    -56     92    259       C
ATOM   3863  CG  PHE B 135     -42.708  66.776  15.645  1.00 33.81           C
ANISOU 3863  CG  PHE B 135     4008   2518   6321     22    137    309       C
ATOM   3864  CD1 PHE B 135     -44.035  67.000  15.324  1.00 26.14           C
ANISOU 3864  CD1 PHE B 135     2994   1645   5290     77    174    303       C
ATOM   3865  CD2 PHE B 135     -42.087  67.634  16.538  1.00 41.89           C
ANISOU 3865  CD2 PHE B 135     5044   3472   7399     36    136    373       C
ATOM   3866  CE1 PHE B 135     -44.727  68.064  15.875  1.00 26.19           C
ANISOU 3866  CE1 PHE B 135     2966   1683   5301    140    202    363       C
ATOM   3867  CE2 PHE B 135     -42.774  68.699  17.093  1.00 46.80           C
ANISOU 3867  CE2 PHE B 135     5639   4128   8017    107    166    427       C
ATOM   3868  CZ  PHE B 135     -44.096  68.912  16.762  1.00 26.72           C
ANISOU 3868  CZ  PHE B 135     3046   1685   5422    156    195    424       C
ATOM   3869  N   ARG B 136     -39.560  67.191  13.635  1.00 34.65           N
ANISOU 3869  N   ARG B 136     4357   2277   6532     14      2    141       N
ATOM   3870  CA  ARG B 136     -38.807  68.420  13.414  1.00 33.81           C
ANISOU 3870  CA  ARG B 136     4347   2039   6458     92     -9    117       C
ATOM   3871  C   ARG B 136     -38.783  68.805  11.941  1.00 32.58           C
ANISOU 3871  C   ARG B 136     4303   1835   6242    186    -20     -1       C
ATOM   3872  O   ARG B 136     -38.745  69.996  11.612  1.00 33.06           O
ANISOU 3872  O   ARG B 136     4432   1842   6288    309     15    -23       O
ATOM   3873  CB  ARG B 136     -37.379  68.267  13.940  1.00 35.49           C
ANISOU 3873  CB  ARG B 136     4600   2112   6773      4    -82    151       C
ATOM   3874  CG  ARG B 136     -37.270  68.048  15.441  1.00 32.63           C
ANISOU 3874  CG  ARG B 136     4145   1786   6468    -68    -60    279       C
ATOM   3875  CD  ARG B 136     -35.810  67.995  15.870  1.00 35.20           C
ANISOU 3875  CD  ARG B 136     4510   2014   6849   -147   -126    316       C
ATOM   3876  NE  ARG B 136     -35.656  67.867  17.316  1.00 38.01           N
ANISOU 3876  NE  ARG B 136     4787   2424   7229   -197    -94    443       N
ATOM   3877  CZ  ARG B 136     -35.617  68.898  18.155  1.00 38.34           C
ANISOU 3877  CZ  ARG B 136     4837   2452   7279   -141    -61    506       C
ATOM   3878  NH1 ARG B 136     -35.728  70.135  17.693  1.00 37.19           N
ANISOU 3878  NH1 ARG B 136     4763   2244   7126    -31    -52    459       N
ATOM   3879  NH2 ARG B 136     -35.469  68.693  19.457  1.00 36.12           N
ANISOU 3879  NH2 ARG B 136     4494   2220   7010   -186    -35    620       N
ATOM   3880  N   ASN B 137     -38.807  67.820  11.045  1.00 34.34           N
ANISOU 3880  N   ASN B 137     4549   2078   6422    141    -65    -73       N
ATOM   3881  CA  ASN B 137     -38.758  68.072   9.612  1.00 41.40           C
ANISOU 3881  CA  ASN B 137     5566   2925   7239    230    -82   -189       C
ATOM   3882  C   ASN B 137     -40.134  68.234   8.982  1.00 43.97           C
ANISOU 3882  C   ASN B 137     5851   3393   7462    329      9   -204       C
ATOM   3883  O   ASN B 137     -40.220  68.671   7.830  1.00 47.70           O
ANISOU 3883  O   ASN B 137     6427   3842   7856    438     24   -286       O
ATOM   3884  CB  ASN B 137     -38.009  66.938   8.905  1.00 49.09           C
ANISOU 3884  CB  ASN B 137     6596   3836   8220    129   -197   -259       C
ATOM   3885  CG  ASN B 137     -36.562  66.838   9.340  1.00 63.29           C
ANISOU 3885  CG  ASN B 137     8444   5471  10130     32   -302   -244       C
ATOM   3886  OD1 ASN B 137     -35.877  67.849   9.495  1.00 66.46           O
ANISOU 3886  OD1 ASN B 137     8933   5748  10569     88   -312   -249       O
ATOM   3887  ND2 ASN B 137     -36.090  65.614   9.548  1.00 69.18           N
ANISOU 3887  ND2 ASN B 137     9130   6218  10938   -114   -380   -214       N
ATOM   3888  N   ALA B 138     -41.201  67.896   9.698  1.00 42.99           N
ANISOU 3888  N   ALA B 138     5589   3411   7335    295     68   -124       N
ATOM   3889  CA  ALA B 138     -42.544  68.013   9.154  1.00 42.86           C
ANISOU 3889  CA  ALA B 138     5522   3526   7237    372    146   -122       C
ATOM   3890  C   ALA B 138     -43.037  69.452   9.238  1.00 44.27           C
ANISOU 3890  C   ALA B 138     5690   3719   7412    508    232    -78       C
ATOM   3891  O   ALA B 138     -42.715  70.190  10.173  1.00 43.97           O
ANISOU 3891  O   ALA B 138     5628   3638   7442    514    240    -14       O
ATOM   3892  CB  ALA B 138     -43.508  67.087   9.897  1.00 43.52           C
ANISOU 3892  CB  ALA B 138     5471   3740   7323    282    161    -54       C
ATOM   3893  N   ARG B 139     -43.829  69.848   8.241  1.00 41.00           N
ANISOU 3893  N   ARG B 139     5289   3369   6919    620    300   -103       N
ATOM   3894  CA  ARG B 139     -44.383  71.197   8.220  1.00 37.49           C
ANISOU 3894  CA  ARG B 139     4815   2954   6475    759    394    -46       C
ATOM   3895  C   ARG B 139     -45.520  71.343   9.224  1.00 34.73           C
ANISOU 3895  C   ARG B 139     4301   2722   6170    721    431     74       C
ATOM   3896  O   ARG B 139     -45.528  72.275  10.035  1.00 32.48           O
ANISOU 3896  O   ARG B 139     3968   2424   5948    756    452    151       O
ATOM   3897  CB  ARG B 139     -44.856  71.544   6.808  1.00 44.13           C
ANISOU 3897  CB  ARG B 139     5720   3832   7216    899    465    -97       C
ATOM   3898  CG  ARG B 139     -45.399  72.952   6.670  1.00 51.84           C
ANISOU 3898  CG  ARG B 139     6659   4844   8195   1061    576    -27       C
ATOM   3899  CD  ARG B 139     -45.415  73.400   5.220  1.00 59.93           C
ANISOU 3899  CD  ARG B 139     7799   5860   9111   1227    648    -94       C
ATOM   3900  NE  ARG B 139     -45.733  74.820   5.099  1.00 67.52           N
ANISOU 3900  NE  ARG B 139     8734   6841  10082   1400    762    -22       N
ATOM   3901  CZ  ARG B 139     -44.851  75.799   5.273  1.00 69.63           C
ANISOU 3901  CZ  ARG B 139     9086   6991  10379   1497    770    -36       C
ATOM   3902  NH1 ARG B 139     -43.592  75.516   5.578  1.00 68.66           N
ANISOU 3902  NH1 ARG B 139     9085   6719  10284   1426    664   -118       N
ATOM   3903  NH2 ARG B 139     -45.229  77.064   5.144  1.00 72.34           N
ANISOU 3903  NH2 ARG B 139     9388   7365  10732   1664    885     43       N
ATOM   3904  N   ASN B 140     -46.489  70.434   9.181  1.00 33.22           N
ANISOU 3904  N   ASN B 140     4032   2641   5949    652    430     91       N
ATOM   3905  CA  ASN B 140     -47.576  70.383  10.146  1.00 32.38           C
ANISOU 3905  CA  ASN B 140     3788   2633   5880    596    438    194       C
ATOM   3906  C   ASN B 140     -47.541  69.034  10.844  1.00 33.47           C
ANISOU 3906  C   ASN B 140     3904   2792   6023    451    369    185       C
ATOM   3907  O   ASN B 140     -47.382  67.996  10.195  1.00 34.19           O
ANISOU 3907  O   ASN B 140     4034   2887   6068    405    342    116       O
ATOM   3908  CB  ASN B 140     -48.935  70.585   9.469  1.00 27.51           C
ANISOU 3908  CB  ASN B 140     3095   2133   5226    657    505    238       C
ATOM   3909  CG  ASN B 140     -49.007  71.872   8.678  1.00 37.46           C
ANISOU 3909  CG  ASN B 140     4370   3388   6474    819    594    258       C
ATOM   3910  OD1 ASN B 140     -49.360  72.922   9.213  1.00 39.88           O
ANISOU 3910  OD1 ASN B 140     4599   3713   6840    875    629    351       O
ATOM   3911  ND2 ASN B 140     -48.671  71.798   7.395  1.00 36.18           N
ANISOU 3911  ND2 ASN B 140     4312   3204   6232    904    630    174       N
ATOM   3912  N   GLY B 141     -47.681  69.044  12.164  1.00 26.11           N
ANISOU 3912  N   GLY B 141     2910   1870   5140    387    341    258       N
ATOM   3913  CA  GLY B 141     -47.600  67.789  12.888  1.00 26.09           C
ANISOU 3913  CA  GLY B 141     2893   1885   5136    268    290    258       C
ATOM   3914  C   GLY B 141     -47.965  67.941  14.346  1.00 27.20           C
ANISOU 3914  C   GLY B 141     2975   2051   5311    223    268    346       C
ATOM   3915  O   GLY B 141     -48.076  69.049  14.879  1.00 30.08           O
ANISOU 3915  O   GLY B 141     3313   2401   5714    272    278    408       O
ATOM   3916  N   VAL B 142     -48.155  66.787  14.984  1.00 24.23           N
ANISOU 3916  N   VAL B 142     2582   1710   4913    137    238    353       N
ATOM   3917  CA  VAL B 142     -48.400  66.680  16.417  1.00 27.18           C
ANISOU 3917  CA  VAL B 142     2928   2102   5296     92    211    426       C
ATOM   3918  C   VAL B 142     -47.525  65.558  16.954  1.00 27.77           C
ANISOU 3918  C   VAL B 142     3033   2151   5369     18    194    416       C
ATOM   3919  O   VAL B 142     -47.491  64.464  16.379  1.00 35.24           O
ANISOU 3919  O   VAL B 142     3982   3120   6287    -20    192    368       O
ATOM   3920  CB  VAL B 142     -49.884  66.410  16.732  1.00 29.26           C
ANISOU 3920  CB  VAL B 142     3138   2457   5523     79    197    462       C
ATOM   3921  CG1 VAL B 142     -50.061  66.031  18.195  1.00 24.80           C
ANISOU 3921  CG1 VAL B 142     2578   1904   4943     32    160    519       C
ATOM   3922  CG2 VAL B 142     -50.727  67.628  16.391  1.00 33.03           C
ANISOU 3922  CG2 VAL B 142     3564   2960   6027    145    210    506       C
ATOM   3923  N   LEU B 143     -46.814  65.827  18.045  1.00 26.86           N
ANISOU 3923  N   LEU B 143     2930   1989   5285      0    183    472       N
ATOM   3924  CA  LEU B 143     -45.878  64.875  18.624  1.00 24.27           C
ANISOU 3924  CA  LEU B 143     2619   1634   4968    -65    178    488       C
ATOM   3925  C   LEU B 143     -46.252  64.586  20.070  1.00 30.76           C
ANISOU 3925  C   LEU B 143     3433   2498   5756    -82    176    566       C
ATOM   3926  O   LEU B 143     -46.606  65.498  20.823  1.00 29.02           O
ANISOU 3926  O   LEU B 143     3214   2276   5536    -49    163    618       O
ATOM   3927  CB  LEU B 143     -44.440  65.403  18.555  1.00 28.93           C
ANISOU 3927  CB  LEU B 143     3248   2114   5631    -70    169    491       C
ATOM   3928  CG  LEU B 143     -43.357  64.557  19.230  1.00 30.73           C
ANISOU 3928  CG  LEU B 143     3477   2304   5895   -142    164    536       C
ATOM   3929  CD1 LEU B 143     -43.216  63.209  18.544  1.00 28.90           C
ANISOU 3929  CD1 LEU B 143     3226   2101   5654   -198    158    492       C
ATOM   3930  CD2 LEU B 143     -42.026  65.293  19.250  1.00 31.50           C
ANISOU 3930  CD2 LEU B 143     3616   2278   6074   -147    144    552       C
ATOM   3931  N   ILE B 144     -46.176  63.314  20.449  1.00 33.92           N
ANISOU 3931  N   ILE B 144     3828   2937   6125   -127    188    576       N
ATOM   3932  CA  ILE B 144     -46.315  62.895  21.837  1.00 29.56           C
ANISOU 3932  CA  ILE B 144     3288   2417   5527   -133    198    650       C
ATOM   3933  C   ILE B 144     -45.028  62.202  22.258  1.00 29.71           C
ANISOU 3933  C   ILE B 144     3304   2400   5585   -176    226    697       C
ATOM   3934  O   ILE B 144     -44.440  61.437  21.485  1.00 30.45           O
ANISOU 3934  O   ILE B 144     3372   2481   5716   -217    232    665       O
ATOM   3935  CB  ILE B 144     -47.533  61.971  22.056  1.00 29.94           C
ANISOU 3935  CB  ILE B 144     3338   2550   5488   -129    197    636       C
ATOM   3936  CG1 ILE B 144     -47.381  60.666  21.271  1.00 31.11           C
ANISOU 3936  CG1 ILE B 144     3460   2728   5632   -161    220    592       C
ATOM   3937  CG2 ILE B 144     -48.816  62.683  21.665  1.00 29.88           C
ANISOU 3937  CG2 ILE B 144     3323   2570   5458    -99    159    607       C
ATOM   3938  CD1 ILE B 144     -48.262  59.547  21.779  1.00 27.75           C
ANISOU 3938  CD1 ILE B 144     3046   2375   5122   -152    233    598       C
ATOM   3939  N   THR B 145     -44.576  62.497  23.474  1.00 26.33           N
ANISOU 3939  N   THR B 145     2897   1954   5153   -168    239    782       N
ATOM   3940  CA  THR B 145     -43.403  61.855  24.044  1.00 27.79           C
ANISOU 3940  CA  THR B 145     3070   2113   5377   -207    276    856       C
ATOM   3941  C   THR B 145     -43.675  61.545  25.507  1.00 30.68           C
ANISOU 3941  C   THR B 145     3467   2529   5661   -175    310    944       C
ATOM   3942  O   THR B 145     -44.569  62.123  26.131  1.00 33.03           O
ANISOU 3942  O   THR B 145     3810   2854   5888   -128    286    947       O
ATOM   3943  CB  THR B 145     -42.142  62.728  23.933  1.00 29.24           C
ANISOU 3943  CB  THR B 145     3259   2187   5663   -229    259    885       C
ATOM   3944  OG1 THR B 145     -42.355  63.969  24.617  1.00 36.63           O
ANISOU 3944  OG1 THR B 145     4232   3097   6587   -180    242    919       O
ATOM   3945  CG2 THR B 145     -41.792  63.005  22.477  1.00 28.63           C
ANISOU 3945  CG2 THR B 145     3176   2048   5653   -249    221    792       C
ATOM   3946  N   GLU B 146     -42.890  60.619  26.051  1.00 30.96           N
ANISOU 3946  N   GLU B 146     3480   2577   5707   -198    366   1021       N
ATOM   3947  CA  GLU B 146     -42.962  60.316  27.473  1.00 33.81           C
ANISOU 3947  CA  GLU B 146     3880   2982   5984   -155    414   1117       C
ATOM   3948  C   GLU B 146     -42.076  61.231  28.303  1.00 42.07           C
ANISOU 3948  C   GLU B 146     4950   3964   7070   -152    417   1208       C
ATOM   3949  O   GLU B 146     -42.398  61.507  29.464  1.00 48.36           O
ANISOU 3949  O   GLU B 146     5809   4787   7778    -98    428   1269       O
ATOM   3950  CB  GLU B 146     -42.569  58.858  27.722  1.00 35.65           C
ANISOU 3950  CB  GLU B 146     4070   3272   6204   -164    492   1178       C
ATOM   3951  CG  GLU B 146     -43.339  57.861  26.878  1.00 39.67           C
ANISOU 3951  CG  GLU B 146     4550   3840   6682   -167    492   1097       C
ATOM   3952  CD  GLU B 146     -43.016  56.426  27.236  1.00 49.82           C
ANISOU 3952  CD  GLU B 146     5789   5191   7950   -158    576   1171       C
ATOM   3953  OE1 GLU B 146     -43.921  55.714  27.721  1.00 51.93           O
ANISOU 3953  OE1 GLU B 146     6100   5531   8100    -92    612   1164       O
ATOM   3954  OE2 GLU B 146     -41.854  56.012  27.042  1.00 55.82           O
ANISOU 3954  OE2 GLU B 146     6468   5924   8816   -216    605   1242       O
ATOM   3955  N   GLY B 147     -40.974  61.709  27.731  1.00 42.68           N
ANISOU 3955  N   GLY B 147     4990   3952   7274   -206    400   1219       N
ATOM   3956  CA  GLY B 147     -40.074  62.597  28.436  1.00 41.51           C
ANISOU 3956  CA  GLY B 147     4865   3730   7178   -207    398   1306       C
ATOM   3957  C   GLY B 147     -39.840  63.900  27.701  1.00 40.14           C
ANISOU 3957  C   GLY B 147     4706   3461   7086   -211    331   1245       C
ATOM   3958  O   GLY B 147     -40.631  64.285  26.835  1.00 36.75           O
ANISOU 3958  O   GLY B 147     4280   3041   6644   -192    290   1140       O
ATOM   3959  N   SER B 148     -38.748  64.581  28.033  1.00 43.60           N
ANISOU 3959  N   SER B 148     5153   3805   7608   -229    325   1317       N
ATOM   3960  CA  SER B 148     -38.458  65.884  27.454  1.00 38.04           C
ANISOU 3960  CA  SER B 148     4476   3001   6977   -214    268   1270       C
ATOM   3961  C   SER B 148     -37.741  65.740  26.120  1.00 37.05           C
ANISOU 3961  C   SER B 148     4332   2812   6935   -266    232   1180       C
ATOM   3962  O   SER B 148     -36.927  64.832  25.927  1.00 41.89           O
ANISOU 3962  O   SER B 148     4909   3423   7585   -333    240   1200       O
ATOM   3963  CB  SER B 148     -37.601  66.712  28.411  1.00 38.07           C
ANISOU 3963  CB  SER B 148     4512   2949   7003   -200    268   1367       C
ATOM   3964  OG  SER B 148     -36.327  66.119  28.596  1.00 41.35           O
ANISOU 3964  OG  SER B 148     4900   3341   7468   -263    288   1428       O
ATOM   3965  N   VAL B 149     -38.053  66.644  25.196  1.00 35.89           N
ANISOU 3965  N   VAL B 149     4212   2618   6806   -228    190   1084       N
ATOM   3966  CA  VAL B 149     -37.316  66.801  23.949  1.00 35.75           C
ANISOU 3966  CA  VAL B 149     4213   2523   6848   -253    145    992       C
ATOM   3967  C   VAL B 149     -36.530  68.099  24.047  1.00 41.12           C
ANISOU 3967  C   VAL B 149     4949   3107   7567   -217    115   1000       C
ATOM   3968  O   VAL B 149     -37.085  69.137  24.427  1.00 47.46           O
ANISOU 3968  O   VAL B 149     5772   3911   8352   -143    121   1016       O
ATOM   3969  CB  VAL B 149     -38.254  66.812  22.731  1.00 32.78           C
ANISOU 3969  CB  VAL B 149     3839   2162   6456   -221    133    877       C
ATOM   3970  CG1 VAL B 149     -37.446  66.803  21.444  1.00 34.91           C
ANISOU 3970  CG1 VAL B 149     4146   2348   6772   -246     83    783       C
ATOM   3971  CG2 VAL B 149     -39.199  65.627  22.784  1.00 33.30           C
ANISOU 3971  CG2 VAL B 149     3854   2346   6452   -242    164    869       C
ATOM   3972  N   LYS B 150     -35.241  68.041  23.717  1.00 37.37           N
ANISOU 3972  N   LYS B 150     4499   2548   7151   -269     77    995       N
ATOM   3973  CA  LYS B 150     -34.372  69.196  23.907  1.00 40.36           C
ANISOU 3973  CA  LYS B 150     4939   2826   7569   -240     48   1012       C
ATOM   3974  C   LYS B 150     -34.837  70.370  23.054  1.00 41.00           C
ANISOU 3974  C   LYS B 150     5077   2856   7646   -145     32    921       C
ATOM   3975  O   LYS B 150     -34.984  70.249  21.833  1.00 35.68           O
ANISOU 3975  O   LYS B 150     4431   2152   6974   -134      9    815       O
ATOM   3976  CB  LYS B 150     -32.921  68.833  23.582  1.00 39.38           C
ANISOU 3976  CB  LYS B 150     4839   2611   7512   -322     -3   1015       C
ATOM   3977  CG  LYS B 150     -32.717  68.051  22.294  1.00 34.70           C
ANISOU 3977  CG  LYS B 150     4253   1993   6938   -374    -52    916       C
ATOM   3978  CD  LYS B 150     -31.237  67.965  21.949  1.00 36.20           C
ANISOU 3978  CD  LYS B 150     4486   2068   7200   -447   -127    916       C
ATOM   3979  CE  LYS B 150     -30.939  66.788  21.033  1.00 57.91           C
ANISOU 3979  CE  LYS B 150     7209   4822   9972   -531   -179    865       C
ATOM   3980  NZ  LYS B 150     -31.700  66.845  19.756  1.00 55.68           N
ANISOU 3980  NZ  LYS B 150     6974   4535   9648   -483   -201    728       N
ATOM   3981  N   GLY B 151     -35.086  71.505  23.709  1.00 43.91           N
ANISOU 3981  N   GLY B 151     5461   3216   8006    -69     47    969       N
ATOM   3982  CA  GLY B 151     -35.465  72.726  23.039  1.00 39.74           C
ANISOU 3982  CA  GLY B 151     4974   2643   7480     36     44    908       C
ATOM   3983  C   GLY B 151     -36.954  72.931  22.851  1.00 38.00           C
ANISOU 3983  C   GLY B 151     4703   2516   7220    103     77    890       C
ATOM   3984  O   GLY B 151     -37.377  74.058  22.570  1.00 39.82           O
ANISOU 3984  O   GLY B 151     4943   2731   7455    202     86    877       O
ATOM   3985  N   LEU B 152     -37.762  71.884  23.001  1.00 33.51           N
ANISOU 3985  N   LEU B 152     4076   2042   6614     55     94    896       N
ATOM   3986  CA  LEU B 152     -39.196  71.955  22.748  1.00 32.77           C
ANISOU 3986  CA  LEU B 152     3933   2030   6487    105    116    877       C
ATOM   3987  C   LEU B 152     -39.942  72.147  24.062  1.00 35.08           C
ANISOU 3987  C   LEU B 152     4186   2398   6743    116    119    978       C
ATOM   3988  O   LEU B 152     -39.812  71.329  24.980  1.00 37.74           O
ANISOU 3988  O   LEU B 152     4517   2774   7050     56    124   1039       O
ATOM   3989  CB  LEU B 152     -39.684  70.695  22.035  1.00 29.83           C
ANISOU 3989  CB  LEU B 152     3534   1723   6076     50    124    808       C
ATOM   3990  CG  LEU B 152     -39.068  70.414  20.663  1.00 35.37           C
ANISOU 3990  CG  LEU B 152     4281   2349   6809     38    106    703       C
ATOM   3991  CD1 LEU B 152     -39.753  69.231  19.994  1.00 31.36           C
ANISOU 3991  CD1 LEU B 152     3739   1936   6242     -5    113    639       C
ATOM   3992  CD2 LEU B 152     -39.146  71.646  19.783  1.00 30.63           C
ANISOU 3992  CD2 LEU B 152     3727   1692   6221    148    112    645       C
ATOM   3993  N   GLN B 153     -40.725  73.217  24.145  1.00 33.06           N
ANISOU 3993  N   GLN B 153     3908   2174   6480    197    113    997       N
ATOM   3994  CA  GLN B 153     -41.503  73.495  25.348  1.00 34.35           C
ANISOU 3994  CA  GLN B 153     4041   2413   6597    208     91   1084       C
ATOM   3995  C   GLN B 153     -42.691  72.545  25.424  1.00 35.40           C
ANISOU 3995  C   GLN B 153     4139   2668   6642    170     86   1058       C
ATOM   3996  O   GLN B 153     -43.558  72.580  24.541  1.00 34.96           O
ANISOU 3996  O   GLN B 153     4045   2664   6574    193     90    997       O
ATOM   3997  CB  GLN B 153     -41.974  74.944  25.352  1.00 38.50           C
ANISOU 3997  CB  GLN B 153     4539   2932   7158    301     74   1121       C
ATOM   3998  CG  GLN B 153     -40.841  75.948  25.228  1.00 41.39           C
ANISOU 3998  CG  GLN B 153     4948   3188   7589    353     81   1133       C
ATOM   3999  CD  GLN B 153     -39.720  75.678  26.212  1.00 40.93           C
ANISOU 3999  CD  GLN B 153     4943   3084   7523    297     71   1189       C
ATOM   4000  OE1 GLN B 153     -38.598  75.355  25.820  1.00 40.79           O
ANISOU 4000  OE1 GLN B 153     4974   2993   7530    260     80   1149       O
ATOM   4001  NE2 GLN B 153     -40.018  75.809  27.499  1.00 43.96           N
ANISOU 4001  NE2 GLN B 153     5320   3512   7872    292     46   1286       N
ATOM   4002  N   PRO B 154     -42.778  71.699  26.444  1.00 32.12           N
ANISOU 4002  N   PRO B 154     3740   2300   6163    122     81   1106       N
ATOM   4003  CA  PRO B 154     -43.797  70.647  26.450  1.00 33.55           C
ANISOU 4003  CA  PRO B 154     3906   2581   6259     88     79   1070       C
ATOM   4004  C   PRO B 154     -45.153  71.142  26.927  1.00 37.92           C
ANISOU 4004  C   PRO B 154     4440   3207   6762    120     25   1094       C
ATOM   4005  O   PRO B 154     -45.289  72.192  27.559  1.00 34.36           O
ANISOU 4005  O   PRO B 154     3985   2740   6330    160    -16   1160       O
ATOM   4006  CB  PRO B 154     -43.220  69.619  27.427  1.00 34.41           C
ANISOU 4006  CB  PRO B 154     4053   2702   6320     42    104   1123       C
ATOM   4007  CG  PRO B 154     -42.457  70.454  28.400  1.00 33.58           C
ANISOU 4007  CG  PRO B 154     3980   2535   6244     66     94   1220       C
ATOM   4008  CD  PRO B 154     -41.880  71.604  27.607  1.00 32.23           C
ANISOU 4008  CD  PRO B 154     3796   2273   6178    101     86   1198       C
ATOM   4009  N   SER B 155     -46.169  70.346  26.600  1.00 38.51           N
ANISOU 4009  N   SER B 155     4498   3357   6777     96     16   1043       N
ATOM   4010  CA  SER B 155     -47.515  70.506  27.132  1.00 33.65           C
ANISOU 4010  CA  SER B 155     3875   2807   6105    104    -51   1065       C
ATOM   4011  C   SER B 155     -47.928  69.177  27.742  1.00 31.14           C
ANISOU 4011  C   SER B 155     3610   2542   5681     69    -52   1051       C
ATOM   4012  O   SER B 155     -48.022  68.170  27.034  1.00 31.79           O
ANISOU 4012  O   SER B 155     3682   2651   5745     41    -12    986       O
ATOM   4013  CB  SER B 155     -48.503  70.933  26.044  1.00 32.91           C
ANISOU 4013  CB  SER B 155     3709   2747   6049    119    -66   1022       C
ATOM   4014  OG  SER B 155     -49.824  70.978  26.553  1.00 37.64           O
ANISOU 4014  OG  SER B 155     4298   3401   6603    110   -146   1048       O
ATOM   4015  N   VAL B 156     -48.159  69.171  29.053  1.00 31.13           N
ANISOU 4015  N   VAL B 156     3671   2552   5604     80    -98   1112       N
ATOM   4016  CA  VAL B 156     -48.505  67.936  29.748  1.00 34.96           C
ANISOU 4016  CA  VAL B 156     4228   3084   5973     68    -90   1104       C
ATOM   4017  C   VAL B 156     -49.935  67.554  29.394  1.00 41.33           C
ANISOU 4017  C   VAL B 156     5030   3940   6734     56   -150   1049       C
ATOM   4018  O   VAL B 156     -50.878  68.315  29.644  1.00 43.79           O
ANISOU 4018  O   VAL B 156     5335   4256   7047     62   -245   1069       O
ATOM   4019  CB  VAL B 156     -48.328  68.090  31.264  1.00 35.71           C
ANISOU 4019  CB  VAL B 156     4411   3173   5982     99   -122   1186       C
ATOM   4020  CG1 VAL B 156     -48.705  66.799  31.969  1.00 28.06           C
ANISOU 4020  CG1 VAL B 156     3531   2253   4879    109   -102   1176       C
ATOM   4021  CG2 VAL B 156     -46.896  68.481  31.592  1.00 35.53           C
ANISOU 4021  CG2 VAL B 156     4388   3098   6016    107    -61   1253       C
ATOM   4022  N   GLY B 157     -50.102  66.371  28.810  1.00 41.38           N
ANISOU 4022  N   GLY B 157     5035   3979   6708     36   -100    986       N
ATOM   4023  CA  GLY B 157     -51.401  65.904  28.396  1.00 25.55           C
ANISOU 4023  CA  GLY B 157     3029   2013   4666     21   -149    933       C
ATOM   4024  C   GLY B 157     -52.190  65.291  29.534  1.00 34.05           C
ANISOU 4024  C   GLY B 157     4215   3110   5612     38   -209    944       C
ATOM   4025  O   GLY B 157     -51.819  65.396  30.707  1.00 32.32           O
ANISOU 4025  O   GLY B 157     4075   2879   5325     69   -221    998       O
ATOM   4026  N   PRO B 158     -53.303  64.640  29.205  1.00 34.40           N
ANISOU 4026  N   PRO B 158     4277   3181   5615     25   -251    891       N
ATOM   4027  CA  PRO B 158     -54.131  64.023  30.245  1.00 28.85           C
ANISOU 4027  CA  PRO B 158     3701   2484   4779     49   -319    888       C
ATOM   4028  C   PRO B 158     -53.445  62.816  30.866  1.00 27.58           C
ANISOU 4028  C   PRO B 158     3620   2344   4514     92   -222    889       C
ATOM   4029  O   PRO B 158     -52.511  62.235  30.310  1.00 28.64           O
ANISOU 4029  O   PRO B 158     3696   2494   4690     86   -108    884       O
ATOM   4030  CB  PRO B 158     -55.402  63.614  29.492  1.00 25.57           C
ANISOU 4030  CB  PRO B 158     3266   2080   4368     18   -378    830       C
ATOM   4031  CG  PRO B 158     -54.960  63.452  28.077  1.00 24.71           C
ANISOU 4031  CG  PRO B 158     3038   1991   4359     -9   -286    793       C
ATOM   4032  CD  PRO B 158     -53.880  64.472  27.860  1.00 24.81           C
ANISOU 4032  CD  PRO B 158     2976   1983   4466     -8   -242    834       C
ATOM   4033  N   LYS B 159     -53.931  62.445  32.053  1.00 28.42           N
ANISOU 4033  N   LYS B 159     3868   2449   4483    139   -272    902       N
ATOM   4034  CA  LYS B 159     -53.370  61.294  32.751  1.00 29.38           C
ANISOU 4034  CA  LYS B 159     4076   2599   4490    201   -170    917       C
ATOM   4035  C   LYS B 159     -53.677  59.989  32.032  1.00 31.72           C
ANISOU 4035  C   LYS B 159     4356   2928   4767    204   -104    856       C
ATOM   4036  O   LYS B 159     -52.893  59.037  32.117  1.00 34.30           O
ANISOU 4036  O   LYS B 159     4676   3289   5066    238     20    878       O
ATOM   4037  CB  LYS B 159     -53.905  61.225  34.182  1.00 29.67           C
ANISOU 4037  CB  LYS B 159     4289   2622   4362    269   -243    939       C
ATOM   4038  CG  LYS B 159     -53.379  62.298  35.115  1.00 35.15           C
ANISOU 4038  CG  LYS B 159     5018   3291   5045    285   -287   1017       C
ATOM   4039  CD  LYS B 159     -53.878  62.062  36.533  1.00 46.53           C
ANISOU 4039  CD  LYS B 159     6659   4723   6297    365   -354   1033       C
ATOM   4040  CE  LYS B 159     -53.285  63.066  37.508  1.00 58.30           C
ANISOU 4040  CE  LYS B 159     8192   6193   7765    389   -391   1119       C
ATOM   4041  NZ  LYS B 159     -53.722  62.802  38.909  1.00 63.02           N
ANISOU 4041  NZ  LYS B 159     9004   6783   8159    478   -454   1134       N
ATOM   4042  N   GLN B 160     -54.801  59.922  31.328  1.00 29.40           N
ANISOU 4042  N   GLN B 160     4049   2627   4495    170   -183    791       N
ATOM   4043  CA  GLN B 160     -55.290  58.674  30.765  1.00 32.71           C
ANISOU 4043  CA  GLN B 160     4478   3072   4878    182   -140    733       C
ATOM   4044  C   GLN B 160     -55.036  58.608  29.264  1.00 31.85           C
ANISOU 4044  C   GLN B 160     4216   2981   4903    120    -90    699       C
ATOM   4045  O   GLN B 160     -54.894  59.626  28.582  1.00 30.10           O
ANISOU 4045  O   GLN B 160     3898   2744   4794     68   -120    705       O
ATOM   4046  CB  GLN B 160     -56.786  58.503  31.046  1.00 32.57           C
ANISOU 4046  CB  GLN B 160     4572   3025   4779    191   -270    684       C
ATOM   4047  CG  GLN B 160     -57.695  59.410  30.221  1.00 39.58           C
ANISOU 4047  CG  GLN B 160     5379   3884   5775    111   -387    663       C
ATOM   4048  CD  GLN B 160     -57.831  60.810  30.794  1.00 43.74           C
ANISOU 4048  CD  GLN B 160     5905   4376   6339     86   -499    714       C
ATOM   4049  OE1 GLN B 160     -56.976  61.275  31.546  1.00 46.74           O
ANISOU 4049  OE1 GLN B 160     6307   4756   6697    115   -469    765       O
ATOM   4050  NE2 GLN B 160     -58.918  61.488  30.441  1.00 44.82           N
ANISOU 4050  NE2 GLN B 160     6009   4483   6537     31   -630    710       N
ATOM   4051  N   ALA B 161     -54.981  57.377  28.760  1.00 31.36           N
ANISOU 4051  N   ALA B 161     4140   2953   4821    136    -12    667       N
ATOM   4052  CA  ALA B 161     -54.851  57.126  27.334  1.00 29.56           C
ANISOU 4052  CA  ALA B 161     3790   2744   4696     85     26    628       C
ATOM   4053  C   ALA B 161     -55.627  55.861  27.005  1.00 31.66           C
ANISOU 4053  C   ALA B 161     4094   3034   4901    111     38    579       C
ATOM   4054  O   ALA B 161     -56.078  55.135  27.894  1.00 34.89           O
ANISOU 4054  O   ALA B 161     4622   3444   5190    176     36    578       O
ATOM   4055  CB  ALA B 161     -53.383  57.003  26.914  1.00 27.81           C
ANISOU 4055  CB  ALA B 161     3473   2540   4555     67    130    660       C
ATOM   4056  N   SER B 162     -55.779  55.602  25.711  1.00 30.48           N
ANISOU 4056  N   SER B 162     3852   2900   4827     68     51    538       N
ATOM   4057  CA  SER B 162     -56.538  54.455  25.231  1.00 30.21           C
ANISOU 4057  CA  SER B 162     3841   2886   4752     87     58    493       C
ATOM   4058  C   SER B 162     -55.581  53.310  24.927  1.00 29.33           C
ANISOU 4058  C   SER B 162     3675   2821   4649    110    175    506       C
ATOM   4059  O   SER B 162     -54.643  53.472  24.140  1.00 33.85           O
ANISOU 4059  O   SER B 162     4140   3406   5316     66    219    514       O
ATOM   4060  CB  SER B 162     -57.351  54.820  23.990  1.00 29.39           C
ANISOU 4060  CB  SER B 162     3670   2775   4721     30     -1    451       C
ATOM   4061  OG  SER B 162     -58.036  53.689  23.483  1.00 35.66           O
ANISOU 4061  OG  SER B 162     4483   3587   5480     48      8    412       O
ATOM   4062  N   LEU B 163     -55.817  52.161  25.551  1.00 29.00           N
ANISOU 4062  N   LEU B 163     3710   2800   4510    183    219    511       N
ATOM   4063  CA  LEU B 163     -55.044  50.948  25.303  1.00 32.04           C
ANISOU 4063  CA  LEU B 163     4035   3236   4904    214    329    537       C
ATOM   4064  C   LEU B 163     -56.005  49.879  24.794  1.00 33.66           C
ANISOU 4064  C   LEU B 163     4270   3455   5065    247    322    488       C
ATOM   4065  O   LEU B 163     -56.752  49.286  25.579  1.00 37.56           O
ANISOU 4065  O   LEU B 163     4888   3940   5444    327    315    478       O
ATOM   4066  CB  LEU B 163     -54.315  50.487  26.560  1.00 34.03           C
ANISOU 4066  CB  LEU B 163     4340   3512   5080    291    417    610       C
ATOM   4067  CG  LEU B 163     -53.547  49.173  26.407  1.00 34.39           C
ANISOU 4067  CG  LEU B 163     4311   3617   5141    331    538    660       C
ATOM   4068  CD1 LEU B 163     -52.498  49.291  25.312  1.00 31.33           C
ANISOU 4068  CD1 LEU B 163     3760   3241   4904    238    558    677       C
ATOM   4069  CD2 LEU B 163     -52.909  48.757  27.721  1.00 34.44           C
ANISOU 4069  CD2 LEU B 163     4371   3651   5064    421    637    750       C
ATOM   4070  N   ASN B 164     -55.984  49.643  23.481  1.00 29.47           N
ANISOU 4070  N   ASN B 164     3637   2941   4619    192    319    457       N
ATOM   4071  CA  ASN B 164     -56.839  48.640  22.843  1.00 30.80           C
ANISOU 4071  CA  ASN B 164     3818   3124   4761    217    311    416       C
ATOM   4072  C   ASN B 164     -58.315  48.910  23.129  1.00 36.94           C
ANISOU 4072  C   ASN B 164     4716   3850   5469    232    211    370       C
ATOM   4073  O   ASN B 164     -59.082  48.002  23.454  1.00 42.40           O
ANISOU 4073  O   ASN B 164     5500   4534   6077    300    209    351       O
ATOM   4074  CB  ASN B 164     -56.452  47.226  23.279  1.00 30.98           C
ANISOU 4074  CB  ASN B 164     3848   3194   4731    304    412    455       C
ATOM   4075  CG  ASN B 164     -54.986  46.931  23.050  1.00 34.29           C
ANISOU 4075  CG  ASN B 164     4135   3658   5235    279    500    519       C
ATOM   4076  OD1 ASN B 164     -54.423  47.287  22.015  1.00 39.13           O
ANISOU 4076  OD1 ASN B 164     4640   4273   5953    195    479    507       O
ATOM   4077  ND2 ASN B 164     -54.354  46.285  24.023  1.00 34.31           N
ANISOU 4077  ND2 ASN B 164     4151   3694   5190    353    595    592       N
ATOM   4078  N   GLY B 165     -58.714  50.173  23.010  1.00 34.78           N
ANISOU 4078  N   GLY B 165     4441   3537   5236    168    124    358       N
ATOM   4079  CA  GLY B 165     -60.079  50.569  23.270  1.00 28.39           C
ANISOU 4079  CA  GLY B 165     3729   2673   4386    161      9    329       C
ATOM   4080  C   GLY B 165     -60.421  50.780  24.725  1.00 28.04           C
ANISOU 4080  C   GLY B 165     3833   2586   4236    215    -40    339       C
ATOM   4081  O   GLY B 165     -61.563  51.149  25.026  1.00 34.71           O
ANISOU 4081  O   GLY B 165     4769   3370   5048    202   -159    317       O
ATOM   4082  N   VAL B 166     -59.477  50.564  25.636  1.00 28.79           N
ANISOU 4082  N   VAL B 166     3958   2705   4276    274     41    376       N
ATOM   4083  CA  VAL B 166     -59.703  50.724  27.067  1.00 30.19           C
ANISOU 4083  CA  VAL B 166     4292   2847   4333    342      5    389       C
ATOM   4084  C   VAL B 166     -58.988  51.989  27.518  1.00 27.27           C
ANISOU 4084  C   VAL B 166     3884   2472   4007    298    -14    433       C
ATOM   4085  O   VAL B 166     -57.754  52.067  27.467  1.00 31.91           O
ANISOU 4085  O   VAL B 166     4379   3101   4645    293     85    479       O
ATOM   4086  CB  VAL B 166     -59.214  49.502  27.858  1.00 34.80           C
ANISOU 4086  CB  VAL B 166     4952   3467   4802    463    123    412       C
ATOM   4087  CG1 VAL B 166     -59.579  49.645  29.328  1.00 36.78           C
ANISOU 4087  CG1 VAL B 166     5397   3676   4902    548     78    417       C
ATOM   4088  CG2 VAL B 166     -59.797  48.225  27.275  1.00 25.09           C
ANISOU 4088  CG2 VAL B 166     3735   2249   3547    510    156    376       C
ATOM   4089  N   THR B 167     -59.762  52.979  27.952  1.00 26.06           N
ANISOU 4089  N   THR B 167     3798   2261   3844    264   -148    425       N
ATOM   4090  CA  THR B 167     -59.197  54.215  28.472  1.00 32.19           C
ANISOU 4090  CA  THR B 167     4550   3026   4656    232   -180    471       C
ATOM   4091  C   THR B 167     -58.847  54.037  29.944  1.00 35.15           C
ANISOU 4091  C   THR B 167     5069   3394   4892    322   -159    502       C
ATOM   4092  O   THR B 167     -59.700  53.652  30.751  1.00 36.09           O
ANISOU 4092  O   THR B 167     5357   3472   4882    384   -231    473       O
ATOM   4093  CB  THR B 167     -60.182  55.369  28.293  1.00 35.27           C
ANISOU 4093  CB  THR B 167     4934   3363   5105    157   -336    464       C
ATOM   4094  OG1 THR B 167     -60.480  55.528  26.901  1.00 44.64           O
ANISOU 4094  OG1 THR B 167     5983   4564   6413     86   -336    446       O
ATOM   4095  CG2 THR B 167     -59.590  56.660  28.829  1.00 28.04           C
ANISOU 4095  CG2 THR B 167     3986   2437   4230    132   -369    518       C
ATOM   4096  N   LEU B 168     -57.595  54.323  30.294  1.00 33.45           N
ANISOU 4096  N   LEU B 168     4798   3214   4699    334    -65    562       N
ATOM   4097  CA  LEU B 168     -57.113  54.023  31.633  1.00 35.66           C
ANISOU 4097  CA  LEU B 168     5203   3502   4844    431    -11    608       C
ATOM   4098  C   LEU B 168     -55.940  54.929  31.979  1.00 34.31           C
ANISOU 4098  C   LEU B 168     4960   3344   4734    405     32    683       C
ATOM   4099  O   LEU B 168     -55.230  55.416  31.096  1.00 33.26           O
ANISOU 4099  O   LEU B 168     4670   3223   4744    329     67    698       O
ATOM   4100  CB  LEU B 168     -56.697  52.551  31.745  1.00 40.28           C
ANISOU 4100  CB  LEU B 168     5807   4141   5357    523    136    621       C
ATOM   4101  CG  LEU B 168     -55.765  52.031  30.642  1.00 38.13           C
ANISOU 4101  CG  LEU B 168     5346   3924   5217    476    255    644       C
ATOM   4102  CD1 LEU B 168     -54.295  52.209  31.005  1.00 37.02           C
ANISOU 4102  CD1 LEU B 168     5122   3820   5123    477    367    737       C
ATOM   4103  CD2 LEU B 168     -56.066  50.576  30.316  1.00 36.64           C
ANISOU 4103  CD2 LEU B 168     5169   3772   4982    542    332    621       C
ATOM   4104  N   ILE B 169     -55.747  55.138  33.277  1.00 33.14           N
ANISOU 4104  N   ILE B 169     4941   3186   4466    476     27    727       N
ATOM   4105  CA  ILE B 169     -54.543  55.774  33.799  1.00 33.59           C
ANISOU 4105  CA  ILE B 169     4950   3257   4554    476     92    814       C
ATOM   4106  C   ILE B 169     -53.562  54.656  34.129  1.00 38.78           C
ANISOU 4106  C   ILE B 169     5593   3975   5166    552    269    878       C
ATOM   4107  O   ILE B 169     -53.762  53.903  35.086  1.00 43.74           O
ANISOU 4107  O   ILE B 169     6364   4622   5634    666    317    896       O
ATOM   4108  CB  ILE B 169     -54.843  56.637  35.029  1.00 35.52           C
ANISOU 4108  CB  ILE B 169     5340   3462   4695    512    -12    840       C
ATOM   4109  CG1 ILE B 169     -55.853  57.730  34.675  1.00 37.50           C
ANISOU 4109  CG1 ILE B 169     5584   3655   5010    430   -196    792       C
ATOM   4110  CG2 ILE B 169     -53.560  57.245  35.571  1.00 31.09           C
ANISOU 4110  CG2 ILE B 169     4731   2915   4166    516     64    939       C
ATOM   4111  CD1 ILE B 169     -56.222  58.615  35.842  1.00 41.94           C
ANISOU 4111  CD1 ILE B 169     6283   4172   5480    456   -326    819       C
ATOM   4112  N   GLY B 170     -52.505  54.545  33.332  1.00 36.78           N
ANISOU 4112  N   GLY B 170     5168   3751   5055    492    365    918       N
ATOM   4113  CA  GLY B 170     -51.650  53.378  33.405  1.00 38.71           C
ANISOU 4113  CA  GLY B 170     5359   4056   5292    544    525    984       C
ATOM   4114  C   GLY B 170     -50.875  53.288  34.706  1.00 41.22           C
ANISOU 4114  C   GLY B 170     5750   4400   5512    632    619   1094       C
ATOM   4115  O   GLY B 170     -50.468  54.290  35.296  1.00 39.15           O
ANISOU 4115  O   GLY B 170     5514   4109   5254    616    581   1140       O
ATOM   4116  N   GLU B 171     -50.675  52.050  35.155  1.00 40.06           N
ANISOU 4116  N   GLU B 171     5634   4311   5275    736    751   1145       N
ATOM   4117  CA  GLU B 171     -49.821  51.738  36.294  1.00 40.03           C
ANISOU 4117  CA  GLU B 171     5673   4350   5185    832    881   1274       C
ATOM   4118  C   GLU B 171     -48.627  50.891  35.889  1.00 41.30           C
ANISOU 4118  C   GLU B 171     5656   4572   5464    815   1039   1382       C
ATOM   4119  O   GLU B 171     -47.489  51.217  36.246  1.00 43.50           O
ANISOU 4119  O   GLU B 171     5859   4859   5810    790   1109   1499       O
ATOM   4120  CB  GLU B 171     -50.632  51.018  37.383  1.00 46.31           C
ANISOU 4120  CB  GLU B 171     6683   5165   5746    998    911   1262       C
ATOM   4121  CG  GLU B 171     -51.855  51.785  37.855  1.00 53.72           C
ANISOU 4121  CG  GLU B 171     7815   6034   6563   1013    733   1158       C
ATOM   4122  CD  GLU B 171     -52.655  51.019  38.892  1.00 63.66           C
ANISOU 4122  CD  GLU B 171     9308   7298   7581   1183    751   1135       C
ATOM   4123  OE1 GLU B 171     -52.160  49.979  39.376  1.00 66.83           O
ANISOU 4123  OE1 GLU B 171     9726   7767   7898   1307    923   1216       O
ATOM   4124  OE2 GLU B 171     -53.778  51.456  39.220  1.00 66.05           O
ANISOU 4124  OE2 GLU B 171     9782   7534   7780   1196    589   1039       O
ATOM   4125  N   ALA B 172     -48.857  49.804  35.152  1.00 39.81           N
ANISOU 4125  N   ALA B 172     5395   4422   5308    825   1090   1353       N
ATOM   4126  CA  ALA B 172     -47.772  49.033  34.560  1.00 43.09           C
ANISOU 4126  CA  ALA B 172     5615   4888   5869    783   1208   1450       C
ATOM   4127  C   ALA B 172     -47.262  49.647  33.265  1.00 40.10           C
ANISOU 4127  C   ALA B 172     5072   4465   5701    614   1124   1408       C
ATOM   4128  O   ALA B 172     -46.250  49.182  32.731  1.00 42.55           O
ANISOU 4128  O   ALA B 172     5216   4798   6152    553   1191   1488       O
ATOM   4129  CB  ALA B 172     -48.228  47.594  34.305  1.00 44.04           C
ANISOU 4129  CB  ALA B 172     5723   5070   5939    871   1294   1442       C
ATOM   4130  N   VAL B 173     -47.942  50.672  32.751  1.00 38.64           N
ANISOU 4130  N   VAL B 173     4931   4215   5537    541    977   1290       N
ATOM   4131  CA  VAL B 173     -47.534  51.387  31.550  1.00 42.94           C
ANISOU 4131  CA  VAL B 173     5348   4711   6257    400    896   1241       C
ATOM   4132  C   VAL B 173     -47.834  52.864  31.773  1.00 43.10           C
ANISOU 4132  C   VAL B 173     5440   4664   6271    362    781   1194       C
ATOM   4133  O   VAL B 173     -48.614  53.235  32.652  1.00 48.11           O
ANISOU 4133  O   VAL B 173     6222   5289   6770    430    735   1172       O
ATOM   4134  CB  VAL B 173     -48.255  50.859  30.287  1.00 48.16           C
ANISOU 4134  CB  VAL B 173     5956   5377   6965    359    844   1133       C
ATOM   4135  CG1 VAL B 173     -49.699  51.346  30.249  1.00 44.96           C
ANISOU 4135  CG1 VAL B 173     5678   4939   6464    379    730   1015       C
ATOM   4136  CG2 VAL B 173     -47.499  51.246  29.020  1.00 54.49           C
ANISOU 4136  CG2 VAL B 173     6609   6145   7948    231    801   1113       C
ATOM   4137  N   LYS B 174     -47.192  53.715  30.979  1.00 40.40           N
ANISOU 4137  N   LYS B 174     5000   4272   6078    255    729   1181       N
ATOM   4138  CA  LYS B 174     -47.349  55.157  31.107  1.00 42.85           C
ANISOU 4138  CA  LYS B 174     5354   4521   6407    220    630   1151       C
ATOM   4139  C   LYS B 174     -48.349  55.660  30.074  1.00 38.33           C
ANISOU 4139  C   LYS B 174     4775   3921   5868    172    520   1027       C
ATOM   4140  O   LYS B 174     -48.200  55.393  28.877  1.00 36.07           O
ANISOU 4140  O   LYS B 174     4392   3633   5679    112    515    979       O
ATOM   4141  CB  LYS B 174     -46.005  55.870  30.947  1.00 49.16           C
ANISOU 4141  CB  LYS B 174     6063   5274   7343    150    646   1221       C
ATOM   4142  CG  LYS B 174     -45.956  57.236  31.614  1.00 56.73           C
ANISOU 4142  CG  LYS B 174     7086   6179   8288    153    582   1242       C
ATOM   4143  CD  LYS B 174     -44.529  57.642  31.948  1.00 60.65           C
ANISOU 4143  CD  LYS B 174     7526   6638   8879    118    633   1352       C
ATOM   4144  CE  LYS B 174     -44.022  58.719  31.008  1.00 64.10           C
ANISOU 4144  CE  LYS B 174     7895   6995   9463     34    561   1310       C
ATOM   4145  NZ  LYS B 174     -44.827  59.968  31.110  1.00 66.61           N
ANISOU 4145  NZ  LYS B 174     8279   7280   9750     49    460   1252       N
ATOM   4146  N   THR B 175     -49.366  56.384  30.543  1.00 37.69           N
ANISOU 4146  N   THR B 175     4796   3820   5706    199    428    984       N
ATOM   4147  CA  THR B 175     -50.411  56.923  29.683  1.00 32.52           C
ANISOU 4147  CA  THR B 175     4133   3142   5081    158    323    888       C
ATOM   4148  C   THR B 175     -50.412  58.445  29.620  1.00 34.19           C
ANISOU 4148  C   THR B 175     4330   3301   5358    118    237    888       C
ATOM   4149  O   THR B 175     -51.212  59.018  28.873  1.00 36.90           O
ANISOU 4149  O   THR B 175     4647   3628   5743     84    158    827       O
ATOM   4150  CB  THR B 175     -51.789  56.431  30.147  1.00 26.62           C
ANISOU 4150  CB  THR B 175     3505   2408   4200    215    267    839       C
ATOM   4151  OG1 THR B 175     -51.991  56.784  31.521  1.00 27.24           O
ANISOU 4151  OG1 THR B 175     3715   2474   4160    278    236    882       O
ATOM   4152  CG2 THR B 175     -51.899  54.923  29.994  1.00 25.82           C
ANISOU 4152  CG2 THR B 175     3410   2357   4045    261    351    828       C
ATOM   4153  N   GLN B 176     -49.547  59.114  30.377  1.00 35.73           N
ANISOU 4153  N   GLN B 176     4536   3472   5566    126    256    964       N
ATOM   4154  CA  GLN B 176     -49.450  60.568  30.360  1.00 33.77           C
ANISOU 4154  CA  GLN B 176     4270   3173   5386     99    182    975       C
ATOM   4155  C   GLN B 176     -48.264  60.974  29.493  1.00 35.38           C
ANISOU 4155  C   GLN B 176     4366   3342   5735     45    226    987       C
ATOM   4156  O   GLN B 176     -47.136  60.528  29.730  1.00 36.86           O
ANISOU 4156  O   GLN B 176     4527   3525   5952     38    305   1048       O
ATOM   4157  CB  GLN B 176     -49.303  61.124  31.775  1.00 37.61           C
ANISOU 4157  CB  GLN B 176     4853   3647   5791    148    159   1051       C
ATOM   4158  CG  GLN B 176     -49.305  62.642  31.838  1.00 37.21           C
ANISOU 4158  CG  GLN B 176     4785   3547   5806    128     73   1070       C
ATOM   4159  CD  GLN B 176     -49.675  63.164  33.210  1.00 43.51           C
ANISOU 4159  CD  GLN B 176     5700   4337   6496    179      5   1124       C
ATOM   4160  OE1 GLN B 176     -49.301  62.586  34.231  1.00 49.49           O
ANISOU 4160  OE1 GLN B 176     6543   5113   7146    234     60   1180       O
ATOM   4161  NE2 GLN B 176     -50.425  64.259  33.242  1.00 45.85           N
ANISOU 4161  NE2 GLN B 176     5999   4606   6816    167   -115   1115       N
ATOM   4162  N   PHE B 177     -48.519  61.817  28.496  1.00 36.99           N
ANISOU 4162  N   PHE B 177     4511   3517   6027     10    173    934       N
ATOM   4163  CA  PHE B 177     -47.502  62.215  27.537  1.00 36.84           C
ANISOU 4163  CA  PHE B 177     4411   3453   6133    -32    202    924       C
ATOM   4164  C   PHE B 177     -47.310  63.724  27.546  1.00 34.31           C
ANISOU 4164  C   PHE B 177     4082   3077   5879    -27    152    944       C
ATOM   4165  O   PHE B 177     -48.161  64.484  28.016  1.00 34.55           O
ANISOU 4165  O   PHE B 177     4140   3112   5874     -1     85    954       O
ATOM   4166  CB  PHE B 177     -47.866  61.778  26.111  1.00 35.09           C
ANISOU 4166  CB  PHE B 177     4131   3247   5956    -63    202    836       C
ATOM   4167  CG  PHE B 177     -48.406  60.384  26.018  1.00 34.41           C
ANISOU 4167  CG  PHE B 177     4053   3220   5800    -60    232    807       C
ATOM   4168  CD1 PHE B 177     -47.603  59.295  26.304  1.00 33.85           C
ANISOU 4168  CD1 PHE B 177     3970   3170   5723    -64    305    848       C
ATOM   4169  CD2 PHE B 177     -49.717  60.163  25.625  1.00 32.72           C
ANISOU 4169  CD2 PHE B 177     3854   3040   5536    -50    187    748       C
ATOM   4170  CE1 PHE B 177     -48.100  58.009  26.212  1.00 37.54           C
ANISOU 4170  CE1 PHE B 177     4441   3693   6128    -49    339    828       C
ATOM   4171  CE2 PHE B 177     -50.220  58.881  25.529  1.00 29.95           C
ANISOU 4171  CE2 PHE B 177     3518   2738   5123    -40    214    720       C
ATOM   4172  CZ  PHE B 177     -49.411  57.802  25.823  1.00 33.05           C
ANISOU 4172  CZ  PHE B 177     3901   3154   5504    -34    292    759       C
ATOM   4173  N   ASN B 178     -46.165  64.145  27.019  1.00 32.86           N
ANISOU 4173  N   ASN B 178     3856   2833   5794    -50    180    953       N
ATOM   4174  CA  ASN B 178     -45.988  65.520  26.590  1.00 33.42           C
ANISOU 4174  CA  ASN B 178     3905   2847   5944    -37    144    948       C
ATOM   4175  C   ASN B 178     -46.539  65.678  25.180  1.00 34.34           C
ANISOU 4175  C   ASN B 178     3975   2972   6101    -42    131    860       C
ATOM   4176  O   ASN B 178     -46.489  64.753  24.366  1.00 34.44           O
ANISOU 4176  O   ASN B 178     3967   3004   6114    -70    158    804       O
ATOM   4177  CB  ASN B 178     -44.512  65.919  26.621  1.00 35.79           C
ANISOU 4177  CB  ASN B 178     4202   3066   6332    -53    173    992       C
ATOM   4178  CG  ASN B 178     -43.940  65.934  28.022  1.00 33.49           C
ANISOU 4178  CG  ASN B 178     3953   2764   6006    -42    190   1097       C
ATOM   4179  OD1 ASN B 178     -44.659  66.151  28.996  1.00 33.53           O
ANISOU 4179  OD1 ASN B 178     4004   2808   5927     -6    160   1136       O
ATOM   4180  ND2 ASN B 178     -42.637  65.707  28.131  1.00 30.62           N
ANISOU 4180  ND2 ASN B 178     3582   2346   5708    -74    232   1149       N
ATOM   4181  N   TYR B 179     -47.078  66.857  24.895  1.00 31.99           N
ANISOU 4181  N   TYR B 179     3657   2662   5836     -8     92    857       N
ATOM   4182  CA  TYR B 179     -47.680  67.134  23.601  1.00 27.83           C
ANISOU 4182  CA  TYR B 179     3085   2150   5340      4     91    790       C
ATOM   4183  C   TYR B 179     -46.962  68.295  22.930  1.00 26.46           C
ANISOU 4183  C   TYR B 179     2895   1907   5251     42    104    785       C
ATOM   4184  O   TYR B 179     -46.559  69.256  23.592  1.00 32.15           O
ANISOU 4184  O   TYR B 179     3625   2584   6006     72     88    846       O
ATOM   4185  CB  TYR B 179     -49.172  67.441  23.742  1.00 26.83           C
ANISOU 4185  CB  TYR B 179     2936   2083   5177     18     38    800       C
ATOM   4186  CG  TYR B 179     -50.027  66.207  23.911  1.00 33.06           C
ANISOU 4186  CG  TYR B 179     3745   2932   5883    -12     26    771       C
ATOM   4187  CD1 TYR B 179     -50.093  65.544  25.129  1.00 32.76           C
ANISOU 4187  CD1 TYR B 179     3770   2910   5768    -20     11    806       C
ATOM   4188  CD2 TYR B 179     -50.768  65.701  22.850  1.00 40.05           C
ANISOU 4188  CD2 TYR B 179     4597   3856   6763    -23     33    711       C
ATOM   4189  CE1 TYR B 179     -50.872  64.412  25.286  1.00 35.30           C
ANISOU 4189  CE1 TYR B 179     4124   3279   6008    -32      3    777       C
ATOM   4190  CE2 TYR B 179     -51.552  64.571  22.998  1.00 43.10           C
ANISOU 4190  CE2 TYR B 179     5008   4290   7077    -46     21    686       C
ATOM   4191  CZ  TYR B 179     -51.600  63.931  24.218  1.00 41.86           C
ANISOU 4191  CZ  TYR B 179     4919   4143   6845    -48      5    716       C
ATOM   4192  OH  TYR B 179     -52.378  62.806  24.371  1.00 42.41           O
ANISOU 4192  OH  TYR B 179     5025   4252   6837    -55     -4    687       O
ATOM   4193  N   TYR B 180     -46.800  68.189  21.613  1.00 29.82           N
ANISOU 4193  N   TYR B 180     3307   2320   5703     50    131    712       N
ATOM   4194  CA  TYR B 180     -46.147  69.210  20.809  1.00 32.09           C
ANISOU 4194  CA  TYR B 180     3599   2537   6055    102    149    690       C
ATOM   4195  C   TYR B 180     -46.891  69.334  19.488  1.00 33.09           C
ANISOU 4195  C   TYR B 180     3697   2704   6172    141    170    628       C
ATOM   4196  O   TYR B 180     -47.413  68.348  18.963  1.00 32.37           O
ANISOU 4196  O   TYR B 180     3596   2666   6036    106    175    581       O
ATOM   4197  CB  TYR B 180     -44.670  68.872  20.555  1.00 29.76           C
ANISOU 4197  CB  TYR B 180     3355   2151   5802     73    161    662       C
ATOM   4198  CG  TYR B 180     -43.918  68.421  21.789  1.00 29.82           C
ANISOU 4198  CG  TYR B 180     3382   2132   5815     22    153    731       C
ATOM   4199  CD1 TYR B 180     -43.902  67.085  22.167  1.00 29.37           C
ANISOU 4199  CD1 TYR B 180     3320   2122   5718    -42    162    737       C
ATOM   4200  CD2 TYR B 180     -43.222  69.331  22.573  1.00 32.81           C
ANISOU 4200  CD2 TYR B 180     3784   2443   6240     45    145    800       C
ATOM   4201  CE1 TYR B 180     -43.219  66.668  23.291  1.00 26.55           C
ANISOU 4201  CE1 TYR B 180     2977   1749   5361    -77    172    815       C
ATOM   4202  CE2 TYR B 180     -42.532  68.922  23.699  1.00 34.16           C
ANISOU 4202  CE2 TYR B 180     3973   2594   6412      3    146    876       C
ATOM   4203  CZ  TYR B 180     -42.536  67.590  24.054  1.00 31.46           C
ANISOU 4203  CZ  TYR B 180     3623   2305   6025    -56    164    886       C
ATOM   4204  OH  TYR B 180     -41.852  67.178  25.174  1.00 30.28           O
ANISOU 4204  OH  TYR B 180     3488   2144   5873    -86    182    975       O
ATOM   4205  N   LYS B 181     -46.937  70.552  18.952  1.00 34.25           N
ANISOU 4205  N   LYS B 181     3829   2825   6359    222    190    636       N
ATOM   4206  CA  LYS B 181     -47.679  70.817  17.728  1.00 31.54           C
ANISOU 4206  CA  LYS B 181     3455   2526   6004    277    224    598       C
ATOM   4207  C   LYS B 181     -46.936  71.828  16.868  1.00 30.01           C
ANISOU 4207  C   LYS B 181     3299   2259   5846    373    266    569       C
ATOM   4208  O   LYS B 181     -46.406  72.820  17.376  1.00 29.21           O
ANISOU 4208  O   LYS B 181     3206   2098   5795    420    265    617       O
ATOM   4209  CB  LYS B 181     -49.091  71.336  18.033  1.00 33.22           C
ANISOU 4209  CB  LYS B 181     3580   2822   6218    296    210    670       C
ATOM   4210  CG  LYS B 181     -49.945  71.566  16.797  1.00 35.84           C
ANISOU 4210  CG  LYS B 181     3864   3212   6542    351    255    652       C
ATOM   4211  CD  LYS B 181     -51.291  72.170  17.155  1.00 43.13           C
ANISOU 4211  CD  LYS B 181     4686   4208   7492    359    231    746       C
ATOM   4212  CE  LYS B 181     -52.147  72.378  15.915  1.00 51.13           C
ANISOU 4212  CE  LYS B 181     5640   5284   8503    413    286    748       C
ATOM   4213  NZ  LYS B 181     -53.449  73.028  16.233  1.00 58.97           N
ANISOU 4213  NZ  LYS B 181     6517   6343   9546    414    256    858       N
ATOM   4214  N   LYS B 182     -46.907  71.569  15.563  1.00 32.49           N
ANISOU 4214  N   LYS B 182     3644   2573   6127    408    301    489       N
ATOM   4215  CA  LYS B 182     -46.324  72.473  14.583  1.00 30.45           C
ANISOU 4215  CA  LYS B 182     3442   2249   5878    519    347    448       C
ATOM   4216  C   LYS B 182     -47.369  72.824  13.536  1.00 31.26           C
ANISOU 4216  C   LYS B 182     3497   2433   5945    603    408    448       C
ATOM   4217  O   LYS B 182     -48.128  71.958  13.091  1.00 30.72           O
ANISOU 4217  O   LYS B 182     3400   2441   5829    558    409    425       O
ATOM   4218  CB  LYS B 182     -45.104  71.852  13.897  1.00 33.96           C
ANISOU 4218  CB  LYS B 182     4002   2596   6306    496    325    345       C
ATOM   4219  CG  LYS B 182     -43.881  71.728  14.781  1.00 44.73           C
ANISOU 4219  CG  LYS B 182     5415   3856   7724    431    273    357       C
ATOM   4220  CD  LYS B 182     -42.740  71.054  14.037  1.00 45.07           C
ANISOU 4220  CD  LYS B 182     5562   3800   7763    392    233    262       C
ATOM   4221  CE  LYS B 182     -42.324  71.863  12.821  1.00 39.47           C
ANISOU 4221  CE  LYS B 182     4952   3014   7032    513    257    186       C
ATOM   4222  NZ  LYS B 182     -41.300  71.153  12.005  1.00 33.97           N
ANISOU 4222  NZ  LYS B 182     4368   2217   6323    470    195     84       N
ATOM   4223  N   VAL B 183     -47.403  74.095  13.148  1.00 34.50           N
ANISOU 4223  N   VAL B 183     3898   2830   6382    731    466    484       N
ATOM   4224  CA  VAL B 183     -48.281  74.579  12.091  1.00 34.13           C
ANISOU 4224  CA  VAL B 183     3806   2858   6305    835    545    500       C
ATOM   4225  C   VAL B 183     -47.437  75.401  11.129  1.00 38.88           C
ANISOU 4225  C   VAL B 183     4512   3377   6885    981    608    443       C
ATOM   4226  O   VAL B 183     -46.860  76.422  11.523  1.00 44.73           O
ANISOU 4226  O   VAL B 183     5268   4049   7677   1056    622    480       O
ATOM   4227  CB  VAL B 183     -49.447  75.418  12.641  1.00 35.99           C
ANISOU 4227  CB  VAL B 183     3892   3182   6599    863    565    637       C
ATOM   4228  CG1 VAL B 183     -50.250  76.017  11.499  1.00 34.35           C
ANISOU 4228  CG1 VAL B 183     3629   3050   6374    985    663    673       C
ATOM   4229  CG2 VAL B 183     -50.341  74.567  13.527  1.00 32.63           C
ANISOU 4229  CG2 VAL B 183     3389   2828   6182    724    490    680       C
ATOM   4230  N   ASP B 184     -47.360  74.952   9.875  1.00 39.89           N
ANISOU 4230  N   ASP B 184     4698   3448   7012     34    322    474       N
ATOM   4231  CA  ASP B 184     -46.595  75.635   8.829  1.00 42.95           C
ANISOU 4231  CA  ASP B 184     5153   3796   7369     32    403    382       C
ATOM   4232  C   ASP B 184     -45.123  75.771   9.213  1.00 40.70           C
ANISOU 4232  C   ASP B 184     5032   3408   7024    109    259    431       C
ATOM   4233  O   ASP B 184     -44.499  76.813   9.004  1.00 41.84           O
ANISOU 4233  O   ASP B 184     5214   3471   7215    221    234    309       O
ATOM   4234  CB  ASP B 184     -47.202  77.002   8.502  1.00 48.56           C
ANISOU 4234  CB  ASP B 184     5664   4548   8237     93    514    127       C
ATOM   4235  CG  ASP B 184     -48.646  76.903   8.048  1.00 52.47           C
ANISOU 4235  CG  ASP B 184     6049   5146   8742    -83    718     42       C
ATOM   4236  OD1 ASP B 184     -49.022  75.854   7.483  1.00 50.66           O
ANISOU 4236  OD1 ASP B 184     6004   4898   8348   -253    789    193       O
ATOM   4237  OD2 ASP B 184     -49.404  77.874   8.256  1.00 55.21           O
ANISOU 4237  OD2 ASP B 184     6146   5586   9246    -55    794   -201       O
ATOM   4238  N   GLY B 185     -44.562  74.704   9.780  1.00 38.50           N
ANISOU 4238  N   GLY B 185     4868   3132   6626     32    170    577       N
ATOM   4239  CA  GLY B 185     -43.168  74.682  10.164  1.00 33.27           C
ANISOU 4239  CA  GLY B 185     4420   2375   5845      2     77    612       C
ATOM   4240  C   GLY B 185     -42.829  75.437  11.430  1.00 32.07           C
ANISOU 4240  C   GLY B 185     4386   2078   5722    120    -92    593       C
ATOM   4241  O   GLY B 185     -41.650  75.485  11.802  1.00 44.22           O
ANISOU 4241  O   GLY B 185     6208   3485   7110     55   -167    621       O
ATOM   4242  N   VAL B 186     -43.813  76.022  12.106  1.00 32.34           N
ANISOU 4242  N   VAL B 186     4257   2115   5914    272   -164    536       N
ATOM   4243  CA  VAL B 186     -43.594  76.799  13.320  1.00 37.79           C
ANISOU 4243  CA  VAL B 186     5087   2645   6626    430   -385    504       C
ATOM   4244  C   VAL B 186     -44.243  76.068  14.486  1.00 37.34           C
ANISOU 4244  C   VAL B 186     4975   2647   6564    355   -436    595       C
ATOM   4245  O   VAL B 186     -45.420  75.696  14.417  1.00 39.09           O
ANISOU 4245  O   VAL B 186     4926   3025   6903    341   -344    590       O
ATOM   4246  CB  VAL B 186     -44.156  78.225  13.186  1.00 40.60           C
ANISOU 4246  CB  VAL B 186     5267   2973   7188    714   -474    290       C
ATOM   4247  CG1 VAL B 186     -43.872  79.029  14.447  1.00 37.36           C
ANISOU 4247  CG1 VAL B 186     5056   2360   6779    937   -788    243       C
ATOM   4248  CG2 VAL B 186     -43.569  78.912  11.963  1.00 42.11           C
ANISOU 4248  CG2 VAL B 186     5477   3129   7394    776   -389    161       C
ATOM   4249  N   VAL B 187     -43.475  75.864  15.556  1.00 37.43           N
ANISOU 4249  N   VAL B 187     5290   2517   6414    275   -568    669       N
ATOM   4250  CA  VAL B 187     -43.999  75.197  16.741  1.00 33.50           C
ANISOU 4250  CA  VAL B 187     4774   2064   5889    179   -609    736       C
ATOM   4251  C   VAL B 187     -45.008  76.104  17.430  1.00 40.09           C
ANISOU 4251  C   VAL B 187     5468   2865   6898    417   -772    663       C
ATOM   4252  O   VAL B 187     -44.721  77.272  17.722  1.00 51.18           O
ANISOU 4252  O   VAL B 187     7024   4091   8330    645   -989    572       O
ATOM   4253  CB  VAL B 187     -42.857  74.815  17.693  1.00 33.27           C
ANISOU 4253  CB  VAL B 187     5165   1880   5596    -36   -675    798       C
ATOM   4254  CG1 VAL B 187     -43.410  74.172  18.956  1.00 32.83           C
ANISOU 4254  CG1 VAL B 187     5098   1872   5505   -157   -700    840       C
ATOM   4255  CG2 VAL B 187     -41.878  73.884  16.999  1.00 34.66           C
ANISOU 4255  CG2 VAL B 187     5410   2151   5608   -306   -492    806       C
ATOM   4256  N  AGLN B 188     -46.199  75.570  17.677  0.73 42.21           N
ANISOU 4256  N  AGLN B 188     5452   3304   7282    382   -688    674       N
ATOM   4257  N  BGLN B 188     -46.195  75.572  17.703  0.27 41.82           N
ANISOU 4257  N  BGLN B 188     5406   3252   7231    383   -692    675       N
ATOM   4258  CA AGLN B 188     -47.244  76.282  18.394  0.73 43.79           C
ANISOU 4258  CA AGLN B 188     5480   3519   7638    554   -818    586       C
ATOM   4259  CA BGLN B 188     -47.242  76.325  18.380  0.27 44.06           C
ANISOU 4259  CA BGLN B 188     5513   3552   7677    562   -822    581       C
ATOM   4260  C  AGLN B 188     -47.132  75.995  19.883  0.73 45.84           C
ANISOU 4260  C  AGLN B 188     5970   3670   7778    491   -980    670       C
ATOM   4261  C  BGLN B 188     -47.278  75.976  19.862  0.27 45.65           C
ANISOU 4261  C  BGLN B 188     5903   3667   7774    494   -968    665       C
ATOM   4262  O  AGLN B 188     -46.777  74.885  20.289  0.73 47.72           O
ANISOU 4262  O  AGLN B 188     6334   3935   7864    248   -880    781       O
ATOM   4263  O  BGLN B 188     -47.170  74.806  20.240  0.27 45.91           O
ANISOU 4263  O  BGLN B 188     5995   3761   7689    261   -851    772       O
ATOM   4264  CB AGLN B 188     -48.626  75.862  17.893  0.73 44.20           C
ANISOU 4264  CB AGLN B 188     5167   3787   7838    498   -623    550       C
ATOM   4265  CB BGLN B 188     -48.612  76.060  17.753  0.27 44.87           C
ANISOU 4265  CB BGLN B 188     5236   3871   7943    528   -626    523       C
ATOM   4266  CG AGLN B 188     -48.889  76.169  16.431  0.73 47.14           C
ANISOU 4266  CG AGLN B 188     5361   4257   8292    502   -438    450       C
ATOM   4267  CG BGLN B 188     -48.940  76.962  16.577  0.27 49.05           C
ANISOU 4267  CG BGLN B 188     5549   4476   8612    630   -526    340       C
ATOM   4268  CD AGLN B 188     -49.128  77.643  16.181  0.73 51.41           C
ANISOU 4268  CD AGLN B 188     5725   4807   9002    717   -514    203       C
ATOM   4269  CD BGLN B 188     -50.432  77.105  16.356  0.27 49.94           C
ANISOU 4269  CD BGLN B 188     5339   4765   8869    582   -377    210       C
ATOM   4270  OE1AGLN B 188     -48.199  78.393  15.885  0.73 54.37           O
ANISOU 4270  OE1AGLN B 188     6224   5068   9368    866   -623    126       O
ATOM   4271  OE1BGLN B 188     -51.231  76.377  16.946  0.27 47.58           O
ANISOU 4271  OE1BGLN B 188     5002   4521   8556    472   -339    298       O
ATOM   4272  NE2AGLN B 188     -50.382  78.067  16.300  0.73 52.26           N
ANISOU 4272  NE2AGLN B 188     5532   5061   9262    732   -456     38       N
ATOM   4273  NE2BGLN B 188     -50.818  78.052  15.508  0.27 52.56           N
ANISOU 4273  NE2BGLN B 188     5449   5193   9327    637   -274    -30       N
ATOM   4274  N   GLN B 189     -47.433  77.002  20.696  1.00 43.97           N
ANISOU 4274  N   GLN B 189     5781   3321   7604    708  -1238    581       N
ATOM   4275  CA  GLN B 189     -47.540  76.813  22.136  1.00 44.21           C
ANISOU 4275  CA  GLN B 189     6028   3283   7488    639  -1384    639       C
ATOM   4276  C   GLN B 189     -48.963  76.377  22.461  1.00 45.84           C
ANISOU 4276  C   GLN B 189     5874   3663   7882    608  -1299    631       C
ATOM   4277  O   GLN B 189     -49.920  77.105  22.180  1.00 47.43           O
ANISOU 4277  O   GLN B 189     5743   3982   8294    785  -1325    475       O
ATOM   4278  CB  GLN B 189     -47.184  78.092  22.889  1.00 45.73           C
ANISOU 4278  CB  GLN B 189     6473   3340   7563    876  -1696    520       C
ATOM   4279  CG  GLN B 189     -47.238  77.927  24.399  1.00 52.31           C
ANISOU 4279  CG  GLN B 189     7597   4078   8202    781  -1854    583       C
ATOM   4280  CD  GLN B 189     -47.325  79.248  25.134  1.00 69.49           C
ANISOU 4280  CD  GLN B 189     9900   6166  10337   1069  -2205    426       C
ATOM   4281  OE1 GLN B 189     -47.013  80.303  24.581  1.00 75.40           O
ANISOU 4281  OE1 GLN B 189    10618   6892  11139   1327  -2345    268       O
ATOM   4282  NE2 GLN B 189     -47.759  79.197  26.388  1.00 75.85           N
ANISOU 4282  NE2 GLN B 189    10848   6922  11048   1029  -2364    447       N
ATOM   4283  N   LEU B 190     -49.102  75.190  23.040  1.00 43.63           N
ANISOU 4283  N   LEU B 190     5644   3440   7492    357  -1165    752       N
ATOM   4284  CA  LEU B 190     -50.425  74.670  23.344  1.00 36.98           C
ANISOU 4284  CA  LEU B 190     4509   2769   6772    305  -1058    744       C
ATOM   4285  C   LEU B 190     -51.023  75.419  24.533  1.00 39.13           C
ANISOU 4285  C   LEU B 190     4815   2972   7082    429  -1301    685       C
ATOM   4286  O   LEU B 190     -50.307  75.756  25.482  1.00 41.22           O
ANISOU 4286  O   LEU B 190     5452   3028   7180    442  -1530    722       O
ATOM   4287  CB  LEU B 190     -50.357  73.171  23.633  1.00 34.63           C
ANISOU 4287  CB  LEU B 190     4249   2554   6357     43   -872    844       C
ATOM   4288  CG  LEU B 190     -50.011  72.316  22.412  1.00 38.88           C
ANISOU 4288  CG  LEU B 190     4680   3206   6888    -38   -664    861       C
ATOM   4289  CD1 LEU B 190     -50.042  70.831  22.738  1.00 40.67           C
ANISOU 4289  CD1 LEU B 190     4871   3548   7034   -230   -530    878       C
ATOM   4290  CD2 LEU B 190     -50.958  72.633  21.264  1.00 37.98           C
ANISOU 4290  CD2 LEU B 190     4295   3192   6946     82   -565    812       C
ATOM   4291  N   PRO B 191     -52.323  75.697  24.514  1.00 39.11           N
ANISOU 4291  N   PRO B 191     4471   3124   7264    499  -1266    580       N
ATOM   4292  CA  PRO B 191     -52.918  76.536  25.556  1.00 42.22           C
ANISOU 4292  CA  PRO B 191     4841   3485   7718    650  -1528    472       C
ATOM   4293  C   PRO B 191     -53.145  75.776  26.854  1.00 40.76           C
ANISOU 4293  C   PRO B 191     4853   3243   7389    470  -1560    595       C
ATOM   4294  O   PRO B 191     -53.241  74.549  26.887  1.00 40.20           O
ANISOU 4294  O   PRO B 191     4793   3237   7244    232  -1327    712       O
ATOM   4295  CB  PRO B 191     -54.250  76.967  24.935  1.00 43.77           C
ANISOU 4295  CB  PRO B 191     4565   3917   8147    698  -1392    280       C
ATOM   4296  CG  PRO B 191     -54.615  75.821  24.054  1.00 32.49           C
ANISOU 4296  CG  PRO B 191     3046   2599   6701    466  -1039    393       C
ATOM   4297  CD  PRO B 191     -53.315  75.291  23.501  1.00 31.49           C
ANISOU 4297  CD  PRO B 191     3166   2361   6436    422   -991    534       C
ATOM   4298  N   GLU B 192     -53.221  76.545  27.939  1.00 44.89           N
ANISOU 4298  N   GLU B 192     5540   3641   7873    607  -1879    537       N
ATOM   4299  CA  GLU B 192     -53.624  75.993  29.225  1.00 47.10           C
ANISOU 4299  CA  GLU B 192     5988   3878   8029    439  -1924    619       C
ATOM   4300  C   GLU B 192     -55.045  75.459  29.119  1.00 45.41           C
ANISOU 4300  C   GLU B 192     5366   3906   7981    334  -1692    575       C
ATOM   4301  O   GLU B 192     -55.950  76.160  28.657  1.00 50.70           O
ANISOU 4301  O   GLU B 192     5675   4733   8856    470  -1694    402       O
ATOM   4302  CB  GLU B 192     -53.536  77.068  30.308  1.00 59.21           C
ANISOU 4302  CB  GLU B 192     7782   5222   9493    653  -2366    539       C
ATOM   4303  CG  GLU B 192     -53.099  76.565  31.672  1.00 71.91           C
ANISOU 4303  CG  GLU B 192     9904   6615  10802    434  -2478    683       C
ATOM   4304  CD  GLU B 192     -51.594  76.622  31.860  1.00 83.26           C
ANISOU 4304  CD  GLU B 192    11886   7879  11871    324  -2512    740       C
ATOM   4305  OE1 GLU B 192     -50.860  76.563  30.850  1.00 84.79           O
ANISOU 4305  OE1 GLU B 192    12046   8098  12070    332  -2364    749       O
ATOM   4306  OE2 GLU B 192     -51.145  76.736  33.020  1.00 88.96           O
ANISOU 4306  OE2 GLU B 192    13085   8436  12282    212  -2684    766       O
ATOM   4307  N   THR B 193     -55.246  74.213  29.538  1.00 41.54           N
ANISOU 4307  N   THR B 193     4944   3448   7390     76  -1482    697       N
ATOM   4308  CA  THR B 193     -56.503  73.531  29.276  1.00 41.29           C
ANISOU 4308  CA  THR B 193     4608   3600   7481    -28  -1242    676       C
ATOM   4309  C   THR B 193     -56.883  72.628  30.440  1.00 41.99           C
ANISOU 4309  C   THR B 193     4830   3670   7455   -227  -1195    744       C
ATOM   4310  O   THR B 193     -56.025  72.145  31.184  1.00 31.49           O
ANISOU 4310  O   THR B 193     3807   2226   5933   -366  -1228    818       O
ATOM   4311  CB  THR B 193     -56.427  72.694  27.989  1.00 40.50           C
ANISOU 4311  CB  THR B 193     4382   3588   7420    -92   -964    719       C
ATOM   4312  OG1 THR B 193     -57.662  71.996  27.793  1.00 44.49           O
ANISOU 4312  OG1 THR B 193     4711   4201   7992   -190   -771    706       O
ATOM   4313  CG2 THR B 193     -55.291  71.688  28.071  1.00 39.54           C
ANISOU 4313  CG2 THR B 193     4488   3403   7131   -227   -888    821       C
ATOM   4314  N   TYR B 194     -58.188  72.424  30.595  1.00 41.49           N
ANISOU 4314  N   TYR B 194     4552   3721   7493   -274  -1097    693       N
ATOM   4315  CA  TYR B 194     -58.723  71.337  31.397  1.00 38.95           C
ANISOU 4315  CA  TYR B 194     4293   3412   7094   -462   -972    741       C
ATOM   4316  C   TYR B 194     -58.799  70.073  30.545  1.00 35.70           C
ANISOU 4316  C   TYR B 194     3806   3064   6695   -530   -713    777       C
ATOM   4317  O   TYR B 194     -58.698  70.113  29.317  1.00 33.21           O
ANISOU 4317  O   TYR B 194     3384   2785   6450   -446   -627    774       O
ATOM   4318  CB  TYR B 194     -60.111  71.682  31.941  1.00 38.45           C
ANISOU 4318  CB  TYR B 194     4071   3421   7116   -484   -993    660       C
ATOM   4319  CG  TYR B 194     -60.156  72.816  32.943  1.00 41.73           C
ANISOU 4319  CG  TYR B 194     4550   3789   7516   -395  -1300    588       C
ATOM   4320  CD1 TYR B 194     -59.876  72.595  34.286  1.00 44.57           C
ANISOU 4320  CD1 TYR B 194     5204   4028   7703   -504  -1439    648       C
ATOM   4321  CD2 TYR B 194     -60.508  74.102  32.551  1.00 43.18           C
ANISOU 4321  CD2 TYR B 194     4501   4054   7850   -201  -1464    421       C
ATOM   4322  CE1 TYR B 194     -59.926  73.628  35.207  1.00 45.00           C
ANISOU 4322  CE1 TYR B 194     5380   4004   7715   -394  -1780    580       C
ATOM   4323  CE2 TYR B 194     -60.561  75.139  33.465  1.00 45.19           C
ANISOU 4323  CE2 TYR B 194     4799   4270   8101    -55  -1813    308       C
ATOM   4324  CZ  TYR B 194     -60.269  74.897  34.792  1.00 46.07           C
ANISOU 4324  CZ  TYR B 194     5264   4221   8019   -138  -1993    406       C
ATOM   4325  OH  TYR B 194     -60.320  75.928  35.705  1.00 49.14           O
ANISOU 4325  OH  TYR B 194     5759   4536   8375     34  -2398    295       O
ATOM   4326  N   PHE B 195     -58.991  68.939  31.209  1.00 35.33           N
ANISOU 4326  N   PHE B 195     3824   3026   6572   -667   -608    784       N
ATOM   4327  CA  PHE B 195     -59.161  67.669  30.520  1.00 34.78           C
ANISOU 4327  CA  PHE B 195     3685   3011   6520   -670   -430    767       C
ATOM   4328  C   PHE B 195     -60.396  66.957  31.047  1.00 38.67           C
ANISOU 4328  C   PHE B 195     4150   3512   7029   -727   -349    732       C
ATOM   4329  O   PHE B 195     -60.638  66.927  32.257  1.00 40.32           O
ANISOU 4329  O   PHE B 195     4429   3708   7182   -844   -382    714       O
ATOM   4330  CB  PHE B 195     -57.935  66.765  30.684  1.00 31.84           C
ANISOU 4330  CB  PHE B 195     3391   2668   6039   -755   -377    728       C
ATOM   4331  CG  PHE B 195     -56.717  67.263  29.965  1.00 32.24           C
ANISOU 4331  CG  PHE B 195     3495   2701   6055   -716   -420    758       C
ATOM   4332  CD1 PHE B 195     -56.712  67.382  28.585  1.00 30.99           C
ANISOU 4332  CD1 PHE B 195     3225   2564   5984   -565   -390    779       C
ATOM   4333  CD2 PHE B 195     -55.572  67.603  30.667  1.00 30.86           C
ANISOU 4333  CD2 PHE B 195     3542   2461   5724   -856   -487    762       C
ATOM   4334  CE1 PHE B 195     -55.591  67.838  27.919  1.00 32.43           C
ANISOU 4334  CE1 PHE B 195     3464   2728   6132   -534   -424    801       C
ATOM   4335  CE2 PHE B 195     -54.446  68.059  30.008  1.00 32.15           C
ANISOU 4335  CE2 PHE B 195     3803   2580   5833   -832   -526    788       C
ATOM   4336  CZ  PHE B 195     -54.455  68.177  28.631  1.00 35.39           C
ANISOU 4336  CZ  PHE B 195     4047   3036   6363   -660   -493    805       C
ATOM   4337  N   THR B 196     -61.178  66.395  30.131  1.00 39.12           N
ANISOU 4337  N   THR B 196     4164   3563   7139   -651   -254    722       N
ATOM   4338  CA  THR B 196     -62.285  65.545  30.534  1.00 35.12           C
ANISOU 4338  CA  THR B 196     3701   3021   6620   -684   -184    682       C
ATOM   4339  C   THR B 196     -61.752  64.242  31.119  1.00 32.12           C
ANISOU 4339  C   THR B 196     3329   2682   6194   -687   -156    586       C
ATOM   4340  O   THR B 196     -60.646  63.796  30.800  1.00 27.70           O
ANISOU 4340  O   THR B 196     2722   2189   5615   -651   -157    533       O
ATOM   4341  CB  THR B 196     -63.212  65.261  29.351  1.00 37.05           C
ANISOU 4341  CB  THR B 196     4016   3187   6876   -608   -116    694       C
ATOM   4342  OG1 THR B 196     -62.449  64.767  28.243  1.00 40.27           O
ANISOU 4342  OG1 THR B 196     4436   3589   7276   -467   -132    698       O
ATOM   4343  CG2 THR B 196     -63.937  66.526  28.931  1.00 28.27           C
ANISOU 4343  CG2 THR B 196     2864   2078   5798   -696    -79    710       C
ATOM   4344  N   GLN B 197     -62.549  63.634  31.994  1.00 32.07           N
ANISOU 4344  N   GLN B 197     3362   2655   6168   -750   -118    525       N
ATOM   4345  CA  GLN B 197     -62.106  62.452  32.721  1.00 32.18           C
ANISOU 4345  CA  GLN B 197     3338   2743   6147   -782    -70    364       C
ATOM   4346  C   GLN B 197     -62.361  61.150  31.972  1.00 36.96           C
ANISOU 4346  C   GLN B 197     3910   3342   6793   -561    -73    228       C
ATOM   4347  O   GLN B 197     -61.792  60.119  32.348  1.00 42.36           O
ANISOU 4347  O   GLN B 197     4474   4143   7477   -542    -43     15       O
ATOM   4348  CB  GLN B 197     -62.782  62.402  34.093  1.00 37.32           C
ANISOU 4348  CB  GLN B 197     4051   3377   6750   -954    -32    330       C
ATOM   4349  CG  GLN B 197     -62.462  63.607  34.965  1.00 36.87           C
ANISOU 4349  CG  GLN B 197     4073   3310   6624  -1143    -94    432       C
ATOM   4350  CD  GLN B 197     -60.976  63.750  35.236  1.00 44.78           C
ANISOU 4350  CD  GLN B 197     5122   4364   7528  -1261   -106    407       C
ATOM   4351  OE1 GLN B 197     -60.317  62.802  35.665  1.00 49.27           O
ANISOU 4351  OE1 GLN B 197     5670   5021   8028  -1379      3    245       O
ATOM   4352  NE2 GLN B 197     -60.439  64.937  34.979  1.00 46.83           N
ANISOU 4352  NE2 GLN B 197     5454   4570   7768  -1244   -232    532       N
ATOM   4353  N   SER B 198     -63.202  61.174  30.935  1.00 35.41           N
ANISOU 4353  N   SER B 198     3835   3006   6613   -402   -120    312       N
ATOM   4354  CA  SER B 198     -63.405  60.026  30.045  1.00 35.86           C
ANISOU 4354  CA  SER B 198     3955   2993   6675   -134   -204    200       C
ATOM   4355  C   SER B 198     -63.914  58.799  30.799  1.00 36.89           C
ANISOU 4355  C   SER B 198     4084   3117   6816    -34   -223    -10       C
ATOM   4356  O   SER B 198     -63.508  57.668  30.526  1.00 39.66           O
ANISOU 4356  O   SER B 198     4332   3534   7204    194   -314   -237       O
ATOM   4357  CB  SER B 198     -62.124  59.692  29.276  1.00 40.00           C
ANISOU 4357  CB  SER B 198     4324   3647   7226    -11   -260    114       C
ATOM   4358  OG  SER B 198     -61.688  60.797  28.504  1.00 43.82           O
ANISOU 4358  OG  SER B 198     4834   4115   7700    -79   -247    297       O
ATOM   4359  N   ARG B 199     -64.813  59.017  31.751  1.00 36.27           N
ANISOU 4359  N   ARG B 199     4097   2972   6710   -191   -151     28       N
ATOM   4360  CA  ARG B 199     -65.449  57.915  32.454  1.00 40.86           C
ANISOU 4360  CA  ARG B 199     4713   3515   7296    -95   -163   -169       C
ATOM   4361  C   ARG B 199     -66.743  57.518  31.750  1.00 45.21           C
ANISOU 4361  C   ARG B 199     5615   3780   7784     95   -262   -117       C
ATOM   4362  O   ARG B 199     -67.286  58.260  30.929  1.00 49.45           O
ANISOU 4362  O   ARG B 199     6380   4160   8249     37   -259     87       O
ATOM   4363  CB  ARG B 199     -65.727  58.291  33.910  1.00 40.56           C
ANISOU 4363  CB  ARG B 199     4636   3540   7234   -385    -31   -166       C
ATOM   4364  CG  ARG B 199     -64.480  58.328  34.776  1.00 44.85           C
ANISOU 4364  CG  ARG B 199     4946   4317   7776   -588     61   -287       C
ATOM   4365  CD  ARG B 199     -64.735  59.007  36.110  1.00 44.38           C
ANISOU 4365  CD  ARG B 199     4951   4268   7644   -906    153   -211       C
ATOM   4366  NE  ARG B 199     -64.911  60.449  35.962  1.00 43.24           N
ANISOU 4366  NE  ARG B 199     4904   4054   7472  -1026    108     55       N
ATOM   4367  CZ  ARG B 199     -64.922  61.308  36.975  1.00 45.31           C
ANISOU 4367  CZ  ARG B 199     5230   4324   7663  -1266    111    140       C
ATOM   4368  NH1 ARG B 199     -64.765  60.874  38.219  1.00 44.91           N
ANISOU 4368  NH1 ARG B 199     5208   4325   7531  -1464    188     16       N
ATOM   4369  NH2 ARG B 199     -65.088  62.604  36.746  1.00 44.47           N
ANISOU 4369  NH2 ARG B 199     5161   4176   7561  -1303     24    318       N
ATOM   4370  N   ASN B 200     -67.225  56.322  32.069  1.00 43.37           N
ANISOU 4370  N   ASN B 200     5451   3470   7558    312   -348   -335       N
ATOM   4371  CA  ASN B 200     -68.485  55.832  31.538  1.00 47.66           C
ANISOU 4371  CA  ASN B 200     6432   3680   7995    497   -470   -306       C
ATOM   4372  C   ASN B 200     -69.524  55.763  32.649  1.00 47.67           C
ANISOU 4372  C   ASN B 200     6569   3590   7955    331   -365   -324       C
ATOM   4373  O   ASN B 200     -69.199  55.771  33.840  1.00 46.35           O
ANISOU 4373  O   ASN B 200     6127   3628   7857    157   -239   -428       O
ATOM   4374  CB  ASN B 200     -68.317  54.459  30.876  1.00 56.19           C
ANISOU 4374  CB  ASN B 200     7578   4672   9098    973   -736   -563       C
ATOM   4375  CG  ASN B 200     -67.844  53.399  31.844  1.00 64.53           C
ANISOU 4375  CG  ASN B 200     8272   5956  10291   1123   -752   -944       C
ATOM   4376  OD1 ASN B 200     -68.643  52.802  32.564  1.00 67.87           O
ANISOU 4376  OD1 ASN B 200     8817   6270  10703   1186   -762  -1082       O
ATOM   4377  ND2 ASN B 200     -66.540  53.152  31.860  1.00 67.71           N
ANISOU 4377  ND2 ASN B 200     8230   6687  10812   1151   -734  -1149       N
ATOM   4378  N   LEU B 201     -70.790  55.696  32.237  1.00 45.26           N
ANISOU 4378  N   LEU B 201     6743   2952   7501    351   -410   -224       N
ATOM   4379  CA  LEU B 201     -71.883  55.793  33.198  1.00 52.07           C
ANISOU 4379  CA  LEU B 201     7785   3704   8294    134   -290   -207       C
ATOM   4380  C   LEU B 201     -71.985  54.538  34.054  1.00 60.75           C
ANISOU 4380  C   LEU B 201     8817   4807   9458    370   -368   -500       C
ATOM   4381  O   LEU B 201     -72.231  54.621  35.263  1.00 62.12           O
ANISOU 4381  O   LEU B 201     8857   5087   9657    152   -220   -557       O
ATOM   4382  CB  LEU B 201     -73.196  56.049  32.465  1.00 54.70           C
ANISOU 4382  CB  LEU B 201     8706   3666   8410     37   -290    -46       C
ATOM   4383  CG  LEU B 201     -74.249  56.740  33.323  1.00 56.80           C
ANISOU 4383  CG  LEU B 201     9093   3898   8592   -365    -82     40       C
ATOM   4384  CD1 LEU B 201     -73.653  58.012  33.891  1.00 56.85           C
ANISOU 4384  CD1 LEU B 201     8642   4244   8713   -690     86    139       C
ATOM   4385  CD2 LEU B 201     -75.496  57.036  32.512  1.00 59.23           C
ANISOU 4385  CD2 LEU B 201    10001   3857   8648   -548    -32    167       C
ATOM   4386  N   GLN B 202     -71.802  53.369  33.441  1.00 65.57           N
ANISOU 4386  N   GLN B 202     9513   5306  10093    827   -615   -720       N
ATOM   4387  CA  GLN B 202     -71.896  52.110  34.171  1.00 72.81           C
ANISOU 4387  CA  GLN B 202    10325   6244  11094   1115   -717  -1083       C
ATOM   4388  C   GLN B 202     -70.800  52.002  35.226  1.00 73.54           C
ANISOU 4388  C   GLN B 202     9798   6780  11362    961   -543  -1315       C
ATOM   4389  O   GLN B 202     -71.078  51.823  36.417  1.00 74.91           O
ANISOU 4389  O   GLN B 202     9865   7041  11556    782   -390  -1444       O
ATOM   4390  CB  GLN B 202     -71.820  50.941  33.188  1.00 83.74           C
ANISOU 4390  CB  GLN B 202    11890   7443  12484   1697  -1082  -1318       C
ATOM   4391  CG  GLN B 202     -71.434  49.614  33.818  1.00 96.98           C
ANISOU 4391  CG  GLN B 202    13215   9300  14332   2071  -1216  -1824       C
ATOM   4392  CD  GLN B 202     -70.864  48.642  32.805  1.00108.06           C
ANISOU 4392  CD  GLN B 202    14541  10753  15764   2592  -1560  -2070       C
ATOM   4393  OE1 GLN B 202     -70.431  47.543  33.153  1.00115.29           O
ANISOU 4393  OE1 GLN B 202    15078  11944  16784   2862  -1668  -2490       O
ATOM   4394  NE2 GLN B 202     -70.856  49.047  31.540  1.00107.94           N
ANISOU 4394  NE2 GLN B 202    14836  10604  15572   2609  -1677  -1761       N
ATOM   4395  N   GLU B 203     -69.542  52.115  34.804  1.00 73.47           N
ANISOU 4395  N   GLU B 203     9420   7045  11452    987   -548  -1376       N
ATOM   4396  CA  GLU B 203     -68.388  51.919  35.680  1.00 72.46           C
ANISOU 4396  CA  GLU B 203     8763   7325  11442    812   -377  -1641       C
ATOM   4397  C   GLU B 203     -67.818  53.238  36.184  1.00 60.16           C
ANISOU 4397  C   GLU B 203     7095   5928   9836    314   -139  -1353       C
ATOM   4398  O   GLU B 203     -66.598  53.412  36.240  1.00 62.07           O
ANISOU 4398  O   GLU B 203     7026   6439  10120    176    -54  -1435       O
ATOM   4399  CB  GLU B 203     -67.315  51.115  34.953  1.00 85.70           C
ANISOU 4399  CB  GLU B 203    10108   9215  13237   1138   -534  -1962       C
ATOM   4400  CG  GLU B 203     -67.797  49.777  34.414  1.00100.14           C
ANISOU 4400  CG  GLU B 203    12032  10892  15125   1722   -857  -2307       C
ATOM   4401  CD  GLU B 203     -66.875  49.211  33.352  1.00107.62           C
ANISOU 4401  CD  GLU B 203    12746  11982  16161   2088  -1094  -2535       C
ATOM   4402  OE1 GLU B 203     -67.214  49.305  32.153  1.00109.17           O
ANISOU 4402  OE1 GLU B 203    13319  11889  16273   2363  -1354  -2325       O
ATOM   4403  OE2 GLU B 203     -65.804  48.682  33.717  1.00110.90           O
ANISOU 4403  OE2 GLU B 203    12618  12809  16711   2064  -1007  -2942       O
ATOM   4404  N   PHE B 204     -68.672  54.186  36.561  1.00 44.12           N
ANISOU 4404  N   PHE B 204     5201   4851   6712   -209    660    -45       N
ATOM   4405  CA  PHE B 204     -68.186  55.473  37.035  1.00 38.92           C
ANISOU 4405  CA  PHE B 204     4711   4233   5843   -290    635     56       C
ATOM   4406  C   PHE B 204     -67.548  55.331  38.410  1.00 41.45           C
ANISOU 4406  C   PHE B 204     5137   4591   6021   -379    852     34       C
ATOM   4407  O   PHE B 204     -68.081  54.661  39.299  1.00 46.27           O
ANISOU 4407  O   PHE B 204     5796   5207   6576   -380   1001    -74       O
ATOM   4408  CB  PHE B 204     -69.323  56.492  37.094  1.00 39.65           C
ANISOU 4408  CB  PHE B 204     4955   4326   5784   -268    480     86       C
ATOM   4409  CG  PHE B 204     -68.863  57.895  37.383  1.00 42.21           C
ANISOU 4409  CG  PHE B 204     5416   4675   5947   -326    401    201       C
ATOM   4410  CD1 PHE B 204     -68.590  58.772  36.348  1.00 42.68           C
ANISOU 4410  CD1 PHE B 204     5436   4717   6063   -310    252    286       C
ATOM   4411  CD2 PHE B 204     -68.699  58.334  38.688  1.00 42.64           C
ANISOU 4411  CD2 PHE B 204     5647   4758   5795   -396    473    223       C
ATOM   4412  CE1 PHE B 204     -68.166  60.062  36.607  1.00 42.66           C
ANISOU 4412  CE1 PHE B 204     5538   4717   5953   -344    179    385       C
ATOM   4413  CE2 PHE B 204     -68.272  59.622  38.954  1.00 40.98           C
ANISOU 4413  CE2 PHE B 204     5558   4551   5462   -436    370    342       C
ATOM   4414  CZ  PHE B 204     -68.008  60.487  37.911  1.00 42.71           C
ANISOU 4414  CZ  PHE B 204     5707   4744   5778   -400    223    421       C
ATOM   4415  N   LYS B 205     -66.393  55.974  38.584  1.00 43.44           N
ANISOU 4415  N   LYS B 205     5443   4858   6204   -465    876    136       N
ATOM   4416  CA  LYS B 205     -65.658  55.932  39.840  1.00 50.92           C
ANISOU 4416  CA  LYS B 205     6520   5834   6992   -577   1077    144       C
ATOM   4417  C   LYS B 205     -65.143  57.334  40.152  1.00 46.05           C
ANISOU 4417  C   LYS B 205     6096   5213   6187   -642    965    294       C
ATOM   4418  O   LYS B 205     -64.463  57.945  39.306  1.00 41.21           O
ANISOU 4418  O   LYS B 205     5422   4569   5665   -637    846    386       O
ATOM   4419  CB  LYS B 205     -64.500  54.930  39.769  1.00 61.10           C
ANISOU 4419  CB  LYS B 205     7634   7125   8456   -633   1276    108       C
ATOM   4420  CG  LYS B 205     -64.950  53.491  39.536  1.00 69.35           C
ANISOU 4420  CG  LYS B 205     8460   8161   9727   -557   1390    -45       C
ATOM   4421  CD  LYS B 205     -63.780  52.562  39.257  1.00 75.95           C
ANISOU 4421  CD  LYS B 205     9063   8996  10797   -604   1540    -72       C
ATOM   4422  CE  LYS B 205     -64.266  51.157  38.926  1.00 80.69           C
ANISOU 4422  CE  LYS B 205     9411   9572  11676   -502   1611   -218       C
ATOM   4423  NZ  LYS B 205     -63.142  50.235  38.606  1.00 86.87           N
ANISOU 4423  NZ  LYS B 205     9924  10353  12729   -546   1732   -248       N
ATOM   4424  N   PRO B 206     -65.441  57.870  41.333  1.00 48.50           N
ANISOU 4424  N   PRO B 206     6644   5542   6242   -704    987    322       N
ATOM   4425  CA  PRO B 206     -65.010  59.234  41.658  1.00 48.68           C
ANISOU 4425  CA  PRO B 206     6848   5544   6104   -752    842    478       C
ATOM   4426  C   PRO B 206     -63.498  59.330  41.793  1.00 53.84           C
ANISOU 4426  C   PRO B 206     7523   6168   6766   -853    946    574       C
ATOM   4427  O   PRO B 206     -62.798  58.345  42.038  1.00 58.37           O
ANISOU 4427  O   PRO B 206     8024   6756   7397   -926   1174    518       O
ATOM   4428  CB  PRO B 206     -65.706  59.518  42.993  1.00 47.86           C
ANISOU 4428  CB  PRO B 206     7000   5469   5718   -811    850    470       C
ATOM   4429  CG  PRO B 206     -65.914  58.172  43.598  1.00 49.95           C
ANISOU 4429  CG  PRO B 206     7245   5768   5965   -848   1116    314       C
ATOM   4430  CD  PRO B 206     -66.176  57.241  42.445  1.00 49.74           C
ANISOU 4430  CD  PRO B 206     6925   5731   6242   -737   1140    209       C
ATOM   4431  N   ARG B 207     -62.994  60.557  41.626  1.00 52.80           N
ANISOU 4431  N   ARG B 207     7484   5983   6595   -857    777    718       N
ATOM   4432  CA  ARG B 207     -61.557  60.805  41.631  1.00 51.05           C
ANISOU 4432  CA  ARG B 207     7293   5704   6398   -949    838    824       C
ATOM   4433  C   ARG B 207     -61.176  61.983  42.522  1.00 50.10           C
ANISOU 4433  C   ARG B 207     7441   5530   6065  -1012    732    985       C
ATOM   4434  O   ARG B 207     -60.069  62.517  42.392  1.00 49.16           O
ANISOU 4434  O   ARG B 207     7367   5330   5981  -1064    712   1100       O
ATOM   4435  CB  ARG B 207     -61.048  61.030  40.205  1.00 48.91           C
ANISOU 4435  CB  ARG B 207     6827   5384   6374   -882    734    836       C
ATOM   4436  CG  ARG B 207     -61.183  59.804  39.316  1.00 50.36           C
ANISOU 4436  CG  ARG B 207     6756   5605   6772   -843    821    703       C
ATOM   4437  CD  ARG B 207     -60.794  60.090  37.878  1.00 51.68           C
ANISOU 4437  CD  ARG B 207     6772   5725   7140   -789    686    714       C
ATOM   4438  NE  ARG B 207     -60.921  58.895  37.048  1.00 53.23           N
ANISOU 4438  NE  ARG B 207     6741   5952   7533   -758    732    603       N
ATOM   4439  CZ  ARG B 207     -60.715  58.868  35.735  1.00 50.31           C
ANISOU 4439  CZ  ARG B 207     6235   5552   7330   -720    616    588       C
ATOM   4440  NH1 ARG B 207     -60.372  59.974  35.091  1.00 47.54           N
ANISOU 4440  NH1 ARG B 207     5949   5141   6974   -708    480    658       N
ATOM   4441  NH2 ARG B 207     -60.855  57.731  35.066  1.00 50.59           N
ANISOU 4441  NH2 ARG B 207     6074   5610   7537   -696    631    501       N
ATOM   4442  N   SER B 208     -62.063  62.397  43.423  1.00 49.05           N
ANISOU 4442  N   SER B 208     7493   5427   5716  -1013    647   1000       N
ATOM   4443  CA  SER B 208     -61.747  63.451  44.376  1.00 47.05           C
ANISOU 4443  CA  SER B 208     7513   5119   5244  -1080    519   1163       C
ATOM   4444  C   SER B 208     -62.689  63.329  45.563  1.00 48.10           C
ANISOU 4444  C   SER B 208     7860   5316   5101  -1135    520   1128       C
ATOM   4445  O   SER B 208     -63.766  62.736  45.465  1.00 48.77           O
ANISOU 4445  O   SER B 208     7860   5470   5202  -1080    551    982       O
ATOM   4446  CB  SER B 208     -61.859  64.843  43.745  1.00 45.44           C
ANISOU 4446  CB  SER B 208     7277   4838   5151   -965    225   1271       C
ATOM   4447  OG  SER B 208     -63.214  65.209  43.552  1.00 44.63           O
ANISOU 4447  OG  SER B 208     7115   4782   5059   -860     56   1209       O
ATOM   4448  N   GLN B 209     -62.262  63.901  46.693  1.00 49.34           N
ANISOU 4448  N   GLN B 209     8316   5436   4995  -1252    475   1266       N
ATOM   4449  CA  GLN B 209     -63.103  63.894  47.886  1.00 50.68           C
ANISOU 4449  CA  GLN B 209     8742   5658   4858  -1328    446   1246       C
ATOM   4450  C   GLN B 209     -64.428  64.597  47.626  1.00 50.19           C
ANISOU 4450  C   GLN B 209     8621   5615   4833  -1202    163   1216       C
ATOM   4451  O   GLN B 209     -65.473  64.180  48.138  1.00 49.79           O
ANISOU 4451  O   GLN B 209     8644   5630   4643  -1220    181   1099       O
ATOM   4452  CB  GLN B 209     -62.364  64.550  49.053  1.00 55.61           C
ANISOU 4452  CB  GLN B 209     9722   6221   5187  -1479    387   1435       C
ATOM   4453  CG  GLN B 209     -63.204  64.704  50.313  1.00 63.01           C
ANISOU 4453  CG  GLN B 209    10972   7203   5768  -1574    302   1435       C
ATOM   4454  CD  GLN B 209     -63.735  63.380  50.827  1.00 70.17           C
ANISOU 4454  CD  GLN B 209    11915   8208   6537  -1657    619   1224       C
ATOM   4455  OE1 GLN B 209     -63.062  62.352  50.742  1.00 70.93           O
ANISOU 4455  OE1 GLN B 209    11925   8328   6698  -1721    954   1136       O
ATOM   4456  NE2 GLN B 209     -64.950  63.398  51.362  1.00 74.72           N
ANISOU 4456  NE2 GLN B 209    12610   8836   6943  -1655    515   1134       N
ATOM   4457  N   MET B 210     -64.404  65.664  46.825  1.00 46.65           N
ANISOU 4457  N   MET B 210     8037   5104   4583  -1080    -88   1311       N
ATOM   4458  CA  MET B 210     -65.645  66.328  46.446  1.00 45.45           C
ANISOU 4458  CA  MET B 210     7779   4972   4517   -963   -334   1274       C
ATOM   4459  C   MET B 210     -66.548  65.391  45.654  1.00 51.11           C
ANISOU 4459  C   MET B 210     8269   5761   5390   -889   -207   1076       C
ATOM   4460  O   MET B 210     -67.762  65.345  45.884  1.00 49.21           O
ANISOU 4460  O   MET B 210     8043   5566   5086   -872   -292    989       O
ATOM   4461  CB  MET B 210     -65.337  67.588  45.639  1.00 45.76           C
ANISOU 4461  CB  MET B 210     7682   4925   4782   -844   -570   1394       C
ATOM   4462  CG  MET B 210     -66.568  68.326  45.149  1.00 48.27           C
ANISOU 4462  CG  MET B 210     7849   5261   5231   -728   -802   1353       C
ATOM   4463  SD  MET B 210     -66.154  69.751  44.129  1.00 54.70           S
ANISOU 4463  SD  MET B 210     8468   5967   6348   -582  -1015   1460       S
ATOM   4464  CE  MET B 210     -65.231  70.753  45.292  1.00 56.48           C
ANISOU 4464  CE  MET B 210     8972   6080   6408   -643  -1211   1693       C
ATOM   4465  N   GLU B 211     -65.971  64.629  44.721  1.00 46.63           N
ANISOU 4465  N   GLU B 211     7497   5193   5028   -853    -19   1008       N
ATOM   4466  CA  GLU B 211     -66.767  63.671  43.961  1.00 43.48           C
ANISOU 4466  CA  GLU B 211     6893   4845   4781   -783     88    836       C
ATOM   4467  C   GLU B 211     -67.268  62.541  44.852  1.00 48.82           C
ANISOU 4467  C   GLU B 211     7682   5579   5289   -860    289    703       C
ATOM   4468  O   GLU B 211     -68.380  62.037  44.655  1.00 52.19           O
ANISOU 4468  O   GLU B 211     8036   6035   5757   -808    291    571       O
ATOM   4469  CB  GLU B 211     -65.954  63.118  42.792  1.00 43.22           C
ANISOU 4469  CB  GLU B 211     6632   4792   5000   -737    212    808       C
ATOM   4470  CG  GLU B 211     -65.651  64.140  41.712  1.00 49.19           C
ANISOU 4470  CG  GLU B 211     7257   5488   5943   -649     35    891       C
ATOM   4471  CD  GLU B 211     -65.176  63.502  40.422  1.00 57.45           C
ANISOU 4471  CD  GLU B 211     8080   6524   7225   -603    129    828       C
ATOM   4472  OE1 GLU B 211     -64.780  62.318  40.451  1.00 60.31           O
ANISOU 4472  OE1 GLU B 211     8382   6913   7620   -649    324    752       O
ATOM   4473  OE2 GLU B 211     -65.205  64.185  39.377  1.00 60.62           O
ANISOU 4473  OE2 GLU B 211     8363   6888   7781   -526      5    848       O
ATOM   4474  N   ILE B 212     -66.462  62.129  45.833  1.00 49.04           N
ANISOU 4474  N   ILE B 212     7894   5612   5125   -990    473    729       N
ATOM   4475  CA  ILE B 212     -66.920  61.132  46.796  1.00 50.81           C
ANISOU 4475  CA  ILE B 212     8257   5885   5162  -1076    690    590       C
ATOM   4476  C   ILE B 212     -68.106  61.667  47.586  1.00 54.33           C
ANISOU 4476  C   ILE B 212     8911   6350   5381  -1098    509    572       C
ATOM   4477  O   ILE B 212     -69.094  60.957  47.814  1.00 54.72           O
ANISOU 4477  O   ILE B 212     8969   6429   5395  -1089    592    408       O
ATOM   4478  CB  ILE B 212     -65.764  60.712  47.723  1.00 48.18           C
ANISOU 4478  CB  ILE B 212     8107   5553   4644  -1236    937    635       C
ATOM   4479  CG1 ILE B 212     -64.669  60.004  46.923  1.00 49.95           C
ANISOU 4479  CG1 ILE B 212     8090   5763   5125  -1224   1136    621       C
ATOM   4480  CG2 ILE B 212     -66.273  59.822  48.847  1.00 50.52           C
ANISOU 4480  CG2 ILE B 212     8596   5898   4701  -1341   1172    486       C
ATOM   4481  CD1 ILE B 212     -63.473  59.594  47.757  1.00 52.59           C
ANISOU 4481  CD1 ILE B 212     8577   6095   5311  -1397   1397    667       C
ATOM   4482  N   ASP B 213     -68.033  62.932  48.004  1.00 54.54           N
ANISOU 4482  N   ASP B 213     9104   6350   5269  -1127    244    738       N
ATOM   4483  CA  ASP B 213     -69.133  63.536  48.747  1.00 53.54           C
ANISOU 4483  CA  ASP B 213     9166   6239   4938  -1159     23    735       C
ATOM   4484  C   ASP B 213     -70.385  63.645  47.885  1.00 54.61           C
ANISOU 4484  C   ASP B 213     9082   6385   5284  -1032   -125    636       C
ATOM   4485  O   ASP B 213     -71.491  63.331  48.340  1.00 59.87           O
ANISOU 4485  O   ASP B 213     9835   7076   5838  -1058   -144    514       O
ATOM   4486  CB  ASP B 213     -68.717  64.912  49.270  1.00 54.80           C
ANISOU 4486  CB  ASP B 213     9507   6354   4961  -1200   -267    953       C
ATOM   4487  CG  ASP B 213     -67.602  64.834  50.296  1.00 62.45           C
ANISOU 4487  CG  ASP B 213    10768   7302   5658  -1358   -141   1065       C
ATOM   4488  OD1 ASP B 213     -67.278  63.714  50.741  1.00 65.16           O
ANISOU 4488  OD1 ASP B 213    11194   7682   5884  -1455    189    954       O
ATOM   4489  OD2 ASP B 213     -67.047  65.894  50.656  1.00 65.02           O
ANISOU 4489  OD2 ASP B 213    11241   7567   5899  -1387   -366   1266       O
ATOM   4490  N   PHE B 214     -70.227  64.081  46.632  1.00 53.04           N
ANISOU 4490  N   PHE B 214     8612   6159   5382   -905   -221    683       N
ATOM   4491  CA  PHE B 214     -71.380  64.293  45.759  1.00 49.84           C
ANISOU 4491  CA  PHE B 214     8009   5758   5171   -801   -362    610       C
ATOM   4492  C   PHE B 214     -72.206  63.023  45.608  1.00 52.09           C
ANISOU 4492  C   PHE B 214     8234   6064   5494   -787   -176    414       C
ATOM   4493  O   PHE B 214     -73.442  63.074  45.607  1.00 53.74           O
ANISOU 4493  O   PHE B 214     8440   6276   5701   -773   -284    331       O
ATOM   4494  CB  PHE B 214     -70.913  64.789  44.390  1.00 45.57           C
ANISOU 4494  CB  PHE B 214     7207   5184   4924   -687   -422    674       C
ATOM   4495  CG  PHE B 214     -72.023  64.937  43.384  1.00 44.18           C
ANISOU 4495  CG  PHE B 214     6829   5010   4946   -597   -524    600       C
ATOM   4496  CD1 PHE B 214     -72.323  63.911  42.500  1.00 43.83           C
ANISOU 4496  CD1 PHE B 214     6624   4968   5061   -544   -372    480       C
ATOM   4497  CD2 PHE B 214     -72.760  66.106  43.317  1.00 43.29           C
ANISOU 4497  CD2 PHE B 214     6687   4891   4872   -571   -777    655       C
ATOM   4498  CE1 PHE B 214     -73.341  64.049  41.573  1.00 45.11           C
ANISOU 4498  CE1 PHE B 214     6632   5123   5384   -480   -463    426       C
ATOM   4499  CE2 PHE B 214     -73.776  66.250  42.392  1.00 40.50           C
ANISOU 4499  CE2 PHE B 214     6153   4539   4696   -511   -846    587       C
ATOM   4500  CZ  PHE B 214     -74.068  65.220  41.521  1.00 40.49           C
ANISOU 4500  CZ  PHE B 214     6026   4537   4821   -471   -685    476       C
ATOM   4501  N   LEU B 215     -71.541  61.875  45.476  1.00 55.45           N
ANISOU 4501  N   LEU B 215     8601   6493   5975   -790    100    337       N
ATOM   4502  CA  LEU B 215     -72.250  60.610  45.332  1.00 55.84           C
ANISOU 4502  CA  LEU B 215     8576   6541   6100   -759    282    150       C
ATOM   4503  C   LEU B 215     -72.850  60.148  46.653  1.00 62.96           C
ANISOU 4503  C   LEU B 215     9736   7458   6729   -861    382     35       C
ATOM   4504  O   LEU B 215     -73.942  59.570  46.671  1.00 66.08           O
ANISOU 4504  O   LEU B 215    10125   7835   7148   -834    408   -114       O
ATOM   4505  CB  LEU B 215     -71.305  59.543  44.781  1.00 52.73           C
ANISOU 4505  CB  LEU B 215     8007   6141   5887   -725    531    104       C
ATOM   4506  CG  LEU B 215     -70.688  59.852  43.416  1.00 46.51           C
ANISOU 4506  CG  LEU B 215     6977   5332   5360   -637    446    195       C
ATOM   4507  CD1 LEU B 215     -69.705  58.766  43.003  1.00 45.81           C
ANISOU 4507  CD1 LEU B 215     6730   5239   5436   -628    675    150       C
ATOM   4508  CD2 LEU B 215     -71.783  60.017  42.376  1.00 41.66           C
ANISOU 4508  CD2 LEU B 215     6213   4696   4921   -536    282    157       C
ATOM   4509  N   GLU B 216     -72.152  60.388  47.764  1.00 67.87           N
ANISOU 4509  N   GLU B 216    10606   8104   7079   -988    444    101       N
ATOM   4510  CA  GLU B 216     -72.653  59.940  49.059  1.00 74.52           C
ANISOU 4510  CA  GLU B 216    11735   8962   7619  -1109    561    -16       C
ATOM   4511  C   GLU B 216     -73.696  60.897  49.624  1.00 73.69           C
ANISOU 4511  C   GLU B 216    11820   8858   7320  -1159    260     16       C
ATOM   4512  O   GLU B 216     -74.723  60.456  50.152  1.00 75.23           O
ANISOU 4512  O   GLU B 216    12142   9047   7397  -1198    288   -140       O
ATOM   4513  CB  GLU B 216     -71.497  59.785  50.046  1.00 85.31           C
ANISOU 4513  CB  GLU B 216    13326  10351   8738  -1252    760     44       C
ATOM   4514  CG  GLU B 216     -71.417  58.417  50.710  1.00 97.41           C
ANISOU 4514  CG  GLU B 216    14935  11894  10182  -1321   1152   -155       C
ATOM   4515  CD  GLU B 216     -70.648  57.403  49.880  1.00106.62           C
ANISOU 4515  CD  GLU B 216    15792  13052  11667  -1236   1415   -217       C
ATOM   4516  OE1 GLU B 216     -71.200  56.893  48.880  1.00107.35           O
ANISOU 4516  OE1 GLU B 216    15608  13116  12064  -1088   1394   -306       O
ATOM   4517  OE2 GLU B 216     -69.482  57.121  50.228  1.00110.97           O
ANISOU 4517  OE2 GLU B 216    16380  13620  12163  -1327   1631   -170       O
ATOM   4518  N   LEU B 217     -73.457  62.200  49.517  1.00 72.59           N
ANISOU 4518  N   LEU B 217    11694   8719   7167  -1157    -35    208       N
ATOM   4519  CA  LEU B 217     -74.265  63.186  50.218  1.00 73.16           C
ANISOU 4519  CA  LEU B 217    11960   8796   7042  -1226   -344    264       C
ATOM   4520  C   LEU B 217     -75.540  63.517  49.449  1.00 74.67           C
ANISOU 4520  C   LEU B 217    11954   8973   7444  -1135   -545    202       C
ATOM   4521  O   LEU B 217     -75.645  63.313  48.238  1.00 73.29           O
ANISOU 4521  O   LEU B 217    11488   8781   7577  -1009   -506    177       O
ATOM   4522  CB  LEU B 217     -73.462  64.467  50.454  1.00 68.80           C
ANISOU 4522  CB  LEU B 217    11488   8232   6420  -1252   -592    503       C
ATOM   4523  CG  LEU B 217     -72.812  64.682  51.821  1.00 71.10           C
ANISOU 4523  CG  LEU B 217    12161   8529   6325  -1420   -596    601       C
ATOM   4524  CD1 LEU B 217     -72.541  63.364  52.534  1.00 73.13           C
ANISOU 4524  CD1 LEU B 217    12605   8812   6371  -1531   -205    443       C
ATOM   4525  CD2 LEU B 217     -71.525  65.471  51.649  1.00 70.56           C
ANISOU 4525  CD2 LEU B 217    12077   8422   6311  -1403   -684    826       C
ATOM   4526  N   ALA B 218     -76.518  64.039  50.183  1.00 76.05           N
ANISOU 4526  N   ALA B 218    12306   9152   7437  -1218   -767    179       N
ATOM   4527  CA  ALA B 218     -77.734  64.545  49.574  1.00 71.70           C
ANISOU 4527  CA  ALA B 218    11587   8586   7068  -1164   -993    142       C
ATOM   4528  C   ALA B 218     -77.473  65.915  48.955  1.00 70.18           C
ANISOU 4528  C   ALA B 218    11208   8393   7063  -1093  -1278    331       C
ATOM   4529  O   ALA B 218     -76.460  66.567  49.223  1.00 71.30           O
ANISOU 4529  O   ALA B 218    11410   8534   7146  -1100  -1354    495       O
ATOM   4530  CB  ALA B 218     -78.863  64.630  50.602  1.00 70.48           C
ANISOU 4530  CB  ALA B 218    11686   8433   6661  -1294  -1142     44       C
ATOM   4531  N   MET B 219     -78.411  66.345  48.110  1.00 66.86           N
ANISOU 4531  N   MET B 219    10559   7962   6884  -1027  -1423    303       N
ATOM   4532  CA  MET B 219     -78.219  67.577  47.352  1.00 65.22           C
ANISOU 4532  CA  MET B 219    10121   7747   6913   -943  -1641    448       C
ATOM   4533  C   MET B 219     -78.082  68.782  48.276  1.00 65.81           C
ANISOU 4533  C   MET B 219    10339   7824   6843  -1007  -1959    598       C
ATOM   4534  O   MET B 219     -77.142  69.575  48.148  1.00 67.15           O
ANISOU 4534  O   MET B 219    10455   7973   7087   -952  -2055    759       O
ATOM   4535  CB  MET B 219     -79.380  67.772  46.379  1.00 67.57           C
ANISOU 4535  CB  MET B 219    10174   8035   7466   -893  -1714    371       C
ATOM   4536  CG  MET B 219     -79.234  68.981  45.480  1.00 69.77           C
ANISOU 4536  CG  MET B 219    10184   8306   8019   -804  -1881    489       C
ATOM   4537  SD  MET B 219     -80.613  69.159  44.337  1.00 72.94           S
ANISOU 4537  SD  MET B 219    10318   8698   8699   -778  -1921    393       S
ATOM   4538  CE  MET B 219     -81.930  69.615  45.462  1.00 75.88           C
ANISOU 4538  CE  MET B 219    10836   9080   8916   -917  -2201    344       C
ATOM   4539  N   ASP B 220     -79.013  68.932  49.221  1.00 68.68           N
ANISOU 4539  N   ASP B 220    10893   8199   7001  -1125  -2143    548       N
ATOM   4540  CA  ASP B 220     -78.964  70.074  50.127  1.00 72.59           C
ANISOU 4540  CA  ASP B 220    11533   8692   7357  -1194  -2495    696       C
ATOM   4541  C   ASP B 220     -77.774  69.995  51.074  1.00 70.74           C
ANISOU 4541  C   ASP B 220    11599   8450   6829  -1262  -2452    816       C
ATOM   4542  O   ASP B 220     -77.242  71.032  51.485  1.00 69.01           O
ANISOU 4542  O   ASP B 220    11436   8204   6582  -1263  -2719   1003       O
ATOM   4543  CB  ASP B 220     -80.270  70.172  50.913  1.00 80.38           C
ANISOU 4543  CB  ASP B 220    12672   9693   8176  -1326  -2708    601       C
ATOM   4544  CG  ASP B 220     -81.479  70.323  50.010  1.00 86.18           C
ANISOU 4544  CG  ASP B 220    13117  10425   9204  -1282  -2765    495       C
ATOM   4545  OD1 ASP B 220     -81.369  71.025  48.982  1.00 86.61           O
ANISOU 4545  OD1 ASP B 220    12848  10471   9591  -1162  -2818    567       O
ATOM   4546  OD2 ASP B 220     -82.536  69.736  50.323  1.00 88.91           O
ANISOU 4546  OD2 ASP B 220    13568  10769   9444  -1375  -2741    336       O
ATOM   4547  N   GLU B 221     -77.339  68.786  51.431  1.00 72.11           N
ANISOU 4547  N   GLU B 221    11964   8640   6796  -1320  -2119    715       N
ATOM   4548  CA  GLU B 221     -76.166  68.663  52.289  1.00 75.79           C
ANISOU 4548  CA  GLU B 221    12716   9097   6983  -1404  -2033    827       C
ATOM   4549  C   GLU B 221     -74.889  68.982  51.522  1.00 70.02           C
ANISOU 4549  C   GLU B 221    11800   8331   6473  -1286  -1951    972       C
ATOM   4550  O   GLU B 221     -73.980  69.628  52.057  1.00 71.29           O
ANISOU 4550  O   GLU B 221    12119   8454   6513  -1322  -2080   1158       O
ATOM   4551  CB  GLU B 221     -76.101  67.261  52.889  1.00 85.93           C
ANISOU 4551  CB  GLU B 221    14235  10409   8005  -1508  -1665    654       C
ATOM   4552  CG  GLU B 221     -77.254  66.938  53.820  1.00100.47           C
ANISOU 4552  CG  GLU B 221    16334  12269   9569  -1648  -1732    503       C
ATOM   4553  CD  GLU B 221     -77.623  65.471  53.791  1.00108.57           C
ANISOU 4553  CD  GLU B 221    17391  13305  10558  -1664  -1339    255       C
ATOM   4554  OE1 GLU B 221     -78.776  65.137  54.135  1.00111.43           O
ANISOU 4554  OE1 GLU B 221    17850  13662  10827  -1726  -1371     89       O
ATOM   4555  OE2 GLU B 221     -76.760  64.651  53.410  1.00109.89           O
ANISOU 4555  OE2 GLU B 221    17472  13473  10809  -1610  -1003    223       O
ATOM   4556  N   PHE B 222     -74.809  68.550  50.262  1.00 63.73           N
ANISOU 4556  N   PHE B 222    10685   7534   5994  -1153  -1752    894       N
ATOM   4557  CA  PHE B 222     -73.598  68.768  49.477  1.00 61.21           C
ANISOU 4557  CA  PHE B 222    10198   7178   5883  -1052  -1655   1007       C
ATOM   4558  C   PHE B 222     -73.429  70.237  49.108  1.00 61.21           C
ANISOU 4558  C   PHE B 222    10044   7124   6088   -961  -1979   1178       C
ATOM   4559  O   PHE B 222     -72.315  70.772  49.164  1.00 61.84           O
ANISOU 4559  O   PHE B 222    10165   7146   6188   -937  -2022   1337       O
ATOM   4560  CB  PHE B 222     -73.631  67.896  48.222  1.00 57.91           C
ANISOU 4560  CB  PHE B 222     9500   6773   5731   -948  -1382    871       C
ATOM   4561  CG  PHE B 222     -72.428  68.054  47.336  1.00 58.21           C
ANISOU 4561  CG  PHE B 222     9365   6771   5982   -856  -1278    962       C
ATOM   4562  CD1 PHE B 222     -71.263  67.349  47.592  1.00 59.99           C
ANISOU 4562  CD1 PHE B 222     9701   6987   6104   -907  -1035    987       C
ATOM   4563  CD2 PHE B 222     -72.465  68.900  46.239  1.00 56.45           C
ANISOU 4563  CD2 PHE B 222     8869   6516   6065   -730  -1409   1012       C
ATOM   4564  CE1 PHE B 222     -70.157  67.490  46.775  1.00 58.35           C
ANISOU 4564  CE1 PHE B 222     9342   6735   6094   -836   -951   1064       C
ATOM   4565  CE2 PHE B 222     -71.362  69.046  45.420  1.00 54.81           C
ANISOU 4565  CE2 PHE B 222     8524   6261   6040   -654  -1311   1080       C
ATOM   4566  CZ  PHE B 222     -70.207  68.340  45.688  1.00 55.44           C
ANISOU 4566  CZ  PHE B 222     8722   6328   6014   -708  -1094   1108       C
ATOM   4567  N   ILE B 223     -74.521  70.905  48.731  1.00 60.08           N
ANISOU 4567  N   ILE B 223     9718   6991   6118   -911  -2201   1142       N
ATOM   4568  CA  ILE B 223     -74.431  72.289  48.277  1.00 59.86           C
ANISOU 4568  CA  ILE B 223     9484   6910   6350   -806  -2482   1277       C
ATOM   4569  C   ILE B 223     -74.012  73.207  49.420  1.00 65.80           C
ANISOU 4569  C   ILE B 223    10472   7613   6916   -867  -2795   1467       C
ATOM   4570  O   ILE B 223     -73.200  74.122  49.234  1.00 68.52           O
ANISOU 4570  O   ILE B 223    10742   7876   7415   -781  -2938   1627       O
ATOM   4571  CB  ILE B 223     -75.766  72.723  47.645  1.00 55.62           C
ANISOU 4571  CB  ILE B 223     8687   6402   6045   -761  -2620   1179       C
ATOM   4572  CG1 ILE B 223     -75.992  71.967  46.332  1.00 54.13           C
ANISOU 4572  CG1 ILE B 223     8257   6237   6074   -685  -2329   1034       C
ATOM   4573  CG2 ILE B 223     -75.799  74.225  47.415  1.00 55.74           C
ANISOU 4573  CG2 ILE B 223     8498   6364   6315   -670  -2937   1309       C
ATOM   4574  CD1 ILE B 223     -77.292  72.304  45.643  1.00 57.45           C
ANISOU 4574  CD1 ILE B 223     8438   6680   6711   -661  -2419    936       C
ATOM   4575  N   GLU B 224     -74.547  72.976  50.621  1.00 70.05           N
ANISOU 4575  N   GLU B 224    11315   8187   7115  -1018  -2914   1454       N
ATOM   4576  CA  GLU B 224     -74.126  73.771  51.769  1.00 74.80           C
ANISOU 4576  CA  GLU B 224    12195   8737   7487  -1099  -3226   1648       C
ATOM   4577  C   GLU B 224     -72.703  73.430  52.195  1.00 75.01           C
ANISOU 4577  C   GLU B 224    12468   8715   7316  -1148  -3050   1771       C
ATOM   4578  O   GLU B 224     -71.972  74.308  52.668  1.00 78.69           O
ANISOU 4578  O   GLU B 224    13058   9094   7746  -1144  -3292   1983       O
ATOM   4579  CB  GLU B 224     -75.094  73.568  52.936  1.00 79.96           C
ANISOU 4579  CB  GLU B 224    13145   9444   7794  -1273  -3394   1589       C
ATOM   4580  CG  GLU B 224     -74.725  74.351  54.189  1.00 89.50           C
ANISOU 4580  CG  GLU B 224    14690  10600   8714  -1383  -3750   1796       C
ATOM   4581  CD  GLU B 224     -75.704  74.137  55.325  1.00 98.34           C
ANISOU 4581  CD  GLU B 224    16080  11769   9513  -1559  -3869   1698       C
ATOM   4582  OE1 GLU B 224     -76.886  73.846  55.047  1.00100.84           O
ANISOU 4582  OE1 GLU B 224    16292  12146   9876  -1580  -3899   1535       O
ATOM   4583  OE2 GLU B 224     -75.289  74.257  56.498  1.00103.12           O
ANISOU 4583  OE2 GLU B 224    16997  12346   9838  -1681  -3913   1771       O
ATOM   4584  N   ARG B 225     -72.292  72.171  52.026  1.00 72.36           N
ANISOU 4584  N   ARG B 225    12196   8424   6872  -1193  -2637   1645       N
ATOM   4585  CA  ARG B 225     -70.952  71.762  52.438  1.00 73.97           C
ANISOU 4585  CA  ARG B 225    12626   8587   6891  -1264  -2434   1747       C
ATOM   4586  C   ARG B 225     -69.883  72.501  51.645  1.00 72.58           C
ANISOU 4586  C   ARG B 225    12252   8312   7015  -1126  -2477   1899       C
ATOM   4587  O   ARG B 225     -68.959  73.088  52.220  1.00 76.79           O
ANISOU 4587  O   ARG B 225    12987   8754   7436  -1166  -2614   2100       O
ATOM   4588  CB  ARG B 225     -70.793  70.251  52.270  1.00 76.06           C
ANISOU 4588  CB  ARG B 225    12915   8922   7063  -1322  -1972   1557       C
ATOM   4589  CG  ARG B 225     -69.489  69.694  52.819  1.00 78.44           C
ANISOU 4589  CG  ARG B 225    13463   9195   7144  -1435  -1721   1637       C
ATOM   4590  CD  ARG B 225     -69.251  68.281  52.315  1.00 79.85           C
ANISOU 4590  CD  ARG B 225    13525   9432   7384  -1438  -1266   1445       C
ATOM   4591  NE  ARG B 225     -68.239  67.573  53.094  1.00 84.27           N
ANISOU 4591  NE  ARG B 225    14360   9989   7670  -1597   -988   1476       N
ATOM   4592  CZ  ARG B 225     -68.517  66.733  54.085  1.00 89.04           C
ANISOU 4592  CZ  ARG B 225    15249  10651   7933  -1760   -786   1363       C
ATOM   4593  NH1 ARG B 225     -69.779  66.495  54.419  1.00 85.96           N
ANISOU 4593  NH1 ARG B 225    14913  10316   7433  -1782   -850   1209       N
ATOM   4594  NH2 ARG B 225     -67.536  66.129  54.742  1.00 95.99           N
ANISOU 4594  NH2 ARG B 225    16363  11527   8584  -1912   -505   1394       N
ATOM   4595  N   TYR B 226     -69.990  72.482  50.317  1.00 68.21           N
ANISOU 4595  N   TYR B 226    11321   7763   6835   -970  -2361   1804       N
ATOM   4596  CA  TYR B 226     -69.027  73.144  49.448  1.00 65.93           C
ANISOU 4596  CA  TYR B 226    10829   7374   6847   -836  -2373   1910       C
ATOM   4597  C   TYR B 226     -69.477  74.542  49.037  1.00 64.86           C
ANISOU 4597  C   TYR B 226    10465   7174   7005   -695  -2722   1992       C
ATOM   4598  O   TYR B 226     -68.983  75.074  48.037  1.00 61.44           O
ANISOU 4598  O   TYR B 226     9779   6670   6896   -554  -2700   2012       O
ATOM   4599  CB  TYR B 226     -68.746  72.280  48.219  1.00 60.86           C
ANISOU 4599  CB  TYR B 226     9936   6766   6421   -764  -2024   1759       C
ATOM   4600  CG  TYR B 226     -67.966  71.024  48.542  1.00 58.85           C
ANISOU 4600  CG  TYR B 226     9858   6544   5958   -881  -1680   1710       C
ATOM   4601  CD1 TYR B 226     -66.581  71.047  48.625  1.00 57.85           C
ANISOU 4601  CD1 TYR B 226     9837   6335   5810   -914  -1578   1836       C
ATOM   4602  CD2 TYR B 226     -68.615  69.819  48.775  1.00 56.68           C
ANISOU 4602  CD2 TYR B 226     9636   6372   5527   -961  -1452   1532       C
ATOM   4603  CE1 TYR B 226     -65.863  69.905  48.925  1.00 59.31           C
ANISOU 4603  CE1 TYR B 226    10156   6552   5827  -1034  -1251   1787       C
ATOM   4604  CE2 TYR B 226     -67.906  68.671  49.076  1.00 55.50           C
ANISOU 4604  CE2 TYR B 226     9613   6250   5223  -1063  -1123   1474       C
ATOM   4605  CZ  TYR B 226     -66.531  68.721  49.150  1.00 58.43           C
ANISOU 4605  CZ  TYR B 226    10070   6552   5580  -1105  -1020   1603       C
ATOM   4606  OH  TYR B 226     -65.821  67.580  49.450  1.00 61.84           O
ANISOU 4606  OH  TYR B 226    10602   7013   5880  -1218   -679   1541       O
ATOM   4607  N   LYS B 227     -70.392  75.143  49.797  1.00 70.61           N
ANISOU 4607  N   LYS B 227    11276   7922   7632   -737  -3041   2030       N
ATOM   4608  CA  LYS B 227     -70.784  76.547  49.657  1.00 76.50           C
ANISOU 4608  CA  LYS B 227    11826   8597   8643   -621  -3422   2133       C
ATOM   4609  C   LYS B 227     -71.158  76.883  48.212  1.00 73.12           C
ANISOU 4609  C   LYS B 227    10959   8173   8652   -454  -3328   2013       C
ATOM   4610  O   LYS B 227     -70.574  77.760  47.573  1.00 75.00           O
ANISOU 4610  O   LYS B 227    10997   8306   9192   -313  -3400   2091       O
ATOM   4611  CB  LYS B 227     -69.674  77.474  50.164  1.00 84.37           C
ANISOU 4611  CB  LYS B 227    12969   9442   9645   -587  -3652   2378       C
ATOM   4612  CG  LYS B 227     -68.896  76.943  51.366  1.00 92.28           C
ANISOU 4612  CG  LYS B 227    14406  10433  10224   -761  -3579   2475       C
ATOM   4613  CD  LYS B 227     -67.531  76.413  50.941  1.00 96.42           C
ANISOU 4613  CD  LYS B 227    15007  10884  10744   -761  -3293   2537       C
ATOM   4614  CE  LYS B 227     -66.885  75.570  52.029  1.00100.45           C
ANISOU 4614  CE  LYS B 227    15929  11419  10816   -967  -3110   2579       C
ATOM   4615  NZ  LYS B 227     -65.687  74.843  51.522  1.00 98.67           N
ANISOU 4615  NZ  LYS B 227    15726  11153  10610   -988  -2759   2584       N
ATOM   4616  N   LEU B 228     -72.160  76.165  47.702  1.00 65.75           N
ANISOU 4616  N   LEU B 228     9891   7352   7740   -478  -3156   1818       N
ATOM   4617  CA  LEU B 228     -72.583  76.299  46.314  1.00 60.70           C
ANISOU 4617  CA  LEU B 228     8880   6729   7455   -357  -3019   1690       C
ATOM   4618  C   LEU B 228     -73.954  76.953  46.175  1.00 64.30           C
ANISOU 4618  C   LEU B 228     9120   7229   8083   -340  -3236   1623       C
ATOM   4619  O   LEU B 228     -74.633  76.748  45.164  1.00 67.48           O
ANISOU 4619  O   LEU B 228     9277   7680   8683   -300  -3080   1480       O
ATOM   4620  CB  LEU B 228     -72.578  74.933  45.628  1.00 53.53           C
ANISOU 4620  CB  LEU B 228     7961   5896   6482   -391  -2632   1526       C
ATOM   4621  CG  LEU B 228     -71.208  74.381  45.232  1.00 51.33           C
ANISOU 4621  CG  LEU B 228     7743   5570   6190   -370  -2375   1559       C
ATOM   4622  CD1 LEU B 228     -71.320  72.931  44.798  1.00 46.82           C
ANISOU 4622  CD1 LEU B 228     7186   5080   5524   -425  -2041   1401       C
ATOM   4623  CD2 LEU B 228     -70.605  75.223  44.122  1.00 52.90           C
ANISOU 4623  CD2 LEU B 228     7684   5680   6734   -223  -2370   1592       C
ATOM   4624  N   GLU B 229     -74.376  77.736  47.165  1.00 62.70           N
ANISOU 4624  N   GLU B 229     9009   7006   7807   -382  -3600   1729       N
ATOM   4625  CA  GLU B 229     -75.650  78.435  47.065  1.00 63.98           C
ANISOU 4625  CA  GLU B 229     8942   7204   8162   -376  -3832   1673       C
ATOM   4626  C   GLU B 229     -75.600  79.472  45.951  1.00 62.10           C
ANISOU 4626  C   GLU B 229     8299   6905   8390   -207  -3854   1671       C
ATOM   4627  O   GLU B 229     -74.604  80.181  45.782  1.00 64.72           O
ANISOU 4627  O   GLU B 229     8576   7129   8887    -90  -3910   1791       O
ATOM   4628  CB  GLU B 229     -76.003  79.110  48.391  1.00 73.05           C
ANISOU 4628  CB  GLU B 229    10279   8334   9144   -459  -4260   1804       C
ATOM   4629  CG  GLU B 229     -76.302  78.152  49.534  1.00 81.78           C
ANISOU 4629  CG  GLU B 229    11792   9508   9772   -652  -4252   1774       C
ATOM   4630  CD  GLU B 229     -75.055  77.718  50.281  1.00 91.64           C
ANISOU 4630  CD  GLU B 229    13407  10710  10702   -708  -4169   1902       C
ATOM   4631  OE1 GLU B 229     -73.938  78.003  49.799  1.00 93.15           O
ANISOU 4631  OE1 GLU B 229    13530  10817  11046   -597  -4074   2000       O
ATOM   4632  OE2 GLU B 229     -75.193  77.096  51.355  1.00 96.69           O
ANISOU 4632  OE2 GLU B 229    14413  11391  10932   -874  -4188   1901       O
ATOM   4633  N   GLY B 230     -76.684  79.556  45.185  1.00 59.20           N
ANISOU 4633  N   GLY B 230     7655   6599   8237   -202  -3793   1527       N
ATOM   4634  CA  GLY B 230     -76.769  80.506  44.097  1.00 58.21           C
ANISOU 4634  CA  GLY B 230     7139   6430   8549    -63  -3770   1494       C
ATOM   4635  C   GLY B 230     -76.047  80.106  42.833  1.00 57.27           C
ANISOU 4635  C   GLY B 230     6913   6289   8557     23  -3397   1417       C
ATOM   4636  O   GLY B 230     -75.859  80.954  41.953  1.00 60.18           O
ANISOU 4636  O   GLY B 230     6996   6598   9271    147  -3356   1399       O
ATOM   4637  N   TYR B 231     -75.634  78.845  42.707  1.00 54.22           N
ANISOU 4637  N   TYR B 231     6744   5946   7911    -42  -3125   1363       N
ATOM   4638  CA  TYR B 231     -74.935  78.379  41.516  1.00 53.25           C
ANISOU 4638  CA  TYR B 231     6542   5806   7885     22  -2794   1292       C
ATOM   4639  C   TYR B 231     -75.730  77.343  40.731  1.00 49.75           C
ANISOU 4639  C   TYR B 231     6059   5455   7388    -49  -2537   1128       C
ATOM   4640  O   TYR B 231     -75.184  76.737  39.800  1.00 50.26           O
ANISOU 4640  O   TYR B 231     6107   5517   7474    -22  -2271   1067       O
ATOM   4641  CB  TYR B 231     -73.557  77.829  41.891  1.00 54.45           C
ANISOU 4641  CB  TYR B 231     6947   5904   7837     22  -2694   1384       C
ATOM   4642  CG  TYR B 231     -72.574  78.919  42.247  1.00 55.38           C
ANISOU 4642  CG  TYR B 231     7064   5890   8087    123  -2888   1544       C
ATOM   4643  CD1 TYR B 231     -71.965  79.677  41.255  1.00 56.40           C
ANISOU 4643  CD1 TYR B 231     6972   5925   8535    260  -2808   1535       C
ATOM   4644  CD2 TYR B 231     -72.264  79.201  43.571  1.00 57.94           C
ANISOU 4644  CD2 TYR B 231     7625   6173   8217     77  -3155   1704       C
ATOM   4645  CE1 TYR B 231     -71.069  80.681  41.570  1.00 59.36           C
ANISOU 4645  CE1 TYR B 231     7343   6153   9059    365  -2989   1678       C
ATOM   4646  CE2 TYR B 231     -71.367  80.205  43.896  1.00 60.92           C
ANISOU 4646  CE2 TYR B 231     8014   6406   8726    173  -3357   1868       C
ATOM   4647  CZ  TYR B 231     -70.773  80.941  42.891  1.00 59.69           C
ANISOU 4647  CZ  TYR B 231     7617   6145   8918    325  -3274   1853       C
ATOM   4648  OH  TYR B 231     -69.880  81.940  43.205  1.00 57.94           O
ANISOU 4648  OH  TYR B 231     7405   5756   8854    434  -3476   2012       O
ATOM   4649  N   ALA B 232     -76.999  77.128  41.082  1.00 47.32           N
ANISOU 4649  N   ALA B 232     5746   5219   7014   -143  -2628   1059       N
ATOM   4650  CA  ALA B 232     -77.931  76.330  40.281  1.00 47.36           C
ANISOU 4650  CA  ALA B 232     5682   5288   7024   -204  -2426    911       C
ATOM   4651  C   ALA B 232     -77.429  74.904  40.064  1.00 45.35           C
ANISOU 4651  C   ALA B 232     5621   5056   6554   -238  -2165    859       C
ATOM   4652  O   ALA B 232     -77.627  74.313  39.001  1.00 45.44           O
ANISOU 4652  O   ALA B 232     5550   5082   6631   -235  -1948    767       O
ATOM   4653  CB  ALA B 232     -78.223  77.008  38.940  1.00 41.91           C
ANISOU 4653  CB  ALA B 232     4684   4583   6655   -140  -2310    844       C
ATOM   4654  N   PHE B 233     -76.775  74.340  41.080  1.00 47.45           N
ANISOU 4654  N   PHE B 233     6146   5320   6562   -275  -2189    920       N
ATOM   4655  CA  PHE B 233     -76.339  72.952  40.974  1.00 48.77           C
ANISOU 4655  CA  PHE B 233     6473   5510   6549   -310  -1942    861       C
ATOM   4656  C   PHE B 233     -77.520  71.992  40.990  1.00 48.57           C
ANISOU 4656  C   PHE B 233     6495   5535   6426   -393  -1868    731       C
ATOM   4657  O   PHE B 233     -77.447  70.915  40.387  1.00 46.23           O
ANISOU 4657  O   PHE B 233     6214   5247   6105   -393  -1648    651       O
ATOM   4658  CB  PHE B 233     -75.356  72.619  42.094  1.00 53.37           C
ANISOU 4658  CB  PHE B 233     7316   6077   6886   -347  -1959    952       C
ATOM   4659  CG  PHE B 233     -73.925  72.591  41.646  1.00 53.26           C
ANISOU 4659  CG  PHE B 233     7302   6010   6926   -282  -1823   1022       C
ATOM   4660  CD1 PHE B 233     -73.385  73.658  40.948  1.00 56.68           C
ANISOU 4660  CD1 PHE B 233     7557   6376   7602   -181  -1882   1086       C
ATOM   4661  CD2 PHE B 233     -73.119  71.499  41.921  1.00 51.07           C
ANISOU 4661  CD2 PHE B 233     7194   5741   6471   -328  -1626   1013       C
ATOM   4662  CE1 PHE B 233     -72.068  73.636  40.529  1.00 55.93           C
ANISOU 4662  CE1 PHE B 233     7476   6217   7557   -131  -1760   1141       C
ATOM   4663  CE2 PHE B 233     -71.800  71.472  41.507  1.00 51.29           C
ANISOU 4663  CE2 PHE B 233     7217   5714   6556   -286  -1507   1075       C
ATOM   4664  CZ  PHE B 233     -71.274  72.542  40.810  1.00 52.39           C
ANISOU 4664  CZ  PHE B 233     7202   5781   6924   -190  -1581   1140       C
ATOM   4665  N   GLU B 234     -78.616  72.368  41.657  1.00 52.64           N
ANISOU 4665  N   GLU B 234     7030   6072   6898   -463  -2063    708       N
ATOM   4666  CA  GLU B 234     -79.826  71.554  41.621  1.00 56.16           C
ANISOU 4666  CA  GLU B 234     7514   6544   7282   -543  -2005    578       C
ATOM   4667  C   GLU B 234     -80.320  71.357  40.195  1.00 52.12           C
ANISOU 4667  C   GLU B 234     6795   6025   6983   -511  -1848    503       C
ATOM   4668  O   GLU B 234     -80.987  70.358  39.899  1.00 55.81           O
ANISOU 4668  O   GLU B 234     7312   6490   7404   -552  -1721    403       O
ATOM   4669  CB  GLU B 234     -80.926  72.198  42.468  1.00 67.20           C
ANISOU 4669  CB  GLU B 234     8936   7958   8640   -632  -2270    569       C
ATOM   4670  CG  GLU B 234     -80.474  72.717  43.825  1.00 75.86           C
ANISOU 4670  CG  GLU B 234    10226   9056   9542   -670  -2498    673       C
ATOM   4671  CD  GLU B 234     -80.043  74.172  43.782  1.00 80.50           C
ANISOU 4671  CD  GLU B 234    10641   9616  10328   -596  -2726    808       C
ATOM   4672  OE1 GLU B 234     -79.748  74.676  42.678  1.00 80.63           O
ANISOU 4672  OE1 GLU B 234    10408   9612  10617   -496  -2637    818       O
ATOM   4673  OE2 GLU B 234     -80.007  74.813  44.854  1.00 84.20           O
ANISOU 4673  OE2 GLU B 234    11231  10078  10683   -639  -3000    901       O
ATOM   4674  N   HIS B 235     -80.005  72.294  39.304  1.00 46.72           N
ANISOU 4674  N   HIS B 235     5895   5327   6530   -440  -1851    548       N
ATOM   4675  CA  HIS B 235     -80.406  72.238  37.905  1.00 41.98           C
ANISOU 4675  CA  HIS B 235     5118   4720   6115   -424  -1696    486       C
ATOM   4676  C   HIS B 235     -79.282  71.760  36.995  1.00 42.38           C
ANISOU 4676  C   HIS B 235     5163   4749   6191   -351  -1490    499       C
ATOM   4677  O   HIS B 235     -79.477  70.837  36.200  1.00 43.37           O
ANISOU 4677  O   HIS B 235     5304   4869   6304   -367  -1329    436       O
ATOM   4678  CB  HIS B 235     -80.891  73.621  37.455  1.00 40.41           C
ANISOU 4678  CB  HIS B 235     4670   4518   6164   -411  -1807    502       C
ATOM   4679  CG  HIS B 235     -81.255  73.693  36.006  1.00 44.54           C
ANISOU 4679  CG  HIS B 235     5025   5035   6863   -412  -1628    440       C
ATOM   4680  ND1 HIS B 235     -82.461  73.237  35.519  1.00 47.21           N
ANISOU 4680  ND1 HIS B 235     5343   5380   7214   -506  -1569    359       N
ATOM   4681  CD2 HIS B 235     -80.573  74.169  34.937  1.00 45.80           C
ANISOU 4681  CD2 HIS B 235     5053   5172   7176   -344  -1489    445       C
ATOM   4682  CE1 HIS B 235     -82.507  73.429  34.212  1.00 47.74           C
ANISOU 4682  CE1 HIS B 235     5282   5436   7421   -503  -1402    328       C
ATOM   4683  NE2 HIS B 235     -81.373  73.992  33.835  1.00 45.93           N
ANISOU 4683  NE2 HIS B 235     4985   5193   7274   -406  -1346    371       N
ATOM   4684  N   ILE B 236     -78.099  72.365  37.109  1.00 46.18           N
ANISOU 4684  N   ILE B 236     5630   5207   6710   -277  -1511    583       N
ATOM   4685  CA  ILE B 236     -77.015  72.082  36.173  1.00 44.13           C
ANISOU 4685  CA  ILE B 236     5347   4918   6501   -217  -1333    591       C
ATOM   4686  C   ILE B 236     -76.511  70.654  36.345  1.00 42.64           C
ANISOU 4686  C   ILE B 236     5327   4739   6137   -238  -1198    568       C
ATOM   4687  O   ILE B 236     -76.389  69.900  35.373  1.00 39.28           O
ANISOU 4687  O   ILE B 236     4879   4306   5738   -236  -1046    518       O
ATOM   4688  CB  ILE B 236     -75.876  73.102  36.352  1.00 39.89           C
ANISOU 4688  CB  ILE B 236     4769   4333   6055   -136  -1401    686       C
ATOM   4689  CG1 ILE B 236     -76.381  74.519  36.079  1.00 38.21           C
ANISOU 4689  CG1 ILE B 236     4342   4100   6075    -95  -1521    693       C
ATOM   4690  CG2 ILE B 236     -74.710  72.758  35.442  1.00 37.55           C
ANISOU 4690  CG2 ILE B 236     4474   3999   5796    -90  -1221    685       C
ATOM   4691  CD1 ILE B 236     -75.390  75.598  36.454  1.00 39.74           C
ANISOU 4691  CD1 ILE B 236     4495   4224   6381     -2  -1639    794       C
ATOM   4692  N   VAL B 237     -76.206  70.263  37.576  1.00 42.51           N
ANISOU 4692  N   VAL B 237     5480   4734   5940   -265  -1252    602       N
ATOM   4693  CA  VAL B 237     -75.573  68.980  37.854  1.00 40.14           C
ANISOU 4693  CA  VAL B 237     5319   4438   5495   -283  -1104    579       C
ATOM   4694  C   VAL B 237     -76.596  67.914  38.218  1.00 43.83           C
ANISOU 4694  C   VAL B 237     5871   4928   5854   -339  -1061    480       C
ATOM   4695  O   VAL B 237     -76.557  66.802  37.692  1.00 45.38           O
ANISOU 4695  O   VAL B 237     6068   5116   6058   -332   -913    416       O
ATOM   4696  CB  VAL B 237     -74.510  69.142  38.963  1.00 39.10           C
ANISOU 4696  CB  VAL B 237     5339   4297   5221   -292  -1141    672       C
ATOM   4697  CG1 VAL B 237     -73.764  67.838  39.175  1.00 40.83           C
ANISOU 4697  CG1 VAL B 237     5668   4523   5323   -316   -950    640       C
ATOM   4698  CG2 VAL B 237     -73.546  70.261  38.605  1.00 38.80           C
ANISOU 4698  CG2 VAL B 237     5218   4209   5315   -227  -1202    772       C
ATOM   4699  N   TYR B 238     -77.523  68.236  39.123  1.00 42.89           N
ANISOU 4699  N   TYR B 238     5826   4826   5644   -395  -1202    462       N
ATOM   4700  CA  TYR B 238     -78.496  67.245  39.567  1.00 40.36           C
ANISOU 4700  CA  TYR B 238     5612   4508   5214   -453  -1161    355       C
ATOM   4701  C   TYR B 238     -79.609  67.028  38.550  1.00 41.62           C
ANISOU 4701  C   TYR B 238     5651   4646   5516   -459  -1141    281       C
ATOM   4702  O   TYR B 238     -80.096  65.902  38.405  1.00 40.48           O
ANISOU 4702  O   TYR B 238     5559   4474   5347   -469  -1036    194       O
ATOM   4703  CB  TYR B 238     -79.084  67.656  40.918  1.00 41.16           C
ANISOU 4703  CB  TYR B 238     5866   4628   5144   -530  -1329    355       C
ATOM   4704  CG  TYR B 238     -78.095  67.578  42.060  1.00 47.99           C
ANISOU 4704  CG  TYR B 238     6925   5507   5801   -556  -1325    417       C
ATOM   4705  CD1 TYR B 238     -77.942  66.408  42.791  1.00 50.99           C
ANISOU 4705  CD1 TYR B 238     7489   5891   5994   -601  -1166    338       C
ATOM   4706  CD2 TYR B 238     -77.314  68.672  42.405  1.00 50.20           C
ANISOU 4706  CD2 TYR B 238     7208   5786   6080   -538  -1469    553       C
ATOM   4707  CE1 TYR B 238     -77.041  66.331  43.836  1.00 50.64           C
ANISOU 4707  CE1 TYR B 238     7641   5861   5740   -648  -1134    394       C
ATOM   4708  CE2 TYR B 238     -76.408  68.605  43.447  1.00 52.56           C
ANISOU 4708  CE2 TYR B 238     7713   6086   6171   -579  -1467    626       C
ATOM   4709  CZ  TYR B 238     -76.278  67.433  44.160  1.00 54.28           C
ANISOU 4709  CZ  TYR B 238     8126   6320   6178   -644  -1291    547       C
ATOM   4710  OH  TYR B 238     -75.378  67.360  45.198  1.00 58.58           O
ANISOU 4710  OH  TYR B 238     8893   6866   6497   -707  -1262    619       O
ATOM   4711  N   GLY B 239     -80.021  68.072  37.847  1.00 44.40           N
ANISOU 4711  N   GLY B 239     5845   5001   6025   -455  -1230    314       N
ATOM   4712  CA  GLY B 239     -81.043  67.915  36.822  1.00 42.90           C
ANISOU 4712  CA  GLY B 239     5554   4786   5959   -482  -1193    256       C
ATOM   4713  C   GLY B 239     -82.448  68.044  37.374  1.00 43.39           C
ANISOU 4713  C   GLY B 239     5650   4842   5994   -571  -1314    196       C
ATOM   4714  O   GLY B 239     -82.740  67.696  38.518  1.00 44.89           O
ANISOU 4714  O   GLY B 239     5993   5034   6029   -614  -1379    158       O
ATOM   4715  N   ASP B 240     -83.341  68.554  36.530  1.00 42.12           N
ANISOU 4715  N   ASP B 240     5353   4668   5982   -614  -1333    179       N
ATOM   4716  CA  ASP B 240     -84.740  68.766  36.879  1.00 46.10           C
ANISOU 4716  CA  ASP B 240     5858   5157   6499   -717  -1448    122       C
ATOM   4717  C   ASP B 240     -85.600  67.792  36.085  1.00 43.79           C
ANISOU 4717  C   ASP B 240     5604   4798   6236   -759  -1337     55       C
ATOM   4718  O   ASP B 240     -85.570  67.795  34.849  1.00 40.28           O
ANISOU 4718  O   ASP B 240     5068   4336   5902   -749  -1232     75       O
ATOM   4719  CB  ASP B 240     -85.160  70.210  36.600  1.00 52.02           C
ANISOU 4719  CB  ASP B 240     6403   5939   7424   -752  -1565    158       C
ATOM   4720  CG  ASP B 240     -86.578  70.506  37.054  1.00 56.99           C
ANISOU 4720  CG  ASP B 240     7017   6556   8080   -876  -1707    101       C
ATOM   4721  OD1 ASP B 240     -87.153  69.691  37.806  1.00 60.41           O
ANISOU 4721  OD1 ASP B 240     7633   6958   8364   -932  -1744     36       O
ATOM   4722  OD2 ASP B 240     -87.121  71.557  36.653  1.00 59.67           O
ANISOU 4722  OD2 ASP B 240     7156   6913   8601   -923  -1774    112       O
ATOM   4723  N   PHE B 241     -86.369  66.968  36.795  1.00 45.57           N
ANISOU 4723  N   PHE B 241     5983   4975   6355   -810  -1363    -26       N
ATOM   4724  CA  PHE B 241     -87.235  65.972  36.182  1.00 44.79           C
ANISOU 4724  CA  PHE B 241     5947   4784   6288   -844  -1282    -88       C
ATOM   4725  C   PHE B 241     -88.711  66.250  36.432  1.00 48.49           C
ANISOU 4725  C   PHE B 241     6431   5207   6788   -975  -1391   -149       C
ATOM   4726  O   PHE B 241     -89.558  65.432  36.060  1.00 49.67           O
ANISOU 4726  O   PHE B 241     6658   5256   6958  -1016  -1344   -203       O
ATOM   4727  CB  PHE B 241     -86.878  64.575  36.694  1.00 43.56           C
ANISOU 4727  CB  PHE B 241     5957   4576   6017   -779  -1187   -151       C
ATOM   4728  CG  PHE B 241     -85.416  64.254  36.611  1.00 44.23           C
ANISOU 4728  CG  PHE B 241     6028   4707   6070   -668  -1084   -100       C
ATOM   4729  CD1 PHE B 241     -84.886  63.673  35.472  1.00 43.95           C
ANISOU 4729  CD1 PHE B 241     5932   4642   6125   -602   -973    -63       C
ATOM   4730  CD2 PHE B 241     -84.571  64.529  37.674  1.00 50.53           C
ANISOU 4730  CD2 PHE B 241     6887   5572   6741   -645  -1108    -83       C
ATOM   4731  CE1 PHE B 241     -83.538  63.375  35.393  1.00 44.54           C
ANISOU 4731  CE1 PHE B 241     5986   4756   6182   -516   -888    -21       C
ATOM   4732  CE2 PHE B 241     -83.223  64.235  37.601  1.00 50.51           C
ANISOU 4732  CE2 PHE B 241     6873   5603   6716   -562  -1006    -34       C
ATOM   4733  CZ  PHE B 241     -82.706  63.656  36.459  1.00 47.26           C
ANISOU 4733  CZ  PHE B 241     6380   5164   6414   -497   -895     -8       C
ATOM   4734  N   SER B 242     -89.038  67.384  37.055  1.00 50.08           N
ANISOU 4734  N   SER B 242     6555   5468   7006  -1044  -1549   -137       N
ATOM   4735  CA  SER B 242     -90.421  67.668  37.414  1.00 46.96           C
ANISOU 4735  CA  SER B 242     6171   5032   6640  -1186  -1675   -201       C
ATOM   4736  C   SER B 242     -91.287  67.989  36.204  1.00 45.71           C
ANISOU 4736  C   SER B 242     5874   4832   6662  -1271  -1620   -188       C
ATOM   4737  O   SER B 242     -92.510  67.831  36.276  1.00 49.23           O
ANISOU 4737  O   SER B 242     6366   5205   7136  -1396  -1672   -250       O
ATOM   4738  CB  SER B 242     -90.472  68.827  38.410  1.00 47.98           C
ANISOU 4738  CB  SER B 242     6237   5238   6754  -1238  -1892   -181       C
ATOM   4739  OG  SER B 242     -89.778  69.957  37.909  1.00 49.69           O
ANISOU 4739  OG  SER B 242     6233   5532   7114  -1182  -1910    -86       O
ATOM   4740  N   HIS B 243     -90.690  68.428  35.102  1.00 41.94           N
ANISOU 4740  N   HIS B 243     5247   4392   6296  -1220  -1508   -116       N
ATOM   4741  CA  HIS B 243     -91.425  68.840  33.917  1.00 41.01           C
ANISOU 4741  CA  HIS B 243     5005   4247   6331  -1316  -1427   -100       C
ATOM   4742  C   HIS B 243     -91.238  67.823  32.798  1.00 39.80           C
ANISOU 4742  C   HIS B 243     4952   4018   6151  -1280  -1259    -77       C
ATOM   4743  O   HIS B 243     -90.373  66.946  32.858  1.00 38.53           O
ANISOU 4743  O   HIS B 243     4900   3844   5894  -1160  -1205    -66       O
ATOM   4744  CB  HIS B 243     -90.974  70.231  33.457  1.00 51.62           C
ANISOU 4744  CB  HIS B 243     6100   5685   7830  -1306  -1418    -49       C
ATOM   4745  CG  HIS B 243     -91.204  71.306  34.473  1.00 67.72           C
ANISOU 4745  CG  HIS B 243     8008   7786   9936  -1340  -1619    -57       C
ATOM   4746  ND1 HIS B 243     -90.639  71.277  35.730  1.00 71.35           N
ANISOU 4746  ND1 HIS B 243     8562   8280  10266  -1272  -1773    -51       N
ATOM   4747  CD2 HIS B 243     -91.940  72.442  34.419  1.00 73.63           C
ANISOU 4747  CD2 HIS B 243     8538   8566  10872  -1442  -1701    -67       C
ATOM   4748  CE1 HIS B 243     -91.016  72.347  36.406  1.00 73.89           C
ANISOU 4748  CE1 HIS B 243     8743   8647  10683  -1328  -1970    -47       C
ATOM   4749  NE2 HIS B 243     -91.806  73.071  35.633  1.00 75.12           N
ANISOU 4749  NE2 HIS B 243     8689   8804  11051  -1425  -1934    -60       N
ATOM   4750  N   SER B 244     -92.074  67.955  31.764  1.00 38.88           N
ANISOU 4750  N   SER B 244     4798   3849   6124  -1396  -1183    -65       N
ATOM   4751  CA  SER B 244     -91.991  67.044  30.627  1.00 39.33           C
ANISOU 4751  CA  SER B 244     4969   3824   6150  -1384  -1054    -25       C
ATOM   4752  C   SER B 244     -90.643  67.161  29.931  1.00 41.43           C
ANISOU 4752  C   SER B 244     5184   4159   6398  -1267   -952     34       C
ATOM   4753  O   SER B 244     -90.069  66.155  29.498  1.00 40.30           O
ANISOU 4753  O   SER B 244     5160   3967   6185  -1186   -904     62       O
ATOM   4754  CB  SER B 244     -93.125  67.324  29.642  1.00 40.21           C
ANISOU 4754  CB  SER B 244     5064   3872   6344  -1558   -988    -10       C
ATOM   4755  OG  SER B 244     -92.882  68.517  28.916  1.00 44.48           O
ANISOU 4755  OG  SER B 244     5413   4504   6983  -1607   -891     17       O
ATOM   4756  N   GLN B 245     -90.122  68.378  29.816  1.00 42.57           N
ANISOU 4756  N   GLN B 245     5145   4407   6623  -1257   -926     49       N
ATOM   4757  CA  GLN B 245     -88.812  68.607  29.226  1.00 39.32           C
ANISOU 4757  CA  GLN B 245     4684   4053   6203  -1150   -832     92       C
ATOM   4758  C   GLN B 245     -87.760  68.557  30.326  1.00 37.24           C
ANISOU 4758  C   GLN B 245     4424   3844   5883  -1011   -918     94       C
ATOM   4759  O   GLN B 245     -87.844  69.301  31.310  1.00 39.69           O
ANISOU 4759  O   GLN B 245     4648   4204   6227  -1007  -1033     79       O
ATOM   4760  CB  GLN B 245     -88.772  69.947  28.493  1.00 42.86           C
ANISOU 4760  CB  GLN B 245     4937   4563   6786  -1204   -737     95       C
ATOM   4761  CG  GLN B 245     -87.563  70.118  27.582  1.00 50.82           C
ANISOU 4761  CG  GLN B 245     5929   5601   7778  -1126   -604    125       C
ATOM   4762  CD  GLN B 245     -87.599  69.197  26.372  1.00 56.51           C
ANISOU 4762  CD  GLN B 245     6820   6255   8396  -1176   -497    155       C
ATOM   4763  OE1 GLN B 245     -88.613  68.557  26.089  1.00 57.30           O
ANISOU 4763  OE1 GLN B 245     7033   6279   8459  -1278   -507    162       O
ATOM   4764  NE2 GLN B 245     -86.487  69.131  25.649  1.00 57.84           N
ANISOU 4764  NE2 GLN B 245     7018   6441   8518  -1110   -410    178       N
ATOM   4765  N   LEU B 246     -86.781  67.672  30.161  1.00 36.79           N
ANISOU 4765  N   LEU B 246     4469   3773   5737   -908   -871    118       N
ATOM   4766  CA  LEU B 246     -85.719  67.529  31.146  1.00 38.55           C
ANISOU 4766  CA  LEU B 246     4714   4041   5894   -793   -921    126       C
ATOM   4767  C   LEU B 246     -84.878  68.798  31.203  1.00 44.47           C
ANISOU 4767  C   LEU B 246     5312   4866   6718   -745   -926    159       C
ATOM   4768  O   LEU B 246     -84.544  69.389  30.172  1.00 48.58           O
ANISOU 4768  O   LEU B 246     5741   5398   7318   -749   -827    177       O
ATOM   4769  CB  LEU B 246     -84.847  66.322  30.801  1.00 36.16           C
ANISOU 4769  CB  LEU B 246     4520   3703   5516   -708   -851    142       C
ATOM   4770  CG  LEU B 246     -84.152  65.588  31.949  1.00 37.38           C
ANISOU 4770  CG  LEU B 246     4758   3867   5576   -622   -881    125       C
ATOM   4771  CD1 LEU B 246     -83.815  64.168  31.530  1.00 40.13           C
ANISOU 4771  CD1 LEU B 246     5197   4151   5899   -567   -816    118       C
ATOM   4772  CD2 LEU B 246     -82.895  66.315  32.396  1.00 34.18           C
ANISOU 4772  CD2 LEU B 246     4291   3536   5159   -552   -884    167       C
ATOM   4773  N   GLY B 247     -84.542  69.222  32.418  1.00 44.44           N
ANISOU 4773  N   GLY B 247     5298   4903   6685   -701  -1044    167       N
ATOM   4774  CA  GLY B 247     -83.807  70.456  32.641  1.00 42.73           C
ANISOU 4774  CA  GLY B 247     4942   4736   6558   -646  -1091    209       C
ATOM   4775  C   GLY B 247     -82.425  70.179  33.215  1.00 46.14           C
ANISOU 4775  C   GLY B 247     5455   5181   6896   -541  -1094    256       C
ATOM   4776  O   GLY B 247     -82.285  69.435  34.186  1.00 48.99           O
ANISOU 4776  O   GLY B 247     5958   5541   7115   -530  -1144    251       O
ATOM   4777  N   GLY B 248     -81.418  70.791  32.594  1.00 44.94           N
ANISOU 4777  N   GLY B 248     5216   5034   6826   -474  -1024    293       N
ATOM   4778  CA  GLY B 248     -80.061  70.699  33.110  1.00 44.66           C
ANISOU 4778  CA  GLY B 248     5244   5001   6725   -387  -1030    346       C
ATOM   4779  C   GLY B 248     -79.437  69.334  32.887  1.00 41.75           C
ANISOU 4779  C   GLY B 248     5013   4615   6236   -368   -922    338       C
ATOM   4780  O   GLY B 248     -79.565  68.731  31.815  1.00 37.89           O
ANISOU 4780  O   GLY B 248     4530   4104   5763   -388   -816    312       O
ATOM   4781  N   LEU B 249     -78.738  68.845  33.916  1.00 43.49           N
ANISOU 4781  N   LEU B 249     5345   4843   6337   -336   -952    365       N
ATOM   4782  CA  LEU B 249     -78.052  67.551  33.894  1.00 44.27           C
ANISOU 4782  CA  LEU B 249     5547   4929   6345   -315   -849    353       C
ATOM   4783  C   LEU B 249     -76.987  67.520  32.792  1.00 46.36           C
ANISOU 4783  C   LEU B 249     5760   5175   6679   -276   -746    378       C
ATOM   4784  O   LEU B 249     -77.110  66.837  31.773  1.00 43.33           O
ANISOU 4784  O   LEU B 249     5372   4770   6322   -289   -672    350       O
ATOM   4785  CB  LEU B 249     -79.060  66.406  33.727  1.00 42.52           C
ANISOU 4785  CB  LEU B 249     5386   4683   6088   -354   -815    283       C
ATOM   4786  CG  LEU B 249     -78.613  65.006  34.159  1.00 41.98           C
ANISOU 4786  CG  LEU B 249     5417   4598   5938   -328   -735    250       C
ATOM   4787  CD1 LEU B 249     -78.490  64.917  35.674  1.00 43.08           C
ANISOU 4787  CD1 LEU B 249     5667   4762   5940   -339   -767    239       C
ATOM   4788  CD2 LEU B 249     -79.576  63.956  33.631  1.00 40.59           C
ANISOU 4788  CD2 LEU B 249     5266   4367   5790   -344   -706    188       C
ATOM   4789  N   HIS B 250     -75.919  68.282  33.035  1.00 44.63           N
ANISOU 4789  N   HIS B 250     5519   4955   6484   -233   -759    435       N
ATOM   4790  CA  HIS B 250     -74.858  68.454  32.052  1.00 41.58           C
ANISOU 4790  CA  HIS B 250     5090   4541   6168   -203   -673    452       C
ATOM   4791  C   HIS B 250     -73.514  67.887  32.488  1.00 38.14           C
ANISOU 4791  C   HIS B 250     4727   4091   5672   -180   -627    492       C
ATOM   4792  O   HIS B 250     -72.554  67.956  31.712  1.00 32.57           O
ANISOU 4792  O   HIS B 250     4000   3355   5020   -166   -563    501       O
ATOM   4793  CB  HIS B 250     -74.694  69.940  31.706  1.00 40.25           C
ANISOU 4793  CB  HIS B 250     4812   4353   6129   -171   -703    472       C
ATOM   4794  CG  HIS B 250     -75.926  70.560  31.126  1.00 41.31           C
ANISOU 4794  CG  HIS B 250     4843   4500   6353   -207   -713    425       C
ATOM   4795  ND1 HIS B 250     -76.314  70.361  29.819  1.00 40.44           N
ANISOU 4795  ND1 HIS B 250     4706   4381   6276   -251   -606    374       N
ATOM   4796  CD2 HIS B 250     -76.860  71.370  31.677  1.00 40.74           C
ANISOU 4796  CD2 HIS B 250     4690   4446   6342   -220   -817    424       C
ATOM   4797  CE1 HIS B 250     -77.434  71.022  29.588  1.00 39.57           C
ANISOU 4797  CE1 HIS B 250     4504   4285   6246   -295   -619    341       C
ATOM   4798  NE2 HIS B 250     -77.786  71.643  30.699  1.00 41.76           N
ANISOU 4798  NE2 HIS B 250     4731   4581   6556   -274   -751    367       N
ATOM   4799  N   LEU B 251     -73.409  67.335  33.692  1.00 38.25           N
ANISOU 4799  N   LEU B 251     4835   4125   5572   -190   -647    508       N
ATOM   4800  CA  LEU B 251     -72.177  66.720  34.166  1.00 39.87           C
ANISOU 4800  CA  LEU B 251     5110   4321   5718   -191   -576    541       C
ATOM   4801  C   LEU B 251     -72.389  65.224  34.338  1.00 43.18           C
ANISOU 4801  C   LEU B 251     5567   4758   6081   -213   -489    480       C
ATOM   4802  O   LEU B 251     -73.384  64.800  34.935  1.00 49.28           O
ANISOU 4802  O   LEU B 251     6385   5550   6788   -229   -510    432       O
ATOM   4803  CB  LEU B 251     -71.713  67.345  35.482  1.00 40.85           C
ANISOU 4803  CB  LEU B 251     5329   4445   5748   -196   -645    617       C
ATOM   4804  CG  LEU B 251     -70.696  68.478  35.333  1.00 44.38           C
ANISOU 4804  CG  LEU B 251     5753   4837   6274   -160   -689    700       C
ATOM   4805  CD1 LEU B 251     -71.363  69.751  34.831  1.00 43.17           C
ANISOU 4805  CD1 LEU B 251     5484   4666   6252   -115   -792    700       C
ATOM   4806  CD2 LEU B 251     -69.964  68.719  36.643  1.00 51.87           C
ANISOU 4806  CD2 LEU B 251     6840   5768   7099   -181   -738    794       C
ATOM   4807  N   LEU B 252     -71.442  64.434  33.823  1.00 40.39           N
ANISOU 4807  N   LEU B 252     5186   4389   5770   -213   -397    476       N
ATOM   4808  CA  LEU B 252     -71.589  62.982  33.829  1.00 41.67           C
ANISOU 4808  CA  LEU B 252     5340   4557   5938   -217   -317    412       C
ATOM   4809  C   LEU B 252     -71.742  62.428  35.238  1.00 44.49           C
ANISOU 4809  C   LEU B 252     5789   4938   6178   -237   -259    384       C
ATOM   4810  O   LEU B 252     -72.446  61.431  35.438  1.00 47.33           O
ANISOU 4810  O   LEU B 252     6150   5294   6537   -229   -213    305       O
ATOM   4811  CB  LEU B 252     -70.391  62.334  33.136  1.00 38.31           C
ANISOU 4811  CB  LEU B 252     4851   4111   5595   -221   -246    422       C
ATOM   4812  CG  LEU B 252     -70.451  60.815  32.977  1.00 40.34           C
ANISOU 4812  CG  LEU B 252     5050   4362   5916   -212   -180    358       C
ATOM   4813  CD1 LEU B 252     -71.540  60.426  31.989  1.00 42.04           C
ANISOU 4813  CD1 LEU B 252     5227   4550   6196   -187   -256    321       C
ATOM   4814  CD2 LEU B 252     -69.107  60.266  32.544  1.00 41.44           C
ANISOU 4814  CD2 LEU B 252     5118   4488   6140   -233   -122    375       C
ATOM   4815  N   ILE B 253     -71.092  63.049  36.225  1.00 42.48           N
ANISOU 4815  N   ILE B 253     5627   4696   5816   -267   -257    445       N
ATOM   4816  CA  ILE B 253     -71.217  62.572  37.598  1.00 41.34           C
ANISOU 4816  CA  ILE B 253     5611   4577   5518   -310   -190    416       C
ATOM   4817  C   ILE B 253     -72.650  62.725  38.088  1.00 37.92           C
ANISOU 4817  C   ILE B 253     5242   4157   5007   -315   -277    361       C
ATOM   4818  O   ILE B 253     -73.133  61.913  38.887  1.00 36.99           O
ANISOU 4818  O   ILE B 253     5209   4049   4798   -340   -198    279       O
ATOM   4819  CB  ILE B 253     -70.209  63.302  38.511  1.00 40.82           C
ANISOU 4819  CB  ILE B 253     5666   4512   5331   -358   -195    517       C
ATOM   4820  CG1 ILE B 253     -70.219  62.697  39.916  1.00 47.22           C
ANISOU 4820  CG1 ILE B 253     6642   5351   5949   -428    -92    484       C
ATOM   4821  CG2 ILE B 253     -70.495  64.797  38.553  1.00 36.08           C
ANISOU 4821  CG2 ILE B 253     5091   3897   4719   -340   -385    603       C
ATOM   4822  CD1 ILE B 253     -69.181  63.290  40.843  1.00 50.06           C
ANISOU 4822  CD1 ILE B 253     7156   5702   6163   -498    -86    597       C
ATOM   4823  N   GLY B 254     -73.360  63.748  37.609  1.00 36.66           N
ANISOU 4823  N   GLY B 254     5040   3993   4895   -297   -428    392       N
ATOM   4824  CA  GLY B 254     -74.771  63.867  37.926  1.00 34.38           C
ANISOU 4824  CA  GLY B 254     4790   3711   4564   -315   -518    334       C
ATOM   4825  C   GLY B 254     -75.601  62.762  37.312  1.00 38.49           C
ANISOU 4825  C   GLY B 254     5258   4203   5164   -294   -453    233       C
ATOM   4826  O   GLY B 254     -76.583  62.313  37.910  1.00 44.37           O
ANISOU 4826  O   GLY B 254     6081   4937   5842   -318   -458    153       O
ATOM   4827  N   LEU B 255     -75.222  62.304  36.116  1.00 36.10           N
ANISOU 4827  N   LEU B 255     4839   3875   5003   -254   -405    237       N
ATOM   4828  CA  LEU B 255     -75.916  61.175  35.507  1.00 32.46           C
ANISOU 4828  CA  LEU B 255     4335   3369   4630   -227   -365    161       C
ATOM   4829  C   LEU B 255     -75.619  59.882  36.253  1.00 36.79           C
ANISOU 4829  C   LEU B 255     4916   3903   5158   -212   -227     83       C
ATOM   4830  O   LEU B 255     -76.508  59.040  36.424  1.00 39.11           O
ANISOU 4830  O   LEU B 255     5233   4152   5476   -194   -200     -8       O
ATOM   4831  CB  LEU B 255     -75.524  61.040  34.035  1.00 31.43           C
ANISOU 4831  CB  LEU B 255     4092   3213   4637   -200   -376    198       C
ATOM   4832  CG  LEU B 255     -76.114  61.988  32.988  1.00 35.72           C
ANISOU 4832  CG  LEU B 255     4596   3748   5227   -219   -470    238       C
ATOM   4833  CD1 LEU B 255     -75.480  63.367  33.054  1.00 34.35           C
ANISOU 4833  CD1 LEU B 255     4405   3613   5035   -230   -505    305       C
ATOM   4834  CD2 LEU B 255     -75.960  61.395  31.594  1.00 36.44           C
ANISOU 4834  CD2 LEU B 255     4630   3799   5419   -207   -469    248       C
ATOM   4835  N   ALA B 256     -74.374  59.707  36.702  1.00 38.73           N
ANISOU 4835  N   ALA B 256     5162   4181   5374   -221   -125    110       N
ATOM   4836  CA  ALA B 256     -74.009  58.491  37.420  1.00 40.60           C
ANISOU 4836  CA  ALA B 256     5409   4410   5608   -216     44     26       C
ATOM   4837  C   ALA B 256     -74.763  58.384  38.737  1.00 41.76           C
ANISOU 4837  C   ALA B 256     5717   4564   5586   -256     91    -56       C
ATOM   4838  O   ALA B 256     -75.136  57.284  39.162  1.00 46.35           O
ANISOU 4838  O   ALA B 256     6308   5110   6193   -235    217   -175       O
ATOM   4839  CB  ALA B 256     -72.500  58.453  37.656  1.00 42.72           C
ANISOU 4839  CB  ALA B 256     5652   4713   5868   -245    152     82       C
ATOM   4840  N   LYS B 257     -74.998  59.519  39.398  1.00 39.33           N
ANISOU 4840  N   LYS B 257     5539   4294   5111   -315    -16      0       N
ATOM   4841  CA  LYS B 257     -75.756  59.500  40.643  1.00 42.24           C
ANISOU 4841  CA  LYS B 257     6091   4669   5290   -373     -6    -76       C
ATOM   4842  C   LYS B 257     -77.205  59.104  40.397  1.00 46.17           C
ANISOU 4842  C   LYS B 257     6588   5109   5846   -350    -64   -177       C
ATOM   4843  O   LYS B 257     -77.769  58.292  41.140  1.00 48.60           O
ANISOU 4843  O   LYS B 257     6994   5384   6090   -364     40   -306       O
ATOM   4844  CB  LYS B 257     -75.676  60.867  41.321  1.00 40.87           C
ANISOU 4844  CB  LYS B 257     6045   4540   4944   -441   -162     27       C
ATOM   4845  CG  LYS B 257     -76.287  60.911  42.708  1.00 41.41           C
ANISOU 4845  CG  LYS B 257     6341   4623   4771   -528   -173    -36       C
ATOM   4846  CD  LYS B 257     -76.096  62.276  43.346  1.00 43.84           C
ANISOU 4846  CD  LYS B 257     6766   4968   4923   -591   -367     91       C
ATOM   4847  CE  LYS B 257     -76.615  62.292  44.774  1.00 51.83           C
ANISOU 4847  CE  LYS B 257     8042   5995   5657   -698   -394     35       C
ATOM   4848  NZ  LYS B 257     -75.915  61.293  45.627  1.00 58.53           N
ANISOU 4848  NZ  LYS B 257     9039   6853   6348   -752   -137    -37       N
ATOM   4849  N   ARG B 258     -77.822  59.659  39.352  1.00 46.96           N
ANISOU 4849  N   ARG B 258     6586   5187   6068   -324   -214   -127       N
ATOM   4850  CA  ARG B 258     -79.204  59.318  39.035  1.00 47.17           C
ANISOU 4850  CA  ARG B 258     6618   5145   6159   -317   -274   -207       C
ATOM   4851  C   ARG B 258     -79.333  57.879  38.554  1.00 45.83           C
ANISOU 4851  C   ARG B 258     6375   4893   6144   -240   -153   -297       C
ATOM   4852  O   ARG B 258     -80.352  57.229  38.813  1.00 47.35           O
ANISOU 4852  O   ARG B 258     6629   5007   6354   -233   -136   -406       O
ATOM   4853  CB  ARG B 258     -79.747  60.284  37.980  1.00 48.70           C
ANISOU 4853  CB  ARG B 258     6719   5337   6446   -324   -438   -123       C
ATOM   4854  CG  ARG B 258     -81.152  59.971  37.478  1.00 57.12           C
ANISOU 4854  CG  ARG B 258     7788   6323   7593   -334   -502   -184       C
ATOM   4855  CD  ARG B 258     -82.226  60.471  38.434  1.00 63.10           C
ANISOU 4855  CD  ARG B 258     8674   7077   8224   -417   -594   -244       C
ATOM   4856  NE  ARG B 258     -83.568  60.286  37.885  1.00 64.81           N
ANISOU 4856  NE  ARG B 258     8890   7206   8529   -444   -662   -290       N
ATOM   4857  CZ  ARG B 258     -84.681  60.729  38.461  1.00 69.27           C
ANISOU 4857  CZ  ARG B 258     9544   7751   9026   -530   -766   -343       C
ATOM   4858  NH1 ARG B 258     -84.618  61.388  39.610  1.00 71.79           N
ANISOU 4858  NH1 ARG B 258     9965   8135   9177   -595   -833   -354       N
ATOM   4859  NH2 ARG B 258     -85.858  60.514  37.889  1.00 70.52           N
ANISOU 4859  NH2 ARG B 258     9700   7816   9278   -564   -816   -380       N
ATOM   4860  N   PHE B 259     -78.310  57.359  37.873  1.00 48.35           N
ANISOU 4860  N   PHE B 259     6561   5217   6591   -182    -78   -255       N
ATOM   4861  CA  PHE B 259     -78.428  56.040  37.258  1.00 53.71           C
ANISOU 4861  CA  PHE B 259     7135   5809   7462    -98    -11   -320       C
ATOM   4862  C   PHE B 259     -78.462  54.932  38.303  1.00 56.46           C
ANISOU 4862  C   PHE B 259     7530   6119   7801    -73    175   -467       C
ATOM   4863  O   PHE B 259     -79.205  53.955  38.152  1.00 58.17           O
ANISOU 4863  O   PHE B 259     7721   6229   8151     -8    205   -565       O
ATOM   4864  CB  PHE B 259     -77.282  55.814  36.276  1.00 58.33           C
ANISOU 4864  CB  PHE B 259     7561   6413   8187    -56     -5   -235       C
ATOM   4865  CG  PHE B 259     -77.443  54.580  35.439  1.00 69.87           C
ANISOU 4865  CG  PHE B 259     8899   7779   9870     31     -6   -271       C
ATOM   4866  CD1 PHE B 259     -78.229  54.602  34.298  1.00 72.78           C
ANISOU 4866  CD1 PHE B 259     9248   8075  10328     49   -160   -222       C
ATOM   4867  CD2 PHE B 259     -76.818  53.398  35.796  1.00 76.77           C
ANISOU 4867  CD2 PHE B 259     9673   8628  10869     90    144   -351       C
ATOM   4868  CE1 PHE B 259     -78.385  53.468  33.526  1.00 74.98           C
ANISOU 4868  CE1 PHE B 259     9429   8250  10808    130   -197   -236       C
ATOM   4869  CE2 PHE B 259     -76.970  52.260  35.028  1.00 81.26           C
ANISOU 4869  CE2 PHE B 259    10106   9096  11674    182    112   -378       C
ATOM   4870  CZ  PHE B 259     -77.754  52.296  33.891  1.00 80.58           C
ANISOU 4870  CZ  PHE B 259    10020   8930  11665    205    -76   -312       C
ATOM   4871  N   LYS B 260     -77.662  55.059  39.365  1.00 58.05           N
ANISOU 4871  N   LYS B 260     7809   6397   7852   -126    312   -487       N
ATOM   4872  CA  LYS B 260     -77.666  54.043  40.412  1.00 65.76           C
ANISOU 4872  CA  LYS B 260     8846   7343   8796   -121    531   -644       C
ATOM   4873  C   LYS B 260     -79.016  53.964  41.111  1.00 71.19           C
ANISOU 4873  C   LYS B 260     9706   7966   9377   -147    513   -768       C
ATOM   4874  O   LYS B 260     -79.375  52.911  41.653  1.00 73.72           O
ANISOU 4874  O   LYS B 260    10051   8211   9748   -108    680   -930       O
ATOM   4875  CB  LYS B 260     -76.557  54.326  41.425  1.00 67.07           C
ANISOU 4875  CB  LYS B 260     9103   7608   8774   -206    681   -625       C
ATOM   4876  CG  LYS B 260     -75.191  53.829  40.989  1.00 70.63           C
ANISOU 4876  CG  LYS B 260     9374   8090   9374   -178    801   -576       C
ATOM   4877  CD  LYS B 260     -75.150  52.309  40.966  1.00 72.83           C
ANISOU 4877  CD  LYS B 260     9500   8296   9876    -92    997   -722       C
ATOM   4878  CE  LYS B 260     -73.954  51.798  40.182  1.00 71.36           C
ANISOU 4878  CE  LYS B 260     9075   8125   9914    -52   1042   -661       C
ATOM   4879  NZ  LYS B 260     -74.056  52.155  38.740  1.00 67.46           N
ANISOU 4879  NZ  LYS B 260     8458   7605   9569      5    794   -537       N
ATOM   4880  N   GLU B 261     -79.777  55.058  41.103  1.00 76.27           N
ANISOU 4880  N   GLU B 261    10459   8630   9890   -214    316   -704       N
ATOM   4881  CA  GLU B 261     -81.094  55.067  41.730  1.00 79.63           C
ANISOU 4881  CA  GLU B 261    11051   8991  10214   -260    270   -817       C
ATOM   4882  C   GLU B 261     -82.152  54.492  40.792  1.00 77.87           C
ANISOU 4882  C   GLU B 261    10745   8634  10208   -185    188   -856       C
ATOM   4883  O   GLU B 261     -82.752  53.450  41.076  1.00 84.38           O
ANISOU 4883  O   GLU B 261    11602   9343  11117   -133    296  -1007       O
ATOM   4884  CB  GLU B 261     -81.457  56.493  42.147  1.00 86.35           C
ANISOU 4884  CB  GLU B 261    12035   9919  10855   -374     77   -730       C
ATOM   4885  CG  GLU B 261     -80.332  57.221  42.867  1.00 95.13           C
ANISOU 4885  CG  GLU B 261    13221  11150  11774   -441    100   -639       C
ATOM   4886  CD  GLU B 261     -80.592  58.707  43.004  1.00100.82           C
ANISOU 4886  CD  GLU B 261    14005  11935  12366   -522   -140   -517       C
ATOM   4887  OE1 GLU B 261     -79.971  59.340  43.883  1.00103.67           O
ANISOU 4887  OE1 GLU B 261    14498  12369  12524   -596   -161   -458       O
ATOM   4888  OE2 GLU B 261     -81.418  59.241  42.233  1.00101.27           O
ANISOU 4888  OE2 GLU B 261    13978  11964  12537   -514   -308   -478       O
ATOM   4889  N   SER B 262     -82.392  55.163  39.669  1.00 65.71           N
ANISOU 4889  N   SER B 262     9109   7098   8760   -182      4   -723       N
ATOM   4890  CA  SER B 262     -83.351  54.718  38.673  1.00 62.05           C
ANISOU 4890  CA  SER B 262     8588   6507   8483   -132    -92   -725       C
ATOM   4891  C   SER B 262     -82.729  54.814  37.286  1.00 56.57           C
ANISOU 4891  C   SER B 262     7722   5829   7944    -80   -169   -580       C
ATOM   4892  O   SER B 262     -82.092  55.823  36.956  1.00 54.35           O
ANISOU 4892  O   SER B 262     7399   5657   7593   -126   -234   -461       O
ATOM   4893  CB  SER B 262     -84.637  55.556  38.726  1.00 63.97           C
ANISOU 4893  CB  SER B 262     8945   6721   8640   -230   -253   -722       C
ATOM   4894  OG  SER B 262     -84.358  56.927  38.502  1.00 65.16           O
ANISOU 4894  OG  SER B 262     9069   6993   8697   -307   -378   -591       O
ATOM   4895  N   PRO B 263     -82.898  53.790  36.456  1.00 57.44           N
ANISOU 4895  N   PRO B 263     7739   5822   8263     13   -174   -589       N
ATOM   4896  CA  PRO B 263     -82.273  53.798  35.129  1.00 57.02           C
ANISOU 4896  CA  PRO B 263     7548   5780   8336     50   -259   -456       C
ATOM   4897  C   PRO B 263     -82.965  54.771  34.185  1.00 52.99           C
ANISOU 4897  C   PRO B 263     7074   5271   7789    -28   -424   -345       C
ATOM   4898  O   PRO B 263     -84.051  55.290  34.452  1.00 53.62           O
ANISOU 4898  O   PRO B 263     7258   5320   7795   -101   -483   -372       O
ATOM   4899  CB  PRO B 263     -82.435  52.352  34.655  1.00 61.24           C
ANISOU 4899  CB  PRO B 263     7998   6166   9105    169   -244   -507       C
ATOM   4900  CG  PRO B 263     -83.659  51.874  35.364  1.00 63.17           C
ANISOU 4900  CG  PRO B 263     8364   6284   9354    178   -212   -642       C
ATOM   4901  CD  PRO B 263     -83.654  52.552  36.707  1.00 61.80           C
ANISOU 4901  CD  PRO B 263     8316   6213   8952     92   -110   -725       C
ATOM   4902  N   PHE B 264     -82.305  55.008  33.055  1.00 49.51           N
ANISOU 4902  N   PHE B 264     6543   4866   7402    -24   -488   -227       N
ATOM   4903  CA  PHE B 264     -82.830  55.872  32.006  1.00 44.98           C
ANISOU 4903  CA  PHE B 264     5994   4294   6801   -102   -608   -124       C
ATOM   4904  C   PHE B 264     -82.162  55.487  30.694  1.00 41.89           C
ANISOU 4904  C   PHE B 264     5527   3883   6506    -70   -667    -28       C
ATOM   4905  O   PHE B 264     -81.228  54.683  30.663  1.00 43.30           O
ANISOU 4905  O   PHE B 264     5614   4062   6777      8   -629    -35       O
ATOM   4906  CB  PHE B 264     -82.610  57.352  32.333  1.00 43.86           C
ANISOU 4906  CB  PHE B 264     5863   4287   6516   -190   -611    -85       C
ATOM   4907  CG  PHE B 264     -81.232  57.663  32.835  1.00 48.90           C
ANISOU 4907  CG  PHE B 264     6440   5039   7100   -164   -534    -68       C
ATOM   4908  CD1 PHE B 264     -80.188  57.878  31.950  1.00 49.74           C
ANISOU 4908  CD1 PHE B 264     6464   5192   7243   -152   -539     16       C
ATOM   4909  CD2 PHE B 264     -80.979  57.744  34.195  1.00 53.89           C
ANISOU 4909  CD2 PHE B 264     7122   5724   7631   -166   -458   -135       C
ATOM   4910  CE1 PHE B 264     -78.919  58.165  32.412  1.00 53.13           C
ANISOU 4910  CE1 PHE B 264     6848   5708   7631   -138   -469     35       C
ATOM   4911  CE2 PHE B 264     -79.712  58.031  34.663  1.00 57.25           C
ANISOU 4911  CE2 PHE B 264     7514   6240   7998   -158   -386   -105       C
ATOM   4912  CZ  PHE B 264     -78.680  58.242  33.771  1.00 57.12           C
ANISOU 4912  CZ  PHE B 264     7402   6260   8041   -141   -392    -19       C
ATOM   4913  N   GLU B 265     -82.651  56.077  29.608  1.00 39.55           N
ANISOU 4913  N   GLU B 265     5274   3569   6184   -146   -758     59       N
ATOM   4914  CA  GLU B 265     -82.229  55.716  28.262  1.00 42.46           C
ANISOU 4914  CA  GLU B 265     5623   3900   6610   -143   -839    154       C
ATOM   4915  C   GLU B 265     -81.364  56.823  27.677  1.00 41.38           C
ANISOU 4915  C   GLU B 265     5457   3887   6380   -209   -819    219       C
ATOM   4916  O   GLU B 265     -81.756  57.995  27.688  1.00 38.39           O
ANISOU 4916  O   GLU B 265     5108   3568   5910   -292   -795    229       O
ATOM   4917  CB  GLU B 265     -83.440  55.461  27.362  1.00 48.45           C
ANISOU 4917  CB  GLU B 265     6492   4525   7392   -196   -947    206       C
ATOM   4918  CG  GLU B 265     -83.194  54.445  26.258  1.00 57.00           C
ANISOU 4918  CG  GLU B 265     7580   5503   8574   -152  -1069    284       C
ATOM   4919  CD  GLU B 265     -83.090  53.025  26.784  1.00 68.98           C
ANISOU 4919  CD  GLU B 265     9022   6912  10275     -9  -1088    222       C
ATOM   4920  OE1 GLU B 265     -83.487  52.783  27.944  1.00 72.77           O
ANISOU 4920  OE1 GLU B 265     9488   7372  10788     42   -995    110       O
ATOM   4921  OE2 GLU B 265     -82.610  52.148  26.035  1.00 74.90           O
ANISOU 4921  OE2 GLU B 265     9724   7594  11142     51  -1198    281       O
ATOM   4922  N   LEU B 266     -80.194  56.447  27.168  1.00 46.66           N
ANISOU 4922  N   LEU B 266     6057   4582   7088   -171   -830    256       N
ATOM   4923  CA  LEU B 266     -79.280  57.363  26.496  1.00 47.17           C
ANISOU 4923  CA  LEU B 266     6105   4738   7078   -228   -812    309       C
ATOM   4924  C   LEU B 266     -79.184  56.970  25.030  1.00 47.14           C
ANISOU 4924  C   LEU B 266     6156   4674   7081   -269   -921    388       C
ATOM   4925  O   LEU B 266     -78.740  55.862  24.709  1.00 58.41           O
ANISOU 4925  O   LEU B 266     7543   6042   8608   -211  -1003    406       O
ATOM   4926  CB  LEU B 266     -77.894  57.336  27.136  1.00 55.74           C
ANISOU 4926  CB  LEU B 266     7089   5905   8184   -177   -737    286       C
ATOM   4927  CG  LEU B 266     -77.736  57.838  28.566  1.00 64.20           C
ANISOU 4927  CG  LEU B 266     8137   7048   9208   -156   -633    228       C
ATOM   4928  CD1 LEU B 266     -76.287  57.690  28.989  1.00 70.47           C
ANISOU 4928  CD1 LEU B 266     8851   7902  10024   -125   -562    226       C
ATOM   4929  CD2 LEU B 266     -78.180  59.282  28.676  1.00 63.61           C
ANISOU 4929  CD2 LEU B 266     8104   7031   9033   -224   -621    242       C
ATOM   4930  N   GLU B 267     -79.586  57.876  24.147  1.00 39.62           N
ANISOU 4930  N   GLU B 267     5294   3735   6024   -376   -921    432       N
ATOM   4931  CA  GLU B 267     -79.494  57.671  22.707  1.00 43.19           C
ANISOU 4931  CA  GLU B 267     5846   4139   6427   -448  -1013    508       C
ATOM   4932  C   GLU B 267     -78.370  58.558  22.185  1.00 39.15           C
ANISOU 4932  C   GLU B 267     5319   3719   5836   -499   -948    510       C
ATOM   4933  O   GLU B 267     -78.500  59.787  22.158  1.00 38.64           O
ANISOU 4933  O   GLU B 267     5265   3718   5699   -560   -840    487       O
ATOM   4934  CB  GLU B 267     -80.824  57.982  22.022  1.00 53.38           C
ANISOU 4934  CB  GLU B 267     7279   5362   7641   -555  -1036    549       C
ATOM   4935  CG  GLU B 267     -81.106  57.144  20.779  1.00 65.05           C
ANISOU 4935  CG  GLU B 267     8899   6726   9091   -607  -1189    643       C
ATOM   4936  CD  GLU B 267     -80.380  57.652  19.549  1.00 76.69           C
ANISOU 4936  CD  GLU B 267    10466   8243  10429   -713  -1192    688       C
ATOM   4937  OE1 GLU B 267     -79.895  58.801  19.579  1.00 81.19           O
ANISOU 4937  OE1 GLU B 267    11000   8919  10931   -758  -1047    640       O
ATOM   4938  OE2 GLU B 267     -80.298  56.903  18.552  1.00 79.65           O
ANISOU 4938  OE2 GLU B 267    10958   8537  10768   -752  -1347    770       O
ATOM   4939  N   ASP B 268     -77.262  57.933  21.785  1.00 38.54           N
ANISOU 4939  N   ASP B 268     5208   3641   5793   -471  -1016    530       N
ATOM   4940  CA  ASP B 268     -76.084  58.647  21.293  1.00 35.01           C
ANISOU 4940  CA  ASP B 268     4757   3262   5284   -517   -964    523       C
ATOM   4941  C   ASP B 268     -76.191  58.753  19.775  1.00 31.20           C
ANISOU 4941  C   ASP B 268     4440   2739   4675   -639  -1034    575       C
ATOM   4942  O   ASP B 268     -75.619  57.966  19.019  1.00 34.03           O
ANISOU 4942  O   ASP B 268     4842   3056   5033   -658  -1172    619       O
ATOM   4943  CB  ASP B 268     -74.814  57.927  21.733  1.00 41.33           C
ANISOU 4943  CB  ASP B 268     5433   4081   6190   -443   -995    509       C
ATOM   4944  CG  ASP B 268     -73.552  58.683  21.369  1.00 47.00           C
ANISOU 4944  CG  ASP B 268     6147   4855   6857   -490   -935    493       C
ATOM   4945  OD1 ASP B 268     -73.648  59.859  20.957  1.00 50.75           O
ANISOU 4945  OD1 ASP B 268     6695   5360   7229   -557   -844    476       O
ATOM   4946  OD2 ASP B 268     -72.459  58.094  21.497  1.00 47.97           O
ANISOU 4946  OD2 ASP B 268     6184   4983   7059   -462   -973    490       O
ATOM   4947  N   PHE B 269     -76.944  59.760  19.322  1.00 30.99           N
ANISOU 4947  N   PHE B 269     4512   2727   4537   -734   -935    568       N
ATOM   4948  CA  PHE B 269     -77.228  59.883  17.896  1.00 33.90           C
ANISOU 4948  CA  PHE B 269     5075   3054   4752   -874   -972    614       C
ATOM   4949  C   PHE B 269     -76.024  60.344  17.085  1.00 37.39           C
ANISOU 4949  C   PHE B 269     5573   3532   5102   -939   -941    589       C
ATOM   4950  O   PHE B 269     -76.107  60.368  15.852  1.00 40.56           O
ANISOU 4950  O   PHE B 269     6164   3899   5347  -1069   -978    622       O
ATOM   4951  CB  PHE B 269     -78.420  60.821  17.658  1.00 37.11           C
ANISOU 4951  CB  PHE B 269     5560   3464   5075   -974   -841    603       C
ATOM   4952  CG  PHE B 269     -78.338  62.137  18.388  1.00 40.85           C
ANISOU 4952  CG  PHE B 269     5899   4026   5596   -948   -652    518       C
ATOM   4953  CD1 PHE B 269     -77.879  63.274  17.744  1.00 41.91           C
ANISOU 4953  CD1 PHE B 269     6062   4206   5655  -1025   -502    466       C
ATOM   4954  CD2 PHE B 269     -78.753  62.244  19.707  1.00 42.37           C
ANISOU 4954  CD2 PHE B 269     5944   4245   5910   -850   -632    489       C
ATOM   4955  CE1 PHE B 269     -77.814  64.488  18.406  1.00 42.06           C
ANISOU 4955  CE1 PHE B 269     5937   4289   5753   -986   -349    394       C
ATOM   4956  CE2 PHE B 269     -78.689  63.455  20.376  1.00 42.58           C
ANISOU 4956  CE2 PHE B 269     5850   4344   5986   -827   -499    427       C
ATOM   4957  CZ  PHE B 269     -78.220  64.578  19.723  1.00 40.79           C
ANISOU 4957  CZ  PHE B 269     5626   4155   5717   -887   -365    383       C
ATOM   4958  N   ILE B 270     -74.921  60.705  17.732  1.00 38.04           N
ANISOU 4958  N   ILE B 270     5517   3672   5263   -865   -874    532       N
ATOM   4959  CA  ILE B 270     -73.663  60.960  17.034  1.00 36.06           C
ANISOU 4959  CA  ILE B 270     5316   3436   4951   -918   -870    504       C
ATOM   4960  C   ILE B 270     -72.590  60.097  17.686  1.00 33.32           C
ANISOU 4960  C   ILE B 270     4826   3093   4743   -823   -971    511       C
ATOM   4961  O   ILE B 270     -71.772  60.610  18.463  1.00 31.65           O
ANISOU 4961  O   ILE B 270     4494   2924   4606   -763   -871    462       O
ATOM   4962  CB  ILE B 270     -73.280  62.448  17.069  1.00 41.04           C
ANISOU 4962  CB  ILE B 270     5927   4115   5550   -941   -659    419       C
ATOM   4963  CG1 ILE B 270     -74.484  63.326  16.728  1.00 44.55           C
ANISOU 4963  CG1 ILE B 270     6440   4567   5920  -1015   -524    400       C
ATOM   4964  CG2 ILE B 270     -72.151  62.725  16.089  1.00 37.58           C
ANISOU 4964  CG2 ILE B 270     5599   3664   5014  -1027   -648    380       C
ATOM   4965  CD1 ILE B 270     -74.189  64.811  16.761  1.00 47.41           C
ANISOU 4965  CD1 ILE B 270     6749   4968   6298  -1022   -312    308       C
ATOM   4966  N   PRO B 271     -72.559  58.787  17.413  1.00 37.30           N
ANISOU 4966  N   PRO B 271     5331   3544   5298   -808  -1169    572       N
ATOM   4967  CA  PRO B 271     -71.605  57.910  18.108  1.00 35.60           C
ANISOU 4967  CA  PRO B 271     4941   3335   5252   -718  -1243    569       C
ATOM   4968  C   PRO B 271     -70.164  58.170  17.702  1.00 37.22           C
ANISOU 4968  C   PRO B 271     5143   3560   5439   -775  -1242    536       C
ATOM   4969  O   PRO B 271     -69.667  57.604  16.723  1.00 41.12           O
ANISOU 4969  O   PRO B 271     5717   4016   5890   -853  -1405    566       O
ATOM   4970  CB  PRO B 271     -72.063  56.505  17.700  1.00 34.35           C
ANISOU 4970  CB  PRO B 271     4787   3097   5166   -696  -1469    643       C
ATOM   4971  CG  PRO B 271     -72.734  56.700  16.387  1.00 35.19           C
ANISOU 4971  CG  PRO B 271     5135   3156   5082   -825  -1556    698       C
ATOM   4972  CD  PRO B 271     -73.399  58.047  16.457  1.00 35.15           C
ANISOU 4972  CD  PRO B 271     5215   3196   4946   -876  -1337    652       C
ATOM   4973  N   MET B 272     -69.485  59.027  18.459  1.00 36.36           N
ANISOU 4973  N   MET B 272     4952   3500   5364   -741  -1075    478       N
ATOM   4974  CA  MET B 272     -68.097  59.367  18.182  1.00 35.06           C
ANISOU 4974  CA  MET B 272     4787   3338   5196   -793  -1054    440       C
ATOM   4975  C   MET B 272     -67.467  59.910  19.453  1.00 31.81           C
ANISOU 4975  C   MET B 272     4237   2964   4887   -713   -903    407       C
ATOM   4976  O   MET B 272     -68.161  60.293  20.399  1.00 35.80           O
ANISOU 4976  O   MET B 272     4684   3500   5420   -635   -805    406       O
ATOM   4977  CB  MET B 272     -67.983  60.392  17.051  1.00 33.76           C
ANISOU 4977  CB  MET B 272     4816   3158   4853   -910   -991    398       C
ATOM   4978  CG  MET B 272     -68.636  61.722  17.376  1.00 39.81           C
ANISOU 4978  CG  MET B 272     5602   3951   5572   -885   -788    353       C
ATOM   4979  SD  MET B 272     -68.212  63.009  16.193  1.00 48.21           S
ANISOU 4979  SD  MET B 272     6850   4990   6479  -1006   -650    265       S
ATOM   4980  CE  MET B 272     -66.431  63.064  16.372  1.00 48.29           C
ANISOU 4980  CE  MET B 272     6809   4970   6569  -1007   -658    222       C
ATOM   4981  N   ASP B 273     -66.139  59.940  19.460  1.00 33.11           N
ANISOU 4981  N   ASP B 273     4364   3118   5098   -746   -897    385       N
ATOM   4982  CA  ASP B 273     -65.396  60.490  20.586  1.00 37.62           C
ANISOU 4982  CA  ASP B 273     4838   3706   5749   -693   -763    368       C
ATOM   4983  C   ASP B 273     -65.348  62.008  20.458  1.00 35.88           C
ANISOU 4983  C   ASP B 273     4709   3473   5450   -701   -626    326       C
ATOM   4984  O   ASP B 273     -64.874  62.536  19.446  1.00 34.83           O
ANISOU 4984  O   ASP B 273     4694   3301   5241   -782   -618    282       O
ATOM   4985  CB  ASP B 273     -63.987  59.904  20.631  1.00 41.65           C
ANISOU 4985  CB  ASP B 273     5274   4195   6355   -739   -809    365       C
ATOM   4986  CG  ASP B 273     -63.366  59.982  22.012  1.00 42.35           C
ANISOU 4986  CG  ASP B 273     5242   4302   6545   -683   -691    374       C
ATOM   4987  OD1 ASP B 273     -64.113  60.213  22.988  1.00 43.67           O
ANISOU 4987  OD1 ASP B 273     5376   4506   6712   -600   -608    389       O
ATOM   4988  OD2 ASP B 273     -62.133  59.814  22.122  1.00 40.43           O
ANISOU 4988  OD2 ASP B 273     4954   4034   6372   -737   -683    369       O
ATOM   4989  N   SER B 274     -65.847  62.709  21.473  1.00 28.14           N
ANISOU 4989  N   SER B 274     3676   2519   4496   -618   -522    332       N
ATOM   4990  CA  SER B 274     -65.816  64.163  21.474  1.00 38.55           C
ANISOU 4990  CA  SER B 274     5039   3818   5792   -602   -402    295       C
ATOM   4991  C   SER B 274     -65.803  64.660  22.911  1.00 31.75           C
ANISOU 4991  C   SER B 274     4088   2974   5001   -510   -341    327       C
ATOM   4992  O   SER B 274     -66.283  63.982  23.823  1.00 29.25           O
ANISOU 4992  O   SER B 274     3705   2702   4707   -465   -368    366       O
ATOM   4993  CB  SER B 274     -67.005  64.758  20.708  1.00 43.25           C
ANISOU 4993  CB  SER B 274     5708   4424   6302   -626   -366    265       C
ATOM   4994  OG  SER B 274     -68.238  64.326  21.251  1.00 50.57           O
ANISOU 4994  OG  SER B 274     6587   5396   7230   -582   -400    303       O
ATOM   4995  N   THR B 275     -65.239  65.857  23.100  1.00 31.31           N
ANISOU 4995  N   THR B 275     4044   2873   4978   -485   -262    310       N
ATOM   4996  CA  THR B 275     -65.134  66.432  24.438  1.00 31.57           C
ANISOU 4996  CA  THR B 275     4019   2908   5067   -405   -232    356       C
ATOM   4997  C   THR B 275     -66.511  66.647  25.058  1.00 31.73           C
ANISOU 4997  C   THR B 275     3996   2989   5071   -350   -244    373       C
ATOM   4998  O   THR B 275     -66.715  66.367  26.246  1.00 34.70           O
ANISOU 4998  O   THR B 275     4337   3399   5447   -310   -266    420       O
ATOM   4999  CB  THR B 275     -64.352  67.747  24.380  1.00 34.88           C
ANISOU 4999  CB  THR B 275     4463   3243   5548   -378   -169    337       C
ATOM   5000  OG1 THR B 275     -63.005  67.484  23.966  1.00 35.36           O
ANISOU 5000  OG1 THR B 275     4572   3235   5626   -439   -163    323       O
ATOM   5001  CG2 THR B 275     -64.332  68.430  25.740  1.00 33.10           C
ANISOU 5001  CG2 THR B 275     4194   3007   5374   -296   -174    404       C
ATOM   5002  N   VAL B 276     -67.467  67.135  24.273  1.00 32.64           N
ANISOU 5002  N   VAL B 276     4123   3115   5162   -364   -222    329       N
ATOM   5003  CA  VAL B 276     -68.851  67.294  24.706  1.00 33.39           C
ANISOU 5003  CA  VAL B 276     4176   3262   5247   -336   -238    336       C
ATOM   5004  C   VAL B 276     -69.708  66.300  23.935  1.00 32.44           C
ANISOU 5004  C   VAL B 276     4101   3168   5056   -395   -278    326       C
ATOM   5005  O   VAL B 276     -69.601  66.201  22.706  1.00 31.39           O
ANISOU 5005  O   VAL B 276     4041   3011   4873   -465   -264    294       O
ATOM   5006  CB  VAL B 276     -69.352  68.733  24.496  1.00 34.09           C
ANISOU 5006  CB  VAL B 276     4223   3336   5396   -310   -174    299       C
ATOM   5007  CG1 VAL B 276     -70.825  68.843  24.866  1.00 37.71           C
ANISOU 5007  CG1 VAL B 276     4631   3848   5850   -306   -200    303       C
ATOM   5008  CG2 VAL B 276     -68.524  69.707  25.317  1.00 32.26           C
ANISOU 5008  CG2 VAL B 276     3944   3056   5257   -234   -170    325       C
ATOM   5009  N   LYS B 277     -70.552  65.566  24.654  1.00 32.95           N
ANISOU 5009  N   LYS B 277     4140   3270   5110   -372   -333    353       N
ATOM   5010  CA  LYS B 277     -71.429  64.565  24.065  1.00 35.97           C
ANISOU 5010  CA  LYS B 277     4565   3655   5448   -413   -390    356       C
ATOM   5011  C   LYS B 277     -72.879  65.023  24.147  1.00 36.75           C
ANISOU 5011  C   LYS B 277     4661   3771   5532   -424   -381    346       C
ATOM   5012  O   LYS B 277     -73.315  65.562  25.170  1.00 40.02           O
ANISOU 5012  O   LYS B 277     5016   4211   5978   -379   -376    348       O
ATOM   5013  CB  LYS B 277     -71.270  63.214  24.768  1.00 34.03           C
ANISOU 5013  CB  LYS B 277     4286   3414   5228   -377   -453    380       C
ATOM   5014  CG  LYS B 277     -69.931  62.541  24.529  1.00 30.74           C
ANISOU 5014  CG  LYS B 277     3855   2979   4845   -389   -472    388       C
ATOM   5015  CD  LYS B 277     -69.758  62.165  23.068  1.00 30.68           C
ANISOU 5015  CD  LYS B 277     3920   2938   4801   -463   -536    384       C
ATOM   5016  CE  LYS B 277     -70.846  61.209  22.604  1.00 29.86           C
ANISOU 5016  CE  LYS B 277     3848   2815   4682   -474   -632    404       C
ATOM   5017  NZ  LYS B 277     -70.674  60.833  21.172  1.00 29.75           N
ANISOU 5017  NZ  LYS B 277     3936   2762   4606   -560   -724    418       N
ATOM   5018  N   ASN B 278     -73.621  64.805  23.066  1.00 34.31           N
ANISOU 5018  N   ASN B 278     4427   3442   5168   -498   -390    340       N
ATOM   5019  CA  ASN B 278     -75.039  65.128  22.994  1.00 38.77           C
ANISOU 5019  CA  ASN B 278     5000   4011   5718   -536   -376    334       C
ATOM   5020  C   ASN B 278     -75.846  63.839  23.014  1.00 42.11           C
ANISOU 5020  C   ASN B 278     5477   4403   6120   -544   -475    366       C
ATOM   5021  O   ASN B 278     -75.573  62.919  22.234  1.00 42.94           O
ANISOU 5021  O   ASN B 278     5657   4468   6191   -572   -544    394       O
ATOM   5022  CB  ASN B 278     -75.355  65.935  21.733  1.00 46.61           C
ANISOU 5022  CB  ASN B 278     6057   4993   6659   -634   -284    304       C
ATOM   5023  CG  ASN B 278     -74.755  67.326  21.765  1.00 54.77           C
ANISOU 5023  CG  ASN B 278     7012   6042   7755   -611   -168    253       C
ATOM   5024  OD1 ASN B 278     -74.786  68.004  22.793  1.00 57.75           O
ANISOU 5024  OD1 ASN B 278     7273   6443   8226   -537   -166    250       O
ATOM   5025  ND2 ASN B 278     -74.202  67.757  20.639  1.00 58.46           N
ANISOU 5025  ND2 ASN B 278     7554   6486   8173   -674    -78    210       N
ATOM   5026  N   TYR B 279     -76.838  63.775  23.901  1.00 43.55           N
ANISOU 5026  N   TYR B 279     5624   4591   6332   -519   -496    362       N
ATOM   5027  CA  TYR B 279     -77.648  62.580  24.077  1.00 39.72           C
ANISOU 5027  CA  TYR B 279     5184   4054   5852   -509   -582    379       C
ATOM   5028  C   TYR B 279     -79.128  62.925  24.038  1.00 36.52           C
ANISOU 5028  C   TYR B 279     4813   3627   5435   -574   -578    373       C
ATOM   5029  O   TYR B 279     -79.543  63.992  24.502  1.00 32.46           O
ANISOU 5029  O   TYR B 279     4237   3157   4940   -592   -524    345       O
ATOM   5030  CB  TYR B 279     -77.338  61.875  25.406  1.00 37.78           C
ANISOU 5030  CB  TYR B 279     4876   3820   5660   -412   -607    361       C
ATOM   5031  CG  TYR B 279     -75.923  61.365  25.538  1.00 39.40           C
ANISOU 5031  CG  TYR B 279     5035   4040   5894   -360   -603    368       C
ATOM   5032  CD1 TYR B 279     -75.478  60.289  24.784  1.00 41.65           C
ANISOU 5032  CD1 TYR B 279     5337   4279   6208   -359   -671    392       C
ATOM   5033  CD2 TYR B 279     -75.037  61.949  26.433  1.00 39.64           C
ANISOU 5033  CD2 TYR B 279     5007   4124   5931   -322   -544    357       C
ATOM   5034  CE1 TYR B 279     -74.183  59.817  24.908  1.00 43.58           C
ANISOU 5034  CE1 TYR B 279     5520   4538   6500   -326   -669    393       C
ATOM   5035  CE2 TYR B 279     -73.744  61.484  26.566  1.00 38.17           C
ANISOU 5035  CE2 TYR B 279     4782   3945   5775   -294   -528    366       C
ATOM   5036  CZ  TYR B 279     -73.321  60.418  25.801  1.00 40.18           C
ANISOU 5036  CZ  TYR B 279     5034   4161   6072   -299   -585    378       C
ATOM   5037  OH  TYR B 279     -72.033  59.953  25.929  1.00 46.50           O
ANISOU 5037  OH  TYR B 279     5777   4970   6923   -286   -570    382       O
ATOM   5038  N   PHE B 280     -79.915  62.009  23.480  1.00 38.40           N
ANISOU 5038  N   PHE B 280     5148   3787   5657   -611   -650    404       N
ATOM   5039  CA  PHE B 280     -81.367  62.022  23.614  1.00 35.36           C
ANISOU 5039  CA  PHE B 280     4807   3353   5274   -669   -666    401       C
ATOM   5040  C   PHE B 280     -81.699  61.201  24.855  1.00 36.15           C
ANISOU 5040  C   PHE B 280     4876   3422   5437   -579   -722    368       C
ATOM   5041  O   PHE B 280     -81.556  59.974  24.852  1.00 37.25           O
ANISOU 5041  O   PHE B 280     5044   3492   5617   -516   -794    380       O
ATOM   5042  CB  PHE B 280     -82.025  61.453  22.358  1.00 37.29           C
ANISOU 5042  CB  PHE B 280     5201   3505   5462   -763   -718    462       C
ATOM   5043  CG  PHE B 280     -83.489  61.798  22.208  1.00 41.47           C
ANISOU 5043  CG  PHE B 280     5794   3986   5977   -872   -699    467       C
ATOM   5044  CD1 PHE B 280     -84.302  61.996  23.314  1.00 43.15           C
ANISOU 5044  CD1 PHE B 280     5941   4200   6253   -854   -699    418       C
ATOM   5045  CD2 PHE B 280     -84.051  61.915  20.947  1.00 42.54           C
ANISOU 5045  CD2 PHE B 280     6069   4070   6023  -1011   -680    522       C
ATOM   5046  CE1 PHE B 280     -85.643  62.305  23.164  1.00 40.54           C
ANISOU 5046  CE1 PHE B 280     5664   3817   5922   -970   -686    420       C
ATOM   5047  CE2 PHE B 280     -85.391  62.225  20.791  1.00 39.10           C
ANISOU 5047  CE2 PHE B 280     5694   3583   5578  -1132   -649    531       C
ATOM   5048  CZ  PHE B 280     -86.188  62.420  21.901  1.00 39.53           C
ANISOU 5048  CZ  PHE B 280     5661   3636   5721  -1110   -654    479       C
ATOM   5049  N   ILE B 281     -82.131  61.875  25.917  1.00 40.02           N
ANISOU 5049  N   ILE B 281     5306   3959   5941   -573   -693    319       N
ATOM   5050  CA  ILE B 281     -82.310  61.260  27.226  1.00 40.89           C
ANISOU 5050  CA  ILE B 281     5402   4056   6078   -498   -720    268       C
ATOM   5051  C   ILE B 281     -83.796  61.102  27.512  1.00 37.37           C
ANISOU 5051  C   ILE B 281     5020   3536   5644   -556   -761    238       C
ATOM   5052  O   ILE B 281     -84.594  62.002  27.226  1.00 37.28           O
ANISOU 5052  O   ILE B 281     5006   3536   5622   -656   -750    244       O
ATOM   5053  CB  ILE B 281     -81.622  62.090  28.327  1.00 45.23           C
ANISOU 5053  CB  ILE B 281     5872   4707   6608   -458   -683    238       C
ATOM   5054  CG1 ILE B 281     -80.126  62.207  28.039  1.00 54.68           C
ANISOU 5054  CG1 ILE B 281     7018   5956   7803   -408   -641    269       C
ATOM   5055  CG2 ILE B 281     -81.851  61.470  29.696  1.00 45.07           C
ANISOU 5055  CG2 ILE B 281     5876   4675   6575   -406   -696    177       C
ATOM   5056  CD1 ILE B 281     -79.334  62.838  29.161  1.00 61.07           C
ANISOU 5056  CD1 ILE B 281     7775   6839   8590   -363   -616    258       C
ATOM   5057  N   THR B 282     -84.165  59.950  28.074  1.00 34.99           N
ANISOU 5057  N   THR B 282     4769   3149   5379   -495   -798    199       N
ATOM   5058  CA  THR B 282     -85.529  59.675  28.514  1.00 36.32           C
ANISOU 5058  CA  THR B 282     5012   3224   5564   -540   -838    153       C
ATOM   5059  C   THR B 282     -85.458  59.052  29.902  1.00 38.29           C
ANISOU 5059  C   THR B 282     5267   3465   5817   -457   -821     58       C
ATOM   5060  O   THR B 282     -84.971  57.927  30.054  1.00 39.63           O
ANISOU 5060  O   THR B 282     5434   3581   6042   -356   -806     33       O
ATOM   5061  CB  THR B 282     -86.256  58.744  27.541  1.00 36.39           C
ANISOU 5061  CB  THR B 282     5120   3082   5623   -560   -900    200       C
ATOM   5062  OG1 THR B 282     -86.303  59.346  26.242  1.00 39.60           O
ANISOU 5062  OG1 THR B 282     5555   3502   5988   -661   -899    287       O
ATOM   5063  CG2 THR B 282     -87.675  58.478  28.021  1.00 32.87           C
ANISOU 5063  CG2 THR B 282     4764   2521   5206   -612   -939    148       C
ATOM   5064  N   ASP B 283     -85.937  59.778  30.910  1.00 37.95           N
ANISOU 5064  N   ASP B 283     5231   3472   5716   -506   -824      1       N
ATOM   5065  CA  ASP B 283     -85.951  59.262  32.272  1.00 35.60           C
ANISOU 5065  CA  ASP B 283     4980   3168   5380   -456   -799    -99       C
ATOM   5066  C   ASP B 283     -87.102  58.278  32.439  1.00 39.71           C
ANISOU 5066  C   ASP B 283     5604   3528   5954   -456   -822   -173       C
ATOM   5067  O   ASP B 283     -88.260  58.611  32.169  1.00 43.63           O
ANISOU 5067  O   ASP B 283     6156   3960   6464   -554   -884   -172       O
ATOM   5068  CB  ASP B 283     -86.074  60.403  33.280  1.00 38.66           C
ANISOU 5068  CB  ASP B 283     5364   3657   5667   -522   -828   -126       C
ATOM   5069  CG  ASP B 283     -86.068  59.912  34.714  1.00 45.73           C
ANISOU 5069  CG  ASP B 283     6350   4550   6476   -494   -799   -232       C
ATOM   5070  OD1 ASP B 283     -85.032  59.369  35.155  1.00 46.65           O
ANISOU 5070  OD1 ASP B 283     6459   4703   6564   -413   -713   -248       O
ATOM   5071  OD2 ASP B 283     -87.099  60.067  35.402  1.00 48.85           O
ANISOU 5071  OD2 ASP B 283     6832   4905   6824   -568   -855   -304       O
ATOM   5072  N   ALA B 284     -86.779  57.066  32.891  1.00 43.73           N
ANISOU 5072  N   ALA B 284     6134   3968   6513   -348   -765   -244       N
ATOM   5073  CA  ALA B 284     -87.772  55.999  32.943  1.00 43.73           C
ANISOU 5073  CA  ALA B 284     6222   3787   6606   -318   -781   -317       C
ATOM   5074  C   ALA B 284     -88.746  56.161  34.103  1.00 48.79           C
ANISOU 5074  C   ALA B 284     6978   4388   7170   -383   -779   -442       C
ATOM   5075  O   ALA B 284     -89.892  55.707  34.008  1.00 53.21           O
ANISOU 5075  O   ALA B 284     7633   4791   7792   -414   -824   -488       O
ATOM   5076  CB  ALA B 284     -87.075  54.641  33.036  1.00 44.42           C
ANISOU 5076  CB  ALA B 284     6260   3803   6812   -167   -708   -365       C
ATOM   5077  N   GLN B 285     -88.322  56.797  35.196  1.00 47.31           N
ANISOU 5077  N   GLN B 285     6804   4330   6841   -415   -741   -494       N
ATOM   5078  CA  GLN B 285     -89.183  56.878  36.370  1.00 49.72           C
ANISOU 5078  CA  GLN B 285     7245   4599   7047   -485   -751   -623       C
ATOM   5079  C   GLN B 285     -90.248  57.957  36.221  1.00 46.81           C
ANISOU 5079  C   GLN B 285     6903   4237   6644   -638   -883   -590       C
ATOM   5080  O   GLN B 285     -91.414  57.733  36.566  1.00 48.09           O
ANISOU 5080  O   GLN B 285     7180   4281   6813   -708   -928   -678       O
ATOM   5081  CB  GLN B 285     -88.343  57.133  37.622  1.00 53.54           C
ANISOU 5081  CB  GLN B 285     7764   5211   7367   -479   -678   -682       C
ATOM   5082  CG  GLN B 285     -89.115  56.991  38.926  1.00 61.21           C
ANISOU 5082  CG  GLN B 285     8915   6136   8206   -548   -670   -838       C
ATOM   5083  CD  GLN B 285     -89.524  55.556  39.211  1.00 72.03           C
ANISOU 5083  CD  GLN B 285    10369   7337   9664   -464   -547   -989       C
ATOM   5084  OE1 GLN B 285     -90.490  55.045  38.641  1.00 71.90           O
ANISOU 5084  OE1 GLN B 285    10378   7157   9785   -457   -592  -1014       O
ATOM   5085  NE2 GLN B 285     -88.786  54.898  40.097  1.00 78.94           N
ANISOU 5085  NE2 GLN B 285    11287   8238  10468   -400   -382  -1092       N
ATOM   5086  N   THR B 286     -89.872  59.127  35.708  1.00 47.74           N
ANISOU 5086  N   THR B 286     6908   4485   6744   -693   -941   -474       N
ATOM   5087  CA  THR B 286     -90.774  60.270  35.654  1.00 49.31           C
ANISOU 5087  CA  THR B 286     7089   4715   6932   -840  -1054   -448       C
ATOM   5088  C   THR B 286     -91.338  60.541  34.269  1.00 44.77           C
ANISOU 5088  C   THR B 286     6448   4087   6476   -902  -1077   -353       C
ATOM   5089  O   THR B 286     -92.417  61.132  34.160  1.00 48.00           O
ANISOU 5089  O   THR B 286     6864   4460   6912  -1038  -1148   -360       O
ATOM   5090  CB  THR B 286     -90.057  61.532  36.144  1.00 37.05           C
ANISOU 5090  CB  THR B 286     5443   3338   5295   -867  -1105   -396       C
ATOM   5091  OG1 THR B 286     -89.024  61.884  35.214  1.00 35.47           O
ANISOU 5091  OG1 THR B 286     5109   3218   5151   -801  -1053   -283       O
ATOM   5092  CG2 THR B 286     -89.438  61.291  37.508  1.00 37.65           C
ANISOU 5092  CG2 THR B 286     5619   3469   5219   -826  -1083   -471       C
ATOM   5093  N   GLY B 287     -90.644  60.134  33.213  1.00 40.65           N
ANISOU 5093  N   GLY B 287     5871   3558   6015   -823  -1018   -267       N
ATOM   5094  CA  GLY B 287     -91.055  60.461  31.866  1.00 36.96           C
ANISOU 5094  CA  GLY B 287     5368   3055   5619   -899  -1026   -168       C
ATOM   5095  C   GLY B 287     -90.514  61.768  31.335  1.00 38.53           C
ANISOU 5095  C   GLY B 287     5426   3404   5811   -949  -1010    -89       C
ATOM   5096  O   GLY B 287     -90.921  62.190  30.246  1.00 36.98           O
ANISOU 5096  O   GLY B 287     5203   3189   5658  -1040   -992    -21       O
ATOM   5097  N   SER B 288     -89.622  62.427  32.069  1.00 38.91           N
ANISOU 5097  N   SER B 288     5390   3588   5807   -898  -1009    -98       N
ATOM   5098  CA  SER B 288     -89.000  63.654  31.595  1.00 37.40           C
ANISOU 5098  CA  SER B 288     5052   3521   5635   -919   -990    -30       C
ATOM   5099  C   SER B 288     -87.931  63.324  30.561  1.00 36.16           C
ANISOU 5099  C   SER B 288     4871   3382   5489   -839   -907     41       C
ATOM   5100  O   SER B 288     -87.215  62.326  30.687  1.00 39.34           O
ANISOU 5100  O   SER B 288     5324   3756   5868   -734   -882     36       O
ATOM   5101  CB  SER B 288     -88.388  64.425  32.764  1.00 34.90           C
ANISOU 5101  CB  SER B 288     4675   3318   5265   -884  -1043    -52       C
ATOM   5102  OG  SER B 288     -88.068  65.751  32.389  1.00 40.20           O
ANISOU 5102  OG  SER B 288     5190   4084   5999   -914  -1049      1       O
ATOM   5103  N   SER B 289     -87.825  64.163  29.533  1.00 33.02           N
ANISOU 5103  N   SER B 289     4390   3027   5130   -899   -859     99       N
ATOM   5104  CA  SER B 289     -86.919  63.881  28.430  1.00 32.69           C
ANISOU 5104  CA  SER B 289     4352   2989   5079   -853   -789    161       C
ATOM   5105  C   SER B 289     -86.434  65.185  27.814  1.00 34.05           C
ANISOU 5105  C   SER B 289     4400   3256   5282   -891   -719    189       C
ATOM   5106  O   SER B 289     -86.929  66.270  28.126  1.00 40.66           O
ANISOU 5106  O   SER B 289     5130   4143   6175   -955   -726    166       O
ATOM   5107  CB  SER B 289     -87.592  63.004  27.369  1.00 35.98           C
ANISOU 5107  CB  SER B 289     4892   3283   5495   -910   -788    200       C
ATOM   5108  OG  SER B 289     -88.644  63.700  26.725  1.00 40.56           O
ANISOU 5108  OG  SER B 289     5474   3839   6097  -1063   -759    216       O
ATOM   5109  N   LYS B 290     -85.448  65.059  26.927  1.00 31.02           N
ANISOU 5109  N   LYS B 290     4024   2888   4873   -851   -655    230       N
ATOM   5110  CA  LYS B 290     -84.903  66.193  26.192  1.00 33.32           C
ANISOU 5110  CA  LYS B 290     4219   3248   5192   -881   -561    242       C
ATOM   5111  C   LYS B 290     -84.111  65.658  25.008  1.00 29.99           C
ANISOU 5111  C   LYS B 290     3884   2801   4708   -873   -506    284       C
ATOM   5112  O   LYS B 290     -83.312  64.731  25.166  1.00 29.65           O
ANISOU 5112  O   LYS B 290     3893   2740   4632   -782   -554    302       O
ATOM   5113  CB  LYS B 290     -84.020  67.066  27.093  1.00 35.55           C
ANISOU 5113  CB  LYS B 290     4370   3616   5519   -791   -576    224       C
ATOM   5114  CG  LYS B 290     -83.331  68.210  26.370  1.00 40.33           C
ANISOU 5114  CG  LYS B 290     4869   4272   6183   -793   -473    224       C
ATOM   5115  CD  LYS B 290     -82.830  69.261  27.349  1.00 43.08           C
ANISOU 5115  CD  LYS B 290     5073   4681   6616   -719   -521    214       C
ATOM   5116  CE  LYS B 290     -81.924  68.653  28.406  1.00 45.91           C
ANISOU 5116  CE  LYS B 290     5487   5050   6908   -610   -606    236       C
ATOM   5117  NZ  LYS B 290     -81.463  69.666  29.395  1.00 49.99           N
ANISOU 5117  NZ  LYS B 290     5898   5611   7487   -548   -680    247       N
ATOM   5118  N   CYS B 291     -84.336  66.243  23.829  1.00 33.65           N
ANISOU 5118  N   CYS B 291     4367   3264   5156   -979   -405    294       N
ATOM   5119  CA  CYS B 291     -83.748  65.704  22.606  1.00 36.60           C
ANISOU 5119  CA  CYS B 291     4868   3603   5437  -1007   -371    336       C
ATOM   5120  C   CYS B 291     -82.236  65.887  22.580  1.00 37.09           C
ANISOU 5120  C   CYS B 291     4882   3717   5493   -909   -347    327       C
ATOM   5121  O   CYS B 291     -81.495  64.960  22.233  1.00 41.84           O
ANISOU 5121  O   CYS B 291     5569   4289   6041   -866   -406    361       O
ATOM   5122  CB  CYS B 291     -84.385  66.363  21.383  1.00 40.47           C
ANISOU 5122  CB  CYS B 291     5415   4081   5882  -1169   -242    339       C
ATOM   5123  SG  CYS B 291     -86.113  65.937  21.127  1.00 49.03           S
ANISOU 5123  SG  CYS B 291     6612   5070   6945  -1320   -270    374       S
ATOM   5124  N   VAL B 292     -81.759  67.077  22.929  1.00 40.12           N
ANISOU 5124  N   VAL B 292     5126   4169   5950   -876   -271    283       N
ATOM   5125  CA  VAL B 292     -80.338  67.407  22.872  1.00 39.91           C
ANISOU 5125  CA  VAL B 292     5059   4175   5931   -794   -236    272       C
ATOM   5126  C   VAL B 292     -79.897  67.761  24.284  1.00 39.08           C
ANISOU 5126  C   VAL B 292     4830   4110   5908   -679   -301    264       C
ATOM   5127  O   VAL B 292     -80.162  68.867  24.770  1.00 41.50           O
ANISOU 5127  O   VAL B 292     5007   4450   6309   -670   -279    237       O
ATOM   5128  CB  VAL B 292     -80.046  68.554  21.899  1.00 43.48           C
ANISOU 5128  CB  VAL B 292     5476   4644   6400   -855    -77    226       C
ATOM   5129  CG1 VAL B 292     -78.548  68.830  21.844  1.00 29.53           C
ANISOU 5129  CG1 VAL B 292     3688   2886   4645   -770    -49    210       C
ATOM   5130  CG2 VAL B 292     -80.588  68.230  20.522  1.00 42.71           C
ANISOU 5130  CG2 VAL B 292     5538   4507   6183   -999     -3    236       C
ATOM   5131  N  ACYS B 293     -79.221  66.826  24.945  0.58 39.04           N
ANISOU 5131  N  ACYS B 293     4865   4098   5870   -597   -383    290       N
ATOM   5132  N  BCYS B 293     -79.219  66.833  24.951  0.42 39.01           N
ANISOU 5132  N  BCYS B 293     4861   4095   5867   -597   -383    290       N
ATOM   5133  CA ACYS B 293     -78.670  67.030  26.280  0.58 38.80           C
ANISOU 5133  CA ACYS B 293     4765   4101   5874   -504   -438    293       C
ATOM   5134  CA BCYS B 293     -78.687  67.063  26.290  0.42 38.79           C
ANISOU 5134  CA BCYS B 293     4762   4102   5876   -505   -437    293       C
ATOM   5135  C  ACYS B 293     -77.151  67.038  26.163  0.58 37.40           C
ANISOU 5135  C  ACYS B 293     4588   3928   5694   -443   -408    308       C
ATOM   5136  C  BCYS B 293     -77.166  67.037  26.206  0.42 37.39           C
ANISOU 5136  C  BCYS B 293     4585   3927   5693   -442   -411    308       C
ATOM   5137  O  ACYS B 293     -76.542  66.005  25.866  0.58 34.53           O
ANISOU 5137  O  ACYS B 293     4292   3543   5286   -431   -423    324       O
ATOM   5138  O  BCYS B 293     -76.569  65.980  25.972  0.42 34.94           O
ANISOU 5138  O  BCYS B 293     4342   3596   5338   -427   -428    325       O
ATOM   5139  CB ACYS B 293     -79.136  65.938  27.239  0.58 39.29           C
ANISOU 5139  CB ACYS B 293     4882   4150   5898   -476   -522    297       C
ATOM   5140  CB BCYS B 293     -79.208  66.022  27.277  0.42 39.44           C
ANISOU 5140  CB BCYS B 293     4895   4170   5919   -479   -523    295       C
ATOM   5141  SG ACYS B 293     -80.885  65.533  27.111  0.58 46.22           S
ANISOU 5141  SG ACYS B 293     5810   4982   6768   -562   -561    278       S
ATOM   5142  SG BCYS B 293     -78.882  66.425  29.009  0.42 37.11           S
ANISOU 5142  SG BCYS B 293     4556   3921   5623   -409   -589    295       S
ATOM   5143  N   SER B 294     -76.544  68.199  26.390  1.00 39.54           N
ANISOU 5143  N   SER B 294     4775   4215   6032   -405   -376    303       N
ATOM   5144  CA  SER B 294     -75.093  68.315  26.330  1.00 37.77           C
ANISOU 5144  CA  SER B 294     4558   3976   5817   -353   -348    317       C
ATOM   5145  C   SER B 294     -74.493  67.833  27.645  1.00 32.19           C
ANISOU 5145  C   SER B 294     3864   3283   5085   -290   -418    357       C
ATOM   5146  O   SER B 294     -74.863  68.319  28.720  1.00 30.81           O
ANISOU 5146  O   SER B 294     3654   3129   4924   -261   -480    374       O
ATOM   5147  CB  SER B 294     -74.686  69.755  26.037  1.00 44.78           C
ANISOU 5147  CB  SER B 294     5358   4851   6807   -329   -282    292       C
ATOM   5148  OG  SER B 294     -75.179  70.168  24.776  1.00 52.72           O
ANISOU 5148  OG  SER B 294     6363   5846   7822   -402   -176    240       O
ATOM   5149  N   VAL B 295     -73.578  66.870  27.560  1.00 36.67           N
ANISOU 5149  N   VAL B 295     4486   3836   5611   -280   -408    372       N
ATOM   5150  CA  VAL B 295     -72.936  66.276  28.725  1.00 35.90           C
ANISOU 5150  CA  VAL B 295     4409   3749   5480   -241   -434    403       C
ATOM   5151  C   VAL B 295     -71.428  66.369  28.546  1.00 35.39           C
ANISOU 5151  C   VAL B 295     4352   3658   5437   -228   -394    426       C
ATOM   5152  O   VAL B 295     -70.917  66.254  27.426  1.00 34.99           O
ANISOU 5152  O   VAL B 295     4312   3579   5404   -257   -360    408       O
ATOM   5153  CB  VAL B 295     -73.371  64.808  28.930  1.00 33.24           C
ANISOU 5153  CB  VAL B 295     4110   3417   5103   -249   -448    386       C
ATOM   5154  CG1 VAL B 295     -72.844  64.266  30.254  1.00 32.76           C
ANISOU 5154  CG1 VAL B 295     4071   3375   5002   -221   -437    398       C
ATOM   5155  CG2 VAL B 295     -74.887  64.685  28.870  1.00 31.39           C
ANISOU 5155  CG2 VAL B 295     3887   3184   4857   -275   -487    358       C
ATOM   5156  N   ILE B 296     -70.718  66.589  29.649  1.00 32.91           N
ANISOU 5156  N   ILE B 296     4052   3344   5110   -198   -403    469       N
ATOM   5157  CA  ILE B 296     -69.261  66.626  29.654  1.00 36.03           C
ANISOU 5157  CA  ILE B 296     4465   3700   5524   -197   -365    501       C
ATOM   5158  C   ILE B 296     -68.770  66.009  30.957  1.00 35.02           C
ANISOU 5158  C   ILE B 296     4384   3590   5333   -199   -356    542       C
ATOM   5159  O   ILE B 296     -69.369  66.214  32.019  1.00 32.43           O
ANISOU 5159  O   ILE B 296     4090   3291   4942   -188   -396    562       O
ATOM   5160  CB  ILE B 296     -68.729  68.065  29.473  1.00 37.50           C
ANISOU 5160  CB  ILE B 296     4633   3832   5783   -164   -369    521       C
ATOM   5161  CG1 ILE B 296     -67.201  68.067  29.391  1.00 35.07           C
ANISOU 5161  CG1 ILE B 296     4362   3463   5501   -173   -329    550       C
ATOM   5162  CG2 ILE B 296     -69.218  68.974  30.595  1.00 33.52           C
ANISOU 5162  CG2 ILE B 296     4119   3337   5281   -119   -447    568       C
ATOM   5163  CD1 ILE B 296     -66.614  69.406  29.008  1.00 35.65           C
ANISOU 5163  CD1 ILE B 296     4420   3453   5672   -133   -321    553       C
ATOM   5164  N   ASP B 297     -67.686  65.235  30.874  1.00 35.51           N
ANISOU 5164  N   ASP B 297     4452   3635   5404   -230   -298    549       N
ATOM   5165  CA  ASP B 297     -67.147  64.526  32.034  1.00 37.51           C
ANISOU 5165  CA  ASP B 297     4746   3907   5599   -253   -246    576       C
ATOM   5166  C   ASP B 297     -65.905  65.258  32.536  1.00 36.76           C
ANISOU 5166  C   ASP B 297     4709   3760   5500   -269   -230    651       C
ATOM   5167  O   ASP B 297     -64.767  64.854  32.302  1.00 38.20           O
ANISOU 5167  O   ASP B 297     4885   3908   5722   -313   -171    663       O
ATOM   5168  CB  ASP B 297     -66.840  63.073  31.686  1.00 36.72           C
ANISOU 5168  CB  ASP B 297     4589   3822   5542   -282   -183    531       C
ATOM   5169  CG  ASP B 297     -66.306  62.289  32.873  1.00 39.60           C
ANISOU 5169  CG  ASP B 297     4977   4209   5860   -315    -85    539       C
ATOM   5170  OD1 ASP B 297     -66.477  62.747  34.023  1.00 41.24           O
ANISOU 5170  OD1 ASP B 297     5279   4432   5958   -320    -75    574       O
ATOM   5171  OD2 ASP B 297     -65.707  61.217  32.655  1.00 43.51           O
ANISOU 5171  OD2 ASP B 297     5397   4705   6428   -344    -18    509       O
ATOM   5172  N   LEU B 298     -66.140  66.351  33.248  1.00 35.69           N
ANISOU 5172  N   LEU B 298     4630   3607   5323   -238   -299    708       N
ATOM   5173  CA  LEU B 298     -65.076  67.058  33.941  1.00 36.79           C
ANISOU 5173  CA  LEU B 298     4852   3681   5444   -250   -310    801       C
ATOM   5174  C   LEU B 298     -64.980  66.571  35.381  1.00 36.23           C
ANISOU 5174  C   LEU B 298     4897   3645   5225   -301   -279    850       C
ATOM   5175  O   LEU B 298     -65.944  66.059  35.954  1.00 40.14           O
ANISOU 5175  O   LEU B 298     5413   4210   5630   -307   -279    810       O
ATOM   5176  CB  LEU B 298     -65.319  68.569  33.923  1.00 36.68           C
ANISOU 5176  CB  LEU B 298     4834   3610   5491   -181   -426    846       C
ATOM   5177  CG  LEU B 298     -65.186  69.302  32.590  1.00 38.89           C
ANISOU 5177  CG  LEU B 298     5023   3833   5921   -135   -424    796       C
ATOM   5178  CD1 LEU B 298     -65.613  70.752  32.743  1.00 39.10           C
ANISOU 5178  CD1 LEU B 298     5010   3811   6034    -55   -530    828       C
ATOM   5179  CD2 LEU B 298     -63.760  69.217  32.071  1.00 41.40           C
ANISOU 5179  CD2 LEU B 298     5370   4065   6296   -168   -354    807       C
ATOM   5180  N   LEU B 299     -63.794  66.727  35.961  1.00 34.84           N
ANISOU 5180  N   LEU B 299     4815   3410   5014   -351   -242    934       N
ATOM   5181  CA  LEU B 299     -63.664  66.569  37.401  1.00 40.32           C
ANISOU 5181  CA  LEU B 299     5664   4122   5534   -413   -222   1003       C
ATOM   5182  C   LEU B 299     -64.539  67.607  38.089  1.00 44.14           C
ANISOU 5182  C   LEU B 299     6223   4607   5943   -366   -394   1058       C
ATOM   5183  O   LEU B 299     -64.521  68.786  37.723  1.00 48.97           O
ANISOU 5183  O   LEU B 299     6798   5151   6658   -294   -525   1108       O
ATOM   5184  CB  LEU B 299     -62.206  66.728  37.830  1.00 34.87           C
ANISOU 5184  CB  LEU B 299     5080   3347   4822   -486   -165   1104       C
ATOM   5185  CG  LEU B 299     -61.913  66.497  39.314  1.00 39.59           C
ANISOU 5185  CG  LEU B 299     5876   3957   5210   -583   -114   1186       C
ATOM   5186  CD1 LEU B 299     -62.102  65.032  39.674  1.00 38.08           C
ANISOU 5186  CD1 LEU B 299     5662   3862   4944   -658     82   1086       C
ATOM   5187  CD2 LEU B 299     -60.512  66.967  39.671  1.00 38.13           C
ANISOU 5187  CD2 LEU B 299     5817   3658   5012   -653    -98   1315       C
ATOM   5188  N   LEU B 300     -65.323  67.163  39.073  1.00 42.82           N
ANISOU 5188  N   LEU B 300     6150   4511   5607   -405   -394   1039       N
ATOM   5189  CA  LEU B 300     -66.274  68.065  39.716  1.00 43.58           C
ANISOU 5189  CA  LEU B 300     6309   4618   5632   -374   -582   1080       C
ATOM   5190  C   LEU B 300     -65.568  69.268  40.328  1.00 43.61           C
ANISOU 5190  C   LEU B 300     6430   4529   5612   -366   -734   1235       C
ATOM   5191  O   LEU B 300     -66.102  70.383  40.316  1.00 46.50           O
ANISOU 5191  O   LEU B 300     6752   4862   6054   -295   -929   1280       O
ATOM   5192  CB  LEU B 300     -67.078  67.316  40.776  1.00 45.80           C
ANISOU 5192  CB  LEU B 300     6719   4980   5704   -443   -546   1030       C
ATOM   5193  CG  LEU B 300     -68.252  68.089  41.378  1.00 45.17           C
ANISOU 5193  CG  LEU B 300     6692   4924   5548   -427   -752   1044       C
ATOM   5194  CD1 LEU B 300     -69.198  68.557  40.283  1.00 37.49           C
ANISOU 5194  CD1 LEU B 300     5509   3961   4776   -336   -838    975       C
ATOM   5195  CD2 LEU B 300     -68.988  67.235  42.397  1.00 48.67           C
ANISOU 5195  CD2 LEU B 300     7287   5438   5769   -511   -691    971       C
ATOM   5196  N   ASP B 301     -64.360  69.063  40.856  1.00 41.58           N
ANISOU 5196  N   ASP B 301     6313   4217   5270   -442   -651   1323       N
ATOM   5197  CA  ASP B 301     -63.591  70.178  41.396  1.00 39.86           C
ANISOU 5197  CA  ASP B 301     6222   3881   5041   -435   -804   1488       C
ATOM   5198  C   ASP B 301     -63.247  71.185  40.307  1.00 39.67           C
ANISOU 5198  C   ASP B 301     6034   3755   5284   -315   -890   1500       C
ATOM   5199  O   ASP B 301     -63.233  72.397  40.552  1.00 42.79           O
ANISOU 5199  O   ASP B 301     6448   4059   5752   -243  -1091   1600       O
ATOM   5200  CB  ASP B 301     -62.322  69.657  42.067  1.00 44.06           C
ANISOU 5200  CB  ASP B 301     6939   4365   5435   -559   -664   1574       C
ATOM   5201  CG  ASP B 301     -62.593  68.485  42.987  1.00 52.29           C
ANISOU 5201  CG  ASP B 301     8118   5515   6235   -685   -499   1521       C
ATOM   5202  OD1 ASP B 301     -63.163  67.480  42.513  1.00 55.11           O
ANISOU 5202  OD1 ASP B 301     8338   5968   6633   -680   -351   1368       O
ATOM   5203  OD2 ASP B 301     -62.233  68.564  44.180  1.00 58.12           O
ANISOU 5203  OD2 ASP B 301     9107   6232   6742   -792   -513   1630       O
ATOM   5204  N   ASP B 302     -62.967  70.700  39.095  1.00 40.23           N
ANISOU 5204  N   ASP B 302     5945   3832   5507   -292   -743   1392       N
ATOM   5205  CA  ASP B 302     -62.678  71.602  37.985  1.00 44.42           C
ANISOU 5205  CA  ASP B 302     6334   4269   6277   -189   -789   1373       C
ATOM   5206  C   ASP B 302     -63.904  72.429  37.622  1.00 44.73           C
ANISOU 5206  C   ASP B 302     6229   4338   6427    -85   -925   1323       C
ATOM   5207  O   ASP B 302     -63.812  73.650  37.448  1.00 49.17           O
ANISOU 5207  O   ASP B 302     6732   4801   7149      9  -1055   1371       O
ATOM   5208  CB  ASP B 302     -62.186  70.809  36.773  1.00 46.80           C
ANISOU 5208  CB  ASP B 302     6524   4581   6675   -212   -609   1260       C
ATOM   5209  CG  ASP B 302     -60.784  70.264  36.962  1.00 52.98           C
ANISOU 5209  CG  ASP B 302     7410   5298   7422   -309   -492   1314       C
ATOM   5210  OD1 ASP B 302     -60.155  70.574  37.995  1.00 57.68           O
ANISOU 5210  OD1 ASP B 302     8174   5825   7916   -357   -537   1446       O
ATOM   5211  OD2 ASP B 302     -60.310  69.526  36.073  1.00 54.62           O
ANISOU 5211  OD2 ASP B 302     7534   5517   7700   -348   -363   1229       O
ATOM   5212  N   PHE B 303     -65.064  71.779  37.509  1.00 42.84           N
ANISOU 5212  N   PHE B 303     5924   4227   6126   -103   -893   1224       N
ATOM   5213  CA  PHE B 303     -66.283  72.499  37.158  1.00 43.13           C
ANISOU 5213  CA  PHE B 303     5819   4298   6270    -29  -1006   1172       C
ATOM   5214  C   PHE B 303     -66.638  73.533  38.219  1.00 44.94           C
ANISOU 5214  C   PHE B 303     6105   4492   6477      4  -1238   1283       C
ATOM   5215  O   PHE B 303     -67.117  74.626  37.895  1.00 45.22           O
ANISOU 5215  O   PHE B 303     5997   4487   6696     94  -1364   1282       O
ATOM   5216  CB  PHE B 303     -67.433  71.514  36.955  1.00 42.62           C
ANISOU 5216  CB  PHE B 303     5709   4361   6123    -73   -933   1057       C
ATOM   5217  CG  PHE B 303     -68.742  72.171  36.622  1.00 41.86           C
ANISOU 5217  CG  PHE B 303     5474   4303   6126    -26  -1034   1002       C
ATOM   5218  CD1 PHE B 303     -68.943  72.757  35.383  1.00 42.20           C
ANISOU 5218  CD1 PHE B 303     5347   4320   6369     34   -992    933       C
ATOM   5219  CD2 PHE B 303     -69.774  72.197  37.545  1.00 41.03           C
ANISOU 5219  CD2 PHE B 303     5418   4260   5912    -57  -1162   1010       C
ATOM   5220  CE1 PHE B 303     -70.148  73.362  35.073  1.00 44.78           C
ANISOU 5220  CE1 PHE B 303     5535   4683   6798     60  -1061    879       C
ATOM   5221  CE2 PHE B 303     -70.981  72.798  37.241  1.00 41.46           C
ANISOU 5221  CE2 PHE B 303     5332   4347   6074    -30  -1256    958       C
ATOM   5222  CZ  PHE B 303     -71.168  73.381  36.003  1.00 44.32           C
ANISOU 5222  CZ  PHE B 303     5506   4685   6650     27  -1198    895       C
ATOM   5223  N   VAL B 304     -66.408  73.207  39.493  1.00 44.22           N
ANISOU 5223  N   VAL B 304     6223   4414   6166    -74  -1298   1378       N
ATOM   5224  CA  VAL B 304     -66.625  74.182  40.558  1.00 44.06           C
ANISOU 5224  CA  VAL B 304     6296   4346   6098    -57  -1554   1508       C
ATOM   5225  C   VAL B 304     -65.678  75.362  40.394  1.00 46.79           C
ANISOU 5225  C   VAL B 304     6614   4530   6635     37  -1670   1622       C
ATOM   5226  O   VAL B 304     -66.078  76.524  40.537  1.00 50.00           O
ANISOU 5226  O   VAL B 304     6926   4876   7196    128  -1890   1677       O
ATOM   5227  CB  VAL B 304     -66.468  73.512  41.935  1.00 47.07           C
ANISOU 5227  CB  VAL B 304     6956   4768   6160   -186  -1568   1586       C
ATOM   5228  CG1 VAL B 304     -66.437  74.558  43.037  1.00 44.52           C
ANISOU 5228  CG1 VAL B 304     6779   4371   5767   -182  -1860   1754       C
ATOM   5229  CG2 VAL B 304     -67.597  72.526  42.172  1.00 46.77           C
ANISOU 5229  CG2 VAL B 304     6933   4872   5965   -258  -1487   1459       C
ATOM   5230  N   GLU B 305     -64.410  75.083  40.085  1.00 48.02           N
ANISOU 5230  N   GLU B 305     6841   4601   6804     18  -1529   1654       N
ATOM   5231  CA  GLU B 305     -63.454  76.156  39.834  1.00 48.21           C
ANISOU 5231  CA  GLU B 305     6843   4444   7029    111  -1616   1746       C
ATOM   5232  C   GLU B 305     -63.887  77.011  38.650  1.00 43.77           C
ANISOU 5232  C   GLU B 305     6009   3844   6778    250  -1620   1639       C
ATOM   5233  O   GLU B 305     -63.699  78.233  38.653  1.00 48.27           O
ANISOU 5233  O   GLU B 305     6501   4280   7560    367  -1782   1705       O
ATOM   5234  CB  GLU B 305     -62.063  75.566  39.599  1.00 54.61           C
ANISOU 5234  CB  GLU B 305     7774   5177   7800     42  -1434   1772       C
ATOM   5235  CG  GLU B 305     -61.010  76.572  39.161  1.00 64.20           C
ANISOU 5235  CG  GLU B 305     8967   6185   9241    135  -1485   1839       C
ATOM   5236  CD  GLU B 305     -59.631  75.951  39.033  1.00 72.39           C
ANISOU 5236  CD  GLU B 305    10143   7139  10221     39  -1316   1872       C
ATOM   5237  OE1 GLU B 305     -59.375  74.926  39.701  1.00 75.58           O
ANISOU 5237  OE1 GLU B 305    10706   7624  10385   -106  -1213   1905       O
ATOM   5238  OE2 GLU B 305     -58.803  76.483  38.264  1.00 75.36           O
ANISOU 5238  OE2 GLU B 305    10466   7366  10801    101  -1276   1854       O
ATOM   5239  N   ILE B 306     -64.483  76.386  37.634  1.00 42.01           N
ANISOU 5239  N   ILE B 306     5641   3730   6591    237  -1439   1473       N
ATOM   5240  CA  ILE B 306     -64.927  77.128  36.458  1.00 44.10           C
ANISOU 5240  CA  ILE B 306     5666   3969   7120    341  -1398   1356       C
ATOM   5241  C   ILE B 306     -66.119  78.013  36.801  1.00 51.20           C
ANISOU 5241  C   ILE B 306     6419   4904   8132    409  -1591   1361       C
ATOM   5242  O   ILE B 306     -66.118  79.218  36.525  1.00 56.57           O
ANISOU 5242  O   ILE B 306     6942   5479   9074    530  -1687   1368       O
ATOM   5243  CB  ILE B 306     -65.264  76.159  35.310  1.00 43.60           C
ANISOU 5243  CB  ILE B 306     5529   4013   7025    284  -1166   1194       C
ATOM   5244  CG1 ILE B 306     -64.011  75.416  34.846  1.00 42.59           C
ANISOU 5244  CG1 ILE B 306     5508   3833   6841    224  -1000   1183       C
ATOM   5245  CG2 ILE B 306     -65.905  76.908  34.152  1.00 37.53           C
ANISOU 5245  CG2 ILE B 306     4538   3236   6484    364  -1110   1070       C
ATOM   5246  CD1 ILE B 306     -64.297  74.292  33.873  1.00 34.98           C
ANISOU 5246  CD1 ILE B 306     4502   2977   5812    152   -817   1050       C
ATOM   5247  N   ILE B 307     -67.153  77.428  37.411  1.00 49.48           N
ANISOU 5247  N   ILE B 307     6239   4824   7735    331  -1649   1350       N
ATOM   5248  CA  ILE B 307     -68.394  78.162  37.641  1.00 48.93           C
ANISOU 5248  CA  ILE B 307     6013   4803   7775    370  -1822   1333       C
ATOM   5249  C   ILE B 307     -68.188  79.291  38.644  1.00 49.17           C
ANISOU 5249  C   ILE B 307     6065   4727   7889    441  -2120   1489       C
ATOM   5250  O   ILE B 307     -68.858  80.328  38.565  1.00 53.00           O
ANISOU 5250  O   ILE B 307     6342   5187   8609    527  -2276   1481       O
ATOM   5251  CB  ILE B 307     -69.508  77.193  38.090  1.00 51.60           C
ANISOU 5251  CB  ILE B 307     6419   5299   7887    256  -1814   1278       C
ATOM   5252  CG1 ILE B 307     -70.859  77.909  38.168  1.00 54.91           C
ANISOU 5252  CG1 ILE B 307     6655   5771   8438    276  -1975   1238       C
ATOM   5253  CG2 ILE B 307     -69.173  76.557  39.430  1.00 53.27           C
ANISOU 5253  CG2 ILE B 307     6909   5533   7800    162  -1902   1388       C
ATOM   5254  CD1 ILE B 307     -71.412  78.325  36.826  1.00 54.57           C
ANISOU 5254  CD1 ILE B 307     6349   5738   8647    328  -1831   1102       C
ATOM   5255  N   LYS B 308     -67.257  79.131  39.583  1.00 49.41           N
ANISOU 5255  N   LYS B 308     6342   4686   7744    404  -2210   1638       N
ATOM   5256  CA  LYS B 308     -67.062  80.121  40.634  1.00 53.21           C
ANISOU 5256  CA  LYS B 308     6895   5059   8262    454  -2529   1814       C
ATOM   5257  C   LYS B 308     -66.175  81.285  40.213  1.00 59.21           C
ANISOU 5257  C   LYS B 308     7540   5619   9337    610  -2600   1877       C
ATOM   5258  O   LYS B 308     -65.914  82.168  41.037  1.00 66.94           O
ANISOU 5258  O   LYS B 308     8574   6476  10384    671  -2888   2040       O
ATOM   5259  CB  LYS B 308     -66.479  79.458  41.884  1.00 54.99           C
ANISOU 5259  CB  LYS B 308     7474   5288   8132    326  -2596   1960       C
ATOM   5260  CG  LYS B 308     -67.495  78.671  42.694  1.00 56.68           C
ANISOU 5260  CG  LYS B 308     7819   5666   8051    191  -2638   1929       C
ATOM   5261  CD  LYS B 308     -66.923  78.244  44.034  1.00 60.71           C
ANISOU 5261  CD  LYS B 308     8692   6161   8214     64  -2727   2082       C
ATOM   5262  CE  LYS B 308     -68.002  77.659  44.929  1.00 65.35           C
ANISOU 5262  CE  LYS B 308     9421   6892   8518    -64  -2806   2046       C
ATOM   5263  NZ  LYS B 308     -67.469  77.249  46.257  1.00 72.43           N
ANISOU 5263  NZ  LYS B 308    10700   7776   9044   -207  -2871   2184       N
ATOM   5264  N   SER B 309     -65.709  81.318  38.966  1.00 56.70           N
ANISOU 5264  N   SER B 309     7078   5252   9214    673  -2357   1752       N
ATOM   5265  CA  SER B 309     -64.890  82.418  38.474  1.00 60.39           C
ANISOU 5265  CA  SER B 309     7428   5515  10003    827  -2390   1776       C
ATOM   5266  C   SER B 309     -65.625  83.284  37.458  1.00 60.55           C
ANISOU 5266  C   SER B 309     7099   5531  10377    952  -2333   1622       C
ATOM   5267  O   SER B 309     -64.992  84.092  36.771  1.00 63.36           O
ANISOU 5267  O   SER B 309     7327   5726  11022   1081  -2270   1580       O
ATOM   5268  CB  SER B 309     -63.591  81.880  37.867  1.00 60.05           C
ANISOU 5268  CB  SER B 309     7522   5382   9912    796  -2152   1752       C
ATOM   5269  OG  SER B 309     -63.856  80.972  36.814  1.00 59.81           O
ANISOU 5269  OG  SER B 309     7430   5483   9812    722  -1859   1570       O
ATOM   5270  N   GLN B 310     -66.942  83.144  37.355  1.00 59.53           N
ANISOU 5270  N   GLN B 310     6817   5564  10237    910  -2340   1531       N
ATOM   5271  CA  GLN B 310     -67.734  83.864  36.370  1.00 60.61           C
ANISOU 5271  CA  GLN B 310     6624   5720  10687    993  -2244   1373       C
ATOM   5272  C   GLN B 310     -68.367  85.104  36.989  1.00 62.14           C
ANISOU 5272  C   GLN B 310     6601   5855  11154   1104  -2552   1446       C
ATOM   5273  O   GLN B 310     -68.620  85.160  38.195  1.00 61.78           O
ANISOU 5273  O   GLN B 310     6683   5842  10950   1056  -2827   1583       O
ATOM   5274  CB  GLN B 310     -68.823  82.960  35.789  1.00 60.19           C
ANISOU 5274  CB  GLN B 310     6523   5869  10476    866  -2052   1227       C
ATOM   5275  CG  GLN B 310     -68.299  81.654  35.220  1.00 60.30           C
ANISOU 5275  CG  GLN B 310     6737   5949  10225    754  -1787   1163       C
ATOM   5276  CD  GLN B 310     -67.336  81.866  34.070  1.00 64.24           C
ANISOU 5276  CD  GLN B 310     7200   6334  10874    814  -1557   1071       C
ATOM   5277  OE1 GLN B 310     -67.504  82.783  33.265  1.00 70.04           O
ANISOU 5277  OE1 GLN B 310     7712   7002  11898    911  -1476    968       O
ATOM   5278  NE2 GLN B 310     -66.316  81.021  33.988  1.00 60.08           N
ANISOU 5278  NE2 GLN B 310     6892   5780  10156    749  -1443   1097       N
ATOM   5279  N   ASP B 311     -68.619  86.103  36.144  1.00 64.51           N
ANISOU 5279  N   ASP B 311     6594   6099  11820   1220  -2458   1318       N
ATOM   5280  CA  ASP B 311     -69.313  87.311  36.571  1.00 67.52           C
ANISOU 5280  CA  ASP B 311     6747   6483  12424   1275  -2648   1312       C
ATOM   5281  C   ASP B 311     -70.816  87.063  36.503  1.00 67.41           C
ANISOU 5281  C   ASP B 311     6557   6640  12416   1190  -2673   1236       C
ATOM   5282  O   ASP B 311     -71.360  86.798  35.425  1.00 63.72           O
ANISOU 5282  O   ASP B 311     5914   6233  12064   1176  -2427   1083       O
ATOM   5283  CB  ASP B 311     -68.920  88.498  35.694  1.00 68.48           C
ANISOU 5283  CB  ASP B 311     6619   6475  12925   1418  -2497   1190       C
ATOM   5284  CG  ASP B 311     -69.204  89.832  36.358  1.00 76.36           C
ANISOU 5284  CG  ASP B 311     7444   7418  14152   1496  -2741   1234       C
ATOM   5285  OD1 ASP B 311     -68.296  90.689  36.392  1.00 81.15           O
ANISOU 5285  OD1 ASP B 311     8042   7862  14928   1611  -2773   1263       O
ATOM   5286  OD2 ASP B 311     -70.329  90.020  36.865  1.00 78.72           O
ANISOU 5286  OD2 ASP B 311     7621   7826  14464   1439  -2911   1244       O
ATOM   5287  N   LEU B 312     -71.486  87.152  37.651  1.00 71.37           N
ANISOU 5287  N   LEU B 312     7120   7214  12783   1119  -2965   1337       N
ATOM   5288  CA  LEU B 312     -72.902  86.832  37.759  1.00 71.04           C
ANISOU 5288  CA  LEU B 312     6962   7332  12699   1010  -3023   1279       C
ATOM   5289  C   LEU B 312     -73.805  88.044  37.546  1.00 72.93           C
ANISOU 5289  C   LEU B 312     6852   7577  13280   1052  -3071   1185       C
ATOM   5290  O   LEU B 312     -74.994  87.982  37.880  1.00 74.87           O
ANISOU 5290  O   LEU B 312     7010   7939  13500    953  -3185   1159       O
ATOM   5291  CB  LEU B 312     -73.193  86.200  39.123  1.00 72.94           C
ANISOU 5291  CB  LEU B 312     7485   7648  12581    887  -3300   1420       C
ATOM   5292  CG  LEU B 312     -73.025  84.685  39.292  1.00 72.00           C
ANISOU 5292  CG  LEU B 312     7668   7610  12077    770  -3213   1456       C
ATOM   5293  CD1 LEU B 312     -71.620  84.214  38.947  1.00 73.99           C
ANISOU 5293  CD1 LEU B 312     8128   7771  12213    806  -3008   1488       C
ATOM   5294  CD2 LEU B 312     -73.392  84.261  40.706  1.00 72.54           C
ANISOU 5294  CD2 LEU B 312     8001   7743  11817    649  -3499   1582       C
ATOM   5295  N   SER B 313     -73.275  89.136  36.995  1.00 77.35           N
ANISOU 5295  N   SER B 313     7216   8012  14162   1189  -2979   1128       N
ATOM   5296  CA  SER B 313     -74.018  90.383  36.866  1.00 83.06           C
ANISOU 5296  CA  SER B 313     7608   8720  15231   1240  -3032   1050       C
ATOM   5297  C   SER B 313     -74.565  90.611  35.462  1.00 85.04           C
ANISOU 5297  C   SER B 313     7562   9005  15745   1251  -2682    841       C
ATOM   5298  O   SER B 313     -74.997  91.725  35.153  1.00 91.08           O
ANISOU 5298  O   SER B 313     8035   9732  16839   1310  -2652    754       O
ATOM   5299  CB  SER B 313     -73.138  91.567  37.274  1.00 87.54           C
ANISOU 5299  CB  SER B 313     8140   9116  16008   1385  -3183   1125       C
ATOM   5300  OG  SER B 313     -72.213  91.896  36.251  1.00 88.46           O
ANISOU 5300  OG  SER B 313     8185   9112  16315   1503  -2907   1029       O
ATOM   5301  N   VAL B 314     -74.558  89.591  34.609  1.00 81.77           N
ANISOU 5301  N   VAL B 314     7217   8657  15193   1188  -2412    758       N
ATOM   5302  CA  VAL B 314     -75.051  89.697  33.241  1.00 81.88           C
ANISOU 5302  CA  VAL B 314     6996   8710  15406   1171  -2050    558       C
ATOM   5303  C   VAL B 314     -76.149  88.664  33.034  1.00 75.92           C
ANISOU 5303  C   VAL B 314     6252   8126  14469   1003  -1982    513       C
ATOM   5304  O   VAL B 314     -76.074  87.550  33.563  1.00 73.81           O
ANISOU 5304  O   VAL B 314     6234   7921  13891    928  -2097    612       O
ATOM   5305  CB  VAL B 314     -73.925  89.503  32.205  1.00 86.74           C
ANISOU 5305  CB  VAL B 314     7683   9221  16052   1252  -1743    475       C
ATOM   5306  CG1 VAL B 314     -73.613  90.818  31.508  1.00 88.17           C
ANISOU 5306  CG1 VAL B 314     7626   9282  16593   1371  -1571    347       C
ATOM   5307  CG2 VAL B 314     -72.679  88.931  32.870  1.00 89.60           C
ANISOU 5307  CG2 VAL B 314     8372   9495  16177   1299  -1892    634       C
ATOM   5308  N   VAL B 315     -77.160  89.035  32.246  1.00 74.45           N
ANISOU 5308  N   VAL B 315     5804   8009  14472    935  -1779    361       N
ATOM   5309  CA  VAL B 315     -78.296  88.146  32.016  1.00 70.96           C
ANISOU 5309  CA  VAL B 315     5359   7723  13881    754  -1708    312       C
ATOM   5310  C   VAL B 315     -77.872  86.932  31.198  1.00 64.67           C
ANISOU 5310  C   VAL B 315     4864   6972  12735    661  -1407    259       C
ATOM   5311  O   VAL B 315     -78.216  85.790  31.528  1.00 61.64           O
ANISOU 5311  O   VAL B 315     4746   6684  11991    527  -1448    307       O
ATOM   5312  CB  VAL B 315     -79.446  88.911  31.336  1.00 74.90           C
ANISOU 5312  CB  VAL B 315     5550   8276  14632    679  -1526    161       C
ATOM   5313  CG1 VAL B 315     -80.541  87.951  30.899  1.00 73.54           C
ANISOU 5313  CG1 VAL B 315     5397   8247  14299    473  -1392     98       C
ATOM   5314  CG2 VAL B 315     -80.000  89.971  32.273  1.00 78.16           C
ANISOU 5314  CG2 VAL B 315     5807   8670  15220    714  -1821    218       C
ATOM   5315  N   SER B 316     -77.132  87.156  30.115  1.00 62.82           N
ANISOU 5315  N   SER B 316     4612   6663  12592    723  -1099    151       N
ATOM   5316  CA  SER B 316     -76.674  86.062  29.269  1.00 60.70           C
ANISOU 5316  CA  SER B 316     4642   6430  11992    628   -826     99       C
ATOM   5317  C   SER B 316     -75.309  86.417  28.702  1.00 59.25           C
ANISOU 5317  C   SER B 316     4513   6106  11892    761   -672     60       C
ATOM   5318  O   SER B 316     -75.126  87.510  28.159  1.00 58.30           O
ANISOU 5318  O   SER B 316     4139   5891  12122    870   -539    -43       O
ATOM   5319  CB  SER B 316     -77.665  85.778  28.136  1.00 65.97           C
ANISOU 5319  CB  SER B 316     5250   7195  12620    465   -517    -49       C
ATOM   5320  OG  SER B 316     -77.637  86.803  27.159  1.00 74.74           O
ANISOU 5320  OG  SER B 316     6100   8245  14053    519   -251   -202       O
ATOM   5321  N   LYS B 317     -74.357  85.496  28.837  1.00 56.59           N
ANISOU 5321  N   LYS B 317     4500   5749  11252    749   -683    135       N
ATOM   5322  CA  LYS B 317     -73.004  85.684  28.336  1.00 57.39           C
ANISOU 5322  CA  LYS B 317     4703   5712  11390    850   -551    106       C
ATOM   5323  C   LYS B 317     -72.471  84.357  27.820  1.00 55.98           C
ANISOU 5323  C   LYS B 317     4856   5584  10828    730   -403    101       C
ATOM   5324  O   LYS B 317     -72.696  83.311  28.436  1.00 56.35           O
ANISOU 5324  O   LYS B 317     5097   5726  10589    638   -534    199       O
ATOM   5325  CB  LYS B 317     -72.065  86.224  29.423  1.00 59.67           C
ANISOU 5325  CB  LYS B 317     5012   5863  11798   1010   -839    257       C
ATOM   5326  CG  LYS B 317     -70.644  86.473  28.935  1.00 65.04           C
ANISOU 5326  CG  LYS B 317     5798   6375  12542   1113   -711    228       C
ATOM   5327  CD  LYS B 317     -69.616  86.202  30.021  1.00 70.90           C
ANISOU 5327  CD  LYS B 317     6762   7026  13152   1172   -972    419       C
ATOM   5328  CE  LYS B 317     -69.809  87.115  31.219  1.00 76.14           C
ANISOU 5328  CE  LYS B 317     7270   7618  14043   1296  -1326    563       C
ATOM   5329  NZ  LYS B 317     -68.786  86.861  32.272  1.00 76.26           N
ANISOU 5329  NZ  LYS B 317     7539   7534  13901   1332  -1570    761       N
ATOM   5330  N   VAL B 318     -71.771  84.403  26.690  1.00 55.38           N
ANISOU 5330  N   VAL B 318     4842   5440  10760    731   -133    -22       N
ATOM   5331  CA  VAL B 318     -71.053  83.232  26.201  1.00 53.68           C
ANISOU 5331  CA  VAL B 318     4931   5245  10220    634    -27    -20       C
ATOM   5332  C   VAL B 318     -69.706  83.153  26.906  1.00 54.35           C
ANISOU 5332  C   VAL B 318     5167   5209  10274    729   -180     95       C
ATOM   5333  O   VAL B 318     -69.027  84.168  27.109  1.00 59.57           O
ANISOU 5333  O   VAL B 318     5720   5718  11196    876   -226    101       O
ATOM   5334  CB  VAL B 318     -70.891  83.282  24.669  1.00 57.54           C
ANISOU 5334  CB  VAL B 318     5453   5713  10695    566    312   -202       C
ATOM   5335  CG1 VAL B 318     -72.253  83.266  23.992  1.00 56.98           C
ANISOU 5335  CG1 VAL B 318     5271   5765  10614    441    471   -299       C
ATOM   5336  CG2 VAL B 318     -70.091  84.507  24.240  1.00 67.61           C
ANISOU 5336  CG2 VAL B 318     6592   6818  12281    710    440   -306       C
ATOM   5337  N   VAL B 319     -69.324  81.944  27.307  1.00 50.96           N
ANISOU 5337  N   VAL B 319     4984   4839   9540    643   -259    191       N
ATOM   5338  CA  VAL B 319     -68.093  81.710  28.051  1.00 47.54           C
ANISOU 5338  CA  VAL B 319     4718   4307   9037    696   -397    314       C
ATOM   5339  C   VAL B 319     -67.307  80.624  27.333  1.00 41.19           C
ANISOU 5339  C   VAL B 319     4142   3515   7995    590   -247    275       C
ATOM   5340  O   VAL B 319     -67.793  79.496  27.187  1.00 42.18           O
ANISOU 5340  O   VAL B 319     4374   3772   7883    467   -221    278       O
ATOM   5341  CB  VAL B 319     -68.368  81.304  29.509  1.00 48.11           C
ANISOU 5341  CB  VAL B 319     4859   4442   8981    687   -670    488       C
ATOM   5342  CG1 VAL B 319     -67.068  80.968  30.218  1.00 51.76           C
ANISOU 5342  CG1 VAL B 319     5524   4806   9335    708   -772    615       C
ATOM   5343  CG2 VAL B 319     -69.106  82.416  30.239  1.00 47.93           C
ANISOU 5343  CG2 VAL B 319     4614   4399   9200    786   -863    535       C
ATOM   5344  N   LYS B 320     -66.101  80.960  26.885  1.00 42.26           N
ANISOU 5344  N   LYS B 320     4346   3501   8208    639   -162    238       N
ATOM   5345  CA  LYS B 320     -65.225  80.022  26.198  1.00 42.37           C
ANISOU 5345  CA  LYS B 320     4567   3505   8025    538    -43    199       C
ATOM   5346  C   LYS B 320     -64.205  79.475  27.188  1.00 43.82           C
ANISOU 5346  C   LYS B 320     4911   3636   8103    535   -198    351       C
ATOM   5347  O   LYS B 320     -63.468  80.244  27.814  1.00 52.54           O
ANISOU 5347  O   LYS B 320     6009   4593   9362    640   -299    428       O
ATOM   5348  CB  LYS B 320     -64.520  80.692  25.019  1.00 46.39           C
ANISOU 5348  CB  LYS B 320     5077   3880   8671    565    164     42       C
ATOM   5349  CG  LYS B 320     -65.455  81.165  23.919  1.00 53.69           C
ANISOU 5349  CG  LYS B 320     5874   4858   9667    536    372   -127       C
ATOM   5350  CD  LYS B 320     -64.682  81.829  22.790  1.00 65.66           C
ANISOU 5350  CD  LYS B 320     7421   6229  11299    556    597   -298       C
ATOM   5351  CE  LYS B 320     -65.613  82.339  21.701  1.00 73.51           C
ANISOU 5351  CE  LYS B 320     8301   7276  12354    511    840   -475       C
ATOM   5352  NZ  LYS B 320     -64.866  83.014  20.603  1.00 78.50           N
ANISOU 5352  NZ  LYS B 320     8978   7760  13087    524   1087   -664       N
ATOM   5353  N   VAL B 321     -64.168  78.153  27.329  1.00 41.02           N
ANISOU 5353  N   VAL B 321     4697   3392   7495    414   -211    397       N
ATOM   5354  CA  VAL B 321     -63.226  77.471  28.207  1.00 40.50           C
ANISOU 5354  CA  VAL B 321     4786   3296   7307    379   -312    527       C
ATOM   5355  C   VAL B 321     -62.443  76.469  27.372  1.00 38.68           C
ANISOU 5355  C   VAL B 321     4687   3070   6938    262   -191    465       C
ATOM   5356  O   VAL B 321     -63.026  75.740  26.561  1.00 36.64           O
ANISOU 5356  O   VAL B 321     4433   2922   6567    178   -107    381       O
ATOM   5357  CB  VAL B 321     -63.940  76.768  29.376  1.00 41.10           C
ANISOU 5357  CB  VAL B 321     4888   3505   7225    341   -453    643       C
ATOM   5358  CG1 VAL B 321     -62.923  76.149  30.325  1.00 40.71           C
ANISOU 5358  CG1 VAL B 321     5000   3415   7051    295   -525    773       C
ATOM   5359  CG2 VAL B 321     -64.840  77.745  30.114  1.00 44.09           C
ANISOU 5359  CG2 VAL B 321     5131   3891   7731    437   -596    693       C
ATOM   5360  N   THR B 322     -61.128  76.438  27.566  1.00 40.64           N
ANISOU 5360  N   THR B 322     5048   3192   7202    251   -199    513       N
ATOM   5361  CA  THR B 322     -60.271  75.505  26.844  1.00 37.71           C
ANISOU 5361  CA  THR B 322     4794   2814   6721    132   -112    461       C
ATOM   5362  C   THR B 322     -60.274  74.170  27.578  1.00 37.99           C
ANISOU 5362  C   THR B 322     4890   2970   6573     35   -171    555       C
ATOM   5363  O   THR B 322     -59.762  74.064  28.697  1.00 38.81           O
ANISOU 5363  O   THR B 322     5054   3042   6651     36   -250    682       O
ATOM   5364  CB  THR B 322     -58.857  76.060  26.715  1.00 37.08           C
ANISOU 5364  CB  THR B 322     4803   2533   6754    148    -87    461       C
ATOM   5365  OG1 THR B 322     -58.908  77.351  26.096  1.00 38.58           O
ANISOU 5365  OG1 THR B 322     4918   2596   7144    258    -19    360       O
ATOM   5366  CG2 THR B 322     -58.002  75.135  25.862  1.00 39.10           C
ANISOU 5366  CG2 THR B 322     5168   2780   6907      8     -6    390       C
ATOM   5367  N   ILE B 323     -60.866  73.154  26.953  1.00 34.59           N
ANISOU 5367  N   ILE B 323     4450   2672   6019    -48   -128    492       N
ATOM   5368  CA  ILE B 323     -60.954  71.810  27.511  1.00 34.57           C
ANISOU 5368  CA  ILE B 323     4476   2784   5875   -130   -163    552       C
ATOM   5369  C   ILE B 323     -60.487  70.832  26.444  1.00 33.55           C
ANISOU 5369  C   ILE B 323     4384   2676   5686   -240   -108    474       C
ATOM   5370  O   ILE B 323     -60.930  70.910  25.294  1.00 35.64           O
ANISOU 5370  O   ILE B 323     4643   2958   5941   -260    -63    372       O
ATOM   5371  CB  ILE B 323     -62.388  71.471  27.964  1.00 30.98           C
ANISOU 5371  CB  ILE B 323     3952   2472   5347   -107   -208    566       C
ATOM   5372  CG1 ILE B 323     -62.911  72.536  28.929  1.00 31.72           C
ANISOU 5372  CG1 ILE B 323     4002   2543   5507     -7   -292    635       C
ATOM   5373  CG2 ILE B 323     -62.433  70.096  28.614  1.00 30.21           C
ANISOU 5373  CG2 ILE B 323     3881   2471   5125   -177   -226    615       C
ATOM   5374  CD1 ILE B 323     -64.360  72.352  29.312  1.00 38.66           C
ANISOU 5374  CD1 ILE B 323     4813   3547   6328      8   -343    634       C
ATOM   5375  N   ASP B 324     -59.593  69.917  26.824  1.00 33.32           N
ANISOU 5375  N   ASP B 324     4398   2644   5619   -320   -116    524       N
ATOM   5376  CA  ASP B 324     -59.006  68.959  25.886  1.00 34.74           C
ANISOU 5376  CA  ASP B 324     4599   2833   5768   -431    -99    461       C
ATOM   5377  C   ASP B 324     -58.358  69.674  24.701  1.00 34.40           C
ANISOU 5377  C   ASP B 324     4623   2672   5776   -456    -54    362       C
ATOM   5378  O   ASP B 324     -58.463  69.233  23.555  1.00 32.18           O
ANISOU 5378  O   ASP B 324     4369   2417   5442   -527    -50    274       O
ATOM   5379  CB  ASP B 324     -60.043  67.942  25.402  1.00 37.08           C
ANISOU 5379  CB  ASP B 324     4842   3265   5983   -460   -128    424       C
ATOM   5380  CG  ASP B 324     -60.553  67.051  26.515  1.00 38.28           C
ANISOU 5380  CG  ASP B 324     4935   3517   6092   -449   -154    497       C
ATOM   5381  OD1 ASP B 324     -59.805  66.821  27.487  1.00 38.18           O
ANISOU 5381  OD1 ASP B 324     4933   3482   6090   -471   -136    567       O
ATOM   5382  OD2 ASP B 324     -61.704  66.573  26.412  1.00 37.99           O
ANISOU 5382  OD2 ASP B 324     4854   3573   6007   -427   -180    479       O
ATOM   5383  N   TYR B 325     -57.696  70.797  24.985  1.00 33.33           N
ANISOU 5383  N   TYR B 325     4528   2396   5741   -397    -26    375       N
ATOM   5384  CA  TYR B 325     -56.980  71.634  24.024  1.00 34.54           C
ANISOU 5384  CA  TYR B 325     4753   2402   5967   -403     38    272       C
ATOM   5385  C   TYR B 325     -57.894  72.333  23.026  1.00 37.50           C
ANISOU 5385  C   TYR B 325     5109   2797   6343   -357    109    151       C
ATOM   5386  O   TYR B 325     -57.400  72.886  22.035  1.00 37.17           O
ANISOU 5386  O   TYR B 325     5142   2649   6332   -383    190     31       O
ATOM   5387  CB  TYR B 325     -55.918  70.847  23.248  1.00 35.03           C
ANISOU 5387  CB  TYR B 325     4899   2421   5991   -550     37    217       C
ATOM   5388  CG  TYR B 325     -54.787  70.322  24.098  1.00 42.05           C
ANISOU 5388  CG  TYR B 325     5810   3254   6914   -617      3    317       C
ATOM   5389  CD1 TYR B 325     -53.865  71.187  24.670  1.00 41.71           C
ANISOU 5389  CD1 TYR B 325     5831   3040   6978   -581     21    368       C
ATOM   5390  CD2 TYR B 325     -54.632  68.960  24.315  1.00 43.11           C
ANISOU 5390  CD2 TYR B 325     5896   3494   6988   -721    -41    360       C
ATOM   5391  CE1 TYR B 325     -52.825  70.710  25.445  1.00 45.64           C
ANISOU 5391  CE1 TYR B 325     6366   3479   7494   -666      5    466       C
ATOM   5392  CE2 TYR B 325     -53.594  68.473  25.087  1.00 44.77           C
ANISOU 5392  CE2 TYR B 325     6115   3657   7237   -801    -42    443       C
ATOM   5393  CZ  TYR B 325     -52.694  69.352  25.650  1.00 44.56           C
ANISOU 5393  CZ  TYR B 325     6175   3465   7291   -783    -14    499       C
ATOM   5394  OH  TYR B 325     -51.660  68.871  26.420  1.00 47.02           O
ANISOU 5394  OH  TYR B 325     6513   3723   7630   -884     -1    590       O
ATOM   5395  N   THR B 326     -59.206  72.331  23.248  1.00 30.90           N
ANISOU 5395  N   THR B 326     3007   3047   5687    394   -206    553       N
ATOM   5396  CA  THR B 326     -60.131  73.036  22.375  1.00 31.53           C
ANISOU 5396  CA  THR B 326     3098   3228   5654    330   -150    488       C
ATOM   5397  C   THR B 326     -61.006  73.963  23.208  1.00 35.93           C
ANISOU 5397  C   THR B 326     3632   3701   6318    414   -102    468       C
ATOM   5398  O   THR B 326     -61.261  73.708  24.389  1.00 36.79           O
ANISOU 5398  O   THR B 326     3762   3704   6511    506   -146    564       O
ATOM   5399  CB  THR B 326     -61.001  72.061  21.556  1.00 40.22           C
ANISOU 5399  CB  THR B 326     4251   4445   6586    227   -237    666       C
ATOM   5400  OG1 THR B 326     -61.613  72.762  20.467  1.00 44.12           O
ANISOU 5400  OG1 THR B 326     4771   5128   6864     38   -156    610       O
ATOM   5401  CG2 THR B 326     -62.088  71.436  22.417  1.00 31.58           C
ANISOU 5401  CG2 THR B 326     3173   3214   5613    330   -304    824       C
ATOM   5402  N  AGLU B 327     -61.450  75.052  22.586  0.49 37.14           N
ANISOU 5402  N  AGLU B 327     3714   3944   6456    358     -2    301       N
ATOM   5403  N  BGLU B 327     -61.460  75.044  22.581  0.51 37.12           N
ANISOU 5403  N  BGLU B 327     3711   3942   6450    357     -2    302       N
ATOM   5404  CA AGLU B 327     -62.297  76.024  23.267  0.49 38.89           C
ANISOU 5404  CA AGLU B 327     3852   4109   6816    426     21    250       C
ATOM   5405  CA BGLU B 327     -62.301  76.026  23.254  0.51 38.91           C
ANISOU 5405  CA BGLU B 327     3854   4114   6817    424     22    249       C
ATOM   5406  C  AGLU B 327     -63.742  75.540  23.260  0.49 38.30           C
ANISOU 5406  C  AGLU B 327     3825   4095   6631    329     22    417       C
ATOM   5407  C  BGLU B 327     -63.748  75.547  23.258  0.51 38.31           C
ANISOU 5407  C  BGLU B 327     3826   4098   6633    328     22    416       C
ATOM   5408  O  AGLU B 327     -64.334  75.343  22.194  0.49 37.97           O
ANISOU 5408  O  AGLU B 327     3807   4222   6397    132     83    461       O
ATOM   5409  O  BGLU B 327     -64.349  75.360  22.194  0.51 37.98           O
ANISOU 5409  O  BGLU B 327     3806   4224   6398    131     85    460       O
ATOM   5410  CB AGLU B 327     -62.187  77.397  22.608  0.49 42.17           C
ANISOU 5410  CB AGLU B 327     4080   4608   7333    413    144    -70       C
ATOM   5411  CB BGLU B 327     -62.185  77.386  22.569  0.51 42.18           C
ANISOU 5411  CB BGLU B 327     4082   4617   7328    407    148    -73       C
ATOM   5412  CG AGLU B 327     -61.074  78.268  23.169  0.49 45.19           C
ANISOU 5412  CG AGLU B 327     4375   4750   8045    598     43   -238       C
ATOM   5413  CG BGLU B 327     -61.474  78.456  23.391  0.51 44.72           C
ANISOU 5413  CG BGLU B 327     4286   4693   8012    613     38   -220       C
ATOM   5414  CD AGLU B 327     -61.269  79.738  22.849  0.49 49.87           C
ANISOU 5414  CD AGLU B 327     4692   5354   8901    674    119   -602       C
ATOM   5415  CD BGLU B 327     -59.959  78.373  23.305  0.51 46.58           C
ANISOU 5415  CD BGLU B 327     4573   4751   8375    669    -46   -291       C
ATOM   5416  OE1AGLU B 327     -62.003  80.048  21.887  0.49 53.10           O
ANISOU 5416  OE1AGLU B 327     4965   6062   9147    519    344   -808       O
ATOM   5417  OE1BGLU B 327     -59.416  77.255  23.184  0.51 45.97           O
ANISOU 5417  OE1BGLU B 327     4649   4703   8114    585    -66   -125       O
ATOM   5418  OE2AGLU B 327     -60.694  80.585  23.565  0.49 51.48           O
ANISOU 5418  OE2AGLU B 327     4797   5272   9489    872    -62   -680       O
ATOM   5419  OE2BGLU B 327     -59.307  79.437  23.354  0.51 50.27           O
ANISOU 5419  OE2BGLU B 327     4900   5018   9180    797   -117   -528       O
ATOM   5420  N   ILE B 328     -64.305  75.349  24.450  1.00 37.69           N
ANISOU 5420  N   ILE B 328     3780   3880   6662    427    -66    513       N
ATOM   5421  CA  ILE B 328     -65.690  74.924  24.614  1.00 37.25           C
ANISOU 5421  CA  ILE B 328     3768   3792   6591    351   -103    631       C
ATOM   5422  C   ILE B 328     -66.515  76.130  25.036  1.00 41.11           C
ANISOU 5422  C   ILE B 328     4131   4302   7188    327    -74    522       C
ATOM   5423  O   ILE B 328     -66.192  76.800  26.025  1.00 40.80           O
ANISOU 5423  O   ILE B 328     4031   4192   7279    461   -145    445       O
ATOM   5424  CB  ILE B 328     -65.808  73.789  25.645  1.00 39.33           C
ANISOU 5424  CB  ILE B 328     4121   3904   6917    466   -211    713       C
ATOM   5425  CG1 ILE B 328     -64.982  72.580  25.203  1.00 42.99           C
ANISOU 5425  CG1 ILE B 328     4624   4365   7343    502   -249    783       C
ATOM   5426  CG2 ILE B 328     -67.262  73.392  25.830  1.00 38.42           C
ANISOU 5426  CG2 ILE B 328     4047   3675   6877    404   -283    776       C
ATOM   5427  CD1 ILE B 328     -65.470  71.947  23.919  1.00 42.09           C
ANISOU 5427  CD1 ILE B 328     4563   4269   7159    369   -326    941       C
ATOM   5428  N   SER B 329     -67.577  76.411  24.286  1.00 43.78           N
ANISOU 5428  N   SER B 329     4421   4747   7465    120      3    543       N
ATOM   5429  CA  SER B 329     -68.450  77.540  24.575  1.00 42.56           C
ANISOU 5429  CA  SER B 329     4083   4653   7434     53     46    417       C
ATOM   5430  C   SER B 329     -69.545  77.118  25.545  1.00 43.89           C
ANISOU 5430  C   SER B 329     4332   4648   7697     42    -99    521       C
ATOM   5431  O   SER B 329     -70.160  76.059  25.379  1.00 38.71           O
ANISOU 5431  O   SER B 329     3842   3864   7002    -47   -170    694       O
ATOM   5432  CB  SER B 329     -69.066  78.091  23.288  1.00 44.86           C
ANISOU 5432  CB  SER B 329     4249   5211   7583   -248    249    359       C
ATOM   5433  OG  SER B 329     -68.079  78.686  22.464  1.00 49.46           O
ANISOU 5433  OG  SER B 329     4702   5994   8097   -235    414    125       O
ATOM   5434  N   PHE B 330     -69.780  77.947  26.558  1.00 48.38           N
ANISOU 5434  N   PHE B 330     4774   5187   8419    135   -185    399       N
ATOM   5435  CA  PHE B 330     -70.835  77.727  27.533  1.00 47.12           C
ANISOU 5435  CA  PHE B 330     4667   4902   8337     97   -325    415       C
ATOM   5436  C   PHE B 330     -71.819  78.887  27.496  1.00 52.46           C
ANISOU 5436  C   PHE B 330     5099   5681   9151    -59   -313    305       C
ATOM   5437  O   PHE B 330     -71.450  80.025  27.194  1.00 60.81           O
ANISOU 5437  O   PHE B 330     5899   6895  10312    -21   -245    152       O
ATOM   5438  CB  PHE B 330     -70.271  77.585  28.952  1.00 43.35           C
ANISOU 5438  CB  PHE B 330     4273   4350   7848    288   -487    375       C
ATOM   5439  CG  PHE B 330     -69.555  76.290  29.198  1.00 41.74           C
ANISOU 5439  CG  PHE B 330     4266   4073   7520    387   -474    436       C
ATOM   5440  CD1 PHE B 330     -68.264  76.096  28.735  1.00 42.92           C
ANISOU 5440  CD1 PHE B 330     4441   4268   7600    475   -404    490       C
ATOM   5441  CD2 PHE B 330     -70.168  75.271  29.907  1.00 42.71           C
ANISOU 5441  CD2 PHE B 330     4506   4084   7639    388   -528    383       C
ATOM   5442  CE1 PHE B 330     -67.601  74.906  28.966  1.00 31.21           C
ANISOU 5442  CE1 PHE B 330     3074   2753   6030    544   -382    523       C
ATOM   5443  CE2 PHE B 330     -69.511  74.079  30.141  1.00 41.12           C
ANISOU 5443  CE2 PHE B 330     4397   3851   7375    490   -488    364       C
ATOM   5444  CZ  PHE B 330     -68.225  73.897  29.669  1.00 39.02           C
ANISOU 5444  CZ  PHE B 330     4133   3666   7026    558   -412    450       C
ATOM   5445  N   MET B 331     -73.076  78.589  27.804  1.00 48.05           N
ANISOU 5445  N   MET B 331     4588   5019   8651   -232   -389    344       N
ATOM   5446  CA  MET B 331     -74.103  79.608  27.958  1.00 49.42           C
ANISOU 5446  CA  MET B 331     4514   5284   8979   -412   -410    233       C
ATOM   5447  C   MET B 331     -74.304  79.874  29.443  1.00 45.56           C
ANISOU 5447  C   MET B 331     4018   4711   8580   -282   -663    122       C
ATOM   5448  O   MET B 331     -74.709  78.976  30.188  1.00 44.48           O
ANISOU 5448  O   MET B 331     4104   4398   8398   -277   -784    130       O
ATOM   5449  CB  MET B 331     -75.416  79.179  27.304  1.00 57.97           C
ANISOU 5449  CB  MET B 331     5659   6294  10074   -772   -361    370       C
ATOM   5450  CG  MET B 331     -75.490  79.475  25.816  1.00 66.39           C
ANISOU 5450  CG  MET B 331     6624   7602  10998  -1059   -105    461       C
ATOM   5451  SD  MET B 331     -75.168  81.212  25.444  1.00 75.15           S
ANISOU 5451  SD  MET B 331     7229   9124  12202  -1071    120    127       S
ATOM   5452  CE  MET B 331     -76.414  82.025  26.442  1.00 74.00           C
ANISOU 5452  CE  MET B 331     6819   8946  12354  -1189    -51    -10       C
ATOM   5453  N   LEU B 332     -74.014  81.099  29.868  1.00 48.59           N
ANISOU 5453  N   LEU B 332     4134   5227   9101   -180   -766     -7       N
ATOM   5454  CA  LEU B 332     -74.159  81.512  31.259  1.00 50.22           C
ANISOU 5454  CA  LEU B 332     4326   5407   9347    -98  -1074    -70       C
ATOM   5455  C   LEU B 332     -75.376  82.421  31.370  1.00 52.13           C
ANISOU 5455  C   LEU B 332     4260   5732   9814   -297  -1163   -205       C
ATOM   5456  O   LEU B 332     -75.360  83.553  30.876  1.00 54.87           O
ANISOU 5456  O   LEU B 332     4222   6232  10395   -291  -1119   -323       O
ATOM   5457  CB  LEU B 332     -72.902  82.221  31.757  1.00 50.54           C
ANISOU 5457  CB  LEU B 332     4300   5475   9427    160  -1251    -47       C
ATOM   5458  CG  LEU B 332     -73.006  82.812  33.164  1.00 54.25           C
ANISOU 5458  CG  LEU B 332     4753   5957   9903    196  -1650    -40       C
ATOM   5459  CD1 LEU B 332     -73.225  81.714  34.196  1.00 52.43           C
ANISOU 5459  CD1 LEU B 332     4889   5708   9326    104  -1722     -6       C
ATOM   5460  CD2 LEU B 332     -71.773  83.637  33.500  1.00 58.32           C
ANISOU 5460  CD2 LEU B 332     5188   6429  10543    424  -1896     60       C
ATOM   5461  N   TRP B 333     -76.426  81.924  32.014  1.00 50.51           N
ANISOU 5461  N   TRP B 333     4189   5427   9576   -476  -1283   -238       N
ATOM   5462  CA  TRP B 333     -77.622  82.704  32.296  1.00 54.72           C
ANISOU 5462  CA  TRP B 333     4450   6021  10319   -703  -1418   -372       C
ATOM   5463  C   TRP B 333     -77.650  83.040  33.779  1.00 54.88           C
ANISOU 5463  C   TRP B 333     4500   6066  10286   -624  -1807   -459       C
ATOM   5464  O   TRP B 333     -77.544  82.144  34.623  1.00 54.51           O
ANISOU 5464  O   TRP B 333     4794   5930   9986   -594  -1903   -469       O
ATOM   5465  CB  TRP B 333     -78.886  81.940  31.899  1.00 58.89           C
ANISOU 5465  CB  TRP B 333     5112   6379  10884  -1030  -1316   -350       C
ATOM   5466  CG  TRP B 333     -79.044  81.775  30.422  1.00 60.44           C
ANISOU 5466  CG  TRP B 333     5265   6609  11093  -1231   -996   -200       C
ATOM   5467  CD1 TRP B 333     -78.570  80.752  29.655  1.00 59.44           C
ANISOU 5467  CD1 TRP B 333     5425   6358  10802  -1194   -831     -7       C
ATOM   5468  CD2 TRP B 333     -79.725  82.664  29.529  1.00 64.98           C
ANISOU 5468  CD2 TRP B 333     5476   7406  11809  -1551   -808   -230       C
ATOM   5469  NE1 TRP B 333     -78.915  80.946  28.340  1.00 62.60           N
ANISOU 5469  NE1 TRP B 333     5714   6895  11177  -1495   -583    125       N
ATOM   5470  CE2 TRP B 333     -79.624  82.114  28.236  1.00 65.63           C
ANISOU 5470  CE2 TRP B 333     5695   7516  11726  -1738   -526    -23       C
ATOM   5471  CE3 TRP B 333     -80.411  83.871  29.697  1.00 70.31           C
ANISOU 5471  CE3 TRP B 333     5693   8297  12724  -1726   -851   -424       C
ATOM   5472  CZ2 TRP B 333     -80.183  82.729  27.118  1.00 70.87           C
ANISOU 5472  CZ2 TRP B 333     6086   8462  12380  -2142   -245     -4       C
ATOM   5473  CZ3 TRP B 333     -80.966  84.480  28.586  1.00 73.58           C
ANISOU 5473  CZ3 TRP B 333     5779   8979  13200  -2094   -546   -447       C
ATOM   5474  CH2 TRP B 333     -80.848  83.909  27.313  1.00 73.92           C
ANISOU 5474  CH2 TRP B 333     5999   9089  12998  -2323   -226   -237       C
ATOM   5475  N   CYS B 334     -77.781  84.326  34.093  1.00 56.14           N
ANISOU 5475  N   CYS B 334     4280   6375  10677   -604  -2038   -544       N
ATOM   5476  CA  CYS B 334     -77.820  84.783  35.472  1.00 58.51           C
ANISOU 5476  CA  CYS B 334     4589   6734  10908   -570  -2492   -578       C
ATOM   5477  C   CYS B 334     -79.023  85.687  35.682  1.00 72.11           C
ANISOU 5477  C   CYS B 334     5920   8555  12925   -793  -2693   -754       C
ATOM   5478  O   CYS B 334     -79.523  86.315  34.745  1.00 75.93           O
ANISOU 5478  O   CYS B 334     6005   9116  13730   -905  -2489   -848       O
ATOM   5479  CB  CYS B 334     -76.537  85.526  35.861  1.00 58.75           C
ANISOU 5479  CB  CYS B 334     4547   6807  10969   -274  -2756   -435       C
ATOM   5480  SG  CYS B 334     -75.031  84.550  35.681  1.00 65.04           S
ANISOU 5480  SG  CYS B 334     5772   7501  11440    -62  -2551   -217       S
ATOM   5481  N   LYS B 335     -79.479  85.748  36.931  1.00 73.64           N
ANISOU 5481  N   LYS B 335     6215   8792  12973   -896  -3086   -822       N
ATOM   5482  CA  LYS B 335     -80.654  86.533  37.288  1.00 79.09           C
ANISOU 5482  CA  LYS B 335     6553   9577  13921  -1139  -3344  -1006       C
ATOM   5483  C   LYS B 335     -80.533  86.929  38.750  1.00 81.09           C
ANISOU 5483  C   LYS B 335     6892   9954  13964  -1128  -3913   -998       C
ATOM   5484  O   LYS B 335     -80.479  86.056  39.620  1.00 81.78           O
ANISOU 5484  O   LYS B 335     7432  10042  13597  -1209  -3992  -1020       O
ATOM   5485  CB  LYS B 335     -81.939  85.735  37.052  1.00 84.45           C
ANISOU 5485  CB  LYS B 335     7370  10113  14603  -1492  -3134  -1159       C
ATOM   5486  CG  LYS B 335     -83.200  86.575  36.930  1.00 93.96           C
ANISOU 5486  CG  LYS B 335     8163  11408  16129  -1794  -3209  -1318       C
ATOM   5487  CD  LYS B 335     -83.414  87.035  35.496  1.00 99.58           C
ANISOU 5487  CD  LYS B 335     8549  12198  17090  -1882  -2762  -1269       C
ATOM   5488  CE  LYS B 335     -84.823  87.570  35.290  1.00108.31           C
ANISOU 5488  CE  LYS B 335     9402  13399  18352  -2268  -2691  -1385       C
ATOM   5489  NZ  LYS B 335     -85.108  87.841  33.853  1.00111.09           N
ANISOU 5489  NZ  LYS B 335     9503  13882  18825  -2478  -2216  -1328       N
ATOM   5490  N   ASP B 336     -80.476  88.236  39.011  1.00 84.07           N
ANISOU 5490  N   ASP B 336     6956  10468  14519  -1002  -4162   -948       N
ATOM   5491  CA  ASP B 336     -80.461  88.775  40.372  1.00 87.37           C
ANISOU 5491  CA  ASP B 336     7473  11031  14693  -1024  -4698   -875       C
ATOM   5492  C   ASP B 336     -79.282  88.231  41.181  1.00 84.28           C
ANISOU 5492  C   ASP B 336     7521  10650  13852   -921  -4956   -625       C
ATOM   5493  O   ASP B 336     -79.443  87.707  42.285  1.00 85.01           O
ANISOU 5493  O   ASP B 336     7948  10886  13466  -1140  -5232   -652       O
ATOM   5494  CB  ASP B 336     -81.789  88.498  41.084  1.00 90.83           C
ANISOU 5494  CB  ASP B 336     7971  11565  14976  -1395  -4842  -1123       C
ATOM   5495  CG  ASP B 336     -82.970  89.149  40.389  1.00 92.93           C
ANISOU 5495  CG  ASP B 336     7803  11849  15655  -1558  -4636  -1312       C
ATOM   5496  OD1 ASP B 336     -82.747  89.935  39.445  1.00 92.96           O
ANISOU 5496  OD1 ASP B 336     7431  11866  16024  -1384  -4406  -1275       O
ATOM   5497  OD2 ASP B 336     -84.121  88.873  40.786  1.00 94.46           O
ANISOU 5497  OD2 ASP B 336     8040  12061  15789  -1887  -4686  -1524       O
ATOM   5498  N   GLY B 337     -78.083  88.360  40.618  1.00 81.26           N
ANISOU 5498  N   GLY B 337     7150  10140  13584   -624  -4837   -400       N
ATOM   5499  CA  GLY B 337     -76.867  88.018  41.325  1.00 81.58           C
ANISOU 5499  CA  GLY B 337     7585  10186  13225   -546  -5078    -88       C
ATOM   5500  C   GLY B 337     -76.554  86.542  41.431  1.00 76.74           C
ANISOU 5500  C   GLY B 337     7432   9601  12123   -673  -4781   -113       C
ATOM   5501  O   GLY B 337     -75.560  86.185  42.075  1.00 72.56           O
ANISOU 5501  O   GLY B 337     7269   9144  11158   -680  -4903    143       O
ATOM   5502  N   HIS B 338     -77.364  85.673  40.834  1.00 72.93           N
ANISOU 5502  N   HIS B 338     6998   9057  11656   -778  -4296   -402       N
ATOM   5503  CA  HIS B 338     -77.098  84.244  40.810  1.00 70.95           C
ANISOU 5503  CA  HIS B 338     7169   8781  11007   -821  -3871   -481       C
ATOM   5504  C   HIS B 338     -77.304  83.725  39.395  1.00 64.27           C
ANISOU 5504  C   HIS B 338     6214   7705  10500   -712  -3352   -561       C
ATOM   5505  O   HIS B 338     -77.968  84.359  38.572  1.00 62.78           O
ANISOU 5505  O   HIS B 338     5665   7440  10748   -725  -3282   -628       O
ATOM   5506  CB  HIS B 338     -77.999  83.478  41.791  1.00 78.04           C
ANISOU 5506  CB  HIS B 338     8321   9814  11518  -1112  -3910   -802       C
ATOM   5507  CG  HIS B 338     -79.463  83.631  41.517  1.00 84.43           C
ANISOU 5507  CG  HIS B 338     8895  10508  12677  -1286  -3903  -1104       C
ATOM   5508  ND1 HIS B 338     -80.287  84.417  42.294  1.00 90.36           N
ANISOU 5508  ND1 HIS B 338     9473  11409  13449  -1500  -4348  -1232       N
ATOM   5509  CD2 HIS B 338     -80.252  83.099  40.553  1.00 84.35           C
ANISOU 5509  CD2 HIS B 338     8803  10236  13009  -1321  -3541  -1267       C
ATOM   5510  CE1 HIS B 338     -81.519  84.361  41.822  1.00 91.24           C
ANISOU 5510  CE1 HIS B 338     9394  11354  13920  -1666  -4227  -1490       C
ATOM   5511  NE2 HIS B 338     -81.525  83.570  40.765  1.00 87.07           N
ANISOU 5511  NE2 HIS B 338     8932  10563  13587  -1574  -3746  -1488       N
ATOM   5512  N   VAL B 339     -76.732  82.558  39.118  1.00 62.92           N
ANISOU 5512  N   VAL B 339     6345   7461  10101   -641  -2998   -548       N
ATOM   5513  CA  VAL B 339     -76.845  81.966  37.791  1.00 63.73           C
ANISOU 5513  CA  VAL B 339     6401   7353  10459   -560  -2568   -561       C
ATOM   5514  C   VAL B 339     -78.174  81.236  37.672  1.00 65.19           C
ANISOU 5514  C   VAL B 339     6638   7378  10753   -764  -2441   -819       C
ATOM   5515  O   VAL B 339     -78.684  80.659  38.642  1.00 63.53           O
ANISOU 5515  O   VAL B 339     6620   7193  10325   -897  -2549  -1061       O
ATOM   5516  CB  VAL B 339     -75.660  81.023  37.500  1.00 61.68           C
ANISOU 5516  CB  VAL B 339     6401   7058   9977   -390  -2301   -429       C
ATOM   5517  CG1 VAL B 339     -74.344  81.710  37.800  1.00 67.04           C
ANISOU 5517  CG1 VAL B 339     7082   7843  10545   -242  -2494   -162       C
ATOM   5518  CG2 VAL B 339     -75.780  79.732  38.284  1.00 59.16           C
ANISOU 5518  CG2 VAL B 339     6395   6769   9313   -474  -2194   -639       C
ATOM   5519  N   GLU B 340     -78.755  81.284  36.475  1.00 70.81           N
ANISOU 5519  N   GLU B 340     7178   7924  11804   -824  -2225   -778       N
ATOM   5520  CA  GLU B 340     -79.906  80.457  36.130  1.00 74.33           C
ANISOU 5520  CA  GLU B 340     7720   8104  12417  -1023  -2108   -920       C
ATOM   5521  C   GLU B 340     -79.449  79.080  35.658  1.00 66.02           C
ANISOU 5521  C   GLU B 340     6951   6839  11296   -884  -1859   -878       C
ATOM   5522  O   GLU B 340     -79.816  78.057  36.244  1.00 63.72           O
ANISOU 5522  O   GLU B 340     6872   6376  10964   -891  -1875  -1114       O
ATOM   5523  CB  GLU B 340     -80.746  81.145  35.047  1.00 85.41           C
ANISOU 5523  CB  GLU B 340     8825   9458  14170  -1244  -2012   -825       C
ATOM   5524  CG  GLU B 340     -81.643  82.268  35.542  1.00 97.07           C
ANISOU 5524  CG  GLU B 340     9978  11075  15830  -1464  -2266   -967       C
ATOM   5525  CD  GLU B 340     -83.075  81.816  35.750  1.00108.73           C
ANISOU 5525  CD  GLU B 340    11523  12303  17487  -1799  -2353  -1146       C
ATOM   5526  OE1 GLU B 340     -83.467  81.583  36.913  1.00113.76           O
ANISOU 5526  OE1 GLU B 340    12296  12917  18010  -1847  -2607  -1406       O
ATOM   5527  OE2 GLU B 340     -83.808  81.682  34.747  1.00112.98           O
ANISOU 5527  OE2 GLU B 340    11995  12667  18266  -2051  -2177  -1028       O
ATOM   5528  N   THR B 341     -78.642  79.047  34.600  1.00 58.76           N
ANISOU 5528  N   THR B 341     6002   5933  10392   -749  -1643   -626       N
ATOM   5529  CA  THR B 341     -78.076  77.808  34.093  1.00 57.53           C
ANISOU 5529  CA  THR B 341     6068   5607  10184   -600  -1453   -552       C
ATOM   5530  C   THR B 341     -76.694  78.103  33.530  1.00 57.39           C
ANISOU 5530  C   THR B 341     6011   5776  10018   -400  -1311   -339       C
ATOM   5531  O   THR B 341     -76.326  79.258  33.298  1.00 58.43           O
ANISOU 5531  O   THR B 341     5926   6095  10179   -384  -1337   -255       O
ATOM   5532  CB  THR B 341     -78.972  77.170  33.026  1.00 59.10           C
ANISOU 5532  CB  THR B 341     6315   5481  10658   -767  -1374   -437       C
ATOM   5533  OG1 THR B 341     -78.383  75.943  32.577  1.00 60.20           O
ANISOU 5533  OG1 THR B 341     6644   5442  10789   -588  -1269   -359       O
ATOM   5534  CG2 THR B 341     -79.138  78.108  31.841  1.00 56.64           C
ANISOU 5534  CG2 THR B 341     5786   5306  10427   -955  -1252   -195       C
ATOM   5535  N   PHE B 342     -75.927  77.034  33.313  1.00 53.74           N
ANISOU 5535  N   PHE B 342     5728   5237   9452   -239  -1177   -294       N
ATOM   5536  CA  PHE B 342     -74.575  77.163  32.774  1.00 50.27           C
ANISOU 5536  CA  PHE B 342     5279   4936   8884    -71  -1049   -114       C
ATOM   5537  C   PHE B 342     -74.219  75.821  32.134  1.00 53.00           C
ANISOU 5537  C   PHE B 342     5775   5118   9243     22   -908    -56       C
ATOM   5538  O   PHE B 342     -73.773  74.903  32.826  1.00 58.64           O
ANISOU 5538  O   PHE B 342     6605   5824   9852    139   -888   -192       O
ATOM   5539  CB  PHE B 342     -73.583  77.553  33.857  1.00 48.08           C
ANISOU 5539  CB  PHE B 342     5040   4865   8362     38  -1157   -135       C
ATOM   5540  CG  PHE B 342     -72.179  77.723  33.361  1.00 47.26           C
ANISOU 5540  CG  PHE B 342     4934   4839   8183    187  -1066     47       C
ATOM   5541  CD1 PHE B 342     -71.818  78.844  32.634  1.00 49.84           C
ANISOU 5541  CD1 PHE B 342     5059   5208   8670    230  -1075    143       C
ATOM   5542  CD2 PHE B 342     -71.217  76.762  33.625  1.00 46.43           C
ANISOU 5542  CD2 PHE B 342     4993   4766   7884    273   -965     68       C
ATOM   5543  CE1 PHE B 342     -70.523  79.003  32.177  1.00 51.22           C
ANISOU 5543  CE1 PHE B 342     5234   5401   8827    365  -1013    255       C
ATOM   5544  CE2 PHE B 342     -69.922  76.916  33.171  1.00 44.35           C
ANISOU 5544  CE2 PHE B 342     4730   4543   7577    373   -904    232       C
ATOM   5545  CZ  PHE B 342     -69.574  78.037  32.447  1.00 47.73           C
ANISOU 5545  CZ  PHE B 342     4995   4960   8182    424   -942    325       C
ATOM   5546  N   TYR B 343     -74.421  75.724  30.824  1.00 49.19           N
ANISOU 5546  N   TYR B 343     5268   4544   8878    -59   -819    136       N
ATOM   5547  CA  TYR B 343     -74.276  74.463  30.117  1.00 46.23           C
ANISOU 5547  CA  TYR B 343     5023   3970   8573     -1   -784    242       C
ATOM   5548  C   TYR B 343     -73.364  74.624  28.913  1.00 42.85           C
ANISOU 5548  C   TYR B 343     4570   3688   8024      7   -654    462       C
ATOM   5549  O   TYR B 343     -73.221  75.728  28.378  1.00 42.06           O
ANISOU 5549  O   TYR B 343     4334   3793   7855    -94   -562    509       O
ATOM   5550  CB  TYR B 343     -75.644  73.940  29.656  1.00 48.65           C
ANISOU 5550  CB  TYR B 343     5398   3946   9140   -191   -906    314       C
ATOM   5551  CG  TYR B 343     -76.399  74.891  28.754  1.00 46.96           C
ANISOU 5551  CG  TYR B 343     5093   3810   8938   -511   -870    512       C
ATOM   5552  CD1 TYR B 343     -77.219  75.878  29.286  1.00 48.19           C
ANISOU 5552  CD1 TYR B 343     5106   4044   9160   -682   -906    382       C
ATOM   5553  CD2 TYR B 343     -76.300  74.795  27.371  1.00 46.10           C
ANISOU 5553  CD2 TYR B 343     5022   3747   8748   -686   -795    813       C
ATOM   5554  CE1 TYR B 343     -77.916  76.745  28.468  1.00 48.52           C
ANISOU 5554  CE1 TYR B 343     5000   4214   9222  -1012   -828    518       C
ATOM   5555  CE2 TYR B 343     -76.994  75.659  26.545  1.00 48.52           C
ANISOU 5555  CE2 TYR B 343     5221   4215   8999  -1052   -700    958       C
ATOM   5556  CZ  TYR B 343     -77.801  76.632  27.100  1.00 48.66           C
ANISOU 5556  CZ  TYR B 343     5053   4315   9121  -1211   -696    796       C
ATOM   5557  OH  TYR B 343     -78.495  77.497  26.287  1.00 51.87           O
ANISOU 5557  OH  TYR B 343     5289   4937   9483  -1610   -558    897       O
ATOM   5558  N   PRO B 344     -72.730  73.541  28.466  1.00 44.93           N
ANISOU 5558  N   PRO B 344     4927   3863   8281    127   -647    546       N
ATOM   5559  CA  PRO B 344     -71.935  73.616  27.238  1.00 48.07           C
ANISOU 5559  CA  PRO B 344     5321   4405   8540     87   -552    741       C
ATOM   5560  C   PRO B 344     -72.826  73.568  26.009  1.00 58.13           C
ANISOU 5560  C   PRO B 344     6648   5611   9826   -198   -592    991       C
ATOM   5561  O   PRO B 344     -73.841  72.869  25.979  1.00 60.12           O
ANISOU 5561  O   PRO B 344     7003   5564  10276   -294   -765   1098       O
ATOM   5562  CB  PRO B 344     -71.036  72.377  27.325  1.00 42.06           C
ANISOU 5562  CB  PRO B 344     4619   3568   7795    296   -585    732       C
ATOM   5563  CG  PRO B 344     -71.833  71.406  28.119  1.00 38.13           C
ANISOU 5563  CG  PRO B 344     4158   2788   7541    387   -717    586       C
ATOM   5564  CD  PRO B 344     -72.624  72.219  29.114  1.00 39.43           C
ANISOU 5564  CD  PRO B 344     4298   2973   7712    312   -719    402       C
ATOM   5565  N   LYS B 345     -72.444  74.334  24.993  1.00 70.14           N
ANISOU 5565  N   LYS B 345     8102   7415  11134   -366   -436   1072       N
ATOM   5566  CA  LYS B 345     -73.158  74.262  23.731  1.00 79.48           C
ANISOU 5566  CA  LYS B 345     9360   8641  12196   -728   -443   1347       C
ATOM   5567  C   LYS B 345     -72.885  72.931  23.037  1.00 86.51           C
ANISOU 5567  C   LYS B 345    10447   9352  13070   -713   -644   1620       C
ATOM   5568  O   LYS B 345     -71.858  72.278  23.252  1.00 85.30           O
ANISOU 5568  O   LYS B 345    10299   9174  12936   -434   -681   1544       O
ATOM   5569  CB  LYS B 345     -72.765  75.417  22.810  1.00 81.21           C
ANISOU 5569  CB  LYS B 345     9421   9296  12140   -939   -171   1266       C
ATOM   5570  CG  LYS B 345     -73.402  76.748  23.161  1.00 81.66           C
ANISOU 5570  CG  LYS B 345     9224   9528  12277  -1061    -13   1049       C
ATOM   5571  CD  LYS B 345     -73.760  77.514  21.897  1.00 85.09           C
ANISOU 5571  CD  LYS B 345     9525  10356  12448  -1490    238   1065       C
ATOM   5572  CE  LYS B 345     -73.566  79.011  22.067  1.00 83.54           C
ANISOU 5572  CE  LYS B 345     8932  10465  12342  -1443    482    658       C
ATOM   5573  NZ  LYS B 345     -73.852  79.746  20.802  1.00 85.33           N
ANISOU 5573  NZ  LYS B 345     8967  11166  12289  -1880    808    563       N
ATOM   5574  N   LEU B 346     -73.832  72.540  22.182  1.00 91.34           N
ANISOU 5574  N   LEU B 346    11211   9837  13658  -1053   -806   1969       N
ATOM   5575  CA  LEU B 346     -73.722  71.277  21.462  1.00 93.01           C
ANISOU 5575  CA  LEU B 346    11611   9823  13904  -1068  -1110   2305       C
ATOM   5576  C   LEU B 346     -72.534  71.264  20.504  1.00 91.43           C
ANISOU 5576  C   LEU B 346    11419   9990  13331  -1104  -1018   2356       C
ATOM   5577  O   LEU B 346     -71.950  70.199  20.269  1.00 92.45           O
ANISOU 5577  O   LEU B 346    11613   9971  13543   -932  -1255   2482       O
ATOM   5578  CB  LEU B 346     -75.027  70.992  20.709  1.00 98.04           C
ANISOU 5578  CB  LEU B 346    12446  10233  14570  -1509  -1361   2756       C
ATOM   5579  CG  LEU B 346     -75.972  72.158  20.381  1.00100.95           C
ANISOU 5579  CG  LEU B 346    12774  10855  14726  -1989  -1138   2814       C
ATOM   5580  CD1 LEU B 346     -76.696  71.880  19.073  1.00105.49           C
ANISOU 5580  CD1 LEU B 346    13588  11465  15027  -2563  -1324   3365       C
ATOM   5581  CD2 LEU B 346     -76.980  72.400  21.505  1.00102.19           C
ANISOU 5581  CD2 LEU B 346    12856  10683  15287  -1919  -1181   2625       C
ATOM   5582  N   GLN B 347     -72.166  72.427  19.958  1.00 91.54           N
ANISOU 5582  N   GLN B 347    11329  10477  12976  -1318   -686   2206       N
ATOM   5583  CA  GLN B 347     -71.053  72.608  19.010  1.00 93.10           C
ANISOU 5583  CA  GLN B 347    11514  11068  12792  -1399   -549   2148       C
ATOM   5584  C   GLN B 347     -69.946  71.563  19.075  1.00 90.49           C
ANISOU 5584  C   GLN B 347    11224  10605  12554  -1084   -746   2156       C
ATOM   5585  O   GLN B 347     -69.158  71.431  18.142  1.00 91.27           O
ANISOU 5585  O   GLN B 347    11366  10971  12341  -1213   -745   2196       O
ATOM   5586  CB  GLN B 347     -70.416  73.984  19.216  1.00 94.22           C
ANISOU 5586  CB  GLN B 347    11406  11556  12836  -1326   -155   1691       C
ATOM   5587  CG  GLN B 347     -70.834  75.019  18.196  1.00 97.71           C
ANISOU 5587  CG  GLN B 347    11757  12463  12904  -1785    134   1619       C
ATOM   5588  CD  GLN B 347     -70.389  76.413  18.579  1.00 95.05           C
ANISOU 5588  CD  GLN B 347    11089  12357  12667  -1632    472   1104       C
ATOM   5589  OE1 GLN B 347     -70.051  76.673  19.734  1.00 89.17           O
ANISOU 5589  OE1 GLN B 347    10226  11368  12286  -1232    429    906       O
ATOM   5590  NE2 GLN B 347     -70.388  77.320  17.610  1.00 99.15           N
ANISOU 5590  NE2 GLN B 347    11443  13358  12872  -1965    791    872       N
TER    5591      GLN B 347
HETATM 5592  C1  GOL A 401     -76.464  55.270 -16.457  1.00 61.23           C
HETATM 5593  O1  GOL A 401     -77.759  55.671 -16.136  1.00 65.57           O
HETATM 5594  C2  GOL A 401     -75.786  54.839 -15.134  1.00 59.32           C
HETATM 5595  O2  GOL A 401     -76.344  53.679 -14.616  1.00 50.98           O
HETATM 5596  C3  GOL A 401     -74.290  54.664 -15.488  1.00 67.18           C
HETATM 5597  O3  GOL A 401     -73.690  54.042 -14.395  1.00 70.21           O
HETATM 5598  C1  GOL A 402     -61.771  79.796 -25.759  1.00 61.54           C
HETATM 5599  O1  GOL A 402     -62.806  79.016 -26.271  1.00 58.12           O
HETATM 5600  C2  GOL A 402     -60.511  78.899 -25.699  1.00 59.84           C
HETATM 5601  O2  GOL A 402     -60.627  77.897 -24.746  1.00 56.28           O
HETATM 5602  C3  GOL A 402     -59.340  79.865 -25.398  1.00 60.57           C
HETATM 5603  O3  GOL A 402     -58.677  80.082 -26.604  1.00 61.32           O
HETATM 5604 MG    MG A 403     -61.697  34.055 -36.300  1.00 49.76          MG
HETATM 5605  C1  GOL A 404     -48.213  63.901  -9.689  1.00 79.85           C
HETATM 5606  O1  GOL A 404     -49.430  63.731 -10.351  1.00 79.48           O
HETATM 5607  C2  GOL A 404     -48.460  63.619  -8.186  1.00 80.65           C
HETATM 5608  O2  GOL A 404     -48.852  64.761  -7.502  1.00 78.07           O
HETATM 5609  C3  GOL A 404     -49.549  62.521  -8.161  1.00 84.17           C
HETATM 5610  O3  GOL A 404     -49.186  61.571  -9.115  1.00 85.24           O
HETATM 5611  C1  GOL A 405     -63.993  53.903 -28.620  1.00 77.67           C
HETATM 5612  O1  GOL A 405     -64.127  54.547 -29.848  1.00 77.81           O
HETATM 5613  C2  GOL A 405     -62.688  54.427 -27.976  1.00 75.76           C
HETATM 5614  O2  GOL A 405     -62.941  55.229 -26.872  1.00 74.89           O
HETATM 5615  C3  GOL A 405     -61.883  53.156 -27.613  1.00 73.76           C
HETATM 5616  O3  GOL A 405     -60.548  53.543 -27.491  1.00 69.40           O
HETATM 5617  C   ACY A 406     -62.633  47.036 -29.533  1.00 62.72           C
HETATM 5618  O   ACY A 406     -62.576  47.598 -30.618  1.00 62.59           O
HETATM 5619  OXT ACY A 406     -61.660  46.931 -28.701  1.00 61.39           O
HETATM 5620  CH3 ACY A 406     -63.923  46.371 -29.038  1.00 61.36           C
HETATM 5621  C1  GOL B 401     -65.749  69.643  19.263  1.00 65.38           C
HETATM 5622  O1  GOL B 401     -64.967  70.790  19.389  1.00 66.88           O
HETATM 5623  C2  GOL B 401     -65.318  68.684  20.395  1.00 60.28           C
HETATM 5624  O2  GOL B 401     -66.367  68.390  21.256  1.00 53.91           O
HETATM 5625  C3  GOL B 401     -64.780  67.430  19.665  1.00 59.16           C
HETATM 5626  O3  GOL B 401     -64.018  66.712  20.590  1.00 50.58           O
HETATM 5627  C1  GOL B 402     -65.362  57.227  27.149  1.00 81.03           C
HETATM 5628  O1  GOL B 402     -65.863  58.405  27.697  1.00 79.72           O
HETATM 5629  C2  GOL B 402     -65.583  56.106  28.189  1.00 82.30           C
HETATM 5630  O2  GOL B 402     -66.914  55.724  28.263  1.00 81.86           O
HETATM 5631  C3  GOL B 402     -64.667  54.949  27.725  1.00 82.86           C
HETATM 5632  O3  GOL B 402     -63.446  55.520  27.374  1.00 83.39           O
HETATM 5633  C1  GOL B 403     -55.859  70.150   9.926  1.00 75.79           C
HETATM 5634  O1  GOL B 403     -55.415  70.973  10.956  1.00 73.13           O
HETATM 5635  C2  GOL B 403     -55.467  70.829   8.591  1.00 81.11           C
HETATM 5636  O2  GOL B 403     -56.244  70.378   7.536  1.00 80.59           O
HETATM 5637  C3  GOL B 403     -53.966  70.499   8.391  1.00 85.66           C
HETATM 5638  O3  GOL B 403     -53.240  71.576   8.889  1.00 89.22           O
HETATM 5639 CL    CL B 404     -35.685  70.911  27.265  1.00 49.72          CL
HETATM 5640  C1  GOL B 405     -63.306  43.249  15.303  1.00 69.26           C
HETATM 5641  O1  GOL B 405     -62.733  42.216  14.564  1.00 70.29           O
HETATM 5642  C2  GOL B 405     -64.737  43.460  14.752  1.00 69.69           C
HETATM 5643  O2  GOL B 405     -65.150  42.394  13.964  1.00 67.55           O
HETATM 5644  C3  GOL B 405     -64.674  44.791  13.959  1.00 68.65           C
HETATM 5645  O3  GOL B 405     -64.106  45.745  14.801  1.00 67.28           O
HETATM 5646  C1 AGOL B 406     -59.741  78.904  29.278  0.58 60.14           C
HETATM 5647  C1 BGOL B 406     -58.810  79.802  28.330  0.42 63.68           C
HETATM 5648  O1 AGOL B 406     -59.120  78.353  30.386  0.58 54.46           O
HETATM 5649  O1 BGOL B 406     -57.829  79.000  27.747  0.42 64.71           O
HETATM 5650  C2 AGOL B 406     -58.663  79.672  28.493  0.58 63.89           C
HETATM 5651  C2 BGOL B 406     -59.583  80.479  27.175  0.42 63.75           C
HETATM 5652  O2 AGOL B 406     -57.646  78.836  28.051  0.58 65.10           O
HETATM 5653  O2 BGOL B 406     -60.448  79.598  26.542  0.42 61.86           O
HETATM 5654  C3 AGOL B 406     -59.444  80.313  27.331  0.58 63.97           C
HETATM 5655  C3 BGOL B 406     -58.486  81.008  26.222  0.42 64.13           C
HETATM 5656  O3 AGOL B 406     -58.533  81.051  26.592  0.58 64.60           O
HETATM 5657  O3 BGOL B 406     -57.805  82.010  26.911  0.42 63.71           O
HETATM 5658  C   ACY B 407     -45.414  63.623  31.232  1.00 63.74           C
HETATM 5659  O   ACY B 407     -46.151  64.404  30.647  1.00 64.31           O
HETATM 5660  OXT ACY B 407     -44.980  62.512  30.752  1.00 64.45           O
HETATM 5661  CH3 ACY B 407     -44.912  63.900  32.656  1.00 57.87           C
HETATM 5662  C   ACY B 408     -78.256  89.660  36.474  1.00 92.05           C
HETATM 5663  O   ACY B 408     -78.636  89.036  35.493  1.00 94.87           O
HETATM 5664  OXT ACY B 408     -77.800  89.135  37.554  1.00 93.60           O
HETATM 5665  CH3 ACY B 408     -78.285  91.195  36.514  1.00 90.75           C
HETATM 5666  O   HOH A 501     -51.740  73.020  -7.815  1.00 45.47           O
HETATM 5667  O   HOH A 502     -57.515  61.159 -27.418  1.00 32.27           O
HETATM 5668  O   HOH A 503     -34.117  52.820 -39.714  1.00 41.10           O
HETATM 5669  O   HOH A 504     -57.652  65.700 -26.378  1.00 35.23           O
HETATM 5670  O   HOH A 505     -64.714  72.331 -27.762  1.00 37.08           O
HETATM 5671  O   HOH A 506     -40.781  62.925 -28.404  1.00 38.33           O
HETATM 5672  O   HOH A 507     -66.888  61.999 -22.256  1.00 31.32           O
HETATM 5673  O   HOH A 508     -60.391  80.855 -18.558  1.00 52.63           O
HETATM 5674  O   HOH A 509     -57.076  44.826 -20.714  1.00 30.89           O
HETATM 5675  O   HOH A 510     -62.395  57.748 -41.852  1.00 54.85           O
HETATM 5676  O   HOH A 511     -90.085  60.822  -9.423  1.00 40.29           O
HETATM 5677  O   HOH A 512     -50.341  27.553 -27.191  1.00 46.33           O
HETATM 5678  O   HOH A 513     -53.763  44.400 -46.757  1.00 34.81           O
HETATM 5679  O   HOH A 514     -59.403  54.509 -17.725  1.00 34.63           O
HETATM 5680  O   HOH A 515     -46.874  59.758 -18.741  1.00 34.90           O
HETATM 5681  O   HOH A 516     -87.002  60.579  -1.356  1.00 36.13           O
HETATM 5682  O   HOH A 517     -63.295  68.349  -9.645  1.00 39.82           O
HETATM 5683  O   HOH A 518     -50.808  60.849 -10.995  1.00 45.65           O
HETATM 5684  O   HOH A 519     -70.505  63.310 -20.290  1.00 26.51           O
HETATM 5685  O   HOH A 520     -65.449  51.042 -12.073  1.00 37.93           O
HETATM 5686  O   HOH A 521     -50.265  79.602 -27.381  1.00 46.99           O
HETATM 5687  O   HOH A 522     -58.248  52.733 -24.094  1.00 36.54           O
HETATM 5688  O   HOH A 523     -57.678  67.433 -28.682  1.00 30.82           O
HETATM 5689  O   HOH A 524     -51.603  57.656 -34.971  1.00 37.75           O
HETATM 5690  O   HOH A 525     -67.721  52.621  -1.072  1.00 33.14           O
HETATM 5691  O   HOH A 526     -55.963  74.029   1.624  1.00 60.32           O
HETATM 5692  O   HOH A 527     -54.594  28.262 -28.598  1.00 32.32           O
HETATM 5693  O   HOH A 528     -70.356  50.860 -19.627  1.00 49.21           O
HETATM 5694  O   HOH A 529     -54.241  27.782 -38.174  1.00 37.10           O
HETATM 5695  O   HOH A 530     -41.801  53.662 -21.364  1.00 50.20           O
HETATM 5696  O   HOH A 531     -70.200  53.377 -20.296  1.00 48.05           O
HETATM 5697  O   HOH A 532     -31.763  46.556 -33.464  1.00 41.16           O
HETATM 5698  O   HOH A 533     -49.369  31.405 -34.568  1.00 31.00           O
HETATM 5699  O   HOH A 534     -60.204  69.709   2.519  1.00 47.33           O
HETATM 5700  O   HOH A 535     -64.428  51.982  -1.394  1.00 43.18           O
HETATM 5701  O   HOH A 536     -29.660  48.593 -33.193  1.00 48.43           O
HETATM 5702  O   HOH A 537     -63.457  54.223 -36.751  1.00 47.31           O
HETATM 5703  O   HOH A 538     -87.882  54.973  -6.060  1.00 48.11           O
HETATM 5704  O   HOH A 539     -58.168  58.572 -14.365  1.00 69.58           O
HETATM 5705  O   HOH A 540     -56.740  53.212 -26.216  1.00 36.77           O
HETATM 5706  O   HOH A 541     -37.302  50.009 -46.734  1.00 55.23           O
HETATM 5707  O   HOH A 542     -59.663  55.611 -25.874  1.00 39.14           O
HETATM 5708  O   HOH A 543     -54.342  55.513 -18.890  1.00 25.26           O
HETATM 5709  O   HOH A 544     -35.550  50.846 -42.479  1.00 48.51           O
HETATM 5710  O   HOH A 545     -55.587  30.341 -24.619  1.00 32.26           O
HETATM 5711  O   HOH A 546     -84.228  44.442  -4.272  1.00 39.50           O
HETATM 5712  O   HOH A 547     -58.982  52.479 -29.392  1.00 50.26           O
HETATM 5713  O   HOH A 548     -68.063  64.795 -22.294  1.00 30.08           O
HETATM 5714  O   HOH A 549     -38.209  58.840 -40.010  1.00 34.57           O
HETATM 5715  O   HOH A 550     -66.430  76.476  -5.716  1.00 54.04           O
HETATM 5716  O   HOH A 551     -51.813  57.136 -46.694  1.00 54.37           O
HETATM 5717  O   HOH A 552     -72.983  52.701  -1.716  1.00 29.75           O
HETATM 5718  O   HOH A 553     -34.322  55.537 -33.970  1.00 28.35           O
HETATM 5719  O   HOH A 554     -62.817  61.801 -21.296  1.00 35.45           O
HETATM 5720  O   HOH A 555     -64.494  55.772 -32.231  1.00 50.81           O
HETATM 5721  O   HOH A 556     -61.679  47.635 -25.511  1.00 51.03           O
HETATM 5722  O   HOH A 557     -72.675  68.320  -2.421  1.00 37.39           O
HETATM 5723  O   HOH A 558     -45.373  56.381 -43.212  1.00 42.50           O
HETATM 5724  O   HOH A 559     -65.283  47.366 -38.806  1.00 40.44           O
HETATM 5725  O   HOH A 560     -65.518  62.144 -20.027  1.00 27.39           O
HETATM 5726  O   HOH A 561     -61.930  63.864  -1.512  1.00 36.64           O
HETATM 5727  O   HOH A 562     -73.508  67.643 -15.591  1.00 46.89           O
HETATM 5728  O   HOH A 563     -62.581  64.931 -12.516  1.00 25.13           O
HETATM 5729  O   HOH A 564     -71.148  53.991 -11.893  1.00 27.47           O
HETATM 5730  O   HOH A 565     -54.529  52.348 -28.748  1.00 27.24           O
HETATM 5731  O   HOH A 566     -58.501  83.470 -17.605  1.00 57.14           O
HETATM 5732  O   HOH A 567     -81.269  70.062 -19.932  1.00 48.48           O
HETATM 5733  O   HOH A 568     -69.329  71.795  -3.519  1.00 41.53           O
HETATM 5734  O   HOH A 569     -33.607  44.714 -32.257  1.00 43.75           O
HETATM 5735  O   HOH A 570     -33.311  52.117 -33.415  1.00 36.80           O
HETATM 5736  O   HOH A 571     -43.723  43.110 -44.057  1.00 37.02           O
HETATM 5737  O   HOH A 572     -83.955  60.366   1.407  1.00 28.11           O
HETATM 5738  O   HOH A 573     -62.839  55.968  -9.980  1.00 36.74           O
HETATM 5739  O   HOH A 574     -55.397  46.969 -21.310  1.00 38.60           O
HETATM 5740  O   HOH A 575     -71.174  55.436 -16.995  1.00 36.85           O
HETATM 5741  O   HOH A 576     -79.293  47.421  -0.244  1.00 43.45           O
HETATM 5742  O   HOH A 577     -47.683  57.923 -45.365  1.00 52.18           O
HETATM 5743  O   HOH A 578     -64.315  53.952  -8.184  1.00 24.71           O
HETATM 5744  O   HOH A 579     -68.790  70.834 -15.726  1.00 48.63           O
HETATM 5745  O   HOH A 580     -46.325  68.198 -28.872  1.00 42.87           O
HETATM 5746  O   HOH A 581     -77.216  62.555 -15.577  1.00 57.08           O
HETATM 5747  O   HOH A 582     -66.914  63.865 -18.333  1.00 30.03           O
HETATM 5748  O   HOH A 583     -47.394  59.861 -40.916  1.00 50.01           O
HETATM 5749  O   HOH A 584     -43.089  63.397 -39.992  1.00 46.39           O
HETATM 5750  O   HOH A 585     -49.844  60.849 -34.287  1.00 44.40           O
HETATM 5751  O   HOH A 586     -58.196  63.663  -7.017  1.00 45.50           O
HETATM 5752  O   HOH A 587     -41.121  40.905 -43.622  1.00 46.72           O
HETATM 5753  O   HOH A 588     -50.731  56.954 -17.857  1.00 53.79           O
HETATM 5754  O   HOH A 589     -45.018  39.419 -31.554  1.00 41.32           O
HETATM 5755  O   HOH A 590     -53.139  60.590  -9.418  1.00 63.72           O
HETATM 5756  O   HOH A 591     -41.583  37.255 -38.114  1.00 47.71           O
HETATM 5757  O   HOH A 592     -46.814  79.867 -11.080  1.00 57.71           O
HETATM 5758  O   HOH A 593     -58.549  63.324 -26.639  1.00 28.50           O
HETATM 5759  O   HOH A 594     -29.870  42.084 -37.155  1.00 38.59           O
HETATM 5760  O   HOH A 595     -50.091  33.159 -24.232  1.00 54.84           O
HETATM 5761  O   HOH A 596     -56.001  62.022 -15.078  1.00 26.63           O
HETATM 5762  O   HOH A 597     -73.560  70.479 -14.014  1.00 62.08           O
HETATM 5763  O   HOH A 598     -53.276  36.869 -40.821  1.00 44.10           O
HETATM 5764  O   HOH A 599     -44.549  50.764 -22.174  1.00 38.03           O
HETATM 5765  O   HOH A 600     -50.943  48.923 -20.575  1.00 39.22           O
HETATM 5766  O   HOH A 601     -47.087  33.691 -27.798  1.00 52.06           O
HETATM 5767  O   HOH A 602     -54.648  50.667 -35.952  1.00 42.33           O
HETATM 5768  O   HOH A 603     -55.219  40.635 -39.915  1.00 37.55           O
HETATM 5769  O   HOH A 604     -35.927  50.600 -39.965  1.00 47.80           O
HETATM 5770  O   HOH A 605     -62.006  65.975 -10.064  1.00 28.39           O
HETATM 5771  O   HOH A 606     -56.607  54.173 -29.108  1.00 30.95           O
HETATM 5772  O   HOH A 607     -66.901  71.372 -39.595  1.00 49.57           O
HETATM 5773  O   HOH A 608     -52.313  32.747 -40.173  1.00 43.06           O
HETATM 5774  O   HOH A 609     -45.905  33.263 -34.687  1.00 41.48           O
HETATM 5775  O   HOH A 610     -46.223  63.594 -17.973  1.00 46.10           O
HETATM 5776  O   HOH A 611     -57.060  61.076  -9.092  1.00 39.45           O
HETATM 5777  O   HOH A 612     -54.920  60.152 -28.716  1.00 31.97           O
HETATM 5778  O   HOH A 613     -63.466  62.678 -11.696  1.00 29.18           O
HETATM 5779  O   HOH A 614     -84.269  76.691 -10.982  1.00 37.06           O
HETATM 5780  O   HOH A 615     -82.251  43.947  -1.196  1.00 37.04           O
HETATM 5781  O   HOH A 616     -67.712  50.642 -19.835  1.00 42.74           O
HETATM 5782  O   HOH A 617     -45.534  64.279 -20.735  1.00 65.27           O
HETATM 5783  O   HOH A 618     -45.822  66.280 -31.502  1.00 64.25           O
HETATM 5784  O   HOH A 619     -65.005  39.678 -27.612  1.00 51.68           O
HETATM 5785  O   HOH A 620     -32.608  47.535 -24.600  1.00 41.82           O
HETATM 5786  O   HOH A 621     -76.462  65.916  -2.465  1.00 48.41           O
HETATM 5787  O   HOH A 622     -62.888  61.635  -2.893  1.00 45.59           O
HETATM 5788  O   HOH A 623     -73.927  51.411 -15.752  1.00 58.47           O
HETATM 5789  O   HOH A 624     -61.884  58.273 -32.512  1.00 49.74           O
HETATM 5790  O   HOH A 625     -84.838  73.094  -4.553  1.00 49.30           O
HETATM 5791  O   HOH A 626     -64.411  58.236 -20.910  1.00 37.26           O
HETATM 5792  O   HOH A 627     -86.391  50.716 -13.836  1.00 32.39           O
HETATM 5793  O   HOH A 628     -50.657  52.376 -21.928  1.00 35.38           O
HETATM 5794  O   HOH A 629     -60.424  35.099 -25.244  1.00 37.88           O
HETATM 5795  O   HOH A 630     -40.250  58.050 -36.030  1.00 35.94           O
HETATM 5796  O   HOH A 631     -88.767  51.622  -2.972  1.00 38.90           O
HETATM 5797  O   HOH A 632     -52.905  66.008 -34.060  1.00 43.93           O
HETATM 5798  O   HOH A 633     -62.009  57.555 -24.073  1.00 49.83           O
HETATM 5799  O   HOH A 634     -56.060  62.220 -34.555  1.00 42.20           O
HETATM 5800  O   HOH A 635     -47.605  71.067 -31.314  1.00 54.58           O
HETATM 5801  O   HOH A 636     -48.267  40.821 -27.138  1.00 35.33           O
HETATM 5802  O   HOH A 637     -46.357  37.094 -30.454  1.00 39.85           O
HETATM 5803  O   HOH A 638     -43.301  37.869 -40.901  1.00 45.93           O
HETATM 5804  O   HOH A 639     -61.441  49.685 -21.773  1.00 55.25           O
HETATM 5805  O   HOH A 640     -52.605  55.404 -20.776  1.00 28.37           O
HETATM 5806  O   HOH A 641     -66.284  55.442 -23.544  1.00 68.79           O
HETATM 5807  O   HOH A 642     -47.204  73.575 -23.781  1.00 30.44           O
HETATM 5808  O   HOH A 643     -62.651  69.738 -34.176  1.00 43.08           O
HETATM 5809  O   HOH A 644     -70.526  70.455 -18.731  1.00 38.98           O
HETATM 5810  O   HOH A 645     -66.945  37.965 -38.068  1.00 55.07           O
HETATM 5811  O   HOH A 646     -64.506  72.502 -17.571  1.00 65.03           O
HETATM 5812  O   HOH A 647     -47.985  67.589 -30.946  1.00 49.20           O
HETATM 5813  O   HOH A 648     -46.486  38.816 -28.304  1.00 53.90           O
HETATM 5814  O   HOH A 649     -76.473  62.396  -2.261  1.00 48.73           O
HETATM 5815  O   HOH A 650     -49.174  35.712 -23.731  1.00 35.40           O
HETATM 5816  O   HOH A 651     -64.098  41.831 -22.074  1.00 39.19           O
HETATM 5817  O   HOH A 652     -87.162  80.640  -6.295  1.00 56.34           O
HETATM 5818  O   HOH A 653     -46.406  32.656 -32.180  1.00 46.98           O
HETATM 5819  O   HOH A 654     -91.948  49.685  -7.797  1.00 42.13           O
HETATM 5820  O   HOH A 655     -60.497  67.986 -35.105  1.00 52.06           O
HETATM 5821  O   HOH A 656     -55.144  85.010 -21.206  1.00 56.54           O
HETATM 5822  O   HOH A 657     -75.007  50.858  -1.055  1.00 34.57           O
HETATM 5823  O   HOH A 658     -66.669  55.890 -28.463  1.00 57.68           O
HETATM 5824  O   HOH A 659     -42.901  75.780  -6.655  1.00 71.65           O
HETATM 5825  O   HOH A 660     -58.027  55.427 -15.713  1.00 51.34           O
HETATM 5826  O   HOH A 661     -39.594  71.431 -20.216  1.00 54.19           O
HETATM 5827  O   HOH A 662     -54.031  59.913 -47.312  1.00 56.66           O
HETATM 5828  O   HOH A 663     -90.271  66.035 -11.980  1.00 52.80           O
HETATM 5829  O   HOH A 664     -68.448  81.988 -21.150  1.00 63.92           O
HETATM 5830  O   HOH A 665     -60.007  77.546 -33.185  1.00 59.93           O
HETATM 5831  O   HOH A 666     -45.020  72.677 -26.121  1.00 45.84           O
HETATM 5832  O   HOH A 667     -67.734  80.242 -18.962  1.00 43.58           O
HETATM 5833  O   HOH A 668     -79.926  73.606  -6.674  1.00 55.41           O
HETATM 5834  O   HOH A 669     -71.380  68.607 -40.090  1.00 52.64           O
HETATM 5835  O   HOH A 670     -88.225  48.715  -9.977  1.00 42.69           O
HETATM 5836  O   HOH A 671     -64.809  48.307 -16.383  1.00 49.09           O
HETATM 5837  O   HOH A 672     -62.421  58.726 -22.111  1.00 43.25           O
HETATM 5838  O   HOH A 673     -70.429  51.295  -1.912  1.00 36.02           O
HETATM 5839  O   HOH A 674     -43.125  59.142 -19.585  1.00 50.63           O
HETATM 5840  O   HOH A 675     -51.851  37.333 -49.678  1.00 44.22           O
HETATM 5841  O   HOH A 676     -80.815  53.720 -15.731  1.00 40.82           O
HETATM 5842  O   HOH A 677     -56.009  38.843 -42.198  1.00 61.01           O
HETATM 5843  O   HOH A 678     -52.246  60.187 -13.114  1.00 52.38           O
HETATM 5844  O   HOH A 679     -60.570  50.812 -23.967  1.00 47.51           O
HETATM 5845  O   HOH A 680     -57.221  49.357 -28.542  1.00 74.02           O
HETATM 5846  O   HOH A 681     -69.331  54.339 -23.276  1.00 60.77           O
HETATM 5847  O   HOH A 682     -47.137  81.010 -16.337  1.00 44.46           O
HETATM 5848  O   HOH A 683     -54.168  26.517 -26.869  1.00 35.75           O
HETATM 5849  O   HOH A 684     -41.232  34.714 -35.885  1.00 54.15           O
HETATM 5850  O   HOH A 685     -43.888  38.193 -29.218  1.00 52.60           O
HETATM 5851  O   HOH A 686     -91.049  62.586 -11.952  1.00 46.48           O
HETATM 5852  O   HOH B 501     -66.656  60.084  29.084  1.00 36.02           O
HETATM 5853  O   HOH B 502     -53.192  61.460  26.098  1.00 46.98           O
HETATM 5854  O   HOH B 503     -60.939  38.422  15.041  1.00 50.70           O
HETATM 5855  O   HOH B 504     -62.588  56.411  19.941  1.00 50.92           O
HETATM 5856  O   HOH B 505     -58.088  62.148   8.726  1.00 59.54           O
HETATM 5857  O   HOH B 506     -48.634  36.027   1.381  1.00 68.24           O
HETATM 5858  O   HOH B 507     -46.011  72.652  20.844  1.00 31.54           O
HETATM 5859  O   HOH B 508     -62.863  56.138   9.435  1.00 31.29           O
HETATM 5860  O   HOH B 509     -52.136  73.752   9.198  1.00 35.16           O
HETATM 5861  O   HOH B 510     -68.099  53.317  11.942  1.00 36.70           O
HETATM 5862  O   HOH B 511     -88.762  63.108  24.340  1.00 44.77           O
HETATM 5863  O   HOH B 512     -64.804  59.371  17.453  1.00 48.16           O
HETATM 5864  O   HOH B 513     -63.751  47.936  16.638  1.00 39.13           O
HETATM 5865  O   HOH B 514     -85.465  57.038  35.962  1.00 42.80           O
HETATM 5866  O   HOH B 515     -51.498  61.650  28.088  1.00 29.05           O
HETATM 5867  O   HOH B 516     -65.597  48.550  19.737  1.00 43.32           O
HETATM 5868  O   HOH B 517     -64.999  27.084   4.013  1.00 48.41           O
HETATM 5869  O   HOH B 518     -61.742  67.534  34.708  1.00 39.69           O
HETATM 5870  O   HOH B 519     -90.936  64.075  28.295  1.00 28.18           O
HETATM 5871  O   HOH B 520     -66.480  60.955  23.611  1.00 37.74           O
HETATM 5872  O   HOH B 521     -63.826  59.509  25.435  1.00 77.41           O
HETATM 5873  O   HOH B 522     -48.580  74.147   5.622  1.00 55.06           O
HETATM 5874  O   HOH B 523     -52.704  66.599  32.794  1.00 51.48           O
HETATM 5875  O   HOH B 524     -51.319  45.768  15.531  1.00 31.25           O
HETATM 5876  O   HOH B 525     -64.944  47.748  11.638  1.00 31.77           O
HETATM 5877  O   HOH B 526     -39.926  69.058  26.225  1.00 33.21           O
HETATM 5878  O   HOH B 527     -46.863  40.407  18.944  1.00 51.30           O
HETATM 5879  O   HOH B 528     -66.328  50.966   0.843  1.00 28.40           O
HETATM 5880  O   HOH B 529     -50.894  55.972   8.971  1.00 26.24           O
HETATM 5881  O   HOH B 530     -63.741  64.676  18.465  1.00 31.82           O
HETATM 5882  O   HOH B 531     -55.443  48.654  19.838  1.00 44.55           O
HETATM 5883  O   HOH B 532     -68.383  61.512  51.635  1.00 47.07           O
HETATM 5884  O   HOH B 533     -38.200  59.275  18.218  1.00 33.56           O
HETATM 5885  O   HOH B 534     -47.547  78.844  12.269  1.00 43.26           O
HETATM 5886  O   HOH B 535     -66.931  64.499  28.466  1.00 28.73           O
HETATM 5887  O   HOH B 536     -60.500  53.893  24.444  1.00 54.56           O
HETATM 5888  O   HOH B 537     -71.069  39.205  -0.073  1.00 37.17           O
HETATM 5889  O   HOH B 538     -62.151  67.072  46.562  1.00 59.67           O
HETATM 5890  O   HOH B 539     -69.643  73.682  22.695  1.00 49.34           O
HETATM 5891  O   HOH B 540     -64.863  55.457  36.260  1.00 39.56           O
HETATM 5892  O   HOH B 541     -51.253  73.051  27.886  1.00 33.84           O
HETATM 5893  O   HOH B 542     -56.086  60.857   6.575  1.00 32.12           O
HETATM 5894  O   HOH B 543     -58.089  62.111  26.886  1.00 40.15           O
HETATM 5895  O   HOH B 544     -46.564  67.613   7.654  1.00 28.65           O
HETATM 5896  O   HOH B 545     -48.562  38.055  19.500  1.00 45.73           O
HETATM 5897  O   HOH B 546     -35.502  63.151  27.490  1.00 34.84           O
HETATM 5898  O   HOH B 547     -76.444  75.389  43.550  1.00 41.07           O
HETATM 5899  O   HOH B 548     -66.153  45.925   1.301  1.00 23.78           O
HETATM 5900  O   HOH B 549     -46.516  54.561  26.918  1.00 31.77           O
HETATM 5901  O   HOH B 550     -55.754  57.299   1.019  1.00 37.92           O
HETATM 5902  O   HOH B 551     -43.255  67.928  30.491  1.00 44.67           O
HETATM 5903  O   HOH B 552     -56.787  53.293  19.404  1.00 34.01           O
HETATM 5904  O   HOH B 553     -50.645  46.825   1.943  1.00 40.30           O
HETATM 5905  O   HOH B 554     -54.435  56.655  11.917  1.00 22.16           O
HETATM 5906  O   HOH B 555     -54.150  51.164  21.830  1.00 20.64           O
HETATM 5907  O   HOH B 556     -87.591  60.152  39.989  1.00 59.11           O
HETATM 5908  O   HOH B 557     -58.435  69.141  33.893  1.00 42.28           O
HETATM 5909  O   HOH B 558     -52.654  43.242   2.175  1.00 53.42           O
HETATM 5910  O   HOH B 559     -71.087  57.515  25.052  1.00 52.59           O
HETATM 5911  O   HOH B 560     -57.450  63.049  14.562  1.00 26.73           O
HETATM 5912  O   HOH B 561     -39.907  56.745  25.222  1.00 57.06           O
HETATM 5913  O   HOH B 562     -74.109  34.454   3.724  1.00 39.44           O
HETATM 5914  O   HOH B 563     -46.658  54.518  17.251  1.00 48.52           O
HETATM 5915  O   HOH B 564     -83.842  58.390  25.005  1.00 32.71           O
HETATM 5916  O   HOH B 565     -34.347  65.964  19.691  1.00 37.86           O
HETATM 5917  O   HOH B 566     -67.649  32.603  13.332  1.00 28.53           O
HETATM 5918  O   HOH B 567     -47.218  50.345   3.086  1.00 47.31           O
HETATM 5919  O   HOH B 568     -53.526  57.363   9.560  1.00 30.95           O
HETATM 5920  O   HOH B 569     -56.626  52.112  21.645  1.00 25.28           O
HETATM 5921  O   HOH B 570     -49.922  77.667  27.510  1.00 41.91           O
HETATM 5922  O   HOH B 571     -59.386  71.336  40.593  1.00 52.66           O
HETATM 5923  O   HOH B 572     -62.837  79.622  40.945  1.00 46.75           O
HETATM 5924  O   HOH B 573     -59.156  64.216  28.334  1.00 25.59           O
HETATM 5925  O   HOH B 574     -61.413  56.971  23.775  1.00 50.21           O
HETATM 5926  O   HOH B 575     -41.092  59.244  24.366  1.00 39.46           O
HETATM 5927  O   HOH B 576     -70.153  50.323  15.491  1.00 42.40           O
HETATM 5928  O   HOH B 577     -47.134  74.133  24.766  1.00 41.44           O
HETATM 5929  O   HOH B 578     -46.033  72.143  23.243  1.00 27.68           O
HETATM 5930  O   HOH B 579     -55.781  60.652  26.097  1.00 25.22           O
HETATM 5931  O   HOH B 580     -87.857  69.375  34.140  1.00 34.95           O
HETATM 5932  O   HOH B 581     -57.459  32.368   0.806  1.00 34.27           O
HETATM 5933  O   HOH B 582     -43.849  37.824  18.412  1.00 50.22           O
HETATM 5934  O   HOH B 583     -55.053  52.048  17.927  1.00 22.72           O
HETATM 5935  O   HOH B 584     -35.208  58.331  17.959  1.00 46.32           O
HETATM 5936  O   HOH B 585     -67.937  43.253   0.610  1.00 45.08           O
HETATM 5937  O   HOH B 586     -65.068  62.585  28.792  1.00 35.15           O
HETATM 5938  O   HOH B 587     -67.409  29.927   2.480  1.00 48.40           O
HETATM 5939  O   HOH B 588     -67.035  54.627   0.954  1.00 46.22           O
HETATM 5940  O   HOH B 589     -93.906  66.001  38.000  1.00 48.44           O
HETATM 5941  O   HOH B 590     -56.524  55.717  11.225  1.00 37.83           O
HETATM 5942  O   HOH B 591     -51.744  70.952  30.516  1.00 38.80           O
HETATM 5943  O   HOH B 592     -84.630  73.394  37.468  1.00 55.15           O
HETATM 5944  O   HOH B 593     -63.890  54.808  30.987  1.00 58.83           O
HETATM 5945  O   HOH B 594     -48.252  50.442  14.971  1.00 53.98           O
HETATM 5946  O   HOH B 595     -59.493  62.269  11.289  1.00 61.79           O
HETATM 5947  O   HOH B 596     -57.320  56.128  20.610  1.00 31.26           O
HETATM 5948  O   HOH B 597     -53.408  79.391  27.215  1.00 49.83           O
HETATM 5949  O   HOH B 598     -67.137  46.722  18.488  1.00 60.59           O
HETATM 5950  O   HOH B 599     -48.673  48.805  17.987  1.00 35.36           O
HETATM 5951  O   HOH B 600     -50.721  58.733  34.087  1.00 41.82           O
HETATM 5952  O   HOH B 601     -48.007  71.787  30.411  1.00 53.78           O
HETATM 5953  O   HOH B 602     -81.628  67.090  49.371  1.00 42.95           O
HETATM 5954  O   HOH B 603     -47.094  52.408  38.925  1.00 39.07           O
HETATM 5955  O   HOH B 604     -58.644  68.674  10.788  1.00 48.71           O
HETATM 5956  O   HOH B 605     -72.342  63.596  20.686  1.00 32.17           O
HETATM 5957  O   HOH B 606     -68.483  64.384  35.477  1.00 39.37           O
HETATM 5958  O   HOH B 607     -62.719  68.757  17.422  1.00 43.11           O
HETATM 5959  O   HOH B 608     -42.207  34.535  10.577  1.00 51.17           O
HETATM 5960  O   HOH B 609     -83.783  51.331  30.520  1.00 57.14           O
HETATM 5961  O   HOH B 610     -48.724  45.985  13.419  1.00 48.07           O
HETATM 5962  O   HOH B 611     -45.650  35.095   4.192  1.00 41.18           O
HETATM 5963  O   HOH B 612     -64.658  72.060  51.869  1.00 55.78           O
HETATM 5964  O   HOH B 613     -65.186  54.391   8.208  1.00 34.22           O
HETATM 5965  O   HOH B 614     -38.315  52.123  18.116  1.00 49.16           O
HETATM 5966  O   HOH B 615     -61.230  22.579  15.177  1.00 38.08           O
HETATM 5967  O   HOH B 616     -60.507  54.327  20.479  1.00 43.96           O
HETATM 5968  O   HOH B 617     -80.025  73.917  31.059  1.00 39.27           O
HETATM 5969  O   HOH B 618     -78.393  70.576  26.725  1.00 53.12           O
HETATM 5970  O   HOH B 619     -70.135  54.801  15.669  1.00 36.98           O
HETATM 5971  O   HOH B 620     -69.404  58.099  28.752  1.00 57.76           O
HETATM 5972  O   HOH B 621     -36.038  60.728  16.799  1.00 31.07           O
HETATM 5973  O   HOH B 622     -68.111  50.007  19.421  1.00 54.35           O
HETATM 5974  O   HOH B 623     -40.721  67.119  30.046  1.00 48.94           O
HETATM 5975  O   HOH B 624     -82.177  65.246  40.544  1.00 49.41           O
HETATM 5976  O   HOH B 625     -68.705  26.993   7.587  1.00 48.82           O
HETATM 5977  O   HOH B 626     -44.033  32.980  11.340  1.00 56.35           O
HETATM 5978  O   HOH B 627     -45.036  63.024  -2.291  1.00 43.44           O
HETATM 5979  O   HOH B 628     -69.463  57.315  21.022  1.00 74.25           O
HETATM 5980  O   HOH B 629     -48.942  57.320  33.454  1.00 61.79           O
HETATM 5981  O   HOH B 630     -58.863  80.199  20.370  1.00 56.42           O
HETATM 5982  O   HOH B 631     -40.289  72.881   9.618  1.00 49.50           O
HETATM 5983  O   HOH B 632     -49.851  80.394  18.304  1.00 42.37           O
HETATM 5984  O   HOH B 633     -51.665  29.096  11.072  1.00 50.44           O
HETATM 5985  O   HOH B 634     -59.332  65.000  47.047  1.00 52.93           O
HETATM 5986  O   HOH B 635     -58.102  56.215   2.222  1.00 48.17           O
HETATM 5987  O   HOH B 636     -57.384  53.272  35.232  1.00 40.88           O
HETATM 5988  O   HOH B 637     -63.355  53.207  23.427  1.00 52.47           O
HETATM 5989  O   HOH B 638     -57.121  24.119  10.852  1.00 42.85           O
HETATM 5990  O   HOH B 639     -69.707  30.747   9.675  1.00 34.37           O
HETATM 5991  O   HOH B 640     -54.787  73.342  13.020  1.00 53.68           O
HETATM 5992  O   HOH B 641     -70.054  61.264  28.109  1.00 53.52           O
HETATM 5993  O   HOH B 642     -45.106  39.781   6.631  1.00 50.33           O
HETATM 5994  O   HOH B 643     -46.890  47.335   7.631  1.00 46.36           O
HETATM 5995  O   HOH B 644     -37.412  56.601  20.845  1.00 53.60           O
HETATM 5996  O   HOH B 645     -56.113  74.867  39.434  1.00 56.01           O
HETATM 5997  O   HOH B 646     -67.417  48.421   1.511  1.00 37.64           O
HETATM 5998  O   HOH B 647     -71.905  87.133  24.830  1.00 57.50           O
HETATM 5999  O   HOH B 648     -77.264  54.629  21.195  1.00 38.63           O
HETATM 6000  O   HOH B 649     -36.657  62.781  29.992  1.00 46.76           O
HETATM 6001  O   HOH B 650     -64.394  38.100  15.526  1.00 43.97           O
HETATM 6002  O   HOH B 651     -52.665  72.879  31.283  1.00 38.01           O
HETATM 6003  O   HOH B 652     -55.685  70.691  34.227  1.00 57.26           O
HETATM 6004  O   HOH B 653     -61.026  56.137  39.128  1.00 54.46           O
HETATM 6005  O   HOH B 654     -50.888  28.228   8.696  1.00 52.73           O
HETATM 6006  O   HOH B 655     -37.973  73.520  11.726  1.00 42.37           O
HETATM 6007  O   HOH B 656     -59.491  67.363  12.729  1.00 50.09           O
HETATM 6008  O   HOH B 657     -38.455  51.617  15.484  1.00 76.60           O
HETATM 6009  O   HOH B 658     -39.449  69.298  28.538  1.00 31.13           O
HETATM 6010  O   HOH B 659     -62.500  77.745  43.333  1.00 52.93           O
HETATM 6011  O   HOH B 660     -47.474  48.348   9.891  1.00 45.05           O
ENDMDL
MODEL        3
ATOM      1  N   ALA A   0    -100.122  25.595  -0.250  1.00 84.12           N
ANISOU    1  N   ALA A   0     8694  10754  12515   1463  -1341   1365       N
ATOM      2  CA  ALA A   0     -99.608  25.024  -1.490  1.00 81.50           C
ANISOU    2  CA  ALA A   0     8258  10390  12318   1359  -1177   1154       C
ATOM      3  C   ALA A   0     -98.580  25.951  -2.131  1.00 74.88           C
ANISOU    3  C   ALA A   0     7619   9375  11458   1204  -1039   1038       C
ATOM      4  O   ALA A   0     -97.775  25.523  -2.957  1.00 72.79           O
ANISOU    4  O   ALA A   0     7302   9114  11240   1065   -950    871       O
ATOM      5  CB  ALA A   0    -100.748  24.741  -2.460  1.00 83.08           C
ANISOU    5  CB  ALA A   0     8369  10457  12741   1531   -997   1138       C
ATOM      6  N  AMET A   1     -98.633  27.226  -1.747  0.57 71.75           N
ANISOU    6  N  AMET A   1     7448   8820  10992   1231  -1018   1135       N
ATOM      7  N  BMET A   1     -98.596  27.222  -1.748  0.43 71.64           N
ANISOU    7  N  BMET A   1     7434   8809  10975   1225  -1020   1131       N
ATOM      8  CA AMET A   1     -97.673  28.205  -2.237  0.57 67.18           C
ANISOU    8  CA AMET A   1     7045   8092  10387   1096   -911   1033       C
ATOM      9  CA BMET A   1     -97.674  28.184  -2.334  0.43 67.02           C
ANISOU    9  CA BMET A   1     7022   8065  10378   1095   -898   1022       C
ATOM     10  C  AMET A   1     -96.319  27.968  -1.584  0.57 62.96           C
ANISOU   10  C  AMET A   1     6486   7726   9709    911  -1070    970       C
ATOM     11  C  BMET A   1     -96.333  28.147  -1.611  0.43 62.70           C
ANISOU   11  C  BMET A   1     6482   7665   9678    916  -1055    976       C
ATOM     12  O  AMET A   1     -96.239  27.711  -0.377  0.57 64.38           O
ANISOU   12  O  AMET A   1     6635   8088   9737    884  -1271   1070       O
ATOM     13  O  BMET A   1     -96.278  28.233  -0.379  0.43 63.70           O
ANISOU   13  O  BMET A   1     6646   7926   9631    893  -1225   1087       O
ATOM     14  CB AMET A   1     -98.167  29.624  -1.947  0.57 67.02           C
ANISOU   14  CB AMET A   1     7261   7862  10342   1163   -836   1150       C
ATOM     15  CB BMET A   1     -98.266  29.590  -2.285  0.43 66.82           C
ANISOU   15  CB BMET A   1     7228   7802  10359   1172   -784   1117       C
ATOM     16  CG AMET A   1     -98.786  29.810  -0.560  0.57 68.96           C
ANISOU   16  CG AMET A   1     7559   8181  10461   1259  -1003   1383       C
ATOM     17  CG BMET A   1     -99.032  29.970  -3.533  0.43 65.28           C
ANISOU   17  CG BMET A   1     7090   7386  10327   1240   -538   1032       C
ATOM     18  SD AMET A   1     -97.623  30.247   0.754  0.57 64.50           S
ANISOU   18  SD AMET A   1     7104   7780   9622   1078  -1195   1439       S
ATOM     19  SD BMET A   1     -98.106  29.631  -5.042  0.43 58.41           S
ANISOU   19  SD BMET A   1     6162   6504   9527   1091   -393    787       S
ATOM     20  CE AMET A   1     -97.630  32.036   0.651  0.57 60.65           C
ANISOU   20  CE AMET A   1     6946   7016   9082   1023   -980   1440       C
ATOM     21  CE BMET A   1     -96.605  30.558  -4.741  0.43 54.39           C
ANISOU   21  CE BMET A   1     5805   6003   8857    907   -451    723       C
ATOM     22  N   SER A   2     -95.256  28.031  -2.384  1.00 52.97           N
ANISOU   22  N   SER A   2     5276   6416   8436    758   -956    779       N
ATOM     23  CA  SER A   2     -93.917  27.868  -1.839  1.00 42.55           C
ANISOU   23  CA  SER A   2     4011   5218   6938    558  -1026    660       C
ATOM     24  C   SER A   2     -92.891  28.329  -2.859  1.00 34.48           C
ANISOU   24  C   SER A   2     3104   4069   5928    449   -862    500       C
ATOM     25  O   SER A   2     -93.134  28.291  -4.067  1.00 32.94           O
ANISOU   25  O   SER A   2     2886   3765   5865    489   -728    456       O
ATOM     26  CB  SER A   2     -93.642  26.414  -1.444  1.00 44.73           C
ANISOU   26  CB  SER A   2     4069   5715   7212    476  -1165    610       C
ATOM     27  OG  SER A   2     -92.979  25.709  -2.480  1.00 39.74           O
ANISOU   27  OG  SER A   2     3364   5048   6686    379  -1050    455       O
ATOM     28  N   LEU A   3     -91.736  28.754  -2.348  1.00 30.26           N
ANISOU   28  N   LEU A   3     2691   3558   5249    314   -874    416       N
ATOM     29  CA  LEU A   3     -90.646  29.170  -3.222  1.00 29.43           C
ANISOU   29  CA  LEU A   3     2674   3351   5157    230   -749    290       C
ATOM     30  C   LEU A   3     -90.133  28.004  -4.056  1.00 28.78           C
ANISOU   30  C   LEU A   3     2481   3284   5170    169   -711    205       C
ATOM     31  O   LEU A   3     -89.911  28.146  -5.264  1.00 28.45           O
ANISOU   31  O   LEU A   3     2470   3143   5196    172   -595    170       O
ATOM     32  CB  LEU A   3     -89.515  29.773  -2.389  1.00 35.11           C
ANISOU   32  CB  LEU A   3     3513   4092   5735    121   -761    219       C
ATOM     33  CG  LEU A   3     -88.174  29.980  -3.092  1.00 33.17           C
ANISOU   33  CG  LEU A   3     3320   3764   5518     49   -664    102       C
ATOM     34  CD1 LEU A   3     -88.281  31.047  -4.167  1.00 34.73           C
ANISOU   34  CD1 LEU A   3     3585   3849   5763    106   -566    118       C
ATOM     35  CD2 LEU A   3     -87.090  30.332  -2.087  1.00 27.98           C
ANISOU   35  CD2 LEU A   3     2742   3136   4755    -46   -665     14       C
ATOM     36  N   GLU A   4     -89.943  26.841  -3.429  1.00 27.95           N
ANISOU   36  N   GLU A   4     2252   3311   5055     92   -806    169       N
ATOM     37  CA  GLU A   4     -89.423  25.686  -4.151  1.00 25.41           C
ANISOU   37  CA  GLU A   4     1832   2995   4829     -1   -749     80       C
ATOM     38  C   GLU A   4     -90.411  25.183  -5.195  1.00 24.88           C
ANISOU   38  C   GLU A   4     1634   2908   4911     88   -673    122       C
ATOM     39  O   GLU A   4     -89.999  24.632  -6.222  1.00 28.97           O
ANISOU   39  O   GLU A   4     2137   3369   5501     24   -554     64       O
ATOM     40  CB  GLU A   4     -89.068  24.568  -3.169  1.00 31.88           C
ANISOU   40  CB  GLU A   4     2535   3976   5602   -139   -864      7       C
ATOM     41  CG  GLU A   4     -87.845  24.847  -2.296  1.00 39.35           C
ANISOU   41  CG  GLU A   4     3622   4916   6415   -275   -877    -99       C
ATOM     42  CD  GLU A   4     -88.103  25.877  -1.206  1.00 48.87           C
ANISOU   42  CD  GLU A   4     4932   6177   7459   -229   -961    -38       C
ATOM     43  OE1 GLU A   4     -89.263  26.317  -1.052  1.00 50.66           O
ANISOU   43  OE1 GLU A   4     5127   6444   7676    -92  -1028    106       O
ATOM     44  OE2 GLU A   4     -87.141  26.249  -0.500  1.00 50.35           O
ANISOU   44  OE2 GLU A   4     5243   6352   7537   -331   -938   -136       O
ATOM     45  N   ASN A   5     -91.711  25.359  -4.954  1.00 27.17           N
ANISOU   45  N   ASN A   5     1837   3234   5253    238   -721    228       N
ATOM     46  CA  ASN A   5     -92.699  24.957  -5.948  1.00 29.85           C
ANISOU   46  CA  ASN A   5     2052   3531   5759    341   -610    249       C
ATOM     47  C   ASN A   5     -92.703  25.911  -7.135  1.00 29.00           C
ANISOU   47  C   ASN A   5     2115   3247   5657    369   -435    223       C
ATOM     48  O   ASN A   5     -92.865  25.481  -8.282  1.00 36.57           O
ANISOU   48  O   ASN A   5     3034   4161   6698    353   -288    169       O
ATOM     49  CB  ASN A   5     -94.086  24.879  -5.311  1.00 35.87           C
ANISOU   49  CB  ASN A   5     2673   4355   6602    521   -702    380       C
ATOM     50  CG  ASN A   5     -95.188  24.696  -6.332  1.00 42.39           C
ANISOU   50  CG  ASN A   5     3442   5094   7571    645   -529    383       C
ATOM     51  OD1 ASN A   5     -95.990  25.600  -6.565  1.00 47.47           O
ANISOU   51  OD1 ASN A   5     4196   5594   8246    773   -446    441       O
ATOM     52  ND2 ASN A   5     -95.228  23.524  -6.956  1.00 40.36           N
ANISOU   52  ND2 ASN A   5     3014   4914   7407    589   -455    304       N
ATOM     53  N   VAL A   6     -92.526  27.208  -6.879  1.00 26.57           N
ANISOU   53  N   VAL A   6     1993   2854   5247    391   -444    252       N
ATOM     54  CA  VAL A   6     -92.445  28.172  -7.973  1.00 24.01           C
ANISOU   54  CA  VAL A   6     1822   2400   4900    382   -302    209       C
ATOM     55  C   VAL A   6     -91.250  27.862  -8.861  1.00 25.80           C
ANISOU   55  C   VAL A   6     2101   2628   5075    253   -244    133       C
ATOM     56  O   VAL A   6     -91.343  27.906 -10.095  1.00 31.46           O
ANISOU   56  O   VAL A   6     2860   3296   5799    228   -115     94       O
ATOM     57  CB  VAL A   6     -92.381  29.607  -7.417  1.00 26.04           C
ANISOU   57  CB  VAL A   6     2240   2594   5059    396   -331    242       C
ATOM     58  CG1 VAL A   6     -92.080  30.594  -8.533  1.00 27.19           C
ANISOU   58  CG1 VAL A   6     2521   2654   5157    341   -215    174       C
ATOM     59  CG2 VAL A   6     -93.685  29.968  -6.723  1.00 23.40           C
ANISOU   59  CG2 VAL A   6     1895   2211   4786    532   -351    347       C
ATOM     60  N   ALA A   7     -90.110  27.534  -8.250  1.00 22.11           N
ANISOU   60  N   ALA A   7     1645   2207   4550    166   -328    114       N
ATOM     61  CA  ALA A   7     -88.926  27.199  -9.030  1.00 22.85           C
ANISOU   61  CA  ALA A   7     1800   2267   4616     65   -271     75       C
ATOM     62  C   ALA A   7     -89.113  25.900  -9.800  1.00 29.32           C
ANISOU   62  C   ALA A   7     2516   3106   5519      7   -179     50       C
ATOM     63  O   ALA A   7     -88.573  25.754 -10.903  1.00 30.49           O
ANISOU   63  O   ALA A   7     2742   3204   5640    -55    -78     47       O
ATOM     64  CB  ALA A   7     -87.705  27.115  -8.116  1.00 24.32           C
ANISOU   64  CB  ALA A   7     2026   2458   4758     -4   -350     47       C
ATOM     65  N   PHE A   8     -89.869  24.952  -9.242  1.00 30.37           N
ANISOU   65  N   PHE A   8     2466   3326   5748     21   -214     40       N
ATOM     66  CA  PHE A   8     -90.174  23.725  -9.969  1.00 28.94           C
ANISOU   66  CA  PHE A   8     2147   3180   5670    -40   -103      2       C
ATOM     67  C   PHE A   8     -90.915  24.033 -11.263  1.00 27.85           C
ANISOU   67  C   PHE A   8     2046   2982   5552     10     65     -2       C
ATOM     68  O   PHE A   8     -90.592  23.488 -12.325  1.00 27.71           O
ANISOU   68  O   PHE A   8     2061   2942   5526    -88    208    -32       O
ATOM     69  CB  PHE A   8     -90.996  22.783  -9.087  1.00 26.57           C
ANISOU   69  CB  PHE A   8     1595   3020   5482     -9   -194     -2       C
ATOM     70  CG  PHE A   8     -91.457  21.535  -9.794  1.00 37.77           C
ANISOU   70  CG  PHE A   8     2817   4496   7039    -66    -67    -54       C
ATOM     71  CD1 PHE A   8     -90.694  20.381  -9.760  1.00 39.06           C
ANISOU   71  CD1 PHE A   8     2900   4712   7229   -252    -44   -126       C
ATOM     72  CD2 PHE A   8     -92.656  21.515 -10.489  1.00 40.93           C
ANISOU   72  CD2 PHE A   8     3110   4886   7555     55     58    -48       C
ATOM     73  CE1 PHE A   8     -91.115  19.234 -10.408  1.00 38.02           C
ANISOU   73  CE1 PHE A   8     2573   4642   7230   -328     94   -183       C
ATOM     74  CE2 PHE A   8     -93.079  20.374 -11.143  1.00 41.01           C
ANISOU   74  CE2 PHE A   8     2921   4958   7705     -1    203   -112       C
ATOM     75  CZ  PHE A   8     -92.309  19.231 -11.099  1.00 40.28           C
ANISOU   75  CZ  PHE A   8     2735   4938   7630   -198    218   -176       C
ATOM     76  N   ASN A   9     -91.922  24.905 -11.189  1.00 29.15           N
ANISOU   76  N   ASN A   9     2228   3113   5737    146     69     22       N
ATOM     77  CA  ASN A   9     -92.708  25.231 -12.374  1.00 31.72           C
ANISOU   77  CA  ASN A   9     2599   3371   6082    178    253    -20       C
ATOM     78  C   ASN A   9     -91.860  25.937 -13.422  1.00 27.90           C
ANISOU   78  C   ASN A   9     2335   2842   5426     73    319    -39       C
ATOM     79  O   ASN A   9     -92.030  25.705 -14.624  1.00 33.74           O
ANISOU   79  O   ASN A   9     3119   3572   6128      6    486    -89       O
ATOM     80  CB  ASN A   9     -93.907  26.096 -11.986  1.00 31.80           C
ANISOU   80  CB  ASN A   9     2610   3312   6161    338    254      5       C
ATOM     81  CG  ASN A   9     -95.010  25.301 -11.317  1.00 31.70           C
ANISOU   81  CG  ASN A   9     2356   3343   6346    481    230     46       C
ATOM     82  OD1 ASN A   9     -95.978  24.902 -11.962  1.00 34.08           O
ANISOU   82  OD1 ASN A   9     2549   3607   6794    555    396      2       O
ATOM     83  ND2 ASN A   9     -94.870  25.068 -10.017  1.00 34.15           N
ANISOU   83  ND2 ASN A   9     2572   3743   6658    521     25    130       N
ATOM     84  N   VAL A  10     -90.940  26.797 -12.987  1.00 23.18           N
ANISOU   84  N   VAL A  10     1863   2230   4713     56    189      3       N
ATOM     85  CA  VAL A  10     -90.124  27.544 -13.937  1.00 27.76           C
ANISOU   85  CA  VAL A  10     2618   2796   5132    -21    212     10       C
ATOM     86  C   VAL A  10     -89.206  26.606 -14.709  1.00 30.23           C
ANISOU   86  C   VAL A  10     2965   3122   5400   -132    272     38       C
ATOM     87  O   VAL A  10     -89.071  26.716 -15.933  1.00 34.51           O
ANISOU   87  O   VAL A  10     3615   3675   5822   -205    371     40       O
ATOM     88  CB  VAL A  10     -89.334  28.646 -13.209  1.00 28.33           C
ANISOU   88  CB  VAL A  10     2771   2861   5133      5     62     48       C
ATOM     89  CG1 VAL A  10     -88.361  29.318 -14.163  1.00 30.18           C
ANISOU   89  CG1 VAL A  10     3138   3112   5217    -58     50     79       C
ATOM     90  CG2 VAL A  10     -90.287  29.670 -12.612  1.00 26.78           C
ANISOU   90  CG2 VAL A  10     2580   2636   4960     84     42     26       C
ATOM     91  N   VAL A  11     -88.574  25.658 -14.015  1.00 32.63           N
ANISOU   91  N   VAL A  11     3190   3422   5785   -165    222     58       N
ATOM     92  CA  VAL A  11     -87.608  24.792 -14.681  1.00 35.02           C
ANISOU   92  CA  VAL A  11     3554   3694   6058   -282    294     98       C
ATOM     93  C   VAL A  11     -88.302  23.744 -15.544  1.00 41.84           C
ANISOU   93  C   VAL A  11     4345   4588   6966   -364    482     52       C
ATOM     94  O   VAL A  11     -87.717  23.257 -16.517  1.00 45.71           O
ANISOU   94  O   VAL A  11     4939   5053   7375   -476    594     96       O
ATOM     95  CB  VAL A  11     -86.668  24.136 -13.654  1.00 36.03           C
ANISOU   95  CB  VAL A  11     3640   3780   6268   -322    212    104       C
ATOM     96  CG1 VAL A  11     -85.950  25.196 -12.836  1.00 36.54           C
ANISOU   96  CG1 VAL A  11     3779   3814   6292   -244     66    130       C
ATOM     97  CG2 VAL A  11     -87.433  23.194 -12.747  1.00 42.72           C
ANISOU   97  CG2 VAL A  11     4276   4701   7254   -336    195     25       C
ATOM     98  N   ASN A  12     -89.544  23.384 -15.223  1.00 26.45           N
ANISOU   98  N   ASN A  12     2214   2689   5145   -306    530    -24       N
ATOM     99  CA  ASN A  12     -90.251  22.353 -15.971  1.00 35.54           C
ANISOU   99  CA  ASN A  12     3249   3877   6376   -374    730    -89       C
ATOM    100  C   ASN A  12     -91.254  22.906 -16.972  1.00 36.46           C
ANISOU  100  C   ASN A  12     3418   3993   6443   -338    892   -150       C
ATOM    101  O   ASN A  12     -91.463  22.290 -18.022  1.00 39.47           O
ANISOU  101  O   ASN A  12     3812   4391   6792   -443   1102   -198       O
ATOM    102  CB  ASN A  12     -90.979  21.401 -15.015  1.00 42.27           C
ANISOU  102  CB  ASN A  12     3814   4803   7443   -330    697   -140       C
ATOM    103  CG  ASN A  12     -90.026  20.572 -14.179  1.00 48.37           C
ANISOU  103  CG  ASN A  12     4524   5596   8257   -437    590   -130       C
ATOM    104  OD1 ASN A  12     -89.443  19.600 -14.660  1.00 52.49           O
ANISOU  104  OD1 ASN A  12     5044   6105   8793   -601    708   -148       O
ATOM    105  ND2 ASN A  12     -89.873  20.945 -12.915  1.00 50.76           N
ANISOU  105  ND2 ASN A  12     4789   5926   8573   -364    384   -112       N
ATOM    106  N   LYS A  13     -91.880  24.045 -16.678  1.00 34.55           N
ANISOU  106  N   LYS A  13     3217   3721   6189   -213    825   -165       N
ATOM    107  CA  LYS A  13     -92.911  24.605 -17.540  1.00 33.39           C
ANISOU  107  CA  LYS A  13     3125   3545   6016   -189    999   -259       C
ATOM    108  C   LYS A  13     -92.550  25.965 -18.118  1.00 32.36           C
ANISOU  108  C   LYS A  13     3231   3400   5663   -232    956   -257       C
ATOM    109  O   LYS A  13     -93.371  26.554 -18.830  1.00 36.03           O
ANISOU  109  O   LYS A  13     3770   3837   6081   -244   1102   -362       O
ATOM    110  CB  LYS A  13     -94.238  24.716 -16.775  1.00 31.68           C
ANISOU  110  CB  LYS A  13     2737   3281   6021     -7   1010   -299       C
ATOM    111  CG  LYS A  13     -94.826  23.381 -16.349  1.00 38.11           C
ANISOU  111  CG  LYS A  13     3264   4147   7069     50   1064   -312       C
ATOM    112  CD  LYS A  13     -95.279  22.567 -17.550  1.00 44.29           C
ANISOU  112  CD  LYS A  13     3992   4949   7887    -42   1353   -423       C
ATOM    113  CE  LYS A  13     -95.958  21.275 -17.123  1.00 50.29           C
ANISOU  113  CE  LYS A  13     4413   5781   8916     24   1414   -450       C
ATOM    114  NZ  LYS A  13     -96.485  20.511 -18.288  1.00 51.04           N
ANISOU  114  NZ  LYS A  13     4434   5892   9067    -64   1738   -579       N
ATOM    115  N   GLY A  14     -91.351  26.478 -17.848  1.00 33.40           N
ANISOU  115  N   GLY A  14     3470   3553   5667   -262    770   -156       N
ATOM    116  CA  GLY A  14     -90.965  27.793 -18.312  1.00 30.51           C
ANISOU  116  CA  GLY A  14     3278   3211   5106   -299    696   -149       C
ATOM    117  C   GLY A  14     -91.603  28.947 -17.576  1.00 31.15           C
ANISOU  117  C   GLY A  14     3352   3242   5242   -205    623   -195       C
ATOM    118  O   GLY A  14     -91.173  30.091 -17.764  1.00 27.14           O
ANISOU  118  O   GLY A  14     2953   2768   4591   -245    532   -192       O
ATOM    119  N   HIS A  15     -92.607  28.689 -16.748  1.00 32.39           N
ANISOU  119  N   HIS A  15     3378   3324   5603    -84    658   -225       N
ATOM    120  CA  HIS A  15     -93.288  29.698 -15.945  1.00 30.53           C
ANISOU  120  CA  HIS A  15     3151   3010   5439     12    606   -239       C
ATOM    121  C   HIS A  15     -94.128  28.948 -14.919  1.00 30.80           C
ANISOU  121  C   HIS A  15     3007   2992   5703    165    599   -198       C
ATOM    122  O   HIS A  15     -94.156  27.714 -14.899  1.00 34.54           O
ANISOU  122  O   HIS A  15     3336   3514   6275    179    629   -183       O
ATOM    123  CB  HIS A  15     -94.152  30.621 -16.806  1.00 30.97           C
ANISOU  123  CB  HIS A  15     3330   3003   5435    -41    770   -371       C
ATOM    124  CG  HIS A  15     -95.405  29.974 -17.307  1.00 32.88           C
ANISOU  124  CG  HIS A  15     3509   3159   5825      8   1008   -471       C
ATOM    125  ND1 HIS A  15     -95.404  28.768 -17.975  1.00 33.27           N
ANISOU  125  ND1 HIS A  15     3477   3266   5898    -30   1134   -496       N
ATOM    126  CD2 HIS A  15     -96.700  30.363 -17.234  1.00 29.40           C
ANISOU  126  CD2 HIS A  15     3070   2563   5539     99   1166   -555       C
ATOM    127  CE1 HIS A  15     -96.644  28.443 -18.293  1.00 35.39           C
ANISOU  127  CE1 HIS A  15     3676   3436   6333     41   1361   -603       C
ATOM    128  NE2 HIS A  15     -97.450  29.394 -17.855  1.00 35.91           N
ANISOU  128  NE2 HIS A  15     3796   3359   6489    132   1384   -636       N
ATOM    129  N   PHE A  16     -94.821  29.697 -14.068  1.00 30.88           N
ANISOU  129  N   PHE A  16     3024   2915   5796    274    555   -170       N
ATOM    130  CA  PHE A  16     -95.713  29.067 -13.105  1.00 33.38           C
ANISOU  130  CA  PHE A  16     3173   3195   6317    442    526    -96       C
ATOM    131  C   PHE A  16     -96.945  28.534 -13.825  1.00 40.24           C
ANISOU  131  C   PHE A  16     3952   3980   7356    523    751   -173       C
ATOM    132  O   PHE A  16     -97.680  29.297 -14.461  1.00 47.25           O
ANISOU  132  O   PHE A  16     4960   4734   8258    522    924   -268       O
ATOM    133  CB  PHE A  16     -96.116  30.049 -12.009  1.00 29.40           C
ANISOU  133  CB  PHE A  16     2731   2606   5834    536    426    -12       C
ATOM    134  CG  PHE A  16     -96.923  29.419 -10.909  1.00 29.87           C
ANISOU  134  CG  PHE A  16     2625   2660   6064    718    342    114       C
ATOM    135  CD1 PHE A  16     -96.297  28.734  -9.879  1.00 27.72           C
ANISOU  135  CD1 PHE A  16     2237   2537   5759    720    135    206       C
ATOM    136  CD2 PHE A  16     -98.306  29.498 -10.911  1.00 32.94           C
ANISOU  136  CD2 PHE A  16     2972   2898   6645    886    468    140       C
ATOM    137  CE1 PHE A  16     -97.035  28.147  -8.867  1.00 32.02           C
ANISOU  137  CE1 PHE A  16     2625   3130   6412    868     23    331       C
ATOM    138  CE2 PHE A  16     -99.051  28.912  -9.902  1.00 36.71           C
ANISOU  138  CE2 PHE A  16     3333   3441   7176   1024    348    284       C
ATOM    139  CZ  PHE A  16     -98.413  28.236  -8.878  1.00 39.33           C
ANISOU  139  CZ  PHE A  16     3548   3960   7434   1012    117    380       C
ATOM    140  N   ASP A  17     -97.167  27.223 -13.728  1.00 35.96           N
ANISOU  140  N   ASP A  17     3191   3516   6956    580    765   -153       N
ATOM    141  CA  ASP A  17     -98.300  26.573 -14.371  1.00 33.43           C
ANISOU  141  CA  ASP A  17     2732   3133   6836    672    994   -232       C
ATOM    142  C   ASP A  17     -99.199  25.860 -13.368  1.00 37.00           C
ANISOU  142  C   ASP A  17     2952   3610   7496    873    898   -114       C
ATOM    143  O   ASP A  17    -100.111  25.131 -13.776  1.00 40.64           O
ANISOU  143  O   ASP A  17     3289   4069   8082    939   1037   -155       O
ATOM    144  CB  ASP A  17     -97.808  25.585 -15.435  1.00 43.04           C
ANISOU  144  CB  ASP A  17     3897   4458   7998    515   1137   -332       C
ATOM    145  CG  ASP A  17     -98.862  25.280 -16.481  1.00 56.60           C
ANISOU  145  CG  ASP A  17     5566   6092   9849    544   1456   -479       C
ATOM    146  OD1 ASP A  17     -99.787  26.102 -16.651  1.00 63.42           O
ANISOU  146  OD1 ASP A  17     6522   6785  10790    639   1591   -539       O
ATOM    147  OD2 ASP A  17     -98.770  24.214 -17.127  1.00 61.43           O
ANISOU  147  OD2 ASP A  17     6050   6794  10496    462   1596   -546       O
ATOM    148  N   GLY A  18     -98.967  26.049 -12.072  1.00 35.84           N
ANISOU  148  N   GLY A  18     2802   3528   7287    928    637     37       N
ATOM    149  CA  GLY A  18     -99.785  25.404 -11.064  1.00 34.96           C
ANISOU  149  CA  GLY A  18     2542   3505   7238   1073    494    167       C
ATOM    150  C   GLY A  18     -99.504  23.933 -10.862  1.00 35.96           C
ANISOU  150  C   GLY A  18     2418   3845   7401   1031    408    163       C
ATOM    151  O   GLY A  18    -100.393  23.195 -10.428  1.00 46.31           O
ANISOU  151  O   GLY A  18     3552   5239   8805   1160    362    223       O
ATOM    152  N   GLN A  19     -98.290  23.484 -11.160  1.00 37.43           N
ANISOU  152  N   GLN A  19     2580   4121   7519    850    388     92       N
ATOM    153  CA  GLN A  19     -97.931  22.079 -11.046  1.00 39.71           C
ANISOU  153  CA  GLN A  19     2651   4600   7838    758    337     61       C
ATOM    154  C   GLN A  19     -97.316  21.787  -9.683  1.00 42.17           C
ANISOU  154  C   GLN A  19     2911   5075   8038    718     55    147       C
ATOM    155  O   GLN A  19     -96.699  22.654  -9.057  1.00 46.46           O
ANISOU  155  O   GLN A  19     3614   5580   8460    695    -73    200       O
ATOM    156  CB  GLN A  19     -96.951  21.683 -12.152  1.00 41.04           C
ANISOU  156  CB  GLN A  19     2837   4761   7995    554    506    -66       C
ATOM    157  CG  GLN A  19     -97.391  22.081 -13.553  1.00 46.18           C
ANISOU  157  CG  GLN A  19     3576   5270   8699    551    807   -175       C
ATOM    158  CD  GLN A  19     -98.625  21.332 -14.018  1.00 52.43           C
ANISOU  158  CD  GLN A  19     4214   6069   9637    645    974   -228       C
ATOM    159  OE1 GLN A  19     -98.883  20.207 -13.589  1.00 56.41           O
ANISOU  159  OE1 GLN A  19     4498   6724  10210    657    900   -209       O
ATOM    160  NE2 GLN A  19     -99.396  21.956 -14.902  1.00 55.19           N
ANISOU  160  NE2 GLN A  19     4675   6263  10033    704   1208   -311       N
ATOM    161  N   GLN A  20     -97.492  20.550  -9.228  1.00 44.50           N
ANISOU  161  N   GLN A  20     2974   5568   8367    695    -31    144       N
ATOM    162  CA  GLN A  20     -96.897  20.105  -7.976  1.00 46.28           C
ANISOU  162  CA  GLN A  20     3128   5983   8472    616   -279    186       C
ATOM    163  C   GLN A  20     -95.448  19.688  -8.189  1.00 43.02           C
ANISOU  163  C   GLN A  20     2761   5592   7994    361   -268     78       C
ATOM    164  O   GLN A  20     -95.081  19.150  -9.237  1.00 46.09           O
ANISOU  164  O   GLN A  20     3125   5933   8453    240    -81    -22       O
ATOM    165  CB  GLN A  20     -97.682  18.933  -7.388  1.00 54.62           C
ANISOU  165  CB  GLN A  20     3895   7276   9582    680   -382    214       C
ATOM    166  CG  GLN A  20     -99.020  19.303  -6.779  1.00 70.11           C
ANISOU  166  CG  GLN A  20     5804   9249  11584    948   -467    359       C
ATOM    167  CD  GLN A  20     -99.730  18.100  -6.189  1.00 89.11           C
ANISOU  167  CD  GLN A  20     7888  11928  14040   1019   -592    386       C
ATOM    168  OE1 GLN A  20     -99.498  16.964  -6.603  1.00 92.82           O
ANISOU  168  OE1 GLN A  20     8153  12544  14571    886   -531    276       O
ATOM    169  NE2 GLN A  20    -100.596  18.343  -5.212  1.00 98.18           N
ANISOU  169  NE2 GLN A  20     8989  13155  15160   1225   -770    537       N
ATOM    170  N   GLY A  21     -94.629  19.929  -7.181  1.00 36.47           N
ANISOU  170  N   GLY A  21     2007   4823   7026    274   -452     96       N
ATOM    171  CA  GLY A  21     -93.225  19.565  -7.211  1.00 33.55           C
ANISOU  171  CA  GLY A  21     1701   4447   6598     36   -448     -8       C
ATOM    172  C   GLY A  21     -92.371  20.636  -6.562  1.00 40.06           C
ANISOU  172  C   GLY A  21     2734   5188   7301     10   -556     17       C
ATOM    173  O   GLY A  21     -92.765  21.794  -6.426  1.00 41.41           O
ANISOU  173  O   GLY A  21     3030   5266   7440    158   -583    107       O
ATOM    174  N   GLU A  22     -91.171  20.236  -6.146  1.00 39.34           N
ANISOU  174  N   GLU A  22     2684   5119   7145   -193   -600    -75       N
ATOM    175  CA  GLU A  22     -90.227  21.142  -5.511  1.00 39.83           C
ANISOU  175  CA  GLU A  22     2975   5101   7056   -236   -667    -82       C
ATOM    176  C   GLU A  22     -88.819  20.835  -5.996  1.00 42.20           C
ANISOU  176  C   GLU A  22     3426   5273   7336   -422   -542   -189       C
ATOM    177  O   GLU A  22     -88.455  19.669  -6.170  1.00 44.84           O
ANISOU  177  O   GLU A  22     3649   5648   7742   -590   -487   -281       O
ATOM    178  CB  GLU A  22     -90.275  21.036  -3.979  1.00 46.88           C
ANISOU  178  CB  GLU A  22     3804   6180   7829   -275   -888    -79       C
ATOM    179  CG  GLU A  22     -91.493  21.676  -3.331  1.00 58.49           C
ANISOU  179  CG  GLU A  22     5217   7736   9272    -67  -1030     82       C
ATOM    180  CD  GLU A  22     -92.700  20.760  -3.309  1.00 70.41           C
ANISOU  180  CD  GLU A  22     6501   9416  10835     34  -1065    142       C
ATOM    181  OE1 GLU A  22     -92.548  19.563  -3.634  1.00 74.79           O
ANISOU  181  OE1 GLU A  22     6896  10072  11448    -92  -1016     42       O
ATOM    182  OE2 GLU A  22     -93.802  21.237  -2.965  1.00 75.02           O
ANISOU  182  OE2 GLU A  22     7068  10024  11411    238  -1130    289       O
ATOM    183  N   VAL A  23     -88.035  21.887  -6.213  1.00 41.19           N
ANISOU  183  N   VAL A  23     3542   4985   7125   -389   -492   -169       N
ATOM    184  CA  VAL A  23     -86.616  21.752  -6.536  1.00 40.99           C
ANISOU  184  CA  VAL A  23     3678   4809   7088   -520   -390   -236       C
ATOM    185  C   VAL A  23     -85.823  22.533  -5.495  1.00 34.45           C
ANISOU  185  C   VAL A  23     2989   3951   6149   -528   -466   -273       C
ATOM    186  O   VAL A  23     -86.335  23.518  -4.944  1.00 31.70           O
ANISOU  186  O   VAL A  23     2674   3653   5719   -410   -555   -213       O
ATOM    187  CB  VAL A  23     -86.311  22.235  -7.964  1.00 25.43           C
ANISOU  187  CB  VAL A  23     1848   2678   5137   -463   -241   -166       C
ATOM    188  CG1 VAL A  23     -87.117  21.440  -8.981  1.00 26.40           C
ANISOU  188  CG1 VAL A  23     1843   2838   5349   -478   -130   -152       C
ATOM    189  CG2 VAL A  23     -86.598  23.714  -8.100  1.00 23.75           C
ANISOU  189  CG2 VAL A  23     1751   2429   4846   -301   -277    -85       C
ATOM    190  N   PRO A  24     -84.593  22.130  -5.176  1.00 34.92           N
ANISOU  190  N   PRO A  24     3139   3916   6212   -671   -409   -378       N
ATOM    191  CA  PRO A  24     -83.826  22.860  -4.158  1.00 30.62           C
ANISOU  191  CA  PRO A  24     2720   3338   5574   -682   -445   -442       C
ATOM    192  C   PRO A  24     -83.400  24.231  -4.659  1.00 32.21           C
ANISOU  192  C   PRO A  24     3072   3405   5762   -526   -396   -355       C
ATOM    193  O   PRO A  24     -82.965  24.390  -5.803  1.00 26.60           O
ANISOU  193  O   PRO A  24     2430   2557   5121   -473   -301   -285       O
ATOM    194  CB  PRO A  24     -82.618  21.951  -3.902  1.00 33.62           C
ANISOU  194  CB  PRO A  24     3159   3605   6011   -878   -345   -593       C
ATOM    195  CG  PRO A  24     -82.482  21.146  -5.151  1.00 36.51           C
ANISOU  195  CG  PRO A  24     3509   3859   6507   -921   -220   -549       C
ATOM    196  CD  PRO A  24     -83.877  20.938  -5.663  1.00 32.88           C
ANISOU  196  CD  PRO A  24     2873   3565   6055   -845   -286   -457       C
ATOM    197  N   VAL A  25     -83.518  25.225  -3.782  1.00 31.92           N
ANISOU  197  N   VAL A  25     3080   3426   5622   -466   -464   -357       N
ATOM    198  CA  VAL A  25     -83.284  26.621  -4.130  1.00 27.47           C
ANISOU  198  CA  VAL A  25     2614   2784   5041   -331   -434   -286       C
ATOM    199  C   VAL A  25     -82.331  27.239  -3.117  1.00 28.15           C
ANISOU  199  C   VAL A  25     2788   2832   5076   -364   -403   -387       C
ATOM    200  O   VAL A  25     -82.451  27.000  -1.910  1.00 29.96           O
ANISOU  200  O   VAL A  25     3011   3170   5202   -461   -454   -478       O
ATOM    201  CB  VAL A  25     -84.607  27.415  -4.182  1.00 29.34           C
ANISOU  201  CB  VAL A  25     2811   3122   5216   -220   -510   -181       C
ATOM    202  CG1 VAL A  25     -84.339  28.894  -4.409  1.00 30.15           C
ANISOU  202  CG1 VAL A  25     3002   3163   5290   -128   -476   -142       C
ATOM    203  CG2 VAL A  25     -85.512  26.865  -5.268  1.00 25.68           C
ANISOU  203  CG2 VAL A  25     2263   2669   4824   -176   -496   -106       C
ATOM    204  N   SER A  26     -81.382  28.029  -3.611  1.00 29.62           N
ANISOU  204  N   SER A  26     3047   2878   5329   -283   -318   -372       N
ATOM    205  CA  SER A  26     -80.529  28.861  -2.776  1.00 30.37           C
ANISOU  205  CA  SER A  26     3202   2930   5405   -275   -259   -462       C
ATOM    206  C   SER A  26     -80.650  30.308  -3.233  1.00 31.62           C
ANISOU  206  C   SER A  26     3357   3099   5559   -141   -264   -372       C
ATOM    207  O   SER A  26     -80.642  30.592  -4.435  1.00 33.24           O
ANISOU  207  O   SER A  26     3547   3259   5826    -51   -270   -263       O
ATOM    208  CB  SER A  26     -79.068  28.408  -2.835  1.00 34.36           C
ANISOU  208  CB  SER A  26     3770   3239   6046   -301   -127   -553       C
ATOM    209  OG  SER A  26     -78.540  28.552  -4.141  1.00 44.33           O
ANISOU  209  OG  SER A  26     5043   4365   7435   -182    -91   -424       O
ATOM    210  N   ILE A  27     -80.773  31.219  -2.275  1.00 27.57           N
ANISOU  210  N   ILE A  27     2860   2660   4954   -152   -257   -425       N
ATOM    211  CA  ILE A  27     -80.939  32.639  -2.556  1.00 25.53           C
ANISOU  211  CA  ILE A  27     2584   2430   4686    -66   -250   -368       C
ATOM    212  C   ILE A  27     -79.725  33.378  -2.018  1.00 30.84           C
ANISOU  212  C   ILE A  27     3257   3041   5420    -45   -136   -472       C
ATOM    213  O   ILE A  27     -79.424  33.301  -0.820  1.00 37.01           O
ANISOU  213  O   ILE A  27     4084   3844   6133   -135    -71   -601       O
ATOM    214  CB  ILE A  27     -82.234  33.197  -1.948  1.00 27.57           C
ANISOU  214  CB  ILE A  27     2859   2815   4800    -98   -310   -323       C
ATOM    215  CG1 ILE A  27     -83.449  32.654  -2.703  1.00 22.55           C
ANISOU  215  CG1 ILE A  27     2197   2211   4161    -68   -397   -208       C
ATOM    216  CG2 ILE A  27     -82.217  34.719  -1.964  1.00 24.70           C
ANISOU  216  CG2 ILE A  27     2489   2470   4427    -64   -259   -315       C
ATOM    217  CD1 ILE A  27     -84.761  33.232  -2.238  1.00 27.68           C
ANISOU  217  CD1 ILE A  27     2872   2935   4711    -63   -441   -133       C
ATOM    218  N  AILE A  28     -79.055  34.118  -2.897  0.52 31.75           N
ANISOU  218  N  AILE A  28     3311   3098   5655     71   -112   -418       N
ATOM    219  N  BILE A  28     -79.005  34.061  -2.902  0.48 31.95           N
ANISOU  219  N  BILE A  28     3338   3116   5686     72   -109   -420       N
ATOM    220  CA AILE A  28     -77.894  34.920  -2.532  0.52 34.28           C
ANISOU  220  CA AILE A  28     3581   3361   6082    133      0   -500       C
ATOM    221  CA BILE A  28     -77.827  34.817  -2.500  0.48 34.33           C
ANISOU  221  CA BILE A  28     3594   3357   6095    131      6   -507       C
ATOM    222  C  AILE A  28     -77.721  36.001  -3.592  0.52 34.71           C
ANISOU  222  C  AILE A  28     3523   3455   6210    254    -48   -393       C
ATOM    223  C  BILE A  28     -77.732  36.042  -3.395  0.48 34.81           C
ANISOU  223  C  BILE A  28     3540   3472   6213    241    -34   -414       C
ATOM    224  O  AILE A  28     -77.968  35.771  -4.779  0.52 34.83           O
ANISOU  224  O  AILE A  28     3528   3473   6233    305   -144   -262       O
ATOM    225  O  BILE A  28     -78.136  36.013  -4.561  0.48 33.58           O
ANISOU  225  O  BILE A  28     3363   3344   6050    286   -138   -283       O
ATOM    226  CB AILE A  28     -76.631  34.036  -2.387  0.52 36.24           C
ANISOU  226  CB AILE A  28     3866   3425   6480    160    104   -578       C
ATOM    227  CB BILE A  28     -76.543  33.951  -2.548  0.48 36.20           C
ANISOU  227  CB BILE A  28     3860   3400   6495    175    101   -562       C
ATOM    228  CG1AILE A  28     -75.428  34.866  -1.934  0.52 36.66           C
ANISOU  228  CG1AILE A  28     3852   3398   6677    249    251   -677       C
ATOM    229  CG1BILE A  28     -75.364  34.693  -1.915  0.48 36.80           C
ANISOU  229  CG1BILE A  28     3884   3396   6702    244    258   -684       C
ATOM    230  CG2AILE A  28     -76.328  33.305  -3.687  0.52 36.41           C
ANISOU  230  CG2AILE A  28     3894   3334   6607    245     48   -432       C
ATOM    231  CG2BILE A  28     -76.218  33.531  -3.967  0.48 36.80           C
ANISOU  231  CG2BILE A  28     3919   3381   6680    287     37   -396       C
ATOM    232  CD1AILE A  28     -74.163  34.055  -1.752  0.52 39.24           C
ANISOU  232  CD1AILE A  28     4232   3493   7184    288    393   -766       C
ATOM    233  CD1BILE A  28     -74.099  33.871  -1.843  0.48 39.25           C
ANISOU  233  CD1BILE A  28     4245   3467   7200    290    393   -758       C
ATOM    234  N  AASN A  29     -77.327  37.197  -3.145  0.52 37.36           N
ANISOU  234  N  AASN A  29     3768   3847   6581    277     22   -460       N
ATOM    235  N  BASN A  29     -77.209  37.124  -2.830  0.48 38.03           N
ANISOU  235  N  BASN A  29     3866   3917   6666    262     55   -498       N
ATOM    236  CA AASN A  29     -76.982  38.312  -4.035  0.52 40.71           C
ANISOU  236  CA AASN A  29     4039   4341   7089    380    -25   -387       C
ATOM    237  CA BASN A  29     -77.278  38.462  -3.436  0.48 39.75           C
ANISOU  237  CA BASN A  29     3945   4246   6911    315     16   -447       C
ATOM    238  C  AASN A  29     -78.173  38.762  -4.882  0.52 37.52           C
ANISOU  238  C  AASN A  29     3635   4065   6556    323   -150   -293       C
ATOM    239  C  BASN A  29     -78.765  38.752  -3.664  0.48 37.64           C
ANISOU  239  C  BASN A  29     3736   4092   6472    207    -71   -392       C
ATOM    240  O  AASN A  29     -78.032  39.038  -6.075  0.52 32.27           O
ANISOU  240  O  AASN A  29     2896   3448   5916    391   -249   -188       O
ATOM    241  O  BASN A  29     -79.589  38.485  -2.776  0.48 35.29           O
ANISOU  241  O  BASN A  29     3549   3814   6047     99    -45   -432       O
ATOM    242  CB AASN A  29     -75.794  37.956  -4.936  0.52 43.88           C
ANISOU  242  CB AASN A  29     4374   4629   7668    552    -51   -288       C
ATOM    243  CB BASN A  29     -76.405  38.526  -4.677  0.48 42.49           C
ANISOU  243  CB BASN A  29     4182   4554   7407    478    -57   -326       C
ATOM    244  CG AASN A  29     -74.611  37.411  -4.161  0.52 47.27           C
ANISOU  244  CG AASN A  29     4828   4872   8260    614    105   -390       C
ATOM    245  CG BASN A  29     -75.065  37.839  -4.484  0.48 45.73           C
ANISOU  245  CG BASN A  29     4597   4774   8005    598     39   -348       C
ATOM    246  OD1AASN A  29     -74.045  36.376  -4.519  0.52 47.98           O
ANISOU  246  OD1AASN A  29     4999   4791   8439    669    120   -336       O
ATOM    247  OD1BASN A  29     -74.725  36.903  -5.209  0.48 47.37           O
ANISOU  247  OD1BASN A  29     4872   4861   8266    662     -6   -239       O
ATOM    248  ND2AASN A  29     -74.229  38.105  -3.096  0.52 48.16           N
ANISOU  248  ND2AASN A  29     4882   5003   8414    590    249   -552       N
ATOM    249  ND2BASN A  29     -74.298  38.299  -3.502  0.48 47.79           N
ANISOU  249  ND2BASN A  29     4798   4990   8372    620    198   -496       N
ATOM    250  N  AASN A  30     -79.352  38.846  -4.261  0.52 34.88           N
ANISOU  250  N  AASN A  30     3393   3783   6078    195   -138   -330       N
ATOM    251  N  BASN A  30     -79.143  39.288  -4.821  0.48 34.58           N
ANISOU  251  N  BASN A  30     3284   3778   6076    233   -169   -300       N
ATOM    252  CA AASN A  30     -80.586  39.260  -4.938  0.52 31.35           C
ANISOU  252  CA AASN A  30     2972   3412   5527    132   -211   -267       C
ATOM    253  CA BASN A  30     -80.543  39.421  -5.214  0.48 31.93           C
ANISOU  253  CA BASN A  30     3022   3500   5608    142   -227   -255       C
ATOM    254  C  AASN A  30     -80.865  38.409  -6.177  0.52 26.23           C
ANISOU  254  C  AASN A  30     2359   2737   4868    175   -310   -160       C
ATOM    255  C  BASN A  30     -80.913  38.389  -6.267  0.48 26.49           C
ANISOU  255  C  BASN A  30     2394   2771   4898    175   -316   -154       C
ATOM    256  O  AASN A  30     -81.455  38.879  -7.153  0.52 25.30           O
ANISOU  256  O  AASN A  30     2228   2688   4699    150   -366   -117       O
ATOM    257  O  BASN A  30     -81.623  38.702  -7.227  0.48 25.51           O
ANISOU  257  O  BASN A  30     2274   2705   4714    145   -371   -107       O
ATOM    258  CB AASN A  30     -80.548  40.750  -5.300  0.52 34.68           C
ANISOU  258  CB AASN A  30     3268   3947   5961    102   -205   -296       C
ATOM    259  CB BASN A  30     -80.818  40.831  -5.731  0.48 34.57           C
ANISOU  259  CB BASN A  30     3255   3955   5927     92   -240   -271       C
ATOM    260  CG AASN A  30     -81.864  41.452  -5.022  0.52 35.76           C
ANISOU  260  CG AASN A  30     3479   4122   5984    -34   -170   -320       C
ATOM    261  CG BASN A  30     -81.865  41.565  -4.915  0.48 35.84           C
ANISOU  261  CG BASN A  30     3487   4137   5994    -44   -158   -330       C
ATOM    262  OD1AASN A  30     -82.698  40.957  -4.264  0.52 35.06           O
ANISOU  262  OD1AASN A  30     3528   3976   5815    -83   -137   -309       O
ATOM    263  OD1BASN A  30     -82.687  40.951  -4.234  0.48 35.08           O
ANISOU  263  OD1BASN A  30     3532   3978   5818    -83   -135   -310       O
ATOM    264  ND2AASN A  30     -82.054  42.616  -5.632  0.52 37.61           N
ANISOU  264  ND2AASN A  30     3620   4453   6216    -99   -177   -348       N
ATOM    265  ND2BASN A  30     -81.844  42.891  -4.988  0.48 37.92           N
ANISOU  265  ND2BASN A  30     3645   4494   6269   -118   -116   -391       N
ATOM    266  N   THR A  31     -80.437  37.151  -6.132  1.00 27.41           N
ANISOU  266  N   THR A  31     2564   2789   5061    216   -311   -135       N
ATOM    267  CA  THR A  31     -80.575  36.185  -7.211  1.00 30.22           C
ANISOU  267  CA  THR A  31     2964   3106   5414    241   -368    -39       C
ATOM    268  C   THR A  31     -81.103  34.870  -6.661  1.00 25.92           C
ANISOU  268  C   THR A  31     2502   2500   4847    187   -349    -59       C
ATOM    269  O   THR A  31     -80.776  34.480  -5.537  1.00 26.73           O
ANISOU  269  O   THR A  31     2626   2565   4965    154   -302   -141       O
ATOM    270  CB  THR A  31     -79.224  35.960  -7.919  1.00 32.35           C
ANISOU  270  CB  THR A  31     3193   3307   5793    351   -383     37       C
ATOM    271  OG1 THR A  31     -78.652  37.226  -8.271  1.00 35.43           O
ANISOU  271  OG1 THR A  31     3458   3787   6218    417   -420     56       O
ATOM    272  CG2 THR A  31     -79.398  35.127  -9.181  1.00 30.14           C
ANISOU  272  CG2 THR A  31     2974   3006   5474    357   -434    158       C
ATOM    273  N   VAL A  32     -81.929  34.196  -7.455  1.00 24.15           N
ANISOU  273  N   VAL A  32     2310   2284   4581    164   -381      1       N
ATOM    274  CA  VAL A  32     -82.460  32.883  -7.116  1.00 18.83           C
ANISOU  274  CA  VAL A  32     1668   1581   3907    115   -374    -10       C
ATOM    275  C   VAL A  32     -81.687  31.837  -7.905  1.00 25.50           C
ANISOU  275  C   VAL A  32     2534   2337   4820    122   -352     38       C
ATOM    276  O   VAL A  32     -81.538  31.955  -9.128  1.00 23.88           O
ANISOU  276  O   VAL A  32     2342   2130   4602    154   -362    127       O
ATOM    277  CB  VAL A  32     -83.966  32.797  -7.414  1.00 27.04           C
ANISOU  277  CB  VAL A  32     2710   2678   4888     94   -392     18       C
ATOM    278  CG1 VAL A  32     -84.507  31.436  -7.013  1.00 28.82           C
ANISOU  278  CG1 VAL A  32     2913   2903   5134     56   -400     10       C
ATOM    279  CG2 VAL A  32     -84.712  33.907  -6.695  1.00 25.71           C
ANISOU  279  CG2 VAL A  32     2551   2555   4661     87   -395     -4       C
ATOM    280  N   TYR A  33     -81.190  30.818  -7.208  1.00 21.30           N
ANISOU  280  N   TYR A  33     2017   1733   4344     71   -314    -21       N
ATOM    281  CA  TYR A  33     -80.455  29.727  -7.826  1.00 25.58           C
ANISOU  281  CA  TYR A  33     2598   2155   4965     48   -261     15       C
ATOM    282  C   TYR A  33     -81.147  28.403  -7.538  1.00 23.30           C
ANISOU  282  C   TYR A  33     2285   1893   4674    -68   -250    -38       C
ATOM    283  O   TYR A  33     -81.865  28.260  -6.545  1.00 26.41           O
ANISOU  283  O   TYR A  33     2631   2386   5020   -118   -295   -113       O
ATOM    284  CB  TYR A  33     -79.010  29.658  -7.316  1.00 28.39           C
ANISOU  284  CB  TYR A  33     2994   2361   5433     74   -190    -33       C
ATOM    285  CG  TYR A  33     -78.158  30.857  -7.653  1.00 29.04           C
ANISOU  285  CG  TYR A  33     3057   2413   5563    213   -198     31       C
ATOM    286  CD1 TYR A  33     -78.154  31.979  -6.838  1.00 22.21           C
ANISOU  286  CD1 TYR A  33     2135   1625   4679    246   -207    -47       C
ATOM    287  CD2 TYR A  33     -77.341  30.858  -8.776  1.00 26.45           C
ANISOU  287  CD2 TYR A  33     2758   1993   5300    310   -198    180       C
ATOM    288  CE1 TYR A  33     -77.373  33.073  -7.138  1.00 25.23           C
ANISOU  288  CE1 TYR A  33     2454   2006   5127    371   -213      0       C
ATOM    289  CE2 TYR A  33     -76.554  31.951  -9.083  1.00 28.27           C
ANISOU  289  CE2 TYR A  33     2930   2227   5584    454   -233    254       C
ATOM    290  CZ  TYR A  33     -76.574  33.055  -8.260  1.00 31.79           C
ANISOU  290  CZ  TYR A  33     3283   2764   6033    484   -239    152       C
ATOM    291  OH  TYR A  33     -75.792  34.148  -8.558  1.00 36.42           O
ANISOU  291  OH  TYR A  33     3766   3379   6693    624   -273    215       O
ATOM    292  N   THR A  34     -80.916  27.431  -8.416  1.00 25.21           N
ANISOU  292  N   THR A  34     2555   2059   4966   -113   -192     14       N
ATOM    293  CA  THR A  34     -81.358  26.063  -8.198  1.00 29.19           C
ANISOU  293  CA  THR A  34     3008   2582   5501   -245   -160    -50       C
ATOM    294  C   THR A  34     -80.203  25.118  -8.494  1.00 30.50           C
ANISOU  294  C   THR A  34     3254   2564   5769   -325    -48    -55       C
ATOM    295  O   THR A  34     -79.367  25.385  -9.362  1.00 32.80           O
ANISOU  295  O   THR A  34     3644   2723   6095   -254      2     61       O
ATOM    296  CB  THR A  34     -82.576  25.702  -9.066  1.00 31.12           C
ANISOU  296  CB  THR A  34     3185   2928   5712   -252   -160      6       C
ATOM    297  OG1 THR A  34     -83.031  24.388  -8.726  1.00 28.26           O
ANISOU  297  OG1 THR A  34     2722   2616   5401   -377   -136    -70       O
ATOM    298  CG2 THR A  34     -82.222  25.742 -10.549  1.00 29.53           C
ANISOU  298  CG2 THR A  34     3072   2654   5494   -229    -88    126       C
ATOM    299  N   LYS A  35     -80.152  24.017  -7.751  1.00 33.12           N
ANISOU  299  N   LYS A  35     3547   2890   6148   -480    -12   -184       N
ATOM    300  CA  LYS A  35     -79.096  23.027  -7.914  1.00 37.85           C
ANISOU  300  CA  LYS A  35     4233   3286   6860   -598    124   -220       C
ATOM    301  C   LYS A  35     -79.496  22.052  -9.014  1.00 36.49           C
ANISOU  301  C   LYS A  35     4046   3108   6712   -688    202   -145       C
ATOM    302  O   LYS A  35     -80.526  21.377  -8.907  1.00 32.38           O
ANISOU  302  O   LYS A  35     3380   2754   6170   -781    172   -205       O
ATOM    303  CB  LYS A  35     -78.832  22.287  -6.603  1.00 44.08           C
ANISOU  303  CB  LYS A  35     4990   4084   7675   -772    142   -431       C
ATOM    304  CG  LYS A  35     -77.611  21.379  -6.638  1.00 47.28           C
ANISOU  304  CG  LYS A  35     5517   4229   8219   -908    315   -505       C
ATOM    305  CD  LYS A  35     -77.641  20.361  -5.506  1.00 54.48           C
ANISOU  305  CD  LYS A  35     6366   5209   9125  -1157    331   -744       C
ATOM    306  CE  LYS A  35     -77.385  21.004  -4.152  1.00 58.23           C
ANISOU  306  CE  LYS A  35     6855   5746   9524  -1159    278   -901       C
ATOM    307  NZ  LYS A  35     -75.989  20.775  -3.682  1.00 62.02           N
ANISOU  307  NZ  LYS A  35     7506   6011  10047  -1202    446  -1016       N
ATOM    308  N   VAL A  36     -78.690  21.987 -10.070  1.00 36.82           N
ANISOU  308  N   VAL A  36     4230   2963   6796   -653    304     -3       N
ATOM    309  CA  VAL A  36     -78.922  21.096 -11.201  1.00 36.77           C
ANISOU  309  CA  VAL A  36     4250   2927   6791   -754    414     85       C
ATOM    310  C   VAL A  36     -77.721  20.169 -11.302  1.00 45.31           C
ANISOU  310  C   VAL A  36     5477   3735   8004   -881    584     87       C
ATOM    311  O   VAL A  36     -76.640  20.591 -11.733  1.00 49.78           O
ANISOU  311  O   VAL A  36     6212   4088   8616   -769    631    228       O
ATOM    312  CB  VAL A  36     -79.135  21.867 -12.510  1.00 34.40           C
ANISOU  312  CB  VAL A  36     4025   2669   6377   -618    390    284       C
ATOM    313  CG1 VAL A  36     -79.260  20.901 -13.678  1.00 38.46           C
ANISOU  313  CG1 VAL A  36     4602   3141   6871   -748    539    373       C
ATOM    314  CG2 VAL A  36     -80.365  22.751 -12.411  1.00 27.19           C
ANISOU  314  CG2 VAL A  36     2984   1991   5354   -521    259    254       C
ATOM    315  N   ASP A  37     -77.907  18.909 -10.905  1.00 50.20           N
ANISOU  315  N   ASP A  37     6023   4360   8690  -1111    675    -66       N
ATOM    316  CA  ASP A  37     -76.840  17.907 -10.928  1.00 52.30           C
ANISOU  316  CA  ASP A  37     6441   4445   8988  -1234    829    -97       C
ATOM    317  C   ASP A  37     -75.629  18.364 -10.119  1.00 44.47           C
ANISOU  317  C   ASP A  37     5577   3279   8043  -1142    837   -150       C
ATOM    318  O   ASP A  37     -74.480  18.176 -10.522  1.00 45.43           O
ANISOU  318  O   ASP A  37     5886   3168   8209  -1100    950    -54       O
ATOM    319  CB  ASP A  37     -76.440  17.555 -12.363  1.00 68.87           C
ANISOU  319  CB  ASP A  37     8703   6399  11066  -1234    960    118       C
ATOM    320  CG  ASP A  37     -77.360  16.522 -12.984  1.00 87.72           C
ANISOU  320  CG  ASP A  37    10981   8926  13421  -1425   1047     88       C
ATOM    321  OD1 ASP A  37     -77.511  15.429 -12.396  1.00 94.59           O
ANISOU  321  OD1 ASP A  37    11752   9868  14322  -1618   1095    -93       O
ATOM    322  OD2 ASP A  37     -77.941  16.805 -14.053  1.00 93.48           O
ANISOU  322  OD2 ASP A  37    11717   9711  14089  -1386   1072    236       O
ATOM    323  N   GLY A  38     -75.890  18.976  -8.967  1.00 38.70           N
ANISOU  323  N   GLY A  38     4743   2662   7300  -1108    724   -299       N
ATOM    324  CA  GLY A  38     -74.840  19.346  -8.045  1.00 45.81           C
ANISOU  324  CA  GLY A  38     5738   3430   8238  -1054    760   -402       C
ATOM    325  C   GLY A  38     -74.260  20.732  -8.225  1.00 49.99           C
ANISOU  325  C   GLY A  38     6330   3866   8799   -786    715   -265       C
ATOM    326  O   GLY A  38     -73.390  21.123  -7.436  1.00 55.35           O
ANISOU  326  O   GLY A  38     7065   4445   9522   -724    762   -360       O
ATOM    327  N   VAL A  39     -74.699  21.487  -9.229  1.00 46.14           N
ANISOU  327  N   VAL A  39     5821   3424   8285   -631    630    -54       N
ATOM    328  CA  VAL A  39     -74.200  22.838  -9.447  1.00 42.26           C
ANISOU  328  CA  VAL A  39     5350   2899   7806   -377    556     82       C
ATOM    329  C   VAL A  39     -75.374  23.805  -9.462  1.00 34.68           C
ANISOU  329  C   VAL A  39     4247   2175   6756   -305    386    104       C
ATOM    330  O   VAL A  39     -76.492  23.455  -9.854  1.00 36.94           O
ANISOU  330  O   VAL A  39     4456   2650   6930   -389    330    111       O
ATOM    331  CB  VAL A  39     -73.374  22.958 -10.748  1.00 41.34           C
ANISOU  331  CB  VAL A  39     5372   2637   7698   -233    592    351       C
ATOM    332  CG1 VAL A  39     -72.175  22.026 -10.703  1.00 42.72           C
ANISOU  332  CG1 VAL A  39     5707   2571   7955   -291    760    336       C
ATOM    333  CG2 VAL A  39     -74.236  22.674 -11.968  1.00 40.17           C
ANISOU  333  CG2 VAL A  39     5226   2574   7461   -289    561    515       C
ATOM    334  N   ASP A  40     -75.109  25.034  -9.026  1.00 34.71           N
ANISOU  334  N   ASP A  40     4209   2224   6755   -138    310    102       N
ATOM    335  CA  ASP A  40     -76.143  26.055  -8.947  1.00 38.02           C
ANISOU  335  CA  ASP A  40     4508   2913   7023    -69    154    107       C
ATOM    336  C   ASP A  40     -76.303  26.754 -10.292  1.00 33.31           C
ANISOU  336  C   ASP A  40     3921   2388   6347     61     73    326       C
ATOM    337  O   ASP A  40     -75.314  27.121 -10.935  1.00 36.09           O
ANISOU  337  O   ASP A  40     4337   2610   6767    196     84    483       O
ATOM    338  CB  ASP A  40     -75.802  27.073  -7.860  1.00 41.79           C
ANISOU  338  CB  ASP A  40     4936   3421   7522     14    132     -9       C
ATOM    339  CG  ASP A  40     -75.633  26.432  -6.497  1.00 52.40           C
ANISOU  339  CG  ASP A  40     6290   4722   8897   -139    212   -243       C
ATOM    340  OD1 ASP A  40     -76.374  25.473  -6.195  1.00 55.69           O
ANISOU  340  OD1 ASP A  40     6679   5233   9249   -315    197   -332       O
ATOM    341  OD2 ASP A  40     -74.756  26.883  -5.731  1.00 58.50           O
ANISOU  341  OD2 ASP A  40     7087   5383   9756    -91    293   -347       O
ATOM    342  N   VAL A  41     -77.551  26.932 -10.713  1.00 27.72           N
ANISOU  342  N   VAL A  41     3149   1891   5493     21     -7    336       N
ATOM    343  CA  VAL A  41     -77.885  27.604 -11.962  1.00 31.48           C
ANISOU  343  CA  VAL A  41     3637   2477   5848     95    -81    496       C
ATOM    344  C   VAL A  41     -78.792  28.781 -11.639  1.00 27.29           C
ANISOU  344  C   VAL A  41     3004   2146   5218    138   -188    430       C
ATOM    345  O   VAL A  41     -79.808  28.617 -10.954  1.00 31.30           O
ANISOU  345  O   VAL A  41     3450   2748   5696     66   -195    307       O
ATOM    346  CB  VAL A  41     -78.562  26.646 -12.960  1.00 31.62           C
ANISOU  346  CB  VAL A  41     3701   2526   5785    -23    -20    554       C
ATOM    347  CG1 VAL A  41     -78.978  27.394 -14.217  1.00 34.18           C
ANISOU  347  CG1 VAL A  41     4052   2993   5941     23    -88    685       C
ATOM    348  CG2 VAL A  41     -77.628  25.494 -13.303  1.00 33.08           C
ANISOU  348  CG2 VAL A  41     4007   2493   6070    -90    110    630       C
ATOM    349  N   GLU A  42     -78.419  29.963 -12.123  1.00 24.85           N
ANISOU  349  N   GLU A  42     2675   1903   4865    252   -272    519       N
ATOM    350  CA  GLU A  42     -79.213  31.159 -11.876  1.00 25.06           C
ANISOU  350  CA  GLU A  42     2614   2102   4804    268   -352    451       C
ATOM    351  C   GLU A  42     -80.558  31.060 -12.584  1.00 30.14           C
ANISOU  351  C   GLU A  42     3269   2872   5312    180   -356    437       C
ATOM    352  O   GLU A  42     -80.623  30.756 -13.778  1.00 31.52           O
ANISOU  352  O   GLU A  42     3507   3072   5397    151   -347    536       O
ATOM    353  CB  GLU A  42     -78.464  32.403 -12.347  1.00 23.46           C
ANISOU  353  CB  GLU A  42     2360   1965   4590    386   -443    542       C
ATOM    354  CG  GLU A  42     -79.351  33.628 -12.475  1.00 45.31           C
ANISOU  354  CG  GLU A  42     5052   4924   7239    356   -517    482       C
ATOM    355  CD  GLU A  42     -78.619  34.827 -13.034  1.00 45.73           C
ANISOU  355  CD  GLU A  42     5016   5087   7272    447   -625    567       C
ATOM    356  OE1 GLU A  42     -77.408  34.965 -12.764  1.00 49.09           O
ANISOU  356  OE1 GLU A  42     5389   5428   7834    576   -634    631       O
ATOM    357  OE2 GLU A  42     -79.255  35.628 -13.750  1.00 47.31           O
ANISOU  357  OE2 GLU A  42     5187   5461   7328    387   -697    562       O
ATOM    358  N   LEU A  43     -81.633  31.317 -11.843  1.00 30.83           N
ANISOU  358  N   LEU A  43     3304   3026   5383    140   -354    319       N
ATOM    359  CA  LEU A  43     -82.975  31.334 -12.404  1.00 29.59           C
ANISOU  359  CA  LEU A  43     3149   2956   5137     82   -332    288       C
ATOM    360  C   LEU A  43     -83.552  32.729 -12.565  1.00 27.68           C
ANISOU  360  C   LEU A  43     2887   2816   4812     87   -377    251       C
ATOM    361  O   LEU A  43     -84.357  32.947 -13.472  1.00 28.38           O
ANISOU  361  O   LEU A  43     3008   2968   4806     35   -349    238       O
ATOM    362  CB  LEU A  43     -83.933  30.513 -11.533  1.00 27.83           C
ANISOU  362  CB  LEU A  43     2880   2718   4976     44   -289    206       C
ATOM    363  CG  LEU A  43     -83.734  28.999 -11.491  1.00 27.13           C
ANISOU  363  CG  LEU A  43     2782   2565   4960    -14   -229    206       C
ATOM    364  CD1 LEU A  43     -84.849  28.349 -10.688  1.00 21.65           C
ANISOU  364  CD1 LEU A  43     1994   1918   4313    -40   -224    132       C
ATOM    365  CD2 LEU A  43     -83.671  28.427 -12.898  1.00 30.38           C
ANISOU  365  CD2 LEU A  43     3256   2967   5322    -61   -155    280       C
ATOM    366  N   PHE A  44     -83.155  33.678 -11.721  1.00 26.57           N
ANISOU  366  N   PHE A  44     2698   2692   4706    126   -423    214       N
ATOM    367  CA  PHE A  44     -83.802  34.983 -11.697  1.00 26.21           C
ANISOU  367  CA  PHE A  44     2629   2732   4599     96   -441    154       C
ATOM    368  C   PHE A  44     -82.915  35.963 -10.948  1.00 25.37           C
ANISOU  368  C   PHE A  44     2449   2650   4541    139   -482    134       C
ATOM    369  O   PHE A  44     -82.531  35.704  -9.804  1.00 22.17           O
ANISOU  369  O   PHE A  44     2029   2180   4215    168   -455     99       O
ATOM    370  CB  PHE A  44     -85.179  34.882 -11.032  1.00 27.91           C
ANISOU  370  CB  PHE A  44     2865   2915   4826     63   -380     85       C
ATOM    371  CG  PHE A  44     -85.888  36.197 -10.883  1.00 26.12           C
ANISOU  371  CG  PHE A  44     2642   2726   4556     16   -363     21       C
ATOM    372  CD1 PHE A  44     -86.586  36.747 -11.945  1.00 20.58           C
ANISOU  372  CD1 PHE A  44     1978   2066   3774    -55   -330    -19       C
ATOM    373  CD2 PHE A  44     -85.880  36.872  -9.673  1.00 23.72           C
ANISOU  373  CD2 PHE A  44     2320   2408   4283     17   -359    -13       C
ATOM    374  CE1 PHE A  44     -87.247  37.953 -11.809  1.00 24.81           C
ANISOU  374  CE1 PHE A  44     2530   2614   4283   -129   -291    -98       C
ATOM    375  CE2 PHE A  44     -86.540  38.077  -9.530  1.00 24.50           C
ANISOU  375  CE2 PHE A  44     2437   2522   4351    -50   -318    -70       C
ATOM    376  CZ  PHE A  44     -87.225  38.619 -10.600  1.00 24.82           C
ANISOU  376  CZ  PHE A  44     2512   2587   4334   -125   -283   -116       C
ATOM    377  N   GLU A  45     -82.593  37.080 -11.593  1.00 28.14           N
ANISOU  377  N   GLU A  45     2742   3111   4839    130   -540    141       N
ATOM    378  CA  GLU A  45     -81.871  38.175 -10.958  1.00 25.69           C
ANISOU  378  CA  GLU A  45     2320   2853   4586    161   -564    103       C
ATOM    379  C   GLU A  45     -82.861  39.292 -10.660  1.00 25.07           C
ANISOU  379  C   GLU A  45     2232   2841   4453     50   -526     -4       C
ATOM    380  O   GLU A  45     -83.437  39.879 -11.583  1.00 29.06           O
ANISOU  380  O   GLU A  45     2744   3438   4860    -38   -549    -29       O
ATOM    381  CB  GLU A  45     -80.737  38.683 -11.847  1.00 25.97           C
ANISOU  381  CB  GLU A  45     2254   2989   4624    234   -669    195       C
ATOM    382  CG  GLU A  45     -79.952  39.831 -11.228  1.00 40.16           C
ANISOU  382  CG  GLU A  45     3886   4857   6515    281   -685    148       C
ATOM    383  CD  GLU A  45     -78.995  40.484 -12.205  1.00 51.96           C
ANISOU  383  CD  GLU A  45     5235   6499   8006    360   -822    253       C
ATOM    384  OE1 GLU A  45     -78.963  40.063 -13.380  1.00 57.41           O
ANISOU  384  OE1 GLU A  45     5985   7244   8586    364   -913    373       O
ATOM    385  OE2 GLU A  45     -78.275  41.422 -11.798  1.00 56.31           O
ANISOU  385  OE2 GLU A  45     5606   7129   8662    417   -840    222       O
ATOM    386  N   ASN A  46     -83.058  39.582  -9.377  1.00 21.52           N
ANISOU  386  N   ASN A  46     1784   2339   4054     35   -454    -70       N
ATOM    387  CA  ASN A  46     -84.040  40.575  -8.956  1.00 24.26           C
ANISOU  387  CA  ASN A  46     2155   2704   4359    -78   -388   -152       C
ATOM    388  C   ASN A  46     -83.560  41.970  -9.335  1.00 29.19           C
ANISOU  388  C   ASN A  46     2644   3470   4978   -142   -415   -211       C
ATOM    389  O   ASN A  46     -82.567  42.465  -8.791  1.00 31.15           O
ANISOU  389  O   ASN A  46     2766   3766   5303    -96   -415   -230       O
ATOM    390  CB  ASN A  46     -84.282  40.467  -7.453  1.00 22.65           C
ANISOU  390  CB  ASN A  46     2004   2420   4182    -81   -308   -178       C
ATOM    391  CG  ASN A  46     -85.321  41.450  -6.958  1.00 24.05           C
ANISOU  391  CG  ASN A  46     2242   2580   4317   -195   -221   -230       C
ATOM    392  OD1 ASN A  46     -86.157  41.926  -7.724  1.00 29.64           O
ANISOU  392  OD1 ASN A  46     2988   3285   4989   -271   -201   -255       O
ATOM    393  ND2 ASN A  46     -85.274  41.760  -5.668  1.00 29.78           N
ANISOU  393  ND2 ASN A  46     2994   3282   5038   -223   -150   -251       N
ATOM    394  N   LYS A  47     -84.263  42.607 -10.270  1.00 22.01           N
ANISOU  394  N   LYS A  47     1747   2633   3981   -258   -427   -257       N
ATOM    395  CA  LYS A  47     -83.996  43.986 -10.652  1.00 24.50           C
ANISOU  395  CA  LYS A  47     1921   3113   4273   -369   -457   -340       C
ATOM    396  C   LYS A  47     -85.044  44.951 -10.114  1.00 31.35           C
ANISOU  396  C   LYS A  47     2851   3933   5127   -542   -322   -459       C
ATOM    397  O   LYS A  47     -85.099  46.101 -10.560  1.00 31.56           O
ANISOU  397  O   LYS A  47     2782   4091   5118   -693   -326   -561       O
ATOM    398  CB  LYS A  47     -83.909  44.107 -12.176  1.00 33.94           C
ANISOU  398  CB  LYS A  47     3080   4464   5350   -419   -578   -325       C
ATOM    399  CG  LYS A  47     -82.792  43.289 -12.808  1.00 45.54           C
ANISOU  399  CG  LYS A  47     4495   5985   6822   -254   -714   -173       C
ATOM    400  CD  LYS A  47     -81.439  43.636 -12.202  1.00 57.39           C
ANISOU  400  CD  LYS A  47     5805   7534   8466   -116   -766   -124       C
ATOM    401  CE  LYS A  47     -80.975  45.032 -12.601  1.00 71.32           C
ANISOU  401  CE  LYS A  47     7341   9539  10220   -190   -858   -180       C
ATOM    402  NZ  LYS A  47     -80.461  45.083 -13.999  1.00 79.79           N
ANISOU  402  NZ  LYS A  47     8334  10811  11171   -167  -1054    -71       N
ATOM    403  N   THR A  48     -85.872  44.510  -9.170  1.00 30.83           N
ANISOU  403  N   THR A  48     2942   3685   5085   -530   -208   -442       N
ATOM    404  CA  THR A  48     -86.953  45.315  -8.629  1.00 27.72           C
ANISOU  404  CA  THR A  48     2655   3193   4684   -675    -62   -513       C
ATOM    405  C   THR A  48     -86.589  45.824  -7.236  1.00 26.56           C
ANISOU  405  C   THR A  48     2482   3028   4582   -690     23   -519       C
ATOM    406  O   THR A  48     -85.546  45.489  -6.669  1.00 28.75           O
ANISOU  406  O   THR A  48     2664   3360   4900   -584    -19   -489       O
ATOM    407  CB  THR A  48     -88.253  44.508  -8.581  1.00 30.63           C
ANISOU  407  CB  THR A  48     3226   3365   5047   -638      8   -458       C
ATOM    408  OG1 THR A  48     -88.279  43.716  -7.386  1.00 30.37           O
ANISOU  408  OG1 THR A  48     3257   3238   5044   -517     18   -353       O
ATOM    409  CG2 THR A  48     -88.352  43.586  -9.786  1.00 26.49           C
ANISOU  409  CG2 THR A  48     2716   2862   4488   -573    -68   -434       C
ATOM    410  N   THR A  49     -87.473  46.647  -6.679  1.00 31.92           N
ANISOU  410  N   THR A  49     3266   3614   5250   -836    168   -566       N
ATOM    411  CA  THR A  49     -87.340  47.140  -5.316  1.00 30.76           C
ANISOU  411  CA  THR A  49     3146   3434   5108   -884    285   -562       C
ATOM    412  C   THR A  49     -88.021  46.236  -4.299  1.00 33.50           C
ANISOU  412  C   THR A  49     3691   3622   5416   -788    317   -428       C
ATOM    413  O   THR A  49     -88.076  46.587  -3.116  1.00 25.19           O
ANISOU  413  O   THR A  49     2713   2537   4323   -842    418   -403       O
ATOM    414  CB  THR A  49     -87.913  48.556  -5.208  1.00 33.67           C
ANISOU  414  CB  THR A  49     3536   3782   5476  -1117    442   -668       C
ATOM    415  OG1 THR A  49     -89.293  48.545  -5.595  1.00 35.08           O
ANISOU  415  OG1 THR A  49     3916   3771   5641  -1181    519   -650       O
ATOM    416  CG2 THR A  49     -87.146  49.509  -6.112  1.00 31.77           C
ANISOU  416  CG2 THR A  49     3048   3758   5266  -1232    387   -813       C
ATOM    417  N   LEU A  50     -88.542  45.094  -4.732  1.00 23.39           N
ANISOU  417  N   LEU A  50     2488   2264   4136   -657    232   -339       N
ATOM    418  CA  LEU A  50     -89.209  44.118  -3.889  1.00 24.88           C
ANISOU  418  CA  LEU A  50     2820   2341   4294   -549    219   -200       C
ATOM    419  C   LEU A  50     -88.217  43.075  -3.398  1.00 23.32           C
ANISOU  419  C   LEU A  50     2547   2236   4079   -432    111   -170       C
ATOM    420  O   LEU A  50     -87.123  42.933  -3.953  1.00 23.16           O
ANISOU  420  O   LEU A  50     2384   2317   4100   -396     46   -235       O
ATOM    421  CB  LEU A  50     -90.335  43.442  -4.670  1.00 30.46           C
ANISOU  421  CB  LEU A  50     3611   2921   5041   -473    203   -141       C
ATOM    422  CG  LEU A  50     -91.474  44.344  -5.147  1.00 39.06           C
ANISOU  422  CG  LEU A  50     4815   3860   6166   -585    344   -182       C
ATOM    423  CD1 LEU A  50     -92.446  43.563  -6.015  1.00 38.88           C
ANISOU  423  CD1 LEU A  50     4851   3715   6207   -489    347   -153       C
ATOM    424  CD2 LEU A  50     -92.194  44.964  -3.960  1.00 44.01           C
ANISOU  424  CD2 LEU A  50     5602   4350   6770   -643    468    -93       C
ATOM    425  N   PRO A  51     -88.559  42.337  -2.340  1.00 22.84           N
ANISOU  425  N   PRO A  51     2584   2142   3954   -376     89    -70       N
ATOM    426  CA  PRO A  51     -87.706  41.219  -1.924  1.00 21.43           C
ANISOU  426  CA  PRO A  51     2347   2039   3756   -294     -7    -67       C
ATOM    427  C   PRO A  51     -87.530  40.216  -3.055  1.00 26.35           C
ANISOU  427  C   PRO A  51     2890   2662   4459   -193   -108    -62       C
ATOM    428  O   PRO A  51     -88.396  40.060  -3.918  1.00 27.57           O
ANISOU  428  O   PRO A  51     3068   2752   4654   -164   -115    -25       O
ATOM    429  CB  PRO A  51     -88.468  40.610  -0.743  1.00 22.18           C
ANISOU  429  CB  PRO A  51     2570   2114   3743   -274    -35     55       C
ATOM    430  CG  PRO A  51     -89.251  41.748  -0.189  1.00 23.50           C
ANISOU  430  CG  PRO A  51     2866   2210   3853   -368     84    105       C
ATOM    431  CD  PRO A  51     -89.644  42.588  -1.375  1.00 24.43           C
ANISOU  431  CD  PRO A  51     2956   2245   4081   -408    156     46       C
ATOM    432  N   VAL A  52     -86.384  39.534  -3.039  1.00 28.56           N
ANISOU  432  N   VAL A  52     3087   3000   4764   -150   -160   -107       N
ATOM    433  CA  VAL A  52     -85.999  38.689  -4.168  1.00 28.65           C
ANISOU  433  CA  VAL A  52     3029   3010   4849    -77   -232   -101       C
ATOM    434  C   VAL A  52     -87.016  37.570  -4.376  1.00 29.74           C
ANISOU  434  C   VAL A  52     3209   3101   4988    -24   -283    -19       C
ATOM    435  O   VAL A  52     -87.461  37.316  -5.502  1.00 32.36           O
ANISOU  435  O   VAL A  52     3528   3405   5363      4   -289     -3       O
ATOM    436  CB  VAL A  52     -84.574  38.141  -3.963  1.00 25.95           C
ANISOU  436  CB  VAL A  52     2618   2692   4551    -41   -251   -152       C
ATOM    437  CG1 VAL A  52     -84.408  37.571  -2.560  1.00 23.38           C
ANISOU  437  CG1 VAL A  52     2346   2378   4160    -73   -238   -179       C
ATOM    438  CG2 VAL A  52     -84.243  37.096  -5.017  1.00 18.60           C
ANISOU  438  CG2 VAL A  52     1651   1732   3683     25   -314   -114       C
ATOM    439  N   ASN A  53     -87.413  36.896  -3.293  1.00 27.00           N
ANISOU  439  N   ASN A  53     2904   2767   4589    -14   -318     29       N
ATOM    440  CA  ASN A  53     -88.339  35.776  -3.422  1.00 23.61           C
ANISOU  440  CA  ASN A  53     2463   2322   4184     51   -380    110       C
ATOM    441  C   ASN A  53     -89.730  36.241  -3.823  1.00 29.69           C
ANISOU  441  C   ASN A  53     3287   3005   4989     92   -334    184       C
ATOM    442  O   ASN A  53     -90.461  35.505  -4.496  1.00 32.13           O
ANISOU  442  O   ASN A  53     3556   3277   5375    163   -341    220       O
ATOM    443  CB  ASN A  53     -88.399  34.991  -2.113  1.00 23.32           C
ANISOU  443  CB  ASN A  53     2435   2363   4063     40   -458    148       C
ATOM    444  CG  ASN A  53     -88.997  35.797  -0.980  1.00 25.64           C
ANISOU  444  CG  ASN A  53     2835   2667   4240      9   -442    218       C
ATOM    445  OD1 ASN A  53     -88.386  36.746  -0.487  1.00 27.53           O
ANISOU  445  OD1 ASN A  53     3129   2917   4415    -71   -366    156       O
ATOM    446  ND2 ASN A  53     -90.197  35.420  -0.555  1.00 28.52           N
ANISOU  446  ND2 ASN A  53     3226   3028   4583     76   -505    360       N
ATOM    447  N   VAL A  54     -90.114  37.451  -3.421  1.00 29.38           N
ANISOU  447  N   VAL A  54     3339   2916   4910     43   -259    195       N
ATOM    448  CA  VAL A  54     -91.414  37.985  -3.810  1.00 27.65           C
ANISOU  448  CA  VAL A  54     3197   2565   4745     70   -178    250       C
ATOM    449  C   VAL A  54     -91.424  38.322  -5.294  1.00 29.52           C
ANISOU  449  C   VAL A  54     3406   2760   5049     39   -110    149       C
ATOM    450  O   VAL A  54     -92.332  37.921  -6.033  1.00 28.78           O
ANISOU  450  O   VAL A  54     3320   2580   5034     98    -65    162       O
ATOM    451  CB  VAL A  54     -91.764  39.210  -2.949  1.00 26.05           C
ANISOU  451  CB  VAL A  54     3119   2301   4476     -8    -93    285       C
ATOM    452  CG1 VAL A  54     -93.071  39.816  -3.409  1.00 23.34           C
ANISOU  452  CG1 VAL A  54     2880   1773   4214      7     25    328       C
ATOM    453  CG2 VAL A  54     -91.833  38.817  -1.483  1.00 23.65           C
ANISOU  453  CG2 VAL A  54     2868   2060   4058     13   -166    404       C
ATOM    454  N   ALA A  55     -90.412  39.063  -5.753  1.00 27.04           N
ANISOU  454  N   ALA A  55     3053   2523   4701    -56   -101     44       N
ATOM    455  CA  ALA A  55     -90.338  39.425  -7.166  1.00 25.02           C
ANISOU  455  CA  ALA A  55     2769   2278   4459   -108    -67    -48       C
ATOM    456  C   ALA A  55     -90.210  38.188  -8.044  1.00 24.28           C
ANISOU  456  C   ALA A  55     2620   2213   4394    -36   -116    -34       C
ATOM    457  O   ALA A  55     -90.775  38.133  -9.142  1.00 22.80           O
ANISOU  457  O   ALA A  55     2454   1991   4216    -56    -56    -80       O
ATOM    458  CB  ALA A  55     -89.166  40.376  -7.403  1.00 23.53           C
ANISOU  458  CB  ALA A  55     2506   2208   4226   -201    -90   -132       C
ATOM    459  N   PHE A  56     -89.467  37.185  -7.572  1.00 27.03           N
ANISOU  459  N   PHE A  56     2905   2618   4748     25   -203     12       N
ATOM    460  CA  PHE A  56     -89.336  35.937  -8.316  1.00 23.57           C
ANISOU  460  CA  PHE A  56     2416   2197   4343     72   -230     28       C
ATOM    461  C   PHE A  56     -90.694  35.285  -8.534  1.00 27.63           C
ANISOU  461  C   PHE A  56     2939   2632   4927    134   -170     60       C
ATOM    462  O   PHE A  56     -90.986  34.782  -9.626  1.00 28.29           O
ANISOU  462  O   PHE A  56     3009   2705   5033    133   -113     28       O
ATOM    463  CB  PHE A  56     -88.395  34.994  -7.567  1.00 24.83           C
ANISOU  463  CB  PHE A  56     2518   2405   4509    100   -311     56       C
ATOM    464  CG  PHE A  56     -88.344  33.605  -8.131  1.00 26.63           C
ANISOU  464  CG  PHE A  56     2694   2639   4784    125   -322     74       C
ATOM    465  CD1 PHE A  56     -87.882  33.382  -9.416  1.00 26.62           C
ANISOU  465  CD1 PHE A  56     2694   2646   4774    100   -294     62       C
ATOM    466  CD2 PHE A  56     -88.735  32.519  -7.366  1.00 29.28           C
ANISOU  466  CD2 PHE A  56     2972   2990   5161    157   -362    106       C
ATOM    467  CE1 PHE A  56     -87.826  32.102  -9.935  1.00 20.61           C
ANISOU  467  CE1 PHE A  56     1895   1883   4052    100   -274     78       C
ATOM    468  CE2 PHE A  56     -88.677  31.237  -7.877  1.00 24.77           C
ANISOU  468  CE2 PHE A  56     2331   2434   4646    153   -356    106       C
ATOM    469  CZ  PHE A  56     -88.224  31.028  -9.164  1.00 21.07           C
ANISOU  469  CZ  PHE A  56     1880   1948   4177    121   -296     90       C
ATOM    470  N   GLU A  57     -91.543  35.297  -7.506  1.00 24.89           N
ANISOU  470  N   GLU A  57     2613   2229   4616    195   -174    130       N
ATOM    471  CA  GLU A  57     -92.862  34.690  -7.625  1.00 25.23           C
ANISOU  471  CA  GLU A  57     2637   2185   4764    297   -120    184       C
ATOM    472  C   GLU A  57     -93.742  35.467  -8.597  1.00 27.52           C
ANISOU  472  C   GLU A  57     3013   2347   5098    273     37    114       C
ATOM    473  O   GLU A  57     -94.454  34.870  -9.412  1.00 29.36           O
ANISOU  473  O   GLU A  57     3214   2524   5417    321    129     82       O
ATOM    474  CB  GLU A  57     -93.516  34.606  -6.247  1.00 32.31           C
ANISOU  474  CB  GLU A  57     3542   3061   5673    383   -185    315       C
ATOM    475  CG  GLU A  57     -94.905  34.000  -6.242  1.00 41.64           C
ANISOU  475  CG  GLU A  57     4676   4150   6995    534   -148    409       C
ATOM    476  CD  GLU A  57     -95.452  33.824  -4.839  1.00 51.82           C
ANISOU  476  CD  GLU A  57     5962   5461   8268    631   -261    582       C
ATOM    477  OE1 GLU A  57     -94.642  33.739  -3.892  1.00 56.95           O
ANISOU  477  OE1 GLU A  57     6612   6246   8780    564   -386    604       O
ATOM    478  OE2 GLU A  57     -96.690  33.774  -4.683  1.00 56.91           O
ANISOU  478  OE2 GLU A  57     6608   5983   9031    776   -220    700       O
ATOM    479  N   LEU A  58     -93.695  36.799  -8.533  1.00 24.91           N
ANISOU  479  N   LEU A  58     2786   1968   4710    177     89     66       N
ATOM    480  CA  LEU A  58     -94.524  37.612  -9.418  1.00 24.89           C
ANISOU  480  CA  LEU A  58     2881   1837   4739    112    252    -35       C
ATOM    481  C   LEU A  58     -94.099  37.456 -10.873  1.00 23.61           C
ANISOU  481  C   LEU A  58     2698   1760   4511     18    288   -165       C
ATOM    482  O   LEU A  58     -94.948  37.350 -11.766  1.00 24.40           O
ANISOU  482  O   LEU A  58     2843   1769   4660      8    434   -249       O
ATOM    483  CB  LEU A  58     -94.459  39.078  -8.992  1.00 23.23           C
ANISOU  483  CB  LEU A  58     2772   1582   4474    -12    297    -74       C
ATOM    484  CG  LEU A  58     -94.968  39.373  -7.581  1.00 28.12           C
ANISOU  484  CG  LEU A  58     3460   2101   5125     53    293     66       C
ATOM    485  CD1 LEU A  58     -94.713  40.822  -7.202  1.00 31.38           C
ANISOU  485  CD1 LEU A  58     3960   2493   5470   -109    355      9       C
ATOM    486  CD2 LEU A  58     -96.446  39.042  -7.473  1.00 29.14           C
ANISOU  486  CD2 LEU A  58     3656   2013   5404    193    402    156       C
ATOM    487  N   TRP A  59     -92.790  37.441 -11.130  1.00 23.68           N
ANISOU  487  N   TRP A  59     2648   1940   4408    -47    168   -177       N
ATOM    488  CA  TRP A  59     -92.313  37.259 -12.496  1.00 24.08           C
ANISOU  488  CA  TRP A  59     2692   2094   4363   -131    176   -256       C
ATOM    489  C   TRP A  59     -92.701  35.891 -13.038  1.00 30.96           C
ANISOU  489  C   TRP A  59     3524   2947   5292    -56    231   -236       C
ATOM    490  O   TRP A  59     -93.070  35.761 -14.210  1.00 33.28           O
ANISOU  490  O   TRP A  59     3862   3246   5537   -124    342   -327       O
ATOM    491  CB  TRP A  59     -90.799  37.446 -12.555  1.00 24.62           C
ANISOU  491  CB  TRP A  59     2697   2327   4329   -170     25   -223       C
ATOM    492  CG  TRP A  59     -90.208  37.038 -13.866  1.00 25.73           C
ANISOU  492  CG  TRP A  59     2836   2582   4359   -226      2   -239       C
ATOM    493  CD1 TRP A  59     -90.242  37.739 -15.037  1.00 26.62           C
ANISOU  493  CD1 TRP A  59     2998   2784   4331   -362     28   -332       C
ATOM    494  CD2 TRP A  59     -89.492  35.831 -14.140  1.00 23.38           C
ANISOU  494  CD2 TRP A  59     2498   2327   4060   -168    -49   -152       C
ATOM    495  NE1 TRP A  59     -89.590  37.040 -16.025  1.00 24.25           N
ANISOU  495  NE1 TRP A  59     2700   2590   3922   -379    -14   -284       N
ATOM    496  CE2 TRP A  59     -89.120  35.866 -15.499  1.00 25.55           C
ANISOU  496  CE2 TRP A  59     2816   2709   4183   -260    -49   -170       C
ATOM    497  CE3 TRP A  59     -89.129  34.724 -13.369  1.00 24.08           C
ANISOU  497  CE3 TRP A  59     2525   2376   4247    -71    -90    -66       C
ATOM    498  CZ2 TRP A  59     -88.403  34.836 -16.102  1.00 35.18           C
ANISOU  498  CZ2 TRP A  59     4036   3972   5358   -244    -74    -82       C
ATOM    499  CZ3 TRP A  59     -88.417  33.704 -13.968  1.00 32.27           C
ANISOU  499  CZ3 TRP A  59     3551   3449   5260    -70   -106     -8       C
ATOM    500  CH2 TRP A  59     -88.061  33.766 -15.321  1.00 36.28           C
ANISOU  500  CH2 TRP A  59     4119   4039   5627   -150    -91     -4       C
ATOM    501  N   ALA A  60     -92.621  34.856 -12.199  1.00 29.04           N
ANISOU  501  N   ALA A  60     3193   2699   5143     64    164   -132       N
ATOM    502  CA  ALA A  60     -93.035  33.528 -12.635  1.00 25.76           C
ANISOU  502  CA  ALA A  60     2703   2277   4808    125    226   -121       C
ATOM    503  C   ALA A  60     -94.518  33.490 -12.971  1.00 27.17           C
ANISOU  503  C   ALA A  60     2899   2316   5110    185    403   -176       C
ATOM    504  O   ALA A  60     -94.931  32.760 -13.880  1.00 27.27           O
ANISOU  504  O   ALA A  60     2882   2324   5157    180    531   -239       O
ATOM    505  CB  ALA A  60     -92.705  32.496 -11.558  1.00 26.48           C
ANISOU  505  CB  ALA A  60     2674   2411   4976    216    106    -16       C
ATOM    506  N   LYS A  61     -95.330  34.271 -12.259  1.00 31.83           N
ANISOU  506  N   LYS A  61     3177   3435   5481   -794     73   -317       N
ATOM    507  CA  LYS A  61     -96.766  34.326 -12.487  1.00 32.74           C
ANISOU  507  CA  LYS A  61     3110   3555   5776   -704    -34   -377       C
ATOM    508  C   LYS A  61     -97.173  35.460 -13.422  1.00 30.06           C
ANISOU  508  C   LYS A  61     2774   3157   5488   -611     -3   -360       C
ATOM    509  O   LYS A  61     -98.352  35.831 -13.451  1.00 30.50           O
ANISOU  509  O   LYS A  61     2721   3185   5684   -516   -111   -377       O
ATOM    510  CB  LYS A  61     -97.505  34.459 -11.155  1.00 28.23           C
ANISOU  510  CB  LYS A  61     2507   2966   5253   -647   -240   -307       C
ATOM    511  CG  LYS A  61     -97.261  33.310 -10.192  1.00 29.21           C
ANISOU  511  CG  LYS A  61     2608   3154   5336   -731   -304   -338       C
ATOM    512  CD  LYS A  61     -98.003  33.522  -8.884  1.00 30.07           C
ANISOU  512  CD  LYS A  61     2716   3237   5473   -662   -526   -258       C
ATOM    513  CE  LYS A  61     -97.829  32.335  -7.952  1.00 31.28           C
ANISOU  513  CE  LYS A  61     2833   3462   5589   -743   -611   -306       C
ATOM    514  NZ  LYS A  61     -98.590  32.509  -6.686  1.00 32.36           N
ANISOU  514  NZ  LYS A  61     2986   3572   5739   -667   -848   -228       N
ATOM    515  N   ARG A  62     -96.230  36.017 -14.179  1.00 25.73           N
ANISOU  515  N   ARG A  62     2356   2587   4833   -631    130   -332       N
ATOM    516  CA  ARG A  62     -96.546  37.093 -15.106  1.00 27.04           C
ANISOU  516  CA  ARG A  62     2528   2705   5039   -552    155   -327       C
ATOM    517  C   ARG A  62     -97.513  36.608 -16.183  1.00 28.05           C
ANISOU  517  C   ARG A  62     2505   2857   5296   -527    192   -468       C
ATOM    518  O   ARG A  62     -97.628  35.413 -16.466  1.00 31.70           O
ANISOU  518  O   ARG A  62     2877   3382   5786   -593    255   -580       O
ATOM    519  CB  ARG A  62     -95.272  37.629 -15.758  1.00 28.86           C
ANISOU  519  CB  ARG A  62     2922   2920   5122   -576    280   -288       C
ATOM    520  CG  ARG A  62     -94.655  36.672 -16.765  1.00 27.48           C
ANISOU  520  CG  ARG A  62     2785   2782   4874   -654    435   -384       C
ATOM    521  CD  ARG A  62     -93.224  37.054 -17.099  1.00 24.50           C
ANISOU  521  CD  ARG A  62     2606   2378   4326   -673    530   -325       C
ATOM    522  NE  ARG A  62     -92.598  36.077 -17.985  1.00 28.20           N
ANISOU  522  NE  ARG A  62     3150   2861   4702   -760    678   -405       N
ATOM    523  CZ  ARG A  62     -92.060  34.933 -17.575  1.00 30.97           C
ANISOU  523  CZ  ARG A  62     3543   3234   4989   -871    740   -432       C
ATOM    524  NH1 ARG A  62     -92.073  34.612 -16.288  1.00 30.90           N
ANISOU  524  NH1 ARG A  62     3500   3244   4998   -900    655   -390       N
ATOM    525  NH2 ARG A  62     -91.512  34.105 -18.453  1.00 35.06           N
ANISOU  525  NH2 ARG A  62     4150   3751   5419   -962    888   -504       N
ATOM    526  N   ASN A  63     -98.216  37.561 -16.788  1.00 31.37           N
ANISOU  526  N   ASN A  63     2895   3227   5796   -439    161   -473       N
ATOM    527  CA  ASN A  63     -99.137  37.237 -17.868  1.00 30.49           C
ANISOU  527  CA  ASN A  63     2653   3130   5802   -405    206   -612       C
ATOM    528  C   ASN A  63     -98.353  36.900 -19.131  1.00 29.41           C
ANISOU  528  C   ASN A  63     2593   3025   5556   -475    390   -686       C
ATOM    529  O   ASN A  63     -97.523  37.691 -19.589  1.00 31.71           O
ANISOU  529  O   ASN A  63     3034   3284   5730   -472    441   -623       O
ATOM    530  CB  ASN A  63    -100.083  38.409 -18.124  1.00 30.42           C
ANISOU  530  CB  ASN A  63     2616   3043   5900   -294    118   -594       C
ATOM    531  CG  ASN A  63    -101.340  37.994 -18.859  1.00 35.74           C
ANISOU  531  CG  ASN A  63     3122   3722   6736   -234    116   -741       C
ATOM    532  OD1 ASN A  63    -101.302  37.666 -20.045  1.00 38.48           O
ANISOU  532  OD1 ASN A  63     3448   4101   7070   -262    250   -855       O
ATOM    533  ND2 ASN A  63    -102.467  38.013 -18.157  1.00 37.48           N
ANISOU  533  ND2 ASN A  63     3233   3904   7105   -147    -37   -741       N
ATOM    534  N   ILE A  64     -98.612  35.722 -19.692  1.00 27.53           N
ANISOU  534  N   ILE A  64     2257   2850   5355   -539    490   -823       N
ATOM    535  CA  ILE A  64     -97.895  35.247 -20.868  1.00 27.64           C
ANISOU  535  CA  ILE A  64     2365   2888   5250   -626    679   -897       C
ATOM    536  C   ILE A  64     -98.766  35.323 -22.121  1.00 35.88           C
ANISOU  536  C   ILE A  64     3326   3933   6374   -588    752  -1029       C
ATOM    537  O   ILE A  64     -98.461  34.690 -23.130  1.00 35.15           O
ANISOU  537  O   ILE A  64     3278   3871   6206   -672    919  -1126       O
ATOM    538  CB  ILE A  64     -97.350  33.826 -20.653  1.00 30.80           C
ANISOU  538  CB  ILE A  64     2753   3353   5595   -767    783   -959       C
ATOM    539  CG1 ILE A  64     -98.500  32.841 -20.433  1.00 33.30           C
ANISOU  539  CG1 ILE A  64     2817   3741   6095   -776    754  -1100       C
ATOM    540  CG2 ILE A  64     -96.382  33.800 -19.477  1.00 29.55           C
ANISOU  540  CG2 ILE A  64     2710   3183   5334   -807    721   -831       C
ATOM    541  CD1 ILE A  64     -98.069  31.393 -20.429  1.00 34.70           C
ANISOU  541  CD1 ILE A  64     2952   3994   6237   -937    883  -1200       C
ATOM    542  N   LYS A  65     -99.848  36.084 -22.066  1.00 35.07           N
ANISOU  542  N   LYS A  65     3119   3791   6415   -470    634  -1037       N
ATOM    543  CA  LYS A  65    -100.710  36.346 -23.205  1.00 31.64           C
ANISOU  543  CA  LYS A  65     2620   3342   6059   -416    687  -1157       C
ATOM    544  C   LYS A  65    -100.483  37.765 -23.711  1.00 31.38           C
ANISOU  544  C   LYS A  65     2726   3235   5961   -350    649  -1080       C
ATOM    545  O   LYS A  65     -99.905  38.598 -23.004  1.00 32.06           O
ANISOU  545  O   LYS A  65     2909   3281   5990   -326    556   -937       O
ATOM    546  CB  LYS A  65    -102.182  36.154 -22.813  1.00 35.96           C
ANISOU  546  CB  LYS A  65     2944   3887   6832   -320    576  -1242       C
ATOM    547  CG  LYS A  65    -102.555  34.710 -22.520  1.00 44.99           C
ANISOU  547  CG  LYS A  65     3904   5122   8068   -377    616  -1365       C
ATOM    548  CD  LYS A  65    -103.844  34.615 -21.720  1.00 57.59           C
ANISOU  548  CD  LYS A  65     5297   6705   9878   -255    437  -1402       C
ATOM    549  CE  LYS A  65    -103.670  35.197 -20.325  1.00 62.78           C
ANISOU  549  CE  LYS A  65     6025   7308  10521   -206    242  -1222       C
ATOM    550  NZ  LYS A  65    -104.887  35.018 -19.484  1.00 64.93           N
ANISOU  550  NZ  LYS A  65     6129   7559  10984    -84     50  -1248       N
ATOM    551  N   PRO A  66    -100.895  38.073 -24.943  1.00 32.77           N
ANISOU  551  N   PRO A  66     2914   3397   6140   -326    725  -1180       N
ATOM    552  CA  PRO A  66    -100.781  39.458 -25.427  1.00 28.08           C
ANISOU  552  CA  PRO A  66     2431   2736   5501   -261    670  -1124       C
ATOM    553  C   PRO A  66    -101.546  40.410 -24.522  1.00 28.41           C
ANISOU  553  C   PRO A  66     2403   2708   5685   -167    492  -1045       C
ATOM    554  O   PRO A  66    -102.744  40.242 -24.284  1.00 32.82           O
ANISOU  554  O   PRO A  66     2816   3241   6414   -104    427  -1110       O
ATOM    555  CB  PRO A  66    -101.388  39.392 -26.833  1.00 29.11           C
ANISOU  555  CB  PRO A  66     2550   2868   5642   -253    777  -1279       C
ATOM    556  CG  PRO A  66    -101.207  37.980 -27.251  1.00 30.34           C
ANISOU  556  CG  PRO A  66     2674   3101   5753   -353    944  -1387       C
ATOM    557  CD  PRO A  66    -101.361  37.160 -26.002  1.00 31.61           C
ANISOU  557  CD  PRO A  66     2696   3300   6013   -374    883  -1357       C
ATOM    558  N   VAL A  67    -100.838  41.407 -24.003  1.00 30.32           N
ANISOU  558  N   VAL A  67     2752   2914   5853   -159    417   -907       N
ATOM    559  CA  VAL A  67    -101.425  42.361 -23.065  1.00 31.36           C
ANISOU  559  CA  VAL A  67     2851   2972   6091    -97    265   -815       C
ATOM    560  C   VAL A  67    -101.142  43.769 -23.566  1.00 30.67           C
ANISOU  560  C   VAL A  67     2857   2836   5959    -76    237   -777       C
ATOM    561  O   VAL A  67    -100.210  43.990 -24.357  1.00 31.24           O
ANISOU  561  O   VAL A  67     3033   2943   5893   -104    310   -786       O
ATOM    562  CB  VAL A  67    -100.880  42.159 -21.631  1.00 30.71           C
ANISOU  562  CB  VAL A  67     2789   2901   5977   -127    198   -682       C
ATOM    563  CG1 VAL A  67    -101.373  40.842 -21.058  1.00 31.46           C
ANISOU  563  CG1 VAL A  67     2767   3040   6147   -139    188   -731       C
ATOM    564  CG2 VAL A  67     -99.365  42.209 -21.630  1.00 24.84           C
ANISOU  564  CG2 VAL A  67     2184   2203   5050   -191    270   -609       C
ATOM    565  N   PRO A  68    -101.944  44.747 -23.141  1.00 32.75           N
ANISOU  565  N   PRO A  68     3091   3015   6338    -27    127   -740       N
ATOM    566  CA  PRO A  68    -101.649  46.140 -23.490  1.00 32.19           C
ANISOU  566  CA  PRO A  68     3092   2904   6235    -25     95   -706       C
ATOM    567  C   PRO A  68    -100.283  46.561 -22.973  1.00 33.60           C
ANISOU  567  C   PRO A  68     3360   3127   6279    -70    104   -592       C
ATOM    568  O   PRO A  68     -99.806  46.077 -21.944  1.00 33.07           O
ANISOU  568  O   PRO A  68     3304   3086   6176    -98     96   -504       O
ATOM    569  CB  PRO A  68    -102.770  46.924 -22.800  1.00 27.98           C
ANISOU  569  CB  PRO A  68     2516   2261   5855     14    -21   -668       C
ATOM    570  CG  PRO A  68    -103.882  45.949 -22.673  1.00 28.09           C
ANISOU  570  CG  PRO A  68     2428   2252   5994     67    -43   -741       C
ATOM    571  CD  PRO A  68    -103.235  44.618 -22.441  1.00 27.72           C
ANISOU  571  CD  PRO A  68     2354   2307   5870     31     27   -746       C
ATOM    572  N   GLU A  69     -99.648  47.469 -23.707  1.00 31.29           N
ANISOU  572  N   GLU A  69     3131   2847   5912    -71    115   -605       N
ATOM    573  CA  GLU A  69     -98.377  48.015 -23.262  1.00 28.67           C
ANISOU  573  CA  GLU A  69     2867   2556   5470    -94    114   -513       C
ATOM    574  C   GLU A  69     -98.581  48.874 -22.019  1.00 28.33           C
ANISOU  574  C   GLU A  69     2798   2466   5502   -114     40   -409       C
ATOM    575  O   GLU A  69     -99.623  49.510 -21.841  1.00 28.92           O
ANISOU  575  O   GLU A  69     2828   2461   5699   -108    -22   -415       O
ATOM    576  CB  GLU A  69     -97.722  48.824 -24.381  1.00 31.19           C
ANISOU  576  CB  GLU A  69     3243   2902   5706    -74    121   -567       C
ATOM    577  CG  GLU A  69     -97.145  47.953 -25.489  1.00 35.31           C
ANISOU  577  CG  GLU A  69     3849   3474   6094    -66    205   -639       C
ATOM    578  CD  GLU A  69     -96.487  48.756 -26.593  1.00 41.81           C
ANISOU  578  CD  GLU A  69     4748   4320   6818    -34    188   -688       C
ATOM    579  OE1 GLU A  69     -97.206  49.476 -27.318  1.00 48.02           O
ANISOU  579  OE1 GLU A  69     5504   5076   7666    -17    146   -767       O
ATOM    580  OE2 GLU A  69     -95.249  48.669 -26.734  1.00 45.40           O
ANISOU  580  OE2 GLU A  69     5300   4818   7132    -19    205   -651       O
ATOM    581  N   VAL A  70     -97.567  48.876 -21.151  1.00 31.46           N
ANISOU  581  N   VAL A  70     3237   2903   5814   -141     55   -315       N
ATOM    582  CA  VAL A  70     -97.700  49.494 -19.833  1.00 31.45           C
ANISOU  582  CA  VAL A  70     3230   2862   5859   -176      8   -210       C
ATOM    583  C   VAL A  70     -98.066  50.967 -19.959  1.00 32.01           C
ANISOU  583  C   VAL A  70     3274   2882   6005   -192    -34   -214       C
ATOM    584  O   VAL A  70     -98.861  51.493 -19.169  1.00 39.74           O
ANISOU  584  O   VAL A  70     4246   3782   7073   -223    -82   -160       O
ATOM    585  CB  VAL A  70     -96.406  49.296 -19.021  1.00 31.65           C
ANISOU  585  CB  VAL A  70     3312   2948   5763   -203     51   -127       C
ATOM    586  CG1 VAL A  70     -96.507  49.990 -17.673  1.00 35.27           C
ANISOU  586  CG1 VAL A  70     3779   3369   6252   -251     20    -24       C
ATOM    587  CG2 VAL A  70     -96.123  47.814 -18.837  1.00 26.71           C
ANISOU  587  CG2 VAL A  70     2717   2360   5071   -206     92   -127       C
ATOM    588  N   LYS A  71     -97.504  51.654 -20.958  1.00 27.98           N
ANISOU  588  N   LYS A  71     2759   2413   5457   -176    -22   -282       N
ATOM    589  CA  LYS A  71     -97.828  53.063 -21.160  1.00 27.96           C
ANISOU  589  CA  LYS A  71     2718   2374   5532   -204    -62   -308       C
ATOM    590  C   LYS A  71     -99.324  53.259 -21.374  1.00 31.93           C
ANISOU  590  C   LYS A  71     3196   2768   6169   -206   -111   -350       C
ATOM    591  O   LYS A  71     -99.904  54.241 -20.895  1.00 32.62           O
ANISOU  591  O   LYS A  71     3272   2778   6344   -258   -146   -322       O
ATOM    592  CB  LYS A  71     -97.034  53.622 -22.342  1.00 27.81           C
ANISOU  592  CB  LYS A  71     2694   2425   5448   -171    -61   -395       C
ATOM    593  CG  LYS A  71     -97.260  52.890 -23.655  1.00 26.78           C
ANISOU  593  CG  LYS A  71     2596   2307   5273   -116    -50   -495       C
ATOM    594  CD  LYS A  71     -96.451  53.507 -24.782  1.00 26.18           C
ANISOU  594  CD  LYS A  71     2540   2294   5113    -78    -71   -572       C
ATOM    595  CE  LYS A  71     -96.641  52.739 -26.080  1.00 27.54           C
ANISOU  595  CE  LYS A  71     2777   2474   5213    -34    -46   -666       C
ATOM    596  NZ  LYS A  71     -95.780  53.269 -27.173  1.00 30.94           N
ANISOU  596  NZ  LYS A  71     3260   2964   5533     13    -82   -733       N
ATOM    597  N   ILE A  72     -99.970  52.326 -22.076  1.00 30.45           N
ANISOU  597  N   ILE A  72     3004   2565   6000   -154   -106   -421       N
ATOM    598  CA  ILE A  72    -101.415  52.405 -22.268  1.00 31.69           C
ANISOU  598  CA  ILE A  72     3136   2612   6292   -135   -153   -471       C
ATOM    599  C   ILE A  72    -102.131  52.275 -20.930  1.00 32.40           C
ANISOU  599  C   ILE A  72     3237   2615   6458   -151   -202   -368       C
ATOM    600  O   ILE A  72    -103.021  53.068 -20.600  1.00 34.83           O
ANISOU  600  O   ILE A  72     3559   2807   6868   -172   -257   -349       O
ATOM    601  CB  ILE A  72    -101.883  51.328 -23.263  1.00 30.32           C
ANISOU  601  CB  ILE A  72     2944   2457   6119    -73   -120   -582       C
ATOM    602  CG1 ILE A  72    -101.263  51.566 -24.640  1.00 27.72           C
ANISOU  602  CG1 ILE A  72     2638   2195   5698    -63    -79   -684       C
ATOM    603  CG2 ILE A  72    -103.398  51.311 -23.353  1.00 27.03           C
ANISOU  603  CG2 ILE A  72     2492   1923   5854    -34   -170   -639       C
ATOM    604  CD1 ILE A  72    -101.764  52.816 -25.322  1.00 27.64           C
ANISOU  604  CD1 ILE A  72     2621   2128   5753    -74   -127   -756       C
ATOM    605  N   LEU A  73    -101.746  51.272 -20.137  1.00 33.23           N
ANISOU  605  N   LEU A  73     3352   2766   6506   -143   -189   -298       N
ATOM    606  CA  LEU A  73    -102.379  51.070 -18.838  1.00 29.28           C
ANISOU  606  CA  LEU A  73     2879   2189   6058   -151   -253   -196       C
ATOM    607  C   LEU A  73    -102.128  52.253 -17.913  1.00 27.05           C
ANISOU  607  C   LEU A  73     2656   1858   5763   -232   -263    -91       C
ATOM    608  O   LEU A  73    -103.007  52.637 -17.133  1.00 33.68           O
ANISOU  608  O   LEU A  73     3545   2578   6673   -248   -327    -25       O
ATOM    609  CB  LEU A  73    -101.870  49.775 -18.205  1.00 30.41           C
ANISOU  609  CB  LEU A  73     3021   2409   6126   -138   -237   -153       C
ATOM    610  CG  LEU A  73    -102.052  48.502 -19.035  1.00 31.76           C
ANISOU  610  CG  LEU A  73     3125   2638   6303    -83   -204   -262       C
ATOM    611  CD1 LEU A  73    -101.502  47.294 -18.295  1.00 32.41           C
ANISOU  611  CD1 LEU A  73     3207   2794   6313    -96   -188   -218       C
ATOM    612  CD2 LEU A  73    -103.515  48.293 -19.388  1.00 34.46           C
ANISOU  612  CD2 LEU A  73     3407   2891   6796    -12   -268   -341       C
ATOM    613  N   ASN A  74    -100.935  52.845 -17.986  1.00 29.06           N
ANISOU  613  N   ASN A  74     2912   2201   5928   -283   -198    -78       N
ATOM    614  CA  ASN A  74    -100.640  54.012 -17.163  1.00 28.69           C
ANISOU  614  CA  ASN A  74     2901   2124   5875   -373   -184      1       C
ATOM    615  C   ASN A  74    -101.491  55.204 -17.578  1.00 27.01           C
ANISOU  615  C   ASN A  74     2682   1809   5773   -414   -214    -43       C
ATOM    616  O   ASN A  74    -102.055  55.904 -16.728  1.00 29.05           O
ANISOU  616  O   ASN A  74     3001   1960   6075   -485   -232     32       O
ATOM    617  CB  ASN A  74     -99.154  54.358 -17.253  1.00 32.07           C
ANISOU  617  CB  ASN A  74     3305   2681   6198   -399   -109     -3       C
ATOM    618  CG  ASN A  74     -98.267  53.256 -16.715  1.00 36.24           C
ANISOU  618  CG  ASN A  74     3865   3293   6612   -373    -73     48       C
ATOM    619  OD1 ASN A  74     -98.715  52.401 -15.953  1.00 40.72           O
ANISOU  619  OD1 ASN A  74     4474   3825   7173   -365   -103    109       O
ATOM    620  ND2 ASN A  74     -96.998  53.274 -17.106  1.00 39.66           N
ANISOU  620  ND2 ASN A  74     4283   3833   6953   -356    -16     19       N
ATOM    621  N   ASN A  75    -101.598  55.447 -18.886  1.00 29.85           N
ANISOU  621  N   ASN A  75     2984   2190   6168   -378   -216   -166       N
ATOM    622  CA  ASN A  75    -102.370  56.587 -19.367  1.00 28.09           C
ANISOU  622  CA  ASN A  75     2754   1870   6048   -425   -244   -225       C
ATOM    623  C   ASN A  75    -103.837  56.477 -18.980  1.00 31.44           C
ANISOU  623  C   ASN A  75     3242   2123   6582   -408   -311   -197       C
ATOM    624  O   ASN A  75    -104.513  57.499 -18.815  1.00 40.15           O
ANISOU  624  O   ASN A  75     4386   3105   7765   -479   -332   -191       O
ATOM    625  CB  ASN A  75    -102.234  56.709 -20.882  1.00 30.24           C
ANISOU  625  CB  ASN A  75     2968   2201   6322   -378   -245   -370       C
ATOM    626  CG  ASN A  75    -100.814  56.998 -21.316  1.00 27.34           C
ANISOU  626  CG  ASN A  75     2553   1985   5851   -384   -204   -400       C
ATOM    627  OD1 ASN A  75    -100.005  57.502 -20.539  1.00 29.24           O
ANISOU  627  OD1 ASN A  75     2782   2277   6052   -442   -170   -333       O
ATOM    628  ND2 ASN A  75    -100.502  56.677 -22.564  1.00 27.09           N
ANISOU  628  ND2 ASN A  75     2501   2022   5770   -317   -206   -505       N
ATOM    629  N   LEU A  76    -104.344  55.258 -18.832  1.00 32.01           N
ANISOU  629  N   LEU A  76     3321   2178   6664   -314   -349   -186       N
ATOM    630  CA  LEU A  76    -105.711  55.036 -18.384  1.00 32.27           C
ANISOU  630  CA  LEU A  76     3410   2049   6800   -268   -432   -159       C
ATOM    631  C   LEU A  76    -105.840  55.037 -16.868  1.00 35.57           C
ANISOU  631  C   LEU A  76     3928   2395   7190   -310   -470     -2       C
ATOM    632  O   LEU A  76    -106.953  54.878 -16.356  1.00 38.17           O
ANISOU  632  O   LEU A  76     4330   2585   7589   -264   -557     40       O
ATOM    633  CB  LEU A  76    -106.239  53.715 -18.950  1.00 35.75           C
ANISOU  633  CB  LEU A  76     3790   2514   7280   -140   -462   -240       C
ATOM    634  CG  LEU A  76    -106.410  53.699 -20.469  1.00 38.64           C
ANISOU  634  CG  LEU A  76     4086   2915   7681    -95   -427   -403       C
ATOM    635  CD1 LEU A  76    -106.718  52.299 -20.970  1.00 40.53           C
ANISOU  635  CD1 LEU A  76     4253   3210   7935     10   -420   -487       C
ATOM    636  CD2 LEU A  76    -107.504  54.669 -20.882  1.00 41.06           C
ANISOU  636  CD2 LEU A  76     4431   3063   8108   -101   -473   -461       C
ATOM    637  N   GLY A  77    -104.739  55.215 -16.143  1.00 37.06           N
ANISOU  637  N   GLY A  77     4134   2679   7267   -390   -408     81       N
ATOM    638  CA  GLY A  77    -104.795  55.270 -14.697  1.00 37.49           C
ANISOU  638  CA  GLY A  77     4304   2671   7271   -445   -430    228       C
ATOM    639  C   GLY A  77    -104.985  53.941 -14.011  1.00 34.66           C
ANISOU  639  C   GLY A  77     3967   2327   6876   -358   -500    284       C
ATOM    640  O   GLY A  77    -105.498  53.906 -12.889  1.00 36.11           O
ANISOU  640  O   GLY A  77     4268   2408   7042   -372   -568    397       O
ATOM    641  N   VAL A  78    -104.587  52.840 -14.648  1.00 35.39           N
ANISOU  641  N   VAL A  78     3955   2542   6950   -277   -488    204       N
ATOM    642  CA  VAL A  78    -104.735  51.523 -14.041  1.00 35.39           C
ANISOU  642  CA  VAL A  78     3950   2573   6924   -206   -553    236       C
ATOM    643  C   VAL A  78    -103.807  51.414 -12.839  1.00 38.82           C
ANISOU  643  C   VAL A  78     4462   3067   7220   -281   -523    356       C
ATOM    644  O   VAL A  78    -102.617  51.746 -12.919  1.00 40.74           O
ANISOU  644  O   VAL A  78     4692   3417   7372   -348   -416    358       O
ATOM    645  CB  VAL A  78    -104.447  50.420 -15.068  1.00 38.20           C
ANISOU  645  CB  VAL A  78     4175   3052   7288   -132   -516    110       C
ATOM    646  CG1 VAL A  78    -104.453  49.056 -14.398  1.00 34.19           C
ANISOU  646  CG1 VAL A  78     3644   2598   6751    -84   -570    132       C
ATOM    647  CG2 VAL A  78    -105.467  50.466 -16.196  1.00 28.96           C
ANISOU  647  CG2 VAL A  78     2936   1816   6252    -54   -543    -16       C
ATOM    648  N   ASP A  79    -104.353  50.951 -11.715  1.00 38.04           N
ANISOU  648  N   ASP A  79     4452   2897   7104   -261   -623    450       N
ATOM    649  CA  ASP A  79    -103.591  50.802 -10.483  1.00 39.46           C
ANISOU  649  CA  ASP A  79     4729   3120   7143   -332   -605    565       C
ATOM    650  C   ASP A  79    -103.228  49.363 -10.157  1.00 38.11           C
ANISOU  650  C   ASP A  79     4512   3052   6915   -280   -644    552       C
ATOM    651  O   ASP A  79    -102.221  49.134  -9.483  1.00 40.11           O
ANISOU  651  O   ASP A  79     4811   3390   7038   -343   -587    605       O
ATOM    652  CB  ASP A  79    -104.372  51.386  -9.298  1.00 43.08           C
ANISOU  652  CB  ASP A  79     5363   3420   7584   -370   -691    697       C
ATOM    653  CG  ASP A  79    -104.743  52.840  -9.501  1.00 46.80           C
ANISOU  653  CG  ASP A  79     5900   3775   8107   -451   -641    716       C
ATOM    654  OD1 ASP A  79    -103.906  53.607 -10.023  1.00 50.23           O
ANISOU  654  OD1 ASP A  79     6274   4288   8523   -531   -510    672       O
ATOM    655  OD2 ASP A  79    -105.878  53.215  -9.137  1.00 51.85           O
ANISOU  655  OD2 ASP A  79     6653   4240   8806   -433   -739    770       O
ATOM    656  N   ILE A  80    -104.014  48.393 -10.623  1.00 32.73           N
ANISOU  656  N   ILE A  80     3734   2369   6332   -172   -735    470       N
ATOM    657  CA  ILE A  80    -103.842  47.003 -10.218  1.00 31.94           C
ANISOU  657  CA  ILE A  80     3581   2357   6196   -132   -790    451       C
ATOM    658  C   ILE A  80    -104.555  46.123 -11.232  1.00 31.30           C
ANISOU  658  C   ILE A  80     3337   2304   6252    -27   -825    307       C
ATOM    659  O   ILE A  80    -105.499  46.557 -11.895  1.00 36.76           O
ANISOU  659  O   ILE A  80     3991   2905   7070     38   -861    251       O
ATOM    660  CB  ILE A  80    -104.377  46.786  -8.780  1.00 37.70           C
ANISOU  660  CB  ILE A  80     4440   3007   6879   -121   -937    571       C
ATOM    661  CG1 ILE A  80    -103.814  45.505  -8.165  1.00 43.80           C
ANISOU  661  CG1 ILE A  80     5181   3894   7566   -124   -971    565       C
ATOM    662  CG2 ILE A  80    -105.896  46.769  -8.768  1.00 39.03           C
ANISOU  662  CG2 ILE A  80     4609   3033   7188     -4  -1102    561       C
ATOM    663  CD1 ILE A  80    -104.068  45.401  -6.674  1.00 31.75           C
ANISOU  663  CD1 ILE A  80     3814   2304   5945   -137  -1103    694       C
ATOM    664  N   ALA A  81    -104.092  44.883 -11.364  1.00 32.63           N
ANISOU  664  N   ALA A  81     3407   2597   6393    -20   -804    237       N
ATOM    665  CA  ALA A  81    -104.676  43.923 -12.287  1.00 29.64           C
ANISOU  665  CA  ALA A  81     2860   2268   6136     59   -811     86       C
ATOM    666  C   ALA A  81    -105.460  42.868 -11.518  1.00 36.71           C
ANISOU  666  C   ALA A  81     3693   3161   7094    136   -972     72       C
ATOM    667  O   ALA A  81    -105.136  42.539 -10.373  1.00 33.60           O
ANISOU  667  O   ALA A  81     3378   2783   6607    102  -1045    163       O
ATOM    668  CB  ALA A  81    -103.599  43.254 -13.145  1.00 28.43           C
ANISOU  668  CB  ALA A  81     2632   2257   5913     -2   -652     -6       C
ATOM    669  N   ALA A  82    -106.496  42.338 -12.165  1.00 39.25           N
ANISOU  669  N   ALA A  82     3869   3468   7577    244  -1030    -54       N
ATOM    670  CA  ALA A  82    -107.387  41.361 -11.548  1.00 41.45           C
ANISOU  670  CA  ALA A  82     4054   3745   7952    346  -1203    -94       C
ATOM    671  C   ALA A  82    -106.850  39.955 -11.795  1.00 42.52           C
ANISOU  671  C   ALA A  82     4027   4050   8079    306  -1139   -214       C
ATOM    672  O   ALA A  82    -106.932  39.439 -12.915  1.00 43.09           O
ANISOU  672  O   ALA A  82     3947   4194   8230    314  -1028   -367       O
ATOM    673  CB  ALA A  82    -108.805  41.507 -12.093  1.00 40.58           C
ANISOU  673  CB  ALA A  82     3856   3529   8034    495  -1299   -184       C
ATOM    674  N   ASN A  83    -106.293  39.342 -10.747  1.00 42.19           N
ANISOU  674  N   ASN A  83     4028   4069   7933    250  -1201   -149       N
ATOM    675  CA  ASN A  83    -105.904  37.930 -10.757  1.00 45.39           C
ANISOU  675  CA  ASN A  83     4283   4624   8339    206  -1175   -261       C
ATOM    676  C   ASN A  83    -104.860  37.632 -11.832  1.00 46.49           C
ANISOU  676  C   ASN A  83     4383   4869   8414     91   -937   -345       C
ATOM    677  O   ASN A  83    -104.877  36.572 -12.463  1.00 48.03           O
ANISOU  677  O   ASN A  83     4410   5167   8672     70   -865   -497       O
ATOM    678  CB  ASN A  83    -107.129  37.027 -10.920  1.00 53.48           C
ANISOU  678  CB  ASN A  83     5091   5670   9560    336  -1308   -407       C
ATOM    679  CG  ASN A  83    -108.211  37.328  -9.901  1.00 61.67           C
ANISOU  679  CG  ASN A  83     6186   6584  10662    476  -1567   -323       C
ATOM    680  OD1 ASN A  83    -109.181  38.027 -10.196  1.00 68.69           O
ANISOU  680  OD1 ASN A  83     7092   7346  11662    593  -1636   -319       O
ATOM    681  ND2 ASN A  83    -108.046  36.808  -8.689  1.00 61.43           N
ANISOU  681  ND2 ASN A  83     6207   6582  10553    462  -1715   -253       N
ATOM    682  N   THR A  84    -103.939  38.569 -12.037  1.00 44.69           N
ANISOU  682  N   THR A  84     4313   4612   8054     15   -814   -250       N
ATOM    683  CA  THR A  84    -102.831  38.372 -12.963  1.00 40.39           C
ANISOU  683  CA  THR A  84     3778   4149   7417    -86   -606   -304       C
ATOM    684  C   THR A  84    -101.742  39.377 -12.621  1.00 37.07           C
ANISOU  684  C   THR A  84     3552   3697   6836   -156   -538   -164       C
ATOM    685  O   THR A  84    -101.938  40.286 -11.811  1.00 40.41           O
ANISOU  685  O   THR A  84     4086   4036   7234   -134   -627    -40       O
ATOM    686  CB  THR A  84    -103.276  38.520 -14.423  1.00 37.35           C
ANISOU  686  CB  THR A  84     3298   3763   7129    -48   -500   -431       C
ATOM    687  OG1 THR A  84    -102.207  38.126 -15.294  1.00 37.08           O
ANISOU  687  OG1 THR A  84     3287   3811   6991   -147   -310   -489       O
ATOM    688  CG2 THR A  84    -103.652  39.960 -14.722  1.00 33.23           C
ANISOU  688  CG2 THR A  84     2868   3126   6631      8   -519   -362       C
ATOM    689  N   VAL A  85    -100.583  39.199 -13.251  1.00 33.10           N
ANISOU  689  N   VAL A  85     3094   3260   6222   -240   -374   -190       N
ATOM    690  CA  VAL A  85     -99.440  40.088 -13.075  1.00 27.66           C
ANISOU  690  CA  VAL A  85     2565   2556   5389   -294   -294    -84       C
ATOM    691  C   VAL A  85     -99.014  40.589 -14.445  1.00 26.51           C
ANISOU  691  C   VAL A  85     2428   2417   5228   -294   -160   -143       C
ATOM    692  O   VAL A  85     -98.597  39.798 -15.301  1.00 27.41           O
ANISOU  692  O   VAL A  85     2508   2594   5314   -331    -50   -239       O
ATOM    693  CB  VAL A  85     -98.268  39.391 -12.366  1.00 29.18           C
ANISOU  693  CB  VAL A  85     2841   2811   5435   -385   -244    -46       C
ATOM    694  CG1 VAL A  85     -97.027  40.268 -12.420  1.00 24.36           C
ANISOU  694  CG1 VAL A  85     2376   2193   4688   -423   -140     32       C
ATOM    695  CG2 VAL A  85     -98.631  39.085 -10.929  1.00 33.59           C
ANISOU  695  CG2 VAL A  85     3424   3357   5982   -387   -390     28       C
ATOM    696  N   ILE A  86     -99.116  41.897 -14.652  1.00 25.89           N
ANISOU  696  N   ILE A  86     2402   2273   5161   -260   -168    -89       N
ATOM    697  CA  ILE A  86     -98.584  42.539 -15.847  1.00 27.96           C
ANISOU  697  CA  ILE A  86     2693   2543   5387   -259    -62   -131       C
ATOM    698  C   ILE A  86     -97.116  42.846 -15.578  1.00 30.31           C
ANISOU  698  C   ILE A  86     3114   2875   5528   -312     16    -60       C
ATOM    699  O   ILE A  86     -96.791  43.662 -14.711  1.00 30.94           O
ANISOU  699  O   ILE A  86     3261   2926   5567   -323    -16     40       O
ATOM    700  CB  ILE A  86     -99.363  43.809 -16.201  1.00 27.81           C
ANISOU  700  CB  ILE A  86     2664   2443   5462   -205   -113   -121       C
ATOM    701  CG1 ILE A  86    -100.865  43.520 -16.242  1.00 30.27           C
ANISOU  701  CG1 ILE A  86     2869   2698   5934   -137   -211   -180       C
ATOM    702  CG2 ILE A  86     -98.886  44.368 -17.532  1.00 31.08           C
ANISOU  702  CG2 ILE A  86     3093   2874   5840   -199    -20   -188       C
ATOM    703  CD1 ILE A  86    -101.257  42.461 -17.248  1.00 25.82           C
ANISOU  703  CD1 ILE A  86     2193   2188   5429   -117   -152   -328       C
ATOM    704  N   TRP A  87     -96.225  42.188 -16.312  1.00 28.20           N
ANISOU  704  N   TRP A  87     2883   2663   5168   -343    124   -116       N
ATOM    705  CA  TRP A  87     -94.794  42.370 -16.119  1.00 30.61           C
ANISOU  705  CA  TRP A  87     3312   2994   5325   -375    196    -61       C
ATOM    706  C   TRP A  87     -94.300  43.503 -17.010  1.00 29.36           C
ANISOU  706  C   TRP A  87     3194   2824   5136   -332    232    -67       C
ATOM    707  O   TRP A  87     -94.503  43.476 -18.228  1.00 30.55           O
ANISOU  707  O   TRP A  87     3327   2978   5302   -307    269   -149       O
ATOM    708  CB  TRP A  87     -94.030  41.083 -16.422  1.00 30.37           C
ANISOU  708  CB  TRP A  87     3331   3010   5198   -433    290   -112       C
ATOM    709  CG  TRP A  87     -92.602  41.171 -16.015  1.00 27.26           C
ANISOU  709  CG  TRP A  87     3077   2625   4656   -458    348    -50       C
ATOM    710  CD1 TRP A  87     -91.529  41.398 -16.825  1.00 24.76           C
ANISOU  710  CD1 TRP A  87     2868   2308   4232   -440    429    -62       C
ATOM    711  CD2 TRP A  87     -92.087  41.065 -14.685  1.00 21.50           C
ANISOU  711  CD2 TRP A  87     2405   1897   3866   -494    322     30       C
ATOM    712  NE1 TRP A  87     -90.375  41.427 -16.082  1.00 26.04           N
ANISOU  712  NE1 TRP A  87     3142   2469   4281   -454    458      1       N
ATOM    713  CE2 TRP A  87     -90.691  41.225 -14.764  1.00 21.10           C
ANISOU  713  CE2 TRP A  87     2488   1848   3681   -494    401     56       C
ATOM    714  CE3 TRP A  87     -92.672  40.844 -13.435  1.00 21.87           C
ANISOU  714  CE3 TRP A  87     2417   1941   3953   -521    234     80       C
ATOM    715  CZ2 TRP A  87     -89.869  41.170 -13.642  1.00 26.53           C
ANISOU  715  CZ2 TRP A  87     3265   2535   4279   -524    410    121       C
ATOM    716  CZ3 TRP A  87     -91.856  40.790 -12.322  1.00 22.81           C
ANISOU  716  CZ3 TRP A  87     2635   2063   3968   -561    240    150       C
ATOM    717  CH2 TRP A  87     -90.470  40.953 -12.432  1.00 21.36           C
ANISOU  717  CH2 TRP A  87     2575   1883   3658   -564    335    167       C
ATOM    718  N   ASP A  88     -93.655  44.496 -16.401  1.00 27.42           N
ANISOU  718  N   ASP A  88     3001   2570   4847   -325    220     12       N
ATOM    719  CA  ASP A  88     -93.064  45.612 -17.136  1.00 27.21           C
ANISOU  719  CA  ASP A  88     2998   2547   4794   -281    241      1       C
ATOM    720  C   ASP A  88     -91.656  45.197 -17.539  1.00 26.67           C
ANISOU  720  C   ASP A  88     3040   2514   4581   -272    320     -9       C
ATOM    721  O   ASP A  88     -90.737  45.191 -16.717  1.00 24.20           O
ANISOU  721  O   ASP A  88     2794   2212   4188   -285    345     49       O
ATOM    722  CB  ASP A  88     -93.060  46.880 -16.290  1.00 29.56           C
ANISOU  722  CB  ASP A  88     3280   2825   5127   -285    202     73       C
ATOM    723  CG  ASP A  88     -92.689  48.120 -17.086  1.00 35.77           C
ANISOU  723  CG  ASP A  88     4045   3622   5925   -243    204     39       C
ATOM    724  OD1 ASP A  88     -92.075  47.990 -18.167  1.00 38.29           O
ANISOU  724  OD1 ASP A  88     4397   3968   6182   -198    234    -22       O
ATOM    725  OD2 ASP A  88     -93.011  49.234 -16.623  1.00 40.77           O
ANISOU  725  OD2 ASP A  88     4634   4234   6624   -260    173     71       O
ATOM    726  N   TYR A  89     -91.487  44.842 -18.814  1.00 29.36           N
ANISOU  726  N   TYR A  89     3414   2861   4879   -248    361    -83       N
ATOM    727  CA  TYR A  89     -90.178  44.427 -19.300  1.00 29.57           C
ANISOU  727  CA  TYR A  89     3578   2899   4757   -232    430    -90       C
ATOM    728  C   TYR A  89     -89.233  45.604 -19.496  1.00 34.78           C
ANISOU  728  C   TYR A  89     4276   3568   5369   -155    407    -70       C
ATOM    729  O   TYR A  89     -88.017  45.400 -19.559  1.00 36.58           O
ANISOU  729  O   TYR A  89     4624   3797   5477   -123    445    -55       O
ATOM    730  CB  TYR A  89     -90.330  43.648 -20.605  1.00 28.98           C
ANISOU  730  CB  TYR A  89     3554   2821   4637   -241    487   -174       C
ATOM    731  CG  TYR A  89     -90.888  42.254 -20.423  1.00 31.59           C
ANISOU  731  CG  TYR A  89     3860   3157   4986   -326    541   -210       C
ATOM    732  CD1 TYR A  89     -90.051  41.145 -20.443  1.00 32.09           C
ANISOU  732  CD1 TYR A  89     4046   3218   4929   -386    630   -214       C
ATOM    733  CD2 TYR A  89     -92.248  42.045 -20.226  1.00 29.81           C
ANISOU  733  CD2 TYR A  89     3486   2936   4905   -347    500   -247       C
ATOM    734  CE1 TYR A  89     -90.552  39.869 -20.278  1.00 30.91           C
ANISOU  734  CE1 TYR A  89     3853   3085   4806   -479    684   -264       C
ATOM    735  CE2 TYR A  89     -92.757  40.770 -20.061  1.00 30.25           C
ANISOU  735  CE2 TYR A  89     3490   3010   4993   -418    541   -297       C
ATOM    736  CZ  TYR A  89     -91.904  39.686 -20.087  1.00 33.19           C
ANISOU  736  CZ  TYR A  89     3967   3395   5249   -491    636   -309       C
ATOM    737  OH  TYR A  89     -92.400  38.412 -19.922  1.00 30.60           O
ANISOU  737  OH  TYR A  89     3569   3097   4962   -577    682   -375       O
ATOM    738  N   LYS A  90     -89.762  46.825 -19.598  1.00 36.27           N
ANISOU  738  N   LYS A  90     4364   3762   5655   -123    343    -78       N
ATOM    739  CA  LYS A  90     -88.896  47.996 -19.685  1.00 35.12           C
ANISOU  739  CA  LYS A  90     4216   3641   5486    -56    316    -73       C
ATOM    740  C   LYS A  90     -88.151  48.224 -18.376  1.00 32.68           C
ANISOU  740  C   LYS A  90     3917   3347   5152    -69    340     -3       C
ATOM    741  O   LYS A  90     -86.957  48.543 -18.381  1.00 35.14           O
ANISOU  741  O   LYS A  90     4284   3679   5386     -5    356     -1       O
ATOM    742  CB  LYS A  90     -89.719  49.229 -20.060  1.00 36.30           C
ANISOU  742  CB  LYS A  90     4242   3794   5757    -45    250   -109       C
ATOM    743  CG  LYS A  90     -90.404  49.118 -21.410  1.00 41.70           C
ANISOU  743  CG  LYS A  90     4924   4463   6456    -24    226   -191       C
ATOM    744  CD  LYS A  90     -89.390  49.133 -22.541  1.00 45.49           C
ANISOU  744  CD  LYS A  90     5511   4964   6810     55    224   -238       C
ATOM    745  CE  LYS A  90     -89.999  48.615 -23.832  1.00 51.80           C
ANISOU  745  CE  LYS A  90     6359   5744   7580     56    234   -314       C
ATOM    746  NZ  LYS A  90     -91.268  49.314 -24.168  1.00 54.36           N
ANISOU  746  NZ  LYS A  90     6561   6054   8039     36    183   -368       N
ATOM    747  N   ARG A  91     -88.837  48.061 -17.245  1.00 29.06           N
ANISOU  747  N   ARG A  91     3412   2874   4754   -144    340     52       N
ATOM    748  CA  ARG A  91     -88.218  48.196 -15.936  1.00 29.40           C
ANISOU  748  CA  ARG A  91     3482   2928   4759   -173    373    118       C
ATOM    749  C   ARG A  91     -87.794  46.863 -15.335  1.00 28.04           C
ANISOU  749  C   ARG A  91     3418   2745   4493   -214    418    149       C
ATOM    750  O   ARG A  91     -87.171  46.860 -14.267  1.00 29.68           O
ANISOU  750  O   ARG A  91     3672   2959   4647   -236    452    197       O
ATOM    751  CB  ARG A  91     -89.174  48.901 -14.964  1.00 29.64           C
ANISOU  751  CB  ARG A  91     3430   2942   4890   -238    342    168       C
ATOM    752  CG  ARG A  91     -89.651  50.265 -15.427  1.00 28.91           C
ANISOU  752  CG  ARG A  91     3232   2853   4901   -226    305    136       C
ATOM    753  CD  ARG A  91     -90.578  50.911 -14.401  1.00 30.47           C
ANISOU  753  CD  ARG A  91     3385   3012   5181   -308    287    195       C
ATOM    754  NE  ARG A  91     -91.689  50.037 -14.028  1.00 34.54           N
ANISOU  754  NE  ARG A  91     3922   3472   5731   -347    241    231       N
ATOM    755  CZ  ARG A  91     -91.849  49.498 -12.823  1.00 31.58           C
ANISOU  755  CZ  ARG A  91     3607   3076   5317   -400    240    306       C
ATOM    756  NH1 ARG A  91     -90.974  49.750 -11.859  1.00 30.90           N
ANISOU  756  NH1 ARG A  91     3575   3016   5149   -431    298    354       N
ATOM    757  NH2 ARG A  91     -92.889  48.714 -12.577  1.00 32.06           N
ANISOU  757  NH2 ARG A  91     3670   3091   5420   -416    175    325       N
ATOM    758  N   ASP A  92     -88.106  45.744 -15.991  1.00 25.78           N
ANISOU  758  N   ASP A  92     3169   2442   4183   -233    428    113       N
ATOM    759  CA  ASP A  92     -87.853  44.407 -15.452  1.00 27.88           C
ANISOU  759  CA  ASP A  92     3519   2700   4376   -295    470    127       C
ATOM    760  C   ASP A  92     -88.448  44.270 -14.053  1.00 26.81           C
ANISOU  760  C   ASP A  92     3344   2563   4280   -363    436    187       C
ATOM    761  O   ASP A  92     -87.811  43.786 -13.116  1.00 26.95           O
ANISOU  761  O   ASP A  92     3441   2582   4216   -402    466    224       O
ATOM    762  CB  ASP A  92     -86.357  44.085 -15.453  1.00 33.59           C
ANISOU  762  CB  ASP A  92     4388   3416   4959   -265    537    132       C
ATOM    763  CG  ASP A  92     -85.795  43.927 -16.853  1.00 44.79           C
ANISOU  763  CG  ASP A  92     5890   4817   6310   -203    563     78       C
ATOM    764  OD1 ASP A  92     -86.520  43.410 -17.731  1.00 48.05           O
ANISOU  764  OD1 ASP A  92     6281   5225   6750   -230    565     30       O
ATOM    765  OD2 ASP A  92     -84.630  44.318 -17.077  1.00 48.84           O
ANISOU  765  OD2 ASP A  92     6498   5321   6739   -123    580     80       O
ATOM    766  N   ALA A  93     -89.693  44.714 -13.920  1.00 23.81           N
ANISOU  766  N   ALA A  93     2856   2172   4018   -375    366    197       N
ATOM    767  CA  ALA A  93     -90.382  44.757 -12.641  1.00 22.04           C
ANISOU  767  CA  ALA A  93     2611   1933   3832   -426    311    262       C
ATOM    768  C   ALA A  93     -91.873  44.643 -12.901  1.00 21.80           C
ANISOU  768  C   ALA A  93     2479   1874   3931   -426    228    242       C
ATOM    769  O   ALA A  93     -92.329  44.889 -14.024  1.00 22.65           O
ANISOU  769  O   ALA A  93     2524   1976   4107   -386    224    180       O
ATOM    770  CB  ALA A  93     -90.064  46.053 -11.880  1.00 23.01           C
ANISOU  770  CB  ALA A  93     2742   2052   3950   -426    320    322       C
ATOM    771  N   PRO A  94     -92.661  44.257 -11.898  1.00 25.50           N
ANISOU  771  N   PRO A  94     2936   2321   4433   -463    154    287       N
ATOM    772  CA  PRO A  94     -94.116  44.248 -12.081  1.00 25.62           C
ANISOU  772  CA  PRO A  94     2858   2296   4582   -440     60    268       C
ATOM    773  C   PRO A  94     -94.639  45.658 -12.307  1.00 30.92           C
ANISOU  773  C   PRO A  94     3499   2917   5331   -414     36    292       C
ATOM    774  O   PRO A  94     -94.147  46.625 -11.723  1.00 32.52           O
ANISOU  774  O   PRO A  94     3752   3112   5493   -438     64    354       O
ATOM    775  CB  PRO A  94     -94.639  43.651 -10.770  1.00 25.21           C
ANISOU  775  CB  PRO A  94     2832   2227   4520   -475    -29    328       C
ATOM    776  CG  PRO A  94     -93.545  43.881  -9.784  1.00 27.44           C
ANISOU  776  CG  PRO A  94     3232   2528   4668   -525     24    400       C
ATOM    777  CD  PRO A  94     -92.276  43.757 -10.566  1.00 26.83           C
ANISOU  777  CD  PRO A  94     3186   2496   4511   -518    142    350       C
ATOM    778  N   ALA A  95     -95.648  45.767 -13.172  1.00 33.90           N
ANISOU  778  N   ALA A  95     3792   3263   5827   -372     -7    231       N
ATOM    779  CA  ALA A  95     -96.178  47.076 -13.530  1.00 22.57           C
ANISOU  779  CA  ALA A  95     2330   1774   4473   -355    -27    236       C
ATOM    780  C   ALA A  95     -96.955  47.727 -12.393  1.00 24.86           C
ANISOU  780  C   ALA A  95     2659   1984   4804   -385   -102    330       C
ATOM    781  O   ALA A  95     -97.126  48.950 -12.401  1.00 24.75           O
ANISOU  781  O   ALA A  95     2651   1924   4827   -406    -94    354       O
ATOM    782  CB  ALA A  95     -97.068  46.963 -14.769  1.00 22.76           C
ANISOU  782  CB  ALA A  95     2267   1776   4606   -302    -50    136       C
ATOM    783  N   HIS A  96     -97.424  46.951 -11.418  1.00 24.84           N
ANISOU  783  N   HIS A  96     2691   1959   4788   -394   -176    381       N
ATOM    784  CA  HIS A  96     -98.253  47.479 -10.346  1.00 25.05           C
ANISOU  784  CA  HIS A  96     2787   1892   4839   -415   -264    477       C
ATOM    785  C   HIS A  96     -97.738  46.999  -8.997  1.00 28.45           C
ANISOU  785  C   HIS A  96     3322   2344   5145   -467   -277    564       C
ATOM    786  O   HIS A  96     -97.169  45.911  -8.880  1.00 31.50           O
ANISOU  786  O   HIS A  96     3701   2803   5466   -468   -265    535       O
ATOM    787  CB  HIS A  96     -99.718  47.073 -10.529  1.00 27.94           C
ANISOU  787  CB  HIS A  96     3100   2179   5336   -346   -392    448       C
ATOM    788  CG  HIS A  96    -100.256  47.379 -11.891  1.00 26.08           C
ANISOU  788  CG  HIS A  96     2764   1927   5220   -292   -376    345       C
ATOM    789  ND1 HIS A  96    -100.562  46.398 -12.808  1.00 26.43           N
ANISOU  789  ND1 HIS A  96     2699   2016   5326   -233   -378    232       N
ATOM    790  CD2 HIS A  96    -100.525  48.559 -12.498  1.00 25.64           C
ANISOU  790  CD2 HIS A  96     2702   1814   5225   -299   -349    329       C
ATOM    791  CE1 HIS A  96    -101.007  46.959 -13.919  1.00 30.94           C
ANISOU  791  CE1 HIS A  96     3214   2558   5984   -198   -354    154       C
ATOM    792  NE2 HIS A  96    -100.992  48.270 -13.757  1.00 25.55           N
ANISOU  792  NE2 HIS A  96     2592   1813   5305   -236   -344    210       N
ATOM    793  N   ILE A  97     -97.953  47.826  -7.977  1.00 36.64           N
ANISOU  793  N   ILE A  97     4469   3312   6142   -520   -297    667       N
ATOM    794  CA  ILE A  97     -97.455  47.563  -6.631  1.00 41.90           C
ANISOU  794  CA  ILE A  97     5263   3989   6669   -581   -300    756       C
ATOM    795  C   ILE A  97     -98.093  46.298  -6.068  1.00 42.58           C
ANISOU  795  C   ILE A  97     5359   4068   6751   -542   -441    763       C
ATOM    796  O   ILE A  97     -97.416  45.288  -5.845  1.00 41.71           O
ANISOU  796  O   ILE A  97     5244   4040   6565   -553   -428    734       O
ATOM    797  CB  ILE A  97     -97.725  48.764  -5.706  1.00 47.84           C
ANISOU  797  CB  ILE A  97     6144   4652   7380   -655   -287    863       C
ATOM    798  CG1 ILE A  97     -97.268  50.068  -6.364  1.00 51.44           C
ANISOU  798  CG1 ILE A  97     6550   5117   7877   -695   -159    832       C
ATOM    799  CG2 ILE A  97     -97.045  48.567  -4.360  1.00 49.19           C
ANISOU  799  CG2 ILE A  97     6460   4845   7383   -729   -258    946       C
ATOM    800  CD1 ILE A  97     -97.661  51.308  -5.585  1.00 53.12           C
ANISOU  800  CD1 ILE A  97     6874   5234   8073   -788   -130    921       C
ATOM    801  N   SER A  98     -99.397  46.350  -5.826  1.00 41.14           N
ANISOU  801  N   SER A  98     5192   3785   6653   -493   -584    797       N
ATOM    802  CA  SER A  98    -100.102  45.261  -5.173  1.00 37.33           C
ANISOU  802  CA  SER A  98     4719   3290   6174   -443   -748    807       C
ATOM    803  C   SER A  98    -100.713  44.318  -6.204  1.00 35.03           C
ANISOU  803  C   SER A  98     4242   3037   6029   -349   -806    679       C
ATOM    804  O   SER A  98    -100.716  44.581  -7.408  1.00 34.07           O
ANISOU  804  O   SER A  98     4012   2933   6000   -323   -724    594       O
ATOM    805  CB  SER A  98    -101.180  45.814  -4.243  1.00 38.99           C
ANISOU  805  CB  SER A  98     5072   3358   6385   -428   -889    919       C
ATOM    806  OG  SER A  98    -100.622  46.701  -3.289  1.00 35.53           O
ANISOU  806  OG  SER A  98     4814   2884   5802   -534   -812   1033       O
ATOM    807  N   THR A  99    -101.233  43.198  -5.710  1.00 34.28           N
ANISOU  807  N   THR A  99     4110   2962   5952   -302   -949    656       N
ATOM    808  CA  THR A  99    -101.867  42.185  -6.538  1.00 36.34           C
ANISOU  808  CA  THR A  99     4181   3272   6356   -219  -1007    523       C
ATOM    809  C   THR A  99    -103.194  41.780  -5.911  1.00 37.66           C
ANISOU  809  C   THR A  99     4338   3362   6610   -116  -1232    538       C
ATOM    810  O   THR A  99    -103.503  42.129  -4.768  1.00 38.00           O
ANISOU  810  O   THR A  99     4544   3322   6573   -118  -1349    660       O
ATOM    811  CB  THR A  99    -100.963  40.956  -6.716  1.00 35.50           C
ANISOU  811  CB  THR A  99     3989   3306   6194   -271   -935    434       C
ATOM    812  OG1 THR A  99    -100.509  40.503  -5.434  1.00 38.24           O
ANISOU  812  OG1 THR A  99     4451   3677   6403   -327  -1002    507       O
ATOM    813  CG2 THR A  99     -99.762  41.296  -7.585  1.00 29.79           C
ANISOU  813  CG2 THR A  99     3267   2644   5410   -340   -725    400       C
ATOM    814  N   ILE A 100    -103.985  41.037  -6.681  1.00 36.70           N
ANISOU  814  N   ILE A 100     4028   3266   6650    -21  -1292    408       N
ATOM    815  CA  ILE A 100    -105.281  40.533  -6.242  1.00 37.55           C
ANISOU  815  CA  ILE A 100     4082   3312   6872    108  -1517    390       C
ATOM    816  C   ILE A 100    -105.314  39.042  -6.541  1.00 39.10           C
ANISOU  816  C   ILE A 100     4064   3646   7145    134  -1550    236       C
ATOM    817  O   ILE A 100    -105.333  38.641  -7.711  1.00 37.09           O
ANISOU  817  O   ILE A 100     3633   3460   6998    145  -1438     95       O
ATOM    818  CB  ILE A 100    -106.451  41.250  -6.929  1.00 42.39           C
ANISOU  818  CB  ILE A 100     4663   3797   7647    222  -1566    365       C
ATOM    819  CG1 ILE A 100    -106.469  42.731  -6.550  1.00 42.10           C
ANISOU  819  CG1 ILE A 100     4846   3615   7535    176  -1537    515       C
ATOM    820  CG2 ILE A 100    -107.769  40.588  -6.559  1.00 43.01           C
ANISOU  820  CG2 ILE A 100     4662   3820   7860    380  -1805    321       C
ATOM    821  CD1 ILE A 100    -107.510  43.541  -7.293  1.00 41.53           C
ANISOU  821  CD1 ILE A 100     4761   3406   7612    262  -1560    488       C
ATOM    822  N   GLY A 101    -105.319  38.224  -5.493  1.00 41.89           N
ANISOU  822  N   GLY A 101     4434   4044   7440    134  -1699    256       N
ATOM    823  CA  GLY A 101    -105.396  36.780  -5.665  1.00 44.45           C
ANISOU  823  CA  GLY A 101     4541   4504   7844    147  -1746    102       C
ATOM    824  C   GLY A 101    -104.254  36.188  -6.460  1.00 46.00           C
ANISOU  824  C   GLY A 101     4647   4835   7996     15  -1517      2       C
ATOM    825  O   GLY A 101    -104.476  35.300  -7.292  1.00 47.49           O
ANISOU  825  O   GLY A 101     4620   5116   8309     26  -1467   -163       O
ATOM    826  N   VAL A 102    -103.031  36.661  -6.224  1.00 44.48           N
ANISOU  826  N   VAL A 102     4623   4652   7625   -110  -1372     96       N
ATOM    827  CA  VAL A 102    -101.865  36.185  -6.961  1.00 41.64           C
ANISOU  827  CA  VAL A 102     4223   4396   7202   -230  -1157     20       C
ATOM    828  C   VAL A 102    -100.788  35.720  -5.991  1.00 38.89           C
ANISOU  828  C   VAL A 102     4000   4102   6674   -346  -1141     75       C
ATOM    829  O   VAL A 102    -100.445  34.533  -5.947  1.00 41.04           O
ANISOU  829  O   VAL A 102     4176   4476   6941   -412  -1131    -26       O
ATOM    830  CB  VAL A 102    -101.316  37.274  -7.901  1.00 42.22           C
ANISOU  830  CB  VAL A 102     4372   4425   7245   -254   -969     55       C
ATOM    831  CG1 VAL A 102    -100.015  36.811  -8.530  1.00 42.31           C
ANISOU  831  CG1 VAL A 102     4393   4525   7159   -369   -765     -1       C
ATOM    832  CG2 VAL A 102    -102.337  37.619  -8.973  1.00 44.20           C
ANISOU  832  CG2 VAL A 102     4494   4631   7671   -151   -969    -25       C
ATOM    833  N   CYS A 103    -100.244  36.652  -5.212  1.00 37.72           N
ANISOU  833  N   CYS A 103     4066   3887   6378   -381  -1128    226       N
ATOM    834  CA  CYS A 103     -99.150  36.373  -4.292  1.00 38.30           C
ANISOU  834  CA  CYS A 103     4286   4000   6266   -491  -1091    283       C
ATOM    835  C   CYS A 103     -99.538  36.837  -2.898  1.00 38.90           C
ANISOU  835  C   CYS A 103     4531   4003   6246   -469  -1259    418       C
ATOM    836  O   CYS A 103     -99.898  38.003  -2.710  1.00 43.73           O
ANISOU  836  O   CYS A 103     5257   4511   6846   -429  -1271    528       O
ATOM    837  CB  CYS A 103     -97.862  37.068  -4.741  1.00 40.15           C
ANISOU  837  CB  CYS A 103     4635   4234   6387   -569   -867    322       C
ATOM    838  SG  CYS A 103     -96.564  37.110  -3.489  1.00 44.80           S
ANISOU  838  SG  CYS A 103     5446   4835   6740   -681   -816    416       S
ATOM    839  N   SER A 104     -99.440  35.929  -1.923  1.00 37.57           N
ANISOU  839  N   SER A 104     4390   3885   6000   -506  -1384    409       N
ATOM    840  CA  SER A 104     -99.882  36.239  -0.566  1.00 46.93           C
ANISOU  840  CA  SER A 104     5751   5002   7080   -482  -1569    532       C
ATOM    841  C   SER A 104     -99.127  37.422   0.026  1.00 50.05           C
ANISOU  841  C   SER A 104     6392   5326   7299   -552  -1448    678       C
ATOM    842  O   SER A 104     -99.680  38.160   0.850  1.00 57.34           O
ANISOU  842  O   SER A 104     7479   6150   8159   -521  -1555    803       O
ATOM    843  CB  SER A 104     -99.720  35.013   0.331  1.00 57.72           C
ANISOU  843  CB  SER A 104     7110   6451   8371   -528  -1709    482       C
ATOM    844  OG  SER A 104    -100.459  33.913  -0.171  1.00 70.33           O
ANISOU  844  OG  SER A 104     8454   8126  10144   -467  -1824    331       O
ATOM    845  N   MET A 105     -97.873  37.623  -0.378  1.00 44.95           N
ANISOU  845  N   MET A 105     5780   4725   6574   -644  -1225    662       N
ATOM    846  CA  MET A 105     -97.091  38.720   0.177  1.00 46.70           C
ANISOU  846  CA  MET A 105     6207   4897   6641   -709  -1097    778       C
ATOM    847  C   MET A 105     -97.505  40.070  -0.396  1.00 40.99           C
ANISOU  847  C   MET A 105     5493   4086   5994   -664  -1026    839       C
ATOM    848  O   MET A 105     -97.412  41.086   0.301  1.00 41.18           O
ANISOU  848  O   MET A 105     5690   4039   5918   -700   -992    953       O
ATOM    849  CB  MET A 105     -95.600  38.475  -0.061  1.00 56.46           C
ANISOU  849  CB  MET A 105     7471   6206   7776   -802   -894    730       C
ATOM    850  CG  MET A 105     -94.694  39.478   0.634  1.00 66.54           C
ANISOU  850  CG  MET A 105     8946   7449   8887   -868   -761    828       C
ATOM    851  SD  MET A 105     -94.968  39.551   2.416  1.00 69.89           S
ANISOU  851  SD  MET A 105     9606   7825   9124   -916   -904    946       S
ATOM    852  CE  MET A 105     -94.141  38.062   2.954  1.00 62.19           C
ANISOU  852  CE  MET A 105     8648   6946   8035   -992   -933    859       C
ATOM    853  N   THR A 106     -97.969  40.107  -1.647  1.00 37.86           N
ANISOU  853  N   THR A 106     4919   3693   5771   -597   -995    759       N
ATOM    854  CA  THR A 106     -98.389  41.350  -2.278  1.00 34.82           C
ANISOU  854  CA  THR A 106     4532   3228   5470   -559   -934    799       C
ATOM    855  C   THR A 106     -99.897  41.477  -2.434  1.00 37.30           C
ANISOU  855  C   THR A 106     4788   3453   5932   -452  -1107    805       C
ATOM    856  O   THR A 106    -100.370  42.547  -2.833  1.00 35.73           O
ANISOU  856  O   THR A 106     4611   3166   5799   -426  -1075    846       O
ATOM    857  CB  THR A 106     -97.737  41.499  -3.660  1.00 33.21           C
ANISOU  857  CB  THR A 106     4199   3081   5340   -560   -756    704       C
ATOM    858  OG1 THR A 106     -98.091  40.380  -4.482  1.00 35.82           O
ANISOU  858  OG1 THR A 106     4350   3474   5786   -516   -794    577       O
ATOM    859  CG2 THR A 106     -96.227  41.568  -3.530  1.00 27.66           C
ANISOU  859  CG2 THR A 106     3576   2441   4493   -646   -585    707       C
ATOM    860  N   ASP A 107    -100.661  40.428  -2.137  1.00 41.21           N
ANISOU  860  N   ASP A 107     5206   3966   6486   -386  -1291    758       N
ATOM    861  CA  ASP A 107    -102.109  40.496  -2.280  1.00 37.88           C
ANISOU  861  CA  ASP A 107     4725   3454   6214   -259  -1470    754       C
ATOM    862  C   ASP A 107    -102.705  41.452  -1.258  1.00 38.94           C
ANISOU  862  C   ASP A 107     5088   3442   6267   -250  -1577    913       C
ATOM    863  O   ASP A 107    -102.443  41.340  -0.056  1.00 41.90           O
ANISOU  863  O   ASP A 107     5636   3806   6479   -301  -1648   1004       O
ATOM    864  CB  ASP A 107    -102.735  39.112  -2.116  1.00 37.58           C
ANISOU  864  CB  ASP A 107     4537   3482   6259   -184  -1655    655       C
ATOM    865  CG  ASP A 107    -102.757  38.323  -3.409  1.00 40.45           C
ANISOU  865  CG  ASP A 107     4642   3946   6782   -156  -1572    481       C
ATOM    866  OD1 ASP A 107    -102.362  38.877  -4.455  1.00 40.24           O
ANISOU  866  OD1 ASP A 107     4569   3923   6795   -182  -1389    446       O
ATOM    867  OD2 ASP A 107    -103.168  37.144  -3.375  1.00 43.78           O
ANISOU  867  OD2 ASP A 107     4906   4444   7284   -113  -1689    373       O
ATOM    868  N   ILE A 108    -103.505  42.404  -1.744  1.00 38.77           N
ANISOU  868  N   ILE A 108     5082   3300   6350   -194  -1582    944       N
ATOM    869  CA  ILE A 108    -104.379  43.176  -0.867  1.00 44.71           C
ANISOU  869  CA  ILE A 108     6046   3885   7058   -164  -1718   1083       C
ATOM    870  C   ILE A 108    -105.767  42.563  -0.780  1.00 46.72           C
ANISOU  870  C   ILE A 108     6242   4064   7445      1  -1977   1054       C
ATOM    871  O   ILE A 108    -106.538  42.921   0.123  1.00 44.41           O
ANISOU  871  O   ILE A 108     6148   3629   7096     46  -2145   1173       O
ATOM    872  CB  ILE A 108    -104.499  44.640  -1.334  1.00 46.41           C
ANISOU  872  CB  ILE A 108     6342   3987   7305   -210  -1582   1141       C
ATOM    873  CG1 ILE A 108    -105.044  44.701  -2.761  1.00 40.88           C
ANISOU  873  CG1 ILE A 108     5431   3284   6815   -123  -1547   1017       C
ATOM    874  CG2 ILE A 108    -103.155  45.344  -1.238  1.00 47.72           C
ANISOU  874  CG2 ILE A 108     6577   4222   7333   -365  -1347   1177       C
ATOM    875  CD1 ILE A 108    -105.276  46.104  -3.257  1.00 37.54           C
ANISOU  875  CD1 ILE A 108     5077   2747   6439   -164  -1438   1058       C
ATOM    876  N   ALA A 109    -106.106  41.647  -1.685  1.00 49.91           N
ANISOU  876  N   ALA A 109     6386   4556   8021     95  -2013    896       N
ATOM    877  CA  ALA A 109    -107.401  40.983  -1.693  1.00 50.86           C
ANISOU  877  CA  ALA A 109     6403   4626   8296    270  -2253    836       C
ATOM    878  C   ALA A 109    -107.279  39.713  -2.524  1.00 45.83           C
ANISOU  878  C   ALA A 109     5460   4158   7794    310  -2232    641       C
ATOM    879  O   ALA A 109    -106.305  39.514  -3.252  1.00 39.14           O
ANISOU  879  O   ALA A 109     4506   3433   6931    207  -2021    564       O
ATOM    880  CB  ALA A 109    -108.498  41.899  -2.244  1.00 41.51           C
ANISOU  880  CB  ALA A 109     5252   3269   7250    372  -2292    856       C
ATOM    881  N   LYS A 110    -108.288  38.851  -2.404  1.00 51.48           N
ANISOU  881  N   LYS A 110     6041   4876   8643    461  -2455    558       N
ATOM    882  CA  LYS A 110    -108.331  37.622  -3.186  1.00 56.34           C
ANISOU  882  CA  LYS A 110     6347   5650   9411    500  -2439    356       C
ATOM    883  C   LYS A 110    -109.148  37.779  -4.463  1.00 54.03           C
ANISOU  883  C   LYS A 110     5868   5323   9338    610  -2388    229       C
ATOM    884  O   LYS A 110    -108.772  37.236  -5.508  1.00 48.59           O
ANISOU  884  O   LYS A 110     4969   4759   8734    567  -2221     78       O
ATOM    885  CB  LYS A 110    -108.901  36.477  -2.344  1.00 68.23           C
ANISOU  885  CB  LYS A 110     7765   7211  10949    597  -2708    303       C
ATOM    886  CG  LYS A 110    -108.032  36.079  -1.161  1.00 78.01           C
ANISOU  886  CG  LYS A 110     9154   8516  11971    478  -2755    389       C
ATOM    887  CD  LYS A 110    -108.636  34.901  -0.412  1.00 89.95           C
ANISOU  887  CD  LYS A 110    10552  10095  13531    580  -3038    313       C
ATOM    888  CE  LYS A 110    -107.740  34.447   0.731  1.00 94.03           C
ANISOU  888  CE  LYS A 110    11216  10686  13825    451  -3082    382       C
ATOM    889  NZ  LYS A 110    -108.316  33.279   1.455  1.00 96.93           N
ANISOU  889  NZ  LYS A 110    11461  11130  14238    546  -3374    296       N
ATOM    890  N   LYS A 111    -110.256  38.510  -4.400  1.00 56.70           N
ANISOU  890  N   LYS A 111     6296   5486   9763    746  -2523    287       N
ATOM    891  CA  LYS A 111    -111.111  38.759  -5.548  1.00 55.91           C
ANISOU  891  CA  LYS A 111     6049   5327   9867    860  -2485    172       C
ATOM    892  C   LYS A 111    -111.353  40.253  -5.699  1.00 56.25           C
ANISOU  892  C   LYS A 111     6314   5182   9878    844  -2422    301       C
ATOM    893  O   LYS A 111    -111.314  40.995  -4.712  1.00 56.87           O
ANISOU  893  O   LYS A 111     6657   5137   9813    804  -2495    481       O
ATOM    894  CB  LYS A 111    -112.451  38.020  -5.412  1.00 57.74           C
ANISOU  894  CB  LYS A 111     6128   5522  10289   1080  -2744     69       C
ATOM    895  CG  LYS A 111    -112.413  36.600  -5.958  1.00 59.25           C
ANISOU  895  CG  LYS A 111     5982   5916  10614   1105  -2727   -152       C
ATOM    896  CD  LYS A 111    -113.707  35.851  -5.690  1.00 66.46           C
ANISOU  896  CD  LYS A 111     6781   6830  11642   1284  -2931   -265       C
ATOM    897  CE  LYS A 111    -113.834  35.473  -4.224  1.00 72.19           C
ANISOU  897  CE  LYS A 111     7643   7539  12245   1321  -3185   -158       C
ATOM    898  NZ  LYS A 111    -115.039  34.634  -3.971  1.00 76.32           N
ANISOU  898  NZ  LYS A 111     8047   8092  12858   1482  -3358   -287       N
ATOM    899  N   PRO A 112    -111.595  40.725  -6.927  1.00 56.93           N
ANISOU  899  N   PRO A 112     6303   5241  10086    861  -2278    208       N
ATOM    900  CA  PRO A 112    -111.730  42.176  -7.141  1.00 56.41           C
ANISOU  900  CA  PRO A 112     6435   5009   9990    818  -2197    315       C
ATOM    901  C   PRO A 112    -112.936  42.793  -6.456  1.00 62.10           C
ANISOU  901  C   PRO A 112     7344   5499  10753    946  -2412    421       C
ATOM    902  O   PRO A 112    -112.949  44.013  -6.251  1.00 66.07           O
ANISOU  902  O   PRO A 112     8070   5857  11176    871  -2358    550       O
ATOM    903  CB  PRO A 112    -111.841  42.300  -8.669  1.00 52.48           C
ANISOU  903  CB  PRO A 112     5756   4551   9633    832  -2028    154       C
ATOM    904  CG  PRO A 112    -111.294  41.015  -9.207  1.00 54.36           C
ANISOU  904  CG  PRO A 112     5745   5004   9905    810  -1945     -4       C
ATOM    905  CD  PRO A 112    -111.644  39.974  -8.192  1.00 55.89           C
ANISOU  905  CD  PRO A 112     5886   5241  10107    893  -2158     -4       C
ATOM    906  N   THR A 113    -113.943  42.003  -6.093  1.00 61.69           N
ANISOU  906  N   THR A 113     7219   5446  10773   1105  -2614    355       N
ATOM    907  CA  THR A 113    -115.155  42.533  -5.480  1.00 63.49           C
ANISOU  907  CA  THR A 113     7644   5518  10962   1196  -2762    425       C
ATOM    908  C   THR A 113    -114.970  42.928  -4.021  1.00 62.83           C
ANISOU  908  C   THR A 113     7856   5344  10670   1136  -2879    631       C
ATOM    909  O   THR A 113    -115.921  43.431  -3.412  1.00 68.98           O
ANISOU  909  O   THR A 113     8836   5983  11389   1199  -2994    708       O
ATOM    910  CB  THR A 113    -116.290  41.511  -5.586  1.00 67.34           C
ANISOU  910  CB  THR A 113     7952   6053  11580   1383  -2924    269       C
ATOM    911  OG1 THR A 113    -115.821  40.225  -5.158  1.00 67.10           O
ANISOU  911  OG1 THR A 113     7751   6188  11556   1400  -3014    205       O
ATOM    912  CG2 THR A 113    -116.790  41.418  -7.018  1.00 67.95           C
ANISOU  912  CG2 THR A 113     7809   6171  11837   1441  -2794     77       C
ATOM    913  N   GLU A 114    -113.789  42.720  -3.448  1.00 56.58           N
ANISOU  913  N   GLU A 114     7111   4627   9760   1015  -2845    720       N
ATOM    914  CA  GLU A 114    -113.575  43.054  -2.049  1.00 61.12           C
ANISOU  914  CA  GLU A 114     7978   5130  10114    943  -2938    907       C
ATOM    915  C   GLU A 114    -113.543  44.568  -1.849  1.00 63.18           C
ANISOU  915  C   GLU A 114     8516   5245  10246    813  -2795   1050       C
ATOM    916  O   GLU A 114    -113.386  45.349  -2.793  1.00 62.57           O
ANISOU  916  O   GLU A 114     8391   5143  10241    749  -2611   1012       O
ATOM    917  CB  GLU A 114    -112.287  42.409  -1.536  1.00 63.51           C
ANISOU  917  CB  GLU A 114     8255   5563  10314    837  -2921    953       C
ATOM    918  CG  GLU A 114    -112.476  40.968  -1.079  1.00 70.28           C
ANISOU  918  CG  GLU A 114     8946   6550  11206    948  -3131    861       C
ATOM    919  CD  GLU A 114    -111.167  40.256  -0.799  1.00 72.39           C
ANISOU  919  CD  GLU A 114     9138   7030  11335    790  -3008    832       C
ATOM    920  OE1 GLU A 114    -110.767  39.402  -1.618  1.00 71.36           O
ANISOU  920  OE1 GLU A 114     8724   7078  11312    778  -2906    662       O
ATOM    921  OE2 GLU A 114    -110.536  40.553   0.237  1.00 73.14           O
ANISOU  921  OE2 GLU A 114     9472   7110  11210    673  -3006    977       O
ATOM    922  N   THR A 115    -113.698  44.975  -0.587  1.00 64.39           N
ANISOU  922  N   THR A 115     8957   5310  10198    766  -2876   1204       N
ATOM    923  CA  THR A 115    -113.864  46.389  -0.263  1.00 63.57           C
ANISOU  923  CA  THR A 115     9122   5067   9965    649  -2749   1329       C
ATOM    924  C   THR A 115    -112.607  47.192  -0.576  1.00 63.57           C
ANISOU  924  C   THR A 115     9140   5119   9895    440  -2484   1372       C
ATOM    925  O   THR A 115    -112.695  48.327  -1.059  1.00 63.68           O
ANISOU  925  O   THR A 115     9214   5062   9918    355  -2320   1383       O
ATOM    926  CB  THR A 115    -114.243  46.539   1.211  1.00 65.96           C
ANISOU  926  CB  THR A 115     9727   5281  10054    640  -2882   1475       C
ATOM    927  OG1 THR A 115    -115.511  45.915   1.446  1.00 72.68           O
ANISOU  927  OG1 THR A 115    10567   6070  10979    844  -3128   1429       O
ATOM    928  CG2 THR A 115    -114.325  48.009   1.605  1.00 65.92           C
ANISOU  928  CG2 THR A 115     9997   5144   9906    494  -2720   1600       C
ATOM    929  N   ILE A 116    -111.430  46.617  -0.320  1.00 59.44           N
ANISOU  929  N   ILE A 116     8558   4722   9302    355  -2440   1389       N
ATOM    930  CA  ILE A 116    -110.181  47.351  -0.482  1.00 55.19           C
ANISOU  930  CA  ILE A 116     8049   4243   8677    156  -2189   1431       C
ATOM    931  C   ILE A 116    -109.945  47.759  -1.931  1.00 52.42           C
ANISOU  931  C   ILE A 116     7489   3925   8503    139  -2022   1314       C
ATOM    932  O   ILE A 116    -109.171  48.686  -2.194  1.00 51.83           O
ANISOU  932  O   ILE A 116     7444   3877   8373    -15  -1806   1335       O
ATOM    933  CB  ILE A 116    -109.004  46.511   0.061  1.00 52.90           C
ANISOU  933  CB  ILE A 116     7729   4092   8277     84  -2182   1455       C
ATOM    934  CG1 ILE A 116    -107.786  47.397   0.332  1.00 51.14           C
ANISOU  934  CG1 ILE A 116     7617   3923   7892   -129  -1928   1524       C
ATOM    935  CG2 ILE A 116    -108.650  45.391  -0.905  1.00 50.02           C
ANISOU  935  CG2 ILE A 116     7033   3925   8049    156  -2154   1271       C
ATOM    936  CD1 ILE A 116    -108.031  48.467   1.375  1.00 52.95           C
ANISOU  936  CD1 ILE A 116     8140   4050   7927   -230  -1872   1653       C
ATOM    937  N   CYS A 117    -110.607  47.103  -2.881  1.00 52.94           N
ANISOU  937  N   CYS A 117     7336   4000   8777    296  -2111   1179       N
ATOM    938  CA  CYS A 117    -110.427  47.397  -4.296  1.00 54.49           C
ANISOU  938  CA  CYS A 117     7333   4243   9129    288  -1956   1049       C
ATOM    939  C   CYS A 117    -111.329  48.517  -4.794  1.00 58.35           C
ANISOU  939  C   CYS A 117     7898   4605   9667    295  -1907   1035       C
ATOM    940  O   CYS A 117    -111.272  48.852  -5.982  1.00 58.94           O
ANISOU  940  O   CYS A 117     7826   4704   9863    290  -1789    926       O
ATOM    941  CB  CYS A 117    -110.678  46.138  -5.131  1.00 56.75           C
ANISOU  941  CB  CYS A 117     7331   4662   9569    430  -2014    870       C
ATOM    942  SG  CYS A 117    -109.713  44.705  -4.622  1.00 58.61           S
ANISOU  942  SG  CYS A 117     7437   5128   9703    404  -2029    827       S
ATOM    943  N   ALA A 118    -112.152  49.101  -3.925  1.00 59.65           N
ANISOU  943  N   ALA A 118     8295   4639   9730    302  -1989   1138       N
ATOM    944  CA  ALA A 118    -113.112  50.108  -4.377  1.00 55.22           C
ANISOU  944  CA  ALA A 118     7816   3945   9221    316  -1953   1121       C
ATOM    945  C   ALA A 118    -112.446  51.363  -4.930  1.00 52.15           C
ANISOU  945  C   ALA A 118     7448   3562   8803    140  -1718   1122       C
ATOM    946  O   ALA A 118    -112.789  51.765  -6.056  1.00 51.74           O
ANISOU  946  O   ALA A 118     7282   3493   8883    164  -1654   1014       O
ATOM    947  CB  ALA A 118    -114.087  50.433  -3.240  1.00 55.59           C
ANISOU  947  CB  ALA A 118     8130   3840   9152    356  -2086   1241       C
ATOM    948  N   PRO A 119    -111.513  52.023  -4.238  1.00 54.11           N
ANISOU  948  N   PRO A 119     7826   3844   8890    -36  -1581   1224       N
ATOM    949  CA  PRO A 119    -110.920  53.247  -4.793  1.00 58.12           C
ANISOU  949  CA  PRO A 119     8328   4369   9387   -196  -1363   1202       C
ATOM    950  C   PRO A 119    -109.912  53.006  -5.906  1.00 56.62           C
ANISOU  950  C   PRO A 119     7891   4333   9291   -225  -1247   1086       C
ATOM    951  O   PRO A 119    -109.351  53.978  -6.427  1.00 54.35           O
ANISOU  951  O   PRO A 119     7571   4081   8999   -348  -1079   1053       O
ATOM    952  CB  PRO A 119    -110.232  53.890  -3.572  1.00 62.79           C
ANISOU  952  CB  PRO A 119     9122   4963   9771   -363  -1255   1336       C
ATOM    953  CG  PRO A 119    -110.705  53.113  -2.375  1.00 63.64           C
ANISOU  953  CG  PRO A 119     9387   5021   9773   -281  -1434   1438       C
ATOM    954  CD  PRO A 119    -110.980  51.748  -2.892  1.00 57.23           C
ANISOU  954  CD  PRO A 119     8384   4264   9098   -101  -1612   1352       C
ATOM    955  N   LEU A 120    -109.665  51.756  -6.287  1.00 56.02           N
ANISOU  955  N   LEU A 120     7639   4348   9299   -116  -1330   1019       N
ATOM    956  CA  LEU A 120    -108.620  51.420  -7.242  1.00 48.81           C
ANISOU  956  CA  LEU A 120     6515   3578   8451   -146  -1213    920       C
ATOM    957  C   LEU A 120    -109.210  51.156  -8.619  1.00 41.42           C
ANISOU  957  C   LEU A 120     5395   2643   7700    -32  -1228    763       C
ATOM    958  O   LEU A 120    -110.309  50.609  -8.743  1.00 40.40           O
ANISOU  958  O   LEU A 120     5240   2444   7668    114  -1370    717       O
ATOM    959  CB  LEU A 120    -107.835  50.193  -6.775  1.00 45.33           C
ANISOU  959  CB  LEU A 120     6003   3277   7943   -123  -1246    927       C
ATOM    960  CG  LEU A 120    -107.128  50.310  -5.426  1.00 47.06           C
ANISOU  960  CG  LEU A 120     6400   3514   7968   -235  -1226   1069       C
ATOM    961  CD1 LEU A 120    -106.508  48.980  -5.042  1.00 46.52           C
ANISOU  961  CD1 LEU A 120     6247   3603   7825   -194  -1271   1043       C
ATOM    962  CD2 LEU A 120    -106.072  51.402  -5.467  1.00 47.41           C
ANISOU  962  CD2 LEU A 120     6477   3611   7925   -406  -1015   1095       C
ATOM    963  N   THR A 121    -108.467  51.546  -9.652  1.00 38.00           N
ANISOU  963  N   THR A 121     4835   2299   7306    -96  -1079    673       N
ATOM    964  CA  THR A 121    -108.835  51.260 -11.036  1.00 38.10           C
ANISOU  964  CA  THR A 121     4671   2345   7458     -5  -1061    510       C
ATOM    965  C   THR A 121    -108.260  49.894 -11.391  1.00 38.07           C
ANISOU  965  C   THR A 121     4497   2529   7439     60  -1046    421       C
ATOM    966  O   THR A 121    -107.074  49.766 -11.703  1.00 38.78           O
ANISOU  966  O   THR A 121     4521   2774   7440    -15   -918    394       O
ATOM    967  CB  THR A 121    -108.321  52.349 -11.972  1.00 38.12           C
ANISOU  967  CB  THR A 121     4636   2379   7470   -106   -912    448       C
ATOM    968  OG1 THR A 121    -108.887  53.611 -11.595  1.00 41.62           O
ANISOU  968  OG1 THR A 121     5231   2713   7870   -182   -900    511       O
ATOM    969  CG2 THR A 121    -108.704  52.038 -13.412  1.00 33.94           C
ANISOU  969  CG2 THR A 121     3948   1881   7066    -16   -894    277       C
ATOM    970  N   VAL A 122    -109.102  48.871 -11.335  1.00 38.06           N
ANISOU  970  N   VAL A 122     4426   2508   7527    199  -1179    370       N
ATOM    971  CA  VAL A 122    -108.690  47.492 -11.563  1.00 34.79           C
ANISOU  971  CA  VAL A 122     3849   2261   7109    250  -1174    280       C
ATOM    972  C   VAL A 122    -108.725  47.200 -13.055  1.00 35.91           C
ANISOU  972  C   VAL A 122     3817   2480   7346    291  -1074    105       C
ATOM    973  O   VAL A 122    -109.660  47.594 -13.758  1.00 38.78           O
ANISOU  973  O   VAL A 122     4156   2740   7839    364  -1102     29       O
ATOM    974  CB  VAL A 122    -109.597  46.521 -10.783  1.00 35.75           C
ANISOU  974  CB  VAL A 122     3955   2336   7291    379  -1369    291       C
ATOM    975  CG1 VAL A 122    -109.148  45.082 -10.988  1.00 35.21           C
ANISOU  975  CG1 VAL A 122     3704   2450   7223    409  -1354    186       C
ATOM    976  CG2 VAL A 122    -109.609  46.877  -9.305  1.00 36.54           C
ANISOU  976  CG2 VAL A 122     4267   2343   7274    338  -1476    472       C
ATOM    977  N   PHE A 123    -107.705  46.504 -13.547  1.00 35.32           N
ANISOU  977  N   PHE A 123     3640   2580   7200    241   -955     39       N
ATOM    978  CA  PHE A 123    -107.652  46.104 -14.947  1.00 36.31           C
ANISOU  978  CA  PHE A 123     3621   2789   7386    267   -850   -125       C
ATOM    979  C   PHE A 123    -108.299  44.735 -15.107  1.00 38.77           C
ANISOU  979  C   PHE A 123     3774   3156   7799    370   -909   -243       C
ATOM    980  O   PHE A 123    -107.903  43.773 -14.439  1.00 39.10           O
ANISOU  980  O   PHE A 123     3777   3291   7790    357   -940   -223       O
ATOM    981  CB  PHE A 123    -106.213  46.077 -15.452  1.00 35.57           C
ANISOU  981  CB  PHE A 123     3523   2840   7154    159   -687   -136       C
ATOM    982  CG  PHE A 123    -106.073  45.499 -16.827  1.00 37.84           C
ANISOU  982  CG  PHE A 123     3689   3218   7469    176   -576   -296       C
ATOM    983  CD1 PHE A 123    -106.492  46.213 -17.937  1.00 35.65           C
ANISOU  983  CD1 PHE A 123     3399   2890   7255    198   -530   -383       C
ATOM    984  CD2 PHE A 123    -105.523  44.243 -17.011  1.00 43.80           C
ANISOU  984  CD2 PHE A 123     4357   4106   8179    159   -512   -363       C
ATOM    985  CE1 PHE A 123    -106.365  45.683 -19.204  1.00 35.63           C
ANISOU  985  CE1 PHE A 123     3310   2969   7258    208   -422   -530       C
ATOM    986  CE2 PHE A 123    -105.394  43.708 -18.277  1.00 42.98           C
ANISOU  986  CE2 PHE A 123     4167   4080   8085    158   -393   -508       C
ATOM    987  CZ  PHE A 123    -105.815  44.431 -19.374  1.00 39.77           C
ANISOU  987  CZ  PHE A 123     3760   3623   7730    186   -348   -589       C
ATOM    988  N   PHE A 124    -109.287  44.647 -15.993  1.00 41.36           N
ANISOU  988  N   PHE A 124     4005   3434   8275    469   -921   -376       N
ATOM    989  CA  PHE A 124    -110.005  43.410 -16.260  1.00 37.77           C
ANISOU  989  CA  PHE A 124     3370   3035   7946    575   -965   -518       C
ATOM    990  C   PHE A 124    -109.734  42.950 -17.685  1.00 35.67           C
ANISOU  990  C   PHE A 124     2979   2880   7696    551   -791   -691       C
ATOM    991  O   PHE A 124    -109.609  43.770 -18.601  1.00 33.70           O
ANISOU  991  O   PHE A 124     2780   2596   7427    518   -696   -724       O
ATOM    992  CB  PHE A 124    -111.511  43.588 -16.047  1.00 39.45           C
ANISOU  992  CB  PHE A 124     3569   3088   8333    734  -1132   -548       C
ATOM    993  CG  PHE A 124    -111.885  43.978 -14.645  1.00 37.61           C
ANISOU  993  CG  PHE A 124     3486   2728   8077    768  -1317   -377       C
ATOM    994  CD1 PHE A 124    -112.127  43.012 -13.682  1.00 38.67           C
ANISOU  994  CD1 PHE A 124     3566   2900   8227    836  -1464   -354       C
ATOM    995  CD2 PHE A 124    -112.004  45.313 -14.293  1.00 41.82           C
ANISOU  995  CD2 PHE A 124     4221   3103   8566    724  -1343   -244       C
ATOM    996  CE1 PHE A 124    -112.475  43.370 -12.391  1.00 39.63           C
ANISOU  996  CE1 PHE A 124     3855   2897   8304    868  -1642   -193       C
ATOM    997  CE2 PHE A 124    -112.352  45.677 -13.006  1.00 38.51           C
ANISOU  997  CE2 PHE A 124     3970   2557   8107    742  -1499    -83       C
ATOM    998  CZ  PHE A 124    -112.588  44.705 -12.053  1.00 39.55           C
ANISOU  998  CZ  PHE A 124     4068   2721   8239    818  -1653    -52       C
ATOM    999  N   ASP A 125    -109.648  41.634 -17.865  1.00 38.34           N
ANISOU  999  N   ASP A 125     3157   3349   8063    558   -749   -804       N
ATOM   1000  CA  ASP A 125    -109.361  41.016 -19.156  1.00 41.62           C
ANISOU 1000  CA  ASP A 125     3461   3877   8475    517   -568   -971       C
ATOM   1001  C   ASP A 125    -110.578  40.203 -19.574  1.00 41.58           C
ANISOU 1001  C   ASP A 125     3258   3877   8665    644   -604  -1153       C
ATOM   1002  O   ASP A 125    -110.847  39.143 -19.000  1.00 46.55           O
ANISOU 1002  O   ASP A 125     3747   4576   9365    684   -674  -1203       O
ATOM   1003  CB  ASP A 125    -108.110  40.140 -19.072  1.00 44.49           C
ANISOU 1003  CB  ASP A 125     3813   4396   8695    388   -452   -962       C
ATOM   1004  CG  ASP A 125    -107.667  39.609 -20.427  1.00 43.90           C
ANISOU 1004  CG  ASP A 125     3682   4424   8576    319   -245  -1111       C
ATOM   1005  OD1 ASP A 125    -108.370  39.844 -21.432  1.00 45.63           O
ANISOU 1005  OD1 ASP A 125     3851   4606   8880    376   -191  -1235       O
ATOM   1006  OD2 ASP A 125    -106.605  38.955 -20.484  1.00 41.88           O
ANISOU 1006  OD2 ASP A 125     3448   4276   8191    204   -133  -1104       O
ATOM   1007  N   GLY A 126    -111.302  40.692 -20.582  1.00 43.25           N
ANISOU 1007  N   GLY A 126     3450   4018   8966    709   -554  -1265       N
ATOM   1008  CA  GLY A 126    -112.496  40.009 -21.049  1.00 43.60           C
ANISOU 1008  CA  GLY A 126     3355   4079   9132    802   -570  -1431       C
ATOM   1009  C   GLY A 126    -112.246  38.613 -21.577  1.00 46.08           C
ANISOU 1009  C   GLY A 126     3498   4568   9442    745   -431  -1591       C
ATOM   1010  O   GLY A 126    -113.185  37.815 -21.667  1.00 50.33           O
ANISOU 1010  O   GLY A 126     3910   5146  10067    810   -464  -1716       O
ATOM   1011  N   ARG A 127    -110.998  38.297 -21.929  1.00 46.86           N
ANISOU 1011  N   ARG A 127     3597   4772   9437    617   -269  -1592       N
ATOM   1012  CA  ARG A 127    -110.654  36.960 -22.395  1.00 46.99           C
ANISOU 1012  CA  ARG A 127     3480   4951   9423    527   -117  -1732       C
ATOM   1013  C   ARG A 127    -110.703  35.919 -21.286  1.00 50.31           C
ANISOU 1013  C   ARG A 127     3790   5448   9876    528   -229  -1717       C
ATOM   1014  O   ARG A 127    -110.690  34.720 -21.586  1.00 54.28           O
ANISOU 1014  O   ARG A 127     4168   6077  10377    465   -128  -1851       O
ATOM   1015  CB  ARG A 127    -109.264  36.978 -23.031  1.00 46.90           C
ANISOU 1015  CB  ARG A 127     3569   5014   9236    368     81  -1706       C
ATOM   1016  CG  ARG A 127    -109.121  37.986 -24.160  1.00 48.97           C
ANISOU 1016  CG  ARG A 127     3977   5212   9416    353    183  -1716       C
ATOM   1017  CD  ARG A 127    -107.677  38.119 -24.609  1.00 45.51           C
ANISOU 1017  CD  ARG A 127     3714   4832   8744    200    326  -1637       C
ATOM   1018  NE  ARG A 127    -106.818  38.632 -23.546  1.00 42.21           N
ANISOU 1018  NE  ARG A 127     3430   4389   8220    161    221  -1431       N
ATOM   1019  CZ  ARG A 127    -105.536  38.937 -23.708  1.00 39.34           C
ANISOU 1019  CZ  ARG A 127     3233   4054   7662     57    300  -1333       C
ATOM   1020  NH1 ARG A 127    -104.961  38.783 -24.893  1.00 37.03           N
ANISOU 1020  NH1 ARG A 127     3013   3807   7249    -17    472  -1410       N
ATOM   1021  NH2 ARG A 127    -104.827  39.399 -22.687  1.00 40.89           N
ANISOU 1021  NH2 ARG A 127     3532   4228   7778     32    208  -1160       N
ATOM   1022  N   VAL A 128    -110.756  36.340 -20.027  1.00 48.09           N
ANISOU 1022  N   VAL A 128     3562   5092   9616    591   -433  -1560       N
ATOM   1023  CA  VAL A 128    -110.861  35.435 -18.889  1.00 48.41           C
ANISOU 1023  CA  VAL A 128     3515   5195   9682    607   -574  -1538       C
ATOM   1024  C   VAL A 128    -112.318  35.369 -18.457  1.00 52.93           C
ANISOU 1024  C   VAL A 128     4037   5692  10382    774   -766  -1577       C
ATOM   1025  O   VAL A 128    -113.019  36.389 -18.441  1.00 55.82           O
ANISOU 1025  O   VAL A 128     4508   5909  10791    875   -864  -1513       O
ATOM   1026  CB  VAL A 128    -109.953  35.894 -17.732  1.00 46.04           C
ANISOU 1026  CB  VAL A 128     3339   4865   9290    557   -680  -1333       C
ATOM   1027  CG1 VAL A 128    -109.967  34.877 -16.603  1.00 48.98           C
ANISOU 1027  CG1 VAL A 128     3608   5316   9685    560   -821  -1328       C
ATOM   1028  CG2 VAL A 128    -108.536  36.128 -18.232  1.00 45.42           C
ANISOU 1028  CG2 VAL A 128     3415   4841   9000    378   -479  -1266       C
ATOM   1029  N   ASP A 129    -112.777  34.166 -18.111  1.00 54.67           N
ANISOU 1029  N   ASP A 129     4101   6012  10657    799   -818  -1685       N
ATOM   1030  CA  ASP A 129    -114.178  33.963 -17.764  1.00 59.54           C
ANISOU 1030  CA  ASP A 129     4649   6575  11399    964   -994  -1746       C
ATOM   1031  C   ASP A 129    -114.568  34.803 -16.554  1.00 57.40           C
ANISOU 1031  C   ASP A 129     4525   6153  11132   1076  -1247  -1559       C
ATOM   1032  O   ASP A 129    -113.852  34.841 -15.550  1.00 53.40           O
ANISOU 1032  O   ASP A 129     4088   5651  10553   1032  -1342  -1419       O
ATOM   1033  CB  ASP A 129    -114.444  32.484 -17.481  1.00 70.18           C
ANISOU 1033  CB  ASP A 129     5797   8071  12798    962  -1014  -1888       C
ATOM   1034  CG  ASP A 129    -114.340  31.623 -18.724  1.00 79.00           C
ANISOU 1034  CG  ASP A 129     6773   9319  13925    864   -767  -2092       C
ATOM   1035  OD1 ASP A 129    -114.539  32.155 -19.836  1.00 81.89           O
ANISOU 1035  OD1 ASP A 129     7176   9642  14297    857   -626  -2154       O
ATOM   1036  OD2 ASP A 129    -114.065  30.412 -18.589  1.00 83.11           O
ANISOU 1036  OD2 ASP A 129     7153   9984  14442    786   -712  -2193       O
ATOM   1037  N   GLY A 130    -115.711  35.481 -16.660  1.00 60.54           N
ANISOU 1037  N   GLY A 130     4984   6413  11606   1212  -1352  -1557       N
ATOM   1038  CA  GLY A 130    -116.270  36.236 -15.559  1.00 57.21           C
ANISOU 1038  CA  GLY A 130     4722   5833  11183   1322  -1590  -1391       C
ATOM   1039  C   GLY A 130    -115.682  37.611 -15.338  1.00 51.23           C
ANISOU 1039  C   GLY A 130     4192   4936  10336   1268  -1589  -1198       C
ATOM   1040  O   GLY A 130    -116.213  38.364 -14.512  1.00 56.98           O
ANISOU 1040  O   GLY A 130     5089   5512  11051   1346  -1764  -1056       O
ATOM   1041  N   GLN A 131    -114.609  37.974 -16.042  1.00 45.13           N
ANISOU 1041  N   GLN A 131     3442   4209   9497   1136  -1394  -1186       N
ATOM   1042  CA  GLN A 131    -113.996  39.278 -15.821  1.00 42.69           C
ANISOU 1042  CA  GLN A 131     3339   3775   9108   1080  -1388  -1008       C
ATOM   1043  C   GLN A 131    -114.813  40.409 -16.430  1.00 49.19           C
ANISOU 1043  C   GLN A 131     4281   4446   9963   1131  -1381  -1005       C
ATOM   1044  O   GLN A 131    -114.744  41.545 -15.946  1.00 47.15           O
ANISOU 1044  O   GLN A 131     4220   4045   9651   1114  -1442   -846       O
ATOM   1045  CB  GLN A 131    -112.575  39.290 -16.380  1.00 41.59           C
ANISOU 1045  CB  GLN A 131     3180   3735   8888    933  -1188  -1004       C
ATOM   1046  CG  GLN A 131    -111.656  38.287 -15.712  1.00 48.84           C
ANISOU 1046  CG  GLN A 131     4022   4802   9732    845  -1183   -983       C
ATOM   1047  CD  GLN A 131    -110.489  38.943 -15.005  1.00 52.77           C
ANISOU 1047  CD  GLN A 131     4741   5292  10018    704  -1155   -781       C
ATOM   1048  OE1 GLN A 131    -109.833  39.830 -15.553  1.00 46.60           O
ANISOU 1048  OE1 GLN A 131     4089   4484   9134    615  -1021   -724       O
ATOM   1049  NE2 GLN A 131    -110.224  38.511 -13.778  1.00 58.16           N
ANISOU 1049  NE2 GLN A 131     5464   6000  10635    689  -1287   -682       N
ATOM   1050  N   VAL A 132    -115.581  40.128 -17.483  1.00 49.88           N
ANISOU 1050  N   VAL A 132     4259   4563  10130   1180  -1300  -1181       N
ATOM   1051  CA  VAL A 132    -116.492  41.132 -18.023  1.00 47.92           C
ANISOU 1051  CA  VAL A 132     4116   4173   9919   1238  -1313  -1189       C
ATOM   1052  C   VAL A 132    -117.576  41.461 -17.005  1.00 51.68           C
ANISOU 1052  C   VAL A 132     4702   4503  10430   1365  -1539  -1094       C
ATOM   1053  O   VAL A 132    -117.883  42.632 -16.755  1.00 56.10           O
ANISOU 1053  O   VAL A 132     5455   4903  10956   1367  -1595   -973       O
ATOM   1054  CB  VAL A 132    -117.097  40.651 -19.354  1.00 46.59           C
ANISOU 1054  CB  VAL A 132     3800   4075   9826   1268  -1180  -1407       C
ATOM   1055  CG1 VAL A 132    -118.134  41.644 -19.855  1.00 47.23           C
ANISOU 1055  CG1 VAL A 132     3986   4006   9952   1340  -1211  -1421       C
ATOM   1056  CG2 VAL A 132    -116.007  40.448 -20.390  1.00 44.30           C
ANISOU 1056  CG2 VAL A 132     3449   3910   9471   1133   -949  -1487       C
ATOM   1057  N   ASP A 133    -118.165  40.429 -16.395  1.00 49.58           N
ANISOU 1057  N   ASP A 133     4322   4291  10225   1467  -1670  -1148       N
ATOM   1058  CA  ASP A 133    -119.201  40.657 -15.395  1.00 56.39           C
ANISOU 1058  CA  ASP A 133     5299   5017  11110   1600  -1898  -1059       C
ATOM   1059  C   ASP A 133    -118.628  41.314 -14.146  1.00 53.71           C
ANISOU 1059  C   ASP A 133     5173   4584  10652   1548  -2014   -828       C
ATOM   1060  O   ASP A 133    -119.286  42.156 -13.524  1.00 55.05           O
ANISOU 1060  O   ASP A 133     5545   4583  10790   1600  -2139   -704       O
ATOM   1061  CB  ASP A 133    -119.890  39.338 -15.048  1.00 69.60           C
ANISOU 1061  CB  ASP A 133     6787   6787  12872   1721  -2014  -1183       C
ATOM   1062  CG  ASP A 133    -121.056  39.523 -14.098  1.00 84.43           C
ANISOU 1062  CG  ASP A 133     8781   8522  14777   1881  -2256  -1110       C
ATOM   1063  OD1 ASP A 133    -122.075  40.117 -14.512  1.00 89.63           O
ANISOU 1063  OD1 ASP A 133     9507   9054  15493   1975  -2282  -1141       O
ATOM   1064  OD2 ASP A 133    -120.954  39.075 -12.937  1.00 89.24           O
ANISOU 1064  OD2 ASP A 133     9424   9142  15342   1915  -2423  -1020       O
ATOM   1065  N   LEU A 134    -117.404  40.940 -13.760  1.00 56.09           N
ANISOU 1065  N   LEU A 134     5443   4990  10879   1438  -1964   -768       N
ATOM   1066  CA  LEU A 134    -116.745  41.608 -12.642  1.00 56.89           C
ANISOU 1066  CA  LEU A 134     5754   5005  10855   1368  -2046   -549       C
ATOM   1067  C   LEU A 134    -116.523  43.085 -12.930  1.00 54.91           C
ANISOU 1067  C   LEU A 134     5706   4616  10541   1279  -1955   -437       C
ATOM   1068  O   LEU A 134    -116.590  43.915 -12.015  1.00 54.15           O
ANISOU 1068  O   LEU A 134     5839   4385  10352   1253  -2045   -260       O
ATOM   1069  CB  LEU A 134    -115.412  40.926 -12.329  1.00 54.58           C
ANISOU 1069  CB  LEU A 134     5376   4859  10504   1263  -1986   -523       C
ATOM   1070  CG  LEU A 134    -115.460  39.585 -11.592  1.00 56.17           C
ANISOU 1070  CG  LEU A 134     5434   5184  10722   1318  -2116   -575       C
ATOM   1071  CD1 LEU A 134    -114.067  38.986 -11.492  1.00 52.70           C
ANISOU 1071  CD1 LEU A 134     4903   4897  10224   1190  -2017   -565       C
ATOM   1072  CD2 LEU A 134    -116.069  39.760 -10.213  1.00 58.66           C
ANISOU 1072  CD2 LEU A 134     5929   5382  10977   1401  -2362   -427       C
ATOM   1073  N   PHE A 135    -116.262  43.432 -14.192  1.00 50.60           N
ANISOU 1073  N   PHE A 135     5087   4108  10031   1221  -1770   -542       N
ATOM   1074  CA  PHE A 135    -116.080  44.832 -14.554  1.00 47.37           C
ANISOU 1074  CA  PHE A 135     4850   3583   9566   1131  -1681   -461       C
ATOM   1075  C   PHE A 135    -117.383  45.612 -14.440  1.00 48.54           C
ANISOU 1075  C   PHE A 135     5142   3560   9742   1215  -1781   -434       C
ATOM   1076  O   PHE A 135    -117.364  46.799 -14.093  1.00 53.06           O
ANISOU 1076  O   PHE A 135     5923   4001  10238   1141  -1778   -302       O
ATOM   1077  CB  PHE A 135    -115.511  44.933 -15.969  1.00 48.88           C
ANISOU 1077  CB  PHE A 135     4924   3866   9782   1059  -1473   -596       C
ATOM   1078  CG  PHE A 135    -115.480  46.332 -16.513  1.00 50.33           C
ANISOU 1078  CG  PHE A 135     5254   3944   9924    978  -1389   -553       C
ATOM   1079  CD1 PHE A 135    -114.533  47.240 -16.074  1.00 47.67           C
ANISOU 1079  CD1 PHE A 135     5062   3570   9480    843  -1340   -406       C
ATOM   1080  CD2 PHE A 135    -116.393  46.735 -17.473  1.00 51.53           C
ANISOU 1080  CD2 PHE A 135     5392   4042  10144   1029  -1354   -670       C
ATOM   1081  CE1 PHE A 135    -114.501  48.528 -16.577  1.00 47.69           C
ANISOU 1081  CE1 PHE A 135     5181   3495   9446    756  -1261   -383       C
ATOM   1082  CE2 PHE A 135    -116.366  48.021 -17.980  1.00 50.16           C
ANISOU 1082  CE2 PHE A 135     5346   3780   9933    948  -1283   -641       C
ATOM   1083  CZ  PHE A 135    -115.417  48.917 -17.533  1.00 48.25           C
ANISOU 1083  CZ  PHE A 135     5235   3512   9586    808  -1237   -500       C
ATOM   1084  N  AARG A 136    -118.517  44.972 -14.735  0.49 49.82           N
ANISOU 1084  N  AARG A 136     5198   3721  10012   1362  -1858   -563       N
ATOM   1085  N  BARG A 136    -118.519  44.967 -14.718  0.51 49.88           N
ANISOU 1085  N  BARG A 136     5206   3728  10019   1363  -1861   -562       N
ATOM   1086  CA AARG A 136    -119.801  45.654 -14.618  0.49 50.27           C
ANISOU 1086  CA AARG A 136     5396   3604  10101   1460  -1960   -541       C
ATOM   1087  CA BARG A 136    -119.800  45.657 -14.621  0.51 50.24           C
ANISOU 1087  CA BARG A 136     5393   3600  10098   1460  -1959   -542       C
ATOM   1088  C  AARG A 136    -120.104  46.033 -13.175  0.49 51.88           C
ANISOU 1088  C  AARG A 136     5822   3672  10216   1484  -2134   -349       C
ATOM   1089  C  BARG A 136    -120.148  46.003 -13.179  0.51 51.94           C
ANISOU 1089  C  BARG A 136     5826   3680  10228   1491  -2139   -354       C
ATOM   1090  O  AARG A 136    -120.750  47.056 -12.925  0.49 53.36           O
ANISOU 1090  O  AARG A 136     6221   3685  10368   1486  -2173   -259       O
ATOM   1091  O  BARG A 136    -120.869  46.976 -12.935  0.51 53.48           O
ANISOU 1091  O  BARG A 136     6226   3700  10395   1505  -2185   -271       O
ATOM   1092  CB AARG A 136    -120.923  44.775 -15.170  0.49 53.11           C
ANISOU 1092  CB AARG A 136     5584   3999  10597   1625  -2012   -724       C
ATOM   1093  CB BARG A 136    -120.907  44.804 -15.238  0.51 52.26           C
ANISOU 1093  CB BARG A 136     5473   3892  10490   1620  -2002   -729       C
ATOM   1094  CG AARG A 136    -120.785  44.395 -16.634  0.49 51.60           C
ANISOU 1094  CG AARG A 136     5192   3931  10482   1602  -1831   -925       C
ATOM   1095  CG BARG A 136    -120.629  44.352 -16.659  0.51 55.71           C
ANISOU 1095  CG BARG A 136     5702   4470  10997   1587  -1816   -925       C
ATOM   1096  CD AARG A 136    -122.022  43.637 -17.096  0.49 61.64           C
ANISOU 1096  CD AARG A 136     6320   5216  11886   1766  -1885  -1098       C
ATOM   1097  CD BARG A 136    -121.848  43.678 -17.261  0.51 61.20           C
ANISOU 1097  CD BARG A 136     6254   5177  11823   1741  -1849  -1106       C
ATOM   1098  NE AARG A 136    -121.888  43.105 -18.449  0.49 61.82           N
ANISOU 1098  NE AARG A 136     6145   5374  11970   1739  -1704  -1299       N
ATOM   1099  NE BARG A 136    -122.415  44.461 -18.353  0.51 62.56           N
ANISOU 1099  NE BARG A 136     6468   5268  12033   1745  -1749  -1190       N
ATOM   1100  CZ AARG A 136    -122.237  43.762 -19.550  0.49 62.63           C
ANISOU 1100  CZ AARG A 136     6273   5427  12096   1724  -1588  -1384       C
ATOM   1101  CZ BARG A 136    -122.309  44.137 -19.637  0.51 62.60           C
ANISOU 1101  CZ BARG A 136     6322   5380  12083   1715  -1582  -1365       C
ATOM   1102  NH1AARG A 136    -122.084  43.193 -20.738  0.49 62.54           N
ANISOU 1102  NH1AARG A 136     6093   5546  12123   1694  -1422  -1566       N
ATOM   1103  NH1BARG A 136    -122.854  44.912 -20.564  0.51 62.51           N
ANISOU 1103  NH1BARG A 136     6373   5283  12097   1720  -1508  -1433       N
ATOM   1104  NH2AARG A 136    -122.739  44.987 -19.466  0.49 62.38           N
ANISOU 1104  NH2AARG A 136     6446   5214  12042   1731  -1634  -1291       N
ATOM   1105  NH2BARG A 136    -121.667  43.033 -19.995  0.51 61.51           N
ANISOU 1105  NH2BARG A 136     5984   5431  11957   1674  -1485  -1475       N
ATOM   1106  N   ASN A 137    -119.650  45.227 -12.219  1.00 53.23           N
ANISOU 1106  N   ASN A 137     5964   3919  10341   1495  -2236   -286       N
ATOM   1107  CA  ASN A 137    -119.915  45.458 -10.807  1.00 60.73           C
ANISOU 1107  CA  ASN A 137     7132   4755  11187   1519  -2409   -108       C
ATOM   1108  C   ASN A 137    -118.793  46.211 -10.107  1.00 59.09           C
ANISOU 1108  C   ASN A 137     7106   4524  10821   1343  -2345     76       C
ATOM   1109  O   ASN A 137    -118.885  46.446  -8.899  1.00 61.56           O
ANISOU 1109  O   ASN A 137     7624   4749  11018   1334  -2465    234       O
ATOM   1110  CB  ASN A 137    -120.162  44.125 -10.095  1.00 69.18           C
ANISOU 1110  CB  ASN A 137     8077   5919  12288   1641  -2581   -151       C
ATOM   1111  CG  ASN A 137    -121.328  43.358 -10.686  1.00 74.71           C
ANISOU 1111  CG  ASN A 137     8596   6647  13145   1819  -2649   -337       C
ATOM   1112  OD1 ASN A 137    -122.477  43.553 -10.291  1.00 81.65           O
ANISOU 1112  OD1 ASN A 137     9586   7390  14045   1951  -2796   -315       O
ATOM   1113  ND2 ASN A 137    -121.038  42.480 -11.640  1.00 71.12           N
ANISOU 1113  ND2 ASN A 137     7865   6363  12792   1819  -2534   -523       N
ATOM   1114  N   ALA A 138    -117.743  46.588 -10.826  1.00 56.28           N
ANISOU 1114  N   ALA A 138     6687   4246  10451   1202  -2156     56       N
ATOM   1115  CA  ALA A 138    -116.628  47.313 -10.239  1.00 61.86           C
ANISOU 1115  CA  ALA A 138     7548   4944  11015   1028  -2073    214       C
ATOM   1116  C   ALA A 138    -116.887  48.813 -10.281  1.00 59.06           C
ANISOU 1116  C   ALA A 138     7410   4437  10594    930  -1996    303       C
ATOM   1117  O   ALA A 138    -117.499  49.334 -11.218  1.00 57.32           O
ANISOU 1117  O   ALA A 138     7163   4162  10455    956  -1936    209       O
ATOM   1118  CB  ALA A 138    -115.325  46.988 -10.970  1.00 68.09           C
ANISOU 1118  CB  ALA A 138     8164   5891  11817    926  -1907    147       C
ATOM   1119  N   ARG A 139    -116.412  49.508  -9.246  1.00 57.59           N
ANISOU 1119  N   ARG A 139     7442   4186  10252    809  -1990    480       N
ATOM   1120  CA  ARG A 139    -116.580  50.957  -9.184  1.00 55.77           C
ANISOU 1120  CA  ARG A 139     7421   3822   9947    688  -1897    564       C
ATOM   1121  C   ARG A 139    -115.685  51.652 -10.205  1.00 52.15           C
ANISOU 1121  C   ARG A 139     6868   3441   9507    547  -1694    500       C
ATOM   1122  O   ARG A 139    -116.164  52.400 -11.065  1.00 48.84           O
ANISOU 1122  O   ARG A 139     6449   2959   9150    535  -1625    425       O
ATOM   1123  CB  ARG A 139    -116.287  51.456  -7.767  1.00 61.16           C
ANISOU 1123  CB  ARG A 139     8359   4433  10448    584  -1922    759       C
ATOM   1124  CG  ARG A 139    -116.606  52.924  -7.552  1.00 71.13           C
ANISOU 1124  CG  ARG A 139     9854   5543  11630    459  -1827    846       C
ATOM   1125  CD  ARG A 139    -117.075  53.197  -6.132  1.00 80.65           C
ANISOU 1125  CD  ARG A 139    11339   6617  12686    448  -1921   1012       C
ATOM   1126  NE  ARG A 139    -115.972  53.331  -5.186  1.00 82.60           N
ANISOU 1126  NE  ARG A 139    11682   6936  12766    295  -1847   1134       N
ATOM   1127  CZ  ARG A 139    -116.131  53.470  -3.874  1.00 86.88           C
ANISOU 1127  CZ  ARG A 139    12462   7401  13149    262  -1909   1282       C
ATOM   1128  NH1 ARG A 139    -117.351  53.486  -3.351  1.00 88.64           N
ANISOU 1128  NH1 ARG A 139    12852   7464  13362    377  -2058   1331       N
ATOM   1129  NH2 ARG A 139    -115.074  53.589  -3.083  1.00 87.60           N
ANISOU 1129  NH2 ARG A 139    12627   7571  13085    116  -1819   1376       N
ATOM   1130  N   ASN A 140    -114.379  51.413 -10.125  1.00 50.83           N
ANISOU 1130  N   ASN A 140     6623   3409   9281    443  -1601    524       N
ATOM   1131  CA  ASN A 140    -113.414  51.939 -11.079  1.00 47.02           C
ANISOU 1131  CA  ASN A 140     6033   3023   8810    323  -1421    456       C
ATOM   1132  C   ASN A 140    -112.672  50.771 -11.710  1.00 47.72           C
ANISOU 1132  C   ASN A 140     5891   3273   8966    374  -1393    350       C
ATOM   1133  O   ASN A 140    -112.170  49.895 -10.997  1.00 49.82           O
ANISOU 1133  O   ASN A 140     6133   3603   9194    392  -1451    402       O
ATOM   1134  CB  ASN A 140    -112.427  52.892 -10.400  1.00 47.33           C
ANISOU 1134  CB  ASN A 140     6209   3074   8699    130  -1304    583       C
ATOM   1135  CG  ASN A 140    -113.110  53.858  -9.456  1.00 50.76           C
ANISOU 1135  CG  ASN A 140     6900   3348   9039     70  -1332    709       C
ATOM   1136  OD1 ASN A 140    -113.628  54.893  -9.875  1.00 54.95           O
ANISOU 1136  OD1 ASN A 140     7506   3781   9591     18  -1274    686       O
ATOM   1137  ND2 ASN A 140    -113.112  53.526  -8.170  1.00 50.72           N
ANISOU 1137  ND2 ASN A 140     7042   3310   8921     71  -1417    841       N
ATOM   1138  N   GLY A 141    -112.604  50.752 -13.036  1.00 38.62           N
ANISOU 1138  N   GLY A 141     4584   2183   7908    392  -1301    199       N
ATOM   1139  CA  GLY A 141    -111.962  49.645 -13.715  1.00 37.31           C
ANISOU 1139  CA  GLY A 141     4214   2161   7803    438  -1253     84       C
ATOM   1140  C   GLY A 141    -111.748  49.923 -15.184  1.00 40.18           C
ANISOU 1140  C   GLY A 141     4460   2585   8222    418  -1119    -66       C
ATOM   1141  O   GLY A 141    -112.361  50.824 -15.767  1.00 40.92           O
ANISOU 1141  O   GLY A 141     4603   2604   8339    406  -1096   -106       O
ATOM   1142  N   VAL A 142    -110.860  49.125 -15.776  1.00 36.75           N
ANISOU 1142  N   VAL A 142     3883   2302   7778    408  -1027   -148       N
ATOM   1143  CA  VAL A 142    -110.569  49.158 -17.204  1.00 38.75           C
ANISOU 1143  CA  VAL A 142     4028   2643   8051    394   -897   -300       C
ATOM   1144  C   VAL A 142    -110.693  47.740 -17.742  1.00 37.44           C
ANISOU 1144  C   VAL A 142     3688   2601   7935    485   -877   -436       C
ATOM   1145  O   VAL A 142    -110.146  46.800 -17.156  1.00 35.24           O
ANISOU 1145  O   VAL A 142     3359   2436   7594    475   -884   -403       O
ATOM   1146  CB  VAL A 142    -109.168  49.729 -17.492  1.00 41.45           C
ANISOU 1146  CB  VAL A 142     4396   3108   8246    250   -759   -264       C
ATOM   1147  CG1 VAL A 142    -108.820  49.571 -18.965  1.00 41.07           C
ANISOU 1147  CG1 VAL A 142     4248   3161   8195    250   -641   -420       C
ATOM   1148  CG2 VAL A 142    -109.096  51.191 -17.079  1.00 40.29           C
ANISOU 1148  CG2 VAL A 142     4388   2848   8072    151   -760   -162       C
ATOM   1149  N   LEU A 143    -111.411  47.587 -18.852  1.00 37.79           N
ANISOU 1149  N   LEU A 143     3641   2624   8092    563   -845   -598       N
ATOM   1150  CA  LEU A 143    -111.683  46.284 -19.442  1.00 38.60           C
ANISOU 1150  CA  LEU A 143     3567   2835   8263    645   -809   -753       C
ATOM   1151  C   LEU A 143    -111.193  46.248 -20.882  1.00 40.03           C
ANISOU 1151  C   LEU A 143     3690   3118   8400    594   -638   -894       C
ATOM   1152  O   LEU A 143    -111.330  47.230 -21.619  1.00 42.15           O
ANISOU 1152  O   LEU A 143     4026   3316   8672    569   -599   -929       O
ATOM   1153  CB  LEU A 143    -113.183  45.964 -19.393  1.00 40.75           C
ANISOU 1153  CB  LEU A 143     3789   3035   8659    781   -924   -826       C
ATOM   1154  CG  LEU A 143    -113.647  44.674 -20.074  1.00 44.33           C
ANISOU 1154  CG  LEU A 143     4047   3607   9189    857   -877  -1011       C
ATOM   1155  CD1 LEU A 143    -113.036  43.453 -19.402  1.00 45.51           C
ANISOU 1155  CD1 LEU A 143     4080   3878   9334    857   -892  -1002       C
ATOM   1156  CD2 LEU A 143    -115.165  44.584 -20.083  1.00 46.03           C
ANISOU 1156  CD2 LEU A 143     4241   3745   9505    983   -988  -1079       C
ATOM   1157  N   ILE A 144    -110.620  45.114 -21.279  1.00 42.12           N
ANISOU 1157  N   ILE A 144     3842   3546   8616    571   -537   -977       N
ATOM   1158  CA  ILE A 144    -110.236  44.863 -22.661  1.00 40.38           C
ANISOU 1158  CA  ILE A 144     3575   3422   8345    530   -372  -1122       C
ATOM   1159  C   ILE A 144    -110.935  43.597 -23.133  1.00 38.95           C
ANISOU 1159  C   ILE A 144     3216   3306   8278    610   -329  -1298       C
ATOM   1160  O   ILE A 144    -111.084  42.636 -22.369  1.00 37.12           O
ANISOU 1160  O   ILE A 144     2881   3126   8097    645   -388  -1292       O
ATOM   1161  CB  ILE A 144    -108.706  44.741 -22.833  1.00 36.97           C
ANISOU 1161  CB  ILE A 144     3205   3126   7716    397   -254  -1061       C
ATOM   1162  CG1 ILE A 144    -108.159  43.550 -22.041  1.00 38.79           C
ANISOU 1162  CG1 ILE A 144     3370   3466   7901    367   -250  -1020       C
ATOM   1163  CG2 ILE A 144    -108.017  46.027 -22.407  1.00 32.65           C
ANISOU 1163  CG2 ILE A 144     2806   2527   7073    326   -290   -910       C
ATOM   1164  CD1 ILE A 144    -106.782  43.109 -22.483  1.00 33.71           C
ANISOU 1164  CD1 ILE A 144     2771   2956   7079    252   -106  -1013       C
ATOM   1165  N   THR A 145    -111.385  43.606 -24.386  1.00 39.79           N
ANISOU 1165  N   THR A 145     3281   3413   8426    636   -226  -1464       N
ATOM   1166  CA  THR A 145    -112.026  42.447 -24.991  1.00 43.67           C
ANISOU 1166  CA  THR A 145     3619   4000   8974    670   -151  -1637       C
ATOM   1167  C   THR A 145    -111.582  42.326 -26.441  1.00 45.26           C
ANISOU 1167  C   THR A 145     3833   4278   9087    600     49  -1776       C
ATOM   1168  O   THR A 145    -111.051  43.269 -27.033  1.00 41.91           O
ANISOU 1168  O   THR A 145     3540   3812   8574    554     94  -1751       O
ATOM   1169  CB  THR A 145    -113.561  42.529 -24.940  1.00 46.65           C
ANISOU 1169  CB  THR A 145     3955   4296   9474    783   -266  -1693       C
ATOM   1170  OG1 THR A 145    -113.997  43.745 -25.558  1.00 52.55           O
ANISOU 1170  OG1 THR A 145     4823   4932  10210    791   -276  -1692       O
ATOM   1171  CG2 THR A 145    -114.071  42.473 -23.507  1.00 40.14           C
ANISOU 1171  CG2 THR A 145     3128   3399   8723    861   -468  -1568       C
ATOM   1172  N   GLU A 146    -111.811  41.143 -27.008  1.00 52.86           N
ANISOU 1172  N   GLU A 146     4665   5356  10063    586    167  -1928       N
ATOM   1173  CA  GLU A 146    -111.584  40.917 -28.428  1.00 54.13           C
ANISOU 1173  CA  GLU A 146     4846   5586  10134    520    364  -2076       C
ATOM   1174  C   GLU A 146    -112.818  41.201 -29.271  1.00 55.65           C
ANISOU 1174  C   GLU A 146     5023   5730  10391    584    365  -2200       C
ATOM   1175  O   GLU A 146    -112.685  41.479 -30.468  1.00 58.96           O
ANISOU 1175  O   GLU A 146     5518   6165  10720    538    494  -2293       O
ATOM   1176  CB  GLU A 146    -111.135  39.473 -28.673  1.00 56.56           C
ANISOU 1176  CB  GLU A 146     5038   6047  10404    439    524  -2181       C
ATOM   1177  CG  GLU A 146    -109.892  39.057 -27.907  1.00 59.69           C
ANISOU 1177  CG  GLU A 146     5450   6510  10718    358    544  -2068       C
ATOM   1178  CD  GLU A 146    -109.491  37.622 -28.197  1.00 67.36           C
ANISOU 1178  CD  GLU A 146     6312   7630  11652    256    718  -2183       C
ATOM   1179  OE1 GLU A 146    -110.133  36.987 -29.060  1.00 71.79           O
ANISOU 1179  OE1 GLU A 146     6805   8244  12230    237    828  -2345       O
ATOM   1180  OE2 GLU A 146    -108.536  37.128 -27.563  1.00 67.27           O
ANISOU 1180  OE2 GLU A 146     6336   7686  11535    159    725  -2078       O
ATOM   1181  N   GLY A 147    -114.007  41.139 -28.678  1.00 52.74           N
ANISOU 1181  N   GLY A 147     4572   5299  10168    694    221  -2204       N
ATOM   1182  CA  GLY A 147    -115.235  41.378 -29.407  1.00 54.86           C
ANISOU 1182  CA  GLY A 147     4820   5514  10509    769    216  -2324       C
ATOM   1183  C   GLY A 147    -116.172  42.339 -28.706  1.00 55.72           C
ANISOU 1183  C   GLY A 147     4991   5464  10715    878     16  -2228       C
ATOM   1184  O   GLY A 147    -115.754  43.096 -27.824  1.00 54.23           O
ANISOU 1184  O   GLY A 147     4901   5196  10508    871   -101  -2060       O
ATOM   1185  N   SER A 148    -117.447  42.310 -29.084  1.00 58.36           N
ANISOU 1185  N   SER A 148     5276   5749  11150    975    -16  -2336       N
ATOM   1186  CA  SER A 148    -118.413  43.265 -28.568  1.00 61.50           C
ANISOU 1186  CA  SER A 148     5759   5981  11628   1076   -187  -2259       C
ATOM   1187  C   SER A 148    -118.855  42.897 -27.159  1.00 63.30           C
ANISOU 1187  C   SER A 148     5939   6164  11948   1166   -371  -2157       C
ATOM   1188  O   SER A 148    -118.860  41.728 -26.767  1.00 67.21           O
ANISOU 1188  O   SER A 148     6287   6761  12489   1188   -373  -2207       O
ATOM   1189  CB  SER A 148    -119.634  43.343 -29.484  1.00 66.59           C
ANISOU 1189  CB  SER A 148     6376   6579  12344   1158   -153  -2416       C
ATOM   1190  OG  SER A 148    -119.301  43.934 -30.723  1.00 72.53           O
ANISOU 1190  OG  SER A 148     7217   7342  12998   1081    -14  -2490       O
ATOM   1191  N   VAL A 149    -119.235  43.918 -26.397  1.00 63.99           N
ANISOU 1191  N   VAL A 149     6163   6096  12053   1212   -527  -2014       N
ATOM   1192  CA  VAL A 149    -119.813  43.748 -25.072  1.00 66.27           C
ANISOU 1192  CA  VAL A 149     6455   6310  12416   1311   -720  -1907       C
ATOM   1193  C   VAL A 149    -121.184  44.403 -25.089  1.00 68.89           C
ANISOU 1193  C   VAL A 149     6864   6480  12832   1433   -828  -1923       C
ATOM   1194  O   VAL A 149    -121.301  45.605 -25.363  1.00 67.79           O
ANISOU 1194  O   VAL A 149     6881   6219  12656   1401   -831  -1868       O
ATOM   1195  CB  VAL A 149    -118.921  44.345 -23.973  1.00 65.42           C
ANISOU 1195  CB  VAL A 149     6472   6153  12230   1240   -806  -1695       C
ATOM   1196  CG1 VAL A 149    -119.600  44.236 -22.618  1.00 65.07           C
ANISOU 1196  CG1 VAL A 149     6465   6016  12243   1346  -1013  -1581       C
ATOM   1197  CG2 VAL A 149    -117.583  43.633 -23.948  1.00 67.88           C
ANISOU 1197  CG2 VAL A 149     6707   6620  12464   1133   -699  -1686       C
ATOM   1198  N   LYS A 150    -122.216  43.612 -24.811  1.00 73.04           N
ANISOU 1198  N   LYS A 150     7280   7003  13469   1572   -916  -2006       N
ATOM   1199  CA  LYS A 150    -123.588  44.093 -24.893  1.00 77.56           C
ANISOU 1199  CA  LYS A 150     7915   7424  14131   1709  -1011  -2044       C
ATOM   1200  C   LYS A 150    -123.829  45.233 -23.911  1.00 71.87           C
ANISOU 1200  C   LYS A 150     7414   6511  13380   1727  -1169  -1847       C
ATOM   1201  O   LYS A 150    -123.500  45.132 -22.726  1.00 69.22           O
ANISOU 1201  O   LYS A 150     7125   6158  13016   1727  -1290  -1699       O
ATOM   1202  CB  LYS A 150    -124.551  42.934 -24.629  1.00 89.40           C
ANISOU 1202  CB  LYS A 150     9244   8969  15757   1862  -1092  -2161       C
ATOM   1203  CG  LYS A 150    -125.849  43.308 -23.933  1.00 97.70           C
ANISOU 1203  CG  LYS A 150    10387   9841  16893   2034  -1287  -2112       C
ATOM   1204  CD  LYS A 150    -126.691  42.063 -23.692  1.00105.00           C
ANISOU 1204  CD  LYS A 150    11116  10837  17943   2186  -1366  -2243       C
ATOM   1205  CE  LYS A 150    -127.741  42.284 -22.616  1.00110.90           C
ANISOU 1205  CE  LYS A 150    11966  11419  18754   2358  -1603  -2148       C
ATOM   1206  NZ  LYS A 150    -128.504  41.035 -22.335  1.00113.44           N
ANISOU 1206  NZ  LYS A 150    12081  11821  19198   2512  -1695  -2279       N
ATOM   1207  N   GLY A 151    -124.398  46.326 -24.414  1.00 69.59           N
ANISOU 1207  N   GLY A 151     7272   6078  13092   1732  -1158  -1847       N
ATOM   1208  CA  GLY A 151    -124.733  47.462 -23.583  1.00 72.20           C
ANISOU 1208  CA  GLY A 151     7829   6212  13393   1737  -1285  -1675       C
ATOM   1209  C   GLY A 151    -123.593  48.404 -23.279  1.00 73.27           C
ANISOU 1209  C   GLY A 151     8101   6333  13406   1566  -1245  -1521       C
ATOM   1210  O   GLY A 151    -123.730  49.244 -22.383  1.00 78.27           O
ANISOU 1210  O   GLY A 151     8919   6818  14000   1547  -1346  -1359       O
ATOM   1211  N   LEU A 152    -122.473  48.298 -23.991  1.00 66.94           N
ANISOU 1211  N   LEU A 152     7221   5676  12537   1438  -1096  -1567       N
ATOM   1212  CA  LEU A 152    -121.317  49.150 -23.749  1.00 58.07           C
ANISOU 1212  CA  LEU A 152     6206   4555  11302   1278  -1052  -1434       C
ATOM   1213  C   LEU A 152    -120.700  49.559 -25.076  1.00 57.28           C
ANISOU 1213  C   LEU A 152     6083   4532  11146   1174   -888  -1542       C
ATOM   1214  O   LEU A 152    -120.416  48.706 -25.923  1.00 55.36           O
ANISOU 1214  O   LEU A 152     5696   4433  10906   1177   -776  -1683       O
ATOM   1215  CB  LEU A 152    -120.278  48.436 -22.877  1.00 55.38           C
ANISOU 1215  CB  LEU A 152     5800   4331  10912   1230  -1071  -1335       C
ATOM   1216  CG  LEU A 152    -120.669  48.210 -21.417  1.00 57.38           C
ANISOU 1216  CG  LEU A 152     6116   4503  11181   1305  -1246  -1192       C
ATOM   1217  CD1 LEU A 152    -119.588  47.430 -20.691  1.00 52.42           C
ANISOU 1217  CD1 LEU A 152     5411   4005  10502   1252  -1249  -1118       C
ATOM   1218  CD2 LEU A 152    -120.933  49.539 -20.726  1.00 59.92           C
ANISOU 1218  CD2 LEU A 152     6677   4638  11454   1259  -1323  -1031       C
ATOM   1219  N   GLN A 153    -120.493  50.859 -25.249  1.00 58.73           N
ANISOU 1219  N   GLN A 153     6420   4622  11275   1077   -873  -1480       N
ATOM   1220  CA  GLN A 153    -119.875  51.372 -26.465  1.00 56.68           C
ANISOU 1220  CA  GLN A 153     6159   4427  10948    976   -739  -1575       C
ATOM   1221  C   GLN A 153    -118.362  51.197 -26.387  1.00 50.27           C
ANISOU 1221  C   GLN A 153     5305   3758  10039    860   -666  -1517       C
ATOM   1222  O   GLN A 153    -117.749  51.595 -25.392  1.00 44.58           O
ANISOU 1222  O   GLN A 153     4652   3011   9277    795   -722  -1358       O
ATOM   1223  CB  GLN A 153    -120.229  52.843 -26.663  1.00 65.11           C
ANISOU 1223  CB  GLN A 153     7396   5344  11998    910   -760  -1541       C
ATOM   1224  CG  GLN A 153    -120.028  53.354 -28.079  1.00 74.28           C
ANISOU 1224  CG  GLN A 153     8562   6548  13114    846   -648  -1682       C
ATOM   1225  CD  GLN A 153    -121.120  52.902 -29.030  1.00 84.59           C
ANISOU 1225  CD  GLN A 153     9819   7833  14487    957   -611  -1858       C
ATOM   1226  OE1 GLN A 153    -121.995  52.113 -28.669  1.00 86.42           O
ANISOU 1226  OE1 GLN A 153     9988   8036  14810   1090   -664  -1887       O
ATOM   1227  NE2 GLN A 153    -121.077  53.409 -30.256  1.00 89.44           N
ANISOU 1227  NE2 GLN A 153    10465   8464  15055    906   -524  -1982       N
ATOM   1228  N   PRO A 154    -117.733  50.606 -27.399  1.00 49.91           N
ANISOU 1228  N   PRO A 154     5163   3856   9945    829   -538  -1640       N
ATOM   1229  CA  PRO A 154    -116.309  50.280 -27.308  1.00 48.55           C
ANISOU 1229  CA  PRO A 154     4954   3814   9678    738   -468  -1590       C
ATOM   1230  C   PRO A 154    -115.401  51.389 -27.823  1.00 50.28           C
ANISOU 1230  C   PRO A 154     5269   4040   9794    614   -420  -1565       C
ATOM   1231  O   PRO A 154    -115.821  52.316 -28.518  1.00 53.51           O
ANISOU 1231  O   PRO A 154     5753   4380  10197    589   -416  -1622       O
ATOM   1232  CB  PRO A 154    -116.194  49.036 -28.199  1.00 48.43           C
ANISOU 1232  CB  PRO A 154     4804   3941   9655    770   -346  -1750       C
ATOM   1233  CG  PRO A 154    -117.215  49.277 -29.262  1.00 49.71           C
ANISOU 1233  CG  PRO A 154     4975   4056   9855    821   -309  -1899       C
ATOM   1234  CD  PRO A 154    -118.353  50.034 -28.607  1.00 52.77           C
ANISOU 1234  CD  PRO A 154     5445   4269  10335    889   -447  -1833       C
ATOM   1235  N   SER A 155    -114.126  51.264 -27.458  1.00 45.87           N
ANISOU 1235  N   SER A 155     4704   3567   9156    538   -388  -1483       N
ATOM   1236  CA  SER A 155    -113.061  52.113 -27.976  1.00 42.70           C
ANISOU 1236  CA  SER A 155     4368   3208   8649    427   -339  -1473       C
ATOM   1237  C   SER A 155    -111.969  51.210 -28.524  1.00 36.25           C
ANISOU 1237  C   SER A 155     3495   2538   7739    405   -229  -1531       C
ATOM   1238  O   SER A 155    -111.451  50.353 -27.802  1.00 40.78           O
ANISOU 1238  O   SER A 155     4014   3167   8312    415   -221  -1466       O
ATOM   1239  CB  SER A 155    -112.504  53.038 -26.891  1.00 42.30           C
ANISOU 1239  CB  SER A 155     4391   3100   8580    345   -412  -1302       C
ATOM   1240  OG  SER A 155    -111.428  53.814 -27.387  1.00 42.70           O
ANISOU 1240  OG  SER A 155     4480   3207   8537    243   -370  -1305       O
ATOM   1241  N   VAL A 156    -111.627  51.394 -29.794  1.00 36.29           N
ANISOU 1241  N   VAL A 156     3529   2600   7658    372   -146  -1653       N
ATOM   1242  CA  VAL A 156    -110.640  50.544 -30.450  1.00 45.88           C
ANISOU 1242  CA  VAL A 156     4726   3943   8761    349    -29  -1719       C
ATOM   1243  C   VAL A 156    -109.244  50.983 -30.030  1.00 46.39           C
ANISOU 1243  C   VAL A 156     4846   4054   8726    269    -43  -1606       C
ATOM   1244  O   VAL A 156    -108.906  52.171 -30.095  1.00 50.40           O
ANISOU 1244  O   VAL A 156     5419   4529   9201    211   -100  -1567       O
ATOM   1245  CB  VAL A 156    -110.808  50.596 -31.976  1.00 42.98           C
ANISOU 1245  CB  VAL A 156     4402   3616   8311    343     60  -1887       C
ATOM   1246  CG1 VAL A 156    -109.837  49.640 -32.648  1.00 39.72           C
ANISOU 1246  CG1 VAL A 156     4001   3329   7764    313    194  -1953       C
ATOM   1247  CG2 VAL A 156    -112.242  50.263 -32.359  1.00 43.60           C
ANISOU 1247  CG2 VAL A 156     4427   3648   8490    421     71  -1993       C
ATOM   1248  N   GLY A 157    -108.428  50.023 -29.599  1.00 45.05           N
ANISOU 1248  N   GLY A 157     4646   4001   8470    253     10  -1535       N
ATOM   1249  CA  GLY A 157    -107.095  50.309 -29.127  1.00 37.58           C
ANISOU 1249  CA  GLY A 157     3751   3140   7387    181      0  -1399       C
ATOM   1250  C   GLY A 157    -106.051  50.213 -30.221  1.00 38.41           C
ANISOU 1250  C   GLY A 157     3932   3358   7303    141     82  -1452       C
ATOM   1251  O   GLY A 157    -106.366  50.200 -31.415  1.00 43.05           O
ANISOU 1251  O   GLY A 157     4555   3948   7853    152    136  -1593       O
ATOM   1252  N   PRO A 158    -104.781  50.151 -29.830  1.00 36.17           N
ANISOU 1252  N   PRO A 158     3691   3164   6889     98     88  -1341       N
ATOM   1253  CA  PRO A 158    -103.708  50.038 -30.823  1.00 32.34           C
ANISOU 1253  CA  PRO A 158     3304   2774   6210     72    150  -1377       C
ATOM   1254  C   PRO A 158    -103.726  48.682 -31.508  1.00 32.76           C
ANISOU 1254  C   PRO A 158     3373   2886   6187     74    285  -1466       C
ATOM   1255  O   PRO A 158    -104.295  47.706 -31.012  1.00 33.91           O
ANISOU 1255  O   PRO A 158     3430   3030   6424     87    333  -1479       O
ATOM   1256  CB  PRO A 158    -102.429  50.219 -29.995  1.00 29.10           C
ANISOU 1256  CB  PRO A 158     2923   2425   5707     42    118  -1227       C
ATOM   1257  CG  PRO A 158    -102.880  50.789 -28.680  1.00 29.35           C
ANISOU 1257  CG  PRO A 158     2879   2388   5884     35     33  -1123       C
ATOM   1258  CD  PRO A 158    -104.257  50.257 -28.460  1.00 30.58           C
ANISOU 1258  CD  PRO A 158     2960   2462   6198     74     34  -1179       C
ATOM   1259  N   LYS A 159    -103.086  48.634 -32.677  1.00 32.89           N
ANISOU 1259  N   LYS A 159     3509   2956   6031     56    346  -1534       N
ATOM   1260  CA  LYS A 159    -102.945  47.365 -33.381  1.00 30.95           C
ANISOU 1260  CA  LYS A 159     3311   2768   5680     31    498  -1614       C
ATOM   1261  C   LYS A 159    -102.016  46.414 -32.641  1.00 37.38           C
ANISOU 1261  C   LYS A 159     4137   3647   6419     -8    552  -1507       C
ATOM   1262  O   LYS A 159    -102.190  45.193 -32.720  1.00 43.01           O
ANISOU 1262  O   LYS A 159     4820   4397   7127    -41    676  -1560       O
ATOM   1263  CB  LYS A 159    -102.427  47.596 -34.800  1.00 36.85           C
ANISOU 1263  CB  LYS A 159     4225   3545   6231     15    543  -1699       C
ATOM   1264  CG  LYS A 159    -103.458  48.125 -35.779  1.00 40.28           C
ANISOU 1264  CG  LYS A 159     4663   3926   6716     39    543  -1855       C
ATOM   1265  CD  LYS A 159    -102.895  48.144 -37.192  1.00 46.95           C
ANISOU 1265  CD  LYS A 159     5697   4809   7333     17    601  -1940       C
ATOM   1266  CE  LYS A 159    -103.957  48.517 -38.213  1.00 55.31           C
ANISOU 1266  CE  LYS A 159     6770   5818   8428     33    624  -2114       C
ATOM   1267  NZ  LYS A 159    -104.497  49.885 -37.982  1.00 59.73           N
ANISOU 1267  NZ  LYS A 159     7267   6305   9123     68    464  -2117       N
ATOM   1268  N   GLN A 160    -101.038  46.948 -31.917  1.00 32.52           N
ANISOU 1268  N   GLN A 160     3559   3047   5750    -11    469  -1367       N
ATOM   1269  CA  GLN A 160     -99.987  46.147 -31.311  1.00 34.20           C
ANISOU 1269  CA  GLN A 160     3818   3314   5861    -48    518  -1266       C
ATOM   1270  C   GLN A 160    -100.249  45.920 -29.826  1.00 33.68           C
ANISOU 1270  C   GLN A 160     3624   3235   5937    -49    466  -1168       C
ATOM   1271  O   GLN A 160    -100.944  46.693 -29.162  1.00 32.15           O
ANISOU 1271  O   GLN A 160     3340   2986   5891    -17    363  -1135       O
ATOM   1272  CB  GLN A 160     -98.622  46.815 -31.500  1.00 29.87           C
ANISOU 1272  CB  GLN A 160     3411   2794   5145    -40    464  -1184       C
ATOM   1273  CG  GLN A 160     -98.419  48.090 -30.688  1.00 33.57           C
ANISOU 1273  CG  GLN A 160     3818   3243   5695     -8    322  -1092       C
ATOM   1274  CD  GLN A 160     -99.066  49.309 -31.319  1.00 40.55           C
ANISOU 1274  CD  GLN A 160     4675   4087   6645     20    236  -1168       C
ATOM   1275  OE1 GLN A 160     -99.767  49.208 -32.325  1.00 47.82           O
ANISOU 1275  OE1 GLN A 160     5620   4988   7560     24    274  -1290       O
ATOM   1276  NE2 GLN A 160     -98.828  50.474 -30.728  1.00 42.63           N
ANISOU 1276  NE2 GLN A 160     4888   4340   6969     30    126  -1104       N
ATOM   1277  N   ALA A 161     -99.672  44.835 -29.313  1.00 33.13           N
ANISOU 1277  N   ALA A 161     3565   3212   5810    -93    538  -1121       N
ATOM   1278  CA  ALA A 161     -99.721  44.509 -27.897  1.00 30.42           C
ANISOU 1278  CA  ALA A 161     3129   2867   5560   -101    489  -1022       C
ATOM   1279  C   ALA A 161     -98.397  43.870 -27.507  1.00 31.36           C
ANISOU 1279  C   ALA A 161     3350   3038   5529   -152    543   -936       C
ATOM   1280  O   ALA A 161     -97.576  43.523 -28.360  1.00 34.43           O
ANISOU 1280  O   ALA A 161     3875   3453   5752   -180    629   -962       O
ATOM   1281  CB  ALA A 161    -100.893  43.578 -27.567  1.00 32.08           C
ANISOU 1281  CB  ALA A 161     3189   3073   5926    -97    516  -1098       C
ATOM   1282  N   SER A 162     -98.192  43.714 -26.203  1.00 34.15           N
ANISOU 1282  N   SER A 162     3653   3394   5930   -163    491   -834       N
ATOM   1283  CA  SER A 162     -96.957  43.157 -25.665  1.00 30.79           C
ANISOU 1283  CA  SER A 162     3321   3004   5372   -209    532   -749       C
ATOM   1284  C   SER A 162     -97.160  41.683 -25.340  1.00 29.73           C
ANISOU 1284  C   SER A 162     3134   2906   5256   -276    618   -790       C
ATOM   1285  O   SER A 162     -98.053  41.331 -24.562  1.00 33.79           O
ANISOU 1285  O   SER A 162     3506   3418   5916   -270    567   -799       O
ATOM   1286  CB  SER A 162     -96.511  43.920 -24.419  1.00 32.85           C
ANISOU 1286  CB  SER A 162     3573   3250   5656   -190    432   -617       C
ATOM   1287  OG  SER A 162     -95.393  43.291 -23.817  1.00 34.51           O
ANISOU 1287  OG  SER A 162     3870   3491   5752   -232    475   -546       O
ATOM   1288  N   LEU A 163     -96.331  40.829 -25.933  1.00 30.77           N
ANISOU 1288  N   LEU A 163     3385   3067   5239   -342    742   -819       N
ATOM   1289  CA  LEU A 163     -96.333  39.396 -25.658  1.00 29.77           C
ANISOU 1289  CA  LEU A 163     3220   2981   5110   -433    842   -865       C
ATOM   1290  C   LEU A 163     -94.947  39.007 -25.162  1.00 29.80           C
ANISOU 1290  C   LEU A 163     3376   2988   4959   -488    878   -771       C
ATOM   1291  O   LEU A 163     -93.995  38.955 -25.949  1.00 29.54           O
ANISOU 1291  O   LEU A 163     3529   2941   4755   -509    956   -765       O
ATOM   1292  CB  LEU A 163     -96.716  38.594 -26.900  1.00 30.78           C
ANISOU 1292  CB  LEU A 163     3358   3133   5205   -490    992  -1010       C
ATOM   1293  CG  LEU A 163     -96.663  37.074 -26.734  1.00 32.13           C
ANISOU 1293  CG  LEU A 163     3485   3354   5369   -610   1123  -1079       C
ATOM   1294  CD1 LEU A 163     -97.586  36.631 -25.613  1.00 32.80           C
ANISOU 1294  CD1 LEU A 163     3341   3471   5652   -596   1037  -1096       C
ATOM   1295  CD2 LEU A 163     -97.021  36.378 -28.034  1.00 30.92           C
ANISOU 1295  CD2 LEU A 163     3352   3224   5172   -678   1296  -1230       C
ATOM   1296  N   ASN A 164     -94.838  38.738 -23.860  1.00 29.46           N
ANISOU 1296  N   ASN A 164     3270   2957   4968   -505    817   -699       N
ATOM   1297  CA  ASN A 164     -93.569  38.370 -23.230  1.00 34.83           C
ANISOU 1297  CA  ASN A 164     4087   3632   5513   -554    844   -612       C
ATOM   1298  C   ASN A 164     -92.504  39.438 -23.471  1.00 36.52           C
ANISOU 1298  C   ASN A 164     4463   3810   5603   -484    808   -526       C
ATOM   1299  O   ASN A 164     -91.343  39.133 -23.747  1.00 38.68           O
ANISOU 1299  O   ASN A 164     4917   4064   5716   -509    876   -497       O
ATOM   1300  CB  ASN A 164     -93.084  37.002 -23.714  1.00 37.95           C
ANISOU 1300  CB  ASN A 164     4568   4046   5806   -676   1002   -681       C
ATOM   1301  CG  ASN A 164     -94.156  35.937 -23.617  1.00 36.05           C
ANISOU 1301  CG  ASN A 164     4137   3858   5701   -748   1048   -797       C
ATOM   1302  OD1 ASN A 164     -94.437  35.233 -24.588  1.00 36.51           O
ANISOU 1302  OD1 ASN A 164     4193   3937   5740   -816   1180   -912       O
ATOM   1303  ND2 ASN A 164     -94.767  35.818 -22.444  1.00 31.03           N
ANISOU 1303  ND2 ASN A 164     3341   3247   5201   -731    938   -773       N
ATOM   1304  N   GLY A 165     -92.906  40.702 -23.368  1.00 35.33           N
ANISOU 1304  N   GLY A 165     4248   3646   5532   -393    698   -492       N
ATOM   1305  CA  GLY A 165     -92.000  41.800 -23.624  1.00 32.10           C
ANISOU 1305  CA  GLY A 165     3948   3217   5032   -318    651   -433       C
ATOM   1306  C   GLY A 165     -91.730  42.079 -25.082  1.00 29.94           C
ANISOU 1306  C   GLY A 165     3788   2931   4656   -284    688   -493       C
ATOM   1307  O   GLY A 165     -90.863  42.906 -25.387  1.00 32.70           O
ANISOU 1307  O   GLY A 165     4239   3268   4916   -214    641   -454       O
ATOM   1308  N   VAL A 166     -92.437  41.417 -25.991  1.00 29.48           N
ANISOU 1308  N   VAL A 166     3718   2878   4606   -329    769   -594       N
ATOM   1309  CA  VAL A 166     -92.277  41.623 -27.424  1.00 30.85           C
ANISOU 1309  CA  VAL A 166     4018   3038   4667   -307    811   -660       C
ATOM   1310  C   VAL A 166     -93.529  42.326 -27.925  1.00 26.97           C
ANISOU 1310  C   VAL A 166     3388   2550   4311   -265    757   -738       C
ATOM   1311  O   VAL A 166     -94.621  41.745 -27.929  1.00 31.07           O
ANISOU 1311  O   VAL A 166     3776   3080   4948   -305    802   -816       O
ATOM   1312  CB  VAL A 166     -92.045  40.304 -28.172  1.00 32.66           C
ANISOU 1312  CB  VAL A 166     4374   3263   4771   -407    974   -726       C
ATOM   1313  CG1 VAL A 166     -91.831  40.569 -29.653  1.00 34.22           C
ANISOU 1313  CG1 VAL A 166     4740   3438   4823   -384   1014   -785       C
ATOM   1314  CG2 VAL A 166     -90.859  39.562 -27.580  1.00 31.16           C
ANISOU 1314  CG2 VAL A 166     4326   3056   4460   -461   1029   -650       C
ATOM   1315  N   THR A 167     -93.376  43.580 -28.336  1.00 30.34           N
ANISOU 1315  N   THR A 167     3837   2964   4726   -183    657   -727       N
ATOM   1316  CA  THR A 167     -94.486  44.332 -28.901  1.00 33.31           C
ANISOU 1316  CA  THR A 167     4110   3332   5216   -147    604   -806       C
ATOM   1317  C   THR A 167     -94.624  43.995 -30.380  1.00 37.74           C
ANISOU 1317  C   THR A 167     4789   3889   5661   -162    688   -915       C
ATOM   1318  O   THR A 167     -93.656  44.092 -31.140  1.00 38.31           O
ANISOU 1318  O   THR A 167     5050   3956   5549   -143    699   -904       O
ATOM   1319  CB  THR A 167     -94.270  45.833 -28.711  1.00 31.92           C
ANISOU 1319  CB  THR A 167     3900   3147   5079    -71    464   -761       C
ATOM   1320  OG1 THR A 167     -94.182  46.131 -27.312  1.00 33.69           O
ANISOU 1320  OG1 THR A 167     4025   3373   5404    -73    407   -663       O
ATOM   1321  CG2 THR A 167     -95.422  46.618 -29.317  1.00 25.67           C
ANISOU 1321  CG2 THR A 167     3016   2334   4402    -47    411   -850       C
ATOM   1322  N   LEU A 168     -95.826  43.595 -30.787  1.00 38.64           N
ANISOU 1322  N   LEU A 168     4802   4002   5877   -191    748  -1023       N
ATOM   1323  CA  LEU A 168     -96.035  43.124 -32.147  1.00 36.71           C
ANISOU 1323  CA  LEU A 168     4668   3758   5520   -224    861  -1140       C
ATOM   1324  C   LEU A 168     -97.507  43.249 -32.509  1.00 38.63           C
ANISOU 1324  C   LEU A 168     4760   3993   5926   -213    871  -1264       C
ATOM   1325  O   LEU A 168     -98.380  43.299 -31.638  1.00 41.40           O
ANISOU 1325  O   LEU A 168     4921   4335   6475   -194    819  -1260       O
ATOM   1326  CB  LEU A 168     -95.563  41.674 -32.309  1.00 39.04           C
ANISOU 1326  CB  LEU A 168     5062   4072   5699   -326   1031  -1158       C
ATOM   1327  CG  LEU A 168     -96.138  40.641 -31.330  1.00 41.10           C
ANISOU 1327  CG  LEU A 168     5145   4362   6109   -391   1094  -1170       C
ATOM   1328  CD1 LEU A 168     -97.414  39.998 -31.864  1.00 36.42           C
ANISOU 1328  CD1 LEU A 168     4416   3791   5631   -428   1199  -1327       C
ATOM   1329  CD2 LEU A 168     -95.104  39.578 -30.994  1.00 45.86           C
ANISOU 1329  CD2 LEU A 168     5869   4975   6582   -483   1197  -1115       C
ATOM   1330  N   ILE A 169     -97.764  43.295 -33.812  1.00 37.89           N
ANISOU 1330  N   ILE A 169     4767   3894   5737   -219    936  -1375       N
ATOM   1331  CA  ILE A 169     -99.118  43.219 -34.347  1.00 37.92           C
ANISOU 1331  CA  ILE A 169     4654   3887   5868   -215    985  -1520       C
ATOM   1332  C   ILE A 169     -99.391  41.755 -34.669  1.00 44.86           C
ANISOU 1332  C   ILE A 169     5519   4802   6722   -307   1185  -1617       C
ATOM   1333  O   ILE A 169     -98.797  41.190 -35.592  1.00 47.23           O
ANISOU 1333  O   ILE A 169     6005   5116   6823   -375   1317  -1657       O
ATOM   1334  CB  ILE A 169     -99.292  44.110 -35.582  1.00 35.12           C
ANISOU 1334  CB  ILE A 169     4413   3508   5422   -176    950  -1603       C
ATOM   1335  CG1 ILE A 169     -99.034  45.573 -35.215  1.00 36.58           C
ANISOU 1335  CG1 ILE A 169     4580   3666   5651    -99    752  -1522       C
ATOM   1336  CG2 ILE A 169    -100.686  43.943 -36.165  1.00 35.01           C
ANISOU 1336  CG2 ILE A 169     4291   3478   5534   -174   1021  -1768       C
ATOM   1337  CD1 ILE A 169     -99.203  46.534 -36.369  1.00 39.25           C
ANISOU 1337  CD1 ILE A 169     5017   3985   5911    -62    689  -1608       C
ATOM   1338  N   GLY A 170    -100.292  41.142 -33.907  1.00 45.64           N
ANISOU 1338  N   GLY A 170     5400   4917   7024   -312   1207  -1659       N
ATOM   1339  CA  GLY A 170    -100.450  39.701 -33.967  1.00 32.88           C
ANISOU 1339  CA  GLY A 170     3730   3353   5411   -409   1387  -1745       C
ATOM   1340  C   GLY A 170    -101.014  39.233 -35.298  1.00 39.15           C
ANISOU 1340  C   GLY A 170     4570   4162   6142   -457   1561  -1924       C
ATOM   1341  O   GLY A 170    -101.879  39.875 -35.896  1.00 40.52           O
ANISOU 1341  O   GLY A 170     4703   4307   6386   -392   1531  -2020       O
ATOM   1342  N   GLU A 171    -100.505  38.097 -35.761  1.00 40.65           N
ANISOU 1342  N   GLU A 171     4858   4394   6194   -583   1756  -1972       N
ATOM   1343  CA  GLU A 171    -101.012  37.403 -36.937  1.00 46.01           C
ANISOU 1343  CA  GLU A 171     5573   5100   6808   -663   1970  -2153       C
ATOM   1344  C   GLU A 171    -101.568  36.029 -36.608  1.00 47.13           C
ANISOU 1344  C   GLU A 171     5512   5314   7082   -758   2137  -2273       C
ATOM   1345  O   GLU A 171    -102.634  35.663 -37.110  1.00 53.03           O
ANISOU 1345  O   GLU A 171     6110   6092   7948   -757   2246  -2454       O
ATOM   1346  CB  GLU A 171     -99.904  37.272 -37.991  1.00 55.34           C
ANISOU 1346  CB  GLU A 171     7091   6263   7672   -753   2085  -2124       C
ATOM   1347  CG  GLU A 171     -99.316  38.602 -38.431  1.00 64.17           C
ANISOU 1347  CG  GLU A 171     8411   7322   8650   -654   1913  -2026       C
ATOM   1348  CD  GLU A 171     -98.154  38.439 -39.391  1.00 71.85           C
ANISOU 1348  CD  GLU A 171     9734   8267   9300   -724   1997  -1982       C
ATOM   1349  OE1 GLU A 171     -97.750  37.286 -39.651  1.00 75.29           O
ANISOU 1349  OE1 GLU A 171    10274   8717   9614   -863   2198  -2013       O
ATOM   1350  OE2 GLU A 171     -97.645  39.467 -39.887  1.00 73.41           O
ANISOU 1350  OE2 GLU A 171    10105   8423   9363   -641   1857  -1921       O
ATOM   1351  N   ALA A 172    -100.870  35.257 -35.780  1.00 43.95           N
ANISOU 1351  N   ALA A 172     5092   4942   6666   -838   2159  -2190       N
ATOM   1352  CA  ALA A 172    -101.393  34.015 -35.232  1.00 45.71           C
ANISOU 1352  CA  ALA A 172     5078   5242   7049   -920   2272  -2296       C
ATOM   1353  C   ALA A 172    -102.110  34.224 -33.906  1.00 46.22           C
ANISOU 1353  C   ALA A 172     4864   5316   7379   -802   2072  -2254       C
ATOM   1354  O   ALA A 172    -102.579  33.251 -33.307  1.00 47.53           O
ANISOU 1354  O   ALA A 172     4808   5551   7701   -846   2118  -2337       O
ATOM   1355  CB  ALA A 172    -100.263  32.997 -35.050  1.00 42.14           C
ANISOU 1355  CB  ALA A 172     4764   4814   6435  -1089   2408  -2240       C
ATOM   1356  N   VAL A 173    -102.198  35.470 -33.436  1.00 45.67           N
ANISOU 1356  N   VAL A 173     4811   5180   7361   -660   1850  -2132       N
ATOM   1357  CA  VAL A 173    -102.881  35.803 -32.193  1.00 45.06           C
ANISOU 1357  CA  VAL A 173     4518   5090   7512   -545   1651  -2075       C
ATOM   1358  C   VAL A 173    -103.448  37.209 -32.343  1.00 45.40           C
ANISOU 1358  C   VAL A 173     4581   5050   7619   -403   1490  -2039       C
ATOM   1359  O   VAL A 173    -103.015  37.987 -33.195  1.00 46.24           O
ANISOU 1359  O   VAL A 173     4882   5117   7572   -398   1498  -2016       O
ATOM   1360  CB  VAL A 173    -101.935  35.701 -30.970  1.00 43.84           C
ANISOU 1360  CB  VAL A 173     4402   4938   7317   -573   1545  -1896       C
ATOM   1361  CG1 VAL A 173    -101.006  36.905 -30.904  1.00 38.41           C
ANISOU 1361  CG1 VAL A 173     3930   4182   6481   -525   1423  -1723       C
ATOM   1362  CG2 VAL A 173    -102.728  35.537 -29.678  1.00 49.01           C
ANISOU 1362  CG2 VAL A 173     4812   5604   8204   -495   1391  -1879       C
ATOM   1363  N   LYS A 174    -104.437  37.530 -31.514  1.00 44.22           N
ANISOU 1363  N   LYS A 174     4237   4869   7694   -289   1337  -2038       N
ATOM   1364  CA  LYS A 174    -105.160  38.792 -31.608  1.00 43.44           C
ANISOU 1364  CA  LYS A 174     4138   4680   7688   -164   1192  -2024       C
ATOM   1365  C   LYS A 174    -104.570  39.787 -30.615  1.00 40.72           C
ANISOU 1365  C   LYS A 174     3870   4280   7323   -123   1003  -1819       C
ATOM   1366  O   LYS A 174    -104.510  39.508 -29.413  1.00 39.11           O
ANISOU 1366  O   LYS A 174     3578   4084   7198   -112    909  -1725       O
ATOM   1367  CB  LYS A 174    -106.650  38.575 -31.343  1.00 50.16           C
ANISOU 1367  CB  LYS A 174     4754   5509   8796    -59   1142  -2152       C
ATOM   1368  CG  LYS A 174    -107.559  39.574 -32.034  1.00 60.79           C
ANISOU 1368  CG  LYS A 174     6116   6764  10216     41   1092  -2230       C
ATOM   1369  CD  LYS A 174    -108.917  38.956 -32.327  1.00 66.56           C
ANISOU 1369  CD  LYS A 174     6639   7499  11151    117   1148  -2435       C
ATOM   1370  CE  LYS A 174    -108.775  37.718 -33.203  1.00 69.63           C
ANISOU 1370  CE  LYS A 174     6999   8006  11450     -2   1380  -2582       C
ATOM   1371  NZ  LYS A 174    -110.089  37.093 -33.517  1.00 71.44           N
ANISOU 1371  NZ  LYS A 174     7056   8268  11820     37   1394  -2725       N
ATOM   1372  N   THR A 175    -104.139  40.947 -31.120  1.00 37.00           N
ANISOU 1372  N   THR A 175     3558   3756   6743   -103    948  -1758       N
ATOM   1373  CA  THR A 175    -103.500  41.963 -30.296  1.00 35.14           C
ANISOU 1373  CA  THR A 175     3396   3479   6478    -77    793  -1580       C
ATOM   1374  C   THR A 175    -104.257  43.283 -30.230  1.00 34.58           C
ANISOU 1374  C   THR A 175     3306   3313   6520     10    652  -1567       C
ATOM   1375  O   THR A 175    -103.904  44.131 -29.402  1.00 32.66           O
ANISOU 1375  O   THR A 175     3090   3031   6288     26    525  -1429       O
ATOM   1376  CB  THR A 175    -102.071  42.238 -30.794  1.00 33.63           C
ANISOU 1376  CB  THR A 175     3413   3317   6049   -137    835  -1501       C
ATOM   1377  OG1 THR A 175    -102.093  42.529 -32.196  1.00 38.14           O
ANISOU 1377  OG1 THR A 175     4099   3883   6509   -144    912  -1607       O
ATOM   1378  CG2 THR A 175    -101.176  41.035 -30.546  1.00 33.92           C
ANISOU 1378  CG2 THR A 175     3494   3421   5971   -230    949  -1470       C
ATOM   1379  N   GLN A 176    -105.273  43.488 -31.063  1.00 34.35           N
ANISOU 1379  N   GLN A 176     3235   3242   6574     56    678  -1711       N
ATOM   1380  CA  GLN A 176    -106.065  44.713 -31.046  1.00 35.36           C
ANISOU 1380  CA  GLN A 176     3354   3265   6816    128    552  -1713       C
ATOM   1381  C   GLN A 176    -107.326  44.468 -30.227  1.00 39.38           C
ANISOU 1381  C   GLN A 176     3699   3707   7556    212    473  -1739       C
ATOM   1382  O   GLN A 176    -108.122  43.582 -30.557  1.00 47.62           O
ANISOU 1382  O   GLN A 176     4627   4770   8696    246    551  -1881       O
ATOM   1383  CB  GLN A 176    -106.413  45.158 -32.466  1.00 40.42           C
ANISOU 1383  CB  GLN A 176     4072   3885   7400    133    618  -1859       C
ATOM   1384  CG  GLN A 176    -107.012  46.554 -32.553  1.00 41.62           C
ANISOU 1384  CG  GLN A 176     4250   3927   7635    182    489  -1858       C
ATOM   1385  CD  GLN A 176    -107.056  47.081 -33.975  1.00 46.88           C
ANISOU 1385  CD  GLN A 176     5029   4588   8195    170    542  -1987       C
ATOM   1386  OE1 GLN A 176    -107.075  46.310 -34.935  1.00 52.22           O
ANISOU 1386  OE1 GLN A 176     5739   5319   8782    146    686  -2113       O
ATOM   1387  NE2 GLN A 176    -107.063  48.401 -34.117  1.00 47.91           N
ANISOU 1387  NE2 GLN A 176     5222   4652   8327    175    428  -1961       N
ATOM   1388  N   PHE A 177    -107.506  45.247 -29.165  1.00 36.71           N
ANISOU 1388  N   PHE A 177     3354   3289   7303    246    320  -1608       N
ATOM   1389  CA  PHE A 177    -108.584  45.033 -28.212  1.00 42.84           C
ANISOU 1389  CA  PHE A 177     4010   3989   8278    331    215  -1597       C
ATOM   1390  C   PHE A 177    -109.594  46.173 -28.263  1.00 44.34           C
ANISOU 1390  C   PHE A 177     4224   4028   8594    400    108  -1615       C
ATOM   1391  O   PHE A 177    -109.345  47.243 -28.823  1.00 43.35           O
ANISOU 1391  O   PHE A 177     4204   3862   8404    365     98  -1609       O
ATOM   1392  CB  PHE A 177    -108.034  44.900 -26.786  1.00 40.78           C
ANISOU 1392  CB  PHE A 177     3746   3742   8005    309    122  -1419       C
ATOM   1393  CG  PHE A 177    -106.827  44.015 -26.677  1.00 43.11           C
ANISOU 1393  CG  PHE A 177     4060   4170   8149    222    218  -1375       C
ATOM   1394  CD1 PHE A 177    -106.925  42.652 -26.909  1.00 46.32           C
ANISOU 1394  CD1 PHE A 177     4363   4667   8570    208    321  -1481       C
ATOM   1395  CD2 PHE A 177    -105.596  44.543 -26.326  1.00 43.19           C
ANISOU 1395  CD2 PHE A 177     4190   4211   8008    151    208  -1236       C
ATOM   1396  CE1 PHE A 177    -105.813  41.835 -26.805  1.00 46.21           C
ANISOU 1396  CE1 PHE A 177     4385   4760   8414    113    415  -1442       C
ATOM   1397  CE2 PHE A 177    -104.481  43.732 -26.219  1.00 39.82           C
ANISOU 1397  CE2 PHE A 177     3801   3889   7441     76    294  -1196       C
ATOM   1398  CZ  PHE A 177    -104.589  42.377 -26.458  1.00 41.19           C
ANISOU 1398  CZ  PHE A 177     3890   4138   7622     52    398  -1295       C
ATOM   1399  N   ASN A 178    -110.751  45.918 -27.659  1.00 35.25           N
ANISOU 1399  N   ASN A 178     2976   2789   7627    502     20  -1642       N
ATOM   1400  CA  ASN A 178    -111.729  46.951 -27.355  1.00 36.05           C
ANISOU 1400  CA  ASN A 178     3131   2760   7806    546   -112  -1590       C
ATOM   1401  C   ASN A 178    -111.525  47.401 -25.915  1.00 40.43           C
ANISOU 1401  C   ASN A 178     3732   3239   8390    540   -246  -1402       C
ATOM   1402  O   ASN A 178    -111.379  46.566 -25.017  1.00 35.20           O
ANISOU 1402  O   ASN A 178     3002   2610   7763    568   -283  -1346       O
ATOM   1403  CB  ASN A 178    -113.156  46.438 -27.551  1.00 40.31           C
ANISOU 1403  CB  ASN A 178     3579   3274   8464    645   -142  -1697       C
ATOM   1404  CG  ASN A 178    -113.473  46.138 -29.002  1.00 45.76           C
ANISOU 1404  CG  ASN A 178     4242   4025   9122    643     -6  -1883       C
ATOM   1405  OD1 ASN A 178    -112.893  46.730 -29.911  1.00 50.96           O
ANISOU 1405  OD1 ASN A 178     4992   4700   9671    577     73  -1921       O
ATOM   1406  ND2 ASN A 178    -114.402  45.216 -29.225  1.00 48.54           N
ANISOU 1406  ND2 ASN A 178     4471   4411   9561    714     19  -2003       N
ATOM   1407  N   TYR A 179    -111.514  48.712 -25.696  1.00 38.74           N
ANISOU 1407  N   TYR A 179     3634   2927   8156    496   -313  -1310       N
ATOM   1408  CA  TYR A 179    -111.228  49.281 -24.388  1.00 38.82           C
ANISOU 1408  CA  TYR A 179     3716   2866   8166    462   -415  -1128       C
ATOM   1409  C   TYR A 179    -112.489  49.863 -23.765  1.00 36.03           C
ANISOU 1409  C   TYR A 179     3417   2374   7898    517   -541  -1072       C
ATOM   1410  O   TYR A 179    -113.336  50.431 -24.462  1.00 44.99           O
ANISOU 1410  O   TYR A 179     4581   3445   9070    542   -546  -1153       O
ATOM   1411  CB  TYR A 179    -110.145  50.358 -24.485  1.00 38.35           C
ANISOU 1411  CB  TYR A 179     3752   2815   8003    345   -383  -1055       C
ATOM   1412  CG  TYR A 179    -108.742  49.797 -24.552  1.00 35.02           C
ANISOU 1412  CG  TYR A 179     3317   2572   7415    275   -294  -1014       C
ATOM   1413  CD1 TYR A 179    -107.952  49.716 -23.412  1.00 30.83           C
ANISOU 1413  CD1 TYR A 179     2816   2087   6812    224   -321   -858       C
ATOM   1414  CD2 TYR A 179    -108.212  49.340 -25.751  1.00 34.12           C
ANISOU 1414  CD2 TYR A 179     3182   2571   7209    261   -180  -1132       C
ATOM   1415  CE1 TYR A 179    -106.670  49.203 -23.467  1.00 33.00           C
ANISOU 1415  CE1 TYR A 179     3093   2509   6938    167   -240   -824       C
ATOM   1416  CE2 TYR A 179    -106.933  48.824 -25.815  1.00 34.42           C
ANISOU 1416  CE2 TYR A 179     3236   2750   7090    201   -102  -1089       C
ATOM   1417  CZ  TYR A 179    -106.167  48.758 -24.670  1.00 34.17           C
ANISOU 1417  CZ  TYR A 179     3227   2755   7000    158   -135   -938       C
ATOM   1418  OH  TYR A 179    -104.892  48.246 -24.732  1.00 35.69           O
ANISOU 1418  OH  TYR A 179     3448   3073   7039    106    -59   -900       O
ATOM   1419  N   TYR A 180    -112.604  49.709 -22.448  1.00 36.15           N
ANISOU 1419  N   TYR A 180     3464   2337   7934    535   -644   -934       N
ATOM   1420  CA  TYR A 180    -113.737  50.205 -21.683  1.00 41.60           C
ANISOU 1420  CA  TYR A 180     4239   2883   8682    588   -773   -859       C
ATOM   1421  C   TYR A 180    -113.227  50.697 -20.338  1.00 44.57           C
ANISOU 1421  C   TYR A 180     4731   3206   8999    518   -840   -664       C
ATOM   1422  O   TYR A 180    -112.286  50.125 -19.781  1.00 49.75           O
ANISOU 1422  O   TYR A 180     5354   3941   9606    484   -824   -600       O
ATOM   1423  CB  TYR A 180    -114.798  49.115 -21.476  1.00 39.24           C
ANISOU 1423  CB  TYR A 180     3847   2580   8482    732   -852   -927       C
ATOM   1424  CG  TYR A 180    -115.169  48.353 -22.731  1.00 45.13           C
ANISOU 1424  CG  TYR A 180     4453   3416   9278    791   -760  -1128       C
ATOM   1425  CD1 TYR A 180    -114.442  47.238 -23.131  1.00 46.37           C
ANISOU 1425  CD1 TYR A 180     4475   3728   9417    780   -660  -1213       C
ATOM   1426  CD2 TYR A 180    -116.251  48.741 -23.509  1.00 44.58           C
ANISOU 1426  CD2 TYR A 180     4398   3274   9268    850   -761  -1235       C
ATOM   1427  CE1 TYR A 180    -114.778  46.538 -24.275  1.00 44.95           C
ANISOU 1427  CE1 TYR A 180     4180   3633   9265    815   -555  -1398       C
ATOM   1428  CE2 TYR A 180    -116.596  48.045 -24.652  1.00 44.09           C
ANISOU 1428  CE2 TYR A 180     4216   3295   9239    895   -664  -1420       C
ATOM   1429  CZ  TYR A 180    -115.856  46.946 -25.031  1.00 49.12           C
ANISOU 1429  CZ  TYR A 180     4723   4092   9849    872   -557  -1500       C
ATOM   1430  OH  TYR A 180    -116.197  46.252 -26.170  1.00 55.04           O
ANISOU 1430  OH  TYR A 180     5367   4927  10619    899   -442  -1685       O
ATOM   1431  N   LYS A 181    -113.845  51.756 -19.816  1.00 46.02           N
ANISOU 1431  N   LYS A 181     5059   3251   9176    488   -906   -574       N
ATOM   1432  CA  LYS A 181    -113.411  52.342 -18.556  1.00 44.08           C
ANISOU 1432  CA  LYS A 181     4946   2949   8852    401   -949   -391       C
ATOM   1433  C   LYS A 181    -114.615  52.811 -17.754  1.00 43.80           C
ANISOU 1433  C   LYS A 181     5059   2744   8838    449  -1067   -308       C
ATOM   1434  O   LYS A 181    -115.568  53.362 -18.311  1.00 41.23           O
ANISOU 1434  O   LYS A 181     4779   2319   8566    485  -1080   -375       O
ATOM   1435  CB  LYS A 181    -112.447  53.514 -18.786  1.00 40.37           C
ANISOU 1435  CB  LYS A 181     4532   2506   8300    241   -848   -352       C
ATOM   1436  CG  LYS A 181    -111.819  54.057 -17.511  1.00 37.43           C
ANISOU 1436  CG  LYS A 181     4280   2111   7832    131   -856   -176       C
ATOM   1437  CD  LYS A 181    -110.826  55.170 -17.806  1.00 37.56           C
ANISOU 1437  CD  LYS A 181     4311   2182   7777    -24   -748   -165       C
ATOM   1438  CE  LYS A 181    -110.198  55.698 -16.525  1.00 42.44           C
ANISOU 1438  CE  LYS A 181     5039   2791   8293   -141   -733     -2       C
ATOM   1439  NZ  LYS A 181    -109.244  56.811 -16.785  1.00 47.74           N
ANISOU 1439  NZ  LYS A 181     5701   3530   8907   -289   -626     -6       N
ATOM   1440  N   LYS A 182    -114.560  52.588 -16.442  1.00 41.57           N
ANISOU 1440  N   LYS A 182     4870   2422   8504    448  -1152   -162       N
ATOM   1441  CA  LYS A 182    -115.582  53.042 -15.512  1.00 42.20           C
ANISOU 1441  CA  LYS A 182     5132   2333   8569    484  -1265    -57       C
ATOM   1442  C   LYS A 182    -114.928  53.852 -14.405  1.00 41.91           C
ANISOU 1442  C   LYS A 182     5268   2256   8402    335  -1240    118       C
ATOM   1443  O   LYS A 182    -113.858  53.489 -13.909  1.00 54.22           O
ANISOU 1443  O   LYS A 182     6791   3922   9890    270  -1204    182       O
ATOM   1444  CB  LYS A 182    -116.355  51.866 -14.905  1.00 43.49           C
ANISOU 1444  CB  LYS A 182     5259   2480   8785    652  -1417    -57       C
ATOM   1445  CG  LYS A 182    -117.347  51.218 -15.851  1.00 69.87           C
ANISOU 1445  CG  LYS A 182     8463   5826  12258    806  -1450   -229       C
ATOM   1446  CD  LYS A 182    -118.011  50.009 -15.211  1.00 63.48           C
ANISOU 1446  CD  LYS A 182     7589   5030  11502    967  -1602   -240       C
ATOM   1447  CE  LYS A 182    -118.811  50.402 -13.981  1.00 58.94           C
ANISOU 1447  CE  LYS A 182     7233   4288  10875   1011  -1751    -92       C
ATOM   1448  NZ  LYS A 182    -119.374  49.212 -13.287  1.00 58.06           N
ANISOU 1448  NZ  LYS A 182     7055   4202  10804   1168  -1918   -101       N
ATOM   1449  N   VAL A 183    -115.574  54.951 -14.024  1.00 45.28           N
ANISOU 1449  N   VAL A 183     5886   2526   8791    274  -1246    188       N
ATOM   1450  CA  VAL A 183    -115.099  55.815 -12.949  1.00 48.69           C
ANISOU 1450  CA  VAL A 183     6503   2906   9091    120  -1203    346       C
ATOM   1451  C   VAL A 183    -116.243  56.019 -11.968  1.00 54.41           C
ANISOU 1451  C   VAL A 183     7451   3441   9782    176  -1316    452       C
ATOM   1452  O   VAL A 183    -117.301  56.537 -12.345  1.00 54.37           O
ANISOU 1452  O   VAL A 183     7529   3294   9835    222  -1343    410       O
ATOM   1453  CB  VAL A 183    -114.586  57.166 -13.473  1.00 50.84           C
ANISOU 1453  CB  VAL A 183     6804   3179   9334    -58  -1055    322       C
ATOM   1454  CG1 VAL A 183    -114.334  58.118 -12.316  1.00 51.96           C
ANISOU 1454  CG1 VAL A 183     7153   3243   9346   -219  -1000    472       C
ATOM   1455  CG2 VAL A 183    -113.315  56.972 -14.285  1.00 40.85           C
ANISOU 1455  CG2 VAL A 183     5337   2108   8076   -113   -951    238       C
ATOM   1456  N   ASP A 184    -116.028  55.614 -10.715  1.00 53.62           N
ANISOU 1456  N   ASP A 184     6232   4780   9360    763  -1865    843       N
ATOM   1457  CA  ASP A 184    -117.028  55.744  -9.653  1.00 61.30           C
ANISOU 1457  CA  ASP A 184     7245   5704  10343    818  -2031   1003       C
ATOM   1458  C   ASP A 184    -118.358  55.120 -10.065  1.00 59.79           C
ANISOU 1458  C   ASP A 184     7016   5340  10361    930  -2156    906       C
ATOM   1459  O   ASP A 184    -119.433  55.677  -9.831  1.00 62.52           O
ANISOU 1459  O   ASP A 184     7419   5568  10767    935  -2257   1013       O
ATOM   1460  CB  ASP A 184    -117.206  57.206  -9.242  1.00 71.85           C
ANISOU 1460  CB  ASP A 184     8677   6985  11640    726  -2060   1249       C
ATOM   1461  CG  ASP A 184    -115.984  57.763  -8.535  1.00 81.52           C
ANISOU 1461  CG  ASP A 184     9926   8412  12636    633  -1958   1362       C
ATOM   1462  OD1 ASP A 184    -115.298  56.988  -7.835  1.00 84.76           O
ANISOU 1462  OD1 ASP A 184    10300   9004  12900    669  -1934   1310       O
ATOM   1463  OD2 ASP A 184    -115.708  58.973  -8.680  1.00 83.68           O
ANISOU 1463  OD2 ASP A 184    10248   8664  12881    526  -1904   1494       O
ATOM   1464  N   GLY A 185    -118.282  53.944 -10.688  1.00 56.74           N
ANISOU 1464  N   GLY A 185     6533   4981  10044    997  -2113    679       N
ATOM   1465  CA  GLY A 185    -119.456  53.228 -11.134  1.00 55.94           C
ANISOU 1465  CA  GLY A 185     6382   4795  10078   1078  -2172    534       C
ATOM   1466  C   GLY A 185    -120.031  53.685 -12.455  1.00 54.03           C
ANISOU 1466  C   GLY A 185     6147   4434   9947   1042  -2107    428       C
ATOM   1467  O   GLY A 185    -120.911  53.003 -12.997  1.00 55.53           O
ANISOU 1467  O   GLY A 185     6279   4583  10237   1105  -2128    271       O
ATOM   1468  N   VAL A 186    -119.568  54.807 -12.997  1.00 52.98           N
ANISOU 1468  N   VAL A 186     6077   4256   9795    944  -2032    501       N
ATOM   1469  CA  VAL A 186    -120.098  55.365 -14.235  1.00 53.70           C
ANISOU 1469  CA  VAL A 186     6181   4247   9974    908  -1981    406       C
ATOM   1470  C   VAL A 186    -119.167  54.995 -15.380  1.00 48.90           C
ANISOU 1470  C   VAL A 186     5520   3701   9358    879  -1825    239       C
ATOM   1471  O   VAL A 186    -117.958  55.254 -15.317  1.00 45.25           O
ANISOU 1471  O   VAL A 186     5073   3305   8813    821  -1742    291       O
ATOM   1472  CB  VAL A 186    -120.262  56.890 -14.133  1.00 54.51           C
ANISOU 1472  CB  VAL A 186     6384   4261  10066    813  -2007    588       C
ATOM   1473  CG1 VAL A 186    -120.736  57.462 -15.461  1.00 54.76           C
ANISOU 1473  CG1 VAL A 186     6420   4204  10181    780  -1960    470       C
ATOM   1474  CG2 VAL A 186    -121.230  57.246 -13.015  1.00 55.69           C
ANISOU 1474  CG2 VAL A 186     6591   4346  10224    834  -2159    763       C
ATOM   1475  N   VAL A 187    -119.730  54.388 -16.426  1.00 46.19           N
ANISOU 1475  N   VAL A 187     5115   3340   9096    921  -1785     42       N
ATOM   1476  CA  VAL A 187    -118.958  54.082 -17.623  1.00 42.81           C
ANISOU 1476  CA  VAL A 187     4644   2969   8653    889  -1635   -111       C
ATOM   1477  C   VAL A 187    -118.514  55.379 -18.283  1.00 47.76           C
ANISOU 1477  C   VAL A 187     5349   3553   9246    794  -1574    -46       C
ATOM   1478  O   VAL A 187    -119.279  56.350 -18.368  1.00 58.88           O
ANISOU 1478  O   VAL A 187     6814   4862  10694    771  -1642     24       O
ATOM   1479  CB  VAL A 187    -119.787  53.221 -18.590  1.00 46.97           C
ANISOU 1479  CB  VAL A 187     5086   3492   9266    955  -1613   -320       C
ATOM   1480  CG1 VAL A 187    -118.962  52.838 -19.810  1.00 46.99           C
ANISOU 1480  CG1 VAL A 187     5046   3569   9240    920  -1452   -465       C
ATOM   1481  CG2 VAL A 187    -120.312  51.983 -17.881  1.00 50.61           C
ANISOU 1481  CG2 VAL A 187     5463   3995   9770   1047  -1685   -381       C
ATOM   1482  N   GLN A 188    -117.272  55.405 -18.749  1.00 45.93           N
ANISOU 1482  N   GLN A 188     5117   3392   8942    737  -1451    -72       N
ATOM   1483  CA  GLN A 188    -116.704  56.581 -19.386  1.00 49.31           C
ANISOU 1483  CA  GLN A 188     5611   3799   9327    646  -1387    -20       C
ATOM   1484  C   GLN A 188    -116.662  56.402 -20.898  1.00 51.44           C
ANISOU 1484  C   GLN A 188     5853   4084   9608    642  -1286   -198       C
ATOM   1485  O   GLN A 188    -116.559  55.284 -21.407  1.00 58.46           O
ANISOU 1485  O   GLN A 188     6671   5034  10507    687  -1220   -346       O
ATOM   1486  CB  GLN A 188    -115.293  56.855 -18.863  1.00 55.04           C
ANISOU 1486  CB  GLN A 188     6363   4594   9956    583  -1325     86       C
ATOM   1487  CG  GLN A 188    -115.214  56.984 -17.356  1.00 61.49           C
ANISOU 1487  CG  GLN A 188     7202   5420  10741    593  -1420    267       C
ATOM   1488  CD  GLN A 188    -116.084  58.104 -16.826  1.00 66.94           C
ANISOU 1488  CD  GLN A 188     7959   6020  11456    559  -1525    432       C
ATOM   1489  OE1 GLN A 188    -115.798  59.282 -17.039  1.00 69.65           O
ANISOU 1489  OE1 GLN A 188     8355   6333  11775    470  -1501    526       O
ATOM   1490  NE2 GLN A 188    -117.159  57.742 -16.134  1.00 68.05           N
ANISOU 1490  NE2 GLN A 188     8094   6116  11646    625  -1644    467       N
ATOM   1491  N   GLN A 189    -116.747  57.520 -21.611  1.00 49.46           N
ANISOU 1491  N   GLN A 189     5656   3783   9352    587  -1275   -180       N
ATOM   1492  CA  GLN A 189    -116.566  57.544 -23.057  1.00 53.49           C
ANISOU 1492  CA  GLN A 189     6158   4317   9849    577  -1181   -328       C
ATOM   1493  C   GLN A 189    -115.133  57.978 -23.340  1.00 48.75           C
ANISOU 1493  C   GLN A 189     5594   3782   9148    496  -1077   -287       C
ATOM   1494  O   GLN A 189    -114.752  59.115 -23.045  1.00 51.13           O
ANISOU 1494  O   GLN A 189     5952   4057   9417    426  -1098   -159       O
ATOM   1495  CB  GLN A 189    -117.568  58.479 -23.729  1.00 62.58           C
ANISOU 1495  CB  GLN A 189     7341   5375  11062    578  -1245   -354       C
ATOM   1496  CG  GLN A 189    -117.364  58.602 -25.233  1.00 72.01           C
ANISOU 1496  CG  GLN A 189     8532   6596  12231    573  -1157   -502       C
ATOM   1497  CD  GLN A 189    -118.465  59.388 -25.913  1.00 82.96           C
ANISOU 1497  CD  GLN A 189     9940   7889  13694    594  -1233   -556       C
ATOM   1498  OE1 GLN A 189    -119.431  59.808 -25.275  1.00 85.53           O
ANISOU 1498  OE1 GLN A 189    10279   8119  14099    611  -1353   -486       O
ATOM   1499  NE2 GLN A 189    -118.327  59.591 -27.218  1.00 86.41           N
ANISOU 1499  NE2 GLN A 189    10381   8347  14105    594  -1170   -683       N
ATOM   1500  N   LEU A 190    -114.342  57.071 -23.901  1.00 44.30           N
ANISOU 1500  N   LEU A 190     4991   3302   8537    503   -967   -392       N
ATOM   1501  CA  LEU A 190    -112.943  57.369 -24.154  1.00 39.71           C
ANISOU 1501  CA  LEU A 190     4444   2782   7862    432   -873   -360       C
ATOM   1502  C   LEU A 190    -112.813  58.328 -25.335  1.00 38.60           C
ANISOU 1502  C   LEU A 190     4350   2626   7689    389   -836   -398       C
ATOM   1503  O   LEU A 190    -113.546  58.205 -26.322  1.00 41.07           O
ANISOU 1503  O   LEU A 190     4648   2918   8038    428   -831   -521       O
ATOM   1504  CB  LEU A 190    -112.164  56.082 -24.421  1.00 40.70           C
ANISOU 1504  CB  LEU A 190     4517   2992   7955    448   -771   -459       C
ATOM   1505  CG  LEU A 190    -112.124  55.112 -23.237  1.00 39.23           C
ANISOU 1505  CG  LEU A 190     4278   2830   7798    490   -808   -430       C
ATOM   1506  CD1 LEU A 190    -111.349  53.852 -23.581  1.00 36.54           C
ANISOU 1506  CD1 LEU A 190     3880   2595   7409    486   -700   -533       C
ATOM   1507  CD2 LEU A 190    -111.530  55.788 -22.009  1.00 37.34           C
ANISOU 1507  CD2 LEU A 190     4083   2618   7485    446   -856   -259       C
ATOM   1508  N   PRO A 191    -111.898  59.289 -25.268  1.00 40.42           N
ANISOU 1508  N   PRO A 191     4632   2869   7855    315   -816   -304       N
ATOM   1509  CA  PRO A 191    -111.818  60.321 -26.304  1.00 44.15           C
ANISOU 1509  CA  PRO A 191     5148   3321   8304    275   -803   -333       C
ATOM   1510  C   PRO A 191    -111.119  59.813 -27.558  1.00 41.96           C
ANISOU 1510  C   PRO A 191     4871   3106   7964    278   -695   -463       C
ATOM   1511  O   PRO A 191    -110.505  58.746 -27.580  1.00 41.16           O
ANISOU 1511  O   PRO A 191     4742   3068   7831    292   -618   -511       O
ATOM   1512  CB  PRO A 191    -110.998  61.423 -25.628  1.00 42.83           C
ANISOU 1512  CB  PRO A 191     5021   3158   8096    194   -819   -179       C
ATOM   1513  CG  PRO A 191    -110.096  60.674 -24.705  1.00 37.83           C
ANISOU 1513  CG  PRO A 191     4367   2587   7420    192   -779   -123       C
ATOM   1514  CD  PRO A 191    -110.901  59.500 -24.202  1.00 36.65           C
ANISOU 1514  CD  PRO A 191     4170   2427   7330    268   -811   -170       C
ATOM   1515  N   GLU A 192    -111.237  60.609 -28.621  1.00 42.33           N
ANISOU 1515  N   GLU A 192     4954   3132   7999    263   -694   -518       N
ATOM   1516  CA  GLU A 192    -110.442  60.372 -29.817  1.00 38.00           C
ANISOU 1516  CA  GLU A 192     4424   2638   7377    255   -600   -617       C
ATOM   1517  C   GLU A 192    -108.964  60.464 -29.471  1.00 34.38           C
ANISOU 1517  C   GLU A 192     3990   2239   6835    194   -543   -533       C
ATOM   1518  O   GLU A 192    -108.529  61.410 -28.809  1.00 40.01           O
ANISOU 1518  O   GLU A 192     4725   2942   7536    143   -584   -415       O
ATOM   1519  CB  GLU A 192    -110.787  61.388 -30.905  1.00 34.33           C
ANISOU 1519  CB  GLU A 192     3998   2133   6913    248   -631   -678       C
ATOM   1520  CG  GLU A 192    -112.112  61.159 -31.602  1.00 35.20           C
ANISOU 1520  CG  GLU A 192     4085   2197   7094    320   -669   -809       C
ATOM   1521  CD  GLU A 192    -112.257  62.013 -32.847  1.00 42.44           C
ANISOU 1521  CD  GLU A 192     5041   3089   7994    319   -684   -900       C
ATOM   1522  OE1 GLU A 192    -111.284  62.710 -33.203  1.00 40.43           O
ANISOU 1522  OE1 GLU A 192     4832   2857   7673    263   -663   -864       O
ATOM   1523  OE2 GLU A 192    -113.340  61.987 -33.469  1.00 50.01           O
ANISOU 1523  OE2 GLU A 192     5984   4007   9010    380   -725  -1016       O
ATOM   1524  N   THR A 193    -108.190  59.480 -29.917  1.00 30.31           N
ANISOU 1524  N   THR A 193     3466   1783   6267    200   -448   -597       N
ATOM   1525  CA  THR A 193    -106.778  59.438 -29.576  1.00 32.05           C
ANISOU 1525  CA  THR A 193     3707   2055   6414    151   -397   -528       C
ATOM   1526  C   THR A 193    -105.975  58.861 -30.731  1.00 35.66           C
ANISOU 1526  C   THR A 193     4187   2588   6774    141   -297   -606       C
ATOM   1527  O   THR A 193    -106.445  57.972 -31.448  1.00 32.60           O
ANISOU 1527  O   THR A 193     3775   2217   6395    175   -244   -712       O
ATOM   1528  CB  THR A 193    -106.528  58.609 -28.309  1.00 29.76           C
ANISOU 1528  CB  THR A 193     3374   1816   6116    156   -393   -462       C
ATOM   1529  OG1 THR A 193    -105.118  58.483 -28.088  1.00 32.45           O
ANISOU 1529  OG1 THR A 193     3734   2247   6348    114   -336   -411       O
ATOM   1530  CG2 THR A 193    -107.138  57.225 -28.441  1.00 29.02           C
ANISOU 1530  CG2 THR A 193     3224   1737   6065    206   -355   -559       C
ATOM   1531  N   TYR A 194    -104.771  59.392 -30.913  1.00 35.76           N
ANISOU 1531  N   TYR A 194     4245   2649   6694     95   -273   -551       N
ATOM   1532  CA  TYR A 194    -103.772  58.729 -31.727  1.00 31.33           C
ANISOU 1532  CA  TYR A 194     3711   2164   6028     79   -182   -586       C
ATOM   1533  C   TYR A 194    -103.077  57.654 -30.899  1.00 31.58           C
ANISOU 1533  C   TYR A 194     3712   2253   6033     68   -138   -545       C
ATOM   1534  O   TYR A 194    -103.227  57.578 -29.677  1.00 32.56           O
ANISOU 1534  O   TYR A 194     3800   2372   6199     74   -180   -487       O
ATOM   1535  CB  TYR A 194    -102.750  59.733 -32.260  1.00 28.68           C
ANISOU 1535  CB  TYR A 194     3437   1849   5612     44   -190   -547       C
ATOM   1536  CG  TYR A 194    -103.309  60.751 -33.228  1.00 31.40           C
ANISOU 1536  CG  TYR A 194     3814   2143   5972     51   -235   -604       C
ATOM   1537  CD1 TYR A 194    -103.477  60.442 -34.572  1.00 30.99           C
ANISOU 1537  CD1 TYR A 194     3792   2113   5868     70   -189   -706       C
ATOM   1538  CD2 TYR A 194    -103.652  62.028 -32.802  1.00 31.82           C
ANISOU 1538  CD2 TYR A 194     3866   2133   6091     34   -325   -555       C
ATOM   1539  CE1 TYR A 194    -103.982  61.373 -35.463  1.00 34.07           C
ANISOU 1539  CE1 TYR A 194     4213   2462   6270     83   -239   -774       C
ATOM   1540  CE2 TYR A 194    -104.157  62.967 -33.686  1.00 34.07           C
ANISOU 1540  CE2 TYR A 194     4178   2363   6404     37   -378   -616       C
ATOM   1541  CZ  TYR A 194    -104.319  62.633 -35.015  1.00 35.64           C
ANISOU 1541  CZ  TYR A 194     4408   2583   6549     67   -338   -734       C
ATOM   1542  OH  TYR A 194    -104.821  63.563 -35.897  1.00 35.89           O
ANISOU 1542  OH  TYR A 194     4468   2565   6606     77   -400   -811       O
ATOM   1543  N   PHE A 195    -102.304  56.812 -31.576  1.00 30.85           N
ANISOU 1543  N   PHE A 195     3636   2214   5869     50    -55   -574       N
ATOM   1544  CA  PHE A 195    -101.546  55.768 -30.906  1.00 28.36           C
ANISOU 1544  CA  PHE A 195     3297   1943   5537     32    -16   -545       C
ATOM   1545  C   PHE A 195    -100.112  55.765 -31.404  1.00 32.07           C
ANISOU 1545  C   PHE A 195     3827   2449   5910     -4     24   -510       C
ATOM   1546  O   PHE A 195     -99.861  55.887 -32.607  1.00 29.84           O
ANISOU 1546  O   PHE A 195     3595   2177   5567    -17     64   -536       O
ATOM   1547  CB  PHE A 195    -102.176  54.387 -31.121  1.00 28.12           C
ANISOU 1547  CB  PHE A 195     3205   1930   5549     43     45   -620       C
ATOM   1548  CG  PHE A 195    -103.495  54.212 -30.430  1.00 29.70           C
ANISOU 1548  CG  PHE A 195     3336   2094   5855     90     -7   -654       C
ATOM   1549  CD1 PHE A 195    -103.584  54.313 -29.052  1.00 26.74           C
ANISOU 1549  CD1 PHE A 195     2931   1707   5522    104    -78   -592       C
ATOM   1550  CD2 PHE A 195    -104.644  53.942 -31.155  1.00 27.84           C
ANISOU 1550  CD2 PHE A 195     3064   1842   5672    127     11   -750       C
ATOM   1551  CE1 PHE A 195    -104.797  54.153 -28.409  1.00 27.27           C
ANISOU 1551  CE1 PHE A 195     2941   1736   5685    152   -137   -613       C
ATOM   1552  CE2 PHE A 195    -105.860  53.780 -30.518  1.00 28.37           C
ANISOU 1552  CE2 PHE A 195     3067   1865   5847    181    -50   -784       C
ATOM   1553  CZ  PHE A 195    -105.937  53.885 -29.144  1.00 32.02           C
ANISOU 1553  CZ  PHE A 195     3507   2306   6353    192   -128   -709       C
ATOM   1554  N   THR A 196     -99.175  55.637 -30.470  1.00 33.67           N
ANISOU 1554  N   THR A 196     4027   2670   6098    -15      5   -452       N
ATOM   1555  CA  THR A 196     -97.782  55.461 -30.838  1.00 31.20           C
ANISOU 1555  CA  THR A 196     3766   2378   5711    -42     33   -423       C
ATOM   1556  C   THR A 196     -97.569  54.066 -31.418  1.00 30.26           C
ANISOU 1556  C   THR A 196     3642   2268   5588    -71    113   -456       C
ATOM   1557  O   THR A 196     -98.314  53.123 -31.135  1.00 29.33           O
ANISOU 1557  O   THR A 196     3459   2153   5530    -70    140   -498       O
ATOM   1558  CB  THR A 196     -96.871  55.685 -29.630  1.00 31.28           C
ANISOU 1558  CB  THR A 196     3765   2406   5713    -34    -14   -371       C
ATOM   1559  OG1 THR A 196     -97.345  54.914 -28.520  1.00 31.28           O
ANISOU 1559  OG1 THR A 196     3699   2415   5772    -21    -27   -382       O
ATOM   1560  CG2 THR A 196     -96.852  57.155 -29.247  1.00 24.15           C
ANISOU 1560  CG2 THR A 196     2870   1510   4795    -20    -77   -326       C
ATOM   1561  N   GLN A 197     -96.534  53.942 -32.247  1.00 30.07           N
ANISOU 1561  N   GLN A 197     3685   2248   5492   -100    147   -432       N
ATOM   1562  CA  GLN A 197     -96.296  52.715 -32.995  1.00 29.59           C
ANISOU 1562  CA  GLN A 197     3631   2196   5416   -144    230   -444       C
ATOM   1563  C   GLN A 197     -95.410  51.717 -32.261  1.00 29.26           C
ANISOU 1563  C   GLN A 197     3571   2138   5411   -173    233   -420       C
ATOM   1564  O   GLN A 197     -95.353  50.553 -32.671  1.00 33.58           O
ANISOU 1564  O   GLN A 197     4100   2686   5974   -221    301   -429       O
ATOM   1565  CB  GLN A 197     -95.680  53.048 -34.356  1.00 32.58           C
ANISOU 1565  CB  GLN A 197     4101   2585   5694   -165    263   -419       C
ATOM   1566  CG  GLN A 197     -96.573  53.912 -35.228  1.00 32.13           C
ANISOU 1566  CG  GLN A 197     4062   2548   5598   -137    263   -464       C
ATOM   1567  CD  GLN A 197     -97.895  53.243 -35.547  1.00 38.64           C
ANISOU 1567  CD  GLN A 197     4820   3399   6463   -132    323   -543       C
ATOM   1568  OE1 GLN A 197     -97.939  52.065 -35.899  1.00 44.46           O
ANISOU 1568  OE1 GLN A 197     5528   4165   7199   -169    406   -556       O
ATOM   1569  NE2 GLN A 197     -98.984  53.992 -35.416  1.00 40.66           N
ANISOU 1569  NE2 GLN A 197     5044   3642   6764    -86    278   -596       N
ATOM   1570  N   SER A 198     -94.717  52.142 -31.202  1.00 26.63           N
ANISOU 1570  N   SER A 198     3237   1791   5091   -147    161   -394       N
ATOM   1571  CA  SER A 198     -93.933  51.245 -30.349  1.00 28.17           C
ANISOU 1571  CA  SER A 198     3407   1966   5329   -162    145   -392       C
ATOM   1572  C   SER A 198     -92.846  50.512 -31.135  1.00 34.41           C
ANISOU 1572  C   SER A 198     4259   2719   6098   -214    184   -359       C
ATOM   1573  O   SER A 198     -92.567  49.337 -30.892  1.00 38.20           O
ANISOU 1573  O   SER A 198     4707   3172   6634   -256    207   -369       O
ATOM   1574  CB  SER A 198     -94.837  50.245 -29.625  1.00 27.95           C
ANISOU 1574  CB  SER A 198     3283   1951   5387   -166    158   -442       C
ATOM   1575  OG  SER A 198     -95.857  50.907 -28.899  1.00 30.69           O
ANISOU 1575  OG  SER A 198     3582   2323   5756   -115    113   -459       O
ATOM   1576  N   ARG A 199     -92.223  51.207 -32.080  1.00 35.40           N
ANISOU 1576  N   ARG A 199     4471   2835   6143   -216    184   -316       N
ATOM   1577  CA  ARG A 199     -91.125  50.634 -32.843  1.00 37.23           C
ANISOU 1577  CA  ARG A 199     4777   3021   6346   -262    207   -265       C
ATOM   1578  C   ARG A 199     -89.787  50.990 -32.197  1.00 42.38           C
ANISOU 1578  C   ARG A 199     5469   3627   7004   -228    122   -243       C
ATOM   1579  O   ARG A 199     -89.714  51.766 -31.241  1.00 44.07           O
ANISOU 1579  O   ARG A 199     5651   3865   7228   -169     57   -268       O
ATOM   1580  CB  ARG A 199     -91.179  51.113 -34.295  1.00 33.58           C
ANISOU 1580  CB  ARG A 199     4395   2581   5785   -277    249   -229       C
ATOM   1581  CG  ARG A 199     -92.366  50.562 -35.072  1.00 33.14           C
ANISOU 1581  CG  ARG A 199     4301   2576   5715   -312    344   -261       C
ATOM   1582  CD  ARG A 199     -92.531  51.236 -36.425  1.00 34.63           C
ANISOU 1582  CD  ARG A 199     4565   2805   5790   -308    374   -247       C
ATOM   1583  NE  ARG A 199     -93.013  52.609 -36.301  1.00 33.60           N
ANISOU 1583  NE  ARG A 199     4435   2694   5639   -242    309   -282       N
ATOM   1584  CZ  ARG A 199     -93.481  53.331 -37.314  1.00 32.25           C
ANISOU 1584  CZ  ARG A 199     4305   2561   5386   -225    319   -303       C
ATOM   1585  NH1 ARG A 199     -93.534  52.811 -38.533  1.00 30.15           N
ANISOU 1585  NH1 ARG A 199     4085   2335   5034   -261    396   -292       N
ATOM   1586  NH2 ARG A 199     -93.897  54.574 -37.109  1.00 32.77           N
ANISOU 1586  NH2 ARG A 199     4364   2630   5456   -173    250   -336       N
ATOM   1587  N   ASN A 200     -88.714  50.399 -32.722  1.00 42.80           N
ANISOU 1587  N   ASN A 200     5591   3617   7055   -266    122   -195       N
ATOM   1588  CA  ASN A 200     -87.369  50.668 -32.236  1.00 43.76           C
ANISOU 1588  CA  ASN A 200     5756   3681   7189   -227     36   -182       C
ATOM   1589  C   ASN A 200     -86.441  50.947 -33.411  1.00 41.15           C
ANISOU 1589  C   ASN A 200     5539   3304   6790   -238     24   -107       C
ATOM   1590  O   ASN A 200     -86.758  50.654 -34.566  1.00 39.24           O
ANISOU 1590  O   ASN A 200     5346   3073   6492   -292     92    -58       O
ATOM   1591  CB  ASN A 200     -86.822  49.508 -31.390  1.00 47.55           C
ANISOU 1591  CB  ASN A 200     6200   4096   7770   -252     14   -208       C
ATOM   1592  CG  ASN A 200     -86.742  48.210 -32.162  1.00 54.08           C
ANISOU 1592  CG  ASN A 200     7051   4864   8634   -352     82   -161       C
ATOM   1593  OD1 ASN A 200     -85.834  48.010 -32.969  1.00 58.52           O
ANISOU 1593  OD1 ASN A 200     7704   5356   9174   -386     76    -89       O
ATOM   1594  ND2 ASN A 200     -87.688  47.313 -31.911  1.00 55.64           N
ANISOU 1594  ND2 ASN A 200     7162   5092   8888   -402    146   -197       N
ATOM   1595  N   LEU A 201     -85.274  51.512 -33.090  1.00 45.22           N
ANISOU 1595  N   LEU A 201     6097   3777   7307   -180    -67   -103       N
ATOM   1596  CA  LEU A 201     -84.353  51.992 -34.117  1.00 46.88           C
ANISOU 1596  CA  LEU A 201     6415   3947   7450   -167   -105    -36       C
ATOM   1597  C   LEU A 201     -83.806  50.850 -34.965  1.00 51.74           C
ANISOU 1597  C   LEU A 201     7110   4474   8075   -248    -71     46       C
ATOM   1598  O   LEU A 201     -83.899  50.876 -36.198  1.00 58.75           O
ANISOU 1598  O   LEU A 201     8073   5375   8875   -287    -27    118       O
ATOM   1599  CB  LEU A 201     -83.204  52.764 -33.467  1.00 44.77           C
ANISOU 1599  CB  LEU A 201     6158   3651   7200    -77   -217    -63       C
ATOM   1600  CG  LEU A 201     -83.503  54.191 -33.018  1.00 42.58           C
ANISOU 1600  CG  LEU A 201     5828   3468   6881     -1   -255   -111       C
ATOM   1601  CD1 LEU A 201     -82.238  54.855 -32.510  1.00 41.70           C
ANISOU 1601  CD1 LEU A 201     5725   3335   6785     86   -359   -138       C
ATOM   1602  CD2 LEU A 201     -84.094  54.973 -34.171  1.00 44.41           C
ANISOU 1602  CD2 LEU A 201     6102   3752   7019    -12   -226    -74       C
ATOM   1603  N   GLN A 202     -83.211  49.847 -34.316  1.00 48.38           N
ANISOU 1603  N   GLN A 202     6669   3959   7752   -277    -94     39       N
ATOM   1604  CA  GLN A 202     -82.551  48.770 -35.048  1.00 59.20           C
ANISOU 1604  CA  GLN A 202     8117   5226   9151   -363    -74    130       C
ATOM   1605  C   GLN A 202     -83.515  48.056 -35.986  1.00 59.73           C
ANISOU 1605  C   GLN A 202     8178   5347   9168   -467     57    183       C
ATOM   1606  O   GLN A 202     -83.156  47.718 -37.119  1.00 62.36           O
ANISOU 1606  O   GLN A 202     8603   5650   9439   -529     93    288       O
ATOM   1607  CB  GLN A 202     -81.935  47.777 -34.064  1.00 72.93           C
ANISOU 1607  CB  GLN A 202     9818   6861  11032   -384   -122     91       C
ATOM   1608  CG  GLN A 202     -80.717  48.303 -33.327  1.00 84.29           C
ANISOU 1608  CG  GLN A 202    11282   8225  12519   -284   -257     45       C
ATOM   1609  CD  GLN A 202     -79.456  48.231 -34.166  1.00 92.77           C
ANISOU 1609  CD  GLN A 202    12486   9172  13592   -289   -325    142       C
ATOM   1610  OE1 GLN A 202     -79.427  47.577 -35.209  1.00 96.49           O
ANISOU 1610  OE1 GLN A 202    13031   9595  14037   -385   -269    255       O
ATOM   1611  NE2 GLN A 202     -78.404  48.902 -33.712  1.00 93.19           N
ANISOU 1611  NE2 GLN A 202    12567   9173  13670   -182   -447     98       N
ATOM   1612  N   GLU A 203     -84.746  47.828 -35.535  1.00 57.04           N
ANISOU 1612  N   GLU A 203     7730   5094   8849   -482    129    112       N
ATOM   1613  CA  GLU A 203     -85.720  47.032 -36.268  1.00 57.91           C
ANISOU 1613  CA  GLU A 203     7806   5265   8932   -573    258    136       C
ATOM   1614  C   GLU A 203     -86.889  47.872 -36.772  1.00 49.15           C
ANISOU 1614  C   GLU A 203     6671   4281   7721   -534    312     95       C
ATOM   1615  O   GLU A 203     -88.022  47.390 -36.838  1.00 51.88           O
ANISOU 1615  O   GLU A 203     6936   4700   8077   -569    401     52       O
ATOM   1616  CB  GLU A 203     -86.225  45.890 -35.388  1.00 71.03           C
ANISOU 1616  CB  GLU A 203     9353   6915  10722   -626    294     77       C
ATOM   1617  CG  GLU A 203     -85.120  45.018 -34.811  1.00 84.82           C
ANISOU 1617  CG  GLU A 203    11114   8527  12587   -666    230     98       C
ATOM   1618  CD  GLU A 203     -85.423  44.543 -33.402  1.00 93.09           C
ANISOU 1618  CD  GLU A 203    12046   9568  13758   -643    190    -12       C
ATOM   1619  OE1 GLU A 203     -85.181  45.313 -32.448  1.00 95.24           O
ANISOU 1619  OE1 GLU A 203    12302   9847  14039   -542     99    -82       O
ATOM   1620  OE2 GLU A 203     -85.911  43.404 -33.248  1.00 95.63           O
ANISOU 1620  OE2 GLU A 203    12287   9887  14162   -726    250    -28       O
ATOM   1621  N   PHE A 204     -86.632  49.127 -37.130  1.00 42.47           N
ANISOU 1621  N   PHE A 204     5889   3459   6787   -460    253    101       N
ATOM   1622  CA  PHE A 204     -87.702  50.000 -37.594  1.00 39.96           C
ANISOU 1622  CA  PHE A 204     5551   3246   6387   -421    286     54       C
ATOM   1623  C   PHE A 204     -88.193  49.552 -38.964  1.00 39.37           C
ANISOU 1623  C   PHE A 204     5517   3233   6208   -485    392     99       C
ATOM   1624  O   PHE A 204     -87.394  49.306 -39.873  1.00 45.62           O
ANISOU 1624  O   PHE A 204     6410   3996   6926   -526    400    196       O
ATOM   1625  CB  PHE A 204     -87.225  51.449 -37.654  1.00 44.39           C
ANISOU 1625  CB  PHE A 204     6165   3814   6888   -334    189     49       C
ATOM   1626  CG  PHE A 204     -88.339  52.446 -37.821  1.00 47.77           C
ANISOU 1626  CG  PHE A 204     6552   4329   7268   -289    198    -18       C
ATOM   1627  CD1 PHE A 204     -88.850  52.736 -39.077  1.00 48.02           C
ANISOU 1627  CD1 PHE A 204     6633   4423   7187   -300    246     -9       C
ATOM   1628  CD2 PHE A 204     -88.874  53.093 -36.720  1.00 46.13           C
ANISOU 1628  CD2 PHE A 204     6260   4141   7128   -237    154    -88       C
ATOM   1629  CE1 PHE A 204     -89.875  53.650 -39.229  1.00 45.42           C
ANISOU 1629  CE1 PHE A 204     6268   4159   6830   -257    242    -82       C
ATOM   1630  CE2 PHE A 204     -89.898  54.009 -36.868  1.00 44.18           C
ANISOU 1630  CE2 PHE A 204     5978   3953   6854   -203    153   -141       C
ATOM   1631  CZ  PHE A 204     -90.398  54.287 -38.123  1.00 44.75           C
ANISOU 1631  CZ  PHE A 204     6099   4073   6830   -212    193   -144       C
ATOM   1632  N   LYS A 205     -89.513  49.448 -39.110  1.00 36.34           N
ANISOU 1632  N   LYS A 205     5056   2938   5815   -490    471     29       N
ATOM   1633  CA  LYS A 205     -90.129  49.054 -40.365  1.00 45.22           C
ANISOU 1633  CA  LYS A 205     6200   4148   6834   -538    582     45       C
ATOM   1634  C   LYS A 205     -91.224  50.063 -40.708  1.00 39.79           C
ANISOU 1634  C   LYS A 205     5487   3546   6084   -468    581    -47       C
ATOM   1635  O   LYS A 205     -92.041  50.405 -39.837  1.00 36.39           O
ANISOU 1635  O   LYS A 205     4967   3120   5740   -421    553   -135       O
ATOM   1636  CB  LYS A 205     -90.712  47.636 -40.281  1.00 54.07           C
ANISOU 1636  CB  LYS A 205     7229   5295   8020   -624    696     35       C
ATOM   1637  CG  LYS A 205     -89.821  46.637 -39.558  1.00 59.99           C
ANISOU 1637  CG  LYS A 205     7966   5941   8886   -689    676     92       C
ATOM   1638  CD  LYS A 205     -89.765  45.306 -40.286  1.00 66.84           C
ANISOU 1638  CD  LYS A 205     8825   6827   9742   -812    797    165       C
ATOM   1639  CE  LYS A 205     -89.023  45.438 -41.605  1.00 70.07           C
ANISOU 1639  CE  LYS A 205     9373   7247  10003   -853    823    288       C
ATOM   1640  NZ  LYS A 205     -87.643  45.964 -41.406  1.00 67.96           N
ANISOU 1640  NZ  LYS A 205     9222   6856   9744   -821    694    367       N
ATOM   1641  N   PRO A 206     -91.270  50.557 -41.941  1.00 39.02           N
ANISOU 1641  N   PRO A 206     5470   3514   5843   -459    602    -30       N
ATOM   1642  CA  PRO A 206     -92.305  51.532 -42.300  1.00 39.71           C
ANISOU 1642  CA  PRO A 206     5535   3671   5880   -392    590   -131       C
ATOM   1643  C   PRO A 206     -93.675  50.881 -42.389  1.00 44.41           C
ANISOU 1643  C   PRO A 206     6026   4342   6504   -404    692   -224       C
ATOM   1644  O   PRO A 206     -93.817  49.727 -42.802  1.00 46.49           O
ANISOU 1644  O   PRO A 206     6262   4653   6750   -474    804   -200       O
ATOM   1645  CB  PRO A 206     -91.843  52.049 -43.667  1.00 33.29           C
ANISOU 1645  CB  PRO A 206     4844   2911   4895   -385    586    -83       C
ATOM   1646  CG  PRO A 206     -91.058  50.916 -44.238  1.00 43.44           C
ANISOU 1646  CG  PRO A 206     6187   4194   6124   -474    662     36       C
ATOM   1647  CD  PRO A 206     -90.375  50.253 -43.071  1.00 40.42           C
ANISOU 1647  CD  PRO A 206     5765   3699   5892   -509    631     83       C
ATOM   1648  N   ARG A 207     -94.697  51.642 -41.993  1.00 42.22           N
ANISOU 1648  N   ARG A 207     5687   4076   6280   -335    650   -332       N
ATOM   1649  CA  ARG A 207     -96.070  51.150 -41.978  1.00 38.17           C
ANISOU 1649  CA  ARG A 207     5068   3620   5814   -324    723   -438       C
ATOM   1650  C   ARG A 207     -96.992  51.980 -42.867  1.00 37.71           C
ANISOU 1650  C   ARG A 207     5023   3630   5675   -263    720   -539       C
ATOM   1651  O   ARG A 207     -98.216  51.902 -42.727  1.00 38.86           O
ANISOU 1651  O   ARG A 207     5081   3803   5883   -224    742   -650       O
ATOM   1652  CB  ARG A 207     -96.601  51.104 -40.544  1.00 37.69           C
ANISOU 1652  CB  ARG A 207     4905   3496   5920   -296    670   -483       C
ATOM   1653  CG  ARG A 207     -95.886  50.083 -39.672  1.00 42.20           C
ANISOU 1653  CG  ARG A 207     5442   4016   6578   -355    683   -415       C
ATOM   1654  CD  ARG A 207     -96.349  50.137 -38.225  1.00 43.63           C
ANISOU 1654  CD  ARG A 207     5533   4143   6903   -318    616   -457       C
ATOM   1655  NE  ARG A 207     -95.689  49.117 -37.414  1.00 45.20           N
ANISOU 1655  NE  ARG A 207     5694   4298   7182   -370    624   -411       N
ATOM   1656  CZ  ARG A 207     -95.790  49.027 -36.092  1.00 45.15           C
ANISOU 1656  CZ  ARG A 207     5623   4247   7286   -346    560   -431       C
ATOM   1657  NH1 ARG A 207     -96.523  49.901 -35.418  1.00 46.41           N
ANISOU 1657  NH1 ARG A 207     5748   4398   7486   -276    489   -479       N
ATOM   1658  NH2 ARG A 207     -95.152  48.063 -35.442  1.00 45.08           N
ANISOU 1658  NH2 ARG A 207     5583   4200   7345   -394    563   -401       N
ATOM   1659  N   SER A 208     -96.429  52.769 -43.779  1.00 33.21           N
ANISOU 1659  N   SER A 208     4561   3084   4973   -247    682   -510       N
ATOM   1660  CA  SER A 208     -97.221  53.522 -44.741  1.00 33.91           C
ANISOU 1660  CA  SER A 208     4671   3243   4970   -190    675   -613       C
ATOM   1661  C   SER A 208     -96.326  53.895 -45.911  1.00 34.76           C
ANISOU 1661  C   SER A 208     4908   3402   4898   -200    668   -547       C
ATOM   1662  O   SER A 208     -95.100  53.954 -45.782  1.00 46.43           O
ANISOU 1662  O   SER A 208     6460   4828   6352   -230    624   -426       O
ATOM   1663  CB  SER A 208     -97.838  54.778 -44.117  1.00 35.61           C
ANISOU 1663  CB  SER A 208     4856   3388   5284   -119    553   -693       C
ATOM   1664  OG  SER A 208     -96.863  55.791 -43.934  1.00 39.04           O
ANISOU 1664  OG  SER A 208     5366   3764   5704   -108    444   -624       O
ATOM   1665  N   GLN A 209     -96.959  54.149 -47.060  1.00 35.96           N
ANISOU 1665  N   GLN A 209     5085   3657   4920   -167    703   -634       N
ATOM   1666  CA  GLN A 209     -96.206  54.567 -48.239  1.00 36.95           C
ANISOU 1666  CA  GLN A 209     5337   3847   4855   -166    687   -581       C
ATOM   1667  C   GLN A 209     -95.464  55.873 -47.990  1.00 43.93           C
ANISOU 1667  C   GLN A 209     6288   4647   5757   -124    530   -550       C
ATOM   1668  O   GLN A 209     -94.373  56.082 -48.533  1.00 45.29           O
ANISOU 1668  O   GLN A 209     6566   4824   5818   -136    491   -449       O
ATOM   1669  CB  GLN A 209     -97.140  54.705 -49.442  1.00 42.04           C
ANISOU 1669  CB  GLN A 209     5988   4627   5358   -122    741   -709       C
ATOM   1670  CG  GLN A 209     -96.434  55.052 -50.745  1.00 44.71           C
ANISOU 1670  CG  GLN A 209     6459   5058   5473   -118    731   -659       C
ATOM   1671  CD  GLN A 209     -95.575  53.916 -51.268  1.00 48.64           C
ANISOU 1671  CD  GLN A 209     7017   5617   5846   -207    844   -501       C
ATOM   1672  OE1 GLN A 209     -95.981  52.754 -51.246  1.00 50.37           O
ANISOU 1672  OE1 GLN A 209     7166   5895   6076   -264    983   -493       O
ATOM   1673  NE2 GLN A 209     -94.378  54.247 -51.741  1.00 49.33           N
ANISOU 1673  NE2 GLN A 209     7234   5688   5823   -221    780   -372       N
ATOM   1674  N   MET A 210     -96.035  56.758 -47.170  1.00 34.91           N
ANISOU 1674  N   MET A 210     5081   3427   4755    -76    437   -631       N
ATOM   1675  CA  MET A 210     -95.334  57.984 -46.806  1.00 42.83           C
ANISOU 1675  CA  MET A 210     6123   4354   5794    -45    296   -600       C
ATOM   1676  C   MET A 210     -94.060  57.674 -46.031  1.00 46.89           C
ANISOU 1676  C   MET A 210     6662   4795   6359    -83    271   -460       C
ATOM   1677  O   MET A 210     -93.005  58.264 -46.292  1.00 46.50           O
ANISOU 1677  O   MET A 210     6690   4726   6250    -71    191   -392       O
ATOM   1678  CB  MET A 210     -96.256  58.891 -45.992  1.00 39.74           C
ANISOU 1678  CB  MET A 210     5647   3895   5557     -4    215   -700       C
ATOM   1679  CG  MET A 210     -95.628  60.214 -45.591  1.00 43.58           C
ANISOU 1679  CG  MET A 210     6152   4316   6090     20     77   -675       C
ATOM   1680  SD  MET A 210     -96.692  61.188 -44.509  1.00 48.54           S
ANISOU 1680  SD  MET A 210     6675   4856   6911     45     -7   -758       S
ATOM   1681  CE  MET A 210     -98.099  61.471 -45.580  1.00 47.48           C
ANISOU 1681  CE  MET A 210     6536   4769   6735     91     -2   -927       C
ATOM   1682  N   GLU A 211     -94.136  56.744 -45.075  1.00 51.26           N
ANISOU 1682  N   GLU A 211     7145   5306   7025   -123    331   -426       N
ATOM   1683  CA  GLU A 211     -92.940  56.337 -44.346  1.00 32.03           C
ANISOU 1683  CA  GLU A 211     4730   2798   4640   -157    309   -309       C
ATOM   1684  C   GLU A 211     -91.954  55.625 -45.261  1.00 41.53           C
ANISOU 1684  C   GLU A 211     6038   4030   5712   -202    355   -200       C
ATOM   1685  O   GLU A 211     -90.739  55.811 -45.136  1.00 43.93           O
ANISOU 1685  O   GLU A 211     6408   4276   6007   -202    286   -107       O
ATOM   1686  CB  GLU A 211     -93.318  55.441 -43.168  1.00 31.30           C
ANISOU 1686  CB  GLU A 211     4537   2662   4692   -189    361   -311       C
ATOM   1687  CG  GLU A 211     -94.134  56.132 -42.094  1.00 39.02           C
ANISOU 1687  CG  GLU A 211     5423   3599   5805   -148    302   -388       C
ATOM   1688  CD  GLU A 211     -94.225  55.317 -40.821  1.00 41.42           C
ANISOU 1688  CD  GLU A 211     5643   3856   6241   -173    326   -371       C
ATOM   1689  OE1 GLU A 211     -94.024  54.087 -40.885  1.00 44.27           O
ANISOU 1689  OE1 GLU A 211     5994   4226   6600   -225    410   -334       O
ATOM   1690  OE2 GLU A 211     -94.488  55.909 -39.753  1.00 43.91           O
ANISOU 1690  OE2 GLU A 211     5899   4127   6658   -143    260   -393       O
ATOM   1691  N   ILE A 212     -92.459  54.800 -46.182  1.00 39.25           N
ANISOU 1691  N   ILE A 212     5762   3831   5320   -239    471   -207       N
ATOM   1692  CA  ILE A 212     -91.587  54.151 -47.155  1.00 39.18           C
ANISOU 1692  CA  ILE A 212     5859   3859   5167   -291    521    -88       C
ATOM   1693  C   ILE A 212     -90.879  55.195 -48.006  1.00 40.00           C
ANISOU 1693  C   ILE A 212     6080   3981   5138   -241    418    -58       C
ATOM   1694  O   ILE A 212     -89.667  55.112 -48.239  1.00 42.50           O
ANISOU 1694  O   ILE A 212     6492   4251   5405   -257    370     65       O
ATOM   1695  CB  ILE A 212     -92.393  53.166 -48.022  1.00 47.34           C
ANISOU 1695  CB  ILE A 212     6871   5016   6099   -340    675   -112       C
ATOM   1696  CG1 ILE A 212     -92.957  52.033 -47.163  1.00 48.48           C
ANISOU 1696  CG1 ILE A 212     6894   5140   6386   -395    772   -131       C
ATOM   1697  CG2 ILE A 212     -91.528  52.604 -49.141  1.00 48.78           C
ANISOU 1697  CG2 ILE A 212     7175   5254   6107   -397    727     24       C
ATOM   1698  CD1 ILE A 212     -93.821  51.056 -47.931  1.00 48.94           C
ANISOU 1698  CD1 ILE A 212     6902   5330   6363   -440    930   -171       C
ATOM   1699  N   ASP A 213     -91.620  56.202 -48.474  1.00 41.63           N
ANISOU 1699  N   ASP A 213     6279   4246   5293   -175    371   -176       N
ATOM   1700  CA  ASP A 213     -91.001  57.270 -49.251  1.00 41.79           C
ANISOU 1700  CA  ASP A 213     6398   4286   5196   -122    258   -165       C
ATOM   1701  C   ASP A 213     -90.077  58.124 -48.395  1.00 40.32           C
ANISOU 1701  C   ASP A 213     6211   3988   5120    -86    120   -128       C
ATOM   1702  O   ASP A 213     -89.068  58.631 -48.896  1.00 40.85           O
ANISOU 1702  O   ASP A 213     6371   4043   5105    -59     29    -60       O
ATOM   1703  CB  ASP A 213     -92.077  58.137 -49.903  1.00 44.00           C
ANISOU 1703  CB  ASP A 213     6657   4647   5414    -63    233   -318       C
ATOM   1704  CG  ASP A 213     -92.863  57.391 -50.963  1.00 49.82           C
ANISOU 1704  CG  ASP A 213     7408   5521   6000    -81    363   -365       C
ATOM   1705  OD1 ASP A 213     -92.515  56.227 -51.252  1.00 50.74           O
ANISOU 1705  OD1 ASP A 213     7554   5676   6048   -149    476   -262       O
ATOM   1706  OD2 ASP A 213     -93.828  57.969 -51.507  1.00 52.08           O
ANISOU 1706  OD2 ASP A 213     7672   5877   6238    -29    352   -510       O
ATOM   1707  N   PHE A 214     -90.396  58.293 -47.109  1.00 38.77           N
ANISOU 1707  N   PHE A 214     5909   3717   5104    -82    100   -171       N
ATOM   1708  CA  PHE A 214     -89.532  59.080 -46.236  1.00 38.85           C
ANISOU 1708  CA  PHE A 214     5905   3642   5215    -48    -18   -142       C
ATOM   1709  C   PHE A 214     -88.150  58.452 -46.118  1.00 41.96           C
ANISOU 1709  C   PHE A 214     6370   3974   5601    -70    -36     -9       C
ATOM   1710  O   PHE A 214     -87.134  59.154 -46.158  1.00 47.85           O
ANISOU 1710  O   PHE A 214     7165   4682   6334    -26   -147     32       O
ATOM   1711  CB  PHE A 214     -90.170  59.229 -44.855  1.00 35.81           C
ANISOU 1711  CB  PHE A 214     5394   3205   5007    -47    -18   -201       C
ATOM   1712  CG  PHE A 214     -89.289  59.922 -43.854  1.00 34.14           C
ANISOU 1712  CG  PHE A 214     5152   2925   4895    -17   -119   -172       C
ATOM   1713  CD1 PHE A 214     -89.242  61.305 -43.793  1.00 32.20           C
ANISOU 1713  CD1 PHE A 214     4884   2683   4667     32   -225   -221       C
ATOM   1714  CD2 PHE A 214     -88.505  59.191 -42.976  1.00 34.76           C
ANISOU 1714  CD2 PHE A 214     5217   2939   5050    -37   -108   -103       C
ATOM   1715  CE1 PHE A 214     -88.431  61.943 -42.875  1.00 34.81           C
ANISOU 1715  CE1 PHE A 214     5173   2971   5083     60   -308   -199       C
ATOM   1716  CE2 PHE A 214     -87.693  59.824 -42.057  1.00 33.95           C
ANISOU 1716  CE2 PHE A 214     5081   2790   5030      0   -196    -91       C
ATOM   1717  CZ  PHE A 214     -87.655  61.202 -42.006  1.00 34.57           C
ANISOU 1717  CZ  PHE A 214     5131   2888   5117     49   -291   -137       C
ATOM   1718  N   LEU A 215     -88.094  57.129 -45.972  1.00 41.98           N
ANISOU 1718  N   LEU A 215     6373   3957   5619   -136     67     56       N
ATOM   1719  CA  LEU A 215     -86.814  56.449 -45.827  1.00 43.63           C
ANISOU 1719  CA  LEU A 215     6650   4085   5842   -165     47    182       C
ATOM   1720  C   LEU A 215     -86.084  56.311 -47.156  1.00 46.01           C
ANISOU 1720  C   LEU A 215     7093   4417   5972   -175     34    284       C
ATOM   1721  O   LEU A 215     -84.850  56.365 -47.186  1.00 47.56           O
ANISOU 1721  O   LEU A 215     7368   4536   6167   -159    -52    378       O
ATOM   1722  CB  LEU A 215     -87.030  55.073 -45.196  1.00 44.22           C
ANISOU 1722  CB  LEU A 215     6670   4124   6009   -243    155    214       C
ATOM   1723  CG  LEU A 215     -87.672  55.099 -43.807  1.00 44.59           C
ANISOU 1723  CG  LEU A 215     6583   4138   6222   -232    159    126       C
ATOM   1724  CD1 LEU A 215     -88.093  53.701 -43.378  1.00 44.90           C
ANISOU 1724  CD1 LEU A 215     6562   4166   6334   -310    273    140       C
ATOM   1725  CD2 LEU A 215     -86.714  55.710 -42.796  1.00 40.74           C
ANISOU 1725  CD2 LEU A 215     6080   3564   5835   -180     42    134       C
ATOM   1726  N   GLU A 216     -86.819  56.142 -48.256  1.00 49.28           N
ANISOU 1726  N   GLU A 216     7542   4944   6237   -196    114    266       N
ATOM   1727  CA  GLU A 216     -86.177  55.955 -49.552  1.00 56.58           C
ANISOU 1727  CA  GLU A 216     8607   5916   6975   -210    111    374       C
ATOM   1728  C   GLU A 216     -85.719  57.280 -50.149  1.00 57.54           C
ANISOU 1728  C   GLU A 216     8798   6060   7005   -120    -33    349       C
ATOM   1729  O   GLU A 216     -84.574  57.405 -50.595  1.00 60.96           O
ANISOU 1729  O   GLU A 216     9341   6450   7373   -101   -121    458       O
ATOM   1730  CB  GLU A 216     -87.129  55.241 -50.513  1.00 66.00           C
ANISOU 1730  CB  GLU A 216     9808   7246   8025   -265    260    359       C
ATOM   1731  CG  GLU A 216     -87.390  53.782 -50.176  1.00 77.08           C
ANISOU 1731  CG  GLU A 216    11158   8638   9489   -368    407    416       C
ATOM   1732  CD  GLU A 216     -88.306  53.107 -51.181  1.00 86.35           C
ANISOU 1732  CD  GLU A 216    12328   9970  10510   -417    561    396       C
ATOM   1733  OE1 GLU A 216     -89.041  53.822 -51.897  1.00 87.88           O
ANISOU 1733  OE1 GLU A 216    12527  10279  10586   -358    556    288       O
ATOM   1734  OE2 GLU A 216     -88.289  51.859 -51.259  1.00 88.42           O
ANISOU 1734  OE2 GLU A 216    12577  10246  10774   -516    686    482       O
ATOM   1735  N   LEU A 217     -86.597  58.278 -50.164  1.00 55.03           N
ANISOU 1735  N   LEU A 217     8415   5803   6690    -64    -68    204       N
ATOM   1736  CA  LEU A 217     -86.299  59.535 -50.830  1.00 54.43           C
ANISOU 1736  CA  LEU A 217     8394   5765   6524     15   -201    163       C
ATOM   1737  C   LEU A 217     -85.390  60.408 -49.968  1.00 54.71           C
ANISOU 1737  C   LEU A 217     8398   5698   6692     72   -345    166       C
ATOM   1738  O   LEU A 217     -85.164  60.149 -48.782  1.00 55.11           O
ANISOU 1738  O   LEU A 217     8373   5661   6907     57   -338    174       O
ATOM   1739  CB  LEU A 217     -87.587  60.288 -51.157  1.00 51.38           C
ANISOU 1739  CB  LEU A 217     7944   5469   6108     48   -193     -1       C
ATOM   1740  CG  LEU A 217     -88.637  59.538 -51.976  1.00 49.23           C
ANISOU 1740  CG  LEU A 217     7679   5316   5710     10    -51    -46       C
ATOM   1741  CD1 LEU A 217     -89.883  60.392 -52.145  1.00 44.27           C
ANISOU 1741  CD1 LEU A 217     6978   4748   5094     58    -71   -229       C
ATOM   1742  CD2 LEU A 217     -88.071  59.129 -53.327  1.00 51.53           C
ANISOU 1742  CD2 LEU A 217     8114   5699   5767     -1    -30     56       C
ATOM   1743  N   ALA A 218     -84.864  61.461 -50.589  1.00 55.21           N
ANISOU 1743  N   ALA A 218     8516   5785   6677    141   -478    151       N
ATOM   1744  CA  ALA A 218     -84.074  62.455 -49.885  1.00 55.72           C
ANISOU 1744  CA  ALA A 218     8535   5779   6856    206   -619    131       C
ATOM   1745  C   ALA A 218     -84.988  63.488 -49.229  1.00 58.08           C
ANISOU 1745  C   ALA A 218     8701   6099   7270    227   -645    -15       C
ATOM   1746  O   ALA A 218     -86.201  63.517 -49.451  1.00 63.35           O
ANISOU 1746  O   ALA A 218     9326   6824   7918    204   -577   -105       O
ATOM   1747  CB  ALA A 218     -83.092  63.134 -50.838  1.00 55.15           C
ANISOU 1747  CB  ALA A 218     8571   5725   6659    273   -759    179       C
ATOM   1748  N   MET A 219     -84.384  64.354 -48.413  1.00 54.61           N
ANISOU 1748  N   MET A 219     8190   5607   6952    272   -749    -39       N
ATOM   1749  CA  MET A 219     -85.165  65.325 -47.651  1.00 51.22           C
ANISOU 1749  CA  MET A 219     7627   5187   6649    279   -773   -154       C
ATOM   1750  C   MET A 219     -85.877  66.309 -48.572  1.00 50.08           C
ANISOU 1750  C   MET A 219     7486   5115   6426    303   -833   -255       C
ATOM   1751  O   MET A 219     -87.097  66.488 -48.482  1.00 48.86           O
ANISOU 1751  O   MET A 219     7271   4985   6311    276   -783   -347       O
ATOM   1752  CB  MET A 219     -84.261  66.066 -46.667  1.00 51.25           C
ANISOU 1752  CB  MET A 219     7553   5141   6779    321   -868   -150       C
ATOM   1753  CG  MET A 219     -84.976  67.135 -45.861  1.00 54.03           C
ANISOU 1753  CG  MET A 219     7764   5507   7258    317   -895   -248       C
ATOM   1754  SD  MET A 219     -83.924  67.865 -44.594  1.00 55.54           S
ANISOU 1754  SD  MET A 219     7847   5668   7590    360   -976   -241       S
ATOM   1755  CE  MET A 219     -82.687  68.671 -45.607  1.00 57.67           C
ANISOU 1755  CE  MET A 219     8188   5957   7769    445  -1136   -230       C
ATOM   1756  N   ASP A 220     -85.127  66.961 -49.464  1.00 55.46           N
ANISOU 1756  N   ASP A 220     8241   5829   7002    360   -952   -246       N
ATOM   1757  CA  ASP A 220     -85.730  67.942 -50.362  1.00 60.38           C
ANISOU 1757  CA  ASP A 220     8868   6523   7551    389  -1028   -354       C
ATOM   1758  C   ASP A 220     -86.755  67.294 -51.282  1.00 61.85           C
ANISOU 1758  C   ASP A 220     9120   6780   7602    361   -930   -394       C
ATOM   1759  O   ASP A 220     -87.795  67.891 -51.585  1.00 62.57           O
ANISOU 1759  O   ASP A 220     9166   6909   7698    363   -942   -521       O
ATOM   1760  CB  ASP A 220     -84.644  68.641 -51.179  1.00 67.76           C
ANISOU 1760  CB  ASP A 220     9878   7484   8385    460  -1179   -328       C
ATOM   1761  CG  ASP A 220     -83.772  69.549 -50.335  1.00 72.76           C
ANISOU 1761  CG  ASP A 220    10418   8068   9159    500  -1292   -331       C
ATOM   1762  OD1 ASP A 220     -84.151  69.836 -49.180  1.00 72.50           O
ANISOU 1762  OD1 ASP A 220    10255   7998   9292    469  -1257   -369       O
ATOM   1763  OD2 ASP A 220     -82.706  69.973 -50.828  1.00 75.34           O
ANISOU 1763  OD2 ASP A 220    10799   8401   9427    566  -1416   -295       O
ATOM   1764  N   GLU A 221     -86.482  66.069 -51.735  1.00 62.34           N
ANISOU 1764  N   GLU A 221     9280   6860   7546    334   -833   -291       N
ATOM   1765  CA  GLU A 221     -87.409  65.393 -52.636  1.00 63.60           C
ANISOU 1765  CA  GLU A 221     9494   7109   7562    308   -725   -328       C
ATOM   1766  C   GLU A 221     -88.670  64.953 -51.902  1.00 55.90           C
ANISOU 1766  C   GLU A 221     8413   6117   6709    260   -604   -407       C
ATOM   1767  O   GLU A 221     -89.768  64.984 -52.470  1.00 54.26           O
ANISOU 1767  O   GLU A 221     8194   5978   6445    263   -560   -518       O
ATOM   1768  CB  GLU A 221     -86.717  64.198 -53.290  1.00 72.95           C
ANISOU 1768  CB  GLU A 221    10805   8321   8590    279   -649   -179       C
ATOM   1769  CG  GLU A 221     -87.505  63.552 -54.415  1.00 83.21           C
ANISOU 1769  CG  GLU A 221    12172   9746   9696    258   -542   -207       C
ATOM   1770  CD  GLU A 221     -86.735  62.434 -55.091  1.00 91.62           C
ANISOU 1770  CD  GLU A 221    13367  10844  10602    218   -470    -36       C
ATOM   1771  OE1 GLU A 221     -85.635  62.094 -54.606  1.00 93.54           O
ANISOU 1771  OE1 GLU A 221    13644  10988  10908    204   -505    101       O
ATOM   1772  OE2 GLU A 221     -87.226  61.898 -56.106  1.00 95.72           O
ANISOU 1772  OE2 GLU A 221    13950  11487  10930    200   -380    -38       O
ATOM   1773  N   PHE A 222     -88.534  64.547 -50.638  1.00 51.77           N
ANISOU 1773  N   PHE A 222     7810   5505   6354    224   -558   -358       N
ATOM   1774  CA  PHE A 222     -89.696  64.105 -49.873  1.00 51.18           C
ANISOU 1774  CA  PHE A 222     7635   5409   6402    183   -455   -423       C
ATOM   1775  C   PHE A 222     -90.594  65.277 -49.499  1.00 51.84           C
ANISOU 1775  C   PHE A 222     7621   5473   6602    205   -528   -558       C
ATOM   1776  O   PHE A 222     -91.823  65.182 -49.601  1.00 51.85           O
ANISOU 1776  O   PHE A 222     7579   5495   6627    198   -474   -659       O
ATOM   1777  CB  PHE A 222     -89.244  63.354 -48.621  1.00 49.51           C
ANISOU 1777  CB  PHE A 222     7372   5113   6327    143   -399   -333       C
ATOM   1778  CG  PHE A 222     -90.374  62.904 -47.742  1.00 50.72           C
ANISOU 1778  CG  PHE A 222     7419   5241   6610    107   -307   -391       C
ATOM   1779  CD1 PHE A 222     -91.065  61.738 -48.025  1.00 53.40           C
ANISOU 1779  CD1 PHE A 222     7763   5621   6904     68   -173   -394       C
ATOM   1780  CD2 PHE A 222     -90.741  63.642 -46.628  1.00 50.00           C
ANISOU 1780  CD2 PHE A 222     7221   5091   6686    112   -356   -438       C
ATOM   1781  CE1 PHE A 222     -92.106  61.319 -47.217  1.00 52.74           C
ANISOU 1781  CE1 PHE A 222     7580   5513   6946     44   -100   -452       C
ATOM   1782  CE2 PHE A 222     -91.781  63.228 -45.818  1.00 49.29           C
ANISOU 1782  CE2 PHE A 222     7041   4974   6712     84   -284   -483       C
ATOM   1783  CZ  PHE A 222     -92.464  62.065 -46.112  1.00 48.97           C
ANISOU 1783  CZ  PHE A 222     7007   4967   6631     55   -161   -494       C
ATOM   1784  N   ILE A 223     -90.000  66.388 -49.058  1.00 48.26           N
ANISOU 1784  N   ILE A 223     7128   4978   6230    231   -653   -560       N
ATOM   1785  CA  ILE A 223     -90.791  67.553 -48.671  1.00 44.26           C
ANISOU 1785  CA  ILE A 223     6525   4444   5848    237   -728   -672       C
ATOM   1786  C   ILE A 223     -91.533  68.124 -49.872  1.00 44.36           C
ANISOU 1786  C   ILE A 223     6576   4518   5759    269   -778   -797       C
ATOM   1787  O   ILE A 223     -92.662  68.614 -49.741  1.00 46.24           O
ANISOU 1787  O   ILE A 223     6748   4733   6087    262   -791   -910       O
ATOM   1788  CB  ILE A 223     -89.883  68.603 -47.999  1.00 40.82           C
ANISOU 1788  CB  ILE A 223     6032   3969   5510    253   -844   -640       C
ATOM   1789  CG1 ILE A 223     -89.276  68.029 -46.716  1.00 37.54           C
ANISOU 1789  CG1 ILE A 223     5565   3498   5200    228   -790   -541       C
ATOM   1790  CG2 ILE A 223     -90.655  69.877 -47.695  1.00 38.54           C
ANISOU 1790  CG2 ILE A 223     5642   3654   5346    246   -927   -744       C
ATOM   1791  CD1 ILE A 223     -88.331  68.971 -46.009  1.00 34.77           C
ANISOU 1791  CD1 ILE A 223     5148   3126   4937    250   -889   -514       C
ATOM   1792  N   GLU A 224     -90.930  68.055 -51.061  1.00 49.01           N
ANISOU 1792  N   GLU A 224     7278   5185   6160    305   -813   -781       N
ATOM   1793  CA  GLU A 224     -91.606  68.543 -52.258  1.00 52.88           C
ANISOU 1793  CA  GLU A 224     7812   5752   6530    343   -861   -911       C
ATOM   1794  C   GLU A 224     -92.760  67.630 -52.654  1.00 52.66           C
ANISOU 1794  C   GLU A 224     7793   5773   6441    331   -730   -980       C
ATOM   1795  O   GLU A 224     -93.830  68.109 -53.046  1.00 53.59           O
ANISOU 1795  O   GLU A 224     7880   5907   6575    352   -757  -1132       O
ATOM   1796  CB  GLU A 224     -90.610  68.672 -53.410  1.00 57.23           C
ANISOU 1796  CB  GLU A 224     8486   6384   6876    390   -935   -864       C
ATOM   1797  CG  GLU A 224     -91.246  69.040 -54.740  1.00 65.88           C
ANISOU 1797  CG  GLU A 224     9643   7582   7806    436   -979   -997       C
ATOM   1798  CD  GLU A 224     -90.266  68.973 -55.894  1.00 77.38           C
ANISOU 1798  CD  GLU A 224    11237   9134   9031    480  -1036   -929       C
ATOM   1799  OE1 GLU A 224     -89.078  68.676 -55.649  1.00 80.17           O
ANISOU 1799  OE1 GLU A 224    11637   9456   9369    476  -1052   -776       O
ATOM   1800  OE2 GLU A 224     -90.684  69.216 -57.046  1.00 81.60           O
ANISOU 1800  OE2 GLU A 224    11836   9774   9396    523  -1072  -1030       O
ATOM   1801  N   ARG A 225     -92.561  66.313 -52.554  1.00 53.21           N
ANISOU 1801  N   ARG A 225     7899   5866   6451    297   -591   -878       N
ATOM   1802  CA  ARG A 225     -93.586  65.373 -52.999  1.00 57.13           C
ANISOU 1802  CA  ARG A 225     8398   6433   6877    286   -456   -942       C
ATOM   1803  C   ARG A 225     -94.856  65.496 -52.168  1.00 54.65           C
ANISOU 1803  C   ARG A 225     7963   6047   6753    276   -430  -1052       C
ATOM   1804  O   ARG A 225     -95.967  65.470 -52.710  1.00 57.25           O
ANISOU 1804  O   ARG A 225     8275   6423   7054    303   -402  -1193       O
ATOM   1805  CB  ARG A 225     -93.046  63.944 -52.943  1.00 61.13           C
ANISOU 1805  CB  ARG A 225     8950   6968   7307    237   -314   -796       C
ATOM   1806  CG  ARG A 225     -94.096  62.877 -53.214  1.00 66.63           C
ANISOU 1806  CG  ARG A 225     9619   7737   7958    216   -158   -855       C
ATOM   1807  CD  ARG A 225     -93.456  61.526 -53.470  1.00 71.22           C
ANISOU 1807  CD  ARG A 225    10262   8373   8424    160    -26   -706       C
ATOM   1808  NE  ARG A 225     -92.502  61.590 -54.572  1.00 80.02           N
ANISOU 1808  NE  ARG A 225    11513   9569   9324    173    -64   -619       N
ATOM   1809  CZ  ARG A 225     -91.858  60.539 -55.066  1.00 87.33           C
ANISOU 1809  CZ  ARG A 225    12520  10553  10110    124     34   -476       C
ATOM   1810  NH1 ARG A 225     -92.066  59.332 -54.558  1.00 87.71           N
ANISOU 1810  NH1 ARG A 225    12518  10588  10219     54    178   -413       N
ATOM   1811  NH2 ARG A 225     -91.006  60.695 -56.070  1.00 90.91           N
ANISOU 1811  NH2 ARG A 225    13103  11074  10364    141    -18   -391       N
ATOM   1812  N   TYR A 226     -94.717  65.631 -50.852  1.00 49.89           N
ANISOU 1812  N   TYR A 226     7278   5333   6344    242   -442   -991       N
ATOM   1813  CA  TYR A 226     -95.861  65.720 -49.958  1.00 48.12           C
ANISOU 1813  CA  TYR A 226     6946   5031   6306    229   -424  -1067       C
ATOM   1814  C   TYR A 226     -96.201  67.156 -49.581  1.00 52.18           C
ANISOU 1814  C   TYR A 226     7399   5466   6961    240   -566  -1144       C
ATOM   1815  O   TYR A 226     -96.976  67.373 -48.644  1.00 54.31           O
ANISOU 1815  O   TYR A 226     7579   5648   7408    220   -571  -1171       O
ATOM   1816  CB  TYR A 226     -95.615  64.874 -48.708  1.00 45.26           C
ANISOU 1816  CB  TYR A 226     6528   4607   6060    180   -340   -952       C
ATOM   1817  CG  TYR A 226     -95.612  63.387 -48.996  1.00 43.49           C
ANISOU 1817  CG  TYR A 226     6335   4448   5739    156   -190   -900       C
ATOM   1818  CD1 TYR A 226     -96.765  62.627 -48.838  1.00 40.80           C
ANISOU 1818  CD1 TYR A 226     5934   4120   5449    152    -93   -975       C
ATOM   1819  CD2 TYR A 226     -94.463  62.747 -49.444  1.00 43.22           C
ANISOU 1819  CD2 TYR A 226     6389   4462   5570    136   -151   -777       C
ATOM   1820  CE1 TYR A 226     -96.770  61.271 -49.107  1.00 41.45           C
ANISOU 1820  CE1 TYR A 226     6029   4271   5449    122     48   -931       C
ATOM   1821  CE2 TYR A 226     -94.460  61.392 -49.717  1.00 42.60           C
ANISOU 1821  CE2 TYR A 226     6334   4441   5411     99    -12   -720       C
ATOM   1822  CZ  TYR A 226     -95.615  60.660 -49.546  1.00 43.73           C
ANISOU 1822  CZ  TYR A 226     6404   4607   5605     89     92   -800       C
ATOM   1823  OH  TYR A 226     -95.614  59.311 -49.816  1.00 52.51           O
ANISOU 1823  OH  TYR A 226     7523   5786   6644     45    235   -746       O
ATOM   1824  N   LYS A 227     -95.639  68.137 -50.294  1.00 55.84           N
ANISOU 1824  N   LYS A 227     7907   5958   7351    269   -684  -1174       N
ATOM   1825  CA  LYS A 227     -96.025  69.544 -50.166  1.00 56.81           C
ANISOU 1825  CA  LYS A 227     7972   6018   7596    276   -825  -1266       C
ATOM   1826  C   LYS A 227     -95.890  70.031 -48.724  1.00 50.47           C
ANISOU 1826  C   LYS A 227     7067   5109   6999    226   -852  -1188       C
ATOM   1827  O   LYS A 227     -96.792  70.658 -48.166  1.00 51.21           O
ANISOU 1827  O   LYS A 227     7082   5120   7254    205   -897  -1249       O
ATOM   1828  CB  LYS A 227     -97.447  69.765 -50.689  1.00 66.11           C
ANISOU 1828  CB  LYS A 227     9129   7184   8805    302   -841  -1441       C
ATOM   1829  CG  LYS A 227     -97.716  69.125 -52.043  1.00 76.41           C
ANISOU 1829  CG  LYS A 227    10523   8614   9895    354   -786  -1530       C
ATOM   1830  CD  LYS A 227     -96.851  69.741 -53.130  1.00 85.66           C
ANISOU 1830  CD  LYS A 227    11782   9873  10893    392   -882  -1542       C
ATOM   1831  CE  LYS A 227     -97.026  69.013 -54.454  1.00 92.82           C
ANISOU 1831  CE  LYS A 227    12785  10927  11554    439   -811  -1605       C
ATOM   1832  NZ  LYS A 227     -96.512  67.616 -54.396  1.00 95.10           N
ANISOU 1832  NZ  LYS A 227    13121  11281  11731    410   -651  -1462       N
ATOM   1833  N   LEU A 228     -94.740  69.737 -48.119  1.00 46.74           N
ANISOU 1833  N   LEU A 228     6600   4643   6518    209   -828  -1049       N
ATOM   1834  CA  LEU A 228     -94.498  70.037 -46.715  1.00 46.53           C
ANISOU 1834  CA  LEU A 228     6479   4544   6656    167   -833   -966       C
ATOM   1835  C   LEU A 228     -93.672  71.303 -46.514  1.00 46.59           C
ANISOU 1835  C   LEU A 228     6445   4544   6714    166   -957   -946       C
ATOM   1836  O   LEU A 228     -93.063  71.474 -45.453  1.00 49.70           O
ANISOU 1836  O   LEU A 228     6774   4915   7196    141   -954   -858       O
ATOM   1837  CB  LEU A 228     -93.816  68.849 -46.036  1.00 47.40           C
ANISOU 1837  CB  LEU A 228     6606   4663   6743    153   -724   -842       C
ATOM   1838  CG  LEU A 228     -94.689  67.610 -45.839  1.00 46.84           C
ANISOU 1838  CG  LEU A 228     6534   4586   6678    138   -597   -850       C
ATOM   1839  CD1 LEU A 228     -93.841  66.405 -45.467  1.00 50.17           C
ANISOU 1839  CD1 LEU A 228     6990   5026   7047    124   -503   -734       C
ATOM   1840  CD2 LEU A 228     -95.738  67.874 -44.772  1.00 45.10           C
ANISOU 1840  CD2 LEU A 228     6212   4286   6636    109   -596   -877       C
ATOM   1841  N   GLU A 229     -93.639  72.191 -47.505  1.00 47.18           N
ANISOU 1841  N   GLU A 229     6546   4647   6732    194  -1065  -1035       N
ATOM   1842  CA  GLU A 229     -92.907  73.442 -47.359  1.00 51.32           C
ANISOU 1842  CA  GLU A 229     7015   5170   7316    192  -1190  -1030       C
ATOM   1843  C   GLU A 229     -93.557  74.312 -46.289  1.00 47.37           C
ANISOU 1843  C   GLU A 229     6385   4592   7022    131  -1222  -1037       C
ATOM   1844  O   GLU A 229     -94.782  74.469 -46.260  1.00 48.01           O
ANISOU 1844  O   GLU A 229     6439   4612   7190    105  -1223  -1112       O
ATOM   1845  CB  GLU A 229     -92.853  74.194 -48.689  1.00 59.24           C
ANISOU 1845  CB  GLU A 229     8071   6220   8218    236  -1308  -1139       C
ATOM   1846  CG  GLU A 229     -92.103  73.477 -49.803  1.00 67.81           C
ANISOU 1846  CG  GLU A 229     9290   7396   9080    297  -1293  -1116       C
ATOM   1847  CD  GLU A 229     -93.023  72.691 -50.718  1.00 78.00           C
ANISOU 1847  CD  GLU A 229    10663   8727  10246    318  -1222  -1196       C
ATOM   1848  OE1 GLU A 229     -93.625  71.702 -50.254  1.00 80.09           O
ANISOU 1848  OE1 GLU A 229    10923   8970  10536    293  -1093  -1168       O
ATOM   1849  OE2 GLU A 229     -93.152  73.071 -51.901  1.00 83.96           O
ANISOU 1849  OE2 GLU A 229    11482   9544  10876    363  -1296  -1296       O
ATOM   1850  N   GLY A 230     -92.735  74.876 -45.409  1.00 42.46           N
ANISOU 1850  N   GLY A 230     5683   3972   6479    107  -1250   -957       N
ATOM   1851  CA  GLY A 230     -93.217  75.754 -44.365  1.00 44.04           C
ANISOU 1851  CA  GLY A 230     5756   4116   6862     39  -1276   -940       C
ATOM   1852  C   GLY A 230     -93.591  75.079 -43.065  1.00 45.54           C
ANISOU 1852  C   GLY A 230     5900   4269   7136     -1  -1167   -850       C
ATOM   1853  O   GLY A 230     -94.138  75.746 -42.178  1.00 51.75           O
ANISOU 1853  O   GLY A 230     6589   5006   8067    -64  -1182   -824       O
ATOM   1854  N   TYR A 231     -93.316  73.784 -42.919  1.00 41.39           N
ANISOU 1854  N   TYR A 231     5440   3765   6522     28  -1063   -796       N
ATOM   1855  CA  TYR A 231     -93.637  73.052 -41.703  1.00 38.80           C
ANISOU 1855  CA  TYR A 231     5071   3408   6262     -3   -965   -717       C
ATOM   1856  C   TYR A 231     -92.403  72.615 -40.925  1.00 39.20           C
ANISOU 1856  C   TYR A 231     5106   3509   6279     14   -921   -620       C
ATOM   1857  O   TYR A 231     -92.542  71.913 -39.917  1.00 38.93           O
ANISOU 1857  O   TYR A 231     5044   3463   6284     -4   -841   -559       O
ATOM   1858  CB  TYR A 231     -94.506  71.833 -42.037  1.00 38.97           C
ANISOU 1858  CB  TYR A 231     5163   3406   6238     12   -877   -748       C
ATOM   1859  CG  TYR A 231     -95.868  72.198 -42.585  1.00 44.48           C
ANISOU 1859  CG  TYR A 231     5860   4044   6995      3   -915   -854       C
ATOM   1860  CD1 TYR A 231     -96.923  72.497 -41.733  1.00 43.96           C
ANISOU 1860  CD1 TYR A 231     5723   3897   7081    -43   -920   -848       C
ATOM   1861  CD2 TYR A 231     -96.097  72.250 -43.954  1.00 51.08           C
ANISOU 1861  CD2 TYR A 231     6771   4905   7732     44   -954   -961       C
ATOM   1862  CE1 TYR A 231     -98.171  72.835 -42.228  1.00 43.43           C
ANISOU 1862  CE1 TYR A 231     5658   3758   7086    -44   -968   -952       C
ATOM   1863  CE2 TYR A 231     -97.341  72.587 -44.460  1.00 51.92           C
ANISOU 1863  CE2 TYR A 231     6876   4956   7897     46   -996  -1078       C
ATOM   1864  CZ  TYR A 231     -98.374  72.878 -43.592  1.00 48.01           C
ANISOU 1864  CZ  TYR A 231     6307   4363   7571      3  -1006  -1076       C
ATOM   1865  OH  TYR A 231     -99.614  73.214 -44.088  1.00 44.74           O
ANISOU 1865  OH  TYR A 231     5893   3876   7231     11  -1061  -1199       O
ATOM   1866  N   ALA A 232     -91.205  73.002 -41.372  1.00 39.40           N
ANISOU 1866  N   ALA A 232     5149   3587   6236     54   -980   -614       N
ATOM   1867  CA  ALA A 232     -89.960  72.798 -40.625  1.00 39.84           C
ANISOU 1867  CA  ALA A 232     5176   3684   6279     79   -963   -541       C
ATOM   1868  C   ALA A 232     -89.673  71.318 -40.377  1.00 39.72           C
ANISOU 1868  C   ALA A 232     5231   3660   6200    100   -865   -488       C
ATOM   1869  O   ALA A 232     -89.207  70.931 -39.304  1.00 39.07           O
ANISOU 1869  O   ALA A 232     5103   3587   6155     99   -819   -431       O
ATOM   1870  CB  ALA A 232     -89.974  73.575 -39.306  1.00 35.92           C
ANISOU 1870  CB  ALA A 232     4542   3201   5903     34   -964   -500       C
ATOM   1871  N   PHE A 233     -89.941  70.480 -41.381  1.00 41.32           N
ANISOU 1871  N   PHE A 233     5542   3851   6305    117   -832   -509       N
ATOM   1872  CA  PHE A 233     -89.633  69.060 -41.243  1.00 40.38           C
ANISOU 1872  CA  PHE A 233     5489   3724   6131    126   -740   -456       C
ATOM   1873  C   PHE A 233     -88.133  68.808 -41.252  1.00 42.20           C
ANISOU 1873  C   PHE A 233     5759   3970   6305    172   -769   -399       C
ATOM   1874  O   PHE A 233     -87.667  67.834 -40.651  1.00 43.74           O
ANISOU 1874  O   PHE A 233     5968   4147   6504    174   -708   -345       O
ATOM   1875  CB  PHE A 233     -90.315  68.261 -42.350  1.00 42.47           C
ANISOU 1875  CB  PHE A 233     5849   3988   6300    126   -689   -491       C
ATOM   1876  CG  PHE A 233     -91.610  67.637 -41.927  1.00 45.14           C
ANISOU 1876  CG  PHE A 233     6155   4297   6700     89   -605   -517       C
ATOM   1877  CD1 PHE A 233     -92.522  68.354 -41.172  1.00 48.19           C
ANISOU 1877  CD1 PHE A 233     6449   4649   7210     59   -626   -546       C
ATOM   1878  CD2 PHE A 233     -91.916  66.335 -42.282  1.00 48.54           C
ANISOU 1878  CD2 PHE A 233     6644   4732   7069     83   -508   -508       C
ATOM   1879  CE1 PHE A 233     -93.717  67.784 -40.777  1.00 51.99           C
ANISOU 1879  CE1 PHE A 233     6904   5095   7756     36   -563   -570       C
ATOM   1880  CE2 PHE A 233     -93.110  65.759 -41.892  1.00 51.33           C
ANISOU 1880  CE2 PHE A 233     6957   5061   7486     59   -438   -542       C
ATOM   1881  CZ  PHE A 233     -94.011  66.484 -41.138  1.00 53.10           C
ANISOU 1881  CZ  PHE A 233     7096   5245   7836     41   -471   -574       C
ATOM   1882  N   GLU A 234     -87.367  69.669 -41.927  1.00 44.47           N
ANISOU 1882  N   GLU A 234     6064   4286   6548    213   -870   -416       N
ATOM   1883  CA  GLU A 234     -85.912  69.578 -41.859  1.00 49.14           C
ANISOU 1883  CA  GLU A 234     6681   4883   7108    268   -919   -369       C
ATOM   1884  C   GLU A 234     -85.428  69.657 -40.418  1.00 51.27           C
ANISOU 1884  C   GLU A 234     6846   5156   7479    271   -901   -344       C
ATOM   1885  O   GLU A 234     -84.474  68.970 -40.034  1.00 59.37           O
ANISOU 1885  O   GLU A 234     7899   6162   8496    306   -891   -301       O
ATOM   1886  CB  GLU A 234     -85.275  70.693 -42.690  1.00 53.94           C
ANISOU 1886  CB  GLU A 234     7295   5526   7674    316  -1047   -405       C
ATOM   1887  CG  GLU A 234     -85.835  70.846 -44.095  1.00 59.66           C
ANISOU 1887  CG  GLU A 234     8109   6266   8292    318  -1081   -450       C
ATOM   1888  CD  GLU A 234     -87.056  71.745 -44.150  1.00 64.33           C
ANISOU 1888  CD  GLU A 234     8628   6866   8950    274  -1100   -534       C
ATOM   1889  OE1 GLU A 234     -87.560  72.137 -43.076  1.00 66.04           O
ANISOU 1889  OE1 GLU A 234     8732   7068   9293    230  -1071   -539       O
ATOM   1890  OE2 GLU A 234     -87.508  72.063 -45.269  1.00 66.32           O
ANISOU 1890  OE2 GLU A 234     8938   7137   9124    284  -1147   -596       O
ATOM   1891  N   HIS A 235     -86.075  70.489 -39.605  1.00 44.61           N
ANISOU 1891  N   HIS A 235     5884   4337   6730    233   -898   -371       N
ATOM   1892  CA  HIS A 235     -85.677  70.629 -38.211  1.00 34.68           C
ANISOU 1892  CA  HIS A 235     4520   3106   5552    234   -875   -348       C
ATOM   1893  C   HIS A 235     -86.364  69.582 -37.339  1.00 35.52           C
ANISOU 1893  C   HIS A 235     4623   3184   5690    195   -769   -317       C
ATOM   1894  O   HIS A 235     -85.702  68.839 -36.606  1.00 36.04           O
ANISOU 1894  O   HIS A 235     4686   3246   5759    220   -736   -290       O
ATOM   1895  CB  HIS A 235     -85.992  72.049 -37.731  1.00 30.54           C
ANISOU 1895  CB  HIS A 235     3865   2632   5108    204   -920   -375       C
ATOM   1896  CG  HIS A 235     -85.766  72.264 -36.268  1.00 31.99           C
ANISOU 1896  CG  HIS A 235     3930   2866   5359    193   -881   -349       C
ATOM   1897  ND1 HIS A 235     -84.589  72.773 -35.761  1.00 31.95           N
ANISOU 1897  ND1 HIS A 235     3850   2927   5364    247   -923   -357       N
ATOM   1898  CD2 HIS A 235     -86.576  72.057 -35.203  1.00 32.28           C
ANISOU 1898  CD2 HIS A 235     3907   2907   5449    140   -807   -317       C
ATOM   1899  CE1 HIS A 235     -84.680  72.859 -34.446  1.00 34.69           C
ANISOU 1899  CE1 HIS A 235     4096   3328   5759    225   -867   -335       C
ATOM   1900  NE2 HIS A 235     -85.875  72.431 -34.082  1.00 32.47           N
ANISOU 1900  NE2 HIS A 235     3826   3009   5501    158   -799   -304       N
ATOM   1901  N   ILE A 236     -87.691  69.489 -37.439  1.00 36.41           N
ANISOU 1901  N   ILE A 236     4736   3272   5828    140   -725   -329       N
ATOM   1902  CA  ILE A 236     -88.466  68.664 -36.514  1.00 36.00           C
ANISOU 1902  CA  ILE A 236     4658   3198   5821    104   -639   -304       C
ATOM   1903  C   ILE A 236     -88.181  67.182 -36.730  1.00 36.35           C
ANISOU 1903  C   ILE A 236     4791   3207   5813    118   -577   -284       C
ATOM   1904  O   ILE A 236     -87.971  66.428 -35.772  1.00 33.95           O
ANISOU 1904  O   ILE A 236     4462   2900   5537    120   -530   -258       O
ATOM   1905  CB  ILE A 236     -89.967  68.971 -36.666  1.00 38.13           C
ANISOU 1905  CB  ILE A 236     4909   3439   6141     51   -623   -330       C
ATOM   1906  CG1 ILE A 236     -90.241  70.441 -36.352  1.00 27.27           C
ANISOU 1906  CG1 ILE A 236     3439   2086   4837     20   -687   -338       C
ATOM   1907  CG2 ILE A 236     -90.794  68.063 -35.774  1.00 35.01           C
ANISOU 1907  CG2 ILE A 236     4493   3019   5792     23   -544   -306       C
ATOM   1908  CD1 ILE A 236     -91.618  70.894 -36.758  1.00 38.92           C
ANISOU 1908  CD1 ILE A 236     4910   3510   6369    -26   -703   -375       C
ATOM   1909  N   VAL A 237     -88.189  66.737 -37.981  1.00 36.47           N
ANISOU 1909  N   VAL A 237     4908   3201   5750    125   -576   -294       N
ATOM   1910  CA  VAL A 237     -88.114  65.315 -38.304  1.00 34.78           C
ANISOU 1910  CA  VAL A 237     4772   2953   5488    118   -505   -267       C
ATOM   1911  C   VAL A 237     -86.697  64.892 -38.661  1.00 32.10           C
ANISOU 1911  C   VAL A 237     4506   2598   5091    159   -538   -225       C
ATOM   1912  O   VAL A 237     -86.184  63.907 -38.129  1.00 35.49           O
ANISOU 1912  O   VAL A 237     4950   2997   5540    159   -501   -191       O
ATOM   1913  CB  VAL A 237     -89.105  64.975 -39.440  1.00 39.59           C
ANISOU 1913  CB  VAL A 237     5445   3560   6038     94   -465   -299       C
ATOM   1914  CG1 VAL A 237     -89.129  63.478 -39.690  1.00 38.90           C
ANISOU 1914  CG1 VAL A 237     5418   3451   5909     72   -375   -267       C
ATOM   1915  CG2 VAL A 237     -90.493  65.488 -39.099  1.00 42.49           C
ANISOU 1915  CG2 VAL A 237     5741   3924   6479     64   -453   -350       C
ATOM   1916  N   TYR A 238     -86.048  65.623 -39.569  1.00 32.34           N
ANISOU 1916  N   TYR A 238     4585   2644   5060    196   -619   -229       N
ATOM   1917  CA  TYR A 238     -84.716  65.234 -40.016  1.00 33.66           C
ANISOU 1917  CA  TYR A 238     4834   2783   5173    240   -666   -182       C
ATOM   1918  C   TYR A 238     -83.636  65.606 -39.008  1.00 36.90           C
ANISOU 1918  C   TYR A 238     5177   3192   5651    292   -723   -182       C
ATOM   1919  O   TYR A 238     -82.610  64.922 -38.928  1.00 38.05           O
ANISOU 1919  O   TYR A 238     5376   3289   5793    324   -742   -144       O
ATOM   1920  CB  TYR A 238     -84.412  65.869 -41.374  1.00 33.61           C
ANISOU 1920  CB  TYR A 238     4907   2798   5066    270   -743   -186       C
ATOM   1921  CG  TYR A 238     -85.291  65.361 -42.496  1.00 34.89           C
ANISOU 1921  CG  TYR A 238     5152   2973   5131    232   -685   -188       C
ATOM   1922  CD1 TYR A 238     -84.921  64.252 -43.244  1.00 41.08           C
ANISOU 1922  CD1 TYR A 238     6051   3735   5824    218   -641   -121       C
ATOM   1923  CD2 TYR A 238     -86.488  65.990 -42.806  1.00 37.01           C
ANISOU 1923  CD2 TYR A 238     5381   3278   5401    208   -676   -260       C
ATOM   1924  CE1 TYR A 238     -85.720  63.783 -44.271  1.00 42.15           C
ANISOU 1924  CE1 TYR A 238     6253   3905   5857    184   -577   -128       C
ATOM   1925  CE2 TYR A 238     -87.295  65.529 -43.830  1.00 38.12           C
ANISOU 1925  CE2 TYR A 238     5591   3444   5449    185   -622   -282       C
ATOM   1926  CZ  TYR A 238     -86.905  64.427 -44.559  1.00 41.74           C
ANISOU 1926  CZ  TYR A 238     6156   3901   5803    174   -568   -216       C
ATOM   1927  OH  TYR A 238     -87.702  63.963 -45.580  1.00 45.43           O
ANISOU 1927  OH  TYR A 238     6684   4415   6164    152   -504   -241       O
ATOM   1928  N   GLY A 239     -83.842  66.672 -38.239  1.00 35.49           N
ANISOU 1928  N   GLY A 239     4882   3066   5536    299   -751   -224       N
ATOM   1929  CA  GLY A 239     -82.872  67.077 -37.241  1.00 32.67           C
ANISOU 1929  CA  GLY A 239     4444   2733   5235    352   -795   -237       C
ATOM   1930  C   GLY A 239     -81.773  67.969 -37.782  1.00 35.75           C
ANISOU 1930  C   GLY A 239     4838   3143   5604    424   -909   -254       C
ATOM   1931  O   GLY A 239     -81.317  67.790 -38.916  1.00 38.00           O
ANISOU 1931  O   GLY A 239     5231   3391   5817    449   -960   -230       O
ATOM   1932  N   ASP A 240     -81.338  68.933 -36.976  1.00 39.65           N
ANISOU 1932  N   ASP A 240     5209   3703   6153    458   -950   -293       N
ATOM   1933  CA  ASP A 240     -80.286  69.872 -37.346  1.00 42.67           C
ANISOU 1933  CA  ASP A 240     5564   4118   6532    535  -1062   -323       C
ATOM   1934  C   ASP A 240     -79.012  69.493 -36.603  1.00 43.85           C
ANISOU 1934  C   ASP A 240     5691   4254   6714    617  -1095   -336       C
ATOM   1935  O   ASP A 240     -78.987  69.495 -35.367  1.00 43.75           O
ANISOU 1935  O   ASP A 240     5576   4290   6755    620  -1048   -363       O
ATOM   1936  CB  ASP A 240     -80.701  71.308 -37.021  1.00 46.73           C
ANISOU 1936  CB  ASP A 240     5937   4726   7093    513  -1088   -368       C
ATOM   1937  CG  ASP A 240     -79.726  72.339 -37.562  1.00 50.58           C
ANISOU 1937  CG  ASP A 240     6387   5254   7578    588  -1210   -408       C
ATOM   1938  OD1 ASP A 240     -78.756  71.953 -38.246  1.00 52.06           O
ANISOU 1938  OD1 ASP A 240     6670   5391   7721    662  -1284   -398       O
ATOM   1939  OD2 ASP A 240     -79.935  73.543 -37.302  1.00 53.18           O
ANISOU 1939  OD2 ASP A 240     6588   5663   7954    569  -1237   -447       O
ATOM   1940  N   PHE A 241     -77.959  69.175 -37.355  1.00 41.98           N
ANISOU 1940  N   PHE A 241     5552   3953   6444    688  -1180   -320       N
ATOM   1941  CA  PHE A 241     -76.695  68.725 -36.788  1.00 40.08           C
ANISOU 1941  CA  PHE A 241     5313   3672   6244    777  -1229   -337       C
ATOM   1942  C   PHE A 241     -75.553  69.700 -37.046  1.00 41.57           C
ANISOU 1942  C   PHE A 241     5453   3893   6448    884  -1360   -386       C
ATOM   1943  O   PHE A 241     -74.398  69.376 -36.750  1.00 42.75           O
ANISOU 1943  O   PHE A 241     5615   3996   6633    977  -1426   -408       O
ATOM   1944  CB  PHE A 241     -76.330  67.347 -37.343  1.00 38.10           C
ANISOU 1944  CB  PHE A 241     5223   3289   5964    772  -1225   -268       C
ATOM   1945  CG  PHE A 241     -77.396  66.310 -37.143  1.00 35.49           C
ANISOU 1945  CG  PHE A 241     4933   2927   5624    670  -1099   -225       C
ATOM   1946  CD1 PHE A 241     -78.404  66.141 -38.078  1.00 37.68           C
ANISOU 1946  CD1 PHE A 241     5283   3203   5832    592  -1047   -180       C
ATOM   1947  CD2 PHE A 241     -77.386  65.498 -36.022  1.00 34.31           C
ANISOU 1947  CD2 PHE A 241     4744   2757   5534    659  -1038   -242       C
ATOM   1948  CE1 PHE A 241     -79.386  65.186 -37.896  1.00 34.07           C
ANISOU 1948  CE1 PHE A 241     4849   2723   5372    507   -933   -151       C
ATOM   1949  CE2 PHE A 241     -78.366  64.541 -35.834  1.00 33.28           C
ANISOU 1949  CE2 PHE A 241     4642   2601   5402    570   -930   -208       C
ATOM   1950  CZ  PHE A 241     -79.366  64.385 -36.773  1.00 32.80           C
ANISOU 1950  CZ  PHE A 241     4646   2539   5279    494   -876   -163       C
ATOM   1951  N   SER A 242     -75.843  70.883 -37.588  1.00 41.86           N
ANISOU 1951  N   SER A 242     5433   4006   6468    879  -1408   -411       N
ATOM   1952  CA  SER A 242     -74.788  71.820 -37.952  1.00 41.82           C
ANISOU 1952  CA  SER A 242     5380   4036   6476    982  -1542   -460       C
ATOM   1953  C   SER A 242     -74.207  72.558 -36.753  1.00 41.20           C
ANISOU 1953  C   SER A 242     5117   4059   6476   1043  -1550   -546       C
ATOM   1954  O   SER A 242     -73.102  73.101 -36.857  1.00 45.92           O
ANISOU 1954  O   SER A 242     5669   4676   7102   1154  -1662   -600       O
ATOM   1955  CB  SER A 242     -75.316  72.835 -38.968  1.00 44.63           C
ANISOU 1955  CB  SER A 242     5729   4440   6790    952  -1598   -467       C
ATOM   1956  OG  SER A 242     -76.395  73.577 -38.429  1.00 50.00           O
ANISOU 1956  OG  SER A 242     6282   5211   7505    862  -1520   -494       O
ATOM   1957  N   HIS A 243     -74.912  72.589 -35.628  1.00 39.80           N
ANISOU 1957  N   HIS A 243     4832   3957   6332    978  -1435   -561       N
ATOM   1958  CA  HIS A 243     -74.484  73.334 -34.455  1.00 41.95           C
ANISOU 1958  CA  HIS A 243     4921   4358   6662   1022  -1422   -638       C
ATOM   1959  C   HIS A 243     -74.199  72.377 -33.304  1.00 42.50           C
ANISOU 1959  C   HIS A 243     4983   4415   6750   1048  -1354   -656       C
ATOM   1960  O   HIS A 243     -74.508  71.185 -33.365  1.00 43.67           O
ANISOU 1960  O   HIS A 243     5257   4457   6880   1011  -1308   -604       O
ATOM   1961  CB  HIS A 243     -75.542  74.367 -34.048  1.00 46.33           C
ANISOU 1961  CB  HIS A 243     5337   5034   7232    919  -1351   -637       C
ATOM   1962  CG  HIS A 243     -75.989  75.243 -35.176  1.00 57.26           C
ANISOU 1962  CG  HIS A 243     6734   6419   8605    878  -1416   -626       C
ATOM   1963  ND1 HIS A 243     -75.191  76.229 -35.714  1.00 62.14           N
ANISOU 1963  ND1 HIS A 243     7284   7086   9241    952  -1535   -682       N
ATOM   1964  CD2 HIS A 243     -77.150  75.277 -35.872  1.00 60.55           C
ANISOU 1964  CD2 HIS A 243     7218   6794   8994    776  -1386   -578       C
ATOM   1965  CE1 HIS A 243     -75.842  76.835 -36.691  1.00 63.70           C
ANISOU 1965  CE1 HIS A 243     7510   7272   9422    894  -1578   -668       C
ATOM   1966  NE2 HIS A 243     -77.033  76.277 -36.807  1.00 61.78           N
ANISOU 1966  NE2 HIS A 243     7350   6974   9150    789  -1488   -608       N
ATOM   1967  N   SER A 244     -73.595  72.920 -32.243  1.00 42.26           N
ANISOU 1967  N   SER A 244     4796   4504   6756   1113  -1349   -737       N
ATOM   1968  CA  SER A 244     -73.241  72.096 -31.092  1.00 41.82           C
ANISOU 1968  CA  SER A 244     4721   4456   6714   1155  -1297   -778       C
ATOM   1969  C   SER A 244     -74.482  71.517 -30.427  1.00 39.15           C
ANISOU 1969  C   SER A 244     4394   4131   6351   1035  -1165   -719       C
ATOM   1970  O   SER A 244     -74.479  70.361 -29.989  1.00 42.43           O
ANISOU 1970  O   SER A 244     4884   4472   6767   1037  -1130   -713       O
ATOM   1971  CB  SER A 244     -72.429  72.912 -30.087  1.00 43.89           C
ANISOU 1971  CB  SER A 244     4795   4876   7003   1248  -1310   -887       C
ATOM   1972  OG  SER A 244     -73.244  73.869 -29.434  1.00 47.86           O
ANISOU 1972  OG  SER A 244     5146   5545   7494   1162  -1219   -877       O
ATOM   1973  N   GLN A 245     -75.549  72.304 -30.341  1.00 36.93           N
ANISOU 1973  N   GLN A 245     4037   3937   6059    932  -1100   -677       N
ATOM   1974  CA  GLN A 245     -76.818  71.833 -29.805  1.00 35.51           C
ANISOU 1974  CA  GLN A 245     3872   3760   5861    819   -988   -614       C
ATOM   1975  C   GLN A 245     -77.631  71.205 -30.928  1.00 36.71           C
ANISOU 1975  C   GLN A 245     4180   3773   5995    745   -984   -538       C
ATOM   1976  O   GLN A 245     -77.910  71.857 -31.941  1.00 38.02           O
ANISOU 1976  O   GLN A 245     4372   3920   6156    715  -1029   -517       O
ATOM   1977  CB  GLN A 245     -77.593  72.975 -29.151  1.00 37.56           C
ANISOU 1977  CB  GLN A 245     3979   4168   6125    741   -925   -596       C
ATOM   1978  CG  GLN A 245     -77.204  73.222 -27.708  1.00 46.19           C
ANISOU 1978  CG  GLN A 245     4926   5416   7208    779   -871   -646       C
ATOM   1979  CD  GLN A 245     -77.452  72.009 -26.835  1.00 55.21           C
ANISOU 1979  CD  GLN A 245     6123   6530   8324    778   -807   -640       C
ATOM   1980  OE1 GLN A 245     -78.534  71.422 -26.863  1.00 56.84           O
ANISOU 1980  OE1 GLN A 245     6404   6671   8522    689   -751   -568       O
ATOM   1981  NE2 GLN A 245     -76.444  71.617 -26.063  1.00 57.11           N
ANISOU 1981  NE2 GLN A 245     6324   6818   8556    885   -822   -728       N
ATOM   1982  N   LEU A 246     -77.999  69.939 -30.753  1.00 33.22           N
ANISOU 1982  N   LEU A 246     3837   3243   5543    717   -933   -507       N
ATOM   1983  CA  LEU A 246     -78.820  69.259 -31.741  1.00 32.86           C
ANISOU 1983  CA  LEU A 246     3926   3083   5475    644   -912   -440       C
ATOM   1984  C   LEU A 246     -80.195  69.910 -31.810  1.00 32.17           C
ANISOU 1984  C   LEU A 246     3794   3040   5387    541   -856   -401       C
ATOM   1985  O   LEU A 246     -80.815  70.201 -30.784  1.00 34.12           O
ANISOU 1985  O   LEU A 246     3944   3368   5651    498   -792   -395       O
ATOM   1986  CB  LEU A 246     -78.943  67.775 -31.395  1.00 33.85           C
ANISOU 1986  CB  LEU A 246     4138   3121   5602    631   -861   -421       C
ATOM   1987  CG  LEU A 246     -79.378  66.821 -32.511  1.00 38.49           C
ANISOU 1987  CG  LEU A 246     4878   3584   6165    581   -848   -362       C
ATOM   1988  CD1 LEU A 246     -78.777  65.448 -32.279  1.00 42.49           C
ANISOU 1988  CD1 LEU A 246     5463   3992   6690    606   -844   -359       C
ATOM   1989  CD2 LEU A 246     -80.894  66.722 -32.607  1.00 37.98           C
ANISOU 1989  CD2 LEU A 246     4815   3526   6089    478   -764   -321       C
ATOM   1990  N   GLY A 247     -80.666  70.146 -33.031  1.00 34.38           N
ANISOU 1990  N   GLY A 247     4150   3266   5647    505   -885   -376       N
ATOM   1991  CA  GLY A 247     -81.924  70.830 -33.264  1.00 35.25           C
ANISOU 1991  CA  GLY A 247     4226   3398   5768    416   -855   -353       C
ATOM   1992  C   GLY A 247     -83.000  69.856 -33.731  1.00 35.75           C
ANISOU 1992  C   GLY A 247     4395   3375   5812    352   -794   -315       C
ATOM   1993  O   GLY A 247     -82.789  69.091 -34.673  1.00 36.75           O
ANISOU 1993  O   GLY A 247     4644   3424   5895    367   -808   -303       O
ATOM   1994  N   GLY A 248     -84.142  69.905 -33.051  1.00 33.51           N
ANISOU 1994  N   GLY A 248     4059   3111   5561    281   -728   -293       N
ATOM   1995  CA  GLY A 248     -85.289  69.122 -33.481  1.00 32.26           C
ANISOU 1995  CA  GLY A 248     3979   2880   5397    224   -674   -270       C
ATOM   1996  C   GLY A 248     -85.072  67.633 -33.296  1.00 34.56           C
ANISOU 1996  C   GLY A 248     4346   3116   5668    240   -624   -257       C
ATOM   1997  O   GLY A 248     -84.583  67.172 -32.258  1.00 34.32           O
ANISOU 1997  O   GLY A 248     4276   3111   5654    267   -602   -260       O
ATOM   1998  N   LEU A 249     -85.449  66.869 -34.324  1.00 33.80           N
ANISOU 1998  N   LEU A 249     4358   2949   5536    222   -606   -247       N
ATOM   1999  CA  LEU A 249     -85.352  65.409 -34.336  1.00 33.31           C
ANISOU 1999  CA  LEU A 249     4371   2827   5460    218   -553   -229       C
ATOM   2000  C   LEU A 249     -86.194  64.805 -33.205  1.00 36.85           C
ANISOU 2000  C   LEU A 249     4760   3285   5957    182   -483   -224       C
ATOM   2001  O   LEU A 249     -85.688  64.299 -32.202  1.00 36.16           O
ANISOU 2001  O   LEU A 249     4637   3209   5892    206   -472   -229       O
ATOM   2002  CB  LEU A 249     -83.888  64.961 -34.250  1.00 37.07           C
ANISOU 2002  CB  LEU A 249     4883   3278   5924    281   -597   -227       C
ATOM   2003  CG  LEU A 249     -83.576  63.512 -34.623  1.00 36.15           C
ANISOU 2003  CG  LEU A 249     4866   3078   5793    271   -563   -198       C
ATOM   2004  CD1 LEU A 249     -83.690  63.300 -36.126  1.00 37.84           C
ANISOU 2004  CD1 LEU A 249     5193   3251   5935    250   -567   -165       C
ATOM   2005  CD2 LEU A 249     -82.195  63.123 -34.124  1.00 34.18           C
ANISOU 2005  CD2 LEU A 249     4626   2795   5567    335   -614   -206       C
ATOM   2006  N   HIS A 250     -87.512  64.871 -33.406  1.00 37.54           N
ANISOU 2006  N   HIS A 250     4840   3364   6061    130   -445   -223       N
ATOM   2007  CA  HIS A 250     -88.471  64.466 -32.388  1.00 32.66           C
ANISOU 2007  CA  HIS A 250     4163   2754   5492     98   -394   -216       C
ATOM   2008  C   HIS A 250     -89.331  63.274 -32.790  1.00 32.13           C
ANISOU 2008  C   HIS A 250     4146   2633   5429     66   -332   -220       C
ATOM   2009  O   HIS A 250     -90.106  62.786 -31.960  1.00 32.79           O
ANISOU 2009  O   HIS A 250     4184   2718   5556     47   -295   -217       O
ATOM   2010  CB  HIS A 250     -89.377  65.650 -32.017  1.00 28.35           C
ANISOU 2010  CB  HIS A 250     3542   2242   4986     65   -412   -208       C
ATOM   2011  CG  HIS A 250     -88.628  66.843 -31.508  1.00 30.41           C
ANISOU 2011  CG  HIS A 250     3729   2574   5251     84   -460   -201       C
ATOM   2012  ND1 HIS A 250     -88.065  66.888 -30.251  1.00 29.39           N
ANISOU 2012  ND1 HIS A 250     3526   2514   5126    107   -452   -190       N
ATOM   2013  CD2 HIS A 250     -88.348  68.035 -32.088  1.00 31.04           C
ANISOU 2013  CD2 HIS A 250     3787   2678   5328     85   -517   -212       C
ATOM   2014  CE1 HIS A 250     -87.469  68.055 -30.078  1.00 29.17           C
ANISOU 2014  CE1 HIS A 250     3430   2555   5097    120   -493   -192       C
ATOM   2015  NE2 HIS A 250     -87.627  68.770 -31.178  1.00 29.36           N
ANISOU 2015  NE2 HIS A 250     3482   2550   5125    105   -535   -204       N
ATOM   2016  N   LEU A 251     -89.227  62.792 -34.025  1.00 33.75           N
ANISOU 2016  N   LEU A 251     4438   2802   5586     61   -318   -225       N
ATOM   2017  CA  LEU A 251     -89.955  61.613 -34.472  1.00 31.55           C
ANISOU 2017  CA  LEU A 251     4197   2488   5303     30   -248   -232       C
ATOM   2018  C   LEU A 251     -88.998  60.440 -34.614  1.00 35.22           C
ANISOU 2018  C   LEU A 251     4718   2920   5745     32   -224   -209       C
ATOM   2019  O   LEU A 251     -87.910  60.582 -35.180  1.00 42.79           O
ANISOU 2019  O   LEU A 251     5736   3864   6657     55   -263   -187       O
ATOM   2020  CB  LEU A 251     -90.665  61.862 -35.806  1.00 34.39           C
ANISOU 2020  CB  LEU A 251     4609   2843   5614     15   -238   -258       C
ATOM   2021  CG  LEU A 251     -92.070  62.462 -35.752  1.00 37.49           C
ANISOU 2021  CG  LEU A 251     4953   3237   6056     -1   -239   -297       C
ATOM   2022  CD1 LEU A 251     -92.703  62.424 -37.132  1.00 44.17           C
ANISOU 2022  CD1 LEU A 251     5858   4081   6844     -6   -221   -343       C
ATOM   2023  CD2 LEU A 251     -92.939  61.727 -34.743  1.00 32.76           C
ANISOU 2023  CD2 LEU A 251     4291   2625   5531    -17   -193   -299       C
ATOM   2024  N   LEU A 252     -89.419  59.277 -34.108  1.00 32.83           N
ANISOU 2024  N   LEU A 252     4392   2598   5483      5   -165   -212       N
ATOM   2025  CA  LEU A 252     -88.557  58.098 -34.128  1.00 35.41           C
ANISOU 2025  CA  LEU A 252     4762   2881   5811     -6   -144   -188       C
ATOM   2026  C   LEU A 252     -88.142  57.719 -35.544  1.00 34.33           C
ANISOU 2026  C   LEU A 252     4726   2718   5600    -28   -123   -154       C
ATOM   2027  O   LEU A 252     -87.027  57.227 -35.751  1.00 38.68           O
ANISOU 2027  O   LEU A 252     5336   3222   6138    -25   -144   -114       O
ATOM   2028  CB  LEU A 252     -89.261  56.921 -33.455  1.00 37.62           C
ANISOU 2028  CB  LEU A 252     4990   3150   6153    -40    -83   -206       C
ATOM   2029  CG  LEU A 252     -88.447  55.627 -33.380  1.00 39.82           C
ANISOU 2029  CG  LEU A 252     5299   3375   6457    -65    -62   -186       C
ATOM   2030  CD1 LEU A 252     -87.237  55.811 -32.479  1.00 39.34           C
ANISOU 2030  CD1 LEU A 252     5230   3293   6423    -18   -134   -189       C
ATOM   2031  CD2 LEU A 252     -89.299  54.465 -32.906  1.00 39.84           C
ANISOU 2031  CD2 LEU A 252     5243   3374   6522   -106      1   -211       C
ATOM   2032  N   ILE A 253     -89.017  57.937 -36.528  1.00 34.40           N
ANISOU 2032  N   ILE A 253     4758   2755   5556    -47    -87   -167       N
ATOM   2033  CA  ILE A 253     -88.660  57.602 -37.902  1.00 33.86           C
ANISOU 2033  CA  ILE A 253     4789   2683   5393    -68    -63   -131       C
ATOM   2034  C   ILE A 253     -87.515  58.481 -38.389  1.00 32.57           C
ANISOU 2034  C   ILE A 253     4693   2511   5172    -23   -153    -98       C
ATOM   2035  O   ILE A 253     -86.697  58.049 -39.211  1.00 37.67           O
ANISOU 2035  O   ILE A 253     5431   3129   5752    -32   -158    -40       O
ATOM   2036  CB  ILE A 253     -89.896  57.707 -38.817  1.00 33.07           C
ANISOU 2036  CB  ILE A 253     4692   2633   5240    -86     -7   -174       C
ATOM   2037  CG1 ILE A 253     -89.563  57.213 -40.226  1.00 35.73           C
ANISOU 2037  CG1 ILE A 253     5130   2988   5458   -111     34   -132       C
ATOM   2038  CG2 ILE A 253     -90.430  59.131 -38.847  1.00 32.49           C
ANISOU 2038  CG2 ILE A 253     4589   2588   5167    -46    -73   -225       C
ATOM   2039  CD1 ILE A 253     -90.753  57.166 -41.152  1.00 37.59           C
ANISOU 2039  CD1 ILE A 253     5365   3288   5629   -124    100   -188       C
ATOM   2040  N   GLY A 254     -87.421  59.713 -37.886  1.00 33.27           N
ANISOU 2040  N   GLY A 254     4733   2622   5287     23   -227   -130       N
ATOM   2041  CA  GLY A 254     -86.285  60.551 -38.226  1.00 29.23           C
ANISOU 2041  CA  GLY A 254     4265   2106   4736     73   -320   -110       C
ATOM   2042  C   GLY A 254     -84.992  60.028 -37.634  1.00 30.49           C
ANISOU 2042  C   GLY A 254     4442   2210   4934     99   -358    -75       C
ATOM   2043  O   GLY A 254     -83.932  60.110 -38.260  1.00 36.56           O
ANISOU 2043  O   GLY A 254     5288   2944   5657    130   -418    -35       O
ATOM   2044  N   LEU A 255     -85.061  59.479 -36.418  1.00 28.41           N
ANISOU 2044  N   LEU A 255     4107   1932   4754     93   -332    -94       N
ATOM   2045  CA  LEU A 255     -83.889  58.843 -35.828  1.00 30.61           C
ANISOU 2045  CA  LEU A 255     4401   2149   5079    118   -368    -78       C
ATOM   2046  C   LEU A 255     -83.528  57.564 -36.572  1.00 35.38           C
ANISOU 2046  C   LEU A 255     5100   2678   5666     67   -330    -15       C
ATOM   2047  O   LEU A 255     -82.344  57.242 -36.728  1.00 39.77           O
ANISOU 2047  O   LEU A 255     5720   3160   6231     90   -387     24       O
ATOM   2048  CB  LEU A 255     -84.134  58.545 -34.347  1.00 31.00           C
ANISOU 2048  CB  LEU A 255     4350   2214   5213    123   -351   -125       C
ATOM   2049  CG  LEU A 255     -84.096  59.669 -33.308  1.00 34.59           C
ANISOU 2049  CG  LEU A 255     4707   2741   5692    177   -396   -173       C
ATOM   2050  CD1 LEU A 255     -85.329  60.552 -33.382  1.00 33.47           C
ANISOU 2050  CD1 LEU A 255     4514   2669   5536    152   -368   -185       C
ATOM   2051  CD2 LEU A 255     -83.947  59.085 -31.912  1.00 37.07           C
ANISOU 2051  CD2 LEU A 255     4952   3062   6071    192   -389   -210       C
ATOM   2052  N   ALA A 256     -84.536  56.821 -37.036  1.00 35.69           N
ANISOU 2052  N   ALA A 256     5144   2733   5685     -3   -234     -2       N
ATOM   2053  CA  ALA A 256     -84.274  55.581 -37.758  1.00 34.36           C
ANISOU 2053  CA  ALA A 256     5053   2507   5496    -68   -180     66       C
ATOM   2054  C   ALA A 256     -83.552  55.849 -39.071  1.00 36.08           C
ANISOU 2054  C   ALA A 256     5393   2708   5610    -60   -218    140       C
ATOM   2055  O   ALA A 256     -82.596  55.144 -39.415  1.00 41.38           O
ANISOU 2055  O   ALA A 256     6145   3296   6282    -81   -240    216       O
ATOM   2056  CB  ALA A 256     -85.583  54.832 -38.006  1.00 30.31           C
ANISOU 2056  CB  ALA A 256     4500   2039   4976   -138    -63     51       C
ATOM   2057  N   LYS A 257     -83.994  56.865 -39.816  1.00 37.41           N
ANISOU 2057  N   LYS A 257     5577   2947   5688    -32   -236    121       N
ATOM   2058  CA  LYS A 257     -83.329  57.208 -41.068  1.00 40.32           C
ANISOU 2058  CA  LYS A 257     6063   3313   5944    -15   -285    186       C
ATOM   2059  C   LYS A 257     -81.886  57.631 -40.823  1.00 44.78           C
ANISOU 2059  C   LYS A 257     6669   3806   6541     54   -409    214       C
ATOM   2060  O   LYS A 257     -80.978  57.231 -41.562  1.00 46.36           O
ANISOU 2060  O   LYS A 257     6979   3942   6693     51   -449    304       O
ATOM   2061  CB  LYS A 257     -84.106  58.315 -41.780  1.00 34.64           C
ANISOU 2061  CB  LYS A 257     5338   2688   5137     12   -296    134       C
ATOM   2062  CG  LYS A 257     -83.593  58.650 -43.170  1.00 34.14           C
ANISOU 2062  CG  LYS A 257     5395   2643   4933     29   -343    192       C
ATOM   2063  CD  LYS A 257     -84.389  59.793 -43.780  1.00 34.88           C
ANISOU 2063  CD  LYS A 257     5470   2828   4954     61   -368    117       C
ATOM   2064  CE  LYS A 257     -83.960  60.069 -45.212  1.00 41.00           C
ANISOU 2064  CE  LYS A 257     6369   3638   5570     80   -413    168       C
ATOM   2065  NZ  LYS A 257     -84.215  58.900 -46.098  1.00 47.33           N
ANISOU 2065  NZ  LYS A 257     7254   4462   6266     10   -306    242       N
ATOM   2066  N   ARG A 258     -81.654  58.432 -39.781  1.00 43.73           N
ANISOU 2066  N   ARG A 258     6445   3682   6487    119   -473    141       N
ATOM   2067  CA  ARG A 258     -80.299  58.859 -39.453  1.00 40.10           C
ANISOU 2067  CA  ARG A 258     6004   3164   6068    199   -592    145       C
ATOM   2068  C   ARG A 258     -79.447  57.687 -38.982  1.00 44.39           C
ANISOU 2068  C   ARG A 258     6583   3590   6691    182   -600    187       C
ATOM   2069  O   ARG A 258     -78.250  57.621 -39.285  1.00 46.51           O
ANISOU 2069  O   ARG A 258     6931   3773   6967    227   -693    235       O
ATOM   2070  CB  ARG A 258     -80.345  59.951 -38.384  1.00 39.67           C
ANISOU 2070  CB  ARG A 258     5825   3171   6076    264   -639     50       C
ATOM   2071  CG  ARG A 258     -78.989  60.362 -37.828  1.00 44.86           C
ANISOU 2071  CG  ARG A 258     6470   3785   6790    357   -752     27       C
ATOM   2072  CD  ARG A 258     -78.243  61.277 -38.784  1.00 49.38           C
ANISOU 2072  CD  ARG A 258     7105   4362   7296    422   -858     48       C
ATOM   2073  NE  ARG A 258     -77.017  61.801 -38.189  1.00 49.91           N
ANISOU 2073  NE  ARG A 258     7135   4403   7427    525   -971      5       N
ATOM   2074  CZ  ARG A 258     -76.230  62.700 -38.771  1.00 52.26           C
ANISOU 2074  CZ  ARG A 258     7457   4708   7692    605  -1084      2       C
ATOM   2075  NH1 ARG A 258     -76.542  63.179 -39.967  1.00 58.25           N
ANISOU 2075  NH1 ARG A 258     8283   5501   8350    591  -1103     43       N
ATOM   2076  NH2 ARG A 258     -75.132  63.121 -38.159  1.00 49.23           N
ANISOU 2076  NH2 ARG A 258     7024   4304   7376    706  -1182    -52       N
ATOM   2077  N   PHE A 259     -80.049  56.747 -38.249  1.00 45.07           N
ANISOU 2077  N   PHE A 259     6613   3665   6846    121   -514    168       N
ATOM   2078  CA  PHE A 259     -79.277  55.654 -37.668  1.00 44.08           C
ANISOU 2078  CA  PHE A 259     6505   3425   6817    104   -531    188       C
ATOM   2079  C   PHE A 259     -78.717  54.723 -38.734  1.00 48.28           C
ANISOU 2079  C   PHE A 259     7170   3860   7315     41   -525    311       C
ATOM   2080  O   PHE A 259     -77.645  54.138 -38.540  1.00 54.12           O
ANISOU 2080  O   PHE A 259     7962   4473   8128     52   -593    347       O
ATOM   2081  CB  PHE A 259     -80.141  54.872 -36.681  1.00 47.47           C
ANISOU 2081  CB  PHE A 259     6838   3876   7324     49   -443    134       C
ATOM   2082  CG  PHE A 259     -79.366  53.917 -35.827  1.00 54.66           C
ANISOU 2082  CG  PHE A 259     7739   4680   8351     47   -478    118       C
ATOM   2083  CD1 PHE A 259     -78.617  54.379 -34.757  1.00 56.14           C
ANISOU 2083  CD1 PHE A 259     7870   4855   8607    140   -567     35       C
ATOM   2084  CD2 PHE A 259     -79.386  52.559 -36.089  1.00 59.24           C
ANISOU 2084  CD2 PHE A 259     8359   5176   8974    -49   -423    179       C
ATOM   2085  CE1 PHE A 259     -77.900  53.505 -33.966  1.00 58.54           C
ANISOU 2085  CE1 PHE A 259     8165   5058   9019    146   -610      2       C
ATOM   2086  CE2 PHE A 259     -78.672  51.679 -35.301  1.00 65.37           C
ANISOU 2086  CE2 PHE A 259     9124   5842   9871    -54   -466    156       C
ATOM   2087  CZ  PHE A 259     -77.928  52.153 -34.238  1.00 64.52           C
ANISOU 2087  CZ  PHE A 259     8967   5717   9831     48   -565     62       C
ATOM   2088  N   LYS A 260     -79.419  54.570 -39.858  1.00 50.59           N
ANISOU 2088  N   LYS A 260     7518   4208   7495    -25   -445    376       N
ATOM   2089  CA  LYS A 260     -78.904  53.733 -40.935  1.00 55.36           C
ANISOU 2089  CA  LYS A 260     8252   4739   8043    -93   -431    510       C
ATOM   2090  C   LYS A 260     -77.671  54.352 -41.579  1.00 59.71           C
ANISOU 2090  C   LYS A 260     8914   5224   8549    -18   -566    574       C
ATOM   2091  O   LYS A 260     -76.788  53.627 -42.051  1.00 61.68           O
ANISOU 2091  O   LYS A 260     9271   5355   8809    -50   -605    686       O
ATOM   2092  CB  LYS A 260     -79.993  53.496 -41.982  1.00 59.11           C
ANISOU 2092  CB  LYS A 260     8751   5320   8389   -172   -308    552       C
ATOM   2093  CG  LYS A 260     -80.110  52.051 -42.441  1.00 65.14           C
ANISOU 2093  CG  LYS A 260     9558   6040   9152   -297   -204    653       C
ATOM   2094  CD  LYS A 260     -81.150  51.901 -43.541  1.00 67.49           C
ANISOU 2094  CD  LYS A 260     9875   6467   9303   -361    -80    682       C
ATOM   2095  CE  LYS A 260     -81.297  50.448 -43.968  1.00 65.17           C
ANISOU 2095  CE  LYS A 260     9604   6149   9008   -494     38    782       C
ATOM   2096  NZ  LYS A 260     -82.226  50.295 -45.122  1.00 61.54           N
ANISOU 2096  NZ  LYS A 260     9166   5831   8386   -550    163    811       N
ATOM   2097  N   GLU A 261     -77.588  55.682 -41.598  1.00 64.53           N
ANISOU 2097  N   GLU A 261     9497   5904   9116     81   -645    508       N
ATOM   2098  CA  GLU A 261     -76.438  56.357 -42.188  1.00 70.45           C
ANISOU 2098  CA  GLU A 261    10339   6601   9826    168   -786    554       C
ATOM   2099  C   GLU A 261     -75.283  56.442 -41.197  1.00 66.49           C
ANISOU 2099  C   GLU A 261     9808   5992   9464    254   -904    505       C
ATOM   2100  O   GLU A 261     -74.182  55.948 -41.461  1.00 67.66           O
ANISOU 2100  O   GLU A 261    10055   6003   9651    270   -990    584       O
ATOM   2101  CB  GLU A 261     -76.837  57.759 -42.657  1.00 84.47           C
ANISOU 2101  CB  GLU A 261    12088   8504  11504    235   -825    494       C
ATOM   2102  CG  GLU A 261     -78.237  57.851 -43.234  1.00 97.41           C
ANISOU 2102  CG  GLU A 261    13702  10270  13038    168   -704    476       C
ATOM   2103  CD  GLU A 261     -78.660  59.283 -43.498  1.00107.36           C
ANISOU 2103  CD  GLU A 261    14914  11641  14237    234   -756    394       C
ATOM   2104  OE1 GLU A 261     -79.391  59.518 -44.483  1.00110.57           O
ANISOU 2104  OE1 GLU A 261    15361  12132  14517    206   -713    403       O
ATOM   2105  OE2 GLU A 261     -78.257  60.175 -42.721  1.00110.30           O
ANISOU 2105  OE2 GLU A 261    15203  12020  14687    314   -838    314       O
ATOM   2106  N   SER A 262     -75.521  57.071 -40.047  1.00 61.42           N
ANISOU 2106  N   SER A 262     9029   5411   8897    313   -911    372       N
ATOM   2107  CA  SER A 262     -74.494  57.303 -39.048  1.00 61.65           C
ANISOU 2107  CA  SER A 262     9007   5373   9044    412  -1018    296       C
ATOM   2108  C   SER A 262     -74.996  56.886 -37.673  1.00 54.80           C
ANISOU 2108  C   SER A 262     8014   4532   8275    393   -950    197       C
ATOM   2109  O   SER A 262     -76.177  57.071 -37.359  1.00 58.06           O
ANISOU 2109  O   SER A 262     8344   5059   8659    346   -849    154       O
ATOM   2110  CB  SER A 262     -74.083  58.782 -39.024  1.00 68.21           C
ANISOU 2110  CB  SER A 262     9785   6284   9847    532  -1119    223       C
ATOM   2111  OG  SER A 262     -73.127  59.028 -38.009  1.00 78.61           O
ANISOU 2111  OG  SER A 262    11036   7559  11274    636  -1212    132       O
ATOM   2112  N   PRO A 263     -74.131  56.321 -36.838  1.00 53.38           N
ANISOU 2112  N   PRO A 263     7822   4247   8213    433  -1013    155       N
ATOM   2113  CA  PRO A 263     -74.547  55.934 -35.488  1.00 50.76           C
ANISOU 2113  CA  PRO A 263     7372   3949   7966    426   -962     52       C
ATOM   2114  C   PRO A 263     -74.561  57.125 -34.540  1.00 47.04           C
ANISOU 2114  C   PRO A 263     6772   3606   7497    527   -993    -73       C
ATOM   2115  O   PRO A 263     -73.995  58.184 -34.813  1.00 51.73           O
ANISOU 2115  O   PRO A 263     7360   4237   8058    616  -1074    -94       O
ATOM   2116  CB  PRO A 263     -73.478  54.917 -35.076  1.00 57.26           C
ANISOU 2116  CB  PRO A 263     8241   4611   8905    438  -1033     51       C
ATOM   2117  CG  PRO A 263     -72.255  55.378 -35.803  1.00 60.14           C
ANISOU 2117  CG  PRO A 263     8692   4913   9247    517  -1153     97       C
ATOM   2118  CD  PRO A 263     -72.736  55.939 -37.120  1.00 56.56           C
ANISOU 2118  CD  PRO A 263     8326   4484   8679    486  -1141    202       C
ATOM   2119  N   PHE A 264     -75.229  56.928 -33.407  1.00 38.01           N
ANISOU 2119  N   PHE A 264     5518   2534   6388    510   -927   -153       N
ATOM   2120  CA  PHE A 264     -75.295  57.946 -32.367  1.00 37.48           C
ANISOU 2120  CA  PHE A 264     5320   2600   6320    592   -940   -263       C
ATOM   2121  C   PHE A 264     -75.643  57.270 -31.050  1.00 40.34           C
ANISOU 2121  C   PHE A 264     5597   2988   6742    579   -895   -342       C
ATOM   2122  O   PHE A 264     -76.055  56.108 -31.014  1.00 42.42           O
ANISOU 2122  O   PHE A 264     5891   3181   7044    497   -844   -311       O
ATOM   2123  CB  PHE A 264     -76.309  59.042 -32.709  1.00 40.62           C
ANISOU 2123  CB  PHE A 264     5666   3140   6629    567   -881   -248       C
ATOM   2124  CG  PHE A 264     -77.628  58.517 -33.194  1.00 47.33           C
ANISOU 2124  CG  PHE A 264     6538   4007   7437    450   -768   -184       C
ATOM   2125  CD1 PHE A 264     -78.606  58.117 -32.298  1.00 49.76           C
ANISOU 2125  CD1 PHE A 264     6764   4373   7767    402   -685   -220       C
ATOM   2126  CD2 PHE A 264     -77.889  58.424 -34.550  1.00 52.67           C
ANISOU 2126  CD2 PHE A 264     7316   4650   8047    396   -749    -94       C
ATOM   2127  CE1 PHE A 264     -79.819  57.631 -32.747  1.00 52.18           C
ANISOU 2127  CE1 PHE A 264     7084   4696   8045    306   -588   -174       C
ATOM   2128  CE2 PHE A 264     -79.099  57.942 -35.005  1.00 55.73           C
ANISOU 2128  CE2 PHE A 264     7716   5065   8395    299   -643    -51       C
ATOM   2129  CZ  PHE A 264     -80.066  57.545 -34.104  1.00 55.00           C
ANISOU 2129  CZ  PHE A 264     7535   5022   8340    256   -564    -95       C
ATOM   2130  N   GLU A 265     -75.474  58.015 -29.963  1.00 39.72           N
ANISOU 2130  N   GLU A 265     5404   3021   6666    661   -916   -445       N
ATOM   2131  CA  GLU A 265     -75.694  57.496 -28.621  1.00 39.63           C
ANISOU 2131  CA  GLU A 265     5307   3056   6695    670   -890   -532       C
ATOM   2132  C   GLU A 265     -77.018  58.014 -28.080  1.00 41.22           C
ANISOU 2132  C   GLU A 265     5416   3413   6835    622   -792   -531       C
ATOM   2133  O   GLU A 265     -77.307  59.211 -28.174  1.00 43.16           O
ANISOU 2133  O   GLU A 265     5608   3769   7021    641   -780   -524       O
ATOM   2134  CB  GLU A 265     -74.551  57.898 -27.688  1.00 46.29           C
ANISOU 2134  CB  GLU A 265     6086   3928   7573    802   -980   -655       C
ATOM   2135  CG  GLU A 265     -74.375  56.967 -26.501  1.00 57.26           C
ANISOU 2135  CG  GLU A 265     7432   5300   9024    823   -989   -752       C
ATOM   2136  CD  GLU A 265     -73.840  55.605 -26.904  1.00 67.67           C
ANISOU 2136  CD  GLU A 265     8852   6434  10426    775  -1028   -721       C
ATOM   2137  OE1 GLU A 265     -72.951  55.547 -27.781  1.00 69.45           O
ANISOU 2137  OE1 GLU A 265     9164   6568  10656    785  -1087   -664       O
ATOM   2138  OE2 GLU A 265     -74.313  54.591 -26.349  1.00 73.11           O
ANISOU 2138  OE2 GLU A 265     9525   7107  11146    712   -986   -737       O
ATOM   2139  N   LEU A 266     -77.817  57.111 -27.517  1.00 43.14           N
ANISOU 2139  N   LEU A 266     5637   3656   7100    557   -730   -535       N
ATOM   2140  CA  LEU A 266     -79.090  57.453 -26.894  1.00 41.73           C
ANISOU 2140  CA  LEU A 266     5375   3606   6875    514   -649   -532       C
ATOM   2141  C   LEU A 266     -79.042  57.040 -25.431  1.00 42.27           C
ANISOU 2141  C   LEU A 266     5361   3738   6964    555   -656   -625       C
ATOM   2142  O   LEU A 266     -78.947  55.847 -25.122  1.00 46.80           O
ANISOU 2142  O   LEU A 266     5956   4229   7598    533   -664   -654       O
ATOM   2143  CB  LEU A 266     -80.261  56.773 -27.607  1.00 40.69           C
ANISOU 2143  CB  LEU A 266     5288   3431   6743    403   -569   -452       C
ATOM   2144  CG  LEU A 266     -80.791  57.434 -28.883  1.00 44.89           C
ANISOU 2144  CG  LEU A 266     5871   3964   7220    358   -537   -370       C
ATOM   2145  CD1 LEU A 266     -82.022  56.699 -29.377  1.00 47.83           C
ANISOU 2145  CD1 LEU A 266     6265   4316   7592    260   -452   -319       C
ATOM   2146  CD2 LEU A 266     -81.107  58.904 -28.655  1.00 43.04           C
ANISOU 2146  CD2 LEU A 266     5565   3856   6932    392   -540   -379       C
ATOM   2147  N   GLU A 267     -79.103  58.022 -24.538  1.00 38.96           N
ANISOU 2147  N   GLU A 267     4844   3470   6489    611   -653   -671       N
ATOM   2148  CA  GLU A 267     -79.072  57.785 -23.100  1.00 40.14           C
ANISOU 2148  CA  GLU A 267     4909   3715   6627    660   -657   -760       C
ATOM   2149  C   GLU A 267     -80.507  57.819 -22.588  1.00 34.71           C
ANISOU 2149  C   GLU A 267     4171   3120   5897    591   -580   -712       C
ATOM   2150  O   GLU A 267     -81.117  58.889 -22.499  1.00 34.08           O
ANISOU 2150  O   GLU A 267     4040   3151   5757    576   -542   -665       O
ATOM   2151  CB  GLU A 267     -78.205  58.826 -22.396  1.00 48.35           C
ANISOU 2151  CB  GLU A 267     5869   4882   7621    767   -697   -839       C
ATOM   2152  CG  GLU A 267     -77.186  58.259 -21.423  1.00 62.86           C
ANISOU 2152  CG  GLU A 267     7676   6721   9486    865   -763   -975       C
ATOM   2153  CD  GLU A 267     -77.602  58.431 -19.977  1.00 75.66           C
ANISOU 2153  CD  GLU A 267     9192   8522  11034    897   -731  -1038       C
ATOM   2154  OE1 GLU A 267     -77.837  57.406 -19.305  1.00 79.07           O
ANISOU 2154  OE1 GLU A 267     9625   8930  11488    888   -739  -1086       O
ATOM   2155  OE2 GLU A 267     -77.699  59.589 -19.515  1.00 80.03           O
ANISOU 2155  OE2 GLU A 267     9658   9244  11504    927   -699  -1035       O
ATOM   2156  N   ASP A 268     -81.044  56.646 -22.259  1.00 32.47           N
ANISOU 2156  N   ASP A 268     3899   2784   5653    547   -564   -722       N
ATOM   2157  CA  ASP A 268     -82.420  56.517 -21.781  1.00 31.40           C
ANISOU 2157  CA  ASP A 268     3722   2717   5491    488   -505   -679       C
ATOM   2158  C   ASP A 268     -82.435  56.715 -20.264  1.00 32.35           C
ANISOU 2158  C   ASP A 268     3752   2985   5553    548   -517   -746       C
ATOM   2159  O   ASP A 268     -82.549  55.776 -19.476  1.00 37.47           O
ANISOU 2159  O   ASP A 268     4382   3635   6221    558   -536   -806       O
ATOM   2160  CB  ASP A 268     -82.985  55.162 -22.191  1.00 35.06           C
ANISOU 2160  CB  ASP A 268     4231   3062   6028    416   -485   -663       C
ATOM   2161  CG  ASP A 268     -84.455  55.016 -21.871  1.00 38.98           C
ANISOU 2161  CG  ASP A 268     4688   3613   6510    360   -431   -618       C
ATOM   2162  OD1 ASP A 268     -85.079  56.011 -21.444  1.00 40.84           O
ANISOU 2162  OD1 ASP A 268     4876   3962   6682    368   -410   -581       O
ATOM   2163  OD2 ASP A 268     -84.987  53.900 -22.048  1.00 42.32           O
ANISOU 2163  OD2 ASP A 268     5124   3963   6993    308   -413   -618       O
ATOM   2164  N   PHE A 269     -82.317  57.983 -19.861  1.00 32.89           N
ANISOU 2164  N   PHE A 269     3761   3192   5544    587   -507   -735       N
ATOM   2165  CA  PHE A 269     -82.121  58.285 -18.447  1.00 36.30           C
ANISOU 2165  CA  PHE A 269     4106   3787   5899    654   -516   -800       C
ATOM   2166  C   PHE A 269     -83.394  58.143 -17.622  1.00 34.58           C
ANISOU 2166  C   PHE A 269     3848   3658   5633    610   -477   -750       C
ATOM   2167  O   PHE A 269     -83.319  58.200 -16.389  1.00 35.66           O
ANISOU 2167  O   PHE A 269     3920   3934   5694    661   -485   -800       O
ATOM   2168  CB  PHE A 269     -81.523  59.687 -18.276  1.00 38.69           C
ANISOU 2168  CB  PHE A 269     4345   4222   6133    705   -510   -804       C
ATOM   2169  CG  PHE A 269     -82.345  60.795 -18.881  1.00 39.43           C
ANISOU 2169  CG  PHE A 269     4428   4350   6205    633   -459   -684       C
ATOM   2170  CD1 PHE A 269     -83.239  61.512 -18.105  1.00 37.75           C
ANISOU 2170  CD1 PHE A 269     4145   4279   5919    599   -412   -617       C
ATOM   2171  CD2 PHE A 269     -82.196  61.143 -20.216  1.00 38.77           C
ANISOU 2171  CD2 PHE A 269     4402   4156   6172    601   -466   -638       C
ATOM   2172  CE1 PHE A 269     -83.986  62.540 -18.649  1.00 37.79           C
ANISOU 2172  CE1 PHE A 269     4138   4300   5922    528   -376   -510       C
ATOM   2173  CE2 PHE A 269     -82.941  62.173 -20.767  1.00 35.25           C
ANISOU 2173  CE2 PHE A 269     3942   3738   5713    538   -430   -544       C
ATOM   2174  CZ  PHE A 269     -83.837  62.872 -19.981  1.00 37.19           C
ANISOU 2174  CZ  PHE A 269     4116   4110   5903    500   -387   -482       C
ATOM   2175  N   ILE A 270     -84.548  57.960 -18.255  1.00 33.32           N
ANISOU 2175  N   ILE A 270     3723   3425   5511    524   -440   -656       N
ATOM   2176  CA  ILE A 270     -85.752  57.543 -17.542  1.00 29.59           C
ANISOU 2176  CA  ILE A 270     3225   2997   5020    489   -423   -617       C
ATOM   2177  C   ILE A 270     -86.208  56.227 -18.160  1.00 30.90           C
ANISOU 2177  C   ILE A 270     3444   3013   5284    442   -426   -627       C
ATOM   2178  O   ILE A 270     -87.134  56.218 -18.985  1.00 32.27           O
ANISOU 2178  O   ILE A 270     3647   3114   5498    374   -391   -553       O
ATOM   2179  CB  ILE A 270     -86.855  58.610 -17.604  1.00 34.69           C
ANISOU 2179  CB  ILE A 270     3848   3706   5628    434   -379   -497       C
ATOM   2180  CG1 ILE A 270     -86.303  59.977 -17.201  1.00 38.49           C
ANISOU 2180  CG1 ILE A 270     4270   4327   6026    464   -367   -479       C
ATOM   2181  CG2 ILE A 270     -88.005  58.233 -16.683  1.00 35.34           C
ANISOU 2181  CG2 ILE A 270     3900   3844   5682    416   -378   -458       C
ATOM   2182  CD1 ILE A 270     -87.336  61.082 -17.223  1.00 40.72           C
ANISOU 2182  CD1 ILE A 270     4526   4665   6282    400   -330   -355       C
ATOM   2183  N   PRO A 271     -85.583  55.099 -17.805  1.00 29.87           N
ANISOU 2183  N   PRO A 271     3321   2833   5197    473   -469   -724       N
ATOM   2184  CA  PRO A 271     -85.916  53.830 -18.467  1.00 30.52           C
ANISOU 2184  CA  PRO A 271     3444   2770   5381    416   -467   -732       C
ATOM   2185  C   PRO A 271     -87.273  53.283 -18.054  1.00 32.47           C
ANISOU 2185  C   PRO A 271     3658   3039   5641    377   -450   -701       C
ATOM   2186  O   PRO A 271     -87.384  52.511 -17.096  1.00 39.00           O
ANISOU 2186  O   PRO A 271     4446   3904   6470    403   -489   -767       O
ATOM   2187  CB  PRO A 271     -84.776  52.902 -18.029  1.00 27.24           C
ANISOU 2187  CB  PRO A 271     3032   2306   5012    464   -530   -851       C
ATOM   2188  CG  PRO A 271     -84.337  53.450 -16.717  1.00 27.78           C
ANISOU 2188  CG  PRO A 271     3040   2530   4983    553   -565   -919       C
ATOM   2189  CD  PRO A 271     -84.513  54.942 -16.805  1.00 29.48           C
ANISOU 2189  CD  PRO A 271     3236   2856   5109    561   -523   -839       C
ATOM   2190  N   MET A 272     -88.312  53.676 -18.783  1.00 29.87           N
ANISOU 2190  N   MET A 272     3343   2683   5323    320   -402   -610       N
ATOM   2191  CA  MET A 272     -89.663  53.212 -18.510  1.00 29.86           C
ANISOU 2191  CA  MET A 272     3311   2689   5347    289   -391   -579       C
ATOM   2192  C   MET A 272     -90.470  53.303 -19.793  1.00 30.79           C
ANISOU 2192  C   MET A 272     3464   2718   5517    223   -338   -514       C
ATOM   2193  O   MET A 272     -90.072  53.968 -20.752  1.00 35.22           O
ANISOU 2193  O   MET A 272     4072   3241   6070    205   -311   -479       O
ATOM   2194  CB  MET A 272     -90.330  54.031 -17.401  1.00 28.02           C
ANISOU 2194  CB  MET A 272     3030   2590   5025    320   -406   -532       C
ATOM   2195  CG  MET A 272     -90.471  55.505 -17.739  1.00 31.06           C
ANISOU 2195  CG  MET A 272     3425   3021   5356    306   -376   -442       C
ATOM   2196  SD  MET A 272     -91.416  56.420 -16.511  1.00 39.43           S
ANISOU 2196  SD  MET A 272     4433   4224   6324    318   -387   -355       S
ATOM   2197  CE  MET A 272     -93.045  55.707 -16.723  1.00 40.39           C
ANISOU 2197  CE  MET A 272     4557   4262   6529    278   -393   -312       C
ATOM   2198  N   ASP A 273     -91.611  52.623 -19.796  1.00 34.61           N
ANISOU 2198  N   ASP A 273     3922   3175   6052    196   -328   -507       N
ATOM   2199  CA  ASP A 273     -92.535  52.694 -20.919  1.00 34.77           C
ANISOU 2199  CA  ASP A 273     3964   3128   6118    145   -279   -461       C
ATOM   2200  C   ASP A 273     -93.371  53.961 -20.792  1.00 35.66           C
ANISOU 2200  C   ASP A 273     4072   3289   6188    150   -280   -383       C
ATOM   2201  O   ASP A 273     -94.107  54.131 -19.813  1.00 35.20           O
ANISOU 2201  O   ASP A 273     3974   3291   6111    173   -312   -358       O
ATOM   2202  CB  ASP A 273     -93.428  51.455 -20.957  1.00 33.85           C
ANISOU 2202  CB  ASP A 273     3808   2970   6083    122   -270   -498       C
ATOM   2203  CG  ASP A 273     -94.008  51.197 -22.334  1.00 34.23           C
ANISOU 2203  CG  ASP A 273     3880   2942   6184     69   -206   -484       C
ATOM   2204  OD1 ASP A 273     -93.421  51.679 -23.326  1.00 32.70           O
ANISOU 2204  OD1 ASP A 273     3746   2712   5965     46   -172   -458       O
ATOM   2205  OD2 ASP A 273     -95.053  50.519 -22.425  1.00 32.85           O
ANISOU 2205  OD2 ASP A 273     3661   2751   6069     56   -193   -504       O
ATOM   2206  N   SER A 274     -93.247  54.857 -21.768  1.00 24.18           N
ANISOU 2206  N   SER A 274     2662   1806   4720    127   -251   -342       N
ATOM   2207  CA  SER A 274     -94.022  56.086 -21.769  1.00 27.31           C
ANISOU 2207  CA  SER A 274     3054   2228   5094    120   -256   -270       C
ATOM   2208  C   SER A 274     -94.290  56.501 -23.207  1.00 26.58           C
ANISOU 2208  C   SER A 274     3009   2061   5028     83   -220   -256       C
ATOM   2209  O   SER A 274     -93.542  56.144 -24.121  1.00 25.34           O
ANISOU 2209  O   SER A 274     2896   1861   4872     70   -193   -286       O
ATOM   2210  CB  SER A 274     -93.308  57.210 -21.008  1.00 32.18           C
ANISOU 2210  CB  SER A 274     3655   2940   5631    144   -278   -233       C
ATOM   2211  OG  SER A 274     -92.056  57.510 -21.595  1.00 45.60           O
ANISOU 2211  OG  SER A 274     5387   4634   7305    152   -269   -260       O
ATOM   2212  N   THR A 275     -95.375  57.257 -23.395  1.00 31.18           N
ANISOU 2212  N   THR A 275     3587   2629   5632     68   -227   -210       N
ATOM   2213  CA  THR A 275     -95.752  57.696 -24.735  1.00 31.93           C
ANISOU 2213  CA  THR A 275     3723   2659   5749     40   -203   -211       C
ATOM   2214  C   THR A 275     -94.682  58.594 -25.342  1.00 30.80           C
ANISOU 2214  C   THR A 275     3619   2530   5554     34   -202   -198       C
ATOM   2215  O   THR A 275     -94.336  58.451 -26.521  1.00 34.01           O
ANISOU 2215  O   THR A 275     4075   2893   5954     21   -175   -224       O
ATOM   2216  CB  THR A 275     -97.100  58.415 -24.687  1.00 35.33           C
ANISOU 2216  CB  THR A 275     4138   3063   6225     30   -229   -171       C
ATOM   2217  OG1 THR A 275     -98.114  57.501 -24.247  1.00 38.43           O
ANISOU 2217  OG1 THR A 275     4496   3432   6675     45   -237   -192       O
ATOM   2218  CG2 THR A 275     -97.472  58.953 -26.060  1.00 36.78           C
ANISOU 2218  CG2 THR A 275     4363   3184   6428      8   -214   -189       C
ATOM   2219  N   VAL A 276     -94.143  59.520 -24.555  1.00 29.47           N
ANISOU 2219  N   VAL A 276     3424   2432   5342     47   -230   -158       N
ATOM   2220  CA  VAL A 276     -93.037  60.375 -24.972  1.00 29.06           C
ANISOU 2220  CA  VAL A 276     3391   2408   5244     52   -238   -154       C
ATOM   2221  C   VAL A 276     -91.786  59.929 -24.230  1.00 26.60           C
ANISOU 2221  C   VAL A 276     3065   2152   4890     94   -246   -187       C
ATOM   2222  O   VAL A 276     -91.787  59.836 -22.997  1.00 27.20           O
ANISOU 2222  O   VAL A 276     3091   2300   4944    116   -259   -181       O
ATOM   2223  CB  VAL A 276     -93.334  61.861 -24.704  1.00 31.08           C
ANISOU 2223  CB  VAL A 276     3612   2708   5489     33   -262    -93       C
ATOM   2224  CG1 VAL A 276     -92.093  62.703 -24.962  1.00 33.54           C
ANISOU 2224  CG1 VAL A 276     3921   3068   5754     48   -274   -100       C
ATOM   2225  CG2 VAL A 276     -94.487  62.334 -25.572  1.00 26.02           C
ANISOU 2225  CG2 VAL A 276     2992   1991   4902     -5   -268    -77       C
ATOM   2226  N   LYS A 277     -90.725  59.649 -24.980  1.00 29.45           N
ANISOU 2226  N   LYS A 277     3472   2477   5239    108   -244   -224       N
ATOM   2227  CA  LYS A 277     -89.444  59.265 -24.408  1.00 32.56           C
ANISOU 2227  CA  LYS A 277     3860   2903   5608    154   -264   -267       C
ATOM   2228  C   LYS A 277     -88.474  60.437 -24.476  1.00 33.25           C
ANISOU 2228  C   LYS A 277     3935   3046   5652    186   -291   -264       C
ATOM   2229  O   LYS A 277     -88.455  61.186 -25.457  1.00 33.17           O
ANISOU 2229  O   LYS A 277     3954   3008   5639    168   -295   -241       O
ATOM   2230  CB  LYS A 277     -88.856  58.056 -25.138  1.00 35.77           C
ANISOU 2230  CB  LYS A 277     4328   3217   6046    150   -255   -307       C
ATOM   2231  CG  LYS A 277     -89.620  56.761 -24.912  1.00 36.53           C
ANISOU 2231  CG  LYS A 277     4414   3272   6191    123   -229   -326       C
ATOM   2232  CD  LYS A 277     -89.582  56.346 -23.449  1.00 35.89           C
ANISOU 2232  CD  LYS A 277     4272   3257   6108    158   -255   -360       C
ATOM   2233  CE  LYS A 277     -88.158  56.097 -22.978  1.00 34.29           C
ANISOU 2233  CE  LYS A 277     4073   3064   5890    208   -294   -416       C
ATOM   2234  NZ  LYS A 277     -88.108  55.732 -21.535  1.00 37.30           N
ANISOU 2234  NZ  LYS A 277     4393   3525   6254    250   -324   -463       N
ATOM   2235  N   ASN A 278     -87.676  60.594 -23.425  1.00 33.32           N
ANISOU 2235  N   ASN A 278     3893   3140   5625    237   -313   -296       N
ATOM   2236  CA  ASN A 278     -86.675  61.649 -23.338  1.00 30.87           C
ANISOU 2236  CA  ASN A 278     3551   2903   5276    279   -338   -308       C
ATOM   2237  C   ASN A 278     -85.294  61.009 -23.319  1.00 32.31           C
ANISOU 2237  C   ASN A 278     3759   3056   5462    345   -374   -386       C
ATOM   2238  O   ASN A 278     -85.014  60.153 -22.472  1.00 27.94           O
ANISOU 2238  O   ASN A 278     3190   2515   4910    377   -383   -438       O
ATOM   2239  CB  ASN A 278     -86.890  62.511 -22.095  1.00 34.91           C
ANISOU 2239  CB  ASN A 278     3967   3561   5735    289   -330   -285       C
ATOM   2240  CG  ASN A 278     -88.173  63.317 -22.161  1.00 46.98           C
ANISOU 2240  CG  ASN A 278     5474   5104   7274    219   -308   -195       C
ATOM   2241  OD1 ASN A 278     -88.628  63.693 -23.242  1.00 49.43           O
ANISOU 2241  OD1 ASN A 278     5824   5335   7622    177   -308   -166       O
ATOM   2242  ND2 ASN A 278     -88.762  63.588 -21.002  1.00 52.59           N
ANISOU 2242  ND2 ASN A 278     6123   5912   7948    208   -294   -151       N
ATOM   2243  N   TYR A 279     -84.438  61.424 -24.249  1.00 36.10           N
ANISOU 2243  N   TYR A 279     4279   3490   5947    367   -404   -395       N
ATOM   2244  CA  TYR A 279     -83.110  60.849 -24.402  1.00 34.81           C
ANISOU 2244  CA  TYR A 279     4155   3269   5803    430   -452   -460       C
ATOM   2245  C   TYR A 279     -82.050  61.938 -24.369  1.00 35.73           C
ANISOU 2245  C   TYR A 279     4228   3456   5893    500   -497   -494       C
ATOM   2246  O   TYR A 279     -82.266  63.048 -24.865  1.00 36.10           O
ANISOU 2246  O   TYR A 279     4252   3545   5920    482   -494   -454       O
ATOM   2247  CB  TYR A 279     -82.982  60.071 -25.718  1.00 32.38           C
ANISOU 2247  CB  TYR A 279     3956   2811   5534    395   -458   -433       C
ATOM   2248  CG  TYR A 279     -83.913  58.889 -25.854  1.00 33.89           C
ANISOU 2248  CG  TYR A 279     4183   2933   5760    328   -411   -410       C
ATOM   2249  CD1 TYR A 279     -83.762  57.765 -25.053  1.00 37.27           C
ANISOU 2249  CD1 TYR A 279     4599   3338   6224    338   -415   -459       C
ATOM   2250  CD2 TYR A 279     -84.927  58.886 -26.802  1.00 32.39           C
ANISOU 2250  CD2 TYR A 279     4032   2704   5570    259   -366   -352       C
ATOM   2251  CE1 TYR A 279     -84.606  56.678 -25.180  1.00 39.21           C
ANISOU 2251  CE1 TYR A 279     4862   3526   6509    276   -374   -444       C
ATOM   2252  CE2 TYR A 279     -85.775  57.803 -26.939  1.00 32.49           C
ANISOU 2252  CE2 TYR A 279     4063   2664   5617    204   -320   -341       C
ATOM   2253  CZ  TYR A 279     -85.610  56.702 -26.126  1.00 37.17           C
ANISOU 2253  CZ  TYR A 279     4636   3238   6251    210   -323   -384       C
ATOM   2254  OH  TYR A 279     -86.452  55.621 -26.257  1.00 43.48           O
ANISOU 2254  OH  TYR A 279     5438   3992   7092    154   -278   -379       O
ATOM   2255  N   PHE A 280     -80.905  61.609 -23.777  1.00 36.16           N
ANISOU 2255  N   PHE A 280     4266   3520   5954    584   -543   -578       N
ATOM   2256  CA  PHE A 280     -79.682  62.388 -23.938  1.00 32.71           C
ANISOU 2256  CA  PHE A 280     3803   3115   5511    669   -602   -631       C
ATOM   2257  C   PHE A 280     -78.964  61.820 -25.157  1.00 32.59           C
ANISOU 2257  C   PHE A 280     3903   2933   5546    679   -657   -621       C
ATOM   2258  O   PHE A 280     -78.455  60.695 -25.118  1.00 36.72           O
ANISOU 2258  O   PHE A 280     4486   3348   6116    696   -688   -655       O
ATOM   2259  CB  PHE A 280     -78.823  62.311 -22.677  1.00 30.14           C
ANISOU 2259  CB  PHE A 280     3399   2885   5169    765   -629   -740       C
ATOM   2260  CG  PHE A 280     -77.742  63.364 -22.590  1.00 33.38           C
ANISOU 2260  CG  PHE A 280     3738   3384   5561    858   -676   -804       C
ATOM   2261  CD1 PHE A 280     -77.145  63.884 -23.728  1.00 38.97           C
ANISOU 2261  CD1 PHE A 280     4491   4018   6298    879   -728   -785       C
ATOM   2262  CD2 PHE A 280     -77.320  63.827 -21.354  1.00 35.19           C
ANISOU 2262  CD2 PHE A 280     3851   3782   5739    931   -667   -887       C
ATOM   2263  CE1 PHE A 280     -76.152  64.844 -23.637  1.00 38.16           C
ANISOU 2263  CE1 PHE A 280     4311   4000   6188    972   -778   -853       C
ATOM   2264  CE2 PHE A 280     -76.328  64.788 -21.256  1.00 36.93           C
ANISOU 2264  CE2 PHE A 280     3988   4097   5946   1023   -705   -958       C
ATOM   2265  CZ  PHE A 280     -75.744  65.296 -22.399  1.00 36.52           C
ANISOU 2265  CZ  PHE A 280     3976   3962   5938   1044   -763   -942       C
ATOM   2266  N   ILE A 281     -78.934  62.589 -26.239  1.00 34.50           N
ANISOU 2266  N   ILE A 281     4178   3153   5778    664   -675   -570       N
ATOM   2267  CA  ILE A 281     -78.455  62.116 -27.531  1.00 35.55           C
ANISOU 2267  CA  ILE A 281     4432   3137   5937    657   -720   -532       C
ATOM   2268  C   ILE A 281     -77.130  62.789 -27.856  1.00 35.19           C
ANISOU 2268  C   ILE A 281     4384   3086   5900    757   -813   -578       C
ATOM   2269  O   ILE A 281     -76.959  63.992 -27.628  1.00 37.05           O
ANISOU 2269  O   ILE A 281     4527   3440   6110    798   -827   -606       O
ATOM   2270  CB  ILE A 281     -79.499  62.375 -28.637  1.00 35.01           C
ANISOU 2270  CB  ILE A 281     4418   3044   5840    566   -676   -442       C
ATOM   2271  CG1 ILE A 281     -78.926  62.035 -30.014  1.00 41.49           C
ANISOU 2271  CG1 ILE A 281     5364   3739   6662    566   -724   -397       C
ATOM   2272  CG2 ILE A 281     -79.992  63.814 -28.584  1.00 38.28           C
ANISOU 2272  CG2 ILE A 281     4744   3581   6219    558   -664   -433       C
ATOM   2273  CD1 ILE A 281     -79.927  62.164 -31.137  1.00 48.34           C
ANISOU 2273  CD1 ILE A 281     6291   4587   7488    484   -680   -323       C
ATOM   2274  N   THR A 282     -76.188  62.003 -28.376  1.00 33.89           N
ANISOU 2274  N   THR A 282     4316   2779   5779    796   -882   -583       N
ATOM   2275  CA  THR A 282     -74.905  62.505 -28.853  1.00 31.45           C
ANISOU 2275  CA  THR A 282     4029   2430   5491    897   -989   -618       C
ATOM   2276  C   THR A 282     -74.644  61.913 -30.229  1.00 35.14           C
ANISOU 2276  C   THR A 282     4649   2737   5966    863  -1030   -528       C
ATOM   2277  O   THR A 282     -74.549  60.690 -30.371  1.00 39.84           O
ANISOU 2277  O   THR A 282     5332   3203   6601    823  -1026   -497       O
ATOM   2278  CB  THR A 282     -73.767  62.143 -27.892  1.00 34.64           C
ANISOU 2278  CB  THR A 282     4392   2819   5950   1008  -1056   -732       C
ATOM   2279  OG1 THR A 282     -74.019  62.720 -26.606  1.00 38.74           O
ANISOU 2279  OG1 THR A 282     4766   3515   6439   1040  -1009   -813       O
ATOM   2280  CG2 THR A 282     -72.440  62.664 -28.423  1.00 32.94           C
ANISOU 2280  CG2 THR A 282     4198   2550   5766   1123  -1179   -771       C
ATOM   2281  N   ASP A 283     -74.536  62.776 -31.237  1.00 31.98           N
ANISOU 2281  N   ASP A 283     4277   2348   5524    874  -1071   -485       N
ATOM   2282  CA  ASP A 283     -74.271  62.324 -32.596  1.00 34.27           C
ANISOU 2282  CA  ASP A 283     4717   2506   5798    846  -1114   -392       C
ATOM   2283  C   ASP A 283     -72.779  62.067 -32.773  1.00 40.19           C
ANISOU 2283  C   ASP A 283     5528   3136   6604    951  -1243   -415       C
ATOM   2284  O   ASP A 283     -71.954  62.949 -32.518  1.00 44.27           O
ANISOU 2284  O   ASP A 283     5976   3705   7139   1062  -1327   -491       O
ATOM   2285  CB  ASP A 283     -74.761  63.358 -33.608  1.00 36.02           C
ANISOU 2285  CB  ASP A 283     4948   2794   5945    823  -1117   -344       C
ATOM   2286  CG  ASP A 283     -74.560  62.908 -35.041  1.00 39.63           C
ANISOU 2286  CG  ASP A 283     5563   3139   6358    793  -1155   -243       C
ATOM   2287  OD1 ASP A 283     -75.273  61.981 -35.480  1.00 40.48           O
ANISOU 2287  OD1 ASP A 283     5749   3193   6440    695  -1077   -171       O
ATOM   2288  OD2 ASP A 283     -73.689  63.481 -35.730  1.00 42.18           O
ANISOU 2288  OD2 ASP A 283     5927   3434   6666    869  -1264   -235       O
ATOM   2289  N   ALA A 284     -72.436  60.856 -33.217  1.00 38.71           N
ANISOU 2289  N   ALA A 284     5468   2788   6454    914  -1260   -350       N
ATOM   2290  CA  ALA A 284     -71.033  60.470 -33.317  1.00 36.99           C
ANISOU 2290  CA  ALA A 284     5318   2425   6311   1007  -1391   -366       C
ATOM   2291  C   ALA A 284     -70.339  61.097 -34.519  1.00 35.78           C
ANISOU 2291  C   ALA A 284     5252   2223   6120   1063  -1498   -303       C
ATOM   2292  O   ALA A 284     -69.130  61.346 -34.467  1.00 45.08           O
ANISOU 2292  O   ALA A 284     6430   3362   7338   1170  -1613   -349       O
ATOM   2293  CB  ALA A 284     -70.911  58.947 -33.380  1.00 38.25           C
ANISOU 2293  CB  ALA A 284     5574   2442   6516    924  -1363   -303       C
ATOM   2294  N   GLN A 285     -71.072  61.360 -35.601  1.00 35.44           N
ANISOU 2294  N   GLN A 285     5273   2215   5979    985  -1452   -203       N
ATOM   2295  CA  GLN A 285     -70.435  61.882 -36.805  1.00 41.62           C
ANISOU 2295  CA  GLN A 285     6152   2952   6711   1035  -1560   -135       C
ATOM   2296  C   GLN A 285     -70.061  63.352 -36.658  1.00 41.71           C
ANISOU 2296  C   GLN A 285     6050   3087   6712   1147  -1638   -229       C
ATOM   2297  O   GLN A 285     -68.959  63.755 -37.044  1.00 45.96           O
ANISOU 2297  O   GLN A 285     6621   3566   7275   1259  -1779   -241       O
ATOM   2298  CB  GLN A 285     -71.353  61.687 -38.013  1.00 41.19           C
ANISOU 2298  CB  GLN A 285     6199   2911   6540    921  -1486    -11       C
ATOM   2299  CG  GLN A 285     -70.728  62.096 -39.338  1.00 48.05           C
ANISOU 2299  CG  GLN A 285     7189   3733   7336    965  -1598     74       C
ATOM   2300  CD  GLN A 285     -69.507  61.265 -39.686  1.00 57.57           C
ANISOU 2300  CD  GLN A 285     8529   4747   8597   1007  -1710    151       C
ATOM   2301  OE1 GLN A 285     -69.618  60.083 -40.013  1.00 59.95           O
ANISOU 2301  OE1 GLN A 285     8939   4939   8900    912  -1659    256       O
ATOM   2302  NE2 GLN A 285     -68.332  61.881 -39.614  1.00 58.58           N
ANISOU 2302  NE2 GLN A 285     8646   4830   8780   1148  -1866     98       N
ATOM   2303  N   THR A 286     -70.959  64.164 -36.103  1.00 43.42           N
ANISOU 2303  N   THR A 286     6128   3470   6899   1117  -1552   -293       N
ATOM   2304  CA  THR A 286     -70.769  65.607 -36.055  1.00 42.26           C
ANISOU 2304  CA  THR A 286     5863   3455   6739   1195  -1608   -369       C
ATOM   2305  C   THR A 286     -70.406  66.141 -34.679  1.00 41.59           C
ANISOU 2305  C   THR A 286     5606   3475   6723   1274  -1605   -505       C
ATOM   2306  O   THR A 286     -69.720  67.161 -34.591  1.00 44.63           O
ANISOU 2306  O   THR A 286     5897   3933   7126   1377  -1690   -581       O
ATOM   2307  CB  THR A 286     -72.037  66.325 -36.534  1.00 38.48           C
ANISOU 2307  CB  THR A 286     5348   3096   6178   1099  -1525   -339       C
ATOM   2308  OG1 THR A 286     -73.097  66.102 -35.597  1.00 36.61           O
ANISOU 2308  OG1 THR A 286     5025   2935   5951   1014  -1388   -362       O
ATOM   2309  CG2 THR A 286     -72.457  65.801 -37.897  1.00 38.91           C
ANISOU 2309  CG2 THR A 286     5568   3072   6146   1025  -1517   -218       C
ATOM   2310  N   GLY A 287     -70.842  65.483 -33.610  1.00 40.26           N
ANISOU 2310  N   GLY A 287     5386   3326   6586   1230  -1509   -540       N
ATOM   2311  CA  GLY A 287     -70.646  65.995 -32.273  1.00 37.20           C
ANISOU 2311  CA  GLY A 287     4831   3068   6235   1294  -1487   -664       C
ATOM   2312  C   GLY A 287     -71.796  66.817 -31.735  1.00 36.58           C
ANISOU 2312  C   GLY A 287     4622   3167   6109   1216  -1373   -674       C
ATOM   2313  O   GLY A 287     -71.701  67.324 -30.610  1.00 36.96           O
ANISOU 2313  O   GLY A 287     4524   3349   6172   1259  -1342   -765       O
ATOM   2314  N   SER A 288     -72.872  66.973 -32.501  1.00 32.90           N
ANISOU 2314  N   SER A 288     4204   2709   5587   1106  -1314   -585       N
ATOM   2315  CA  SER A 288     -74.043  67.686 -32.017  1.00 35.10           C
ANISOU 2315  CA  SER A 288     4373   3130   5836   1022  -1212   -583       C
ATOM   2316  C   SER A 288     -74.773  66.840 -30.980  1.00 36.51           C
ANISOU 2316  C   SER A 288     4529   3322   6021    959  -1105   -583       C
ATOM   2317  O   SER A 288     -74.917  65.625 -31.138  1.00 30.84           O
ANISOU 2317  O   SER A 288     3918   2487   5313    921  -1081   -542       O
ATOM   2318  CB  SER A 288     -74.972  68.022 -33.182  1.00 34.00           C
ANISOU 2318  CB  SER A 288     4300   2974   5643    932  -1194   -500       C
ATOM   2319  OG  SER A 288     -75.842  69.086 -32.849  1.00 43.33           O
ANISOU 2319  OG  SER A 288     5360   4289   6814    876  -1141   -512       O
ATOM   2320  N   SER A 289     -75.230  67.486 -29.908  1.00 35.48           N
ANISOU 2320  N   SER A 289     4255   3342   5886    946  -1041   -625       N
ATOM   2321  CA  SER A 289     -75.836  66.764 -28.799  1.00 35.72           C
ANISOU 2321  CA  SER A 289     4252   3403   5915    904   -953   -634       C
ATOM   2322  C   SER A 289     -76.924  67.618 -28.164  1.00 33.20           C
ANISOU 2322  C   SER A 289     3817   3232   5566    828   -868   -611       C
ATOM   2323  O   SER A 289     -77.010  68.828 -28.391  1.00 34.32           O
ANISOU 2323  O   SER A 289     3878   3463   5699    822   -881   -609       O
ATOM   2324  CB  SER A 289     -74.782  66.362 -27.760  1.00 30.88           C
ANISOU 2324  CB  SER A 289     3588   2813   5332   1011   -989   -737       C
ATOM   2325  OG  SER A 289     -74.122  67.499 -27.236  1.00 31.67           O
ANISOU 2325  OG  SER A 289     3549   3058   5427   1094  -1019   -817       O
ATOM   2326  N   LYS A 290     -77.761  66.966 -27.358  1.00 28.96           N
ANISOU 2326  N   LYS A 290     3272   2714   5019    769   -787   -591       N
ATOM   2327  CA  LYS A 290     -78.835  67.640 -26.637  1.00 31.83           C
ANISOU 2327  CA  LYS A 290     3536   3203   5356    695   -709   -555       C
ATOM   2328  C   LYS A 290     -79.201  66.806 -25.418  1.00 28.28           C
ANISOU 2328  C   LYS A 290     3062   2791   4892    687   -650   -571       C
ATOM   2329  O   LYS A 290     -79.396  65.592 -25.534  1.00 27.86           O
ANISOU 2329  O   LYS A 290     3102   2626   4856    670   -642   -562       O
ATOM   2330  CB  LYS A 290     -80.060  67.853 -27.536  1.00 29.34           C
ANISOU 2330  CB  LYS A 290     3276   2831   5041    588   -678   -468       C
ATOM   2331  CG  LYS A 290     -81.223  68.550 -26.847  1.00 28.97           C
ANISOU 2331  CG  LYS A 290     3138   2885   4984    505   -610   -418       C
ATOM   2332  CD  LYS A 290     -82.174  69.184 -27.853  1.00 31.04           C
ANISOU 2332  CD  LYS A 290     3431   3102   5262    423   -612   -359       C
ATOM   2333  CE  LYS A 290     -82.732  68.158 -28.824  1.00 33.77           C
ANISOU 2333  CE  LYS A 290     3916   3303   5611    388   -606   -330       C
ATOM   2334  NZ  LYS A 290     -83.695  68.767 -29.783  1.00 34.00           N
ANISOU 2334  NZ  LYS A 290     3973   3295   5651    318   -610   -292       N
ATOM   2335  N   CYS A 291     -79.295  67.459 -24.258  1.00 29.34           N
ANISOU 2335  N   CYS A 291     3068   3089   4989    697   -610   -592       N
ATOM   2336  CA  CYS A 291     -79.524  66.737 -23.009  1.00 28.60           C
ANISOU 2336  CA  CYS A 291     2944   3056   4865    706   -565   -619       C
ATOM   2337  C   CYS A 291     -80.900  66.087 -22.983  1.00 27.71           C
ANISOU 2337  C   CYS A 291     2888   2884   4755    606   -510   -535       C
ATOM   2338  O   CYS A 291     -81.042  64.927 -22.581  1.00 34.03           O
ANISOU 2338  O   CYS A 291     3739   3629   5563    611   -503   -556       O
ATOM   2339  CB  CYS A 291     -79.364  67.682 -21.818  1.00 38.02           C
ANISOU 2339  CB  CYS A 291     3986   4462   5999    733   -528   -647       C
ATOM   2340  SG  CYS A 291     -77.695  68.307 -21.576  1.00 45.76           S
ANISOU 2340  SG  CYS A 291     4872   5540   6973    876   -588   -779       S
ATOM   2341  N   VAL A 292     -81.930  66.823 -23.386  1.00 34.99           N
ANISOU 2341  N   VAL A 292     3798   3817   5680    517   -478   -447       N
ATOM   2342  CA  VAL A 292     -83.305  66.341 -23.347  1.00 31.94           C
ANISOU 2342  CA  VAL A 292     3453   3379   5303    429   -432   -372       C
ATOM   2343  C   VAL A 292     -83.858  66.447 -24.760  1.00 36.60           C
ANISOU 2343  C   VAL A 292     4127   3844   5935    372   -446   -326       C
ATOM   2344  O   VAL A 292     -84.245  67.534 -25.208  1.00 40.22           O
ANISOU 2344  O   VAL A 292     4550   4329   6403    329   -450   -286       O
ATOM   2345  CB  VAL A 292     -84.170  67.123 -22.355  1.00 32.79           C
ANISOU 2345  CB  VAL A 292     3465   3618   5376    374   -382   -308       C
ATOM   2346  CG1 VAL A 292     -85.538  66.476 -22.234  1.00 32.58           C
ANISOU 2346  CG1 VAL A 292     3486   3524   5367    303   -350   -241       C
ATOM   2347  CG2 VAL A 292     -83.489  67.200 -21.004  1.00 34.03           C
ANISOU 2347  CG2 VAL A 292     3528   3935   5467    439   -366   -360       C
ATOM   2348  N   CYS A 293     -83.904  65.325 -25.466  1.00 37.31           N
ANISOU 2348  N   CYS A 293     4324   3803   6050    369   -452   -334       N
ATOM   2349  CA  CYS A 293     -84.491  65.256 -26.799  1.00 38.79           C
ANISOU 2349  CA  CYS A 293     4596   3882   6259    318   -456   -296       C
ATOM   2350  C   CYS A 293     -85.772  64.435 -26.692  1.00 36.51           C
ANISOU 2350  C   CYS A 293     4340   3542   5991    256   -405   -260       C
ATOM   2351  O   CYS A 293     -85.726  63.207 -26.586  1.00 30.56           O
ANISOU 2351  O   CYS A 293     3633   2729   5249    262   -390   -279       O
ATOM   2352  CB  CYS A 293     -83.512  64.650 -27.800  1.00 45.54           C
ANISOU 2352  CB  CYS A 293     5547   4639   7118    361   -499   -325       C
ATOM   2353  SG  CYS A 293     -84.007  64.862 -29.523  1.00 54.38           S
ANISOU 2353  SG  CYS A 293     6764   5668   8232    313   -512   -285       S
ATOM   2354  N   SER A 294     -86.912  65.121 -26.705  1.00 38.23           N
ANISOU 2354  N   SER A 294     4526   3778   6221    196   -386   -211       N
ATOM   2355  CA  SER A 294     -88.201  64.447 -26.624  1.00 35.11           C
ANISOU 2355  CA  SER A 294     4155   3333   5854    145   -348   -182       C
ATOM   2356  C   SER A 294     -88.506  63.759 -27.949  1.00 31.85           C
ANISOU 2356  C   SER A 294     3836   2809   5455    125   -340   -193       C
ATOM   2357  O   SER A 294     -88.527  64.403 -29.003  1.00 33.83           O
ANISOU 2357  O   SER A 294     4121   3032   5700    113   -362   -191       O
ATOM   2358  CB  SER A 294     -89.299  65.446 -26.270  1.00 37.29           C
ANISOU 2358  CB  SER A 294     4372   3646   6151     91   -343   -126       C
ATOM   2359  OG  SER A 294     -89.066  66.032 -25.001  1.00 39.28           O
ANISOU 2359  OG  SER A 294     4534   4015   6376     99   -338   -101       O
ATOM   2360  N   VAL A 295     -88.737  62.451 -27.894  1.00 31.83           N
ANISOU 2360  N   VAL A 295     3872   2755   5468    122   -309   -208       N
ATOM   2361  CA  VAL A 295     -88.977  61.639 -29.080  1.00 32.59           C
ANISOU 2361  CA  VAL A 295     4050   2764   5567     99   -285   -216       C
ATOM   2362  C   VAL A 295     -90.296  60.903 -28.907  1.00 31.48           C
ANISOU 2362  C   VAL A 295     3899   2596   5466     62   -241   -214       C
ATOM   2363  O   VAL A 295     -90.606  60.410 -27.816  1.00 30.70           O
ANISOU 2363  O   VAL A 295     3751   2523   5390     67   -232   -215       O
ATOM   2364  CB  VAL A 295     -87.822  60.645 -29.329  1.00 33.14           C
ANISOU 2364  CB  VAL A 295     4177   2789   5627    126   -290   -237       C
ATOM   2365  CG1 VAL A 295     -88.070  59.835 -30.593  1.00 32.54           C
ANISOU 2365  CG1 VAL A 295     4185   2638   5543     90   -255   -229       C
ATOM   2366  CG2 VAL A 295     -86.495  61.383 -29.416  1.00 30.99           C
ANISOU 2366  CG2 VAL A 295     3909   2539   5326    178   -347   -247       C
ATOM   2367  N   ILE A 296     -91.076  60.836 -29.982  1.00 29.63           N
ANISOU 2367  N   ILE A 296     3707   2316   5235     32   -219   -218       N
ATOM   2368  CA  ILE A 296     -92.336  60.106 -29.997  1.00 32.17           C
ANISOU 2368  CA  ILE A 296     4017   2608   5599      6   -179   -231       C
ATOM   2369  C   ILE A 296     -92.403  59.306 -31.292  1.00 32.85           C
ANISOU 2369  C   ILE A 296     4170   2649   5662    -12   -134   -254       C
ATOM   2370  O   ILE A 296     -91.918  59.754 -32.336  1.00 33.54           O
ANISOU 2370  O   ILE A 296     4316   2729   5699    -11   -145   -253       O
ATOM   2371  CB  ILE A 296     -93.545  61.057 -29.849  1.00 31.74           C
ANISOU 2371  CB  ILE A 296     3924   2555   5582     -9   -200   -219       C
ATOM   2372  CG1 ILE A 296     -94.836  60.266 -29.644  1.00 28.38           C
ANISOU 2372  CG1 ILE A 296     3474   2097   5212    -19   -172   -238       C
ATOM   2373  CG2 ILE A 296     -93.662  61.986 -31.050  1.00 29.48           C
ANISOU 2373  CG2 ILE A 296     3678   2248   5274    -18   -222   -231       C
ATOM   2374  CD1 ILE A 296     -96.028  61.133 -29.333  1.00 24.79           C
ANISOU 2374  CD1 ILE A 296     2983   1625   4812    -30   -207   -219       C
ATOM   2375  N   ASP A 297     -92.982  58.107 -31.218  1.00 31.03           N
ANISOU 2375  N   ASP A 297     3927   2398   5465    -29    -84   -275       N
ATOM   2376  CA  ASP A 297     -93.084  57.226 -32.380  1.00 32.21           C
ANISOU 2376  CA  ASP A 297     4127   2524   5589    -56    -25   -293       C
ATOM   2377  C   ASP A 297     -94.519  57.262 -32.896  1.00 35.77           C
ANISOU 2377  C   ASP A 297     4556   2973   6063    -63      5   -334       C
ATOM   2378  O   ASP A 297     -95.334  56.380 -32.629  1.00 37.89           O
ANISOU 2378  O   ASP A 297     4778   3237   6382    -71     44   -364       O
ATOM   2379  CB  ASP A 297     -92.647  55.809 -32.030  1.00 30.89           C
ANISOU 2379  CB  ASP A 297     3950   2339   5449    -77     15   -294       C
ATOM   2380  CG  ASP A 297     -92.690  54.876 -33.226  1.00 36.76           C
ANISOU 2380  CG  ASP A 297     4739   3067   6161   -118     88   -296       C
ATOM   2381  OD1 ASP A 297     -92.768  55.368 -34.373  1.00 37.29           O
ANISOU 2381  OD1 ASP A 297     4863   3144   6161   -122    101   -293       O
ATOM   2382  OD2 ASP A 297     -92.648  53.647 -33.019  1.00 43.34           O
ANISOU 2382  OD2 ASP A 297     5549   3886   7034   -150    132   -302       O
ATOM   2383  N   LEU A 298     -94.821  58.307 -33.655  1.00 32.85           N
ANISOU 2383  N   LEU A 298     4216   2604   5661    -55    -23   -345       N
ATOM   2384  CA  LEU A 298     -96.094  58.427 -34.344  1.00 29.92           C
ANISOU 2384  CA  LEU A 298     3837   2226   5307    -52     -5   -401       C
ATOM   2385  C   LEU A 298     -95.944  57.967 -35.786  1.00 32.82           C
ANISOU 2385  C   LEU A 298     4269   2612   5590    -64     52   -429       C
ATOM   2386  O   LEU A 298     -94.867  58.070 -36.380  1.00 35.79           O
ANISOU 2386  O   LEU A 298     4711   2999   5888    -71     48   -392       O
ATOM   2387  CB  LEU A 298     -96.604  59.869 -34.317  1.00 29.61           C
ANISOU 2387  CB  LEU A 298     3788   2171   5293    -38    -77   -407       C
ATOM   2388  CG  LEU A 298     -97.122  60.429 -32.993  1.00 31.08           C
ANISOU 2388  CG  LEU A 298     3906   2340   5562    -35   -128   -374       C
ATOM   2389  CD1 LEU A 298     -97.368  61.924 -33.117  1.00 29.35           C
ANISOU 2389  CD1 LEU A 298     3686   2104   5362    -39   -199   -365       C
ATOM   2390  CD2 LEU A 298     -98.394  59.710 -32.571  1.00 31.49           C
ANISOU 2390  CD2 LEU A 298     3908   2365   5692    -26   -109   -409       C
ATOM   2391  N   LEU A 299     -97.033  57.446 -36.343  1.00 35.04           N
ANISOU 2391  N   LEU A 299     4527   2902   5883    -62    103   -494       N
ATOM   2392  CA  LEU A 299     -97.086  57.232 -37.780  1.00 33.22           C
ANISOU 2392  CA  LEU A 299     4356   2712   5557    -68    156   -531       C
ATOM   2393  C   LEU A 299     -96.893  58.569 -38.479  1.00 35.85           C
ANISOU 2393  C   LEU A 299     4745   3044   5833    -46     85   -543       C
ATOM   2394  O   LEU A 299     -97.490  59.576 -38.087  1.00 38.73           O
ANISOU 2394  O   LEU A 299     5078   3375   6262    -26     14   -569       O
ATOM   2395  CB  LEU A 299     -98.419  56.602 -38.180  1.00 30.73           C
ANISOU 2395  CB  LEU A 299     3989   2416   5271    -56    215   -621       C
ATOM   2396  CG  LEU A 299     -98.574  56.245 -39.659  1.00 31.71           C
ANISOU 2396  CG  LEU A 299     4161   2608   5282    -59    289   -672       C
ATOM   2397  CD1 LEU A 299     -97.647  55.101 -40.031  1.00 29.95           C
ANISOU 2397  CD1 LEU A 299     3970   2424   4984   -113    376   -604       C
ATOM   2398  CD2 LEU A 299    -100.016  55.897 -39.985  1.00 32.77           C
ANISOU 2398  CD2 LEU A 299     4230   2763   5457    -27    329   -788       C
ATOM   2399  N   LEU A 300     -96.036  58.584 -39.502  1.00 37.77           N
ANISOU 2399  N   LEU A 300     5070   3322   5959    -54     98   -518       N
ATOM   2400  CA  LEU A 300     -95.689  59.844 -40.152  1.00 37.87           C
ANISOU 2400  CA  LEU A 300     5136   3340   5913    -32     19   -528       C
ATOM   2401  C   LEU A 300     -96.927  60.547 -40.694  1.00 38.96           C
ANISOU 2401  C   LEU A 300     5255   3476   6070     -4    -10   -630       C
ATOM   2402  O   LEU A 300     -97.036  61.776 -40.616  1.00 40.91           O
ANISOU 2402  O   LEU A 300     5498   3695   6353     11   -100   -649       O
ATOM   2403  CB  LEU A 300     -94.676  59.597 -41.268  1.00 37.21           C
ANISOU 2403  CB  LEU A 300     5150   3299   5688    -39     40   -486       C
ATOM   2404  CG  LEU A 300     -94.055  60.847 -41.890  1.00 35.17           C
ANISOU 2404  CG  LEU A 300     4949   3048   5364    -12    -56   -485       C
ATOM   2405  CD1 LEU A 300     -93.384  61.691 -40.820  1.00 32.46           C
ANISOU 2405  CD1 LEU A 300     4566   2661   5105     -3   -141   -440       C
ATOM   2406  CD2 LEU A 300     -93.063  60.461 -42.972  1.00 38.21           C
ANISOU 2406  CD2 LEU A 300     5440   3475   5604    -16    -38   -431       C
ATOM   2407  N   ASP A 301     -97.878  59.781 -41.234  1.00 36.60           N
ANISOU 2407  N   ASP A 301     4940   3209   5758      3     64   -705       N
ATOM   2408  CA  ASP A 301     -99.116  60.376 -41.723  1.00 36.35           C
ANISOU 2408  CA  ASP A 301     4887   3168   5758     40     31   -822       C
ATOM   2409  C   ASP A 301     -99.891  61.037 -40.591  1.00 35.65           C
ANISOU 2409  C   ASP A 301     4724   2991   5830     49    -43   -831       C
ATOM   2410  O   ASP A 301    -100.490  62.103 -40.777  1.00 39.93           O
ANISOU 2410  O   ASP A 301     5262   3489   6420     69   -126   -889       O
ATOM   2411  CB  ASP A 301     -99.972  59.310 -42.407  1.00 42.29           C
ANISOU 2411  CB  ASP A 301     5618   3978   6471     53    134   -906       C
ATOM   2412  CG  ASP A 301     -99.176  58.459 -43.375  1.00 49.11           C
ANISOU 2412  CG  ASP A 301     6548   4936   7176     26    228   -866       C
ATOM   2413  OD1 ASP A 301     -98.203  57.808 -42.936  1.00 50.67           O
ANISOU 2413  OD1 ASP A 301     6760   5131   7362    -18    264   -757       O
ATOM   2414  OD2 ASP A 301     -99.525  58.435 -44.574  1.00 51.30           O
ANISOU 2414  OD2 ASP A 301     6863   5290   7340     48    264   -944       O
ATOM   2415  N   ASP A 302     -99.890  60.418 -39.408  1.00 33.15           N
ANISOU 2415  N   ASP A 302     4351   2648   5598     31    -20   -770       N
ATOM   2416  CA  ASP A 302    -100.596  60.998 -38.271  1.00 35.07           C
ANISOU 2416  CA  ASP A 302     4530   2814   5980     36    -90   -757       C
ATOM   2417  C   ASP A 302     -99.940  62.294 -37.817  1.00 33.12           C
ANISOU 2417  C   ASP A 302     4294   2539   5751     18   -180   -691       C
ATOM   2418  O   ASP A 302    -100.632  63.269 -37.503  1.00 31.37           O
ANISOU 2418  O   ASP A 302     4044   2256   5619     18   -258   -705       O
ATOM   2419  CB  ASP A 302    -100.654  59.995 -37.119  1.00 36.81           C
ANISOU 2419  CB  ASP A 302     4692   3029   6264     25    -47   -706       C
ATOM   2420  CG  ASP A 302    -101.641  58.874 -37.372  1.00 41.33           C
ANISOU 2420  CG  ASP A 302     5220   3617   6866     48     23   -786       C
ATOM   2421  OD1 ASP A 302    -102.442  58.988 -38.324  1.00 44.39           O
ANISOU 2421  OD1 ASP A 302     5615   4012   7239     79     31   -889       O
ATOM   2422  OD2 ASP A 302    -101.615  57.877 -36.619  1.00 42.55           O
ANISOU 2422  OD2 ASP A 302     5327   3782   7059     38     67   -757       O
ATOM   2423  N   PHE A 303     -98.606  62.325 -37.775  1.00 32.71           N
ANISOU 2423  N   PHE A 303     4278   2528   5624      0   -172   -618       N
ATOM   2424  CA  PHE A 303     -97.915  63.547 -37.376  1.00 35.68           C
ANISOU 2424  CA  PHE A 303     4650   2894   6012    -14   -252   -564       C
ATOM   2425  C   PHE A 303     -98.155  64.667 -38.379  1.00 35.35           C
ANISOU 2425  C   PHE A 303     4640   2841   5951     -5   -321   -627       C
ATOM   2426  O   PHE A 303     -98.265  65.838 -37.995  1.00 36.83           O
ANISOU 2426  O   PHE A 303     4794   2994   6206    -22   -401   -612       O
ATOM   2427  CB  PHE A 303     -96.419  63.281 -37.217  1.00 39.01           C
ANISOU 2427  CB  PHE A 303     5103   3361   6358    -20   -235   -491       C
ATOM   2428  CG  PHE A 303     -95.624  64.504 -36.862  1.00 41.02           C
ANISOU 2428  CG  PHE A 303     5343   3623   6619    -24   -312   -448       C
ATOM   2429  CD1 PHE A 303     -95.648  65.010 -35.573  1.00 39.09           C
ANISOU 2429  CD1 PHE A 303     5026   3370   6454    -41   -341   -394       C
ATOM   2430  CD2 PHE A 303     -94.858  65.152 -37.817  1.00 41.08           C
ANISOU 2430  CD2 PHE A 303     5403   3656   6550    -12   -356   -461       C
ATOM   2431  CE1 PHE A 303     -94.923  66.137 -35.242  1.00 37.59           C
ANISOU 2431  CE1 PHE A 303     4808   3205   6271    -48   -401   -357       C
ATOM   2432  CE2 PHE A 303     -94.129  66.280 -37.493  1.00 39.58           C
ANISOU 2432  CE2 PHE A 303     5184   3480   6374    -14   -428   -430       C
ATOM   2433  CZ  PHE A 303     -94.161  66.773 -36.204  1.00 41.46           C
ANISOU 2433  CZ  PHE A 303     5340   3717   6696    -34   -445   -380       C
ATOM   2434  N   VAL A 304     -98.240  64.330 -39.667  1.00 37.01           N
ANISOU 2434  N   VAL A 304     4911   3087   6066     17   -293   -699       N
ATOM   2435  CA  VAL A 304     -98.546  65.336 -40.679  1.00 35.37           C
ANISOU 2435  CA  VAL A 304     4733   2873   5831     34   -365   -780       C
ATOM   2436  C   VAL A 304     -99.947  65.893 -40.466  1.00 36.16           C
ANISOU 2436  C   VAL A 304     4785   2894   6061     39   -418   -854       C
ATOM   2437  O   VAL A 304    -100.170  67.106 -40.566  1.00 41.85           O
ANISOU 2437  O   VAL A 304     5492   3569   6841     28   -514   -881       O
ATOM   2438  CB  VAL A 304     -98.378  64.744 -42.090  1.00 34.16           C
ANISOU 2438  CB  VAL A 304     4659   2792   5528     61   -314   -843       C
ATOM   2439  CG1 VAL A 304     -98.935  65.694 -43.137  1.00 34.18           C
ANISOU 2439  CG1 VAL A 304     4689   2793   5507     89   -391   -956       C
ATOM   2440  CG2 VAL A 304     -96.914  64.451 -42.365  1.00 31.18           C
ANISOU 2440  CG2 VAL A 304     4343   2472   5033     54   -293   -756       C
ATOM   2441  N   GLU A 305    -100.909  65.019 -40.159  1.00 36.21           N
ANISOU 2441  N   GLU A 305     4759   2877   6123     54   -364   -890       N
ATOM   2442  CA  GLU A 305    -102.275  65.476 -39.918  1.00 38.76           C
ANISOU 2442  CA  GLU A 305     5037   3107   6582     68   -424   -959       C
ATOM   2443  C   GLU A 305    -102.338  66.426 -38.729  1.00 37.08           C
ANISOU 2443  C   GLU A 305     4773   2817   6498     24   -503   -867       C
ATOM   2444  O   GLU A 305    -103.098  67.400 -38.743  1.00 39.54           O
ANISOU 2444  O   GLU A 305     5065   3043   6914     16   -594   -905       O
ATOM   2445  CB  GLU A 305    -103.198  64.278 -39.692  1.00 39.59           C
ANISOU 2445  CB  GLU A 305     5107   3206   6727     99   -352  -1005       C
ATOM   2446  CG  GLU A 305    -104.668  64.650 -39.556  1.00 42.15           C
ANISOU 2446  CG  GLU A 305     5392   3427   7196    130   -421  -1092       C
ATOM   2447  CD  GLU A 305    -105.541  63.471 -39.170  1.00 43.73           C
ANISOU 2447  CD  GLU A 305     5544   3622   7451    167   -360  -1130       C
ATOM   2448  OE1 GLU A 305    -105.286  62.860 -38.111  1.00 44.50           O
ANISOU 2448  OE1 GLU A 305     5605   3724   7578    146   -325  -1031       O
ATOM   2449  OE2 GLU A 305    -106.481  63.153 -39.928  1.00 47.48           O
ANISOU 2449  OE2 GLU A 305     6010   4092   7937    223   -351  -1269       O
ATOM   2450  N   ILE A 306    -101.539  66.161 -37.694  1.00 35.57           N
ANISOU 2450  N   ILE A 306     4558   2658   6300     -6   -470   -746       N
ATOM   2451  CA  ILE A 306    -101.558  67.004 -36.503  1.00 28.66           C
ANISOU 2451  CA  ILE A 306     3629   1736   5526    -50   -528   -648       C
ATOM   2452  C   ILE A 306    -100.989  68.382 -36.815  1.00 31.04           C
ANISOU 2452  C   ILE A 306     3930   2036   5827    -84   -606   -634       C
ATOM   2453  O   ILE A 306    -101.613  69.409 -36.526  1.00 34.46           O
ANISOU 2453  O   ILE A 306     4328   2393   6371   -119   -687   -624       O
ATOM   2454  CB  ILE A 306    -100.787  66.327 -35.356  1.00 35.97           C
ANISOU 2454  CB  ILE A 306     4527   2716   6423    -64   -470   -540       C
ATOM   2455  CG1 ILE A 306    -101.466  65.017 -34.950  1.00 30.02           C
ANISOU 2455  CG1 ILE A 306     3757   1955   5692    -35   -408   -556       C
ATOM   2456  CG2 ILE A 306    -100.668  67.269 -34.166  1.00 31.88           C
ANISOU 2456  CG2 ILE A 306     3954   2182   5978   -111   -522   -434       C
ATOM   2457  CD1 ILE A 306    -100.678  64.214 -33.933  1.00 26.70           C
ANISOU 2457  CD1 ILE A 306     3315   1593   5236    -42   -353   -472       C
ATOM   2458  N   ILE A 307     -99.797  68.424 -37.414  1.00 28.72           N
ANISOU 2458  N   ILE A 307     3674   1823   5416    -76   -589   -632       N
ATOM   2459  CA  ILE A 307     -99.125  69.700 -37.632  1.00 31.76           C
ANISOU 2459  CA  ILE A 307     4046   2221   5800   -103   -664   -617       C
ATOM   2460  C   ILE A 307     -99.845  70.525 -38.692  1.00 36.25           C
ANISOU 2460  C   ILE A 307     4635   2735   6405    -98   -747   -727       C
ATOM   2461  O   ILE A 307     -99.775  71.761 -38.679  1.00 38.91           O
ANISOU 2461  O   ILE A 307     4935   3043   6806   -137   -833   -722       O
ATOM   2462  CB  ILE A 307     -97.644  69.463 -37.989  1.00 33.01           C
ANISOU 2462  CB  ILE A 307     4241   2474   5827    -82   -635   -588       C
ATOM   2463  CG1 ILE A 307     -96.847  70.764 -37.874  1.00 33.09           C
ANISOU 2463  CG1 ILE A 307     4210   2509   5853   -110   -711   -555       C
ATOM   2464  CG2 ILE A 307     -97.508  68.865 -39.383  1.00 29.01           C
ANISOU 2464  CG2 ILE A 307     3821   2001   5199    -37   -611   -673       C
ATOM   2465  CD1 ILE A 307     -95.354  70.582 -38.039  1.00 37.36           C
ANISOU 2465  CD1 ILE A 307     4776   3134   6285    -81   -696   -520       C
ATOM   2466  N   LYS A 308    -100.558  69.874 -39.613  1.00 36.59           N
ANISOU 2466  N   LYS A 308     4728   2766   6408    -52   -725   -836       N
ATOM   2467  CA  LYS A 308    -101.350  70.605 -40.593  1.00 35.71           C
ANISOU 2467  CA  LYS A 308     4635   2600   6334    -36   -808   -963       C
ATOM   2468  C   LYS A 308    -102.697  71.056 -40.048  1.00 35.26           C
ANISOU 2468  C   LYS A 308     4530   2412   6455    -57   -871   -986       C
ATOM   2469  O   LYS A 308    -103.430  71.758 -40.753  1.00 39.91           O
ANISOU 2469  O   LYS A 308     5126   2931   7106    -48   -958  -1096       O
ATOM   2470  CB  LYS A 308    -101.573  69.753 -41.844  1.00 38.51           C
ANISOU 2470  CB  LYS A 308     5059   3011   6562     29   -757  -1083       C
ATOM   2471  CG  LYS A 308    -100.352  69.614 -42.734  1.00 44.39           C
ANISOU 2471  CG  LYS A 308     5869   3867   7129     49   -734  -1078       C
ATOM   2472  CD  LYS A 308    -100.698  68.875 -44.015  1.00 50.35           C
ANISOU 2472  CD  LYS A 308     6692   4686   7751    107   -685  -1195       C
ATOM   2473  CE  LYS A 308     -99.526  68.864 -44.981  1.00 55.05           C
ANISOU 2473  CE  LYS A 308     7364   5386   8166    125   -681  -1183       C
ATOM   2474  NZ  LYS A 308     -99.848  68.129 -46.236  1.00 61.54           N
ANISOU 2474  NZ  LYS A 308     8254   6291   8836    176   -623  -1285       N
ATOM   2475  N   SER A 309    -103.039  70.677 -38.817  1.00 32.35           N
ANISOU 2475  N   SER A 309     4116   2004   6171    -82   -838   -886       N
ATOM   2476  CA  SER A 309    -104.324  71.009 -38.222  1.00 32.41           C
ANISOU 2476  CA  SER A 309     4084   1894   6334    -98   -895   -881       C
ATOM   2477  C   SER A 309    -104.220  72.125 -37.190  1.00 36.55           C
ANISOU 2477  C   SER A 309     4547   2394   6945   -180   -950   -743       C
ATOM   2478  O   SER A 309    -105.141  72.306 -36.386  1.00 37.08           O
ANISOU 2478  O   SER A 309     4578   2418   7093   -199   -970   -674       O
ATOM   2479  CB  SER A 309    -104.942  69.762 -37.588  1.00 39.54           C
ANISOU 2479  CB  SER A 309     4977   2807   7238    -60   -817   -856       C
ATOM   2480  OG  SER A 309    -105.047  68.710 -38.531  1.00 39.77           O
ANISOU 2480  OG  SER A 309     5050   2866   7194      8   -755   -983       O
ATOM   2481  N   GLN A 310    -103.126  72.880 -37.198  1.00 38.75           N
ANISOU 2481  N   GLN A 310     4766   3076   6880    379   -561  -1731       N
ATOM   2482  CA  GLN A 310    -102.878  73.900 -36.192  1.00 34.64           C
ANISOU 2482  CA  GLN A 310     4135   2330   6698    253   -617  -1552       C
ATOM   2483  C   GLN A 310    -102.894  75.290 -36.814  1.00 37.86           C
ANISOU 2483  C   GLN A 310     4484   2644   7260    190   -863  -1697       C
ATOM   2484  O   GLN A 310    -102.707  75.462 -38.022  1.00 39.39           O
ANISOU 2484  O   GLN A 310     4741   2936   7288    233  -1022  -1954       O
ATOM   2485  CB  GLN A 310    -101.536  73.661 -35.491  1.00 32.41           C
ANISOU 2485  CB  GLN A 310     3812   2147   6354    190   -503  -1267       C
ATOM   2486  CG  GLN A 310    -101.351  72.246 -34.970  1.00 34.28           C
ANISOU 2486  CG  GLN A 310     4105   2519   6401    237   -291  -1121       C
ATOM   2487  CD  GLN A 310    -102.444  71.827 -34.005  1.00 36.16           C
ANISOU 2487  CD  GLN A 310     4326   2640   6774    240   -185  -1065       C
ATOM   2488  OE1 GLN A 310    -102.937  72.634 -33.216  1.00 36.68           O
ANISOU 2488  OE1 GLN A 310     4301   2615   7021    158   -218   -953       O
ATOM   2489  NE2 GLN A 310    -102.834  70.559 -34.069  1.00 32.52           N
ANISOU 2489  NE2 GLN A 310     3926   2284   6147    317    -63  -1062       N
ATOM   2490  N   ASP A 311    -103.124  76.285 -35.962  1.00 40.98           N
ANISOU 2490  N   ASP A 311     4738   2899   7933     82   -900  -1507       N
ATOM   2491  CA  ASP A 311    -103.064  77.685 -36.359  1.00 47.74           C
ANISOU 2491  CA  ASP A 311     5490   3642   9006      2  -1132  -1572       C
ATOM   2492  C   ASP A 311    -101.643  78.196 -36.159  1.00 45.99           C
ANISOU 2492  C   ASP A 311     5178   3446   8848    -84  -1162  -1408       C
ATOM   2493  O   ASP A 311    -101.057  78.017 -35.086  1.00 37.53           O
ANISOU 2493  O   ASP A 311     4029   2400   7830   -126   -982  -1148       O
ATOM   2494  CB  ASP A 311    -104.062  78.515 -35.549  1.00 41.40           C
ANISOU 2494  CB  ASP A 311     4543   2663   8524    -67  -1169  -1426       C
ATOM   2495  CG  ASP A 311    -104.096  79.972 -35.971  1.00 44.38           C
ANISOU 2495  CG  ASP A 311     4793   2900   9170   -145  -1422  -1485       C
ATOM   2496  OD1 ASP A 311    -103.098  80.687 -35.750  1.00 60.34           O
ANISOU 2496  OD1 ASP A 311     6703   4929  11296   -236  -1466  -1330       O
ATOM   2497  OD2 ASP A 311    -105.125  80.404 -36.530  1.00 61.76           O
ANISOU 2497  OD2 ASP A 311     6989   4976  11501   -110  -1582  -1692       O
ATOM   2498  N   LEU A 312    -101.092  78.836 -37.191  1.00 48.66           N
ANISOU 2498  N   LEU A 312     5513   3792   9186   -108  -1400  -1579       N
ATOM   2499  CA  LEU A 312     -99.695  79.250 -37.205  1.00 46.58           C
ANISOU 2499  CA  LEU A 312     5146   3590   8963   -171  -1452  -1420       C
ATOM   2500  C   LEU A 312     -99.537  80.769 -37.171  1.00 49.73           C
ANISOU 2500  C   LEU A 312     5345   3844   9708   -294  -1663  -1365       C
ATOM   2501  O   LEU A 312     -98.560  81.306 -37.696  1.00 55.96           O
ANISOU 2501  O   LEU A 312     6045   4687  10530   -340  -1829  -1337       O
ATOM   2502  CB  LEU A 312     -98.985  78.677 -38.431  1.00 45.21           C
ANISOU 2502  CB  LEU A 312     5091   3696   8389    -95  -1537  -1508       C
ATOM   2503  CG  LEU A 312     -99.213  77.197 -38.742  1.00 43.40           C
ANISOU 2503  CG  LEU A 312     5043   3681   7767     27  -1352  -1548       C
ATOM   2504  CD1 LEU A 312     -98.443  76.793 -39.990  1.00 43.84           C
ANISOU 2504  CD1 LEU A 312     5167   4047   7444     64  -1466  -1550       C
ATOM   2505  CD2 LEU A 312     -98.825  76.321 -37.561  1.00 40.67           C
ANISOU 2505  CD2 LEU A 312     4683   3326   7445     48  -1062  -1293       C
ATOM   2506  N   SER A 313    -100.483  81.473 -36.552  1.00 53.11           N
ANISOU 2506  N   SER A 313     5678   4147  10356   -332  -1648  -1282       N
ATOM   2507  CA  SER A 313    -100.458  82.929 -36.503  1.00 57.28           C
ANISOU 2507  CA  SER A 313     6005   4552  11206   -433  -1833  -1189       C
ATOM   2508  C   SER A 313     -99.943  83.469 -35.174  1.00 58.69           C
ANISOU 2508  C   SER A 313     5955   4716  11627   -519  -1657   -825       C
ATOM   2509  O   SER A 313    -100.011  84.680 -34.943  1.00 61.53           O
ANISOU 2509  O   SER A 313     6122   4975  12282   -606  -1771   -686       O
ATOM   2510  CB  SER A 313    -101.853  83.489 -36.786  1.00 59.71           C
ANISOU 2510  CB  SER A 313     6325   4699  11664   -425  -1984  -1339       C
ATOM   2511  OG  SER A 313    -102.772  83.098 -35.782  1.00 61.98           O
ANISOU 2511  OG  SER A 313     6597   4924  12029   -411  -1798  -1184       O
ATOM   2512  N   VAL A 314     -99.428  82.607 -34.302  1.00 57.75           N
ANISOU 2512  N   VAL A 314     5847   4708  11387   -495  -1381   -677       N
ATOM   2513  CA  VAL A 314     -98.960  83.000 -32.979  1.00 62.39           C
ANISOU 2513  CA  VAL A 314     6218   5338  12151   -571  -1173   -370       C
ATOM   2514  C   VAL A 314     -97.507  82.571 -32.830  1.00 57.24           C
ANISOU 2514  C   VAL A 314     5498   4810  11441   -546  -1035   -339       C
ATOM   2515  O   VAL A 314     -97.103  81.525 -33.351  1.00 57.14           O
ANISOU 2515  O   VAL A 314     5674   4876  11161   -439  -1001   -481       O
ATOM   2516  CB  VAL A 314     -99.845  82.392 -31.869  1.00 74.74           C
ANISOU 2516  CB  VAL A 314     7821   6919  13656   -578   -961   -225       C
ATOM   2517  CG1 VAL A 314     -99.207  82.553 -30.496  1.00 80.57           C
ANISOU 2517  CG1 VAL A 314     8352   7789  14473   -659   -703     65       C
ATOM   2518  CG2 VAL A 314    -101.223  83.039 -31.886  1.00 79.62           C
ANISOU 2518  CG2 VAL A 314     8417   7377  14458   -613  -1120   -193       C
ATOM   2519  N   VAL A 315     -96.720  83.394 -32.131  1.00 53.54           N
ANISOU 2519  N   VAL A 315     4748   4403  11192   -612   -944   -137       N
ATOM   2520  CA  VAL A 315     -95.302  83.101 -31.930  1.00 56.10           C
ANISOU 2520  CA  VAL A 315     4974   4898  11441   -521   -788   -115       C
ATOM   2521  C   VAL A 315     -95.125  81.738 -31.268  1.00 51.08           C
ANISOU 2521  C   VAL A 315     4514   4417  10477   -399   -511   -156       C
ATOM   2522  O   VAL A 315     -94.416  80.866 -31.782  1.00 51.17           O
ANISOU 2522  O   VAL A 315     4665   4480  10296   -275   -506   -271       O
ATOM   2523  CB  VAL A 315     -94.632  84.215 -31.106  1.00 63.13           C
ANISOU 2523  CB  VAL A 315     5491   5874  12621   -594   -674     99       C
ATOM   2524  CG1 VAL A 315     -93.187  83.852 -30.803  1.00 65.27           C
ANISOU 2524  CG1 VAL A 315     5657   6323  12818   -444   -482     71       C
ATOM   2525  CG2 VAL A 315     -94.709  85.540 -31.848  1.00 68.07           C
ANISOU 2525  CG2 VAL A 315     5994   6366  13502   -672   -968    149       C
ATOM   2526  N   SER A 316     -95.765  81.535 -30.118  1.00 46.71           N
ANISOU 2526  N   SER A 316     3939   3940   9868   -449   -299    -35       N
ATOM   2527  CA  SER A 316     -95.643  80.269 -29.410  1.00 45.97           C
ANISOU 2527  CA  SER A 316     3997   4001   9468   -354    -61    -81       C
ATOM   2528  C   SER A 316     -96.901  80.012 -28.597  1.00 49.00           C
ANISOU 2528  C   SER A 316     4437   4394   9787   -441     24     47       C
ATOM   2529  O   SER A 316     -97.518  80.941 -28.069  1.00 55.48           O
ANISOU 2529  O   SER A 316     5075   5184  10820   -581      8    257       O
ATOM   2530  CB  SER A 316     -94.423  80.247 -28.485  1.00 49.57           C
ANISOU 2530  CB  SER A 316     4271   4678   9885   -281    189    -68       C
ATOM   2531  OG  SER A 316     -94.671  80.984 -27.301  1.00 53.67           O
ANISOU 2531  OG  SER A 316     4556   5371  10464   -386    370    131       O
ATOM   2532  N   LYS A 317     -97.272  78.738 -28.503  1.00 44.19           N
ANISOU 2532  N   LYS A 317     4056   3820   8916   -367     97    -42       N
ATOM   2533  CA  LYS A 317     -98.386  78.321 -27.663  1.00 41.04           C
ANISOU 2533  CA  LYS A 317     3704   3450   8441   -434    178     97       C
ATOM   2534  C   LYS A 317     -98.256  76.829 -27.394  1.00 37.69           C
ANISOU 2534  C   LYS A 317     3478   3145   7698   -330    306    -14       C
ATOM   2535  O   LYS A 317     -97.415  76.141 -27.977  1.00 33.46           O
ANISOU 2535  O   LYS A 317     3049   2621   7043   -218    306   -191       O
ATOM   2536  CB  LYS A 317     -99.737  78.647 -28.307  1.00 41.16           C
ANISOU 2536  CB  LYS A 317     3781   3188   8670   -497    -44    110       C
ATOM   2537  CG  LYS A 317    -100.126  77.736 -29.458  1.00 36.83           C
ANISOU 2537  CG  LYS A 317     3485   2516   7994   -378   -166   -146       C
ATOM   2538  CD  LYS A 317    -101.578  77.960 -29.845  1.00 42.27           C
ANISOU 2538  CD  LYS A 317     4220   3037   8804   -387   -335   -170       C
ATOM   2539  CE  LYS A 317    -102.043  76.955 -30.883  1.00 49.43           C
ANISOU 2539  CE  LYS A 317     5350   3955   9476   -249   -390   -423       C
ATOM   2540  NZ  LYS A 317    -103.503  77.083 -31.154  1.00 54.87           N
ANISOU 2540  NZ  LYS A 317     6058   4527  10264   -229   -513   -475       N
ATOM   2541  N   VAL A 318     -99.109  76.337 -26.501  1.00 43.17           N
ANISOU 2541  N   VAL A 318     4199   3918   8286   -384    392    126       N
ATOM   2542  CA  VAL A 318     -99.128  74.933 -26.112  1.00 30.86           C
ANISOU 2542  CA  VAL A 318     2802   2474   6451   -315    492     52       C
ATOM   2543  C   VAL A 318    -100.246  74.232 -26.871  1.00 35.68           C
ANISOU 2543  C   VAL A 318     3583   2886   7087   -280    359      4       C
ATOM   2544  O   VAL A 318    -101.393  74.697 -26.873  1.00 37.34           O
ANISOU 2544  O   VAL A 318     3753   2942   7491   -346    258    128       O
ATOM   2545  CB  VAL A 318     -99.311  74.778 -24.593  1.00 34.50           C
ANISOU 2545  CB  VAL A 318     3166   3208   6735   -397    662    238       C
ATOM   2546  CG1 VAL A 318     -99.535  73.319 -24.230  1.00 30.63           C
ANISOU 2546  CG1 VAL A 318     2842   2804   5994   -348    707    169       C
ATOM   2547  CG2 VAL A 318     -98.102  75.334 -23.858  1.00 34.79           C
ANISOU 2547  CG2 VAL A 318     3026   3506   6687   -393    838    204       C
ATOM   2548  N   VAL A 319     -99.912  73.118 -27.516  1.00 35.81           N
ANISOU 2548  N   VAL A 319     3764   2901   6941   -172    359   -168       N
ATOM   2549  CA  VAL A 319    -100.866  72.309 -28.267  1.00 31.95           C
ANISOU 2549  CA  VAL A 319     3417   2292   6430   -112    278   -239       C
ATOM   2550  C   VAL A 319    -101.046  70.983 -27.541  1.00 33.36           C
ANISOU 2550  C   VAL A 319     3665   2596   6414    -96    383   -190       C
ATOM   2551  O   VAL A 319    -100.066  70.281 -27.265  1.00 36.70           O
ANISOU 2551  O   VAL A 319     4121   3147   6677    -67    465   -251       O
ATOM   2552  CB  VAL A 319    -100.395  72.085 -29.715  1.00 33.00           C
ANISOU 2552  CB  VAL A 319     3652   2372   6513    -17    185   -432       C
ATOM   2553  CG1 VAL A 319    -101.329  71.127 -30.433  1.00 33.74           C
ANISOU 2553  CG1 VAL A 319     3868   2429   6523     61    156   -519       C
ATOM   2554  CG2 VAL A 319    -100.309  73.411 -30.454  1.00 34.73           C
ANISOU 2554  CG2 VAL A 319     3800   2474   6921    -45     35   -493       C
ATOM   2555  N   LYS A 320    -102.295  70.645 -27.233  1.00 33.21           N
ANISOU 2555  N   LYS A 320     3651   2516   6452   -116    356    -84       N
ATOM   2556  CA  LYS A 320    -102.635  69.400 -26.556  1.00 33.29           C
ANISOU 2556  CA  LYS A 320     3705   2635   6307   -113    419    -10       C
ATOM   2557  C   LYS A 320    -103.139  68.390 -27.576  1.00 33.06           C
ANISOU 2557  C   LYS A 320     3778   2522   6259     -4    385   -132       C
ATOM   2558  O   LYS A 320    -104.058  68.687 -28.347  1.00 33.38           O
ANISOU 2558  O   LYS A 320     3821   2402   6460     52    307   -198       O
ATOM   2559  CB  LYS A 320    -103.702  69.632 -25.485  1.00 34.59           C
ANISOU 2559  CB  LYS A 320     3769   2810   6562   -209    400    246       C
ATOM   2560  CG  LYS A 320    -103.437  70.817 -24.574  1.00 40.81           C
ANISOU 2560  CG  LYS A 320     4412   3707   7388   -334    434    430       C
ATOM   2561  CD  LYS A 320    -102.989  70.371 -23.193  1.00 45.23           C
ANISOU 2561  CD  LYS A 320     4927   4599   7661   -413    553    553       C
ATOM   2562  CE  LYS A 320    -103.334  71.424 -22.151  1.00 56.11           C
ANISOU 2562  CE  LYS A 320     6118   6127   9074   -562    577    868       C
ATOM   2563  NZ  LYS A 320    -102.969  71.001 -20.772  1.00 62.83           N
ANISOU 2563  NZ  LYS A 320     6917   7387   9567   -642    696    979       N
ATOM   2564  N   VAL A 321    -102.539  67.202 -27.579  1.00 32.39           N
ANISOU 2564  N   VAL A 321     3758   2554   5996     27    444   -172       N
ATOM   2565  CA  VAL A 321    -102.922  66.125 -28.484  1.00 29.17           C
ANISOU 2565  CA  VAL A 321     3411   2134   5540    116    444   -236       C
ATOM   2566  C   VAL A 321    -103.141  64.864 -27.663  1.00 27.00           C
ANISOU 2566  C   VAL A 321     3125   1952   5182     85    481   -124       C
ATOM   2567  O   VAL A 321    -102.266  64.464 -26.887  1.00 29.59           O
ANISOU 2567  O   VAL A 321     3458   2385   5402     23    507   -109       O
ATOM   2568  CB  VAL A 321    -101.859  65.879 -29.572  1.00 29.31           C
ANISOU 2568  CB  VAL A 321     3488   2194   5455    168    443   -348       C
ATOM   2569  CG1 VAL A 321    -102.335  64.807 -30.541  1.00 31.34           C
ANISOU 2569  CG1 VAL A 321     3774   2504   5631    250    465   -370       C
ATOM   2570  CG2 VAL A 321    -101.541  67.171 -30.311  1.00 31.65           C
ANISOU 2570  CG2 VAL A 321     3783   2423   5820    182    374   -449       C
ATOM   2571  N   THR A 322    -104.302  64.238 -27.835  1.00 30.30           N
ANISOU 2571  N   THR A 322     3513   2328   5673    134    471    -71       N
ATOM   2572  CA  THR A 322    -104.624  63.008 -27.119  1.00 29.34           C
ANISOU 2572  CA  THR A 322     3355   2289   5502    100    478     56       C
ATOM   2573  C   THR A 322    -103.962  61.837 -27.834  1.00 33.36           C
ANISOU 2573  C   THR A 322     3895   2871   5910    135    517      8       C
ATOM   2574  O   THR A 322    -104.355  61.475 -28.948  1.00 35.41           O
ANISOU 2574  O   THR A 322     4145   3129   6179    232    554    -44       O
ATOM   2575  CB  THR A 322    -106.134  62.814 -27.025  1.00 31.21           C
ANISOU 2575  CB  THR A 322     3506   2434   5920    148    443    158       C
ATOM   2576  OG1 THR A 322    -106.726  63.964 -26.408  1.00 37.45           O
ANISOU 2576  OG1 THR A 322     4244   3119   6865     97    379    257       O
ATOM   2577  CG2 THR A 322    -106.458  61.584 -26.191  1.00 32.36           C
ANISOU 2577  CG2 THR A 322     3590   2678   6026     96    422    324       C
ATOM   2578  N   ILE A 323    -102.949  61.251 -27.202  1.00 28.24           N
ANISOU 2578  N   ILE A 323     3266   2295   5170     54    504     20       N
ATOM   2579  CA  ILE A 323    -102.215  60.121 -27.754  1.00 27.19           C
ANISOU 2579  CA  ILE A 323     3133   2188   5008     53    505     26       C
ATOM   2580  C   ILE A 323    -102.159  59.036 -26.691  1.00 29.29           C
ANISOU 2580  C   ILE A 323     3358   2506   5264    -40    448    100       C
ATOM   2581  O   ILE A 323    -101.854  59.322 -25.528  1.00 30.56           O
ANISOU 2581  O   ILE A 323     3533   2719   5360   -115    411     58       O
ATOM   2582  CB  ILE A 323    -100.794  60.520 -28.194  1.00 23.18           C
ANISOU 2582  CB  ILE A 323     2675   1643   4488     48    492    -69       C
ATOM   2583  CG1 ILE A 323    -100.843  61.740 -29.114  1.00 28.65           C
ANISOU 2583  CG1 ILE A 323     3404   2305   5179    119    511   -144       C
ATOM   2584  CG2 ILE A 323    -100.108  59.357 -28.893  1.00 23.62           C
ANISOU 2584  CG2 ILE A 323     2703   1695   4576     34    468      9       C
ATOM   2585  CD1 ILE A 323     -99.489  62.313 -29.443  1.00 26.70           C
ANISOU 2585  CD1 ILE A 323     3178   2013   4954    115    477   -212       C
ATOM   2586  N   ASP A 324    -102.457  57.798 -27.089  1.00 29.96           N
ANISOU 2586  N   ASP A 324     3375   2610   5397    -40    441    207       N
ATOM   2587  CA  ASP A 324    -102.449  56.654 -26.175  1.00 30.86           C
ANISOU 2587  CA  ASP A 324     3430   2761   5534   -141    351    282       C
ATOM   2588  C   ASP A 324    -103.362  56.898 -24.975  1.00 33.06           C
ANISOU 2588  C   ASP A 324     3683   3114   5764   -186    301    343       C
ATOM   2589  O   ASP A 324    -103.052  56.505 -23.849  1.00 26.67           O
ANISOU 2589  O   ASP A 324     2872   2386   4877   -293    204    326       O
ATOM   2590  CB  ASP A 324    -101.028  56.322 -25.712  1.00 31.58           C
ANISOU 2590  CB  ASP A 324     3561   2806   5633   -226    267    162       C
ATOM   2591  CG  ASP A 324    -100.122  55.914 -26.852  1.00 35.61           C
ANISOU 2591  CG  ASP A 324     4057   3219   6253   -207    272    192       C
ATOM   2592  OD1 ASP A 324    -100.642  55.468 -27.895  1.00 38.49           O
ANISOU 2592  OD1 ASP A 324     4359   3626   6640   -160    336    349       O
ATOM   2593  OD2 ASP A 324     -98.887  56.032 -26.702  1.00 37.32           O
ANISOU 2593  OD2 ASP A 324     4306   3332   6540   -236    210     70       O
ATOM   2594  N   TYR A 325    -104.490  57.567 -25.223  1.00 27.06           N
ANISOU 2594  N   TYR A 325     2893   2328   5060   -107    350    414       N
ATOM   2595  CA  TYR A 325    -105.500  57.898 -24.219  1.00 31.71           C
ANISOU 2595  CA  TYR A 325     3425   2958   5664   -148    287    555       C
ATOM   2596  C   TYR A 325    -105.003  58.883 -23.169  1.00 34.85           C
ANISOU 2596  C   TYR A 325     3882   3455   5905   -239    263    524       C
ATOM   2597  O   TYR A 325    -105.541  58.922 -22.058  1.00 39.99           O
ANISOU 2597  O   TYR A 325     4480   4231   6486   -328    184    681       O
ATOM   2598  CB  TYR A 325    -106.041  56.645 -23.520  1.00 31.61           C
ANISOU 2598  CB  TYR A 325     3305   3024   5681   -219    180    719       C
ATOM   2599  CG  TYR A 325    -106.724  55.664 -24.439  1.00 33.12           C
ANISOU 2599  CG  TYR A 325     3377   3156   6050   -127    221    798       C
ATOM   2600  CD1 TYR A 325    -107.997  55.916 -24.933  1.00 32.86           C
ANISOU 2600  CD1 TYR A 325     3245   3036   6206      3    268    869       C
ATOM   2601  CD2 TYR A 325    -106.103  54.477 -24.800  1.00 34.61           C
ANISOU 2601  CD2 TYR A 325     3526   3375   6249   -167    211    800       C
ATOM   2602  CE1 TYR A 325    -108.628  55.017 -25.771  1.00 37.24           C
ANISOU 2602  CE1 TYR A 325     3660   3583   6906    110    340    909       C
ATOM   2603  CE2 TYR A 325    -106.726  53.571 -25.637  1.00 37.77           C
ANISOU 2603  CE2 TYR A 325     3780   3778   6795    -89    276    905       C
ATOM   2604  CZ  TYR A 325    -107.988  53.846 -26.119  1.00 39.41           C
ANISOU 2604  CZ  TYR A 325     3886   3947   7140     60    357    944       C
ATOM   2605  OH  TYR A 325    -108.611  52.946 -26.953  1.00 41.11           O
ANISOU 2605  OH  TYR A 325     3927   4209   7483    161    455   1016       O
ATOM   2606  N   THR A 326    -103.988  59.685 -23.482  1.00 30.49           N
ANISOU 2606  N   THR A 326     3415   2883   5286   -221    332    348       N
ATOM   2607  CA  THR A 326    -103.520  60.710 -22.562  1.00 31.74           C
ANISOU 2607  CA  THR A 326     3593   3168   5300   -290    350    315       C
ATOM   2608  C   THR A 326    -103.248  61.991 -23.339  1.00 32.72           C
ANISOU 2608  C   THR A 326     3747   3176   5510   -221    428    234       C
ATOM   2609  O   THR A 326    -102.950  61.959 -24.536  1.00 35.79           O
ANISOU 2609  O   THR A 326     4178   3426   5996   -131    457    128       O
ATOM   2610  CB  THR A 326    -102.262  60.261 -21.795  1.00 29.21           C
ANISOU 2610  CB  THR A 326     3311   2993   4795   -356    335    125       C
ATOM   2611  OG1 THR A 326    -102.094  61.072 -20.625  1.00 35.35           O
ANISOU 2611  OG1 THR A 326     4064   4004   5363   -432    363    129       O
ATOM   2612  CG2 THR A 326    -101.020  60.383 -22.660  1.00 27.58           C
ANISOU 2612  CG2 THR A 326     3164   2648   4669   -284    385    -94       C
ATOM   2613  N   GLU A 327    -103.374  63.122 -22.650  1.00 29.00           N
ANISOU 2613  N   GLU A 327     3235   2789   4995   -277    450    312       N
ATOM   2614  CA  GLU A 327    -103.137  64.421 -23.267  1.00 36.49           C
ANISOU 2614  CA  GLU A 327     4182   3630   6054   -237    498    257       C
ATOM   2615  C   GLU A 327    -101.644  64.725 -23.270  1.00 32.40           C
ANISOU 2615  C   GLU A 327     3697   3179   5433   -223    566     42       C
ATOM   2616  O   GLU A 327    -101.030  64.868 -22.207  1.00 33.00           O
ANISOU 2616  O   GLU A 327     3738   3468   5332   -285    613     -2       O
ATOM   2617  CB  GLU A 327    -103.903  65.519 -22.532  1.00 46.17           C
ANISOU 2617  CB  GLU A 327     5305   4902   7334   -321    483    486       C
ATOM   2618  CG  GLU A 327    -105.198  65.940 -23.208  1.00 57.46           C
ANISOU 2618  CG  GLU A 327     6690   6076   9067   -276    403    611       C
ATOM   2619  CD  GLU A 327    -105.715  67.271 -22.692  1.00 69.36           C
ANISOU 2619  CD  GLU A 327     8077   7553  10724   -369    368    835       C
ATOM   2620  OE1 GLU A 327    -104.987  67.933 -21.922  1.00 73.03           O
ANISOU 2620  OE1 GLU A 327     8491   8237  11020   -461    440    891       O
ATOM   2621  OE2 GLU A 327    -106.846  67.656 -23.056  1.00 72.55           O
ANISOU 2621  OE2 GLU A 327     8416   7710  11440   -348    267    954       O
ATOM   2622  N   ILE A 328    -101.063  64.827 -24.462  1.00 29.30           N
ANISOU 2622  N   ILE A 328     3356   2626   5150   -136    568    -96       N
ATOM   2623  CA  ILE A 328     -99.657  65.174 -24.631  1.00 29.52           C
ANISOU 2623  CA  ILE A 328     3388   2655   5172   -104    606   -277       C
ATOM   2624  C   ILE A 328     -99.567  66.644 -25.012  1.00 29.68           C
ANISOU 2624  C   ILE A 328     3355   2623   5298    -93    626   -268       C
ATOM   2625  O   ILE A 328    -100.200  67.084 -25.980  1.00 27.00           O
ANISOU 2625  O   ILE A 328     3034   2140   5084    -58    571   -229       O
ATOM   2626  CB  ILE A 328     -98.984  64.287 -25.691  1.00 31.25           C
ANISOU 2626  CB  ILE A 328     3670   2743   5462    -38    560   -366       C
ATOM   2627  CG1 ILE A 328     -99.077  62.813 -25.292  1.00 29.03           C
ANISOU 2627  CG1 ILE A 328     3409   2494   5126    -71    522   -348       C
ATOM   2628  CG2 ILE A 328     -97.529  64.689 -25.871  1.00 30.81           C
ANISOU 2628  CG2 ILE A 328     3590   2639   5477      2    568   -521       C
ATOM   2629  CD1 ILE A 328     -98.330  62.482 -24.020  1.00 26.35           C
ANISOU 2629  CD1 ILE A 328     3048   2278   4686   -125    525   -485       C
ATOM   2630  N   SER A 329     -98.783  67.404 -24.253  1.00 34.74           N
ANISOU 2630  N   SER A 329     3913   3394   5893   -119    702   -326       N
ATOM   2631  CA  SER A 329     -98.604  68.827 -24.504  1.00 32.47           C
ANISOU 2631  CA  SER A 329     3532   3076   5731   -125    722   -295       C
ATOM   2632  C   SER A 329     -97.436  69.033 -25.460  1.00 33.80           C
ANISOU 2632  C   SER A 329     3706   3115   6022    -36    691   -458       C
ATOM   2633  O   SER A 329     -96.312  68.603 -25.179  1.00 35.56           O
ANISOU 2633  O   SER A 329     3912   3372   6226     11    730   -615       O
ATOM   2634  CB  SER A 329     -98.369  69.580 -23.196  1.00 38.98           C
ANISOU 2634  CB  SER A 329     4215   4158   6437   -198    843   -237       C
ATOM   2635  OG  SER A 329     -99.513  69.524 -22.363  1.00 48.06           O
ANISOU 2635  OG  SER A 329     5336   5439   7486   -302    840     -1       O
ATOM   2636  N   PHE A 330     -97.706  69.683 -26.587  1.00 35.23           N
ANISOU 2636  N   PHE A 330     3899   3140   6347    -15    598   -427       N
ATOM   2637  CA  PHE A 330     -96.684  70.062 -27.549  1.00 30.98           C
ANISOU 2637  CA  PHE A 330     3342   2502   5928     50    533   -519       C
ATOM   2638  C   PHE A 330     -96.440  71.563 -27.472  1.00 36.31           C
ANISOU 2638  C   PHE A 330     3869   3179   6749     19    533   -490       C
ATOM   2639  O   PHE A 330     -97.321  72.332 -27.078  1.00 39.00           O
ANISOU 2639  O   PHE A 330     4146   3537   7134    -60    539   -370       O
ATOM   2640  CB  PHE A 330     -97.094  69.689 -28.976  1.00 32.99           C
ANISOU 2640  CB  PHE A 330     3707   2642   6186     90    406   -514       C
ATOM   2641  CG  PHE A 330     -97.096  68.213 -29.248  1.00 30.07           C
ANISOU 2641  CG  PHE A 330     3438   2282   5704    122    408   -511       C
ATOM   2642  CD1 PHE A 330     -98.136  67.412 -28.805  1.00 28.75           C
ANISOU 2642  CD1 PHE A 330     3325   2157   5442    100    450   -458       C
ATOM   2643  CD2 PHE A 330     -96.068  67.629 -29.969  1.00 32.04           C
ANISOU 2643  CD2 PHE A 330     3701   2490   5984    166    350   -518       C
ATOM   2644  CE1 PHE A 330     -98.142  66.054 -29.064  1.00 25.75           C
ANISOU 2644  CE1 PHE A 330     3004   1792   4988    118    449   -431       C
ATOM   2645  CE2 PHE A 330     -96.070  66.272 -30.232  1.00 31.75           C
ANISOU 2645  CE2 PHE A 330     3723   2459   5880    172    343   -463       C
ATOM   2646  CZ  PHE A 330     -97.107  65.484 -29.778  1.00 25.87           C
ANISOU 2646  CZ  PHE A 330     3027   1772   5032    147    399   -428       C
ATOM   2647  N   MET A 331     -95.238  71.974 -27.856  1.00 39.29           N
ANISOU 2647  N   MET A 331     4164   3519   7247     76    509   -570       N
ATOM   2648  CA  MET A 331     -94.881  73.384 -27.929  1.00 39.28           C
ANISOU 2648  CA  MET A 331     3990   3510   7425     52    490   -536       C
ATOM   2649  C   MET A 331     -94.708  73.756 -29.394  1.00 37.42           C
ANISOU 2649  C   MET A 331     3789   3122   7306     77    288   -539       C
ATOM   2650  O   MET A 331     -93.837  73.208 -30.078  1.00 38.13           O
ANISOU 2650  O   MET A 331     3915   3158   7413    150    216   -583       O
ATOM   2651  CB  MET A 331     -93.608  73.674 -27.136  1.00 44.24           C
ANISOU 2651  CB  MET A 331     4445   4242   8124    111    625   -634       C
ATOM   2652  CG  MET A 331     -93.505  75.111 -26.660  1.00 55.39           C
ANISOU 2652  CG  MET A 331     5623   5752   9671     58    695   -550       C
ATOM   2653  SD  MET A 331     -94.879  75.563 -25.582  1.00 58.60           S
ANISOU 2653  SD  MET A 331     5983   6338   9945    -96    802   -336       S
ATOM   2654  CE  MET A 331     -94.513  77.287 -25.260  1.00 57.12           C
ANISOU 2654  CE  MET A 331     5467   6247   9988   -166    861   -192       C
ATOM   2655  N   LEU A 332     -95.544  74.672 -29.874  1.00 37.08           N
ANISOU 2655  N   LEU A 332     3726   3012   7350      8    174   -485       N
ATOM   2656  CA  LEU A 332     -95.541  75.094 -31.268  1.00 35.64           C
ANISOU 2656  CA  LEU A 332     3584   2732   7226     18    -44   -523       C
ATOM   2657  C   LEU A 332     -94.978  76.505 -31.363  1.00 35.56           C
ANISOU 2657  C   LEU A 332     3366   2683   7464    -26   -131   -482       C
ATOM   2658  O   LEU A 332     -95.481  77.422 -30.706  1.00 34.84           O
ANISOU 2658  O   LEU A 332     3139   2580   7518   -116    -96   -402       O
ATOM   2659  CB  LEU A 332     -96.950  75.043 -31.858  1.00 34.63           C
ANISOU 2659  CB  LEU A 332     3586   2534   7036    -14   -147   -570       C
ATOM   2660  CG  LEU A 332     -97.081  75.565 -33.290  1.00 36.23           C
ANISOU 2660  CG  LEU A 332     3832   2684   7248     -8   -384   -674       C
ATOM   2661  CD1 LEU A 332     -96.249  74.722 -34.244  1.00 35.32           C
ANISOU 2661  CD1 LEU A 332     3808   2677   6934     69   -437   -686       C
ATOM   2662  CD2 LEU A 332     -98.539  75.592 -33.721  1.00 38.75           C
ANISOU 2662  CD2 LEU A 332     4252   2918   7554    -19   -469   -797       C
ATOM   2663  N   TRP A 333     -93.943  76.674 -32.180  1.00 32.45           N
ANISOU 2663  N   TRP A 333     2921   2269   7139     25   -259   -497       N
ATOM   2664  CA  TRP A 333     -93.332  77.971 -32.425  1.00 34.25           C
ANISOU 2664  CA  TRP A 333     2932   2456   7625    -11   -380   -449       C
ATOM   2665  C   TRP A 333     -93.492  78.324 -33.895  1.00 35.21           C
ANISOU 2665  C   TRP A 333     3125   2529   7725    -35   -678   -485       C
ATOM   2666  O   TRP A 333     -93.169  77.514 -34.770  1.00 41.06           O
ANISOU 2666  O   TRP A 333     4003   3318   8281     24   -768   -499       O
ATOM   2667  CB  TRP A 333     -91.854  77.969 -32.034  1.00 44.08           C
ANISOU 2667  CB  TRP A 333     3998   3726   9023     81   -292   -430       C
ATOM   2668  CG  TRP A 333     -91.639  77.824 -30.565  1.00 47.16           C
ANISOU 2668  CG  TRP A 333     4282   4222   9417    108     -1   -457       C
ATOM   2669  CD1 TRP A 333     -91.684  76.669 -29.841  1.00 47.14           C
ANISOU 2669  CD1 TRP A 333     4406   4286   9219    160    173   -535       C
ATOM   2670  CD2 TRP A 333     -91.349  78.871 -29.633  1.00 51.96           C
ANISOU 2670  CD2 TRP A 333     4614   4929  10200     79    148   -409       C
ATOM   2671  NE1 TRP A 333     -91.437  76.932 -28.516  1.00 49.61           N
ANISOU 2671  NE1 TRP A 333     4559   4755   9535    169    414   -569       N
ATOM   2672  CE2 TRP A 333     -91.228  78.277 -28.362  1.00 53.64           C
ANISOU 2672  CE2 TRP A 333     4814   5309  10259    123    423   -482       C
ATOM   2673  CE3 TRP A 333     -91.175  80.254 -29.751  1.00 55.04           C
ANISOU 2673  CE3 TRP A 333     4748   5309  10856     12     73   -303       C
ATOM   2674  CZ2 TRP A 333     -90.944  79.017 -27.216  1.00 57.39           C
ANISOU 2674  CZ2 TRP A 333     5030   5991  10784    111    651   -457       C
ATOM   2675  CZ3 TRP A 333     -90.894  80.986 -28.612  1.00 56.18           C
ANISOU 2675  CZ3 TRP A 333     4616   5628  11101     -5    305   -244       C
ATOM   2676  CH2 TRP A 333     -90.781  80.367 -27.362  1.00 57.37           C
ANISOU 2676  CH2 TRP A 333     4762   5994  11043     49    604   -322       C
ATOM   2677  N   CYS A 334     -93.995  79.525 -34.161  1.00 37.05           N
ANISOU 2677  N   CYS A 334     3253   2685   8138   -133   -841   -490       N
ATOM   2678  CA  CYS A 334     -94.235  79.981 -35.520  1.00 39.05           C
ANISOU 2678  CA  CYS A 334     3566   2915   8354   -170  -1154   -580       C
ATOM   2679  C   CYS A 334     -93.678  81.383 -35.702  1.00 43.28           C
ANISOU 2679  C   CYS A 334     3845   3385   9214   -249  -1342   -507       C
ATOM   2680  O   CYS A 334     -93.633  82.180 -34.761  1.00 51.15           O
ANISOU 2680  O   CYS A 334     4623   4326  10486   -311  -1232   -402       O
ATOM   2681  CB  CYS A 334     -95.728  79.977 -35.862  1.00 38.58           C
ANISOU 2681  CB  CYS A 334     3670   2785   8204   -216  -1239   -748       C
ATOM   2682  SG  CYS A 334     -96.536  78.391 -35.609  1.00 42.89           S
ANISOU 2682  SG  CYS A 334     4472   3404   8422   -125  -1016   -821       S
ATOM   2683  N   LYS A 335     -93.254  81.672 -36.928  1.00 44.51           N
ANISOU 2683  N   LYS A 335     4009   3581   9320   -255  -1634   -540       N
ATOM   2684  CA  LYS A 335     -92.813  83.006 -37.304  1.00 49.55           C
ANISOU 2684  CA  LYS A 335     4408   4157  10262   -345  -1887   -483       C
ATOM   2685  C   LYS A 335     -93.267  83.277 -38.728  1.00 53.24           C
ANISOU 2685  C   LYS A 335     5006   4673  10551   -398  -2255   -650       C
ATOM   2686  O   LYS A 335     -93.059  82.443 -39.613  1.00 52.29           O
ANISOU 2686  O   LYS A 335     5067   4727  10074   -331  -2329   -687       O
ATOM   2687  CB  LYS A 335     -91.290  83.153 -37.191  1.00 54.11           C
ANISOU 2687  CB  LYS A 335     4758   4774  11028   -275  -1869   -294       C
ATOM   2688  CG  LYS A 335     -90.776  84.529 -37.589  1.00 63.92           C
ANISOU 2688  CG  LYS A 335     5712   5959  12614   -365  -2141   -206       C
ATOM   2689  CD  LYS A 335     -89.823  85.094 -36.547  1.00 69.67           C
ANISOU 2689  CD  LYS A 335     6094   6654  13722   -323  -1932    -42       C
ATOM   2690  CE  LYS A 335     -89.533  86.565 -36.810  1.00 78.58           C
ANISOU 2690  CE  LYS A 335     6974   7724  15160   -414  -2140     66       C
ATOM   2691  NZ  LYS A 335     -88.686  87.170 -35.745  1.00 81.89           N
ANISOU 2691  NZ  LYS A 335     7120   8154  15840   -349  -1854    214       N
ATOM   2692  N   ASP A 336     -93.901  84.432 -38.934  1.00 55.28           N
ANISOU 2692  N   ASP A 336     5159   4794  11050   -527  -2489   -750       N
ATOM   2693  CA  ASP A 336     -94.352  84.865 -40.257  1.00 59.18           C
ANISOU 2693  CA  ASP A 336     5751   5334  11401   -589  -2880   -978       C
ATOM   2694  C   ASP A 336     -95.267  83.828 -40.906  1.00 59.08           C
ANISOU 2694  C   ASP A 336     6066   5454  10927   -508  -2849  -1246       C
ATOM   2695  O   ASP A 336     -95.224  83.605 -42.118  1.00 61.56           O
ANISOU 2695  O   ASP A 336     6511   5991  10887   -489  -3074  -1393       O
ATOM   2696  CB  ASP A 336     -93.165  85.189 -41.166  1.00 64.27           C
ANISOU 2696  CB  ASP A 336     6279   6142  11999   -596  -3151   -845       C
ATOM   2697  CG  ASP A 336     -92.298  86.306 -40.614  1.00 72.64           C
ANISOU 2697  CG  ASP A 336     6984   7073  13544   -659  -3192   -603       C
ATOM   2698  OD1 ASP A 336     -92.844  87.221 -39.960  1.00 73.99           O
ANISOU 2698  OD1 ASP A 336     7068   7075  13969   -711  -3098   -581       O
ATOM   2699  OD2 ASP A 336     -91.069  86.266 -40.831  1.00 76.79           O
ANISOU 2699  OD2 ASP A 336     7351   7689  14136   -612  -3254   -391       O
ATOM   2700  N   GLY A 337     -96.097  83.182 -40.091  1.00 56.20           N
ANISOU 2700  N   GLY A 337     5813   4989  10552   -459  -2564  -1296       N
ATOM   2701  CA  GLY A 337     -97.093  82.263 -40.601  1.00 55.50           C
ANISOU 2701  CA  GLY A 337     5988   4996  10104   -374  -2511  -1562       C
ATOM   2702  C   GLY A 337     -96.602  80.872 -40.934  1.00 57.19           C
ANISOU 2702  C   GLY A 337     6368   5496   9867   -251  -2322  -1472       C
ATOM   2703  O   GLY A 337     -97.381  80.074 -41.467  1.00 61.40           O
ANISOU 2703  O   GLY A 337     7096   6169  10065   -173  -2270  -1684       O
ATOM   2704  N   HIS A 338     -95.344  80.550 -40.648  1.00 54.42           N
ANISOU 2704  N   HIS A 338     5922   5224   9529   -227  -2223  -1167       N
ATOM   2705  CA  HIS A 338     -94.816  79.217 -40.887  1.00 50.70           C
ANISOU 2705  CA  HIS A 338     5574   4970   8722   -132  -2062  -1026       C
ATOM   2706  C   HIS A 338     -94.271  78.639 -39.589  1.00 41.49           C
ANISOU 2706  C   HIS A 338     4336   3675   7753    -86  -1751   -816       C
ATOM   2707  O   HIS A 338     -93.990  79.363 -38.630  1.00 41.04           O
ANISOU 2707  O   HIS A 338     4103   3439   8051   -122  -1676   -739       O
ATOM   2708  CB  HIS A 338     -93.725  79.227 -41.968  1.00 55.70           C
ANISOU 2708  CB  HIS A 338     6159   5829   9177   -142  -2299   -853       C
ATOM   2709  CG  HIS A 338     -92.558  80.108 -41.648  1.00 67.20           C
ANISOU 2709  CG  HIS A 338     7360   7147  11025   -185  -2418   -630       C
ATOM   2710  ND1 HIS A 338     -91.666  79.827 -40.634  1.00 68.45           N
ANISOU 2710  ND1 HIS A 338     7380   7160  11468   -130  -2199   -415       N
ATOM   2711  CD2 HIS A 338     -92.129  81.259 -42.217  1.00 72.21           C
ANISOU 2711  CD2 HIS A 338     7832   7776  11828   -267  -2737   -608       C
ATOM   2712  CE1 HIS A 338     -90.742  80.770 -40.589  1.00 69.09           C
ANISOU 2712  CE1 HIS A 338     7212   7152  11888   -160  -2353   -274       C
ATOM   2713  NE2 HIS A 338     -91.001  81.652 -41.538  1.00 72.13           N
ANISOU 2713  NE2 HIS A 338     7572   7614  12218   -252  -2687   -361       N
ATOM   2714  N   VAL A 339     -94.123  77.316 -39.572  1.00 39.89           N
ANISOU 2714  N   VAL A 339     4260   3593   7305     -9  -1572   -732       N
ATOM   2715  CA  VAL A 339     -93.688  76.628 -38.363  1.00 37.42           C
ANISOU 2715  CA  VAL A 339     3908   3172   7140     38  -1295   -599       C
ATOM   2716  C   VAL A 339     -92.196  76.844 -38.154  1.00 47.61           C
ANISOU 2716  C   VAL A 339     5007   4403   8678     59  -1332   -392       C
ATOM   2717  O   VAL A 339     -91.382  76.584 -39.048  1.00 47.81           O
ANISOU 2717  O   VAL A 339     5012   4529   8626     72  -1500   -239       O
ATOM   2718  CB  VAL A 339     -94.021  75.132 -38.447  1.00 40.04           C
ANISOU 2718  CB  VAL A 339     4412   3626   7174    100  -1128   -577       C
ATOM   2719  CG1 VAL A 339     -93.503  74.404 -37.219  1.00 38.89           C
ANISOU 2719  CG1 VAL A 339     4224   3367   7185    139   -887   -471       C
ATOM   2720  CG2 VAL A 339     -95.518  74.931 -38.597  1.00 35.73           C
ANISOU 2720  CG2 VAL A 339     4018   3120   6440    107  -1074   -803       C
ATOM   2721  N   GLU A 340     -91.832  77.334 -36.967  1.00 48.93           N
ANISOU 2721  N   GLU A 340     5014   4423   9156     66  -1176   -378       N
ATOM   2722  CA  GLU A 340     -90.430  77.355 -36.564  1.00 54.00           C
ANISOU 2722  CA  GLU A 340     5461   4988  10069    130  -1144   -243       C
ATOM   2723  C   GLU A 340     -90.009  75.992 -36.026  1.00 50.21           C
ANISOU 2723  C   GLU A 340     5062   4487   9530    212   -952   -210       C
ATOM   2724  O   GLU A 340     -89.077  75.366 -36.541  1.00 49.06           O
ANISOU 2724  O   GLU A 340     4888   4316   9435    259  -1049    -65       O
ATOM   2725  CB  GLU A 340     -90.194  78.446 -35.514  1.00 60.28           C
ANISOU 2725  CB  GLU A 340     6018   5694  11191    117  -1028   -272       C
ATOM   2726  CG  GLU A 340     -90.024  79.852 -36.071  1.00 66.66           C
ANISOU 2726  CG  GLU A 340     6635   6475  12218     42  -1268   -228       C
ATOM   2727  CD  GLU A 340     -88.603  80.138 -36.520  1.00 75.91           C
ANISOU 2727  CD  GLU A 340     7591   7604  13646    106  -1425    -81       C
ATOM   2728  OE1 GLU A 340     -88.181  79.595 -37.562  1.00 80.18           O
ANISOU 2728  OE1 GLU A 340     8219   8193  14054    123  -1631     26       O
ATOM   2729  OE2 GLU A 340     -87.903  80.902 -35.822  1.00 79.30           O
ANISOU 2729  OE2 GLU A 340     7740   7968  14421    140  -1340    -52       O
ATOM   2730  N   THR A 341     -90.696  75.516 -34.989  1.00 46.70           N
ANISOU 2730  N   THR A 341     4702   4040   9003    216   -707   -322       N
ATOM   2731  CA  THR A 341     -90.464  74.183 -34.455  1.00 41.85           C
ANISOU 2731  CA  THR A 341     4178   3408   8316    273   -549   -324       C
ATOM   2732  C   THR A 341     -91.749  73.682 -33.813  1.00 41.19           C
ANISOU 2732  C   THR A 341     4255   3390   8005    236   -377   -422       C
ATOM   2733  O   THR A 341     -92.712  74.431 -33.627  1.00 39.88           O
ANISOU 2733  O   THR A 341     4100   3247   7806    176   -364   -481       O
ATOM   2734  CB  THR A 341     -89.314  74.163 -33.442  1.00 42.46           C
ANISOU 2734  CB  THR A 341     4073   3375   8684    357   -421   -372       C
ATOM   2735  OG1 THR A 341     -88.989  72.806 -33.118  1.00 41.84           O
ANISOU 2735  OG1 THR A 341     4083   3242   8573    405   -343   -386       O
ATOM   2736  CG2 THR A 341     -89.712  74.894 -32.171  1.00 43.12           C
ANISOU 2736  CG2 THR A 341     4058   3516   8809    342   -207   -502       C
ATOM   2737  N   PHE A 342     -91.746  72.396 -33.468  1.00 43.66           N
ANISOU 2737  N   PHE A 342     4672   3708   8210    266   -269   -420       N
ATOM   2738  CA  PHE A 342     -92.932  71.736 -32.927  1.00 38.40           C
ANISOU 2738  CA  PHE A 342     4148   3105   7337    236   -130   -478       C
ATOM   2739  C   PHE A 342     -92.465  70.433 -32.293  1.00 42.01           C
ANISOU 2739  C   PHE A 342     4640   3534   7789    270    -26   -478       C
ATOM   2740  O   PHE A 342     -92.011  69.532 -33.004  1.00 44.77           O
ANISOU 2740  O   PHE A 342     5031   3860   8120    286   -109   -372       O
ATOM   2741  CB  PHE A 342     -93.958  71.490 -34.029  1.00 33.98           C
ANISOU 2741  CB  PHE A 342     3733   2633   6545    214   -225   -464       C
ATOM   2742  CG  PHE A 342     -95.222  70.839 -33.554  1.00 37.20           C
ANISOU 2742  CG  PHE A 342     4256   3082   6798    202    -99   -519       C
ATOM   2743  CD1 PHE A 342     -96.043  71.475 -32.640  1.00 38.65           C
ANISOU 2743  CD1 PHE A 342     4408   3224   7051    162    -18   -574       C
ATOM   2744  CD2 PHE A 342     -95.603  69.600 -34.042  1.00 40.05           C
ANISOU 2744  CD2 PHE A 342     4724   3527   6967    224    -70   -474       C
ATOM   2745  CE1 PHE A 342     -97.211  70.881 -32.210  1.00 36.04           C
ANISOU 2745  CE1 PHE A 342     4159   2910   6625    153     69   -589       C
ATOM   2746  CE2 PHE A 342     -96.772  69.001 -33.614  1.00 36.95           C
ANISOU 2746  CE2 PHE A 342     4406   3162   6473    225     37   -517       C
ATOM   2747  CZ  PHE A 342     -97.576  69.641 -32.697  1.00 36.43           C
ANISOU 2747  CZ  PHE A 342     4314   3027   6500    194     96   -577       C
ATOM   2748  N   TYR A 343     -92.565  70.338 -30.970  1.00 40.73           N
ANISOU 2748  N   TYR A 343     4447   3388   7641    269    140   -582       N
ATOM   2749  CA  TYR A 343     -91.972  69.221 -30.251  1.00 38.57           C
ANISOU 2749  CA  TYR A 343     4181   3081   7392    298    209   -644       C
ATOM   2750  C   TYR A 343     -92.816  68.886 -29.039  1.00 38.94           C
ANISOU 2750  C   TYR A 343     4278   3238   7278    258    365   -724       C
ATOM   2751  O   TYR A 343     -93.511  69.762 -28.502  1.00 35.37           O
ANISOU 2751  O   TYR A 343     3790   2889   6761    216    443   -722       O
ATOM   2752  CB  TYR A 343     -90.535  69.541 -29.815  1.00 35.95           C
ANISOU 2752  CB  TYR A 343     3686   2700   7271    359    207   -735       C
ATOM   2753  CG  TYR A 343     -90.414  70.774 -28.949  1.00 36.66           C
ANISOU 2753  CG  TYR A 343     3622   2841   7467    388    340   -864       C
ATOM   2754  CD1 TYR A 343     -90.226  72.027 -29.518  1.00 36.61           C
ANISOU 2754  CD1 TYR A 343     3490   2804   7616    395    272   -798       C
ATOM   2755  CD2 TYR A 343     -90.482  70.686 -27.564  1.00 38.80           C
ANISOU 2755  CD2 TYR A 343     3848   3236   7659    401    532  -1036       C
ATOM   2756  CE1 TYR A 343     -90.113  73.156 -28.734  1.00 34.87           C
ANISOU 2756  CE1 TYR A 343     3091   2691   7466    396    400   -858       C
ATOM   2757  CE2 TYR A 343     -90.371  71.812 -26.771  1.00 39.19           C
ANISOU 2757  CE2 TYR A 343     3726   3442   7722    405    677  -1098       C
ATOM   2758  CZ  TYR A 343     -90.186  73.044 -27.362  1.00 39.39           C
ANISOU 2758  CZ  TYR A 343     3612   3434   7919    402    617   -995       C
ATOM   2759  OH  TYR A 343     -90.074  74.170 -26.580  1.00 45.64           O
ANISOU 2759  OH  TYR A 343     4195   4398   8747    393    770  -1014       O
ATOM   2760  N   PRO A 344     -92.786  67.641 -28.571  1.00 43.40           N
ANISOU 2760  N   PRO A 344     4908   3795   7786    253    391   -764       N
ATOM   2761  CA  PRO A 344     -93.473  67.293 -27.330  1.00 44.67           C
ANISOU 2761  CA  PRO A 344     5100   4099   7775    207    512   -832       C
ATOM   2762  C   PRO A 344     -92.694  67.775 -26.118  1.00 48.64           C
ANISOU 2762  C   PRO A 344     5479   4699   8304    239    629  -1031       C
ATOM   2763  O   PRO A 344     -91.463  67.851 -26.129  1.00 50.32           O
ANISOU 2763  O   PRO A 344     5595   4804   8721    322    612  -1178       O
ATOM   2764  CB  PRO A 344     -93.531  65.759 -27.366  1.00 45.15           C
ANISOU 2764  CB  PRO A 344     5248   4102   7805    188    459   -815       C
ATOM   2765  CG  PRO A 344     -93.039  65.356 -28.737  1.00 41.11           C
ANISOU 2765  CG  PRO A 344     4752   3467   7402    209    323   -672       C
ATOM   2766  CD  PRO A 344     -92.163  66.464 -29.201  1.00 40.02           C
ANISOU 2766  CD  PRO A 344     4517   3292   7397    257    275   -683       C
ATOM   2767  N   LYS A 345     -93.431  68.098 -25.061  1.00 55.65           N
ANISOU 2767  N   LYS A 345     6351   5809   8986    178    750  -1028       N
ATOM   2768  CA  LYS A 345     -92.822  68.563 -23.828  1.00 62.63           C
ANISOU 2768  CA  LYS A 345     7104   6899   9795    201    899  -1213       C
ATOM   2769  C   LYS A 345     -92.491  67.374 -22.925  1.00 68.67           C
ANISOU 2769  C   LYS A 345     7917   7738  10436    208    911  -1429       C
ATOM   2770  O   LYS A 345     -92.694  66.212 -23.281  1.00 65.52           O
ANISOU 2770  O   LYS A 345     7637   7196  10062    186    792  -1401       O
ATOM   2771  CB  LYS A 345     -93.740  69.565 -23.129  1.00 60.52           C
ANISOU 2771  CB  LYS A 345     6761   6884   9349    109   1014  -1045       C
ATOM   2772  CG  LYS A 345     -94.026  70.805 -23.963  1.00 57.45           C
ANISOU 2772  CG  LYS A 345     6300   6391   9138     89    972   -864       C
ATOM   2773  CD  LYS A 345     -94.963  71.763 -23.247  1.00 59.04           C
ANISOU 2773  CD  LYS A 345     6399   6798   9236    -27   1057   -648       C
ATOM   2774  CE  LYS A 345     -94.358  72.262 -21.946  1.00 62.14           C
ANISOU 2774  CE  LYS A 345     6607   7534   9468    -29   1264   -734       C
ATOM   2775  NZ  LYS A 345     -95.229  73.273 -21.286  1.00 63.43           N
ANISOU 2775  NZ  LYS A 345     6627   7920   9552   -168   1342   -434       N
ATOM   2776  N   LEU A 346     -91.968  67.672 -21.738  1.00 77.78           N
ANISOU 2776  N   LEU A 346     8960   9144  11450    238   1055  -1659       N
ATOM   2777  CA  LEU A 346     -91.563  66.646 -20.784  1.00 86.34           C
ANISOU 2777  CA  LEU A 346    10075  10333  12398    251   1054  -1950       C
ATOM   2778  C   LEU A 346     -92.737  65.780 -20.347  1.00 91.22           C
ANISOU 2778  C   LEU A 346    10825  11088  12746    119    992  -1784       C
ATOM   2779  O   LEU A 346     -92.791  64.587 -20.665  1.00 89.01           O
ANISOU 2779  O   LEU A 346    10650  10614  12555     98    843  -1801       O
ATOM   2780  CB  LEU A 346     -90.908  67.291 -19.560  1.00 90.26           C
ANISOU 2780  CB  LEU A 346    10410  11180  12706    311   1253  -2245       C
ATOM   2781  CG  LEU A 346     -89.590  68.024 -19.811  1.00 92.22           C
ANISOU 2781  CG  LEU A 346    10480  11300  13259    476   1326  -2492       C
ATOM   2782  CD1 LEU A 346     -89.084  68.673 -18.531  1.00 95.14           C
ANISOU 2782  CD1 LEU A 346    10663  12107  13377    541   1570  -2790       C
ATOM   2783  CD2 LEU A 346     -88.566  67.057 -20.369  1.00 92.86           C
ANISOU 2783  CD2 LEU A 346    10616  10983  13683    559   1118  -2675       C
ATOM   2784  N   GLN A 347     -93.677  66.371 -19.617  1.00100.87           N
ANISOU 2784  N   GLN A 347    12016  12640  13672     21   1093  -1587       N
ATOM   2785  CA  GLN A 347     -94.824  65.632 -19.107  1.00107.15           C
ANISOU 2785  CA  GLN A 347    12900  13583  14228   -104   1022  -1393       C
ATOM   2786  C   GLN A 347     -96.028  66.548 -18.924  1.00113.23           C
ANISOU 2786  C   GLN A 347    13620  14528  14874   -208   1078  -1006       C
ATOM   2787  O   GLN A 347     -97.143  66.211 -19.323  1.00114.82           O
ANISOU 2787  O   GLN A 347    13892  14609  15124   -274    975   -731       O
ATOM   2788  CB  GLN A 347     -94.472  64.952 -17.782  1.00110.46           C
ANISOU 2788  CB  GLN A 347    13309  14324  14336   -131   1041  -1671       C
ATOM   2789  CG  GLN A 347     -95.624  64.205 -17.140  1.00111.09           C
ANISOU 2789  CG  GLN A 347    13456  14604  14151   -272    945  -1451       C
ATOM   2790  CD  GLN A 347     -95.292  63.726 -15.742  1.00115.71           C
ANISOU 2790  CD  GLN A 347    14015  15606  14345   -315    960  -1728       C
ATOM   2791  OE1 GLN A 347     -96.078  63.021 -15.109  1.00116.93           O
ANISOU 2791  OE1 GLN A 347    14211  15957  14261   -434    851  -1589       O
ATOM   2792  NE2 GLN A 347     -94.121  64.112 -15.249  1.00118.06           N
ANISOU 2792  NE2 GLN A 347    14228  16058  14572   -210   1090  -2143       N
TER    2793      GLN A 347
ATOM   2794  N   ALA B   0     -88.679  71.910   1.138  1.00 82.01           N
ANISOU 2794  N   ALA B   0    11458   8087  11616  -1627   -886   -922       N
ATOM   2795  CA  ALA B   0     -87.438  71.381   0.591  1.00 77.20           C
ANISOU 2795  CA  ALA B   0    10599   7827  10905  -1528   -978   -868       C
ATOM   2796  C   ALA B   0     -87.012  70.118   1.334  1.00 72.65           C
ANISOU 2796  C   ALA B   0     9823   7412  10369  -1183   -734   -735       C
ATOM   2797  O   ALA B   0     -85.964  70.098   1.981  1.00 72.98           O
ANISOU 2797  O   ALA B   0     9505   7676  10549  -1156   -727   -572       O
ATOM   2798  CB  ALA B   0     -86.336  72.425   0.651  1.00 74.38           C
ANISOU 2798  CB  ALA B   0     9866   7699  10697  -1803  -1215   -729       C
ATOM   2799  N  AMET B   1     -87.822  69.065   1.238  0.56 70.10           N
ANISOU 2799  N  AMET B   1     9734   6976   9924   -919   -535   -802       N
ATOM   2800  N  BMET B   1     -87.842  69.081   1.245  0.44 70.09           N
ANISOU 2800  N  BMET B   1     9738   6970   9925   -922   -535   -803       N
ATOM   2801  CA AMET B   1     -87.510  67.811   1.913  0.56 65.53           C
ANISOU 2801  CA AMET B   1     8978   6545   9375   -638   -338   -674       C
ATOM   2802  CA BMET B   1     -87.515  67.801   1.857  0.44 65.52           C
ANISOU 2802  CA BMET B   1     8986   6544   9366   -637   -341   -680       C
ATOM   2803  C  AMET B   1     -86.378  67.090   1.189  0.56 60.74           C
ANISOU 2803  C  AMET B   1     8225   6194   8658   -547   -409   -639       C
ATOM   2804  C  BMET B   1     -86.310  67.184   1.158  0.44 60.86           C
ANISOU 2804  C  BMET B   1     8231   6217   8677   -568   -428   -639       C
ATOM   2805  O  AMET B   1     -86.422  66.910  -0.032  0.56 60.98           O
ANISOU 2805  O  AMET B   1     8440   6249   8479   -536   -488   -740       O
ATOM   2806  O  BMET B   1     -86.215  67.200  -0.074  0.44 61.43           O
ANISOU 2806  O  BMET B   1     8460   6327   8554   -601   -549   -736       O
ATOM   2807  CB AMET B   1     -88.753  66.922   1.979  0.56 66.51           C
ANISOU 2807  CB AMET B   1     9347   6502   9422   -393   -117   -713       C
ATOM   2808  CB BMET B   1     -88.733  66.871   1.797  0.44 66.66           C
ANISOU 2808  CB BMET B   1     9387   6528   9411   -386   -126   -730       C
ATOM   2809  CG AMET B   1     -88.656  65.772   2.972  0.56 63.96           C
ANISOU 2809  CG AMET B   1     8820   6309   9173   -168     61   -549       C
ATOM   2810  CG BMET B   1     -88.477  65.462   1.262  0.44 66.64           C
ANISOU 2810  CG BMET B   1     9354   6705   9263   -133    -19   -695       C
ATOM   2811  SD AMET B   1     -88.495  66.359   4.670  0.56 59.97           S
ANISOU 2811  SD AMET B   1     8087   5807   8893   -269     99   -393       S
ATOM   2812  SD BMET B   1     -88.718  65.335  -0.524  0.44 71.40           S
ANISOU 2812  SD BMET B   1    10281   7299   9550    -97    -72   -879       S
ATOM   2813  CE AMET B   1     -90.019  67.283   4.866  0.56 60.86           C
ANISOU 2813  CE AMET B   1     8496   5557   9070   -347    154   -434       C
ATOM   2814  CE BMET B   1     -88.607  63.563  -0.770  0.44 69.92           C
ANISOU 2814  CE BMET B   1     9984   7322   9261    222    140   -744       C
ATOM   2815  N   SER B   2     -85.369  66.669   1.948  1.00 51.76           N
ANISOU 2815  N   SER B   2     6787   5232   7647   -477   -371   -494       N
ATOM   2816  CA  SER B   2     -84.170  66.075   1.375  1.00 42.81           C
ANISOU 2816  CA  SER B   2     5504   4300   6462   -403   -443   -427       C
ATOM   2817  C   SER B   2     -83.483  65.198   2.406  1.00 36.59           C
ANISOU 2817  C   SER B   2     4510   3597   5796   -258   -312   -307       C
ATOM   2818  O   SER B   2     -83.654  65.373   3.615  1.00 36.84           O
ANISOU 2818  O   SER B   2     4454   3590   5954   -259   -213   -268       O
ATOM   2819  CB  SER B   2     -83.198  67.146   0.873  1.00 45.84           C
ANISOU 2819  CB  SER B   2     5723   4804   6889   -586   -674   -393       C
ATOM   2820  OG  SER B   2     -82.382  67.634   1.925  1.00 44.71           O
ANISOU 2820  OG  SER B   2     5280   4740   6969   -611   -651   -271       O
ATOM   2821  N   LEU B   3     -82.684  64.257   1.899  1.00 29.13           N
ANISOU 2821  N   LEU B   3     3512   2761   4794   -147   -320   -246       N
ATOM   2822  CA  LEU B   3     -81.906  63.385   2.771  1.00 30.67           C
ANISOU 2822  CA  LEU B   3     3556   3004   5095    -41   -229   -156       C
ATOM   2823  C   LEU B   3     -80.901  64.178   3.596  1.00 32.74           C
ANISOU 2823  C   LEU B   3     3609   3305   5527    -80   -255   -110       C
ATOM   2824  O   LEU B   3     -80.746  63.940   4.800  1.00 33.99           O
ANISOU 2824  O   LEU B   3     3701   3446   5766    -33   -139    -95       O
ATOM   2825  CB  LEU B   3     -81.192  62.325   1.934  1.00 33.64           C
ANISOU 2825  CB  LEU B   3     3934   3452   5396     48   -253    -82       C
ATOM   2826  CG  LEU B   3     -80.095  61.517   2.623  1.00 35.68           C
ANISOU 2826  CG  LEU B   3     4066   3717   5775    118   -212      3       C
ATOM   2827  CD1 LEU B   3     -80.682  60.611   3.694  1.00 38.69           C
ANISOU 2827  CD1 LEU B   3     4467   4055   6177    150    -84     -4       C
ATOM   2828  CD2 LEU B   3     -79.304  60.714   1.601  1.00 34.22           C
ANISOU 2828  CD2 LEU B   3     3889   3577   5536    168   -268    107       C
ATOM   2829  N   GLU B   4     -80.198  65.118   2.961  1.00 32.19           N
ANISOU 2829  N   GLU B   4     3426   3310   5495   -156   -402    -76       N
ATOM   2830  CA  GLU B   4     -79.207  65.912   3.677  1.00 28.54           C
ANISOU 2830  CA  GLU B   4     2718   2917   5209   -155   -398      1       C
ATOM   2831  C   GLU B   4     -79.853  66.798   4.732  1.00 26.80           C
ANISOU 2831  C   GLU B   4     2444   2665   5074   -257   -310    -15       C
ATOM   2832  O   GLU B   4     -79.245  67.063   5.775  1.00 28.48           O
ANISOU 2832  O   GLU B   4     2497   2923   5402   -195   -191     40       O
ATOM   2833  CB  GLU B   4     -78.399  66.757   2.691  1.00 34.88           C
ANISOU 2833  CB  GLU B   4     3365   3847   6043   -219   -599     87       C
ATOM   2834  CG  GLU B   4     -77.405  65.968   1.842  1.00 41.10           C
ANISOU 2834  CG  GLU B   4     4143   4684   6788    -83   -669    174       C
ATOM   2835  CD  GLU B   4     -78.068  65.126   0.763  1.00 46.79           C
ANISOU 2835  CD  GLU B   4     5114   5379   7283    -94   -719    121       C
ATOM   2836  OE1 GLU B   4     -79.300  65.233   0.585  1.00 46.94           O
ANISOU 2836  OE1 GLU B   4     5320   5339   7176   -189   -705     -2       O
ATOM   2837  OE2 GLU B   4     -77.353  64.355   0.090  1.00 48.70           O
ANISOU 2837  OE2 GLU B   4     5371   5654   7476      8   -752    216       O
ATOM   2838  N   ASN B   5     -81.080  67.260   4.486  1.00 29.62           N
ANISOU 2838  N   ASN B   5     2956   2930   5367   -401   -349    -84       N
ATOM   2839  CA  ASN B   5     -81.764  68.079   5.480  1.00 30.86           C
ANISOU 2839  CA  ASN B   5     3084   3028   5613   -512   -262    -65       C
ATOM   2840  C   ASN B   5     -82.230  67.236   6.659  1.00 28.17           C
ANISOU 2840  C   ASN B   5     2823   2633   5246   -380    -63    -65       C
ATOM   2841  O   ASN B   5     -82.165  67.681   7.811  1.00 35.78           O
ANISOU 2841  O   ASN B   5     3682   3630   6284   -390     57      2       O
ATOM   2842  CB  ASN B   5     -82.943  68.813   4.843  1.00 26.82           C
ANISOU 2842  CB  ASN B   5     2762   2372   5054   -711   -369   -141       C
ATOM   2843  CG  ASN B   5     -83.787  69.552   5.862  1.00 41.63           C
ANISOU 2843  CG  ASN B   5     4652   4135   7031   -829   -267    -96       C
ATOM   2844  OD1 ASN B   5     -84.901  69.136   6.180  1.00 38.89           O
ANISOU 2844  OD1 ASN B   5     4526   3623   6630   -779   -165   -137       O
ATOM   2845  ND2 ASN B   5     -83.255  70.649   6.388  1.00 40.49           N
ANISOU 2845  ND2 ASN B   5     4252   4091   7041   -973   -282     22       N
ATOM   2846  N   VAL B   6     -82.709  66.020   6.391  1.00 25.39           N
ANISOU 2846  N   VAL B   6     2643   2227   4776   -262    -29   -117       N
ATOM   2847  CA  VAL B   6     -83.095  65.123   7.475  1.00 26.46           C
ANISOU 2847  CA  VAL B   6     2824   2353   4876   -154    113    -94       C
ATOM   2848  C   VAL B   6     -81.899  64.840   8.373  1.00 28.78           C
ANISOU 2848  C   VAL B   6     2979   2747   5210    -78    179    -66       C
ATOM   2849  O   VAL B   6     -82.008  64.851   9.605  1.00 33.34           O
ANISOU 2849  O   VAL B   6     3541   3350   5775    -58    292    -37       O
ATOM   2850  CB  VAL B   6     -83.704  63.827   6.906  1.00 31.60           C
ANISOU 2850  CB  VAL B   6     3618   2974   5416    -49    121   -116       C
ATOM   2851  CG1 VAL B   6     -83.911  62.807   8.008  1.00 31.09           C
ANISOU 2851  CG1 VAL B   6     3546   2949   5319     36    214    -65       C
ATOM   2852  CG2 VAL B   6     -85.023  64.122   6.207  1.00 33.91           C
ANISOU 2852  CG2 VAL B   6     4093   3137   5653    -69    120   -159       C
ATOM   2853  N   ALA B   7     -80.733  64.605   7.768  1.00 30.82           N
ANISOU 2853  N   ALA B   7     3158   3051   5502    -22    117    -72       N
ATOM   2854  CA  ALA B   7     -79.532  64.346   8.551  1.00 26.15           C
ANISOU 2854  CA  ALA B   7     2481   2500   4956     82    197    -69       C
ATOM   2855  C   ALA B   7     -79.097  65.577   9.335  1.00 30.84           C
ANISOU 2855  C   ALA B   7     2905   3171   5642     72    293    -20       C
ATOM   2856  O   ALA B   7     -78.570  65.447  10.445  1.00 33.74           O
ANISOU 2856  O   ALA B   7     3262   3566   5991    164    437    -34       O
ATOM   2857  CB  ALA B   7     -78.406  63.866   7.637  1.00 24.75           C
ANISOU 2857  CB  ALA B   7     2269   2315   4821    162    113    -56       C
ATOM   2858  N   PHE B   8     -79.309  66.773   8.778  1.00 31.46           N
ANISOU 2858  N   PHE B   8     2853   3292   5807    -50    216     43       N
ATOM   2859  CA  PHE B   8     -78.978  67.993   9.506  1.00 31.11           C
ANISOU 2859  CA  PHE B   8     2595   3352   5874    -89    315    138       C
ATOM   2860  C   PHE B   8     -79.797  68.103  10.785  1.00 36.78           C
ANISOU 2860  C   PHE B   8     3390   4060   6525   -123    476    155       C
ATOM   2861  O   PHE B   8     -79.261  68.442  11.846  1.00 43.69           O
ANISOU 2861  O   PHE B   8     4163   5032   7406    -42    656    204       O
ATOM   2862  CB  PHE B   8     -79.205  69.216   8.617  1.00 29.40           C
ANISOU 2862  CB  PHE B   8     2227   3180   5765   -287    152    215       C
ATOM   2863  CG  PHE B   8     -79.042  70.528   9.335  1.00 32.38           C
ANISOU 2863  CG  PHE B   8     2344   3680   6280   -384    246    359       C
ATOM   2864  CD1 PHE B   8     -77.805  71.148   9.403  1.00 35.60           C
ANISOU 2864  CD1 PHE B   8     2436   4262   6826   -286    293    481       C
ATOM   2865  CD2 PHE B   8     -80.127  71.146   9.939  1.00 37.24           C
ANISOU 2865  CD2 PHE B   8     3013   4238   6900   -561    302    405       C
ATOM   2866  CE1 PHE B   8     -77.651  72.356  10.063  1.00 37.37           C
ANISOU 2866  CE1 PHE B   8     2372   4640   7188   -370    406    651       C
ATOM   2867  CE2 PHE B   8     -79.979  72.349  10.604  1.00 41.98           C
ANISOU 2867  CE2 PHE B   8     3352   4964   7633   -674    402    575       C
ATOM   2868  CZ  PHE B   8     -78.740  72.956  10.664  1.00 40.16           C
ANISOU 2868  CZ  PHE B   8     2776   4945   7537   -583    459    702       C
ATOM   2869  N   ASN B   9     -81.100  67.829  10.700  1.00 34.23           N
ANISOU 2869  N   ASN B   9     3254   3624   6126   -219    430    131       N
ATOM   2870  CA  ASN B   9     -81.947  67.904  11.885  1.00 30.80           C
ANISOU 2870  CA  ASN B   9     2900   3180   5625   -243    565    189       C
ATOM   2871  C   ASN B   9     -81.529  66.874  12.924  1.00 27.86           C
ANISOU 2871  C   ASN B   9     2612   2869   5106    -85    680    142       C
ATOM   2872  O   ASN B   9     -81.529  67.159  14.126  1.00 33.66           O
ANISOU 2872  O   ASN B   9     3333   3688   5768    -62    834    202       O
ATOM   2873  CB  ASN B   9     -83.412  67.710  11.496  1.00 30.02           C
ANISOU 2873  CB  ASN B   9     2995   2920   5490   -325    492    185       C
ATOM   2874  CG  ASN B   9     -84.017  68.944  10.863  1.00 25.78           C
ANISOU 2874  CG  ASN B   9     2439   2280   5076   -531    408    228       C
ATOM   2875  OD1 ASN B   9     -84.695  69.726  11.529  1.00 41.71           O
ANISOU 2875  OD1 ASN B   9     4458   4245   7146   -647    480    340       O
ATOM   2876  ND2 ASN B   9     -83.776  69.126   9.571  1.00 27.48           N
ANISOU 2876  ND2 ASN B   9     2654   2460   5326   -598    240    148       N
ATOM   2877  N   VAL B  10     -81.159  65.674  12.477  1.00 22.60           N
ANISOU 2877  N   VAL B  10     2045   2164   4379      5    601     39       N
ATOM   2878  CA  VAL B  10     -80.803  64.613  13.413  1.00 28.61           C
ANISOU 2878  CA  VAL B  10     2921   2957   4993     99    660    -25       C
ATOM   2879  C   VAL B  10     -79.553  64.987  14.200  1.00 33.62           C
ANISOU 2879  C   VAL B  10     3492   3666   5616    206    811    -63       C
ATOM   2880  O   VAL B  10     -79.492  64.800  15.421  1.00 37.34           O
ANISOU 2880  O   VAL B  10     4054   4204   5931    249    933    -85       O
ATOM   2881  CB  VAL B  10     -80.625  63.281  12.663  1.00 28.17           C
ANISOU 2881  CB  VAL B  10     2962   2831   4912    128    529   -101       C
ATOM   2882  CG1 VAL B  10     -80.018  62.232  13.579  1.00 29.56           C
ANISOU 2882  CG1 VAL B  10     3258   3019   4957    177    553   -185       C
ATOM   2883  CG2 VAL B  10     -81.960  62.804  12.118  1.00 20.05           C
ANISOU 2883  CG2 VAL B  10     1999   1762   3857     75    443    -49       C
ATOM   2884  N   VAL B  11     -78.544  65.533  13.521  1.00 33.93           N
ANISOU 2884  N   VAL B  11     3379   3706   5806    270    815    -61       N
ATOM   2885  CA  VAL B  11     -77.292  65.828  14.208  1.00 34.26           C
ANISOU 2885  CA  VAL B  11     3359   3802   5855    436    993    -93       C
ATOM   2886  C   VAL B  11     -77.420  67.071  15.084  1.00 34.81           C
ANISOU 2886  C   VAL B  11     3268   4027   5932    430   1190     27       C
ATOM   2887  O   VAL B  11     -76.738  67.181  16.109  1.00 37.71           O
ANISOU 2887  O   VAL B  11     3659   4468   6200    578   1406     -6       O
ATOM   2888  CB  VAL B  11     -76.140  65.967  13.196  1.00 40.29           C
ANISOU 2888  CB  VAL B  11     3986   4524   6798    547    938    -84       C
ATOM   2889  CG1 VAL B  11     -75.950  64.667  12.429  1.00 42.03           C
ANISOU 2889  CG1 VAL B  11     4383   4590   6998    551    774   -176       C
ATOM   2890  CG2 VAL B  11     -76.395  67.113  12.237  1.00 46.80           C
ANISOU 2890  CG2 VAL B  11     4555   5432   7796    434    832     62       C
ATOM   2891  N   ASN B  12     -78.289  68.011  14.719  1.00 34.81           N
ANISOU 2891  N   ASN B  12     3123   4069   6034    256   1131    169       N
ATOM   2892  CA  ASN B  12     -78.427  69.254  15.469  1.00 37.54           C
ANISOU 2892  CA  ASN B  12     3278   4563   6422    205   1310    332       C
ATOM   2893  C   ASN B  12     -79.560  69.230  16.482  1.00 40.75           C
ANISOU 2893  C   ASN B  12     3836   4985   6662    110   1387    395       C
ATOM   2894  O   ASN B  12     -79.459  69.892  17.520  1.00 46.02           O
ANISOU 2894  O   ASN B  12     4424   5798   7262    138   1610    507       O
ATOM   2895  CB  ASN B  12     -78.646  70.435  14.514  1.00 40.90           C
ANISOU 2895  CB  ASN B  12     3442   5015   7083     22   1185    479       C
ATOM   2896  CG  ASN B  12     -77.404  70.782  13.719  1.00 44.27           C
ANISOU 2896  CG  ASN B  12     3625   5514   7681    130   1142    503       C
ATOM   2897  OD1 ASN B  12     -76.539  71.522  14.188  1.00 49.34           O
ANISOU 2897  OD1 ASN B  12     4011   6323   8414    251   1329    618       O
ATOM   2898  ND2 ASN B  12     -77.315  70.256  12.504  1.00 41.21           N
ANISOU 2898  ND2 ASN B  12     3303   5021   7336    106    907    422       N
ATOM   2899  N   LYS B  13     -80.636  68.491  16.211  1.00 35.78           N
ANISOU 2899  N   LYS B  13     3408   4225   5962     17   1225    354       N
ATOM   2900  CA  LYS B  13     -81.799  68.476  17.086  1.00 33.36           C
ANISOU 2900  CA  LYS B  13     3232   3923   5522    -59   1274    459       C
ATOM   2901  C   LYS B  13     -82.097  67.106  17.677  1.00 32.87           C
ANISOU 2901  C   LYS B  13     3409   3855   5224     23   1225    361       C
ATOM   2902  O   LYS B  13     -83.081  66.969  18.412  1.00 35.43           O
ANISOU 2902  O   LYS B  13     3840   4202   5420    -18   1240    472       O
ATOM   2903  CB  LYS B  13     -83.035  68.984  16.333  1.00 35.64           C
ANISOU 2903  CB  LYS B  13     3529   4056   5957   -241   1138    558       C
ATOM   2904  CG  LYS B  13     -82.906  70.407  15.818  1.00 42.66           C
ANISOU 2904  CG  LYS B  13     4191   4946   7070   -406   1140    674       C
ATOM   2905  CD  LYS B  13     -82.770  71.398  16.963  1.00 49.15           C
ANISOU 2905  CD  LYS B  13     4858   5932   7886   -446   1370    873       C
ATOM   2906  CE  LYS B  13     -82.660  72.825  16.451  1.00 52.07           C
ANISOU 2906  CE  LYS B  13     4950   6324   8508   -658   1349   1028       C
ATOM   2907  NZ  LYS B  13     -82.610  73.811  17.567  1.00 55.06           N
ANISOU 2907  NZ  LYS B  13     5147   6879   8894   -716   1597   1272       N
ATOM   2908  N   GLY B  14     -81.281  66.093  17.389  1.00 33.28           N
ANISOU 2908  N   GLY B  14     3543   3878   5223    122   1153    182       N
ATOM   2909  CA  GLY B  14     -81.541  64.747  17.854  1.00 30.36           C
ANISOU 2909  CA  GLY B  14     3375   3508   4654    143   1058     98       C
ATOM   2910  C   GLY B  14     -82.624  64.012  17.099  1.00 32.31           C
ANISOU 2910  C   GLY B  14     3666   3661   4952     78    869    140       C
ATOM   2911  O   GLY B  14     -82.781  62.801  17.298  1.00 34.26           O
ANISOU 2911  O   GLY B  14     4020   3923   5073     81    758     93       O
ATOM   2912  N   HIS B  15     -83.368  64.696  16.243  1.00 31.34           N
ANISOU 2912  N   HIS B  15     3465   3441   5002     16    832    228       N
ATOM   2913  CA  HIS B  15     -84.451  64.123  15.448  1.00 24.45           C
ANISOU 2913  CA  HIS B  15     2648   2462   4181      0    705    266       C
ATOM   2914  C   HIS B  15     -84.829  65.165  14.401  1.00 23.00           C
ANISOU 2914  C   HIS B  15     2410   2142   4185    -75    686    288       C
ATOM   2915  O   HIS B  15     -84.193  66.221  14.301  1.00 26.25           O
ANISOU 2915  O   HIS B  15     2704   2572   4696   -137    736    290       O
ATOM   2916  CB  HIS B  15     -85.647  63.742  16.320  1.00 26.07           C
ANISOU 2916  CB  HIS B  15     2936   2706   4265     12    711    415       C
ATOM   2917  CG  HIS B  15     -86.385  64.922  16.869  1.00 30.32           C
ANISOU 2917  CG  HIS B  15     3470   3207   4842    -43    821    578       C
ATOM   2918  ND1 HIS B  15     -87.748  65.078  16.729  1.00 32.40           N
ANISOU 2918  ND1 HIS B  15     3803   3339   5170    -41    809    726       N
ATOM   2919  CD2 HIS B  15     -85.950  66.009  17.549  1.00 30.95           C
ANISOU 2919  CD2 HIS B  15     3483   3355   4921   -101    960    640       C
ATOM   2920  CE1 HIS B  15     -88.120  66.209  17.301  1.00 34.73           C
ANISOU 2920  CE1 HIS B  15     4092   3595   5508   -123    917    871       C
ATOM   2921  NE2 HIS B  15     -87.048  66.792  17.809  1.00 34.10           N
ANISOU 2921  NE2 HIS B  15     3911   3658   5387   -170   1012    833       N
ATOM   2922  N   PHE B  16     -85.873  64.884  13.628  1.00 29.38           N
ANISOU 2922  N   PHE B  16     3306   2820   5038    -71    615    308       N
ATOM   2923  CA  PHE B  16     -86.356  65.850  12.652  1.00 32.98           C
ANISOU 2923  CA  PHE B  16     3786   3113   5632   -165    578    296       C
ATOM   2924  C   PHE B  16     -87.167  66.924  13.367  1.00 36.14           C
ANISOU 2924  C   PHE B  16     4212   3429   6090   -266    661    442       C
ATOM   2925  O   PHE B  16     -88.196  66.629  13.983  1.00 38.80           O
ANISOU 2925  O   PHE B  16     4653   3711   6379   -208    710    562       O
ATOM   2926  CB  PHE B  16     -87.195  65.169  11.575  1.00 22.57           C
ANISOU 2926  CB  PHE B  16     2602   1664   4309    -94    510    244       C
ATOM   2927  CG  PHE B  16     -87.615  66.095  10.469  1.00 31.46           C
ANISOU 2927  CG  PHE B  16     3821   2606   5527   -201    450    175       C
ATOM   2928  CD1 PHE B  16     -86.741  66.406   9.440  1.00 31.10           C
ANISOU 2928  CD1 PHE B  16     3716   2593   5506   -275    342     62       C
ATOM   2929  CD2 PHE B  16     -88.878  66.665  10.463  1.00 28.58           C
ANISOU 2929  CD2 PHE B  16     3623   2021   5214   -236    487    227       C
ATOM   2930  CE1 PHE B  16     -87.119  67.263   8.423  1.00 30.59           C
ANISOU 2930  CE1 PHE B  16     3759   2377   5486   -410    247    -16       C
ATOM   2931  CE2 PHE B  16     -89.263  67.522   9.449  1.00 32.60           C
ANISOU 2931  CE2 PHE B  16     4273   2328   5787   -369    410    127       C
ATOM   2932  CZ  PHE B  16     -88.382  67.821   8.427  1.00 35.15           C
ANISOU 2932  CZ  PHE B  16     4536   2716   6102   -471    277     -2       C
ATOM   2933  N   ASP B  17     -86.700  68.170  13.287  1.00 36.66           N
ANISOU 2933  N   ASP B  17     4164   3494   6272   -423    672    466       N
ATOM   2934  CA  ASP B  17     -87.356  69.294  13.944  1.00 36.11           C
ANISOU 2934  CA  ASP B  17     4089   3344   6286   -569    754    634       C
ATOM   2935  C   ASP B  17     -87.788  70.366  12.951  1.00 39.33           C
ANISOU 2935  C   ASP B  17     4538   3540   6865   -784    646    609       C
ATOM   2936  O   ASP B  17     -88.146  71.475  13.365  1.00 45.12           O
ANISOU 2936  O   ASP B  17     5231   4198   7714   -974    689    754       O
ATOM   2937  CB  ASP B  17     -86.429  69.893  15.008  1.00 45.68           C
ANISOU 2937  CB  ASP B  17     5094   4785   7477   -596    895    741       C
ATOM   2938  CG  ASP B  17     -87.174  70.724  16.038  1.00 57.26           C
ANISOU 2938  CG  ASP B  17     6567   6226   8964   -702   1028    974       C
ATOM   2939  OD1 ASP B  17     -88.055  70.169  16.726  1.00 60.04           O
ANISOU 2939  OD1 ASP B  17     7076   6534   9202   -612   1074   1073       O
ATOM   2940  OD2 ASP B  17     -86.872  71.930  16.162  1.00 62.03           O
ANISOU 2940  OD2 ASP B  17     6997   6868   9702   -879   1084   1092       O
ATOM   2941  N   GLY B  18     -87.767  70.067  11.654  1.00 36.28           N
ANISOU 2941  N   GLY B  18     4244   3058   6482   -780    501    433       N
ATOM   2942  CA  GLY B  18     -88.177  71.030  10.654  1.00 35.54           C
ANISOU 2942  CA  GLY B  18     4243   2760   6500  -1005    363    369       C
ATOM   2943  C   GLY B  18     -87.212  72.168  10.416  1.00 39.69           C
ANISOU 2943  C   GLY B  18     4506   3424   7151  -1236    269    408       C
ATOM   2944  O   GLY B  18     -87.590  73.157   9.782  1.00 47.16           O
ANISOU 2944  O   GLY B  18     5510   4219   8191  -1495    130    391       O
ATOM   2945  N   GLN B  19     -85.980  72.065  10.904  1.00 38.67           N
ANISOU 2945  N   GLN B  19     4096   3581   7017  -1143    336    463       N
ATOM   2946  CA  GLN B  19     -84.996  73.115  10.698  1.00 33.63           C
ANISOU 2946  CA  GLN B  19     3144   3117   6516  -1310    269    543       C
ATOM   2947  C   GLN B  19     -84.376  73.000   9.309  1.00 39.01           C
ANISOU 2947  C   GLN B  19     3801   3837   7185  -1333     44    402       C
ATOM   2948  O   GLN B  19     -84.347  71.929   8.697  1.00 38.81           O
ANISOU 2948  O   GLN B  19     3946   3777   7023  -1153      2    253       O
ATOM   2949  CB  GLN B  19     -83.905  73.046  11.766  1.00 37.48           C
ANISOU 2949  CB  GLN B  19     3360   3883   6998  -1142    471    659       C
ATOM   2950  CG  GLN B  19     -84.433  72.956  13.190  1.00 42.79           C
ANISOU 2950  CG  GLN B  19     4090   4568   7599  -1075    702    790       C
ATOM   2951  CD  GLN B  19     -85.209  74.189  13.609  1.00 51.94           C
ANISOU 2951  CD  GLN B  19     5200   5634   8899  -1349    738    992       C
ATOM   2952  OE1 GLN B  19     -84.963  75.290  13.116  1.00 56.73           O
ANISOU 2952  OE1 GLN B  19     5657   6301   9597  -1552    614   1037       O
ATOM   2953  NE2 GLN B  19     -86.154  74.009  14.523  1.00 55.72           N
ANISOU 2953  NE2 GLN B  19     5858   6008   9303  -1321    871   1098       N
ATOM   2954  N   GLN B  20     -83.878  74.127   8.811  1.00 41.55           N
ANISOU 2954  N   GLN B  20     3886   4254   7646  -1571   -109    481       N
ATOM   2955  CA  GLN B  20     -83.217  74.165   7.516  1.00 47.83           C
ANISOU 2955  CA  GLN B  20     4619   5134   8418  -1618   -352    393       C
ATOM   2956  C   GLN B  20     -81.713  73.985   7.674  1.00 45.96           C
ANISOU 2956  C   GLN B  20     4041   5192   8231  -1411   -295    488       C
ATOM   2957  O   GLN B  20     -81.112  74.428   8.655  1.00 44.98           O
ANISOU 2957  O   GLN B  20     3650   5239   8201  -1340   -111    648       O
ATOM   2958  CB  GLN B  20     -83.506  75.481   6.790  1.00 56.13           C
ANISOU 2958  CB  GLN B  20     5674   6191   9462  -1940   -574    403       C
ATOM   2959  CG  GLN B  20     -84.845  75.517   6.077  1.00 67.57           C
ANISOU 2959  CG  GLN B  20     7559   7321  10793  -2106   -692    216       C
ATOM   2960  CD  GLN B  20     -84.962  76.692   5.128  1.00 87.16           C
ANISOU 2960  CD  GLN B  20    10059   9815  13241  -2425   -941    167       C
ATOM   2961  OE1 GLN B  20     -84.158  77.624   5.173  1.00 95.64           O
ANISOU 2961  OE1 GLN B  20    10787  11141  14411  -2550  -1019    317       O
ATOM   2962  NE2 GLN B  20     -85.963  76.652   4.256  1.00 92.62           N
ANISOU 2962  NE2 GLN B  20    11158  10237  13795  -2535  -1054    -51       N
ATOM   2963  N   GLY B  21     -81.113  73.335   6.692  1.00 44.12           N
ANISOU 2963  N   GLY B  21     3849   5009   7905  -1285   -433    394       N
ATOM   2964  CA  GLY B  21     -79.689  73.055   6.687  1.00 44.90           C
ANISOU 2964  CA  GLY B  21     3681   5326   8055  -1057   -392    478       C
ATOM   2965  C   GLY B  21     -79.419  71.692   6.079  1.00 39.35           C
ANISOU 2965  C   GLY B  21     3202   4558   7190   -826   -410    340       C
ATOM   2966  O   GLY B  21     -80.282  70.818   6.026  1.00 35.40           O
ANISOU 2966  O   GLY B  21     3019   3888   6544   -781   -368    201       O
ATOM   2967  N   GLU B  22     -78.189  71.511   5.604  1.00 40.81           N
ANISOU 2967  N   GLU B  22     3198   4889   7417   -671   -469    414       N
ATOM   2968  CA  GLU B  22     -77.776  70.259   4.989  1.00 40.32           C
ANISOU 2968  CA  GLU B  22     3316   4774   7231   -470   -490    333       C
ATOM   2969  C   GLU B  22     -76.400  69.869   5.505  1.00 40.76           C
ANISOU 2969  C   GLU B  22     3187   4907   7392   -191   -344    424       C
ATOM   2970  O   GLU B  22     -75.565  70.726   5.805  1.00 46.42           O
ANISOU 2970  O   GLU B  22     3580   5780   8277   -143   -308    579       O
ATOM   2971  CB  GLU B  22     -77.742  70.354   3.455  1.00 47.27           C
ANISOU 2971  CB  GLU B  22     4253   5699   8008   -583   -778    326       C
ATOM   2972  CG  GLU B  22     -79.106  70.417   2.786  1.00 52.50           C
ANISOU 2972  CG  GLU B  22     5228   6223   8498   -797   -899    169       C
ATOM   2973  CD  GLU B  22     -79.690  71.815   2.770  1.00 65.55           C
ANISOU 2973  CD  GLU B  22     6796   7880  10230  -1115  -1042    190       C
ATOM   2974  OE1 GLU B  22     -78.971  72.767   3.138  1.00 72.24           O
ANISOU 2974  OE1 GLU B  22     7280   8899  11269  -1189  -1078    363       O
ATOM   2975  OE2 GLU B  22     -80.870  71.961   2.387  1.00 69.31           O
ANISOU 2975  OE2 GLU B  22     7568   8179  10588  -1291  -1111     43       O
ATOM   2976  N   VAL B  23     -76.175  68.562   5.608  1.00 35.38           N
ANISOU 2976  N   VAL B  23     2715   4106   6620     -7   -252    335       N
ATOM   2977  CA  VAL B  23     -74.866  68.016   5.959  1.00 35.92           C
ANISOU 2977  CA  VAL B  23     2707   4166   6773    259   -129    385       C
ATOM   2978  C   VAL B  23     -74.531  66.910   4.963  1.00 38.38           C
ANISOU 2978  C   VAL B  23     3192   4390   7000    334   -246    371       C
ATOM   2979  O   VAL B  23     -75.443  66.240   4.457  1.00 37.15           O
ANISOU 2979  O   VAL B  23     3263   4163   6688    226   -316    280       O
ATOM   2980  CB  VAL B  23     -74.836  67.498   7.407  1.00 32.33           C
ANISOU 2980  CB  VAL B  23     2360   3624   6300    387    135    291       C
ATOM   2981  CG1 VAL B  23     -75.011  68.646   8.390  1.00 34.86           C
ANISOU 2981  CG1 VAL B  23     2480   4068   6699    340    283    356       C
ATOM   2982  CG2 VAL B  23     -75.906  66.448   7.620  1.00 30.48           C
ANISOU 2982  CG2 VAL B  23     2430   3256   5894    304    143    147       C
ATOM   2983  N   PRO B  24     -73.256  66.689   4.645  1.00 42.19           N
ANISOU 2983  N   PRO B  24     3573   4871   7586    531   -252    482       N
ATOM   2984  CA  PRO B  24     -72.915  65.653   3.663  1.00 40.46           C
ANISOU 2984  CA  PRO B  24     3515   4566   7293    585   -362    513       C
ATOM   2985  C   PRO B  24     -73.211  64.259   4.196  1.00 35.15           C
ANISOU 2985  C   PRO B  24     3122   3697   6534    612   -236    379       C
ATOM   2986  O   PRO B  24     -72.959  63.952   5.364  1.00 35.02           O
ANISOU 2986  O   PRO B  24     3163   3579   6565    702    -57    290       O
ATOM   2987  CB  PRO B  24     -71.415  65.864   3.432  1.00 43.37           C
ANISOU 2987  CB  PRO B  24     3690   4950   7839    818   -363    694       C
ATOM   2988  CG  PRO B  24     -70.932  66.523   4.681  1.00 44.58           C
ANISOU 2988  CG  PRO B  24     3696   5124   8118    949   -142    677       C
ATOM   2989  CD  PRO B  24     -72.063  67.396   5.143  1.00 44.47           C
ANISOU 2989  CD  PRO B  24     3586   5237   8075    734   -142    614       C
ATOM   2990  N   VAL B  25     -73.751  63.411   3.322  1.00 30.30           N
ANISOU 2990  N   VAL B  25     2679   3055   5780    525   -335    374       N
ATOM   2991  CA  VAL B  25     -74.236  62.088   3.696  1.00 29.35           C
ANISOU 2991  CA  VAL B  25     2775   2800   5575    496   -252    284       C
ATOM   2992  C   VAL B  25     -73.648  61.051   2.749  1.00 31.96           C
ANISOU 2992  C   VAL B  25     3198   3060   5887    537   -321    401       C
ATOM   2993  O   VAL B  25     -73.572  61.275   1.536  1.00 32.43           O
ANISOU 2993  O   VAL B  25     3224   3223   5876    521   -456    518       O
ATOM   2994  CB  VAL B  25     -75.778  62.027   3.673  1.00 31.13           C
ANISOU 2994  CB  VAL B  25     3101   3083   5646    343   -254    188       C
ATOM   2995  CG1 VAL B  25     -76.268  60.608   3.921  1.00 28.47           C
ANISOU 2995  CG1 VAL B  25     2922   2662   5234    319   -190    156       C
ATOM   2996  CG2 VAL B  25     -76.362  62.980   4.702  1.00 27.93           C
ANISOU 2996  CG2 VAL B  25     2626   2713   5273    292   -174    104       C
ATOM   2997  N   SER B  26     -73.230  59.917   3.308  1.00 33.86           N
ANISOU 2997  N   SER B  26     3566   3123   6176    567   -240    377       N
ATOM   2998  CA  SER B  26     -72.782  58.764   2.539  1.00 32.24           C
ANISOU 2998  CA  SER B  26     3463   2819   5966    559   -287    504       C
ATOM   2999  C   SER B  26     -73.672  57.574   2.861  1.00 30.85           C
ANISOU 2999  C   SER B  26     3408   2614   5699    417   -244    449       C
ATOM   3000  O   SER B  26     -73.889  57.257   4.035  1.00 31.22           O
ANISOU 3000  O   SER B  26     3512   2584   5766    375   -172    316       O
ATOM   3001  CB  SER B  26     -71.322  58.422   2.842  1.00 33.28           C
ANISOU 3001  CB  SER B  26     3640   2721   6283    703   -250    565       C
ATOM   3002  OG  SER B  26     -70.447  59.391   2.298  1.00 46.35           O
ANISOU 3002  OG  SER B  26     5142   4432   8037    867   -302    697       O
ATOM   3003  N   ILE B  27     -74.181  56.918   1.823  1.00 29.32           N
ANISOU 3003  N   ILE B  27     3240   2509   5392    348   -286    570       N
ATOM   3004  CA  ILE B  27     -75.006  55.724   1.962  1.00 25.18           C
ANISOU 3004  CA  ILE B  27     2767   2003   4799    228   -240    586       C
ATOM   3005  C   ILE B  27     -74.201  54.526   1.482  1.00 31.79           C
ANISOU 3005  C   ILE B  27     3658   2711   5711    177   -264    763       C
ATOM   3006  O   ILE B  27     -73.706  54.518   0.348  1.00 35.28           O
ANISOU 3006  O   ILE B  27     4098   3184   6125    224   -308    937       O
ATOM   3007  CB  ILE B  27     -76.320  55.847   1.174  1.00 29.26           C
ANISOU 3007  CB  ILE B  27     3266   2729   5125    209   -217    602       C
ATOM   3008  CG1 ILE B  27     -77.153  57.016   1.701  1.00 35.69           C
ANISOU 3008  CG1 ILE B  27     4060   3609   5891    229   -199    430       C
ATOM   3009  CG2 ILE B  27     -77.106  54.548   1.252  1.00 22.86           C
ANISOU 3009  CG2 ILE B  27     2449   1968   4269    123   -148    678       C
ATOM   3010  CD1 ILE B  27     -77.527  56.887   3.155  1.00 38.60           C
ANISOU 3010  CD1 ILE B  27     4422   3918   6326    191   -137    312       C
ATOM   3011  N   ILE B  28     -74.073  53.518   2.341  1.00 25.36           N
ANISOU 3011  N   ILE B  28     2900   1753   4982     58   -252    734       N
ATOM   3012  CA  ILE B  28     -73.377  52.287   1.986  1.00 36.57           C
ANISOU 3012  CA  ILE B  28     4381   3017   6499    -53   -285    909       C
ATOM   3013  C   ILE B  28     -73.810  51.211   2.971  1.00 34.12           C
ANISOU 3013  C   ILE B  28     4092   2654   6219   -257   -300    854       C
ATOM   3014  O   ILE B  28     -74.016  51.485   4.157  1.00 33.16           O
ANISOU 3014  O   ILE B  28     4012   2498   6089   -272   -300    648       O
ATOM   3015  CB  ILE B  28     -71.841  52.492   1.969  1.00 39.90           C
ANISOU 3015  CB  ILE B  28     4915   3155   7091     50   -316    940       C
ATOM   3016  CG1 ILE B  28     -71.127  51.248   1.437  1.00 38.60           C
ANISOU 3016  CG1 ILE B  28     4835   2806   7026    -77   -353   1156       C
ATOM   3017  CG2 ILE B  28     -71.321  52.871   3.343  1.00 39.69           C
ANISOU 3017  CG2 ILE B  28     4995   2932   7153    102   -286    694       C
ATOM   3018  CD1 ILE B  28     -69.622  51.380   1.403  1.00 47.55           C
ANISOU 3018  CD1 ILE B  28     6109   3715   8242     49   -353   1152       C
ATOM   3019  N  AASN B  29     -74.021  49.998   2.462  0.50 39.86           N
ANISOU 3019  N  AASN B  29     4765   3418   6960   -425   -318   1061       N
ATOM   3020  N  BASN B  29     -73.881  49.979   2.479  0.50 40.33           N
ANISOU 3020  N  BASN B  29     4842   3447   7037   -427   -324   1062       N
ATOM   3021  CA AASN B  29     -74.301  48.822   3.295  0.50 43.39           C
ANISOU 3021  CA AASN B  29     5199   3824   7462   -675   -381   1068       C
ATOM   3022  CA BASN B  29     -74.519  48.845   3.156  0.50 43.15           C
ANISOU 3022  CA BASN B  29     5133   3856   7406   -662   -366   1091       C
ATOM   3023  C  AASN B  29     -75.479  49.040   4.251  0.50 41.40           C
ANISOU 3023  C  AASN B  29     4857   3773   7100   -687   -372    918       C
ATOM   3024  C  BASN B  29     -75.981  49.252   3.352  0.50 41.16           C
ANISOU 3024  C  BASN B  29     4727   3912   7000   -586   -298   1034       C
ATOM   3025  O  AASN B  29     -75.408  48.719   5.439  0.50 40.01           O
ANISOU 3025  O  AASN B  29     4755   3504   6942   -822   -454    775       O
ATOM   3026  O  BASN B  29     -76.576  49.861   2.451  0.50 38.87           O
ANISOU 3026  O  BASN B  29     4371   3806   6594   -423   -206   1087       O
ATOM   3027  CB AASN B  29     -73.052  48.406   4.078  0.50 50.12           C
ANISOU 3027  CB AASN B  29     6275   4324   8444   -783   -466    948       C
ATOM   3028  CB BASN B  29     -73.761  48.480   4.424  0.50 45.86           C
ANISOU 3028  CB BASN B  29     5658   3913   7856   -807   -465    909       C
ATOM   3029  CG AASN B  29     -71.860  48.141   3.183  0.50 55.02           C
ANISOU 3029  CG AASN B  29     7002   4773   9131   -734   -457   1090       C
ATOM   3030  CG BASN B  29     -72.280  48.249   4.174  0.50 53.33           C
ANISOU 3030  CG BASN B  29     6808   4573   8884   -785   -481    909       C
ATOM   3031  OD1AASN B  29     -70.784  48.706   3.381  0.50 57.15           O
ANISOU 3031  OD1AASN B  29     7443   4828   9442   -581   -436    969       O
ATOM   3032  OD1BASN B  29     -71.897  47.558   3.230  0.50 56.27           O
ANISOU 3032  OD1BASN B  29     7156   4928   9295   -849   -484   1135       O
ATOM   3033  ND2AASN B  29     -72.044  47.277   2.192  0.50 58.59           N
ANISOU 3033  ND2AASN B  29     7341   5334   9587   -850   -454   1371       N
ATOM   3034  ND2BASN B  29     -71.439  48.840   5.017  0.50 53.44           N
ANISOU 3034  ND2BASN B  29     7025   4376   8904   -670   -463    666       N
ATOM   3035  N  AASN B  30     -76.578  49.588   3.722  0.50 36.06           N
ANISOU 3035  N  AASN B  30     4045   3363   6294   -542   -276    953       N
ATOM   3036  N  BASN B  30     -76.587  48.940   4.491  0.50 36.88           N
ANISOU 3036  N  BASN B  30     4150   3423   6441   -696   -346    932       N
ATOM   3037  CA AASN B  30     -77.833  49.749   4.470  0.50 33.27           C
ANISOU 3037  CA AASN B  30     3591   3204   5847   -524   -248    876       C
ATOM   3038  CA BASN B  30     -77.878  49.511   4.859  0.50 32.90           C
ANISOU 3038  CA BASN B  30     3539   3150   5812   -584   -279    862       C
ATOM   3039  C  AASN B  30     -77.640  50.553   5.757  0.50 29.19           C
ANISOU 3039  C  AASN B  30     3195   2582   5316   -493   -284    620       C
ATOM   3040  C  BASN B  30     -77.703  50.624   5.877  0.50 29.14           C
ANISOU 3040  C  BASN B  30     3190   2580   5301   -488   -284    601       C
ATOM   3041  O  AASN B  30     -78.354  50.360   6.744  0.50 28.06           O
ANISOU 3041  O  AASN B  30     3010   2534   5119   -559   -318    568       O
ATOM   3042  O  BASN B  30     -78.496  50.739   6.815  0.50 27.78           O
ANISOU 3042  O  BASN B  30     2981   2514   5059   -503   -292    526       O
ATOM   3043  CB AASN B  30     -78.472  48.390   4.775  0.50 37.18           C
ANISOU 3043  CB AASN B  30     3920   3839   6370   -724   -299   1053       C
ATOM   3044  CB BASN B  30     -78.805  48.426   5.401  0.50 37.07           C
ANISOU 3044  CB BASN B  30     3892   3860   6334   -746   -327    992       C
ATOM   3045  CG AASN B  30     -79.974  48.385   4.550  0.50 36.92           C
ANISOU 3045  CG AASN B  30     3692   4099   6238   -601   -186   1158       C
ATOM   3046  CG BASN B  30     -80.054  48.245   4.560  0.50 37.17           C
ANISOU 3046  CG BASN B  30     3698   4151   6272   -616   -188   1183       C
ATOM   3047  OD1AASN B  30     -80.519  49.271   3.891  0.50 34.81           O
ANISOU 3047  OD1AASN B  30     3451   3903   5874   -382    -58   1112       O
ATOM   3048  OD1BASN B  30     -80.522  49.181   3.910  0.50 35.40           O
ANISOU 3048  OD1BASN B  30     3515   3982   5953   -395    -63   1124       O
ATOM   3049  ND2AASN B  30     -80.649  47.378   5.092  0.50 39.95           N
ANISOU 3049  ND2AASN B  30     3885   4645   6650   -743   -240   1306       N
ATOM   3050  ND2BASN B  30     -80.604  47.036   4.573  0.50 40.79           N
ANISOU 3050  ND2BASN B  30     3937   4787   6773   -756   -207   1416       N
ATOM   3051  N   THR B  31     -76.668  51.457   5.740  1.00 29.63           N
ANISOU 3051  N   THR B  31     3382   2463   5411   -379   -269    490       N
ATOM   3052  CA  THR B  31     -76.334  52.366   6.825  1.00 28.05           C
ANISOU 3052  CA  THR B  31     3288   2175   5195   -304   -251    268       C
ATOM   3053  C   THR B  31     -76.186  53.781   6.284  1.00 28.14           C
ANISOU 3053  C   THR B  31     3272   2217   5202   -103   -175    223       C
ATOM   3054  O   THR B  31     -75.724  53.979   5.157  1.00 30.29           O
ANISOU 3054  O   THR B  31     3520   2474   5513    -32   -180    330       O
ATOM   3055  CB  THR B  31     -75.039  51.923   7.527  1.00 30.83           C
ANISOU 3055  CB  THR B  31     3834   2248   5634   -376   -304    158       C
ATOM   3056  OG1 THR B  31     -75.143  50.540   7.892  1.00 33.63           O
ANISOU 3056  OG1 THR B  31     4215   2563   5999   -630   -421    217       O
ATOM   3057  CG2 THR B  31     -74.790  52.748   8.782  1.00 30.68           C
ANISOU 3057  CG2 THR B  31     3931   2174   5551   -288   -247    -73       C
ATOM   3058  N   VAL B  32     -76.596  54.758   7.089  1.00 27.18           N
ANISOU 3058  N   VAL B  32     3144   2157   5026    -32   -121     89       N
ATOM   3059  CA  VAL B  32     -76.462  56.171   6.756  1.00 27.00           C
ANISOU 3059  CA  VAL B  32     3068   2173   5018    110    -69     51       C
ATOM   3060  C   VAL B  32     -75.290  56.741   7.541  1.00 29.11           C
ANISOU 3060  C   VAL B  32     3397   2300   5363    205    -17    -62       C
ATOM   3061  O   VAL B  32     -75.236  56.614   8.771  1.00 26.90           O
ANISOU 3061  O   VAL B  32     3208   1977   5037    181     27   -187       O
ATOM   3062  CB  VAL B  32     -77.755  56.944   7.065  1.00 29.56           C
ANISOU 3062  CB  VAL B  32     3329   2651   5250    117    -23     14       C
ATOM   3063  CG1 VAL B  32     -77.636  58.384   6.589  1.00 30.92           C
ANISOU 3063  CG1 VAL B  32     3433   2864   5452    199     -5     -3       C
ATOM   3064  CG2 VAL B  32     -78.953  56.261   6.429  1.00 27.59           C
ANISOU 3064  CG2 VAL B  32     3044   2516   4923     72    -32    115       C
ATOM   3065  N   TYR B  33     -74.353  57.367   6.834  1.00 28.37           N
ANISOU 3065  N   TYR B  33     3256   2151   5373    331    -16     -6       N
ATOM   3066  CA  TYR B  33     -73.195  57.994   7.448  1.00 24.34           C
ANISOU 3066  CA  TYR B  33     2766   1519   4962    488     70    -77       C
ATOM   3067  C   TYR B  33     -73.197  59.489   7.160  1.00 26.15           C
ANISOU 3067  C   TYR B  33     2798   1904   5233    598    103    -32       C
ATOM   3068  O   TYR B  33     -73.835  59.964   6.217  1.00 24.29           O
ANISOU 3068  O   TYR B  33     2451   1816   4964    542     16     57       O
ATOM   3069  CB  TYR B  33     -71.882  57.385   6.938  1.00 26.28           C
ANISOU 3069  CB  TYR B  33     3105   1536   5344    572     45     -5       C
ATOM   3070  CG  TYR B  33     -71.716  55.914   7.231  1.00 27.10           C
ANISOU 3070  CG  TYR B  33     3412   1446   5437    420     -6    -38       C
ATOM   3071  CD1 TYR B  33     -72.218  54.955   6.364  1.00 31.88           C
ANISOU 3071  CD1 TYR B  33     3999   2090   6023    258   -112    109       C
ATOM   3072  CD2 TYR B  33     -71.043  55.484   8.367  1.00 28.91           C
ANISOU 3072  CD2 TYR B  33     3860   1494   5632    420     51   -208       C
ATOM   3073  CE1 TYR B  33     -72.064  53.609   6.624  1.00 36.42           C
ANISOU 3073  CE1 TYR B  33     4718   2502   6618     74   -176    115       C
ATOM   3074  CE2 TYR B  33     -70.883  54.138   8.635  1.00 49.12           C
ANISOU 3074  CE2 TYR B  33     6615   3876   8172    225    -35   -240       C
ATOM   3075  CZ  TYR B  33     -71.396  53.204   7.759  1.00 43.82           C
ANISOU 3075  CZ  TYR B  33     5873   3241   7537     38   -157    -65       C
ATOM   3076  OH  TYR B  33     -71.240  51.861   8.018  1.00 42.56           O
ANISOU 3076  OH  TYR B  33     5866   2937   7369   -196   -254    -64       O
ATOM   3077  N   THR B  34     -72.465  60.228   7.989  1.00 26.90           N
ANISOU 3077  N   THR B  34     2856   1969   5397    748    233    -94       N
ATOM   3078  CA  THR B  34     -72.220  61.641   7.752  1.00 33.70           C
ANISOU 3078  CA  THR B  34     3476   2982   6347    853    266     -8       C
ATOM   3079  C   THR B  34     -70.784  61.954   8.142  1.00 31.14           C
ANISOU 3079  C   THR B  34     3140   2577   6114   1081    391      6       C
ATOM   3080  O   THR B  34     -70.197  61.288   8.998  1.00 30.84           O
ANISOU 3080  O   THR B  34     3322   2375   6020   1149    497   -121       O
ATOM   3081  CB  THR B  34     -73.196  62.540   8.530  1.00 39.51           C
ANISOU 3081  CB  THR B  34     4120   3889   7005    767    340    -62       C
ATOM   3082  OG1 THR B  34     -73.099  63.884   8.043  1.00 37.26           O
ANISOU 3082  OG1 THR B  34     3567   3770   6819    789    312     62       O
ATOM   3083  CG2 THR B  34     -72.879  62.525  10.019  1.00 42.06           C
ANISOU 3083  CG2 THR B  34     4542   4161   7276    860    541   -192       C
ATOM   3084  N   LYS B  35     -70.218  62.966   7.493  1.00 33.96           N
ANISOU 3084  N   LYS B  35     3261   3074   6571   1184    360    165       N
ATOM   3085  CA  LYS B  35     -68.828  63.336   7.712  1.00 38.10           C
ANISOU 3085  CA  LYS B  35     3752   3570   7154   1419    469    220       C
ATOM   3086  C   LYS B  35     -68.753  64.351   8.846  1.00 43.01           C
ANISOU 3086  C   LYS B  35     4246   4328   7769   1520    671    173       C
ATOM   3087  O   LYS B  35     -69.368  65.420   8.772  1.00 45.55           O
ANISOU 3087  O   LYS B  35     4306   4871   8132   1434    653    262       O
ATOM   3088  CB  LYS B  35     -68.209  63.896   6.431  1.00 45.16           C
ANISOU 3088  CB  LYS B  35     4433   4577   8150   1483    321    449       C
ATOM   3089  CG  LYS B  35     -66.745  63.522   6.247  1.00 53.36           C
ANISOU 3089  CG  LYS B  35     5567   5462   9246   1712    367    516       C
ATOM   3090  CD  LYS B  35     -66.287  63.670   4.800  1.00 59.86           C
ANISOU 3090  CD  LYS B  35     6249   6362  10134   1732    172    754       C
ATOM   3091  CE  LYS B  35     -66.025  65.120   4.430  1.00 67.22           C
ANISOU 3091  CE  LYS B  35     6814   7583  11142   1794    119    931       C
ATOM   3092  NZ  LYS B  35     -65.387  65.240   3.088  1.00 69.43           N
ANISOU 3092  NZ  LYS B  35     6976   7943  11462   1842    -77   1171       N
ATOM   3093  N   VAL B  36     -68.016  64.009   9.894  1.00 48.23           N
ANISOU 3093  N   VAL B  36     5104   4854   8367   1687    858     35       N
ATOM   3094  CA  VAL B  36     -67.801  64.896  11.035  1.00 50.63           C
ANISOU 3094  CA  VAL B  36     5314   5289   8634   1823   1089     -8       C
ATOM   3095  C   VAL B  36     -66.297  65.119  11.129  1.00 59.02           C
ANISOU 3095  C   VAL B  36     6373   6290   9763   2119   1203     29       C
ATOM   3096  O   VAL B  36     -65.568  64.320  11.725  1.00 63.93           O
ANISOU 3096  O   VAL B  36     7298   6673  10319   2255   1294   -137       O
ATOM   3097  CB  VAL B  36     -68.369  64.328  12.337  1.00 45.53           C
ANISOU 3097  CB  VAL B  36     4931   4557   7811   1771   1231   -235       C
ATOM   3098  CG1 VAL B  36     -68.128  65.298  13.481  1.00 47.90           C
ANISOU 3098  CG1 VAL B  36     5127   5027   8047   1922   1490   -252       C
ATOM   3099  CG2 VAL B  36     -69.849  64.042  12.184  1.00 34.75           C
ANISOU 3099  CG2 VAL B  36     3562   3235   6406   1498   1110   -257       C
ATOM   3100  N   ASP B  37     -65.826  66.215  10.530  1.00 63.53           N
ANISOU 3100  N   ASP B  37     6600   7068  10472   2211   1182    247       N
ATOM   3101  CA  ASP B  37     -64.409  66.579  10.531  1.00 68.39           C
ANISOU 3101  CA  ASP B  37     7140   7657  11187   2512   1290    326       C
ATOM   3102  C   ASP B  37     -63.548  65.466   9.936  1.00 63.14           C
ANISOU 3102  C   ASP B  37     6744   6688  10560   2616   1196    294       C
ATOM   3103  O   ASP B  37     -62.596  64.986  10.554  1.00 66.98           O
ANISOU 3103  O   ASP B  37     7463   6947  11038   2831   1336    163       O
ATOM   3104  CB  ASP B  37     -63.932  66.951  11.938  1.00 81.33           C
ANISOU 3104  CB  ASP B  37     8838   9310  12754   2716   1593    193       C
ATOM   3105  CG  ASP B  37     -64.381  68.337  12.359  1.00 92.05           C
ANISOU 3105  CG  ASP B  37     9829  11011  14134   2676   1709    333       C
ATOM   3106  OD1 ASP B  37     -64.306  69.267  11.528  1.00 95.92           O
ANISOU 3106  OD1 ASP B  37     9955  11719  14771   2634   1589    578       O
ATOM   3107  OD2 ASP B  37     -64.812  68.496  13.520  1.00 94.95           O
ANISOU 3107  OD2 ASP B  37    10277  11436  14364   2666   1907    208       O
ATOM   3108  N   GLY B  38     -63.898  65.049   8.719  1.00 58.11           N
ANISOU 3108  N   GLY B  38     6084   6035   9962   2453    954    418       N
ATOM   3109  CA  GLY B  38     -63.081  64.163   7.927  1.00 66.10           C
ANISOU 3109  CA  GLY B  38     7276   6808  11032   2533    845    475       C
ATOM   3110  C   GLY B  38     -63.549  62.720   7.876  1.00 69.11           C
ANISOU 3110  C   GLY B  38     8020   6922  11318   2345    753    329       C
ATOM   3111  O   GLY B  38     -63.401  62.073   6.833  1.00 72.48           O
ANISOU 3111  O   GLY B  38     8507   7251  11784   2277    590    454       O
ATOM   3112  N   VAL B  39     -64.100  62.195   8.968  1.00 49.82           N
ANISOU 3112  N   VAL B  39     5586   6061   7282   1355    524    700       N
ATOM   3113  CA  VAL B  39     -64.429  60.777   9.063  1.00 41.25           C
ANISOU 3113  CA  VAL B  39     4681   4868   6125   1299    459    602       C
ATOM   3114  C   VAL B  39     -65.939  60.593   9.040  1.00 35.28           C
ANISOU 3114  C   VAL B  39     3899   4116   5391   1144    418    558       C
ATOM   3115  O   VAL B  39     -66.707  61.482   9.424  1.00 31.98           O
ANISOU 3115  O   VAL B  39     3374   3760   5017   1112    464    591       O
ATOM   3116  CB  VAL B  39     -63.822  60.135  10.328  1.00 41.56           C
ANISOU 3116  CB  VAL B  39     4908   4818   6065   1435    515    570       C
ATOM   3117  CG1 VAL B  39     -62.305  60.111  10.232  1.00 46.22           C
ANISOU 3117  CG1 VAL B  39     5555   5380   6625   1590    540    601       C
ATOM   3118  CG2 VAL B  39     -64.272  60.885  11.571  1.00 38.45           C
ANISOU 3118  CG2 VAL B  39     4491   4466   5654   1500    625    602       C
ATOM   3119  N   ASP B  40     -66.361  59.415   8.585  1.00 34.60           N
ANISOU 3119  N   ASP B  40     3909   3960   5278   1052    333    490       N
ATOM   3120  CA  ASP B  40     -67.774  59.074   8.529  1.00 34.39           C
ANISOU 3120  CA  ASP B  40     3872   3928   5266    916    294    446       C
ATOM   3121  C   ASP B  40     -68.236  58.543   9.880  1.00 34.80           C
ANISOU 3121  C   ASP B  40     4043   3917   5262    940    328    409       C
ATOM   3122  O   ASP B  40     -67.587  57.674  10.471  1.00 33.00           O
ANISOU 3122  O   ASP B  40     3968   3602   4968   1008    317    379       O
ATOM   3123  CB  ASP B  40     -68.030  58.035   7.438  1.00 36.45           C
ANISOU 3123  CB  ASP B  40     4172   4151   5528    817    200    408       C
ATOM   3124  CG  ASP B  40     -67.657  58.536   6.059  1.00 44.56           C
ANISOU 3124  CG  ASP B  40     5096   5241   6595    792    158    441       C
ATOM   3125  OD1 ASP B  40     -67.842  59.743   5.795  1.00 48.39           O
ANISOU 3125  OD1 ASP B  40     5446   5807   7131    784    176    480       O
ATOM   3126  OD2 ASP B  40     -67.177  57.726   5.239  1.00 49.33           O
ANISOU 3126  OD2 ASP B  40     5753   5810   7180    777    102    434       O
ATOM   3127  N   VAL B  41     -69.355  59.071  10.367  1.00 31.48           N
ANISOU 3127  N   VAL B  41     3560   3534   4868    884    359    412       N
ATOM   3128  CA  VAL B  41     -69.966  58.631  11.614  1.00 28.86           C
ANISOU 3128  CA  VAL B  41     3330   3151   4483    895    385    381       C
ATOM   3129  C   VAL B  41     -71.324  58.034  11.283  1.00 29.02           C
ANISOU 3129  C   VAL B  41     3340   3154   4531    751    320    338       C
ATOM   3130  O   VAL B  41     -72.127  58.661  10.582  1.00 25.63           O
ANISOU 3130  O   VAL B  41     2787   2785   4168    665    310    352       O
ATOM   3131  CB  VAL B  41     -70.105  59.788  12.621  1.00 29.92           C
ANISOU 3131  CB  VAL B  41     3403   3345   4619    971    493    436       C
ATOM   3132  CG1 VAL B  41     -70.656  59.280  13.944  1.00 25.58           C
ANISOU 3132  CG1 VAL B  41     2983   2738   3996    997    517    403       C
ATOM   3133  CG2 VAL B  41     -68.767  60.475  12.824  1.00 26.71           C
ANISOU 3133  CG2 VAL B  41     2980   2973   4197   1123    571    495       C
ATOM   3134  N   GLU B  42     -71.573  56.823  11.776  1.00 35.18           N
ANISOU 3134  N   GLU B  42     4254   3848   5264    728    270    291       N
ATOM   3135  CA  GLU B  42     -72.843  56.158  11.519  1.00 32.61           C
ANISOU 3135  CA  GLU B  42     3918   3504   4967    604    214    260       C
ATOM   3136  C   GLU B  42     -73.975  56.872  12.245  1.00 35.54           C
ANISOU 3136  C   GLU B  42     4234   3912   5356    577    263    269       C
ATOM   3137  O   GLU B  42     -73.897  57.119  13.451  1.00 36.65           O
ANISOU 3137  O   GLU B  42     4436   4040   5450    650    315    277       O
ATOM   3138  CB  GLU B  42     -72.780  54.697  11.959  1.00 34.66           C
ANISOU 3138  CB  GLU B  42     4325   3661   5185    587    141    223       C
ATOM   3139  CG  GLU B  42     -74.148  54.048  12.105  1.00 42.25           C
ANISOU 3139  CG  GLU B  42     5280   4602   6170    482     99    204       C
ATOM   3140  CD  GLU B  42     -74.076  52.644  12.668  1.00 50.29           C
ANISOU 3140  CD  GLU B  42     6434   5516   7157    462     16    181       C
ATOM   3141  OE1 GLU B  42     -73.130  51.907  12.319  1.00 53.95           O
ANISOU 3141  OE1 GLU B  42     6968   5922   7610    478    -38    180       O
ATOM   3142  OE2 GLU B  42     -74.966  52.280  13.467  1.00 52.87           O
ANISOU 3142  OE2 GLU B  42     6797   5814   7476    427     -5    168       O
ATOM   3143  N   LEU B  43     -75.033  57.200  11.506  1.00 35.33           N
ANISOU 3143  N   LEU B  43     4103   3929   5392    478    246    269       N
ATOM   3144  CA  LEU B  43     -76.218  57.820  12.080  1.00 36.03           C
ANISOU 3144  CA  LEU B  43     4138   4041   5509    437    280    278       C
ATOM   3145  C   LEU B  43     -77.396  56.873  12.216  1.00 37.30           C
ANISOU 3145  C   LEU B  43     4343   4156   5672    355    231    242       C
ATOM   3146  O   LEU B  43     -78.222  57.063  13.111  1.00 39.58           O
ANISOU 3146  O   LEU B  43     4642   4438   5958    346    256    246       O
ATOM   3147  CB  LEU B  43     -76.659  59.020  11.234  1.00 37.39           C
ANISOU 3147  CB  LEU B  43     4164   4285   5757    386    291    305       C
ATOM   3148  CG  LEU B  43     -75.691  60.197  11.120  1.00 37.84           C
ANISOU 3148  CG  LEU B  43     4135   4402   5840    454    339    363       C
ATOM   3149  CD1 LEU B  43     -76.323  61.307  10.297  1.00 36.60           C
ANISOU 3149  CD1 LEU B  43     3837   4299   5768    378    319    388       C
ATOM   3150  CD2 LEU B  43     -75.297  60.699  12.499  1.00 39.54           C
ANISOU 3150  CD2 LEU B  43     4376   4626   6022    553    430    408       C
ATOM   3151  N   PHE B  44     -77.490  55.856  11.362  1.00 31.69           N
ANISOU 3151  N   PHE B  44     3654   3418   4969    301    166    218       N
ATOM   3152  CA  PHE B  44     -78.677  55.014  11.321  1.00 28.85           C
ANISOU 3152  CA  PHE B  44     3305   3029   4628    223    126    200       C
ATOM   3153  C   PHE B  44     -78.348  53.722  10.592  1.00 27.70           C
ANISOU 3153  C   PHE B  44     3201   2845   4480    192     63    194       C
ATOM   3154  O   PHE B  44     -77.851  53.755   9.463  1.00 24.69           O
ANISOU 3154  O   PHE B  44     2780   2491   4109    187     54    201       O
ATOM   3155  CB  PHE B  44     -79.828  55.749  10.626  1.00 27.93           C
ANISOU 3155  CB  PHE B  44     3086   2960   4565    161    140    197       C
ATOM   3156  CG  PHE B  44     -81.059  54.913  10.425  1.00 25.34           C
ANISOU 3156  CG  PHE B  44     2761   2609   4260     95    109    183       C
ATOM   3157  CD1 PHE B  44     -81.934  54.682  11.472  1.00 20.29           C
ANISOU 3157  CD1 PHE B  44     2151   1939   3621     82    113    184       C
ATOM   3158  CD2 PHE B  44     -81.353  54.377   9.182  1.00 25.96           C
ANISOU 3158  CD2 PHE B  44     2810   2700   4354     56     82    177       C
ATOM   3159  CE1 PHE B  44     -83.072  53.921  11.287  1.00 20.12           C
ANISOU 3159  CE1 PHE B  44     2120   1898   3626     29     87    180       C
ATOM   3160  CE2 PHE B  44     -82.490  53.616   8.991  1.00 25.70           C
ANISOU 3160  CE2 PHE B  44     2771   2651   4342     10     68    176       C
ATOM   3161  CZ  PHE B  44     -83.350  53.387  10.045  1.00 22.58           C
ANISOU 3161  CZ  PHE B  44     2396   2224   3958     -4     69    178       C
ATOM   3162  N   GLU B  45     -78.623  52.594  11.240  1.00 24.46           N
ANISOU 3162  N   GLU B  45     2866   2370   4059    170     16    192       N
ATOM   3163  CA  GLU B  45     -78.506  51.278  10.627  1.00 28.45           C
ANISOU 3163  CA  GLU B  45     3393   2833   4582    123    -49    206       C
ATOM   3164  C   GLU B  45     -79.908  50.772  10.322  1.00 30.55           C
ANISOU 3164  C   GLU B  45     3601   3112   4895     51    -58    217       C
ATOM   3165  O   GLU B  45     -80.700  50.536  11.241  1.00 32.10           O
ANISOU 3165  O   GLU B  45     3820   3281   5097     33    -71    215       O
ATOM   3166  CB  GLU B  45     -77.764  50.304  11.541  1.00 31.57           C
ANISOU 3166  CB  GLU B  45     3913   3137   4946    143   -115    205       C
ATOM   3167  CG  GLU B  45     -77.619  48.909  10.956  1.00 43.41           C
ANISOU 3167  CG  GLU B  45     5427   4585   6483     83   -193    238       C
ATOM   3168  CD  GLU B  45     -77.032  47.919  11.943  1.00 55.28           C
ANISOU 3168  CD  GLU B  45     7062   5978   7965     86   -285    236       C
ATOM   3169  OE1 GLU B  45     -76.636  48.343  13.049  1.00 60.42           O
ANISOU 3169  OE1 GLU B  45     7810   6595   8553    153   -281    200       O
ATOM   3170  OE2 GLU B  45     -76.969  46.715  11.613  1.00 59.38           O
ANISOU 3170  OE2 GLU B  45     7590   6442   8530     24   -364    274       O
ATOM   3171  N   ASN B  46     -80.212  50.611   9.037  1.00 28.67           N
ANISOU 3171  N   ASN B  46     3293   2915   4684     19    -48    232       N
ATOM   3172  CA  ASN B  46     -81.556  50.234   8.612  1.00 25.72           C
ANISOU 3172  CA  ASN B  46     2861   2562   4349    -29    -39    245       C
ATOM   3173  C   ASN B  46     -81.837  48.791   9.010  1.00 28.74           C
ANISOU 3173  C   ASN B  46     3266   2889   4763    -71    -95    287       C
ATOM   3174  O   ASN B  46     -81.256  47.857   8.448  1.00 32.16           O
ANISOU 3174  O   ASN B  46     3705   3302   5213    -89   -131    328       O
ATOM   3175  CB  ASN B  46     -81.707  50.425   7.106  1.00 23.27           C
ANISOU 3175  CB  ASN B  46     2490   2310   4041    -32    -10    251       C
ATOM   3176  CG  ASN B  46     -83.095  50.074   6.612  1.00 22.38           C
ANISOU 3176  CG  ASN B  46     2327   2219   3955    -60     13    263       C
ATOM   3177  OD1 ASN B  46     -84.054  50.063   7.383  1.00 28.50           O
ANISOU 3177  OD1 ASN B  46     3098   2977   4754    -75     16    258       O
ATOM   3178  ND2 ASN B  46     -83.209  49.783   5.322  1.00 23.01           N
ANISOU 3178  ND2 ASN B  46     2376   2338   4027    -55     33    283       N
ATOM   3179  N   LYS B  47     -82.728  48.606   9.981  1.00 29.76           N
ANISOU 3179  N   LYS B  47     3405   2992   4909    -90   -110    286       N
ATOM   3180  CA  LYS B  47     -83.186  47.285  10.383  1.00 25.26           C
ANISOU 3180  CA  LYS B  47     2840   2373   4384   -139   -174    335       C
ATOM   3181  C   LYS B  47     -84.541  46.938   9.785  1.00 29.23           C
ANISOU 3181  C   LYS B  47     3251   2915   4938   -167   -140    370       C
ATOM   3182  O   LYS B  47     -85.130  45.919  10.158  1.00 31.59           O
ANISOU 3182  O   LYS B  47     3531   3184   5288   -207   -187    421       O
ATOM   3183  CB  LYS B  47     -83.249  47.188  11.910  1.00 26.43           C
ANISOU 3183  CB  LYS B  47     3070   2459   4512   -136   -228    317       C
ATOM   3184  CG  LYS B  47     -81.929  47.466  12.606  1.00 35.01           C
ANISOU 3184  CG  LYS B  47     4268   3499   5534    -88   -256    282       C
ATOM   3185  CD  LYS B  47     -80.866  46.478  12.158  1.00 47.91           C
ANISOU 3185  CD  LYS B  47     5942   5080   7182   -107   -326    312       C
ATOM   3186  CE  LYS B  47     -81.260  45.053  12.514  1.00 59.97           C
ANISOU 3186  CE  LYS B  47     7478   6539   8768   -178   -430    366       C
ATOM   3187  NZ  LYS B  47     -80.467  44.048  11.753  1.00 65.66           N
ANISOU 3187  NZ  LYS B  47     8193   7221   9533   -218   -488    420       N
ATOM   3188  N   THR B  48     -85.045  47.756   8.867  1.00 30.60           N
ANISOU 3188  N   THR B  48     3373   3153   5100   -144    -66    346       N
ATOM   3189  CA  THR B  48     -86.368  47.576   8.289  1.00 27.08           C
ANISOU 3189  CA  THR B  48     2858   2743   4688   -148    -23    367       C
ATOM   3190  C   THR B  48     -86.271  46.939   6.906  1.00 28.67           C
ANISOU 3190  C   THR B  48     3012   2984   4897   -142      8    415       C
ATOM   3191  O   THR B  48     -85.187  46.730   6.358  1.00 32.70           O
ANISOU 3191  O   THR B  48     3539   3497   5388   -139     -6    429       O
ATOM   3192  CB  THR B  48     -87.101  48.918   8.195  1.00 30.51           C
ANISOU 3192  CB  THR B  48     3285   3208   5098   -121     31    306       C
ATOM   3193  OG1 THR B  48     -86.735  49.577   6.976  1.00 28.81           O
ANISOU 3193  OG1 THR B  48     3060   3039   4849    -95     67    278       O
ATOM   3194  CG2 THR B  48     -86.726  49.810   9.368  1.00 29.54           C
ANISOU 3194  CG2 THR B  48     3213   3060   4953   -115     17    264       C
ATOM   3195  N   THR B  49     -87.436  46.631   6.344  1.00 32.79           N
ANISOU 3195  N   THR B  49     3477   3538   5442   -130     56    445       N
ATOM   3196  CA  THR B  49     -87.539  46.109   4.988  1.00 31.50           C
ANISOU 3196  CA  THR B  49     3270   3425   5272   -103    108    494       C
ATOM   3197  C   THR B  49     -87.711  47.210   3.949  1.00 28.98           C
ANISOU 3197  C   THR B  49     2974   3154   4885    -51    164    427       C
ATOM   3198  O   THR B  49     -87.911  46.905   2.769  1.00 24.53           O
ANISOU 3198  O   THR B  49     2392   2636   4294    -12    216    458       O
ATOM   3199  CB  THR B  49     -88.707  45.122   4.885  1.00 35.41           C
ANISOU 3199  CB  THR B  49     3694   3934   5827   -100    139    574       C
ATOM   3200  OG1 THR B  49     -89.940  45.805   5.145  1.00 40.47           O
ANISOU 3200  OG1 THR B  49     4335   4579   6463    -71    176    525       O
ATOM   3201  CG2 THR B  49     -88.539  43.996   5.891  1.00 37.84           C
ANISOU 3201  CG2 THR B  49     3974   4189   6213   -163     61    649       C
ATOM   3202  N   LEU B  50     -87.643  48.468   4.359  1.00 24.24           N
ANISOU 3202  N   LEU B  50     2413   2542   4256    -49    151    344       N
ATOM   3203  CA  LEU B  50     -87.737  49.619   3.478  1.00 26.72           C
ANISOU 3203  CA  LEU B  50     2752   2887   4514    -14    175    278       C
ATOM   3204  C   LEU B  50     -86.356  50.020   2.983  1.00 27.25           C
ANISOU 3204  C   LEU B  50     2842   2970   4541    -11    149    264       C
ATOM   3205  O   LEU B  50     -85.338  49.607   3.547  1.00 28.99           O
ANISOU 3205  O   LEU B  50     3069   3167   4777    -33    115    291       O
ATOM   3206  CB  LEU B  50     -88.385  50.787   4.218  1.00 28.25           C
ANISOU 3206  CB  LEU B  50     2961   3055   4718    -24    165    213       C
ATOM   3207  CG  LEU B  50     -89.821  50.585   4.701  1.00 30.86           C
ANISOU 3207  CG  LEU B  50     3276   3365   5086    -21    189    218       C
ATOM   3208  CD1 LEU B  50     -90.231  51.720   5.622  1.00 33.70           C
ANISOU 3208  CD1 LEU B  50     3651   3691   5464    -41    171    168       C
ATOM   3209  CD2 LEU B  50     -90.773  50.486   3.521  1.00 31.34           C
ANISOU 3209  CD2 LEU B  50     3340   3451   5117     32    239    211       C
ATOM   3210  N   PRO B  51     -86.284  50.811   1.910  1.00 20.94           N
ANISOU 3210  N   PRO B  51     2063   2206   3688     20    159    222       N
ATOM   3211  CA  PRO B  51     -84.991  51.369   1.502  1.00 19.87           C
ANISOU 3211  CA  PRO B  51     1944   2087   3520     24    127    208       C
ATOM   3212  C   PRO B  51     -84.360  52.171   2.630  1.00 26.57           C
ANISOU 3212  C   PRO B  51     2792   2907   4396      0     93    181       C
ATOM   3213  O   PRO B  51     -85.047  52.717   3.496  1.00 26.51           O
ANISOU 3213  O   PRO B  51     2778   2876   4419    -18     94    155       O
ATOM   3214  CB  PRO B  51     -85.349  52.258   0.307  1.00 23.48           C
ANISOU 3214  CB  PRO B  51     2426   2576   3918     57    128    157       C
ATOM   3215  CG  PRO B  51     -86.568  51.619  -0.263  1.00 20.62           C
ANISOU 3215  CG  PRO B  51     2072   2225   3537     90    178    170       C
ATOM   3216  CD  PRO B  51     -87.337  51.079   0.915  1.00 20.29           C
ANISOU 3216  CD  PRO B  51     1996   2147   3564     62    195    194       C
ATOM   3217  N   VAL B  52     -83.027  52.238   2.606  1.00 32.06           N
ANISOU 3217  N   VAL B  52     3497   3607   5079      7     69    195       N
ATOM   3218  CA  VAL B  52     -82.281  52.776   3.743  1.00 34.89           C
ANISOU 3218  CA  VAL B  52     3861   3939   5458      3     52    186       C
ATOM   3219  C   VAL B  52     -82.625  54.245   3.973  1.00 28.05           C
ANISOU 3219  C   VAL B  52     2970   3086   4602      0     51    143       C
ATOM   3220  O   VAL B  52     -82.869  54.670   5.108  1.00 33.01           O
ANISOU 3220  O   VAL B  52     3593   3692   5259     -8     60    138       O
ATOM   3221  CB  VAL B  52     -80.768  52.563   3.538  1.00 37.26           C
ANISOU 3221  CB  VAL B  52     4180   4238   5737     27     31    211       C
ATOM   3222  CG1 VAL B  52     -80.334  53.026   2.152  1.00 29.91           C
ANISOU 3222  CG1 VAL B  52     3239   3357   4769     48     22    206       C
ATOM   3223  CG2 VAL B  52     -79.973  53.271   4.624  1.00 19.44           C
ANISOU 3223  CG2 VAL B  52     1935   1962   3488     47     26    200       C
ATOM   3224  N   ASN B  53     -82.661  55.040   2.901  1.00 25.30           N
ANISOU 3224  N   ASN B  53     2607   2772   4233      6     35    118       N
ATOM   3225  CA  ASN B  53     -82.943  56.464   3.055  1.00 21.77           C
ANISOU 3225  CA  ASN B  53     2129   2331   3813     -9     17     89       C
ATOM   3226  C   ASN B  53     -84.389  56.713   3.459  1.00 24.78           C
ANISOU 3226  C   ASN B  53     2508   2684   4222    -37     28     64       C
ATOM   3227  O   ASN B  53     -84.682  57.706   4.135  1.00 27.78           O
ANISOU 3227  O   ASN B  53     2859   3052   4646    -59     23     58       O
ATOM   3228  CB  ASN B  53     -82.624  57.208   1.759  1.00 22.09           C
ANISOU 3228  CB  ASN B  53     2164   2406   3825     -3    -28     69       C
ATOM   3229  CG  ASN B  53     -83.445  56.711   0.588  1.00 22.42           C
ANISOU 3229  CG  ASN B  53     2250   2454   3815      8    -31     42       C
ATOM   3230  OD1 ASN B  53     -83.555  55.508   0.360  1.00 27.03           O
ANISOU 3230  OD1 ASN B  53     2859   3040   4371     28      5     67       O
ATOM   3231  ND2 ASN B  53     -84.036  57.638  -0.156  1.00 23.67           N
ANISOU 3231  ND2 ASN B  53     2421   2612   3960     -1    -77     -2       N
ATOM   3232  N   VAL B  54     -85.303  55.831   3.055  1.00 23.09           N
ANISOU 3232  N   VAL B  54     2323   2460   3989    -31     47     57       N
ATOM   3233  CA  VAL B  54     -86.705  55.992   3.422  1.00 23.84           C
ANISOU 3233  CA  VAL B  54     2423   2524   4112    -47     60     35       C
ATOM   3234  C   VAL B  54     -86.902  55.706   4.905  1.00 27.51           C
ANISOU 3234  C   VAL B  54     2875   2959   4620    -64     83     62       C
ATOM   3235  O   VAL B  54     -87.478  56.517   5.640  1.00 25.36           O
ANISOU 3235  O   VAL B  54     2587   2663   4385    -85     82     53       O
ATOM   3236  CB  VAL B  54     -87.592  55.087   2.549  1.00 22.52           C
ANISOU 3236  CB  VAL B  54     2287   2360   3910    -18     86     30       C
ATOM   3237  CG1 VAL B  54     -89.032  55.171   3.003  1.00 24.62           C
ANISOU 3237  CG1 VAL B  54     2560   2588   4207    -24    104     13       C
ATOM   3238  CG2 VAL B  54     -87.465  55.477   1.085  1.00 20.38           C
ANISOU 3238  CG2 VAL B  54     2050   2116   3577     10     62     -3       C
ATOM   3239  N   ALA B  55     -86.427  54.545   5.366  1.00 25.51           N
ANISOU 3239  N   ALA B  55     2631   2701   4359    -56     95    100       N
ATOM   3240  CA  ALA B  55     -86.538  54.207   6.780  1.00 23.07           C
ANISOU 3240  CA  ALA B  55     2329   2360   4077    -67    101    123       C
ATOM   3241  C   ALA B  55     -85.807  55.216   7.653  1.00 24.82           C
ANISOU 3241  C   ALA B  55     2545   2581   4305    -62    102    123       C
ATOM   3242  O   ALA B  55     -86.247  55.505   8.772  1.00 26.42           O
ANISOU 3242  O   ALA B  55     2752   2761   4527    -68    115    131       O
ATOM   3243  CB  ALA B  55     -85.998  52.797   7.026  1.00 23.25           C
ANISOU 3243  CB  ALA B  55     2372   2368   4092    -64     90    163       C
ATOM   3244  N   PHE B  56     -84.693  55.760   7.159  1.00 24.66           N
ANISOU 3244  N   PHE B  56     2514   2590   4268    -45     93    122       N
ATOM   3245  CA  PHE B  56     -83.981  56.795   7.898  1.00 22.73           C
ANISOU 3245  CA  PHE B  56     2248   2355   4033    -28    107    135       C
ATOM   3246  C   PHE B  56     -84.859  58.021   8.103  1.00 24.26           C
ANISOU 3246  C   PHE B  56     2396   2550   4274    -57    113    131       C
ATOM   3247  O   PHE B  56     -84.892  58.596   9.197  1.00 26.35           O
ANISOU 3247  O   PHE B  56     2646   2807   4557    -50    142    157       O
ATOM   3248  CB  PHE B  56     -82.696  57.162   7.158  1.00 25.43           C
ANISOU 3248  CB  PHE B  56     2573   2732   4356     -1     93    142       C
ATOM   3249  CG  PHE B  56     -81.983  58.352   7.730  1.00 26.90           C
ANISOU 3249  CG  PHE B  56     2715   2941   4564     23    113    169       C
ATOM   3250  CD1 PHE B  56     -81.470  58.317   9.015  1.00 26.43           C
ANISOU 3250  CD1 PHE B  56     2682   2869   4491     67    154    196       C
ATOM   3251  CD2 PHE B  56     -81.809  59.500   6.975  1.00 28.69           C
ANISOU 3251  CD2 PHE B  56     2875   3204   4824      9     90    174       C
ATOM   3252  CE1 PHE B  56     -80.806  59.410   9.543  1.00 21.93           C
ANISOU 3252  CE1 PHE B  56     2064   2329   3939    104    190    236       C
ATOM   3253  CE2 PHE B  56     -81.145  60.596   7.495  1.00 26.64           C
ANISOU 3253  CE2 PHE B  56     2553   2971   4597     32    114    218       C
ATOM   3254  CZ  PHE B  56     -80.643  60.551   8.782  1.00 21.66           C
ANISOU 3254  CZ  PHE B  56     1940   2336   3953     85    174    254       C
ATOM   3255  N   GLU B  57     -85.591  58.425   7.063  1.00 27.93           N
ANISOU 3255  N   GLU B  57     2844   3016   4753    -86     84    100       N
ATOM   3256  CA  GLU B  57     -86.476  59.577   7.181  1.00 23.10           C
ANISOU 3256  CA  GLU B  57     2196   2387   4193   -124     72     94       C
ATOM   3257  C   GLU B  57     -87.628  59.295   8.136  1.00 24.06           C
ANISOU 3257  C   GLU B  57     2336   2468   4337   -137     98    100       C
ATOM   3258  O   GLU B  57     -87.995  60.156   8.944  1.00 28.44           O
ANISOU 3258  O   GLU B  57     2860   3009   4937   -156    112    126       O
ATOM   3259  CB  GLU B  57     -87.001  59.972   5.801  1.00 26.14           C
ANISOU 3259  CB  GLU B  57     2589   2769   4576   -145     19     49       C
ATOM   3260  CG  GLU B  57     -88.024  61.095   5.820  1.00 32.57           C
ANISOU 3260  CG  GLU B  57     3383   3544   5449   -192    -15     36       C
ATOM   3261  CD  GLU B  57     -88.403  61.558   4.426  1.00 41.15           C
ANISOU 3261  CD  GLU B  57     4498   4617   6520   -207    -87    -17       C
ATOM   3262  OE1 GLU B  57     -87.747  61.123   3.457  1.00 46.67           O
ANISOU 3262  OE1 GLU B  57     5223   5350   7161   -178   -104    -36       O
ATOM   3263  OE2 GLU B  57     -89.355  62.356   4.298  1.00 45.65           O
ANISOU 3263  OE2 GLU B  57     5074   5137   7132   -246   -131    -40       O
ATOM   3264  N   LEU B  58     -88.207  58.095   8.063  1.00 23.47           N
ANISOU 3264  N   LEU B  58     2305   2377   4236   -126    107     86       N
ATOM   3265  CA  LEU B  58     -89.315  57.756   8.950  1.00 23.79           C
ANISOU 3265  CA  LEU B  58     2361   2380   4298   -135    126     96       C
ATOM   3266  C   LEU B  58     -88.862  57.696  10.401  1.00 21.37           C
ANISOU 3266  C   LEU B  58     2062   2070   3988   -122    152    137       C
ATOM   3267  O   LEU B  58     -89.569  58.169  11.298  1.00 22.15           O
ANISOU 3267  O   LEU B  58     2155   2145   4115   -133    169    157       O
ATOM   3268  CB  LEU B  58     -89.935  56.426   8.529  1.00 25.78           C
ANISOU 3268  CB  LEU B  58     2642   2622   4530   -121    128     88       C
ATOM   3269  CG  LEU B  58     -90.529  56.400   7.123  1.00 28.28           C
ANISOU 3269  CG  LEU B  58     2969   2943   4833   -112    118     50       C
ATOM   3270  CD1 LEU B  58     -91.163  55.053   6.834  1.00 30.16           C
ANISOU 3270  CD1 LEU B  58     3220   3180   5058    -87    140     65       C
ATOM   3271  CD2 LEU B  58     -91.542  57.516   6.966  1.00 31.96           C
ANISOU 3271  CD2 LEU B  58     3437   3373   5334   -133    101     18       C
ATOM   3272  N   TRP B  59     -87.688  57.115  10.652  1.00 18.99           N
ANISOU 3272  N   TRP B  59     1784   1786   3646    -92    155    150       N
ATOM   3273  CA  TRP B  59     -87.174  57.064  12.014  1.00 27.29           C
ANISOU 3273  CA  TRP B  59     2867   2828   4673    -62    177    181       C
ATOM   3274  C   TRP B  59     -86.896  58.462  12.549  1.00 28.63           C
ANISOU 3274  C   TRP B  59     2993   3019   4864    -52    215    212       C
ATOM   3275  O   TRP B  59     -87.165  58.753  13.719  1.00 28.10           O
ANISOU 3275  O   TRP B  59     2941   2940   4794    -36    248    245       O
ATOM   3276  CB  TRP B  59     -85.913  56.206  12.064  1.00 24.15           C
ANISOU 3276  CB  TRP B  59     2517   2433   4224    -26    163    182       C
ATOM   3277  CG  TRP B  59     -85.210  56.272  13.375  1.00 24.75           C
ANISOU 3277  CG  TRP B  59     2648   2497   4257     23    185    205       C
ATOM   3278  CD1 TRP B  59     -85.577  55.655  14.535  1.00 24.03           C
ANISOU 3278  CD1 TRP B  59     2623   2368   4138     35    175    215       C
ATOM   3279  CD2 TRP B  59     -84.012  56.997  13.666  1.00 26.34           C
ANISOU 3279  CD2 TRP B  59     2850   2725   4431     79    221    223       C
ATOM   3280  NE1 TRP B  59     -84.681  55.953  15.533  1.00 28.35           N
ANISOU 3280  NE1 TRP B  59     3229   2915   4629    100    204    232       N
ATOM   3281  CE2 TRP B  59     -83.710  56.775  15.024  1.00 28.36           C
ANISOU 3281  CE2 TRP B  59     3188   2957   4632    133    240    240       C
ATOM   3282  CE3 TRP B  59     -83.166  57.813  12.911  1.00 24.42           C
ANISOU 3282  CE3 TRP B  59     2550   2526   4204     96    237    231       C
ATOM   3283  CZ2 TRP B  59     -82.598  57.339  15.642  1.00 29.90           C
ANISOU 3283  CZ2 TRP B  59     3410   3170   4780    214    290    264       C
ATOM   3284  CZ3 TRP B  59     -82.063  58.372  13.525  1.00 29.04           C
ANISOU 3284  CZ3 TRP B  59     3145   3132   4757    169    283    262       C
ATOM   3285  CH2 TRP B  59     -81.788  58.133  14.877  1.00 34.10           C
ANISOU 3285  CH2 TRP B  59     3871   3748   5337    233    316    278       C
ATOM   3286  N   ALA B  60     -86.361  59.345  11.703  1.00 27.20           N
ANISOU 3286  N   ALA B  60     2755   2871   4709    -60    210    212       N
ATOM   3287  CA  ALA B  60     -86.113  60.715  12.136  1.00 25.18           C
ANISOU 3287  CA  ALA B  60     2433   2639   4495    -58    242    260       C
ATOM   3288  C   ALA B  60     -87.409  61.445  12.452  1.00 24.98           C
ANISOU 3288  C   ALA B  60     2374   2584   4531   -108    244    276       C
ATOM   3289  O   ALA B  60     -87.431  62.328  13.317  1.00 24.03           O
ANISOU 3289  O   ALA B  60     2214   2474   4443   -102    287    337       O
ATOM   3290  CB  ALA B  60     -85.328  61.471  11.065  1.00 25.75           C
ANISOU 3290  CB  ALA B  60     2442   2749   4594    -66    216    261       C
ATOM   3291  N   LYS B  61     -88.496  61.091  11.769  1.00 28.95           N
ANISOU 3291  N   LYS B  61     2896   3051   5053   -150    201    230       N
ATOM   3292  CA  LYS B  61     -89.793  61.716  11.975  1.00 26.09           C
ANISOU 3292  CA  LYS B  61     2516   2647   4751   -196    192    237       C
ATOM   3293  C   LYS B  61     -90.676  60.924  12.929  1.00 27.73           C
ANISOU 3293  C   LYS B  61     2776   2820   4939   -184    215    243       C
ATOM   3294  O   LYS B  61     -91.889  61.154  12.975  1.00 27.32           O
ANISOU 3294  O   LYS B  61     2726   2724   4929   -215    203    239       O
ATOM   3295  CB  LYS B  61     -90.499  61.909  10.634  1.00 23.07           C
ANISOU 3295  CB  LYS B  61     2135   2236   4394   -236    130    180       C
ATOM   3296  CG  LYS B  61     -89.738  62.799   9.668  1.00 22.11           C
ANISOU 3296  CG  LYS B  61     1964   2141   4297   -258     86    176       C
ATOM   3297  CD  LYS B  61     -90.484  62.958   8.357  1.00 24.31           C
ANISOU 3297  CD  LYS B  61     2273   2383   4582   -289     14    110       C
ATOM   3298  CE  LYS B  61     -89.805  63.978   7.455  1.00 25.48           C
ANISOU 3298  CE  LYS B  61     2373   2549   4760   -320    -51    110       C
ATOM   3299  NZ  LYS B  61     -90.584  64.211   6.208  1.00 28.33           N
ANISOU 3299  NZ  LYS B  61     2787   2862   5116   -346   -134     39       N
ATOM   3300  N   ARG B  62     -90.095  59.998  13.689  1.00 20.01           N
ANISOU 3300  N   ARG B  62     1847   1856   3899   -138    239    253       N
ATOM   3301  CA  ARG B  62     -90.867  59.211  14.638  1.00 24.31           C
ANISOU 3301  CA  ARG B  62     2444   2369   4424   -127    245    264       C
ATOM   3302  C   ARG B  62     -91.465  60.109  15.718  1.00 26.66           C
ANISOU 3302  C   ARG B  62     2726   2652   4752   -132    283    320       C
ATOM   3303  O   ARG B  62     -90.962  61.198  16.016  1.00 25.75           O
ANISOU 3303  O   ARG B  62     2564   2562   4659   -128    319    366       O
ATOM   3304  CB  ARG B  62     -89.990  58.136  15.278  1.00 23.52           C
ANISOU 3304  CB  ARG B  62     2409   2277   4250    -81    243    265       C
ATOM   3305  CG  ARG B  62     -88.998  58.684  16.288  1.00 23.53           C
ANISOU 3305  CG  ARG B  62     2431   2303   4207    -29    290    306       C
ATOM   3306  CD  ARG B  62     -87.879  57.700  16.565  1.00 26.11           C
ANISOU 3306  CD  ARG B  62     2834   2628   4457     20    272    289       C
ATOM   3307  NE  ARG B  62     -86.871  58.270  17.452  1.00 31.18           N
ANISOU 3307  NE  ARG B  62     3508   3295   5046     91    326    324       N
ATOM   3308  CZ  ARG B  62     -85.924  59.118  17.061  1.00 26.92           C
ANISOU 3308  CZ  ARG B  62     2916   2797   4515    120    366    342       C
ATOM   3309  NH1 ARG B  62     -85.856  59.505  15.794  1.00 23.44           N
ANISOU 3309  NH1 ARG B  62     2396   2378   4133     74    344    324       N
ATOM   3310  NH2 ARG B  62     -85.048  59.583  17.940  1.00 23.68           N
ANISOU 3310  NH2 ARG B  62     2537   2411   4051    201    428    383       N
ATOM   3311  N   ASN B  63     -92.560  59.637  16.306  1.00 31.71           N
ANISOU 3311  N   ASN B  63     3399   3253   5397   -139    275    326       N
ATOM   3312  CA  ASN B  63     -93.215  60.380  17.373  1.00 26.29           C
ANISOU 3312  CA  ASN B  63     2706   2548   4736   -142    311    386       C
ATOM   3313  C   ASN B  63     -92.406  60.263  18.658  1.00 26.68           C
ANISOU 3313  C   ASN B  63     2804   2625   4710    -81    356    432       C
ATOM   3314  O   ASN B  63     -92.108  59.158  19.120  1.00 32.12           O
ANISOU 3314  O   ASN B  63     3568   3308   5329    -46    332    412       O
ATOM   3315  CB  ASN B  63     -94.634  59.856  17.584  1.00 26.76           C
ANISOU 3315  CB  ASN B  63     2791   2555   4821   -160    286    380       C
ATOM   3316  CG  ASN B  63     -95.494  60.804  18.392  1.00 31.46           C
ANISOU 3316  CG  ASN B  63     3368   3121   5465   -178    314    442       C
ATOM   3317  OD1 ASN B  63     -95.080  61.304  19.438  1.00 34.82           O
ANISOU 3317  OD1 ASN B  63     3798   3569   5862   -151    364    505       O
ATOM   3318  ND2 ASN B  63     -96.699  61.067  17.902  1.00 30.65           N
ANISOU 3318  ND2 ASN B  63     3250   2966   5431   -217    288    428       N
ATOM   3319  N   ILE B  64     -92.049  61.408  19.236  1.00 29.79           N
ANISOU 3319  N   ILE B  64     3157   3045   5116    -66    417    499       N
ATOM   3320  CA  ILE B  64     -91.221  61.454  20.433  1.00 30.71           C
ANISOU 3320  CA  ILE B  64     3326   3193   5149     13    477    548       C
ATOM   3321  C   ILE B  64     -92.037  61.799  21.671  1.00 31.62           C
ANISOU 3321  C   ILE B  64     3467   3292   5254     29    519    618       C
ATOM   3322  O   ILE B  64     -91.468  62.149  22.710  1.00 35.89           O
ANISOU 3322  O   ILE B  64     4042   3864   5729    101    589    678       O
ATOM   3323  CB  ILE B  64     -90.046  62.429  20.257  1.00 31.03           C
ANISOU 3323  CB  ILE B  64     3301   3290   5198     46    537    591       C
ATOM   3324  CG1 ILE B  64     -90.567  63.847  20.027  1.00 32.89           C
ANISOU 3324  CG1 ILE B  64     3418   3533   5547    -12    565    661       C
ATOM   3325  CG2 ILE B  64     -89.160  61.989  19.098  1.00 30.56           C
ANISOU 3325  CG2 ILE B  64     3231   3247   5134     40    492    523       C
ATOM   3326  CD1 ILE B  64     -89.505  64.912  20.146  1.00 32.25           C
ANISOU 3326  CD1 ILE B  64     3255   3514   5485     27    637    740       C
ATOM   3327  N   LYS B  65     -93.351  61.719  21.587  1.00 31.00           N
ANISOU 3327  N   LYS B  65     3378   3166   5235    -26    482    614       N
ATOM   3328  CA  LYS B  65     -94.223  61.897  22.732  1.00 29.05           C
ANISOU 3328  CA  LYS B  65     3164   2896   4977    -13    510    678       C
ATOM   3329  C   LYS B  65     -94.700  60.544  23.237  1.00 27.88           C
ANISOU 3329  C   LYS B  65     3116   2715   4762      8    451    638       C
ATOM   3330  O   LYS B  65     -94.568  59.532  22.543  1.00 29.03           O
ANISOU 3330  O   LYS B  65     3282   2849   4900     -7    386    567       O
ATOM   3331  CB  LYS B  65     -95.421  62.777  22.353  1.00 36.41           C
ANISOU 3331  CB  LYS B  65     4019   3786   6030    -88    503    711       C
ATOM   3332  CG  LYS B  65     -95.033  64.191  21.949  1.00 50.32           C
ANISOU 3332  CG  LYS B  65     5672   5571   7875   -123    545    769       C
ATOM   3333  CD  LYS B  65     -96.245  65.102  21.841  1.00 63.15           C
ANISOU 3333  CD  LYS B  65     7238   7138   9618   -197    531    818       C
ATOM   3334  CE  LYS B  65     -97.191  64.650  20.741  1.00 71.59           C
ANISOU 3334  CE  LYS B  65     8319   8141  10743   -255    442    726       C
ATOM   3335  NZ  LYS B  65     -98.365  65.560  20.617  1.00 78.04           N
ANISOU 3335  NZ  LYS B  65     9094   8883  11672   -324    417    767       N
ATOM   3336  N   PRO B  66     -95.229  60.475  24.461  1.00 29.91           N
ANISOU 3336  N   PRO B  66     3436   2959   4972     43    468    693       N
ATOM   3337  CA  PRO B  66     -95.790  59.204  24.945  1.00 27.05           C
ANISOU 3337  CA  PRO B  66     3160   2560   4560     53    394    664       C
ATOM   3338  C   PRO B  66     -96.892  58.710  24.020  1.00 29.51           C
ANISOU 3338  C   PRO B  66     3418   2829   4966    -14    331    623       C
ATOM   3339  O   PRO B  66     -97.892  59.394  23.793  1.00 34.39           O
ANISOU 3339  O   PRO B  66     3981   3419   5669    -53    347    650       O
ATOM   3340  CB  PRO B  66     -96.327  59.563  26.334  1.00 26.47           C
ANISOU 3340  CB  PRO B  66     3143   2479   4435     95    432    744       C
ATOM   3341  CG  PRO B  66     -95.490  60.708  26.765  1.00 29.04           C
ANISOU 3341  CG  PRO B  66     3449   2855   4729    144    537    808       C
ATOM   3342  CD  PRO B  66     -95.205  61.500  25.521  1.00 28.58           C
ANISOU 3342  CD  PRO B  66     3267   2814   4779     85    558    792       C
ATOM   3343  N   VAL B  67     -96.693  57.515  23.476  1.00 27.79           N
ANISOU 3343  N   VAL B  67     3220   2603   4734    -22    261    563       N
ATOM   3344  CA  VAL B  67     -97.624  56.945  22.504  1.00 28.78           C
ANISOU 3344  CA  VAL B  67     3294   2700   4941    -66    215    528       C
ATOM   3345  C   VAL B  67     -98.062  55.577  22.998  1.00 29.87           C
ANISOU 3345  C   VAL B  67     3481   2815   5054    -57    140    532       C
ATOM   3346  O   VAL B  67     -97.359  54.928  23.791  1.00 27.86           O
ANISOU 3346  O   VAL B  67     3305   2565   4716    -27    101    535       O
ATOM   3347  CB  VAL B  67     -96.989  56.853  21.095  1.00 32.07           C
ANISOU 3347  CB  VAL B  67     3659   3138   5388    -90    211    468       C
ATOM   3348  CG1 VAL B  67     -96.775  58.242  20.520  1.00 32.16           C
ANISOU 3348  CG1 VAL B  67     3611   3163   5446   -112    265    470       C
ATOM   3349  CG2 VAL B  67     -95.676  56.092  21.155  1.00 34.00           C
ANISOU 3349  CG2 VAL B  67     3951   3410   5557    -64    184    442       C
ATOM   3350  N   PRO B  68     -99.235  55.110  22.563  1.00 29.47           N
ANISOU 3350  N   PRO B  68     3388   2735   5075    -79    111    534       N
ATOM   3351  CA  PRO B  68     -99.675  53.765  22.944  1.00 30.02           C
ANISOU 3351  CA  PRO B  68     3479   2787   5141    -76     32    551       C
ATOM   3352  C   PRO B  68     -98.694  52.709  22.464  1.00 31.84           C
ANISOU 3352  C   PRO B  68     3716   3035   5345    -84    -21    518       C
ATOM   3353  O   PRO B  68     -98.035  52.862  21.433  1.00 32.36           O
ANISOU 3353  O   PRO B  68     3745   3126   5424    -95      6    477       O
ATOM   3354  CB  PRO B  68    -101.032  53.622  22.244  1.00 26.61           C
ANISOU 3354  CB  PRO B  68     2978   2328   4803    -88     36    558       C
ATOM   3355  CG  PRO B  68    -101.498  55.016  22.033  1.00 25.59           C
ANISOU 3355  CG  PRO B  68     2829   2183   4712    -94    105    557       C
ATOM   3356  CD  PRO B  68    -100.264  55.828  21.790  1.00 26.11           C
ANISOU 3356  CD  PRO B  68     2899   2284   4738   -102    146    529       C
ATOM   3357  N   GLU B  69     -98.595  51.629  23.232  1.00 29.67           N
ANISOU 3357  N   GLU B  69     3493   2744   5036    -81   -108    542       N
ATOM   3358  CA  GLU B  69     -97.746  50.521  22.829  1.00 29.59           C
ANISOU 3358  CA  GLU B  69     3489   2736   5018   -100   -177    524       C
ATOM   3359  C   GLU B  69     -98.319  49.844  21.590  1.00 29.22           C
ANISOU 3359  C   GLU B  69     3334   2700   5067   -127   -178    530       C
ATOM   3360  O   GLU B  69     -99.533  49.823  21.372  1.00 33.42           O
ANISOU 3360  O   GLU B  69     3808   3226   5666   -124   -159    558       O
ATOM   3361  CB  GLU B  69     -97.594  49.521  23.974  1.00 33.36           C
ANISOU 3361  CB  GLU B  69     4051   3179   5445   -100   -293    553       C
ATOM   3362  CG  GLU B  69     -96.741  50.050  25.119  1.00 37.59           C
ANISOU 3362  CG  GLU B  69     4721   3706   5857    -55   -292    538       C
ATOM   3363  CD  GLU B  69     -96.430  48.995  26.161  1.00 44.31           C
ANISOU 3363  CD  GLU B  69     5684   4511   6642    -52   -428    552       C
ATOM   3364  OE1 GLU B  69     -97.353  48.593  26.901  1.00 48.78           O
ANISOU 3364  OE1 GLU B  69     6264   5053   7218    -56   -491    597       O
ATOM   3365  OE2 GLU B  69     -95.261  48.563  26.236  1.00 49.23           O
ANISOU 3365  OE2 GLU B  69     6387   5116   7204    -45   -480    516       O
ATOM   3366  N   VAL B  70     -97.422  49.295  20.767  1.00 30.95           N
ANISOU 3366  N   VAL B  70     3534   2937   5290   -144   -193    507       N
ATOM   3367  CA  VAL B  70     -97.816  48.795  19.452  1.00 29.81           C
ANISOU 3367  CA  VAL B  70     3290   2814   5221   -156   -167    514       C
ATOM   3368  C   VAL B  70     -98.833  47.668  19.583  1.00 28.74           C
ANISOU 3368  C   VAL B  70     3094   2667   5160   -166   -222    583       C
ATOM   3369  O   VAL B  70     -99.753  47.546  18.764  1.00 29.97           O
ANISOU 3369  O   VAL B  70     3167   2837   5381   -149   -173    603       O
ATOM   3370  CB  VAL B  70     -96.571  48.356  18.658  1.00 34.74           C
ANISOU 3370  CB  VAL B  70     3912   3459   5830   -172   -178    490       C
ATOM   3371  CG1 VAL B  70     -96.969  47.802  17.299  1.00 36.39           C
ANISOU 3371  CG1 VAL B  70     4022   3698   6106   -174   -143    508       C
ATOM   3372  CG2 VAL B  70     -95.612  49.527  18.497  1.00 30.24           C
ANISOU 3372  CG2 VAL B  70     3388   2906   5195   -154   -120    430       C
ATOM   3373  N   LYS B  71     -98.693  46.833  20.617  1.00 28.61           N
ANISOU 3373  N   LYS B  71     3120   2620   5132   -187   -329    623       N
ATOM   3374  CA  LYS B  71     -99.659  45.759  20.823  1.00 28.68           C
ANISOU 3374  CA  LYS B  71     3060   2617   5222   -201   -396    703       C
ATOM   3375  C   LYS B  71    -101.065  46.305  21.029  1.00 29.11           C
ANISOU 3375  C   LYS B  71     3081   2668   5312   -165   -341    725       C
ATOM   3376  O   LYS B  71    -102.039  45.688  20.585  1.00 31.30           O
ANISOU 3376  O   LYS B  71     3263   2954   5674   -153   -333    783       O
ATOM   3377  CB  LYS B  71     -99.238  44.888  22.010  1.00 29.28           C
ANISOU 3377  CB  LYS B  71     3207   2650   5270   -236   -542    738       C
ATOM   3378  CG  LYS B  71     -99.103  45.631  23.329  1.00 30.55           C
ANISOU 3378  CG  LYS B  71     3500   2781   5328   -211   -564    706       C
ATOM   3379  CD  LYS B  71     -98.687  44.684  24.445  1.00 31.79           C
ANISOU 3379  CD  LYS B  71     3746   2887   5446   -239   -726    734       C
ATOM   3380  CE  LYS B  71     -98.506  45.417  25.764  1.00 31.01           C
ANISOU 3380  CE  LYS B  71     3798   2763   5223   -197   -739    704       C
ATOM   3381  NZ  LYS B  71     -98.056  44.503  26.852  1.00 31.97           N
ANISOU 3381  NZ  LYS B  71     4036   2825   5286   -216   -910    718       N
ATOM   3382  N   ILE B  72    -101.190  47.461  21.683  1.00 28.82           N
ANISOU 3382  N   ILE B  72     3120   2617   5215   -143   -299    687       N
ATOM   3383  CA  ILE B  72    -102.497  48.095  21.829  1.00 28.39           C
ANISOU 3383  CA  ILE B  72     3041   2548   5197   -111   -245    705       C
ATOM   3384  C   ILE B  72    -103.037  48.507  20.466  1.00 28.26           C
ANISOU 3384  C   ILE B  72     2952   2549   5236    -86   -146    679       C
ATOM   3385  O   ILE B  72    -104.182  48.202  20.112  1.00 31.30           O
ANISOU 3385  O   ILE B  72     3274   2927   5690    -56   -124    717       O
ATOM   3386  CB  ILE B  72    -102.405  49.296  22.787  1.00 27.58           C
ANISOU 3386  CB  ILE B  72     3031   2427   5022    -98   -216    682       C
ATOM   3387  CG1 ILE B  72    -102.026  48.829  24.194  1.00 28.45           C
ANISOU 3387  CG1 ILE B  72     3232   2517   5062   -103   -314    712       C
ATOM   3388  CG2 ILE B  72    -103.714  50.067  22.802  1.00 23.23           C
ANISOU 3388  CG2 ILE B  72     2455   1852   4518    -72   -156    699       C
ATOM   3389  CD1 ILE B  72    -103.003  47.841  24.792  1.00 24.06           C
ANISOU 3389  CD1 ILE B  72     2647   1938   4557   -107   -404    786       C
ATOM   3390  N   LEU B  73    -102.214  49.200  19.677  1.00 25.17           N
ANISOU 3390  N   LEU B  73     2575   2178   4809    -91    -90    613       N
ATOM   3391  CA  LEU B  73    -102.641  49.621  18.347  1.00 22.75           C
ANISOU 3391  CA  LEU B  73     2223   1883   4537    -64     -9    577       C
ATOM   3392  C   LEU B  73    -102.930  48.422  17.456  1.00 24.45           C
ANISOU 3392  C   LEU B  73     2355   2127   4807    -46     -8    619       C
ATOM   3393  O   LEU B  73    -103.846  48.461  16.627  1.00 28.83           O
ANISOU 3393  O   LEU B  73     2870   2683   5403      3     53    621       O
ATOM   3394  CB  LEU B  73    -101.575  50.514  17.714  1.00 25.17           C
ANISOU 3394  CB  LEU B  73     2562   2209   4792    -79     31    506       C
ATOM   3395  CG  LEU B  73    -101.121  51.713  18.547  1.00 28.34           C
ANISOU 3395  CG  LEU B  73     3028   2595   5145    -94     40    481       C
ATOM   3396  CD1 LEU B  73    -100.087  52.529  17.790  1.00 29.93           C
ANISOU 3396  CD1 LEU B  73     3239   2821   5312   -106     78    423       C
ATOM   3397  CD2 LEU B  73    -102.309  52.577  18.936  1.00 31.58           C
ANISOU 3397  CD2 LEU B  73     3447   2962   5589    -81     70    493       C
ATOM   3398  N   ASN B  74    -102.155  47.346  17.609  1.00 26.61           N
ANISOU 3398  N   ASN B  74     2606   2421   5084    -79    -73    658       N
ATOM   3399  CA  ASN B  74    -102.408  46.138  16.831  1.00 28.10           C
ANISOU 3399  CA  ASN B  74     2697   2641   5338    -67    -72    724       C
ATOM   3400  C   ASN B  74    -103.741  45.512  17.216  1.00 32.33           C
ANISOU 3400  C   ASN B  74     3167   3165   5951    -36    -85    806       C
ATOM   3401  O   ASN B  74    -104.556  45.178  16.348  1.00 35.40           O
ANISOU 3401  O   ASN B  74     3483   3576   6392     20    -16    841       O
ATOM   3402  CB  ASN B  74    -101.271  45.134  17.023  1.00 37.42           C
ANISOU 3402  CB  ASN B  74     3869   3832   6518   -124   -158    759       C
ATOM   3403  CG  ASN B  74     -99.970  45.597  16.397  1.00 39.05           C
ANISOU 3403  CG  ASN B  74     4122   4055   6659   -141   -134    690       C
ATOM   3404  OD1 ASN B  74     -99.960  46.472  15.532  1.00 38.85           O
ANISOU 3404  OD1 ASN B  74     4109   4049   6605   -109    -47    629       O
ATOM   3405  ND2 ASN B  74     -98.863  45.005  16.829  1.00 38.44           N
ANISOU 3405  ND2 ASN B  74     4078   3966   6561   -190   -219    700       N
ATOM   3406  N   ASN B  75    -103.983  45.351  18.519  1.00 32.12           N
ANISOU 3406  N   ASN B  75     3172   3106   5927    -63   -171    841       N
ATOM   3407  CA  ASN B  75    -105.227  44.740  18.973  1.00 30.78           C
ANISOU 3407  CA  ASN B  75     2937   2924   5834    -35   -197    927       C
ATOM   3408  C   ASN B  75    -106.446  45.552  18.562  1.00 32.86           C
ANISOU 3408  C   ASN B  75     3198   3171   6115     38    -97    905       C
ATOM   3409  O   ASN B  75    -107.543  44.995  18.459  1.00 37.67           O
ANISOU 3409  O   ASN B  75     3731   3782   6798     88    -81    977       O
ATOM   3410  CB  ASN B  75    -105.207  44.562  20.491  1.00 31.07           C
ANISOU 3410  CB  ASN B  75     3032   2924   5850    -76   -315    957       C
ATOM   3411  CG  ASN B  75    -104.136  43.593  20.949  1.00 29.49           C
ANISOU 3411  CG  ASN B  75     2843   2721   5639   -144   -439    986       C
ATOM   3412  OD1 ASN B  75    -103.571  42.849  20.147  1.00 33.54           O
ANISOU 3412  OD1 ASN B  75     3289   3262   6191   -167   -442   1012       O
ATOM   3413  ND2 ASN B  75    -103.852  43.595  22.245  1.00 28.07           N
ANISOU 3413  ND2 ASN B  75     2757   2504   5405   -175   -544    985       N
ATOM   3414  N   LEU B  76    -106.279  46.848  18.322  1.00 30.56           N
ANISOU 3414  N   LEU B  76     2988   2860   5763     47    -36    812       N
ATOM   3415  CA  LEU B  76    -107.367  47.695  17.857  1.00 28.58           C
ANISOU 3415  CA  LEU B  76     2753   2577   5528    109     46    780       C
ATOM   3416  C   LEU B  76    -107.473  47.738  16.340  1.00 31.37           C
ANISOU 3416  C   LEU B  76     3080   2954   5884    164    136    742       C
ATOM   3417  O   LEU B  76    -108.410  48.350  15.818  1.00 38.19           O
ANISOU 3417  O   LEU B  76     3969   3782   6758    228    199    710       O
ATOM   3418  CB  LEU B  76    -107.199  49.115  18.404  1.00 28.89           C
ANISOU 3418  CB  LEU B  76     2890   2573   5514     83     53    711       C
ATOM   3419  CG  LEU B  76    -107.322  49.231  19.924  1.00 33.34           C
ANISOU 3419  CG  LEU B  76     3496   3108   6063     52    -15    752       C
ATOM   3420  CD1 LEU B  76    -107.072  50.656  20.390  1.00 30.35           C
ANISOU 3420  CD1 LEU B  76     3199   2697   5634     29     10    701       C
ATOM   3421  CD2 LEU B  76    -108.689  48.747  20.378  1.00 39.85           C
ANISOU 3421  CD2 LEU B  76     4281   3906   6956     97    -31    828       C
ATOM   3422  N   GLY B  77    -106.542  47.114  15.625  1.00 32.12           N
ANISOU 3422  N   GLY B  77     3139   3102   5965    147    140    744       N
ATOM   3423  CA  GLY B  77    -106.631  47.053  14.180  1.00 35.15           C
ANISOU 3423  CA  GLY B  77     3502   3516   6339    209    228    719       C
ATOM   3424  C   GLY B  77    -106.157  48.289  13.455  1.00 34.53           C
ANISOU 3424  C   GLY B  77     3511   3419   6189    208    267    605       C
ATOM   3425  O   GLY B  77    -106.619  48.557  12.341  1.00 39.49           O
ANISOU 3425  O   GLY B  77     4159   4047   6800    278    338    566       O
ATOM   3426  N   VAL B  78    -105.243  49.054  14.052  1.00 32.36           N
ANISOU 3426  N   VAL B  78     3293   3131   5871    135    220    554       N
ATOM   3427  CA  VAL B  78    -104.726  50.250  13.400  1.00 29.46           C
ANISOU 3427  CA  VAL B  78     2994   2750   5449    123    244    459       C
ATOM   3428  C   VAL B  78    -103.800  49.847  12.262  1.00 29.21           C
ANISOU 3428  C   VAL B  78     2944   2774   5379    130    270    439       C
ATOM   3429  O   VAL B  78    -102.904  49.009  12.433  1.00 32.79           O
ANISOU 3429  O   VAL B  78     3358   3270   5831     93    238    481       O
ATOM   3430  CB  VAL B  78    -104.004  51.149  14.413  1.00 28.26           C
ANISOU 3430  CB  VAL B  78     2890   2578   5271     52    198    433       C
ATOM   3431  CG1 VAL B  78    -103.344  52.324  13.706  1.00 25.42           C
ANISOU 3431  CG1 VAL B  78     2578   2213   4869     32    215    351       C
ATOM   3432  CG2 VAL B  78    -104.980  51.640  15.472  1.00 24.30           C
ANISOU 3432  CG2 VAL B  78     2411   2020   4802     52    182    458       C
ATOM   3433  N   ASP B  79    -104.017  50.442  11.088  1.00 30.01           N
ANISOU 3433  N   ASP B  79     3086   2868   5446    177    320    375       N
ATOM   3434  CA  ASP B  79    -103.200  50.165   9.916  1.00 31.44           C
ANISOU 3434  CA  ASP B  79     3264   3102   5580    194    348    353       C
ATOM   3435  C   ASP B  79    -102.226  51.280   9.577  1.00 30.06           C
ANISOU 3435  C   ASP B  79     3148   2921   5351    147    323    271       C
ATOM   3436  O   ASP B  79    -101.222  51.017   8.909  1.00 35.62           O
ANISOU 3436  O   ASP B  79     3844   3673   6016    137    326    263       O
ATOM   3437  CB  ASP B  79    -104.091  49.916   8.691  1.00 39.51           C
ANISOU 3437  CB  ASP B  79     4298   4130   6585    299    424    345       C
ATOM   3438  CG  ASP B  79    -105.253  48.999   8.993  1.00 47.08           C
ANISOU 3438  CG  ASP B  79     5195   5088   7605    363    461    430       C
ATOM   3439  OD1 ASP B  79    -105.021  47.886   9.512  1.00 52.86           O
ANISOU 3439  OD1 ASP B  79     5835   5861   8387    338    444    526       O
ATOM   3440  OD2 ASP B  79    -106.401  49.399   8.716  1.00 51.26           O
ANISOU 3440  OD2 ASP B  79     5769   5569   8137    439    500    403       O
ATOM   3441  N   ILE B  80    -102.493  52.508  10.019  1.00 28.83           N
ANISOU 3441  N   ILE B  80     3044   2709   5201    116    297    220       N
ATOM   3442  CA  ILE B  80    -101.724  53.667   9.589  1.00 24.97           C
ANISOU 3442  CA  ILE B  80     2600   2212   4676     77    272    150       C
ATOM   3443  C   ILE B  80    -102.007  54.807  10.555  1.00 29.34           C
ANISOU 3443  C   ILE B  80     3176   2708   5266     25    239    140       C
ATOM   3444  O   ILE B  80    -103.062  54.851  11.191  1.00 31.97           O
ANISOU 3444  O   ILE B  80     3514   2992   5640     39    242    165       O
ATOM   3445  CB  ILE B  80    -102.079  54.041   8.127  1.00 27.61           C
ANISOU 3445  CB  ILE B  80     2991   2534   4967    134    294     84       C
ATOM   3446  CG1 ILE B  80    -101.071  55.035   7.549  1.00 29.47           C
ANISOU 3446  CG1 ILE B  80     3258   2775   5164     89    255     23       C
ATOM   3447  CG2 ILE B  80    -103.492  54.593   8.043  1.00 33.79           C
ANISOU 3447  CG2 ILE B  80     3829   3235   5773    179    300     53       C
ATOM   3448  CD1 ILE B  80    -101.237  55.256   6.062  1.00 26.16           C
ANISOU 3448  CD1 ILE B  80     2906   2351   4682    148    263    -42       C
ATOM   3449  N   ALA B  81    -101.053  55.727  10.675  1.00 28.59           N
ANISOU 3449  N   ALA B  81     3086   2619   5157    -32    210    116       N
ATOM   3450  CA  ALA B  81    -101.171  56.866  11.571  1.00 27.57           C
ANISOU 3450  CA  ALA B  81     2963   2446   5066    -83    187    124       C
ATOM   3451  C   ALA B  81    -101.389  58.145  10.774  1.00 32.50           C
ANISOU 3451  C   ALA B  81     3624   3020   5705   -104    157     66       C
ATOM   3452  O   ALA B  81    -100.970  58.259   9.618  1.00 37.44           O
ANISOU 3452  O   ALA B  81     4272   3662   6293    -92    144     14       O
ATOM   3453  CB  ALA B  81     -99.926  57.007  12.452  1.00 20.75           C
ANISOU 3453  CB  ALA B  81     2069   1629   4186   -126    180    159       C
ATOM   3454  N   ALA B  82    -102.047  59.111  11.410  1.00 31.11           N
ANISOU 3454  N   ALA B  82     3457   2777   5585   -140    137     81       N
ATOM   3455  CA  ALA B  82    -102.374  60.382  10.774  1.00 29.16           C
ANISOU 3455  CA  ALA B  82     3246   2461   5372   -176     88     36       C
ATOM   3456  C   ALA B  82    -101.263  61.387  11.058  1.00 32.39           C
ANISOU 3456  C   ALA B  82     3605   2899   5802   -248     63     60       C
ATOM   3457  O   ALA B  82    -101.138  61.883  12.183  1.00 35.37           O
ANISOU 3457  O   ALA B  82     3942   3276   6221   -286     76    127       O
ATOM   3458  CB  ALA B  82    -103.720  60.901  11.271  1.00 30.84           C
ANISOU 3458  CB  ALA B  82     3493   2577   5650   -180     74     50       C
ATOM   3459  N   ASN B  83    -100.454  61.676  10.038  1.00 30.13           N
ANISOU 3459  N   ASN B  83     3321   2641   5485   -258     31     14       N
ATOM   3460  CA  ASN B  83     -99.469  62.757  10.078  1.00 33.49           C
ANISOU 3460  CA  ASN B  83     3694   3087   5942   -323     -4     36       C
ATOM   3461  C   ASN B  83     -98.409  62.540  11.155  1.00 30.69           C
ANISOU 3461  C   ASN B  83     3273   2812   5575   -328     50    107       C
ATOM   3462  O   ASN B  83     -97.914  63.497  11.754  1.00 28.09           O
ANISOU 3462  O   ASN B  83     2888   2492   5294   -374     49    163       O
ATOM   3463  CB  ASN B  83    -100.156  64.114  10.265  1.00 36.92           C
ANISOU 3463  CB  ASN B  83     4126   3433   6470   -390    -61     54       C
ATOM   3464  CG  ASN B  83    -101.259  64.349   9.251  1.00 43.08           C
ANISOU 3464  CG  ASN B  83     4999   4115   7256   -378   -125    -25       C
ATOM   3465  OD1 ASN B  83    -102.432  64.458   9.608  1.00 49.42           O
ANISOU 3465  OD1 ASN B  83     5843   4836   8099   -373   -130    -21       O
ATOM   3466  ND2 ASN B  83    -100.888  64.424   7.978  1.00 42.54           N
ANISOU 3466  ND2 ASN B  83     4975   4051   7139   -366   -177    -98       N
ATOM   3467  N   THR B  84     -98.044  61.285  11.402  1.00 32.92           N
ANISOU 3467  N   THR B  84     3564   3150   5796   -277     95    110       N
ATOM   3468  CA  THR B  84     -96.974  60.969  12.339  1.00 31.70           C
ANISOU 3468  CA  THR B  84     3373   3059   5611   -270    134    162       C
ATOM   3469  C   THR B  84     -96.468  59.568  12.032  1.00 29.74           C
ANISOU 3469  C   THR B  84     3145   2858   5295   -223    150    142       C
ATOM   3470  O   THR B  84     -97.010  58.864  11.176  1.00 32.90           O
ANISOU 3470  O   THR B  84     3573   3249   5678   -196    143    102       O
ATOM   3471  CB  THR B  84     -97.443  61.073  13.795  1.00 34.83           C
ANISOU 3471  CB  THR B  84     3764   3438   6031   -272    168    230       C
ATOM   3472  OG1 THR B  84     -96.329  60.861  14.673  1.00 35.39           O
ANISOU 3472  OG1 THR B  84     3821   3568   6057   -253    204    274       O
ATOM   3473  CG2 THR B  84     -98.511  60.034  14.085  1.00 36.66           C
ANISOU 3473  CG2 THR B  84     4036   3640   6253   -239    174    226       C
ATOM   3474  N   VAL B  85     -95.413  59.175  12.740  1.00 25.00           N
ANISOU 3474  N   VAL B  85     2535   2308   4658   -211    172    175       N
ATOM   3475  CA  VAL B  85     -94.828  57.845  12.610  1.00 23.04           C
ANISOU 3475  CA  VAL B  85     2304   2094   4355   -179    174    169       C
ATOM   3476  C   VAL B  85     -94.716  57.240  14.000  1.00 24.82           C
ANISOU 3476  C   VAL B  85     2551   2320   4561   -164    186    216       C
ATOM   3477  O   VAL B  85     -94.068  57.817  14.882  1.00 27.55           O
ANISOU 3477  O   VAL B  85     2898   2679   4890   -161    204    247       O
ATOM   3478  CB  VAL B  85     -93.450  57.875  11.927  1.00 19.50           C
ANISOU 3478  CB  VAL B  85     1844   1694   3870   -173    168    151       C
ATOM   3479  CG1 VAL B  85     -92.844  56.479  11.902  1.00 19.12           C
ANISOU 3479  CG1 VAL B  85     1818   1671   3778   -147    164    156       C
ATOM   3480  CG2 VAL B  85     -93.569  58.423  10.522  1.00 25.67           C
ANISOU 3480  CG2 VAL B  85     2618   2475   4661   -184    144    103       C
ATOM   3481  N   ILE B  86     -95.349  56.089  14.197  1.00 26.56           N
ANISOU 3481  N   ILE B  86     2787   2526   4778   -151    173    225       N
ATOM   3482  CA  ILE B  86     -95.187  55.309  15.417  1.00 27.06           C
ANISOU 3482  CA  ILE B  86     2882   2584   4813   -139    159    265       C
ATOM   3483  C   ILE B  86     -94.047  54.328  15.176  1.00 29.01           C
ANISOU 3483  C   ILE B  86     3146   2858   5018   -130    133    259       C
ATOM   3484  O   ILE B  86     -94.157  53.426  14.341  1.00 29.23           O
ANISOU 3484  O   ILE B  86     3154   2894   5057   -131    117    254       O
ATOM   3485  CB  ILE B  86     -96.480  54.582  15.801  1.00 29.02           C
ANISOU 3485  CB  ILE B  86     3132   2800   5095   -135    143    290       C
ATOM   3486  CG1 ILE B  86     -97.611  55.590  16.007  1.00 29.66           C
ANISOU 3486  CG1 ILE B  86     3205   2844   5221   -143    166    296       C
ATOM   3487  CG2 ILE B  86     -96.268  53.748  17.054  1.00 27.54           C
ANISOU 3487  CG2 ILE B  86     2985   2604   4875   -128    107    331       C
ATOM   3488  CD1 ILE B  86     -97.320  56.619  17.075  1.00 29.34           C
ANISOU 3488  CD1 ILE B  86     3179   2798   5169   -151    187    328       C
ATOM   3489  N   TRP B  87     -92.945  54.506  15.897  1.00 27.74           N
ANISOU 3489  N   TRP B  87     3023   2708   4807   -116    132    266       N
ATOM   3490  CA  TRP B  87     -91.772  53.668  15.712  1.00 24.54           C
ANISOU 3490  CA  TRP B  87     2647   2314   4362   -106    100    259       C
ATOM   3491  C   TRP B  87     -91.864  52.441  16.609  1.00 29.66           C
ANISOU 3491  C   TRP B  87     3348   2931   4993   -106     40    286       C
ATOM   3492  O   TRP B  87     -92.039  52.563  17.825  1.00 31.11           O
ANISOU 3492  O   TRP B  87     3583   3092   5145    -91     30    305       O
ATOM   3493  CB  TRP B  87     -90.493  54.449  16.010  1.00 22.03           C
ANISOU 3493  CB  TRP B  87     2357   2018   3996    -76    126    252       C
ATOM   3494  CG  TRP B  87     -89.263  53.715  15.595  1.00 21.80           C
ANISOU 3494  CG  TRP B  87     2357   1995   3931    -64     96    238       C
ATOM   3495  CD1 TRP B  87     -88.406  53.027  16.401  1.00 19.51           C
ANISOU 3495  CD1 TRP B  87     2150   1679   3586    -37     57    243       C
ATOM   3496  CD2 TRP B  87     -88.762  53.574  14.262  1.00 20.88           C
ANISOU 3496  CD2 TRP B  87     2200   1904   3830    -75     94    218       C
ATOM   3497  NE1 TRP B  87     -87.396  52.475  15.654  1.00 25.98           N
ANISOU 3497  NE1 TRP B  87     2976   2500   4394    -36     31    230       N
ATOM   3498  CE2 TRP B  87     -87.592  52.795  14.336  1.00 22.27           C
ANISOU 3498  CE2 TRP B  87     2427   2068   3966    -58     58    218       C
ATOM   3499  CE3 TRP B  87     -89.187  54.036  13.012  1.00 22.51           C
ANISOU 3499  CE3 TRP B  87     2343   2137   4072    -93    115    198       C
ATOM   3500  CZ2 TRP B  87     -86.841  52.468  13.211  1.00 23.67           C
ANISOU 3500  CZ2 TRP B  87     2584   2264   4145    -62     48    209       C
ATOM   3501  CZ3 TRP B  87     -88.441  53.709  11.896  1.00 22.91           C
ANISOU 3501  CZ3 TRP B  87     2381   2212   4113    -91    106    185       C
ATOM   3502  CH2 TRP B  87     -87.282  52.932  12.002  1.00 26.97           C
ANISOU 3502  CH2 TRP B  87     2935   2718   4593    -77     76    195       C
ATOM   3503  N   ASP B  88     -91.751  51.261  16.002  1.00 25.47           N
ANISOU 3503  N   ASP B  88     2800   2395   4483   -126     -5    295       N
ATOM   3504  CA  ASP B  88     -91.755  49.999  16.738  1.00 25.16           C
ANISOU 3504  CA  ASP B  88     2799   2318   4442   -141    -86    329       C
ATOM   3505  C   ASP B  88     -90.321  49.714  17.164  1.00 27.27           C
ANISOU 3505  C   ASP B  88     3150   2564   4646   -126   -129    314       C
ATOM   3506  O   ASP B  88     -89.510  49.226  16.374  1.00 26.88           O
ANISOU 3506  O   ASP B  88     3090   2520   4603   -137   -146    310       O
ATOM   3507  CB  ASP B  88     -92.325  48.873  15.882  1.00 30.24           C
ANISOU 3507  CB  ASP B  88     3370   2965   5153   -171   -112    366       C
ATOM   3508  CG  ASP B  88     -92.673  47.635  16.692  1.00 37.03           C
ANISOU 3508  CG  ASP B  88     4244   3784   6040   -198   -204    419       C
ATOM   3509  OD1 ASP B  88     -92.088  47.434  17.777  1.00 38.69           O
ANISOU 3509  OD1 ASP B  88     4545   3954   6201   -198   -272    415       O
ATOM   3510  OD2 ASP B  88     -93.538  46.857  16.236  1.00 39.50           O
ANISOU 3510  OD2 ASP B  88     4479   4105   6425   -216   -213    469       O
ATOM   3511  N   TYR B  89     -90.006  50.025  18.422  1.00 28.75           N
ANISOU 3511  N   TYR B  89     3430   2726   4769    -94   -145    308       N
ATOM   3512  CA  TYR B  89     -88.651  49.824  18.918  1.00 28.91           C
ANISOU 3512  CA  TYR B  89     3553   2718   4714    -60   -182    288       C
ATOM   3513  C   TYR B  89     -88.317  48.354  19.134  1.00 33.64           C
ANISOU 3513  C   TYR B  89     4205   3256   5321    -96   -305    304       C
ATOM   3514  O   TYR B  89     -87.134  48.000  19.149  1.00 38.65           O
ANISOU 3514  O   TYR B  89     4914   3857   5913    -80   -348    285       O
ATOM   3515  CB  TYR B  89     -88.449  50.608  20.213  1.00 27.84           C
ANISOU 3515  CB  TYR B  89     3512   2574   4492      2   -152    280       C
ATOM   3516  CG  TYR B  89     -88.302  52.096  19.997  1.00 31.67           C
ANISOU 3516  CG  TYR B  89     3948   3116   4969     41    -35    275       C
ATOM   3517  CD1 TYR B  89     -87.048  52.681  19.914  1.00 34.30           C
ANISOU 3517  CD1 TYR B  89     4314   3468   5250     96     10    258       C
ATOM   3518  CD2 TYR B  89     -89.418  52.913  19.864  1.00 31.51           C
ANISOU 3518  CD2 TYR B  89     3845   3125   5001     20     24    294       C
ATOM   3519  CE1 TYR B  89     -86.905  54.040  19.714  1.00 34.37           C
ANISOU 3519  CE1 TYR B  89     4260   3531   5267    126    109    269       C
ATOM   3520  CE2 TYR B  89     -89.285  54.273  19.665  1.00 28.64           C
ANISOU 3520  CE2 TYR B  89     3430   2806   4647     42    115    301       C
ATOM   3521  CZ  TYR B  89     -88.026  54.830  19.590  1.00 33.15           C
ANISOU 3521  CZ  TYR B  89     4020   3402   5174     92    156    293       C
ATOM   3522  OH  TYR B  89     -87.883  56.184  19.391  1.00 35.50           O
ANISOU 3522  OH  TYR B  89     4247   3746   5494    108    240    314       O
ATOM   3523  N   LYS B  90     -89.324  47.493  19.306  1.00 35.53           N
ANISOU 3523  N   LYS B  90     4405   3475   5620   -145   -369    346       N
ATOM   3524  CA  LYS B  90     -89.049  46.066  19.427  1.00 38.49           C
ANISOU 3524  CA  LYS B  90     4806   3790   6027   -194   -499    379       C
ATOM   3525  C   LYS B  90     -88.693  45.442  18.087  1.00 37.73           C
ANISOU 3525  C   LYS B  90     4618   3713   6003   -235   -495    404       C
ATOM   3526  O   LYS B  90     -88.048  44.390  18.054  1.00 43.69           O
ANISOU 3526  O   LYS B  90     5403   4415   6780   -274   -596    430       O
ATOM   3527  CB  LYS B  90     -90.247  45.345  20.039  1.00 45.94           C
ANISOU 3527  CB  LYS B  90     5721   4712   7024   -233   -571    431       C
ATOM   3528  CG  LYS B  90     -90.502  45.720  21.482  1.00 53.06           C
ANISOU 3528  CG  LYS B  90     6736   5580   7843   -195   -604    415       C
ATOM   3529  CD  LYS B  90     -91.486  44.771  22.132  1.00 58.28           C
ANISOU 3529  CD  LYS B  90     7382   6205   8556   -240   -714    472       C
ATOM   3530  CE  LYS B  90     -91.465  44.930  23.638  1.00 61.83           C
ANISOU 3530  CE  LYS B  90     7985   6607   8902   -201   -780    454       C
ATOM   3531  NZ  LYS B  90     -91.670  46.348  24.043  1.00 63.53           N
ANISOU 3531  NZ  LYS B  90     8229   6868   9041   -128   -647    422       N
ATOM   3532  N   ARG B  91     -89.103  46.067  16.987  1.00 31.83           N
ANISOU 3532  N   ARG B  91     3769   3036   5291   -226   -387    401       N
ATOM   3533  CA  ARG B  91     -88.737  45.630  15.652  1.00 27.64           C
ANISOU 3533  CA  ARG B  91     3160   2534   4809   -248   -364    424       C
ATOM   3534  C   ARG B  91     -87.718  46.543  14.988  1.00 31.26           C
ANISOU 3534  C   ARG B  91     3640   3025   5214   -208   -294    371       C
ATOM   3535  O   ARG B  91     -87.216  46.199  13.912  1.00 36.65           O
ANISOU 3535  O   ARG B  91     4278   3728   5921   -220   -281    388       O
ATOM   3536  CB  ARG B  91     -89.987  45.539  14.763  1.00 28.10           C
ANISOU 3536  CB  ARG B  91     3092   2645   4938   -257   -298    462       C
ATOM   3537  CG  ARG B  91     -90.926  44.399  15.122  1.00 30.95           C
ANISOU 3537  CG  ARG B  91     3398   2984   5378   -298   -366    540       C
ATOM   3538  CD  ARG B  91     -92.247  44.498  14.365  1.00 36.19           C
ANISOU 3538  CD  ARG B  91     3952   3701   6098   -280   -281    572       C
ATOM   3539  NE  ARG B  91     -92.056  44.752  12.939  1.00 40.55           N
ANISOU 3539  NE  ARG B  91     4450   4308   6650   -256   -192    563       N
ATOM   3540  CZ  ARG B  91     -92.337  45.905  12.338  1.00 35.63           C
ANISOU 3540  CZ  ARG B  91     3829   3723   5987   -212   -100    502       C
ATOM   3541  NH1 ARG B  91     -92.126  46.046  11.037  1.00 35.41           N
ANISOU 3541  NH1 ARG B  91     3766   3739   5948   -188    -37    495       N
ATOM   3542  NH2 ARG B  91     -92.835  46.916  13.037  1.00 32.66           N
ANISOU 3542  NH2 ARG B  91     3493   3336   5582   -194    -80    452       N
ATOM   3543  N   ASP B  92     -87.394  47.683  15.603  1.00 31.69           N
ANISOU 3543  N   ASP B  92     3754   3086   5199   -159   -249    320       N
ATOM   3544  CA  ASP B  92     -86.522  48.693  15.005  1.00 33.94           C
ANISOU 3544  CA  ASP B  92     4040   3410   5444   -118   -179    281       C
ATOM   3545  C   ASP B  92     -87.010  49.056  13.604  1.00 30.12           C
ANISOU 3545  C   ASP B  92     3452   2987   5005   -130   -113    282       C
ATOM   3546  O   ASP B  92     -86.244  49.110  12.640  1.00 32.65           O
ANISOU 3546  O   ASP B  92     3754   3332   5320   -124    -96    276       O
ATOM   3547  CB  ASP B  92     -85.066  48.222  14.984  1.00 40.32           C
ANISOU 3547  CB  ASP B  92     4925   4181   6216   -103   -228    272       C
ATOM   3548  CG  ASP B  92     -84.501  48.013  16.377  1.00 50.02           C
ANISOU 3548  CG  ASP B  92     6288   5341   7377    -71   -292    255       C
ATOM   3549  OD1 ASP B  92     -84.850  48.795  17.287  1.00 54.55           O
ANISOU 3549  OD1 ASP B  92     6899   5924   7904    -30   -253    238       O
ATOM   3550  OD2 ASP B  92     -83.709  47.065  16.564  1.00 53.76           O
ANISOU 3550  OD2 ASP B  92     6837   5748   7840    -84   -383    262       O
ATOM   3551  N   ALA B  93     -88.311  49.305  13.503  1.00 24.84           N
ANISOU 3551  N   ALA B  93     2725   2338   4373   -142    -78    290       N
ATOM   3552  CA  ALA B  93     -88.962  49.536  12.223  1.00 23.96           C
ANISOU 3552  CA  ALA B  93     2536   2273   4296   -144    -24    288       C
ATOM   3553  C   ALA B  93     -90.240  50.320  12.473  1.00 23.19           C
ANISOU 3553  C   ALA B  93     2412   2182   4218   -138     17    274       C
ATOM   3554  O   ALA B  93     -90.752  50.330  13.598  1.00 26.09           O
ANISOU 3554  O   ALA B  93     2806   2519   4587   -142     -2    286       O
ATOM   3555  CB  ALA B  93     -89.270  48.209  11.510  1.00 25.98           C
ANISOU 3555  CB  ALA B  93     2741   2531   4598   -168    -47    344       C
ATOM   3556  N   PRO B  94     -90.771  50.998  11.456  1.00 24.71           N
ANISOU 3556  N   PRO B  94     2563   2404   4420   -128     67    249       N
ATOM   3557  CA  PRO B  94     -92.064  51.667  11.627  1.00 23.82           C
ANISOU 3557  CA  PRO B  94     2433   2283   4334   -124     96    237       C
ATOM   3558  C   PRO B  94     -93.152  50.654  11.940  1.00 27.22           C
ANISOU 3558  C   PRO B  94     2840   2695   4808   -127     83    282       C
ATOM   3559  O   PRO B  94     -93.163  49.541  11.410  1.00 31.62           O
ANISOU 3559  O   PRO B  94     3365   3264   5386   -129     73    322       O
ATOM   3560  CB  PRO B  94     -92.299  52.345  10.272  1.00 22.32           C
ANISOU 3560  CB  PRO B  94     2222   2120   4141   -109    133    199       C
ATOM   3561  CG  PRO B  94     -90.947  52.457   9.658  1.00 25.07           C
ANISOU 3561  CG  PRO B  94     2577   2496   4451   -107    125    185       C
ATOM   3562  CD  PRO B  94     -90.192  51.254  10.125  1.00 24.13           C
ANISOU 3562  CD  PRO B  94     2472   2369   4328   -116     90    227       C
ATOM   3563  N   ALA B  95     -94.071  51.045  12.822  1.00 24.57           N
ANISOU 3563  N   ALA B  95     2513   2332   4492   -128     85    287       N
ATOM   3564  CA  ALA B  95     -95.158  50.147  13.184  1.00 21.99           C
ANISOU 3564  CA  ALA B  95     2157   1986   4210   -127     69    336       C
ATOM   3565  C   ALA B  95     -96.146  49.944  12.044  1.00 24.50           C
ANISOU 3565  C   ALA B  95     2427   2320   4560    -96    118    340       C
ATOM   3566  O   ALA B  95     -96.927  48.989  12.083  1.00 26.92           O
ANISOU 3566  O   ALA B  95     2690   2626   4911    -85    115    396       O
ATOM   3567  CB  ALA B  95     -95.888  50.671  14.421  1.00 21.33           C
ANISOU 3567  CB  ALA B  95     2102   1868   4134   -130     59    343       C
ATOM   3568  N   HIS B  96     -96.126  50.807  11.031  1.00 24.59           N
ANISOU 3568  N   HIS B  96     2449   2347   4548    -76    160    286       N
ATOM   3569  CA  HIS B  96     -97.075  50.733   9.933  1.00 28.90           C
ANISOU 3569  CA  HIS B  96     2977   2901   5101    -28    209    277       C
ATOM   3570  C   HIS B  96     -96.347  50.892   8.605  1.00 33.58           C
ANISOU 3570  C   HIS B  96     3580   3532   5648     -9    231    243       C
ATOM   3571  O   HIS B  96     -95.270  51.488   8.525  1.00 38.79           O
ANISOU 3571  O   HIS B  96     4262   4202   6274    -36    210    210       O
ATOM   3572  CB  HIS B  96     -98.171  51.795  10.076  1.00 29.43           C
ANISOU 3572  CB  HIS B  96     3075   2925   5184    -13    225    236       C
ATOM   3573  CG  HIS B  96     -98.873  51.755  11.396  1.00 27.94           C
ANISOU 3573  CG  HIS B  96     2881   2698   5035    -30    204    272       C
ATOM   3574  ND1 HIS B  96     -98.731  52.744  12.346  1.00 25.36           N
ANISOU 3574  ND1 HIS B  96     2584   2342   4708    -64    184    256       N
ATOM   3575  CD2 HIS B  96     -99.707  50.834  11.934  1.00 24.96           C
ANISOU 3575  CD2 HIS B  96     2470   2311   4700    -14    199    332       C
ATOM   3576  CE1 HIS B  96     -99.456  52.439  13.407  1.00 25.30           C
ANISOU 3576  CE1 HIS B  96     2574   2308   4731    -66    168    300       C
ATOM   3577  NE2 HIS B  96    -100.058  51.285  13.183  1.00 28.34           N
ANISOU 3577  NE2 HIS B  96     2920   2702   5145    -39    171    344       N
ATOM   3578  N   ILE B  97     -96.965  50.349   7.555  1.00 37.53           N
ANISOU 3578  N   ILE B  97     4065   4054   6140     46    279    257       N
ATOM   3579  CA  ILE B  97     -96.329  50.317   6.241  1.00 45.87           C
ANISOU 3579  CA  ILE B  97     5135   5151   7141     76    305    237       C
ATOM   3580  C   ILE B  97     -96.323  51.707   5.614  1.00 47.73           C
ANISOU 3580  C   ILE B  97     5437   5369   7331     84    295    146       C
ATOM   3581  O   ILE B  97     -95.263  52.282   5.341  1.00 48.50           O
ANISOU 3581  O   ILE B  97     5551   5481   7396     55    265    114       O
ATOM   3582  CB  ILE B  97     -97.032  49.295   5.331  1.00 54.65           C
ANISOU 3582  CB  ILE B  97     6215   6298   8252    149    371    292       C
ATOM   3583  CG1 ILE B  97     -96.984  47.902   5.960  1.00 59.94           C
ANISOU 3583  CG1 ILE B  97     6802   6986   8988    126    365    400       C
ATOM   3584  CG2 ILE B  97     -96.404  49.288   3.945  1.00 57.73           C
ANISOU 3584  CG2 ILE B  97     6632   6733   8569    190    404    275       C
ATOM   3585  CD1 ILE B  97     -95.580  47.392   6.211  1.00 64.00           C
ANISOU 3585  CD1 ILE B  97     7297   7514   9505     63    314    433       C
ATOM   3586  N   SER B  98     -97.505  52.260   5.372  1.00 39.20           N
ANISOU 3586  N   SER B  98     4394   4249   6252    122    312    106       N
ATOM   3587  CA  SER B  98     -97.647  53.538   4.694  1.00 31.82           C
ANISOU 3587  CA  SER B  98     3529   3281   5280    127    286     21       C
ATOM   3588  C   SER B  98     -97.761  54.676   5.703  1.00 28.20           C
ANISOU 3588  C   SER B  98     3075   2768   4870     61    236     -4       C
ATOM   3589  O   SER B  98     -97.882  54.467   6.913  1.00 25.46           O
ANISOU 3589  O   SER B  98     2690   2410   4573     28    233     40       O
ATOM   3590  CB  SER B  98     -98.867  53.518   3.770  1.00 36.71           C
ANISOU 3590  CB  SER B  98     4209   3874   5865    214    325    -13       C
ATOM   3591  OG  SER B  98     -98.775  52.461   2.833  1.00 38.18           O
ANISOU 3591  OG  SER B  98     4385   4120   6002    288    388     26       O
ATOM   3592  N   THR B  99     -97.720  55.899   5.182  1.00 30.55           N
ANISOU 3592  N   THR B  99     3420   3033   5154     43    191    -69       N
ATOM   3593  CA  THR B  99     -97.833  57.106   5.987  1.00 30.89           C
ANISOU 3593  CA  THR B  99     3460   3025   5252    -22    144    -81       C
ATOM   3594  C   THR B  99     -98.867  58.034   5.366  1.00 30.85           C
ANISOU 3594  C   THR B  99     3527   2943   5252    -10    107   -145       C
ATOM   3595  O   THR B  99     -99.330  57.828   4.240  1.00 34.02           O
ANISOU 3595  O   THR B  99     3997   3334   5596     54    114   -192       O
ATOM   3596  CB  THR B  99     -96.485  57.831   6.115  1.00 30.83           C
ANISOU 3596  CB  THR B  99     3418   3050   5245    -80    106    -78       C
ATOM   3597  OG1 THR B  99     -95.956  58.096   4.810  1.00 34.89           O
ANISOU 3597  OG1 THR B  99     3967   3585   5703    -63     77   -126       O
ATOM   3598  CG2 THR B  99     -95.492  56.987   6.900  1.00 31.13           C
ANISOU 3598  CG2 THR B  99     3404   3145   5280    -89    135    -20       C
ATOM   3599  N   ILE B 100     -99.231  59.067   6.120  1.00 29.42           N
ANISOU 3599  N   ILE B 100     3338   2702   5137    -70     67   -142       N
ATOM   3600  CA  ILE B 100    -100.162  60.095   5.670  1.00 29.77           C
ANISOU 3600  CA  ILE B 100     3453   2652   5205    -79      9   -197       C
ATOM   3601  C   ILE B 100     -99.505  61.443   5.924  1.00 31.77           C
ANISOU 3601  C   ILE B 100     3671   2886   5514   -172    -64   -191       C
ATOM   3602  O   ILE B 100     -99.355  61.854   7.081  1.00 30.93           O
ANISOU 3602  O   ILE B 100     3499   2779   5475   -226    -55   -130       O
ATOM   3603  CB  ILE B 100    -101.520  60.010   6.381  1.00 31.74           C
ANISOU 3603  CB  ILE B 100     3724   2830   5505    -60     31   -181       C
ATOM   3604  CG1 ILE B 100    -102.224  58.697   6.037  1.00 33.12           C
ANISOU 3604  CG1 ILE B 100     3924   3028   5634     42    104   -177       C
ATOM   3605  CG2 ILE B 100    -102.392  61.195   5.997  1.00 27.87           C
ANISOU 3605  CG2 ILE B 100     3311   2226   5051    -84    -46   -236       C
ATOM   3606  CD1 ILE B 100    -103.524  58.485   6.784  1.00 27.01           C
ANISOU 3606  CD1 ILE B 100     3159   2192   4911     71    131   -150       C
ATOM   3607  N   GLY B 101     -99.113  62.127   4.854  1.00 32.65           N
ANISOU 3607  N   GLY B 101     3823   2984   5597   -187   -136   -246       N
ATOM   3608  CA  GLY B 101     -98.502  63.440   4.990  1.00 37.04           C
ANISOU 3608  CA  GLY B 101     4331   3522   6219   -278   -216   -230       C
ATOM   3609  C   GLY B 101     -97.222  63.446   5.796  1.00 38.59           C
ANISOU 3609  C   GLY B 101     4417   3806   6440   -315   -177   -154       C
ATOM   3610  O   GLY B 101     -97.010  64.351   6.614  1.00 39.59           O
ANISOU 3610  O   GLY B 101     4473   3921   6649   -381   -194    -96       O
ATOM   3611  N   VAL B 102     -96.359  62.452   5.588  1.00 38.89           N
ANISOU 3611  N   VAL B 102     4440   3930   6407   -267   -124   -149       N
ATOM   3612  CA  VAL B 102     -95.116  62.342   6.344  1.00 33.22           C
ANISOU 3612  CA  VAL B 102     3637   3287   5697   -283    -85    -85       C
ATOM   3613  C   VAL B 102     -93.928  62.261   5.394  1.00 30.49           C
ANISOU 3613  C   VAL B 102     3286   3003   5298   -270   -109   -104       C
ATOM   3614  O   VAL B 102     -93.062  63.142   5.389  1.00 36.61           O
ANISOU 3614  O   VAL B 102     4003   3799   6106   -312   -148    -78       O
ATOM   3615  CB  VAL B 102     -95.142  61.125   7.286  1.00 36.26           C
ANISOU 3615  CB  VAL B 102     4010   3706   6060   -243     -1    -45       C
ATOM   3616  CG1 VAL B 102     -93.815  60.997   8.011  1.00 38.23           C
ANISOU 3616  CG1 VAL B 102     4201   4023   6302   -248     31      8       C
ATOM   3617  CG2 VAL B 102     -96.288  61.242   8.279  1.00 37.54           C
ANISOU 3617  CG2 VAL B 102     4176   3811   6275   -255     19    -18       C
ATOM   3618  N   CYS B 103     -93.877  61.202   4.588  1.00 28.96           N
ANISOU 3618  N   CYS B 103     3143   2839   5023   -209    -83   -139       N
ATOM   3619  CA  CYS B 103     -92.759  60.948   3.689  1.00 28.83           C
ANISOU 3619  CA  CYS B 103     3126   2882   4944   -188    -97   -150       C
ATOM   3620  C   CYS B 103     -93.285  60.674   2.289  1.00 32.13           C
ANISOU 3620  C   CYS B 103     3636   3285   5286   -138   -124   -216       C
ATOM   3621  O   CYS B 103     -94.179  59.842   2.114  1.00 36.94           O
ANISOU 3621  O   CYS B 103     4296   3880   5861    -83    -75   -232       O
ATOM   3622  CB  CYS B 103     -91.918  59.765   4.176  1.00 31.43           C
ANISOU 3622  CB  CYS B 103     3424   3276   5244   -155    -27   -103       C
ATOM   3623  SG  CYS B 103     -90.708  59.159   2.978  1.00 40.63           S
ANISOU 3623  SG  CYS B 103     4604   4507   6327   -115    -32   -111       S
ATOM   3624  N   SER B 104     -92.709  61.359   1.296  1.00 31.75           N
ANISOU 3624  N   SER B 104     3611   3245   5207   -149   -199   -250       N
ATOM   3625  CA  SER B 104     -93.178  61.222  -0.080  1.00 38.31           C
ANISOU 3625  CA  SER B 104     4550   4058   5947    -93   -233   -319       C
ATOM   3626  C   SER B 104     -93.094  59.784  -0.572  1.00 38.77           C
ANISOU 3626  C   SER B 104     4637   4174   5918     -8   -142   -306       C
ATOM   3627  O   SER B 104     -93.927  59.354  -1.378  1.00 41.50           O
ANISOU 3627  O   SER B 104     5075   4502   6193     64   -121   -348       O
ATOM   3628  CB  SER B 104     -92.367  62.134  -1.000  1.00 46.72           C
ANISOU 3628  CB  SER B 104     5630   5133   6990   -122   -338   -347       C
ATOM   3629  OG  SER B 104     -92.291  63.446  -0.474  1.00 61.37           O
ANISOU 3629  OG  SER B 104     7426   6944   8947   -212   -422   -332       O
ATOM   3630  N   MET B 105     -92.103  59.026  -0.100  1.00 36.64           N
ANISOU 3630  N   MET B 105     4294   3971   5655     -9    -87   -243       N
ATOM   3631  CA  MET B 105     -91.919  57.666  -0.592  1.00 37.06           C
ANISOU 3631  CA  MET B 105     4362   4079   5643     59    -10   -213       C
ATOM   3632  C   MET B 105     -92.966  56.706  -0.040  1.00 35.81           C
ANISOU 3632  C   MET B 105     4197   3905   5503     94     70   -186       C
ATOM   3633  O   MET B 105     -93.337  55.744  -0.721  1.00 40.14           O
ANISOU 3633  O   MET B 105     4777   4481   5995    167    131   -170       O
ATOM   3634  CB  MET B 105     -90.513  57.175  -0.252  1.00 35.86           C
ANISOU 3634  CB  MET B 105     4139   3985   5500     38      8   -153       C
ATOM   3635  CG  MET B 105     -89.547  57.317  -1.406  1.00 37.59           C
ANISOU 3635  CG  MET B 105     4386   4248   5648     61    -29   -164       C
ATOM   3636  SD  MET B 105     -90.192  56.470  -2.859  1.00 44.75           S
ANISOU 3636  SD  MET B 105     5388   5177   6436    160     17   -182       S
ATOM   3637  CE  MET B 105     -89.087  57.068  -4.122  1.00 45.15           C
ANISOU 3637  CE  MET B 105     5484   5266   6405    173    -59   -207       C
ATOM   3638  N   THR B 106     -93.455  56.945   1.176  1.00 31.52           N
ANISOU 3638  N   THR B 106     3611   3322   5041     49     72   -169       N
ATOM   3639  CA  THR B 106     -94.421  56.054   1.803  1.00 32.25           C
ANISOU 3639  CA  THR B 106     3690   3400   5163     77    137   -135       C
ATOM   3640  C   THR B 106     -95.818  56.646   1.917  1.00 33.24           C
ANISOU 3640  C   THR B 106     3866   3452   5312     90    125   -179       C
ATOM   3641  O   THR B 106     -96.736  55.935   2.340  1.00 34.13           O
ANISOU 3641  O   THR B 106     3971   3551   5447    125    179   -151       O
ATOM   3642  CB  THR B 106     -93.940  55.646   3.203  1.00 29.30           C
ANISOU 3642  CB  THR B 106     3238   3038   4856     27    152    -72       C
ATOM   3643  OG1 THR B 106     -93.755  56.818   4.005  1.00 27.44           O
ANISOU 3643  OG1 THR B 106     2984   2770   4674    -36    105    -85       O
ATOM   3644  CG2 THR B 106     -92.631  54.888   3.112  1.00 28.86           C
ANISOU 3644  CG2 THR B 106     3147   3041   4779     23    163    -27       C
ATOM   3645  N   ASP B 107     -96.007  57.913   1.561  1.00 33.98           N
ANISOU 3645  N   ASP B 107     4009   3494   5409     60     49   -242       N
ATOM   3646  CA  ASP B 107     -97.319  58.531   1.684  1.00 29.58           C
ANISOU 3646  CA  ASP B 107     3510   2849   4881     66     25   -284       C
ATOM   3647  C   ASP B 107     -98.293  57.929   0.685  1.00 32.37           C
ANISOU 3647  C   ASP B 107     3958   3186   5155    173     68   -323       C
ATOM   3648  O   ASP B 107     -97.995  57.825  -0.509  1.00 38.30           O
ANISOU 3648  O   ASP B 107     4776   3963   5814    228     61   -360       O
ATOM   3649  CB  ASP B 107     -97.228  60.040   1.466  1.00 32.51           C
ANISOU 3649  CB  ASP B 107     3913   3159   5282     -2    -85   -336       C
ATOM   3650  CG  ASP B 107     -96.927  60.796   2.740  1.00 38.06           C
ANISOU 3650  CG  ASP B 107     4526   3846   6090    -96   -109   -286       C
ATOM   3651  OD1 ASP B 107     -96.774  60.148   3.795  1.00 39.91           O
ANISOU 3651  OD1 ASP B 107     4691   4115   6358   -102    -44   -224       O
ATOM   3652  OD2 ASP B 107     -96.842  62.040   2.682  1.00 40.88           O
ANISOU 3652  OD2 ASP B 107     4882   4155   6496   -162   -197   -304       O
ATOM   3653  N   ILE B 108     -99.459  57.520   1.182  1.00 30.66           N
ANISOU 3653  N   ILE B 108     3750   2928   4970    214    117   -309       N
ATOM   3654  CA  ILE B 108    -100.592  57.246   0.308  1.00 30.58           C
ANISOU 3654  CA  ILE B 108     3846   2879   4893    325    152   -355       C
ATOM   3655  C   ILE B 108    -101.501  58.461   0.188  1.00 35.54           C
ANISOU 3655  C   ILE B 108     4577   3387   5539    310     65   -436       C
ATOM   3656  O   ILE B 108    -102.340  58.512  -0.724  1.00 35.99           O
ANISOU 3656  O   ILE B 108     4761   3392   5521    405     66   -501       O
ATOM   3657  CB  ILE B 108    -101.398  56.036   0.809  1.00 30.23           C
ANISOU 3657  CB  ILE B 108     3752   2858   4874    394    258   -285       C
ATOM   3658  CG1 ILE B 108    -101.937  56.311   2.212  1.00 26.89           C
ANISOU 3658  CG1 ILE B 108     3271   2385   4562    326    242   -251       C
ATOM   3659  CG2 ILE B 108    -100.538  54.782   0.799  1.00 24.71           C
ANISOU 3659  CG2 ILE B 108     2958   2268   4162    407    330   -199       C
ATOM   3660  CD1 ILE B 108    -102.797  55.204   2.753  1.00 27.69           C
ANISOU 3660  CD1 ILE B 108     3321   2501   4698    390    327   -181       C
ATOM   3661  N   ALA B 109    -101.353  59.438   1.079  1.00 35.49           N
ANISOU 3661  N   ALA B 109     4524   3331   5628    197     -9   -430       N
ATOM   3662  CA  ALA B 109    -102.153  60.652   1.072  1.00 33.03           C
ANISOU 3662  CA  ALA B 109     4294   2897   5359    158   -106   -491       C
ATOM   3663  C   ALA B 109    -101.455  61.686   1.940  1.00 34.17           C
ANISOU 3663  C   ALA B 109     4347   3030   5607     20   -181   -454       C
ATOM   3664  O   ALA B 109    -100.614  61.352   2.777  1.00 36.91           O
ANISOU 3664  O   ALA B 109     4575   3455   5993    -26   -136   -381       O
ATOM   3665  CB  ALA B 109    -103.574  60.396   1.583  1.00 31.52           C
ANISOU 3665  CB  ALA B 109     4141   2630   5204    213    -62   -487       C
ATOM   3666  N   LYS B 110    -101.809  62.950   1.724  1.00 39.98           N
ANISOU 3666  N   LYS B 110     5142   3664   6387    -41   -298   -502       N
ATOM   3667  CA  LYS B 110    -101.314  64.022   2.573  1.00 40.20           C
ANISOU 3667  CA  LYS B 110     5074   3673   6529   -170   -364   -450       C
ATOM   3668  C   LYS B 110    -102.265  64.337   3.717  1.00 39.81           C
ANISOU 3668  C   LYS B 110     4997   3548   6580   -207   -350   -404       C
ATOM   3669  O   LYS B 110    -101.824  64.851   4.751  1.00 39.06           O
ANISOU 3669  O   LYS B 110     4792   3472   6576   -292   -349   -326       O
ATOM   3670  CB  LYS B 110    -101.070  65.284   1.741  1.00 44.18           C
ANISOU 3670  CB  LYS B 110     5632   4108   7047   -237   -515   -504       C
ATOM   3671  CG  LYS B 110    -100.906  65.016   0.255  1.00 53.41           C
ANISOU 3671  CG  LYS B 110     6925   5285   8084   -158   -554   -594       C
ATOM   3672  CD  LYS B 110     -99.786  65.848  -0.345  1.00 64.47           C
ANISOU 3672  CD  LYS B 110     8295   6711   9488   -233   -666   -601       C
ATOM   3673  CE  LYS B 110     -98.432  65.415   0.197  1.00 72.58           C
ANISOU 3673  CE  LYS B 110     9170   7876  10531   -258   -588   -516       C
ATOM   3674  NZ  LYS B 110     -97.305  66.094  -0.503  1.00 77.82           N
ANISOU 3674  NZ  LYS B 110     9806   8577  11186   -309   -686   -520       N
ATOM   3675  N   LYS B 111    -103.550  64.028   3.557  1.00 43.20           N
ANISOU 3675  N   LYS B 111     5526   3896   6992   -135   -333   -446       N
ATOM   3676  CA  LYS B 111    -104.566  64.259   4.567  1.00 44.94           C
ANISOU 3676  CA  LYS B 111     5736   4038   7301   -157   -320   -405       C
ATOM   3677  C   LYS B 111    -105.352  62.978   4.805  1.00 40.27           C
ANISOU 3677  C   LYS B 111     5164   3473   6666    -43   -205   -393       C
ATOM   3678  O   LYS B 111    -105.620  62.227   3.858  1.00 39.71           O
ANISOU 3678  O   LYS B 111     5171   3419   6497     66   -165   -447       O
ATOM   3679  CB  LYS B 111    -105.524  65.380   4.139  1.00 52.50           C
ANISOU 3679  CB  LYS B 111     6809   4834   8305   -190   -442   -467       C
ATOM   3680  CG  LYS B 111    -104.848  66.712   3.861  1.00 61.65           C
ANISOU 3680  CG  LYS B 111     7945   5953   9528   -314   -579   -469       C
ATOM   3681  CD  LYS B 111    -104.217  67.284   5.118  1.00 71.02           C
ANISOU 3681  CD  LYS B 111     8967   7184  10832   -426   -563   -351       C
ATOM   3682  CE  LYS B 111    -103.620  68.658   4.858  1.00 78.59           C
ANISOU 3682  CE  LYS B 111     9884   8101  11876   -550   -699   -333       C
ATOM   3683  NZ  LYS B 111    -103.005  69.240   6.084  1.00 80.99           N
ANISOU 3683  NZ  LYS B 111    10021   8456  12295   -645   -666   -203       N
ATOM   3684  N   PRO B 112    -105.733  62.697   6.054  1.00 36.46           N
ANISOU 3684  N   PRO B 112     4606   2996   6252    -61   -149   -314       N
ATOM   3685  CA  PRO B 112    -106.541  61.496   6.321  1.00 37.18           C
ANISOU 3685  CA  PRO B 112     4702   3107   6315     42    -52   -291       C
ATOM   3686  C   PRO B 112    -107.921  61.542   5.691  1.00 43.74           C
ANISOU 3686  C   PRO B 112     5666   3826   7128    134    -63   -355       C
ATOM   3687  O   PRO B 112    -108.543  60.485   5.525  1.00 49.34           O
ANISOU 3687  O   PRO B 112     6392   4561   7794    248     23   -347       O
ATOM   3688  CB  PRO B 112    -106.633  61.462   7.853  1.00 33.09           C
ANISOU 3688  CB  PRO B 112     4087   2602   5882    -16    -21   -194       C
ATOM   3689  CG  PRO B 112    -105.506  62.326   8.330  1.00 33.16           C
ANISOU 3689  CG  PRO B 112     4019   2647   5933   -130    -66   -158       C
ATOM   3690  CD  PRO B 112    -105.346  63.391   7.292  1.00 33.70           C
ANISOU 3690  CD  PRO B 112     4154   2650   5999   -170   -164   -231       C
ATOM   3691  N   THR B 113    -108.421  62.726   5.340  1.00 44.06           N
ANISOU 3691  N   THR B 113     5802   3736   7202     90   -168   -414       N
ATOM   3692  CA  THR B 113    -109.740  62.853   4.738  1.00 45.75           C
ANISOU 3692  CA  THR B 113     6167   3822   7393    182   -190   -486       C
ATOM   3693  C   THR B 113    -109.775  62.419   3.280  1.00 46.28           C
ANISOU 3693  C   THR B 113     6360   3898   7327    304   -179   -580       C
ATOM   3694  O   THR B 113    -110.869  62.294   2.719  1.00 53.20           O
ANISOU 3694  O   THR B 113     7372   4683   8157    419   -170   -640       O
ATOM   3695  CB  THR B 113    -110.229  64.300   4.845  1.00 51.24           C
ANISOU 3695  CB  THR B 113     6934   4360   8176     85   -327   -517       C
ATOM   3696  OG1 THR B 113    -109.204  65.185   4.374  1.00 49.44           O
ANISOU 3696  OG1 THR B 113     6689   4142   7954    -20   -429   -542       O
ATOM   3697  CG2 THR B 113    -110.572  64.639   6.285  1.00 53.02           C
ANISOU 3697  CG2 THR B 113     7061   4557   8527      1   -316   -416       C
ATOM   3698  N   GLU B 114    -108.621  62.195   2.657  1.00 41.70           N
ANISOU 3698  N   GLU B 114     5744   3424   6678    291   -175   -592       N
ATOM   3699  CA  GLU B 114    -108.596  61.803   1.257  1.00 41.36           C
ANISOU 3699  CA  GLU B 114     5823   3396   6495    409   -162   -674       C
ATOM   3700  C   GLU B 114    -109.265  60.444   1.069  1.00 41.86           C
ANISOU 3700  C   GLU B 114     5893   3518   6494    572    -13   -645       C
ATOM   3701  O   GLU B 114    -109.348  59.626   1.990  1.00 42.05           O
ANISOU 3701  O   GLU B 114     5788   3611   6576    575     79   -550       O
ATOM   3702  CB  GLU B 114    -107.160  61.773   0.736  1.00 41.27           C
ANISOU 3702  CB  GLU B 114     5753   3497   6432    358   -180   -672       C
ATOM   3703  CG  GLU B 114    -106.449  63.116   0.840  1.00 50.01           C
ANISOU 3703  CG  GLU B 114     6839   4554   7606    204   -326   -689       C
ATOM   3704  CD  GLU B 114    -105.091  63.119   0.168  1.00 58.99           C
ANISOU 3704  CD  GLU B 114     7938   5793   8682    173   -352   -696       C
ATOM   3705  OE1 GLU B 114    -104.867  62.280  -0.731  1.00 63.75           O
ANISOU 3705  OE1 GLU B 114     8591   6467   9163    281   -286   -722       O
ATOM   3706  OE2 GLU B 114    -104.244  63.958   0.542  1.00 60.01           O
ANISOU 3706  OE2 GLU B 114     7982   5932   8886     43   -433   -666       O
ATOM   3707  N   THR B 115    -109.752  60.218  -0.154  1.00 42.03           N
ANISOU 3707  N   THR B 115     6070   3510   6392    715      8   -724       N
ATOM   3708  CA  THR B 115    -110.548  59.028  -0.442  1.00 46.47           C
ANISOU 3708  CA  THR B 115     6652   4114   6892    891    154   -694       C
ATOM   3709  C   THR B 115    -109.782  57.743  -0.148  1.00 48.97           C
ANISOU 3709  C   THR B 115     6793   4603   7210    902    278   -581       C
ATOM   3710  O   THR B 115    -110.377  56.748   0.284  1.00 48.77           O
ANISOU 3710  O   THR B 115     6693   4624   7215    984    390   -500       O
ATOM   3711  CB  THR B 115    -111.003  59.052  -1.904  1.00 50.81           C
ANISOU 3711  CB  THR B 115     7406   4615   7284   1051    159   -798       C
ATOM   3712  OG1 THR B 115    -111.641  60.303  -2.185  1.00 54.76           O
ANISOU 3712  OG1 THR B 115     8083   4937   7785   1024     13   -910       O
ATOM   3713  CG2 THR B 115    -111.982  57.925  -2.187  1.00 55.89           C
ANISOU 3713  CG2 THR B 115     8077   5289   7870   1252    319   -760       C
ATOM   3714  N   ILE B 116    -108.464  57.752  -0.356  1.00 50.04           N
ANISOU 3714  N   ILE B 116     6859   4831   7324    818    251   -569       N
ATOM   3715  CA  ILE B 116    -107.672  56.536  -0.222  1.00 45.28           C
ANISOU 3715  CA  ILE B 116     6110   4378   6714    829    355   -468       C
ATOM   3716  C   ILE B 116    -107.635  56.026   1.216  1.00 42.61           C
ANISOU 3716  C   ILE B 116     5605   4080   6503    748    385   -362       C
ATOM   3717  O   ILE B 116    -107.425  54.828   1.440  1.00 39.50           O
ANISOU 3717  O   ILE B 116     5099   3786   6121    784    478   -266       O
ATOM   3718  CB  ILE B 116    -106.250  56.789  -0.763  1.00 43.10           C
ANISOU 3718  CB  ILE B 116     5814   4174   6389    754    303   -487       C
ATOM   3719  CG1 ILE B 116    -105.495  55.471  -0.953  1.00 43.21           C
ANISOU 3719  CG1 ILE B 116     5714   4332   6371    794    412   -392       C
ATOM   3720  CG2 ILE B 116    -105.485  57.719   0.158  1.00 38.80           C
ANISOU 3720  CG2 ILE B 116     5192   3608   5943    578    196   -482       C
ATOM   3721  CD1 ILE B 116    -106.086  54.585  -2.026  1.00 50.07           C
ANISOU 3721  CD1 ILE B 116     6652   5241   7133    974    528   -383       C
ATOM   3722  N   CYS B 117    -107.847  56.897   2.200  1.00 40.98           N
ANISOU 3722  N   CYS B 117     5383   3794   6392    640    304   -368       N
ATOM   3723  CA  CYS B 117    -107.712  56.516   3.599  1.00 38.80           C
ANISOU 3723  CA  CYS B 117     4967   3555   6222    559    321   -273       C
ATOM   3724  C   CYS B 117    -109.003  55.991   4.213  1.00 42.80           C
ANISOU 3724  C   CYS B 117     5462   4020   6782    633    377   -224       C
ATOM   3725  O   CYS B 117    -108.983  55.553   5.368  1.00 44.05           O
ANISOU 3725  O   CYS B 117     5509   4210   7019    580    390   -139       O
ATOM   3726  CB  CYS B 117    -107.220  57.708   4.425  1.00 40.70           C
ANISOU 3726  CB  CYS B 117     5184   3744   6534    409    218   -285       C
ATOM   3727  SG  CYS B 117    -105.720  58.489   3.800  1.00 44.96           S
ANISOU 3727  SG  CYS B 117     5724   4325   7031    316    139   -333       S
ATOM   3728  N   ALA B 118    -110.113  56.024   3.476  1.00 44.72           N
ANISOU 3728  N   ALA B 118     5822   4191   6979    761    408   -274       N
ATOM   3729  CA  ALA B 118    -111.403  55.659   4.059  1.00 45.10           C
ANISOU 3729  CA  ALA B 118     5868   4185   7084    837    456   -231       C
ATOM   3730  C   ALA B 118    -111.467  54.211   4.534  1.00 42.47           C
ANISOU 3730  C   ALA B 118     5389   3962   6786    890    558   -106       C
ATOM   3731  O   ALA B 118    -111.887  53.984   5.682  1.00 42.72           O
ANISOU 3731  O   ALA B 118     5339   3983   6909    849    552    -34       O
ATOM   3732  CB  ALA B 118    -112.524  55.976   3.061  1.00 46.73           C
ANISOU 3732  CB  ALA B 118     6247   4288   7219    984    472   -317       C
ATOM   3733  N   PRO B 119    -111.088  53.198   3.744  1.00 41.99           N
ANISOU 3733  N   PRO B 119     5286   4005   6664    974    645    -66       N
ATOM   3734  CA  PRO B 119    -111.186  51.817   4.242  1.00 42.37           C
ANISOU 3734  CA  PRO B 119     5180   4150   6768   1009    727     69       C
ATOM   3735  C   PRO B 119    -110.142  51.453   5.286  1.00 41.44           C
ANISOU 3735  C   PRO B 119     4924   4102   6720    860    677    143       C
ATOM   3736  O   PRO B 119    -110.173  50.325   5.793  1.00 40.21           O
ANISOU 3736  O   PRO B 119     4639   4016   6622    869    718    257       O
ATOM   3737  CB  PRO B 119    -111.004  50.976   2.971  1.00 42.08           C
ANISOU 3737  CB  PRO B 119     5147   4200   6642   1137    832     92       C
ATOM   3738  CG  PRO B 119    -110.164  51.817   2.100  1.00 41.09           C
ANISOU 3738  CG  PRO B 119     5133   4061   6420   1100    777    -18       C
ATOM   3739  CD  PRO B 119    -110.610  53.229   2.348  1.00 42.22           C
ANISOU 3739  CD  PRO B 119     5403   4066   6571   1045    672   -131       C
ATOM   3740  N   LEU B 120    -109.231  52.357   5.630  1.00 42.13           N
ANISOU 3740  N   LEU B 120     5034   4169   6805    730    586     85       N
ATOM   3741  CA  LEU B 120    -108.157  52.072   6.569  1.00 35.37           C
ANISOU 3741  CA  LEU B 120     4072   3373   5994    604    540    143       C
ATOM   3742  C   LEU B 120    -108.475  52.641   7.946  1.00 34.14           C
ANISOU 3742  C   LEU B 120     3900   3157   5915    519    477    160       C
ATOM   3743  O   LEU B 120    -109.099  53.698   8.075  1.00 37.35           O
ANISOU 3743  O   LEU B 120     4390   3468   6334    509    440    100       O
ATOM   3744  CB  LEU B 120    -106.831  52.648   6.070  1.00 30.20           C
ANISOU 3744  CB  LEU B 120     3443   2748   5282    527    495     83       C
ATOM   3745  CG  LEU B 120    -106.301  52.104   4.743  1.00 29.80           C
ANISOU 3745  CG  LEU B 120     3408   2767   5147    598    550     72       C
ATOM   3746  CD1 LEU B 120    -105.072  52.880   4.311  1.00 27.65           C
ANISOU 3746  CD1 LEU B 120     3174   2508   4824    519    488      6       C
ATOM   3747  CD2 LEU B 120    -105.984  50.622   4.855  1.00 26.71           C
ANISOU 3747  CD2 LEU B 120     2892   2473   4784    620    611    190       C
ATOM   3748  N   THR B 121    -108.033  51.926   8.978  1.00 30.95           N
ANISOU 3748  N   THR B 121     3395   2804   5561    457    460    245       N
ATOM   3749  CA  THR B 121    -108.178  52.383  10.358  1.00 29.37           C
ANISOU 3749  CA  THR B 121     3180   2561   5417    378    402    271       C
ATOM   3750  C   THR B 121    -107.030  53.335  10.663  1.00 28.72           C
ANISOU 3750  C   THR B 121     3122   2480   5312    271    345    224       C
ATOM   3751  O   THR B 121    -105.889  52.912  10.861  1.00 29.48           O
ANISOU 3751  O   THR B 121     3171   2642   5388    219    329    247       O
ATOM   3752  CB  THR B 121    -108.193  51.202  11.321  1.00 26.26           C
ANISOU 3752  CB  THR B 121     2685   2217   5074    365    396    380       C
ATOM   3753  OG1 THR B 121    -109.339  50.385  11.056  1.00 29.45           O
ANISOU 3753  OG1 THR B 121     3053   2621   5515    468    452    437       O
ATOM   3754  CG2 THR B 121    -108.250  51.689  12.759  1.00 24.53           C
ANISOU 3754  CG2 THR B 121     2468   1959   4892    289    335    405       C
ATOM   3755  N   VAL B 122    -107.333  54.626  10.697  1.00 30.43           N
ANISOU 3755  N   VAL B 122     3410   2618   5536    240    312    165       N
ATOM   3756  CA  VAL B 122    -106.330  55.668  10.879  1.00 26.32           C
ANISOU 3756  CA  VAL B 122     2903   2095   5003    148    264    128       C
ATOM   3757  C   VAL B 122    -106.226  56.014  12.357  1.00 29.21           C
ANISOU 3757  C   VAL B 122     3238   2449   5413     79    236    186       C
ATOM   3758  O   VAL B 122    -107.238  56.173  13.048  1.00 33.84           O
ANISOU 3758  O   VAL B 122     3835   2976   6045     91    233    218       O
ATOM   3759  CB  VAL B 122    -106.683  56.911  10.040  1.00 28.02           C
ANISOU 3759  CB  VAL B 122     3206   2230   5212    145    232     44       C
ATOM   3760  CG1 VAL B 122    -105.619  57.980  10.200  1.00 23.81           C
ANISOU 3760  CG1 VAL B 122     2665   1703   4681     47    180     23       C
ATOM   3761  CG2 VAL B 122    -106.849  56.532   8.577  1.00 28.77           C
ANISOU 3761  CG2 VAL B 122     3355   2334   5242    232    261    -16       C
ATOM   3762  N   PHE B 123    -104.996  56.137  12.846  1.00 30.70           N
ANISOU 3762  N   PHE B 123     3393   2692   5579     16    218    201       N
ATOM   3763  CA  PHE B 123    -104.749  56.508  14.232  1.00 27.44           C
ANISOU 3763  CA  PHE B 123     2964   2277   5187    -37    201    255       C
ATOM   3764  C   PHE B 123    -104.649  58.023  14.349  1.00 27.56           C
ANISOU 3764  C   PHE B 123     3000   2242   5228    -94    181    236       C
ATOM   3765  O   PHE B 123    -103.852  58.656  13.650  1.00 25.20           O
ANISOU 3765  O   PHE B 123     2703   1960   4913   -124    167    194       O
ATOM   3766  CB  PHE B 123    -103.470  55.850  14.750  1.00 29.28           C
ANISOU 3766  CB  PHE B 123     3162   2587   5376    -62    195    284       C
ATOM   3767  CG  PHE B 123    -103.071  56.302  16.126  1.00 30.38           C
ANISOU 3767  CG  PHE B 123     3304   2729   5511   -101    184    333       C
ATOM   3768  CD1 PHE B 123    -103.746  55.840  17.243  1.00 29.66           C
ANISOU 3768  CD1 PHE B 123     3216   2619   5433    -89    175    393       C
ATOM   3769  CD2 PHE B 123    -102.019  57.185  16.302  1.00 35.62           C
ANISOU 3769  CD2 PHE B 123     3967   3415   6152   -141    187    326       C
ATOM   3770  CE1 PHE B 123    -103.382  56.253  18.510  1.00 33.65           C
ANISOU 3770  CE1 PHE B 123     3739   3128   5917   -112    170    440       C
ATOM   3771  CE2 PHE B 123    -101.650  57.601  17.567  1.00 36.95           C
ANISOU 3771  CE2 PHE B 123     4143   3591   6306   -158    193    378       C
ATOM   3772  CZ  PHE B 123    -102.332  57.134  18.672  1.00 37.34           C
ANISOU 3772  CZ  PHE B 123     4210   3622   6356   -142    186    433       C
ATOM   3773  N   PHE B 124    -105.458  58.597  15.235  1.00 30.91           N
ANISOU 3773  N   PHE B 124     3436   2606   5701   -110    175    279       N
ATOM   3774  CA  PHE B 124    -105.484  60.032  15.470  1.00 26.06           C
ANISOU 3774  CA  PHE B 124     2830   1939   5134   -171    155    287       C
ATOM   3775  C   PHE B 124    -105.034  60.326  16.893  1.00 29.61           C
ANISOU 3775  C   PHE B 124     3250   2417   5584   -204    173    370       C
ATOM   3776  O   PHE B 124    -105.399  59.610  17.832  1.00 30.94           O
ANISOU 3776  O   PHE B 124     3422   2598   5738   -176    185    420       O
ATOM   3777  CB  PHE B 124    -106.884  60.609  15.235  1.00 25.79           C
ANISOU 3777  CB  PHE B 124     2844   1792   5163   -162    133    274       C
ATOM   3778  CG  PHE B 124    -107.408  60.388  13.844  1.00 25.80           C
ANISOU 3778  CG  PHE B 124     2899   1754   5150   -110    120    188       C
ATOM   3779  CD1 PHE B 124    -107.170  61.316  12.843  1.00 26.83           C
ANISOU 3779  CD1 PHE B 124     3065   1842   5286   -144     74    121       C
ATOM   3780  CD2 PHE B 124    -108.144  59.255  13.538  1.00 29.92           C
ANISOU 3780  CD2 PHE B 124     3437   2282   5650    -22    152    179       C
ATOM   3781  CE1 PHE B 124    -107.654  61.116  11.562  1.00 27.76           C
ANISOU 3781  CE1 PHE B 124     3255   1920   5371    -83     60     37       C
ATOM   3782  CE2 PHE B 124    -108.631  59.050  12.259  1.00 29.14           C
ANISOU 3782  CE2 PHE B 124     3396   2151   5524     45    156    106       C
ATOM   3783  CZ  PHE B 124    -108.386  59.982  11.271  1.00 26.53           C
ANISOU 3783  CZ  PHE B 124     3123   1775   5182     19    109     29       C
ATOM   3784  N   ASP B 125    -104.242  61.383  17.046  1.00 35.21           N
ANISOU 3784  N   ASP B 125     3931   3140   6306   -259    173    390       N
ATOM   3785  CA  ASP B 125    -103.736  61.826  18.342  1.00 36.36           C
ANISOU 3785  CA  ASP B 125     4052   3319   6444   -278    205    475       C
ATOM   3786  C   ASP B 125    -104.483  63.100  18.721  1.00 35.38           C
ANISOU 3786  C   ASP B 125     3918   3117   6406   -327    198    531       C
ATOM   3787  O   ASP B 125    -104.192  64.180  18.200  1.00 38.14           O
ANISOU 3787  O   ASP B 125     4236   3443   6810   -383    177    529       O
ATOM   3788  CB  ASP B 125    -102.227  62.052  18.284  1.00 41.70           C
ANISOU 3788  CB  ASP B 125     4694   4077   7075   -290    224    475       C
ATOM   3789  CG  ASP B 125    -101.627  62.378  19.642  1.00 48.04           C
ANISOU 3789  CG  ASP B 125     5484   4924   7846   -283    273    563       C
ATOM   3790  OD1 ASP B 125    -102.383  62.493  20.630  1.00 49.57           O
ANISOU 3790  OD1 ASP B 125     5696   5085   8052   -276    289    628       O
ATOM   3791  OD2 ASP B 125    -100.388  62.516  19.720  1.00 49.95           O
ANISOU 3791  OD2 ASP B 125     5704   5232   8043   -275    299    571       O
ATOM   3792  N   GLY B 126    -105.440  62.971  19.642  1.00 33.36           N
ANISOU 3792  N   GLY B 126     3686   2818   6169   -311    209    588       N
ATOM   3793  CA  GLY B 126    -106.232  64.107  20.084  1.00 33.85           C
ANISOU 3793  CA  GLY B 126     3742   2800   6320   -357    203    655       C
ATOM   3794  C   GLY B 126    -105.431  65.219  20.729  1.00 40.23           C
ANISOU 3794  C   GLY B 126     4491   3643   7153   -406    239    744       C
ATOM   3795  O   GLY B 126    -105.961  66.324  20.893  1.00 49.40           O
ANISOU 3795  O   GLY B 126     5628   4734   8408   -463    226    806       O
ATOM   3796  N   ARG B 127    -104.178  64.957  21.102  1.00 37.79           N
ANISOU 3796  N   ARG B 127     4157   3437   6766   -381    284    759       N
ATOM   3797  CA  ARG B 127    -103.318  66.000  21.644  1.00 37.12           C
ANISOU 3797  CA  ARG B 127     4007   3398   6699   -410    333    850       C
ATOM   3798  C   ARG B 127    -102.845  66.981  20.580  1.00 39.51           C
ANISOU 3798  C   ARG B 127     4245   3686   7081   -478    294    827       C
ATOM   3799  O   ARG B 127    -102.273  68.019  20.930  1.00 46.50           O
ANISOU 3799  O   ARG B 127     5054   4598   8015   -514    327    919       O
ATOM   3800  CB  ARG B 127    -102.109  65.372  22.338  1.00 34.84           C
ANISOU 3800  CB  ARG B 127     3729   3218   6292   -344    393    864       C
ATOM   3801  CG  ARG B 127    -102.471  64.464  23.498  1.00 36.34           C
ANISOU 3801  CG  ARG B 127     3990   3421   6395   -280    416    894       C
ATOM   3802  CD  ARG B 127    -101.259  63.701  23.999  1.00 37.80           C
ANISOU 3802  CD  ARG B 127     4214   3695   6455   -214    448    880       C
ATOM   3803  NE  ARG B 127    -100.728  62.798  22.982  1.00 36.55           N
ANISOU 3803  NE  ARG B 127     4065   3556   6265   -208    401    771       N
ATOM   3804  CZ  ARG B 127     -99.729  61.946  23.187  1.00 34.39           C
ANISOU 3804  CZ  ARG B 127     3833   3340   5893   -159    403    738       C
ATOM   3805  NH1 ARG B 127     -99.147  61.879  24.376  1.00 31.86           N
ANISOU 3805  NH1 ARG B 127     3562   3060   5482   -103    448    794       N
ATOM   3806  NH2 ARG B 127     -99.312  61.160  22.203  1.00 32.66           N
ANISOU 3806  NH2 ARG B 127     3616   3134   5661   -162    359    652       N
ATOM   3807  N   VAL B 128    -103.065  66.681  19.305  1.00 32.98           N
ANISOU 3807  N   VAL B 128     3445   2819   6266   -492    223    716       N
ATOM   3808  CA  VAL B 128    -102.653  67.542  18.203  1.00 31.81           C
ANISOU 3808  CA  VAL B 128     3252   2650   6183   -556    164    682       C
ATOM   3809  C   VAL B 128    -103.876  68.277  17.678  1.00 37.31           C
ANISOU 3809  C   VAL B 128     3976   3214   6987   -618     84    668       C
ATOM   3810  O   VAL B 128    -104.963  67.695  17.566  1.00 38.84           O
ANISOU 3810  O   VAL B 128     4247   3338   7172   -586     63    619       O
ATOM   3811  CB  VAL B 128    -101.971  66.725  17.089  1.00 29.92           C
ANISOU 3811  CB  VAL B 128     3041   2458   5868   -522    137    566       C
ATOM   3812  CG1 VAL B 128    -101.406  67.643  16.018  1.00 29.72           C
ANISOU 3812  CG1 VAL B 128     2971   2422   5899   -584     71    539       C
ATOM   3813  CG2 VAL B 128    -100.884  65.838  17.671  1.00 28.04           C
ANISOU 3813  CG2 VAL B 128     2799   2332   5524   -456    207    575       C
ATOM   3814  N   ASP B 129    -103.701  69.560  17.360  1.00 41.96           N
ANISOU 3814  N   ASP B 129     4500   3761   7681   -706     33    717       N
ATOM   3815  CA  ASP B 129    -104.812  70.392  16.914  1.00 45.29           C
ANISOU 3815  CA  ASP B 129     4963   4078   8168   -756    -62    698       C
ATOM   3816  C   ASP B 129    -105.456  69.820  15.658  1.00 43.10           C
ANISOU 3816  C   ASP B 129     4791   3711   7872   -736   -141    554       C
ATOM   3817  O   ASP B 129    -104.769  69.467  14.695  1.00 41.28           O
ANISOU 3817  O   ASP B 129     4570   3505   7609   -727   -168    472       O
ATOM   3818  CB  ASP B 129    -104.329  71.819  16.650  1.00 57.08           C
ANISOU 3818  CB  ASP B 129     6373   5582   9732   -838   -121    757       C
ATOM   3819  CG  ASP B 129    -104.018  72.577  17.926  1.00 65.75           C
ANISOU 3819  CG  ASP B 129     7373   6745  10865   -852    -44    916       C
ATOM   3820  OD1 ASP B 129    -104.212  72.008  19.020  1.00 68.25           O
ANISOU 3820  OD1 ASP B 129     7699   7090  11143   -799     52    974       O
ATOM   3821  OD2 ASP B 129    -103.580  73.744  17.833  1.00 68.31           O
ANISOU 3821  OD2 ASP B 129     7610   7090  11254   -912    -79    988       O
ATOM   3822  N   GLY B 130    -106.784  69.728  15.676  1.00 42.00           N
ANISOU 3822  N   GLY B 130     4738   3473   7747   -718   -172    526       N
ATOM   3823  CA  GLY B 130    -107.545  69.316  14.516  1.00 41.15           C
ANISOU 3823  CA  GLY B 130     4745   3267   7624   -684   -242    397       C
ATOM   3824  C   GLY B 130    -107.670  67.824  14.306  1.00 36.08           C
ANISOU 3824  C   GLY B 130     4158   2661   6891   -577   -179    325       C
ATOM   3825  O   GLY B 130    -108.373  67.408  13.377  1.00 38.75           O
ANISOU 3825  O   GLY B 130     4595   2932   7194   -522   -217    224       O
ATOM   3826  N   GLN B 131    -107.023  67.002  15.134  1.00 35.14           N
ANISOU 3826  N   GLN B 131     3983   2664   6705   -533    -85    374       N
ATOM   3827  CA  GLN B 131    -107.075  65.559  14.926  1.00 36.22           C
ANISOU 3827  CA  GLN B 131     4159   2863   6740   -434    -35    315       C
ATOM   3828  C   GLN B 131    -108.393  64.954  15.391  1.00 36.40           C
ANISOU 3828  C   GLN B 131     4237   2821   6771   -374    -14    325       C
ATOM   3829  O   GLN B 131    -108.836  63.946  14.829  1.00 37.30           O
ANISOU 3829  O   GLN B 131     4400   2941   6830   -291      2    262       O
ATOM   3830  CB  GLN B 131    -105.905  64.884  15.641  1.00 35.76           C
ANISOU 3830  CB  GLN B 131     4033   2943   6611   -413     37    361       C
ATOM   3831  CG  GLN B 131    -104.541  65.317  15.132  1.00 40.10           C
ANISOU 3831  CG  GLN B 131     4528   3565   7141   -452     27    348       C
ATOM   3832  CD  GLN B 131    -103.937  64.339  14.142  1.00 44.75           C
ANISOU 3832  CD  GLN B 131     5142   4218   7641   -397     30    260       C
ATOM   3833  OE1 GLN B 131    -103.573  63.218  14.502  1.00 46.03           O
ANISOU 3833  OE1 GLN B 131     5300   4455   7735   -343     81    264       O
ATOM   3834  NE2 GLN B 131    -103.823  64.761  12.889  1.00 43.95           N
ANISOU 3834  NE2 GLN B 131     5071   4085   7543   -414    -32    184       N
ATOM   3835  N   VAL B 132    -109.027  65.540  16.409  1.00 36.21           N
ANISOU 3835  N   VAL B 132     4201   2740   6818   -409    -10    414       N
ATOM   3836  CA  VAL B 132    -110.325  65.041  16.856  1.00 34.78           C
ANISOU 3836  CA  VAL B 132     4073   2489   6653   -351      2    430       C
ATOM   3837  C   VAL B 132    -111.369  65.229  15.764  1.00 37.14           C
ANISOU 3837  C   VAL B 132     4469   2660   6981   -321    -58    340       C
ATOM   3838  O   VAL B 132    -112.181  64.334  15.497  1.00 38.74           O
ANISOU 3838  O   VAL B 132     4726   2842   7151   -227    -36    300       O
ATOM   3839  CB  VAL B 132    -110.744  65.731  18.168  1.00 38.32           C
ANISOU 3839  CB  VAL B 132     4490   2899   7170   -399     18    553       C
ATOM   3840  CG1 VAL B 132    -112.166  65.346  18.542  1.00 29.28           C
ANISOU 3840  CG1 VAL B 132     3406   1666   6053   -342     17    569       C
ATOM   3841  CG2 VAL B 132    -109.781  65.370  19.287  1.00 36.20           C
ANISOU 3841  CG2 VAL B 132     4152   2759   6844   -396     87    635       C
ATOM   3842  N   ASP B 133    -111.360  66.394  15.110  1.00 38.86           N
ANISOU 3842  N   ASP B 133     4714   2788   7262   -396   -139    309       N
ATOM   3843  CA  ASP B 133    -112.297  66.639  14.018  1.00 42.72           C
ANISOU 3843  CA  ASP B 133     5322   3142   7766   -364   -212    210       C
ATOM   3844  C   ASP B 133    -112.057  65.682  12.859  1.00 41.19           C
ANISOU 3844  C   ASP B 133     5182   3006   7464   -268   -192     98       C
ATOM   3845  O   ASP B 133    -113.009  65.166  12.261  1.00 45.80           O
ANISOU 3845  O   ASP B 133     5863   3523   8016   -169   -188     33       O
ATOM   3846  CB  ASP B 133    -112.189  68.088  13.544  1.00 53.17           C
ANISOU 3846  CB  ASP B 133     6664   4408   9129   -468   -318    196       C
ATOM   3847  CG  ASP B 133    -112.994  69.041  14.399  1.00 68.20           C
ANISOU 3847  CG  ASP B 133     8565   6255  11093   -527   -347    282       C
ATOM   3848  OD1 ASP B 133    -112.476  69.490  15.442  1.00 74.17           O
ANISOU 3848  OD1 ASP B 133     9214   7088  11880   -589   -309    397       O
ATOM   3849  OD2 ASP B 133    -114.151  69.335  14.029  1.00 75.02           O
ANISOU 3849  OD2 ASP B 133     9539   6996  11970   -504   -404    237       O
ATOM   3850  N   LEU B 134    -110.787  65.440  12.522  1.00 35.82           N
ANISOU 3850  N   LEU B 134     4439   2448   6724   -287   -173     83       N
ATOM   3851  CA  LEU B 134    -110.470  64.469  11.482  1.00 33.69           C
ANISOU 3851  CA  LEU B 134     4207   2246   6349   -196   -142     -4       C
ATOM   3852  C   LEU B 134    -110.968  63.079  11.851  1.00 33.51           C
ANISOU 3852  C   LEU B 134     4172   2283   6278    -87    -51     19       C
ATOM   3853  O   LEU B 134    -111.390  62.316  10.974  1.00 35.23           O
ANISOU 3853  O   LEU B 134     4451   2501   6433     16    -23    -44       O
ATOM   3854  CB  LEU B 134    -108.962  64.446  11.230  1.00 32.67           C
ANISOU 3854  CB  LEU B 134     4000   2239   6173   -242   -136     -5       C
ATOM   3855  CG  LEU B 134    -108.346  65.722  10.649  1.00 34.96           C
ANISOU 3855  CG  LEU B 134     4290   2487   6505   -341   -232    -30       C
ATOM   3856  CD1 LEU B 134    -106.834  65.700  10.792  1.00 35.83           C
ANISOU 3856  CD1 LEU B 134     4296   2731   6587   -386   -206      5       C
ATOM   3857  CD2 LEU B 134    -108.742  65.889   9.193  1.00 35.94           C
ANISOU 3857  CD2 LEU B 134     4541   2531   6583   -298   -307   -151       C
ATOM   3858  N   PHE B 135    -110.933  62.738  13.141  1.00 30.67           N
ANISOU 3858  N   PHE B 135     3734   1973   5946   -106     -4    117       N
ATOM   3859  CA  PHE B 135    -111.475  61.460  13.585  1.00 30.48           C
ANISOU 3859  CA  PHE B 135     3692   1996   5894    -14     63    153       C
ATOM   3860  C   PHE B 135    -112.983  61.403  13.381  1.00 38.73           C
ANISOU 3860  C   PHE B 135     4820   2923   6972     65     60    134       C
ATOM   3861  O   PHE B 135    -113.524  60.362  12.990  1.00 44.16           O
ANISOU 3861  O   PHE B 135     5522   3634   7623    174    110    121       O
ATOM   3862  CB  PHE B 135    -111.114  61.225  15.051  1.00 31.78           C
ANISOU 3862  CB  PHE B 135     3773   2226   6076    -56     92    259       C
ATOM   3863  CG  PHE B 135    -111.745  59.997  15.645  1.00 33.81           C
ANISOU 3863  CG  PHE B 135     4008   2518   6321     22    137    309       C
ATOM   3864  CD1 PHE B 135    -111.276  58.735  15.324  1.00 26.14           C
ANISOU 3864  CD1 PHE B 135     2994   1645   5290     77    174    303       C
ATOM   3865  CD2 PHE B 135    -112.799  60.106  16.538  1.00 41.89           C
ANISOU 3865  CD2 PHE B 135     5044   3472   7399     36    136    373       C
ATOM   3866  CE1 PHE B 135    -111.851  57.604  15.875  1.00 26.19           C
ANISOU 3866  CE1 PHE B 135     2966   1683   5301    140    202    363       C
ATOM   3867  CE2 PHE B 135    -113.378  58.978  17.093  1.00 46.80           C
ANISOU 3867  CE2 PHE B 135     5639   4128   8017    107    166    427       C
ATOM   3868  CZ  PHE B 135    -112.902  57.726  16.762  1.00 26.72           C
ANISOU 3868  CZ  PHE B 135     3046   1685   5422    156    195    424       C
ATOM   3869  N   ARG B 136    -113.678  62.515  13.635  1.00 34.65           N
ANISOU 3869  N   ARG B 136     4357   2277   6532     14      2    141       N
ATOM   3870  CA  ARG B 136    -115.119  62.553  13.414  1.00 33.81           C
ANISOU 3870  CA  ARG B 136     4347   2039   6458     92     -9    117       C
ATOM   3871  C   ARG B 136    -115.465  62.381  11.941  1.00 32.58           C
ANISOU 3871  C   ARG B 136     4303   1835   6242    186    -20     -1       C
ATOM   3872  O   ARG B 136    -116.515  61.818  11.612  1.00 33.06           O
ANISOU 3872  O   ARG B 136     4432   1842   6288    309     15    -23       O
ATOM   3873  CB  ARG B 136    -115.701  63.865  13.940  1.00 35.49           C
ANISOU 3873  CB  ARG B 136     4600   2112   6773      4    -82    151       C
ATOM   3874  CG  ARG B 136    -115.566  64.070  15.441  1.00 32.63           C
ANISOU 3874  CG  ARG B 136     4145   1786   6468    -68    -60    279       C
ATOM   3875  CD  ARG B 136    -116.250  65.360  15.870  1.00 35.20           C
ANISOU 3875  CD  ARG B 136     4510   2014   6849   -147   -126    316       C
ATOM   3876  NE  ARG B 136    -116.217  65.558  17.316  1.00 38.01           N
ANISOU 3876  NE  ARG B 136     4787   2424   7229   -197    -94    443       N
ATOM   3877  CZ  ARG B 136    -117.128  65.077  18.155  1.00 38.34           C
ANISOU 3877  CZ  ARG B 136     4837   2452   7279   -141    -61    506       C
ATOM   3878  NH1 ARG B 136    -118.144  64.362  17.693  1.00 37.19           N
ANISOU 3878  NH1 ARG B 136     4763   2244   7126    -31    -52    459       N
ATOM   3879  NH2 ARG B 136    -117.025  65.307  19.457  1.00 36.12           N
ANISOU 3879  NH2 ARG B 136     4494   2220   7010   -186    -35    620       N
ATOM   3880  N   ASN B 137    -114.600  62.852  11.045  1.00 34.34           N
ANISOU 3880  N   ASN B 137     4549   2078   6422    141    -65    -73       N
ATOM   3881  CA  ASN B 137    -114.843  62.769   9.612  1.00 41.40           C
ANISOU 3881  CA  ASN B 137     5566   2925   7239    230    -82   -189       C
ATOM   3882  C   ASN B 137    -114.295  61.497   8.982  1.00 43.97           C
ANISOU 3882  C   ASN B 137     5851   3393   7462    329      9   -204       C
ATOM   3883  O   ASN B 137    -114.630  61.203   7.830  1.00 47.70           O
ANISOU 3883  O   ASN B 137     6427   3842   7856    438     24   -286       O
ATOM   3884  CB  ASN B 137    -114.235  63.985   8.905  1.00 49.09           C
ANISOU 3884  CB  ASN B 137     6596   3836   8220    129   -197   -259       C
ATOM   3885  CG  ASN B 137    -114.872  65.288   9.340  1.00 63.29           C
ANISOU 3885  CG  ASN B 137     8444   5471  10130     32   -302   -244       C
ATOM   3886  OD1 ASN B 137    -116.090  65.376   9.495  1.00 66.46           O
ANISOU 3886  OD1 ASN B 137     8933   5748  10569     88   -312   -249       O
ATOM   3887  ND2 ASN B 137    -114.048  66.309   9.548  1.00 69.18           N
ANISOU 3887  ND2 ASN B 137     9130   6218  10938   -114   -380   -214       N
ATOM   3888  N   ALA B 138    -113.469  60.742   9.698  1.00 42.99           N
ANISOU 3888  N   ALA B 138     5589   3411   7335    295     68   -124       N
ATOM   3889  CA  ALA B 138    -112.898  59.520   9.154  1.00 42.86           C
ANISOU 3889  CA  ALA B 138     5522   3526   7237    372    146   -122       C
ATOM   3890  C   ALA B 138    -113.898  58.374   9.238  1.00 44.27           C
ANISOU 3890  C   ALA B 138     5690   3719   7412    508    232    -78       C
ATOM   3891  O   ALA B 138    -114.698  58.283  10.173  1.00 43.97           O
ANISOU 3891  O   ALA B 138     5628   3638   7442    514    240    -14       O
ATOM   3892  CB  ALA B 138    -111.615  59.148   9.897  1.00 43.52           C
ANISOU 3892  CB  ALA B 138     5471   3740   7323    282    161    -54       C
ATOM   3893  N   ARG B 139    -113.845  57.490   8.241  1.00 41.00           N
ANISOU 3893  N   ARG B 139     5289   3369   6919    620    300   -103       N
ATOM   3894  CA  ARG B 139    -114.736  56.336   8.220  1.00 37.49           C
ANISOU 3894  CA  ARG B 139     4815   2954   6475    759    394    -46       C
ATOM   3895  C   ARG B 139    -114.294  55.278   9.224  1.00 34.73           C
ANISOU 3895  C   ARG B 139     4301   2722   6170    721    431     74       C
ATOM   3896  O   ARG B 139    -115.097  54.804  10.035  1.00 32.48           O
ANISOU 3896  O   ARG B 139     3968   2424   5948    756    452    151       O
ATOM   3897  CB  ARG B 139    -114.800  55.752   6.808  1.00 44.13           C
ANISOU 3897  CB  ARG B 139     5720   3832   7216    899    465    -97       C
ATOM   3898  CG  ARG B 139    -115.748  54.578   6.670  1.00 51.84           C
ANISOU 3898  CG  ARG B 139     6659   4844   8195   1061    576    -27       C
ATOM   3899  CD  ARG B 139    -116.129  54.340   5.220  1.00 59.93           C
ANISOU 3899  CD  ARG B 139     7799   5860   9111   1227    648    -94       C
ATOM   3900  NE  ARG B 139    -117.199  53.355   5.099  1.00 67.52           N
ANISOU 3900  NE  ARG B 139     8734   6841  10082   1400    762    -22       N
ATOM   3901  CZ  ARG B 139    -118.488  53.629   5.273  1.00 69.63           C
ANISOU 3901  CZ  ARG B 139     9086   6991  10379   1497    770    -36       C
ATOM   3902  NH1 ARG B 139    -118.872  54.861   5.578  1.00 68.66           N
ANISOU 3902  NH1 ARG B 139     9085   6719  10284   1426    664   -118       N
ATOM   3903  NH2 ARG B 139    -119.394  52.670   5.144  1.00 72.34           N
ANISOU 3903  NH2 ARG B 139     9388   7365  10732   1664    885     43       N
ATOM   3904  N   ASN B 140    -113.023  54.893   9.181  1.00 33.22           N
ANISOU 3904  N   ASN B 140     4032   2641   5949    652    430     91       N
ATOM   3905  CA  ASN B 140    -112.435  53.977  10.146  1.00 32.38           C
ANISOU 3905  CA  ASN B 140     3788   2633   5880    596    438    194       C
ATOM   3906  C   ASN B 140    -111.284  54.682  10.844  1.00 33.47           C
ANISOU 3906  C   ASN B 140     3904   2792   6023    451    369    185       C
ATOM   3907  O   ASN B 140    -110.465  55.339  10.195  1.00 34.19           O
ANISOU 3907  O   ASN B 140     4034   2887   6068    405    342    116       O
ATOM   3908  CB  ASN B 140    -111.931  52.699   9.469  1.00 27.51           C
ANISOU 3908  CB  ASN B 140     3095   2133   5226    657    505    238       C
ATOM   3909  CG  ASN B 140    -113.009  51.993   8.678  1.00 37.46           C
ANISOU 3909  CG  ASN B 140     4370   3388   6474    819    594    258       C
ATOM   3910  OD1 ASN B 140    -113.742  51.162   9.213  1.00 39.88           O
ANISOU 3910  OD1 ASN B 140     4599   3713   6840    875    629    351       O
ATOM   3911  ND2 ASN B 140    -113.113  52.321   7.395  1.00 36.18           N
ANISOU 3911  ND2 ASN B 140     4312   3204   6232    904    630    174       N
ATOM   3912  N   GLY B 141    -111.223  54.556  12.164  1.00 26.11           N
ANISOU 3912  N   GLY B 141     2910   1870   5140    387    341    258       N
ATOM   3913  CA  GLY B 141    -110.177  55.253  12.888  1.00 26.09           C
ANISOU 3913  CA  GLY B 141     2893   1885   5136    268    290    258       C
ATOM   3914  C   GLY B 141    -110.125  54.862  14.346  1.00 27.20           C
ANISOU 3914  C   GLY B 141     2975   2051   5311    223    268    346       C
ATOM   3915  O   GLY B 141    -111.030  54.211  14.879  1.00 30.08           O
ANISOU 3915  O   GLY B 141     3313   2401   5714    272    278    408       O
ATOM   3916  N   VAL B 142    -109.031  55.274  14.984  1.00 24.23           N
ANISOU 3916  N   VAL B 142     2582   1710   4913    137    238    353       N
ATOM   3917  CA  VAL B 142    -108.816  55.115  16.417  1.00 27.18           C
ANISOU 3917  CA  VAL B 142     2928   2102   5296     92    211    426       C
ATOM   3918  C   VAL B 142    -108.282  56.434  16.954  1.00 27.77           C
ANISOU 3918  C   VAL B 142     3033   2151   5369     18    194    416       C
ATOM   3919  O   VAL B 142    -107.351  57.010  16.379  1.00 35.24           O
ANISOU 3919  O   VAL B 142     3982   3120   6287    -20    192    368       O
ATOM   3920  CB  VAL B 142    -107.840  53.965  16.732  1.00 29.26           C
ANISOU 3920  CB  VAL B 142     3138   2457   5523     79    197    462       C
ATOM   3921  CG1 VAL B 142    -107.424  54.001  18.195  1.00 24.80           C
ANISOU 3921  CG1 VAL B 142     2578   1904   4943     32    160    519       C
ATOM   3922  CG2 VAL B 142    -108.473  52.626  16.391  1.00 33.03           C
ANISOU 3922  CG2 VAL B 142     3564   2960   6027    145    210    506       C
ATOM   3923  N   LEU B 143    -108.870  56.915  18.045  1.00 26.86           N
ANISOU 3923  N   LEU B 143     2930   1989   5285      0    183    472       N
ATOM   3924  CA  LEU B 143    -108.513  58.202  18.624  1.00 24.27           C
ANISOU 3924  CA  LEU B 143     2619   1634   4968    -65    178    488       C
ATOM   3925  C   LEU B 143    -108.077  58.022  20.070  1.00 30.76           C
ANISOU 3925  C   LEU B 143     3433   2498   5756    -82    176    566       C
ATOM   3926  O   LEU B 143    -108.689  57.260  20.823  1.00 29.02           O
ANISOU 3926  O   LEU B 143     3214   2276   5536    -49    163    618       O
ATOM   3927  CB  LEU B 143    -109.690  59.183  18.555  1.00 28.93           C
ANISOU 3927  CB  LEU B 143     3248   2114   5631    -70    169    491       C
ATOM   3928  CG  LEU B 143    -109.499  60.543  19.230  1.00 30.73           C
ANISOU 3928  CG  LEU B 143     3477   2304   5895   -142    164    536       C
ATOM   3929  CD1 LEU B 143    -108.402  61.340  18.544  1.00 28.90           C
ANISOU 3929  CD1 LEU B 143     3226   2101   5654   -198    158    492       C
ATOM   3930  CD2 LEU B 143    -110.802  61.328  19.250  1.00 31.50           C
ANISOU 3930  CD2 LEU B 143     3616   2278   6074   -147    144    552       C
ATOM   3931  N   ILE B 144    -107.013  58.725  20.449  1.00 33.92           N
ANISOU 3931  N   ILE B 144     3828   2937   6125   -127    188    576       N
ATOM   3932  CA  ILE B 144    -106.581  58.813  21.837  1.00 29.56           C
ANISOU 3932  CA  ILE B 144     3288   2417   5527   -133    198    650       C
ATOM   3933  C   ILE B 144    -106.624  60.274  22.258  1.00 29.71           C
ANISOU 3933  C   ILE B 144     3304   2400   5585   -176    226    697       C
ATOM   3934  O   ILE B 144    -106.256  61.166  21.485  1.00 30.45           O
ANISOU 3934  O   ILE B 144     3372   2481   5716   -217    232    665       O
ATOM   3935  CB  ILE B 144    -105.172  58.220  22.056  1.00 29.94           C
ANISOU 3935  CB  ILE B 144     3338   2550   5488   -129    197    636       C
ATOM   3936  CG1 ILE B 144    -104.118  59.004  21.271  1.00 31.11           C
ANISOU 3936  CG1 ILE B 144     3460   2728   5632   -161    220    592       C
ATOM   3937  CG2 ILE B 144    -105.147  56.753  21.665  1.00 29.88           C
ANISOU 3937  CG2 ILE B 144     3323   2570   5458    -99    159    607       C
ATOM   3938  CD1 ILE B 144    -102.708  58.801  21.779  1.00 27.75           C
ANISOU 3938  CD1 ILE B 144     3046   2375   5122   -152    233    598       C
ATOM   3939  N   THR B 145    -107.105  60.518  23.474  1.00 26.33           N
ANISOU 3939  N   THR B 145     2897   1954   5153   -168    239    782       N
ATOM   3940  CA  THR B 145    -107.136  61.855  24.044  1.00 27.79           C
ANISOU 3940  CA  THR B 145     3070   2113   5377   -207    276    856       C
ATOM   3941  C   THR B 145    -106.731  61.774  25.507  1.00 30.68           C
ANISOU 3941  C   THR B 145     3467   2529   5661   -175    310    944       C
ATOM   3942  O   THR B 145    -106.785  60.712  26.131  1.00 33.03           O
ANISOU 3942  O   THR B 145     3810   2854   5888   -128    286    947       O
ATOM   3943  CB  THR B 145    -108.523  62.510  23.933  1.00 29.24           C
ANISOU 3943  CB  THR B 145     3259   2187   5663   -229    259    885       C
ATOM   3944  OG1 THR B 145    -109.491  61.706  24.617  1.00 36.63           O
ANISOU 3944  OG1 THR B 145     4232   3097   6587   -180    242    919       O
ATOM   3945  CG2 THR B 145    -108.938  62.676  22.477  1.00 28.63           C
ANISOU 3945  CG2 THR B 145     3176   2048   5653   -249    221    792       C
ATOM   3946  N   GLU B 146    -106.322  62.917  26.051  1.00 30.96           N
ANISOU 3946  N   GLU B 146     3480   2577   5707   -198    366   1021       N
ATOM   3947  CA  GLU B 146    -106.023  63.007  27.473  1.00 33.81           C
ANISOU 3947  CA  GLU B 146     3880   2982   5984   -155    414   1117       C
ATOM   3948  C   GLU B 146    -107.259  63.316  28.303  1.00 42.07           C
ANISOU 3948  C   GLU B 146     4950   3964   7070   -152    417   1208       C
ATOM   3949  O   GLU B 146    -107.337  62.900  29.464  1.00 48.36           O
ANISOU 3949  O   GLU B 146     5809   4787   7778    -98    428   1269       O
ATOM   3950  CB  GLU B 146    -104.958  64.076  27.722  1.00 35.65           C
ANISOU 3950  CB  GLU B 146     4070   3272   6204   -164    492   1178       C
ATOM   3951  CG  GLU B 146    -103.709  63.907  26.878  1.00 39.67           C
ANISOU 3951  CG  GLU B 146     4550   3840   6682   -167    492   1097       C
ATOM   3952  CD  GLU B 146    -102.627  64.904  27.236  1.00 49.82           C
ANISOU 3952  CD  GLU B 146     5789   5191   7950   -158    576   1171       C
ATOM   3953  OE1 GLU B 146    -101.559  64.477  27.721  1.00 51.93           O
ANISOU 3953  OE1 GLU B 146     6100   5531   8100    -92    612   1164       O
ATOM   3954  OE2 GLU B 146    -102.851  66.118  27.042  1.00 55.82           O
ANISOU 3954  OE2 GLU B 146     6468   5924   8816   -216    605   1242       O
ATOM   3955  N   GLY B 147    -108.224  64.032  27.731  1.00 42.68           N
ANISOU 3955  N   GLY B 147     4990   3952   7274   -206    400   1219       N
ATOM   3956  CA  GLY B 147    -109.443  64.367  28.436  1.00 41.51           C
ANISOU 3956  CA  GLY B 147     4865   3730   7178   -207    398   1306       C
ATOM   3957  C   GLY B 147    -110.688  63.919  27.701  1.00 40.14           C
ANISOU 3957  C   GLY B 147     4706   3461   7086   -211    331   1245       C
ATOM   3958  O   GLY B 147    -110.626  63.041  26.835  1.00 36.75           O
ANISOU 3958  O   GLY B 147     4280   3041   6644   -192    290   1140       O
ATOM   3959  N   SER B 148    -111.824  64.523  28.033  1.00 43.60           N
ANISOU 3959  N   SER B 148     5153   3805   7608   -229    325   1317       N
ATOM   3960  CA  SER B 148    -113.097  64.123  27.454  1.00 38.04           C
ANISOU 3960  CA  SER B 148     4476   3001   6977   -214    268   1270       C
ATOM   3961  C   SER B 148    -113.332  64.816  26.120  1.00 37.05           C
ANISOU 3961  C   SER B 148     4332   2812   6935   -266    232   1180       C
ATOM   3962  O   SER B 148    -112.952  65.974  25.927  1.00 41.89           O
ANISOU 3962  O   SER B 148     4909   3423   7585   -333    240   1200       O
ATOM   3963  CB  SER B 148    -114.243  64.451  28.411  1.00 38.07           C
ANISOU 3963  CB  SER B 148     4512   2949   7003   -200    268   1367       C
ATOM   3964  OG  SER B 148    -114.366  65.851  28.596  1.00 41.35           O
ANISOU 3964  OG  SER B 148     4900   3341   7468   -263    288   1428       O
ATOM   3965  N   VAL B 149    -113.958  64.094  25.196  1.00 35.89           N
ANISOU 3965  N   VAL B 149     4212   2618   6806   -228    190   1084       N
ATOM   3966  CA  VAL B 149    -114.463  64.654  23.949  1.00 35.75           C
ANISOU 3966  CA  VAL B 149     4213   2523   6848   -253    145    992       C
ATOM   3967  C   VAL B 149    -115.980  64.686  24.047  1.00 41.12           C
ANISOU 3967  C   VAL B 149     4949   3107   7567   -217    115   1000       C
ATOM   3968  O   VAL B 149    -116.601  63.685  24.427  1.00 47.46           O
ANISOU 3968  O   VAL B 149     5772   3911   8352   -143    121   1016       O
ATOM   3969  CB  VAL B 149    -114.004  63.836  22.731  1.00 32.78           C
ANISOU 3969  CB  VAL B 149     3839   2162   6456   -221    133    877       C
ATOM   3970  CG1 VAL B 149    -114.400  64.539  21.444  1.00 34.91           C
ANISOU 3970  CG1 VAL B 149     4146   2348   6772   -246     83    783       C
ATOM   3971  CG2 VAL B 149    -112.505  63.609  22.784  1.00 33.30           C
ANISOU 3971  CG2 VAL B 149     3854   2346   6452   -242    164    869       C
ATOM   3972  N   LYS B 150    -116.574  65.831  23.717  1.00 37.37           N
ANISOU 3972  N   LYS B 150     4499   2548   7151   -269     77    995       N
ATOM   3973  CA  LYS B 150    -118.009  66.006  23.907  1.00 40.36           C
ANISOU 3973  CA  LYS B 150     4939   2826   7569   -240     48   1012       C
ATOM   3974  C   LYS B 150    -118.793  65.016  23.054  1.00 41.00           C
ANISOU 3974  C   LYS B 150     5077   2856   7646   -145     32    921       C
ATOM   3975  O   LYS B 150    -118.615  64.949  21.833  1.00 35.68           O
ANISOU 3975  O   LYS B 150     4431   2152   6974   -134      9    815       O
ATOM   3976  CB  LYS B 150    -118.420  67.443  23.582  1.00 39.38           C
ANISOU 3976  CB  LYS B 150     4839   2611   7512   -322     -3   1015       C
ATOM   3977  CG  LYS B 150    -117.845  68.011  22.294  1.00 34.70           C
ANISOU 3977  CG  LYS B 150     4253   1993   6938   -374    -52    916       C
ATOM   3978  CD  LYS B 150    -118.510  69.336  21.949  1.00 36.20           C
ANISOU 3978  CD  LYS B 150     4486   2068   7200   -447   -127    916       C
ATOM   3979  CE  LYS B 150    -117.640  70.183  21.033  1.00 57.91           C
ANISOU 3979  CE  LYS B 150     7209   4822   9972   -531   -179    865       C
ATOM   3980  NZ  LYS B 150    -117.309  69.495  19.756  1.00 55.68           N
ANISOU 3980  NZ  LYS B 150     6974   4535   9648   -483   -201    728       N
ATOM   3981  N   GLY B 151    -119.652  64.233  23.709  1.00 43.91           N
ANISOU 3981  N   GLY B 151     5461   3216   8006    -69     47    969       N
ATOM   3982  CA  GLY B 151    -120.520  63.294  23.039  1.00 39.74           C
ANISOU 3982  CA  GLY B 151     4974   2643   7480     36     44    908       C
ATOM   3983  C   GLY B 151    -119.952  61.902  22.851  1.00 38.00           C
ANISOU 3983  C   GLY B 151     4703   2516   7220    103     77    890       C
ATOM   3984  O   GLY B 151    -120.717  60.973  22.570  1.00 39.82           O
ANISOU 3984  O   GLY B 151     4943   2731   7455    202     86    877       O
ATOM   3985  N   LEU B 152    -118.642  61.726  23.001  1.00 33.51           N
ANISOU 3985  N   LEU B 152     4076   2042   6614     55     94    896       N
ATOM   3986  CA  LEU B 152    -117.987  60.448  22.748  1.00 32.77           C
ANISOU 3986  CA  LEU B 152     3933   2030   6487    105    116    877       C
ATOM   3987  C   LEU B 152    -117.780  59.706  24.062  1.00 35.08           C
ANISOU 3987  C   LEU B 152     4186   2398   6743    116    119    978       C
ATOM   3988  O   LEU B 152    -117.136  60.228  24.980  1.00 37.74           O
ANISOU 3988  O   LEU B 152     4517   2774   7050     56    124   1039       O
ATOM   3989  CB  LEU B 152    -116.651  60.655  22.035  1.00 29.83           C
ANISOU 3989  CB  LEU B 152     3534   1723   6076     50    124    808       C
ATOM   3990  CG  LEU B 152    -116.715  61.330  20.663  1.00 35.37           C
ANISOU 3990  CG  LEU B 152     4281   2349   6809     38    106    703       C
ATOM   3991  CD1 LEU B 152    -115.349  61.328  19.994  1.00 31.36           C
ANISOU 3991  CD1 LEU B 152     3739   1936   6242     -5    113    639       C
ATOM   3992  CD2 LEU B 152    -117.743  60.646  19.783  1.00 30.63           C
ANISOU 3992  CD2 LEU B 152     3727   1692   6221    148    112    645       C
ATOM   3993  N   GLN B 153    -118.315  58.493  24.145  1.00 33.06           N
ANISOU 3993  N   GLN B 153     3908   2174   6480    197    113    997       N
ATOM   3994  CA  GLN B 153    -118.167  57.680  25.348  1.00 34.35           C
ANISOU 3994  CA  GLN B 153     4041   2413   6597    208     91   1084       C
ATOM   3995  C   GLN B 153    -116.750  57.127  25.424  1.00 35.40           C
ANISOU 3995  C   GLN B 153     4139   2668   6642    170     86   1058       C
ATOM   3996  O   GLN B 153    -116.346  56.359  24.541  1.00 34.96           O
ANISOU 3996  O   GLN B 153     4045   2664   6574    193     90    997       O
ATOM   3997  CB  GLN B 153    -119.186  56.548  25.352  1.00 38.50           C
ANISOU 3997  CB  GLN B 153     4539   2932   7158    301     74   1121       C
ATOM   3998  CG  GLN B 153    -120.622  57.027  25.228  1.00 41.39           C
ANISOU 3998  CG  GLN B 153     4948   3188   7589    353     81   1133       C
ATOM   3999  CD  GLN B 153    -120.949  58.133  26.212  1.00 40.93           C
ANISOU 3999  CD  GLN B 153     4943   3084   7523    297     71   1189       C
ATOM   4000  OE1 GLN B 153    -121.229  59.266  25.820  1.00 40.79           O
ANISOU 4000  OE1 GLN B 153     4974   2993   7530    260     80   1149       O
ATOM   4001  NE2 GLN B 153    -120.913  57.809  27.499  1.00 43.96           N
ANISOU 4001  NE2 GLN B 153     5320   3512   7872    292     46   1286       N
ATOM   4002  N   PRO B 154    -115.974  57.474  26.444  1.00 32.12           N
ANISOU 4002  N   PRO B 154     3740   2300   6163    122     81   1106       N
ATOM   4003  CA  PRO B 154    -114.553  57.118  26.450  1.00 33.55           C
ANISOU 4003  CA  PRO B 154     3906   2581   6259     88     79   1070       C
ATOM   4004  C   PRO B 154    -114.304  55.696  26.927  1.00 37.92           C
ANISOU 4004  C   PRO B 154     4440   3207   6762    120     25   1094       C
ATOM   4005  O   PRO B 154    -115.145  55.053  27.559  1.00 34.36           O
ANISOU 4005  O   PRO B 154     3985   2740   6330    160    -16   1160       O
ATOM   4006  CB  PRO B 154    -113.951  58.132  27.427  1.00 34.41           C
ANISOU 4006  CB  PRO B 154     4053   2702   6320     42    104   1123       C
ATOM   4007  CG  PRO B 154    -115.056  58.375  28.400  1.00 33.58           C
ANISOU 4007  CG  PRO B 154     3980   2535   6244     66     94   1220       C
ATOM   4008  CD  PRO B 154    -116.341  58.300  27.607  1.00 32.23           C
ANISOU 4008  CD  PRO B 154     3796   2273   6178    101     86   1198       C
ATOM   4009  N   SER B 155    -113.107  55.214  26.600  1.00 38.51           N
ANISOU 4009  N   SER B 155     4498   3357   6777     96     16   1043       N
ATOM   4010  CA  SER B 155    -112.572  53.968  27.132  1.00 33.65           C
ANISOU 4010  CA  SER B 155     3875   2807   6105    104    -51   1065       C
ATOM   4011  C   SER B 155    -111.215  54.275  27.742  1.00 31.14           C
ANISOU 4011  C   SER B 155     3610   2542   5681     69    -52   1051       C
ATOM   4012  O   SER B 155    -110.296  54.698  27.034  1.00 31.79           O
ANISOU 4012  O   SER B 155     3682   2651   5745     41    -12    986       O
ATOM   4013  CB  SER B 155    -112.448  52.899  26.044  1.00 32.91           C
ANISOU 4013  CB  SER B 155     3709   2747   6049    119    -66   1022       C
ATOM   4014  OG  SER B 155    -111.827  51.733  26.553  1.00 37.64           O
ANISOU 4014  OG  SER B 155     4298   3401   6603    110   -146   1048       O
ATOM   4015  N   VAL B 156    -111.094  54.079  29.053  1.00 31.13           N
ANISOU 4015  N   VAL B 156     3671   2552   5604     80    -98   1112       N
ATOM   4016  CA  VAL B 156    -109.852  54.396  29.748  1.00 34.96           C
ANISOU 4016  CA  VAL B 156     4228   3084   5973     68    -90   1104       C
ATOM   4017  C   VAL B 156    -108.805  53.348  29.394  1.00 41.33           C
ANISOU 4017  C   VAL B 156     5030   3940   6734     56   -150   1049       C
ATOM   4018  O   VAL B 156    -108.993  52.152  29.644  1.00 43.79           O
ANISOU 4018  O   VAL B 156     5335   4256   7047     62   -245   1069       O
ATOM   4019  CB  VAL B 156    -110.073  54.472  31.264  1.00 35.71           C
ANISOU 4019  CB  VAL B 156     4411   3173   5982     99   -122   1186       C
ATOM   4020  CG1 VAL B 156    -108.767  54.792  31.969  1.00 28.06           C
ANISOU 4020  CG1 VAL B 156     3531   2253   4879    109   -102   1176       C
ATOM   4021  CG2 VAL B 156    -111.128  55.517  31.592  1.00 35.53           C
ANISOU 4021  CG2 VAL B 156     4388   3098   6016    107    -61   1253       C
ATOM   4022  N   GLY B 157    -107.697  53.795  28.810  1.00 41.38           N
ANISOU 4022  N   GLY B 157     5035   3979   6708     36   -100    986       N
ATOM   4023  CA  GLY B 157    -106.643  52.904  28.396  1.00 25.55           C
ANISOU 4023  CA  GLY B 157     3029   2013   4666     21   -149    933       C
ATOM   4024  C   GLY B 157    -105.718  52.527  29.534  1.00 34.05           C
ANISOU 4024  C   GLY B 157     4215   3110   5612     38   -209    944       C
ATOM   4025  O   GLY B 157    -105.994  52.796  30.707  1.00 32.32           O
ANISOU 4025  O   GLY B 157     4075   2879   5325     69   -221    998       O
ATOM   4026  N   PRO B 158    -104.598  51.888  29.205  1.00 34.40           N
ANISOU 4026  N   PRO B 158     4277   3181   5615     25   -251    891       N
ATOM   4027  CA  PRO B 158    -103.649  51.480  30.245  1.00 28.85           C
ANISOU 4027  CA  PRO B 158     3701   2484   4779     49   -319    888       C
ATOM   4028  C   PRO B 158    -102.947  52.677  30.866  1.00 27.58           C
ANISOU 4028  C   PRO B 158     3620   2344   4514     92   -222    889       C
ATOM   4029  O   PRO B 158    -102.911  53.778  30.310  1.00 28.64           O
ANISOU 4029  O   PRO B 158     3696   2494   4690     86   -108    884       O
ATOM   4030  CB  PRO B 158    -102.660  50.584  29.492  1.00 25.57           C
ANISOU 4030  CB  PRO B 158     3266   2080   4368     18   -378    830       C
ATOM   4031  CG  PRO B 158    -102.740  51.048  28.077  1.00 24.71           C
ANISOU 4031  CG  PRO B 158     3038   1991   4359     -9   -286    793       C
ATOM   4032  CD  PRO B 158    -104.164  51.473  27.860  1.00 24.81           C
ANISOU 4032  CD  PRO B 158     2976   1983   4466     -8   -242    834       C
ATOM   4033  N   LYS B 159    -102.383  52.442  32.053  1.00 28.42           N
ANISOU 4033  N   LYS B 159     3868   2449   4483    139   -272    902       N
ATOM   4034  CA  LYS B 159    -101.667  53.504  32.751  1.00 29.38           C
ANISOU 4034  CA  LYS B 159     4076   2599   4490    201   -170    917       C
ATOM   4035  C   LYS B 159    -100.383  53.890  32.032  1.00 31.72           C
ANISOU 4035  C   LYS B 159     4356   2928   4767    204   -104    856       C
ATOM   4036  O   LYS B 159     -99.951  55.045  32.117  1.00 34.30           O
ANISOU 4036  O   LYS B 159     4676   3289   5066    238     20    878       O
ATOM   4037  CB  LYS B 159    -101.340  53.075  34.182  1.00 29.67           C
ANISOU 4037  CB  LYS B 159     4289   2622   4362    269   -243    939       C
ATOM   4038  CG  LYS B 159    -102.531  52.994  35.115  1.00 35.15           C
ANISOU 4038  CG  LYS B 159     5018   3291   5045    285   -287   1017       C
ATOM   4039  CD  LYS B 159    -102.078  52.680  36.533  1.00 46.53           C
ANISOU 4039  CD  LYS B 159     6659   4723   6297    365   -354   1033       C
ATOM   4040  CE  LYS B 159    -103.244  52.692  37.508  1.00 58.30           C
ANISOU 4040  CE  LYS B 159     8192   6193   7765    389   -391   1119       C
ATOM   4041  NZ  LYS B 159    -102.797  52.445  38.909  1.00 63.02           N
ANISOU 4041  NZ  LYS B 159     9004   6783   8159    478   -454   1134       N
ATOM   4042  N   GLN B 160     -99.763  52.951  31.328  1.00 29.40           N
ANISOU 4042  N   GLN B 160     4049   2627   4495    170   -183    791       N
ATOM   4043  CA  GLN B 160     -98.438  53.151  30.765  1.00 32.71           C
ANISOU 4043  CA  GLN B 160     4478   3072   4878    182   -140    733       C
ATOM   4044  C   GLN B 160     -98.507  53.404  29.264  1.00 31.85           C
ANISOU 4044  C   GLN B 160     4216   2981   4903    120    -90    699       C
ATOM   4045  O   GLN B 160     -99.460  53.018  28.582  1.00 30.10           O
ANISOU 4045  O   GLN B 160     3898   2744   4794     68   -120    705       O
ATOM   4046  CB  GLN B 160     -97.542  51.941  31.046  1.00 32.57           C
ANISOU 4046  CB  GLN B 160     4572   3025   4779    191   -270    684       C
ATOM   4047  CG  GLN B 160     -97.873  50.700  30.221  1.00 39.58           C
ANISOU 4047  CG  GLN B 160     5379   3884   5775    111   -387    663       C
ATOM   4048  CD  GLN B 160     -99.017  49.882  30.794  1.00 43.74           C
ANISOU 4048  CD  GLN B 160     5905   4376   6339     86   -499    714       C
ATOM   4049  OE1 GLN B 160     -99.848  50.391  31.546  1.00 46.74           O
ANISOU 4049  OE1 GLN B 160     6307   4756   6697    115   -469    765       O
ATOM   4050  NE2 GLN B 160     -99.060  48.602  30.441  1.00 44.82           N
ANISOU 4050  NE2 GLN B 160     6009   4483   6537     31   -630    710       N
ATOM   4051  N   ALA B 161     -97.469  54.067  28.760  1.00 31.36           N
ANISOU 4051  N   ALA B 161     4140   2953   4821    136    -12    667       N
ATOM   4052  CA  ALA B 161     -97.317  54.306  27.334  1.00 29.56           C
ANISOU 4052  CA  ALA B 161     3790   2744   4696     85     26    628       C
ATOM   4053  C   ALA B 161     -95.833  54.266  27.005  1.00 31.66           C
ANISOU 4053  C   ALA B 161     4094   3034   4901    111     38    579       C
ATOM   4054  O   ALA B 161     -94.979  54.238  27.894  1.00 34.89           O
ANISOU 4054  O   ALA B 161     4622   3444   5190    176     36    578       O
ATOM   4055  CB  ALA B 161     -97.944  55.638  26.914  1.00 27.81           C
ANISOU 4055  CB  ALA B 161     3473   2540   4555     67    130    660       C
ATOM   4056  N   SER B 162     -95.532  54.263  25.711  1.00 30.48           N
ANISOU 4056  N   SER B 162     3852   2900   4827     68     51    538       N
ATOM   4057  CA  SER B 162     -94.160  54.180  25.231  1.00 30.21           C
ANISOU 4057  CA  SER B 162     3841   2886   4752     87     58    493       C
ATOM   4058  C   SER B 162     -93.647  55.581  24.927  1.00 29.33           C
ANISOU 4058  C   SER B 162     3675   2821   4649    110    175    506       C
ATOM   4059  O   SER B 162     -94.257  56.313  24.140  1.00 33.85           O
ANISOU 4059  O   SER B 162     4140   3406   5316     66    219    514       O
ATOM   4060  CB  SER B 162     -94.070  53.293  23.990  1.00 29.39           C
ANISOU 4060  CB  SER B 162     3670   2775   4721     30     -1    451       C
ATOM   4061  OG  SER B 162     -92.748  53.265  23.483  1.00 35.66           O
ANISOU 4061  OG  SER B 162     4483   3587   5480     48      8    412       O
ATOM   4062  N   LEU B 163     -92.534  55.951  25.551  1.00 29.00           N
ANISOU 4062  N   LEU B 163     3710   2800   4510    183    219    511       N
ATOM   4063  CA  LEU B 163     -91.870  57.228  25.303  1.00 32.04           C
ANISOU 4063  CA  LEU B 163     4035   3236   4904    214    329    537       C
ATOM   4064  C   LEU B 163     -90.464  56.929  24.794  1.00 33.66           C
ANISOU 4064  C   LEU B 163     4270   3455   5065    247    322    488       C
ATOM   4065  O   LEU B 163     -89.576  56.579  25.579  1.00 37.56           O
ANISOU 4065  O   LEU B 163     4888   3940   5444    327    315    478       O
ATOM   4066  CB  LEU B 163     -91.835  58.089  26.560  1.00 34.03           C
ANISOU 4066  CB  LEU B 163     4340   3512   5080    291    417    610       C
ATOM   4067  CG  LEU B 163     -91.081  59.412  26.407  1.00 34.39           C
ANISOU 4067  CG  LEU B 163     4311   3617   5141    331    538    660       C
ATOM   4068  CD1 LEU B 163     -91.707  60.261  25.312  1.00 31.33           C
ANISOU 4068  CD1 LEU B 163     3760   3241   4904    238    558    677       C
ATOM   4069  CD2 LEU B 163     -91.039  60.171  27.721  1.00 34.44           C
ANISOU 4069  CD2 LEU B 163     4371   3651   5064    421    637    750       C
ATOM   4070  N   ASN B 164     -90.269  57.065  23.481  1.00 29.47           N
ANISOU 4070  N   ASN B 164     3637   2941   4619    192    319    457       N
ATOM   4071  CA  ASN B 164     -88.973  56.826  22.843  1.00 30.80           C
ANISOU 4071  CA  ASN B 164     3818   3124   4761    217    311    416       C
ATOM   4072  C   ASN B 164     -88.470  55.414  23.129  1.00 36.94           C
ANISOU 4072  C   ASN B 164     4716   3850   5469    232    211    370       C
ATOM   4073  O   ASN B 164     -87.300  55.203  23.454  1.00 42.40           O
ANISOU 4073  O   ASN B 164     5500   4534   6077    300    209    351       O
ATOM   4074  CB  ASN B 164     -87.942  57.869  23.279  1.00 30.98           C
ANISOU 4074  CB  ASN B 164     3848   3194   4731    304    412    455       C
ATOM   4075  CG  ASN B 164     -88.420  59.286  23.050  1.00 34.29           C
ANISOU 4075  CG  ASN B 164     4135   3658   5235    279    500    519       C
ATOM   4076  OD1 ASN B 164     -89.010  59.595  22.015  1.00 39.13           O
ANISOU 4076  OD1 ASN B 164     4640   4273   5953    195    479    507       O
ATOM   4077  ND2 ASN B 164     -88.176  60.156  24.023  1.00 34.31           N
ANISOU 4077  ND2 ASN B 164     4151   3694   5190    353    595    592       N
ATOM   4078  N   GLY B 165     -89.364  54.436  23.010  1.00 34.78           N
ANISOU 4078  N   GLY B 165     4441   3537   5236    168    124    358       N
ATOM   4079  CA  GLY B 165     -89.024  53.056  23.270  1.00 28.39           C
ANISOU 4079  CA  GLY B 165     3729   2673   4386    161      9    329       C
ATOM   4080  C   GLY B 165     -89.036  52.655  24.725  1.00 28.04           C
ANISOU 4080  C   GLY B 165     3833   2586   4236    215    -40    339       C
ATOM   4081  O   GLY B 165     -88.784  51.481  25.026  1.00 34.71           O
ANISOU 4081  O   GLY B 165     4769   3370   5048    202   -159    317       O
ATOM   4082  N   VAL B 166     -89.320  53.580  25.636  1.00 28.79           N
ANISOU 4082  N   VAL B 166     3958   2705   4276    274     41    376       N
ATOM   4083  CA  VAL B 166     -89.346  53.305  27.067  1.00 30.19           C
ANISOU 4083  CA  VAL B 166     4292   2847   4333    342      5    389       C
ATOM   4084  C   VAL B 166     -90.799  53.291  27.518  1.00 27.27           C
ANISOU 4084  C   VAL B 166     3884   2472   4007    298    -14    433       C
ATOM   4085  O   VAL B 166     -91.484  54.321  27.467  1.00 31.91           O
ANISOU 4085  O   VAL B 166     4379   3101   4645    293     85    479       O
ATOM   4086  CB  VAL B 166     -88.533  54.339  27.858  1.00 34.80           C
ANISOU 4086  CB  VAL B 166     4952   3467   4802    463    123    412       C
ATOM   4087  CG1 VAL B 166     -88.474  53.951  29.328  1.00 36.78           C
ANISOU 4087  CG1 VAL B 166     5397   3676   4902    548     78    417       C
ATOM   4088  CG2 VAL B 166     -87.135  54.473  27.275  1.00 25.09           C
ANISOU 4088  CG2 VAL B 166     3735   2249   3547    510    156    376       C
ATOM   4089  N   THR B 167     -91.270  52.126  27.952  1.00 26.06           N
ANISOU 4089  N   THR B 167     3798   2261   3844    264   -148    425       N
ATOM   4090  CA  THR B 167     -92.623  51.997  28.472  1.00 32.19           C
ANISOU 4090  CA  THR B 167     4550   3026   4656    232   -180    471       C
ATOM   4091  C   THR B 167     -92.644  52.389  29.944  1.00 35.15           C
ANISOU 4091  C   THR B 167     5069   3394   4892    322   -159    502       C
ATOM   4092  O   THR B 167     -91.884  51.843  30.751  1.00 36.09           O
ANISOU 4092  O   THR B 167     5357   3472   4882    384   -231    473       O
ATOM   4093  CB  THR B 167     -93.129  50.567  28.293  1.00 35.27           C
ANISOU 4093  CB  THR B 167     4934   3363   5105    157   -336    464       C
ATOM   4094  OG1 THR B 167     -93.118  50.229  26.901  1.00 44.64           O
ANISOU 4094  OG1 THR B 167     5983   4564   6413     86   -336    446       O
ATOM   4095  CG2 THR B 167     -94.543  50.434  28.829  1.00 28.04           C
ANISOU 4095  CG2 THR B 167     3986   2437   4230    132   -369    518       C
ATOM   4096  N   LEU B 168     -93.517  53.330  30.294  1.00 33.45           N
ANISOU 4096  N   LEU B 168     4798   3214   4699    334    -65    562       N
ATOM   4097  CA  LEU B 168     -93.498  53.898  31.633  1.00 35.66           C
ANISOU 4097  CA  LEU B 168     5203   3502   4844    431    -11    608       C
ATOM   4098  C   LEU B 168     -94.869  54.461  31.979  1.00 34.31           C
ANISOU 4098  C   LEU B 168     4960   3344   4734    405     32    683       C
ATOM   4099  O   LEU B 168     -95.646  54.832  31.096  1.00 33.26           O
ANISOU 4099  O   LEU B 168     4670   3223   4744    329     67    698       O
ATOM   4100  CB  LEU B 168     -92.432  54.994  31.745  1.00 40.28           C
ANISOU 4100  CB  LEU B 168     5807   4141   5357    523    136    621       C
ATOM   4101  CG  LEU B 168     -92.447  56.061  30.642  1.00 38.13           C
ANISOU 4101  CG  LEU B 168     5346   3924   5217    476    255    644       C
ATOM   4102  CD1 LEU B 168     -93.336  57.246  31.005  1.00 37.02           C
ANISOU 4102  CD1 LEU B 168     5122   3820   5123    477    367    737       C
ATOM   4103  CD2 LEU B 168     -91.036  56.529  30.316  1.00 36.64           C
ANISOU 4103  CD2 LEU B 168     5169   3772   4982    542    332    621       C
ATOM   4104  N   ILE B 169     -95.147  54.523  33.277  1.00 33.14           N
ANISOU 4104  N   ILE B 169     4941   3186   4466    476     27    727       N
ATOM   4105  CA  ILE B 169     -96.299  55.248  33.799  1.00 33.59           C
ANISOU 4105  CA  ILE B 169     4950   3257   4554    476     92    814       C
ATOM   4106  C   ILE B 169     -95.822  56.656  34.129  1.00 38.78           C
ANISOU 4106  C   ILE B 169     5593   3975   5166    552    269    878       C
ATOM   4107  O   ILE B 169     -95.070  56.860  35.086  1.00 43.74           O
ANISOU 4107  O   ILE B 169     6364   4622   5634    666    317    896       O
ATOM   4108  CB  ILE B 169     -96.897  54.557  35.029  1.00 35.52           C
ANISOU 4108  CB  ILE B 169     5340   3462   4695    512    -12    840       C
ATOM   4109  CG1 ILE B 169     -97.339  53.136  34.675  1.00 37.50           C
ANISOU 4109  CG1 ILE B 169     5584   3655   5010    430   -196    792       C
ATOM   4110  CG2 ILE B 169     -98.066  55.364  35.571  1.00 31.09           C
ANISOU 4110  CG2 ILE B 169     4731   2915   4166    516     64    939       C
ATOM   4111  CD1 ILE B 169     -97.921  52.374  35.842  1.00 41.94           C
ANISOU 4111  CD1 ILE B 169     6283   4172   5480    456   -326    819       C
ATOM   4112  N   GLY B 170     -96.255  57.628  33.332  1.00 36.78           N
ANISOU 4112  N   GLY B 170     5168   3751   5055    492    365    918       N
ATOM   4113  CA  GLY B 170     -95.671  58.951  33.405  1.00 38.71           C
ANISOU 4113  CA  GLY B 170     5359   4056   5292    544    525    984       C
ATOM   4114  C   GLY B 170     -95.981  59.668  34.706  1.00 41.22           C
ANISOU 4114  C   GLY B 170     5750   4400   5512    632    619   1094       C
ATOM   4115  O   GLY B 170     -97.052  59.519  35.296  1.00 39.15           O
ANISOU 4115  O   GLY B 170     5514   4109   5254    616    581   1140       O
ATOM   4116  N   GLU B 171     -95.009  60.459  35.155  1.00 40.06           N
ANISOU 4116  N   GLU B 171     5634   4311   5275    736    751   1145       N
ATOM   4117  CA  GLU B 171     -95.165  61.355  36.294  1.00 40.03           C
ANISOU 4117  CA  GLU B 171     5673   4350   5185    832    881   1274       C
ATOM   4118  C   GLU B 171     -95.029  62.813  35.889  1.00 41.30           C
ANISOU 4118  C   GLU B 171     5656   4572   5464    815   1039   1382       C
ATOM   4119  O   GLU B 171     -95.880  63.636  36.246  1.00 43.50           O
ANISOU 4119  O   GLU B 171     5859   4859   5810    790   1109   1499       O
ATOM   4120  CB  GLU B 171     -94.137  61.013  37.383  1.00 46.31           C
ANISOU 4120  CB  GLU B 171     6683   5165   5746    998    911   1262       C
ATOM   4121  CG  GLU B 171     -94.189  59.571  37.855  1.00 53.72           C
ANISOU 4121  CG  GLU B 171     7815   6034   6563   1013    733   1158       C
ATOM   4122  CD  GLU B 171     -93.126  59.261  38.892  1.00 63.66           C
ANISOU 4122  CD  GLU B 171     9308   7298   7581   1183    751   1135       C
ATOM   4123  OE1 GLU B 171     -92.472  60.209  39.376  1.00 66.83           O
ANISOU 4123  OE1 GLU B 171     9726   7767   7898   1307    923   1216       O
ATOM   4124  OE2 GLU B 171     -92.943  58.069  39.220  1.00 66.05           O
ANISOU 4124  OE2 GLU B 171     9782   7534   7780   1196    589   1039       O
ATOM   4125  N   ALA B 172     -93.973  63.157  35.152  1.00 39.81           N
ANISOU 4125  N   ALA B 172     5395   4422   5308    825   1090   1353       N
ATOM   4126  CA  ALA B 172     -93.847  64.482  34.560  1.00 43.09           C
ANISOU 4126  CA  ALA B 172     5615   4888   5869    783   1208   1450       C
ATOM   4127  C   ALA B 172     -94.634  64.617  33.265  1.00 40.10           C
ANISOU 4127  C   ALA B 172     5072   4465   5701    614   1124   1408       C
ATOM   4128  O   ALA B 172     -94.737  65.726  32.731  1.00 42.55           O
ANISOU 4128  O   ALA B 172     5216   4798   6152    553   1191   1488       O
ATOM   4129  CB  ALA B 172     -92.373  64.807  34.305  1.00 44.04           C
ANISOU 4129  CB  ALA B 172     5723   5070   5939    871   1294   1442       C
ATOM   4130  N   VAL B 173     -95.182  63.515  32.751  1.00 38.64           N
ANISOU 4130  N   VAL B 173     4931   4215   5537    541    977   1290       N
ATOM   4131  CA  VAL B 173     -96.005  63.511  31.550  1.00 42.94           C
ANISOU 4131  CA  VAL B 173     5348   4711   6257    400    896   1241       C
ATOM   4132  C   VAL B 173     -97.134  62.513  31.773  1.00 43.10           C
ANISOU 4132  C   VAL B 173     5440   4664   6271    362    781   1194       C
ATOM   4133  O   VAL B 173     -97.065  61.652  32.652  1.00 48.11           O
ANISOU 4133  O   VAL B 173     6222   5289   6770    430    735   1172       O
ATOM   4134  CB  VAL B 173     -95.187  63.151  30.287  1.00 48.16           C
ANISOU 4134  CB  VAL B 173     5956   5377   6965    359    844   1133       C
ATOM   4135  CG1 VAL B 173     -94.887  61.657  30.249  1.00 44.96           C
ANISOU 4135  CG1 VAL B 173     5678   4939   6464    379    730   1015       C
ATOM   4136  CG2 VAL B 173     -95.900  63.612  29.020  1.00 54.49           C
ANISOU 4136  CG2 VAL B 173     6609   6145   7948    231    801   1113       C
ATOM   4137  N   LYS B 174     -98.192  62.644  30.979  1.00 40.40           N
ANISOU 4137  N   LYS B 174     5000   4272   6078    255    729   1181       N
ATOM   4138  CA  LYS B 174     -99.363  61.787  31.107  1.00 42.85           C
ANISOU 4138  CA  LYS B 174     5354   4521   6407    220    630   1151       C
ATOM   4139  C   LYS B 174     -99.299  60.669  30.074  1.00 38.33           C
ANISOU 4139  C   LYS B 174     4775   3921   5868    172    520   1027       C
ATOM   4140  O   LYS B 174     -99.141  60.932  28.877  1.00 36.07           O
ANISOU 4140  O   LYS B 174     4392   3633   5679    112    515    979       O
ATOM   4141  CB  LYS B 174    -100.652  62.594  30.947  1.00 49.16           C
ANISOU 4141  CB  LYS B 174     6063   5274   7343    150    646   1221       C
ATOM   4142  CG  LYS B 174    -101.859  61.954  31.614  1.00 56.73           C
ANISOU 4142  CG  LYS B 174     7086   6179   8288    153    582   1242       C
ATOM   4143  CD  LYS B 174    -102.924  62.986  31.948  1.00 60.65           C
ANISOU 4143  CD  LYS B 174     7526   6638   8879    118    633   1352       C
ATOM   4144  CE  LYS B 174    -104.111  62.887  31.008  1.00 64.10           C
ANISOU 4144  CE  LYS B 174     7895   6995   9463     34    561   1310       C
ATOM   4145  NZ  LYS B 174    -104.790  61.565  31.110  1.00 66.61           N
ANISOU 4145  NZ  LYS B 174     8279   7280   9750     49    460   1252       N
ATOM   4146  N   THR B 175     -99.417  59.426  30.543  1.00 37.69           N
ANISOU 4146  N   THR B 175     4796   3820   5706    199    428    984       N
ATOM   4147  CA  THR B 175     -99.361  58.251  29.683  1.00 32.52           C
ANISOU 4147  CA  THR B 175     4133   3142   5081    158    323    888       C
ATOM   4148  C   THR B 175    -100.678  57.490  29.620  1.00 34.19           C
ANISOU 4148  C   THR B 175     4330   3301   5358    118    237    888       C
ATOM   4149  O   THR B 175    -100.775  56.511  28.873  1.00 36.90           O
ANISOU 4149  O   THR B 175     4647   3628   5743     84    158    827       O
ATOM   4150  CB  THR B 175     -98.246  57.304  30.147  1.00 26.62           C
ANISOU 4150  CB  THR B 175     3505   2408   4200    215    267    839       C
ATOM   4151  OG1 THR B 175     -98.450  56.953  31.521  1.00 27.24           O
ANISOU 4151  OG1 THR B 175     3715   2474   4160    278    236    882       O
ATOM   4152  CG2 THR B 175     -96.884  57.963  29.994  1.00 25.82           C
ANISOU 4152  CG2 THR B 175     3410   2357   4045    261    351    828       C
ATOM   4153  N   GLN B 176    -101.690  57.905  30.377  1.00 35.73           N
ANISOU 4153  N   GLN B 176     4536   3472   5566    126    256    964       N
ATOM   4154  CA  GLN B 176    -102.998  57.262  30.360  1.00 33.77           C
ANISOU 4154  CA  GLN B 176     4270   3173   5386     99    182    975       C
ATOM   4155  C   GLN B 176    -103.942  58.086  29.493  1.00 35.38           C
ANISOU 4155  C   GLN B 176     4366   3342   5735     45    226    987       C
ATOM   4156  O   GLN B 176    -104.121  59.286  29.730  1.00 36.86           O
ANISOU 4156  O   GLN B 176     4527   3525   5952     38    305   1048       O
ATOM   4157  CB  GLN B 176    -103.553  57.111  31.775  1.00 37.61           C
ANISOU 4157  CB  GLN B 176     4853   3647   5791    148    159   1051       C
ATOM   4158  CG  GLN B 176    -104.867  56.350  31.838  1.00 37.21           C
ANISOU 4158  CG  GLN B 176     4785   3547   5806    128     73   1070       C
ATOM   4159  CD  GLN B 176    -105.134  55.769  33.210  1.00 43.51           C
ANISOU 4159  CD  GLN B 176     5700   4337   6496    179      5   1124       C
ATOM   4160  OE1 GLN B 176    -104.820  56.381  34.231  1.00 49.49           O
ANISOU 4160  OE1 GLN B 176     6543   5113   7146    234     60   1180       O
ATOM   4161  NE2 GLN B 176    -105.707  54.572  33.242  1.00 45.85           N
ANISOU 4161  NE2 GLN B 176     5999   4606   6816    167   -115   1115       N
ATOM   4162  N   PHE B 177    -104.545  57.444  28.496  1.00 36.99           N
ANISOU 4162  N   PHE B 177     4511   3517   6027     10    173    934       N
ATOM   4163  CA  PHE B 177    -105.398  58.125  27.537  1.00 36.84           C
ANISOU 4163  CA  PHE B 177     4411   3453   6133    -32    202    924       C
ATOM   4164  C   PHE B 177    -106.802  57.537  27.546  1.00 34.31           C
ANISOU 4164  C   PHE B 177     4082   3077   5879    -27    152    944       C
ATOM   4165  O   PHE B 177    -107.033  56.420  28.016  1.00 34.55           O
ANISOU 4165  O   PHE B 177     4140   3112   5874     -1     85    954       O
ATOM   4166  CB  PHE B 177    -104.838  58.029  26.111  1.00 35.09           C
ANISOU 4166  CB  PHE B 177     4131   3247   5956    -63    202    836       C
ATOM   4167  CG  PHE B 177    -103.361  58.257  26.018  1.00 34.41           C
ANISOU 4167  CG  PHE B 177     4053   3220   5800    -60    232    807       C
ATOM   4168  CD1 PHE B 177    -102.819  59.498  26.304  1.00 33.85           C
ANISOU 4168  CD1 PHE B 177     3970   3170   5723    -64    305    848       C
ATOM   4169  CD2 PHE B 177    -102.514  57.233  25.625  1.00 32.72           C
ANISOU 4169  CD2 PHE B 177     3854   3040   5536    -50    187    748       C
ATOM   4170  CE1 PHE B 177    -101.457  59.710  26.212  1.00 37.54           C
ANISOU 4170  CE1 PHE B 177     4441   3693   6128    -49    339    828       C
ATOM   4171  CE2 PHE B 177    -101.152  57.438  25.529  1.00 29.95           C
ANISOU 4171  CE2 PHE B 177     3518   2738   5123    -40    214    720       C
ATOM   4172  CZ  PHE B 177    -100.622  58.678  25.823  1.00 33.05           C
ANISOU 4172  CZ  PHE B 177     3901   3154   5504    -34    292    759       C
ATOM   4173  N   ASN B 178    -107.738  58.318  27.019  1.00 32.86           N
ANISOU 4173  N   ASN B 178     3856   2833   5794    -50    180    953       N
ATOM   4174  CA  ASN B 178    -109.018  57.784  26.590  1.00 33.42           C
ANISOU 4174  CA  ASN B 178     3905   2847   5944    -37    144    948       C
ATOM   4175  C   ASN B 178    -108.879  57.227  25.180  1.00 34.34           C
ANISOU 4175  C   ASN B 178     3975   2972   6101    -42    131    860       C
ATOM   4176  O   ASN B 178    -108.103  57.733  24.366  1.00 34.44           O
ANISOU 4176  O   ASN B 178     3967   3004   6114    -70    158    804       O
ATOM   4177  CB  ASN B 178    -110.101  58.863  26.621  1.00 35.79           C
ANISOU 4177  CB  ASN B 178     4202   3066   6332    -53    173    992       C
ATOM   4178  CG  ASN B 178    -110.400  59.351  28.022  1.00 33.49           C
ANISOU 4178  CG  ASN B 178     3953   2764   6006    -42    190   1097       C
ATOM   4179  OD1 ASN B 178    -110.228  58.620  28.996  1.00 33.53           O
ANISOU 4179  OD1 ASN B 178     4004   2808   5927     -6    160   1136       O
ATOM   4180  ND2 ASN B 178    -110.855  60.593  28.131  1.00 30.62           N
ANISOU 4180  ND2 ASN B 178     3582   2346   5708    -74    232   1149       N
ATOM   4181  N   TYR B 179    -109.630  56.171  24.895  1.00 31.99           N
ANISOU 4181  N   TYR B 179     3657   2662   5836     -8     92    857       N
ATOM   4182  CA  TYR B 179    -109.569  55.511  23.601  1.00 27.83           C
ANISOU 4182  CA  TYR B 179     3085   2150   5340      4     91    790       C
ATOM   4183  C   TYR B 179    -110.933  55.553  22.930  1.00 26.46           C
ANISOU 4183  C   TYR B 179     2895   1907   5251     42    104    785       C
ATOM   4184  O   TYR B 179    -111.968  55.421  23.592  1.00 32.15           O
ANISOU 4184  O   TYR B 179     3625   2584   6006     72     88    846       O
ATOM   4185  CB  TYR B 179    -109.089  54.065  23.742  1.00 26.83           C
ANISOU 4185  CB  TYR B 179     2936   2083   5177     18     38    800       C
ATOM   4186  CG  TYR B 179    -107.592  53.942  23.911  1.00 33.06           C
ANISOU 4186  CG  TYR B 179     3745   2932   5883    -12     26    771       C
ATOM   4187  CD1 TYR B 179    -106.986  54.217  25.129  1.00 32.76           C
ANISOU 4187  CD1 TYR B 179     3770   2910   5768    -20     11    806       C
ATOM   4188  CD2 TYR B 179    -106.784  53.554  22.850  1.00 40.05           C
ANISOU 4188  CD2 TYR B 179     4597   3856   6763    -23     33    711       C
ATOM   4189  CE1 TYR B 179    -105.616  54.108  25.286  1.00 35.30           C
ANISOU 4189  CE1 TYR B 179     4124   3279   6008    -32      3    777       C
ATOM   4190  CE2 TYR B 179    -105.413  53.440  22.998  1.00 43.10           C
ANISOU 4190  CE2 TYR B 179     5008   4290   7077    -46     21    686       C
ATOM   4191  CZ  TYR B 179    -104.835  53.719  24.218  1.00 41.86           C
ANISOU 4191  CZ  TYR B 179     4919   4143   6845    -48      5    716       C
ATOM   4192  OH  TYR B 179    -103.472  53.607  24.371  1.00 42.41           O
ANISOU 4192  OH  TYR B 179     5025   4252   6837    -55     -4    687       O
ATOM   4193  N   TYR B 180    -110.923  55.745  21.613  1.00 29.82           N
ANISOU 4193  N   TYR B 180     3307   2320   5703     50    131    712       N
ATOM   4194  CA  TYR B 180    -112.133  55.802  20.809  1.00 32.09           C
ANISOU 4194  CA  TYR B 180     3599   2537   6055    102    149    690       C
ATOM   4195  C   TYR B 180    -111.869  55.095  19.488  1.00 33.09           C
ANISOU 4195  C   TYR B 180     3697   2704   6172    141    170    628       C
ATOM   4196  O   TYR B 180    -110.754  55.136  18.963  1.00 32.37           O
ANISOU 4196  O   TYR B 180     3596   2666   6036    106    175    581       O
ATOM   4197  CB  TYR B 180    -112.579  57.249  20.555  1.00 29.76           C
ANISOU 4197  CB  TYR B 180     3355   2151   5802     73    161    662       C
ATOM   4198  CG  TYR B 180    -112.565  58.126  21.789  1.00 29.82           C
ANISOU 4198  CG  TYR B 180     3382   2132   5815     22    153    731       C
ATOM   4199  CD1 TYR B 180    -111.415  58.808  22.167  1.00 29.37           C
ANISOU 4199  CD1 TYR B 180     3320   2122   5718    -42    162    737       C
ATOM   4200  CD2 TYR B 180    -113.701  58.274  22.573  1.00 32.81           C
ANISOU 4200  CD2 TYR B 180     3784   2443   6240     45    145    800       C
ATOM   4201  CE1 TYR B 180    -111.396  59.607  23.291  1.00 26.55           C
ANISOU 4201  CE1 TYR B 180     2977   1749   5361    -77    172    815       C
ATOM   4202  CE2 TYR B 180    -113.692  59.076  23.699  1.00 34.16           C
ANISOU 4202  CE2 TYR B 180     3973   2594   6412      3    146    876       C
ATOM   4203  CZ  TYR B 180    -112.536  59.739  24.054  1.00 31.46           C
ANISOU 4203  CZ  TYR B 180     3623   2305   6025    -56    164    886       C
ATOM   4204  OH  TYR B 180    -112.521  60.536  25.174  1.00 30.28           O
ANISOU 4204  OH  TYR B 180     3488   2144   5873    -86    182    975       O
ATOM   4205  N   LYS B 181    -112.901  54.446  18.952  1.00 34.25           N
ANISOU 4205  N   LYS B 181     3829   2825   6359    222    190    636       N
ATOM   4206  CA  LYS B 181    -112.759  53.671  17.728  1.00 31.54           C
ANISOU 4206  CA  LYS B 181     3455   2526   6004    277    224    598       C
ATOM   4207  C   LYS B 181    -114.006  53.809  16.868  1.00 30.01           C
ANISOU 4207  C   LYS B 181     3299   2259   5846    373    266    569       C
ATOM   4208  O   LYS B 181    -115.130  53.772  17.376  1.00 29.21           O
ANISOU 4208  O   LYS B 181     3206   2098   5795    420    265    617       O
ATOM   4209  CB  LYS B 181    -112.503  52.189  18.033  1.00 33.22           C
ANISOU 4209  CB  LYS B 181     3580   2822   6218    296    210    670       C
ATOM   4210  CG  LYS B 181    -112.275  51.334  16.797  1.00 35.84           C
ANISOU 4210  CG  LYS B 181     3864   3212   6542    351    255    652       C
ATOM   4211  CD  LYS B 181    -112.125  49.866  17.155  1.00 43.13           C
ANISOU 4211  CD  LYS B 181     4686   4208   7492    359    231    746       C
ATOM   4212  CE  LYS B 181    -111.878  49.021  15.915  1.00 51.13           C
ANISOU 4212  CE  LYS B 181     5640   5284   8503    413    286    748       C
ATOM   4213  NZ  LYS B 181    -111.789  47.568  16.233  1.00 58.97           N
ANISOU 4213  NZ  LYS B 181     6517   6343   9546    414    256    858       N
ATOM   4214  N   LYS B 182    -113.797  53.964  15.563  1.00 32.49           N
ANISOU 4214  N   LYS B 182     3644   2573   6127    408    301    489       N
ATOM   4215  CA  LYS B 182    -114.871  54.016  14.583  1.00 30.45           C
ANISOU 4215  CA  LYS B 182     3442   2249   5878    519    347    448       C
ATOM   4216  C   LYS B 182    -114.652  52.936  13.536  1.00 31.26           C
ANISOU 4216  C   LYS B 182     3497   2433   5945    603    408    448       C
ATOM   4217  O   LYS B 182    -113.523  52.711  13.091  1.00 30.72           O
ANISOU 4217  O   LYS B 182     3400   2441   5829    558    409    425       O
ATOM   4218  CB  LYS B 182    -114.943  55.384  13.897  1.00 33.96           C
ANISOU 4218  CB  LYS B 182     4002   2596   6306    496    325    345       C
ATOM   4219  CG  LYS B 182    -115.447  56.504  14.781  1.00 44.73           C
ANISOU 4219  CG  LYS B 182     5415   3856   7724    431    273    357       C
ATOM   4220  CD  LYS B 182    -115.434  57.830  14.037  1.00 45.07           C
ANISOU 4220  CD  LYS B 182     5562   3800   7763    392    233    262       C
ATOM   4221  CE  LYS B 182    -116.343  57.786  12.821  1.00 39.47           C
ANISOU 4221  CE  LYS B 182     4952   3014   7032    513    257    186       C
ATOM   4222  NZ  LYS B 182    -116.239  59.027  12.005  1.00 33.97           N
ANISOU 4222  NZ  LYS B 182     4368   2217   6323    470    195     84       N
ATOM   4223  N   VAL B 183    -115.736  52.271  13.148  1.00 34.50           N
ANISOU 4223  N   VAL B 183     3898   2830   6382    731    466    484       N
ATOM   4224  CA  VAL B 183    -115.717  51.268  12.091  1.00 34.13           C
ANISOU 4224  CA  VAL B 183     3806   2858   6305    835    545    500       C
ATOM   4225  C   VAL B 183    -116.850  51.588  11.129  1.00 38.88           C
ANISOU 4225  C   VAL B 183     4512   3377   6885    981    608    443       C
ATOM   4226  O   VAL B 183    -118.023  51.577  11.523  1.00 44.73           O
ANISOU 4226  O   VAL B 183     5268   4049   7677   1056    622    480       O
ATOM   4227  CB  VAL B 183    -115.859  49.839  12.641  1.00 35.99           C
ANISOU 4227  CB  VAL B 183     3892   3182   6599    863    565    637       C
ATOM   4228  CG1 VAL B 183    -115.977  48.844  11.499  1.00 34.35           C
ANISOU 4228  CG1 VAL B 183     3629   3050   6374    985    663    673       C
ATOM   4229  CG2 VAL B 183    -114.676  49.491  13.527  1.00 32.63           C
ANISOU 4229  CG2 VAL B 183     3389   2828   6182    724    490    680       C
ATOM   4230  N   ASP B 184    -116.500  51.880   9.875  1.00 39.89           N
ANISOU 4230  N   ASP B 184     4698   3448   7012     34    322    474       N
ATOM   4231  CA  ASP B 184    -117.474  52.200   8.829  1.00 42.95           C
ANISOU 4231  CA  ASP B 184     5153   3796   7369     32    403    382       C
ATOM   4232  C   ASP B 184    -118.327  53.408   9.213  1.00 40.70           C
ANISOU 4232  C   ASP B 184     5032   3408   7024    109    259    431       C
ATOM   4233  O   ASP B 184    -119.542  53.427   9.004  1.00 41.84           O
ANISOU 4233  O   ASP B 184     5214   3471   7215    221    234    309       O
ATOM   4234  CB  ASP B 184    -118.354  50.991   8.502  1.00 48.56           C
ANISOU 4234  CB  ASP B 184     5664   4548   8237     93    514    127       C
ATOM   4235  CG  ASP B 184    -117.547  49.791   8.048  1.00 52.47           C
ANISOU 4235  CG  ASP B 184     6049   5146   8742    -83    718     42       C
ATOM   4236  OD1 ASP B 184    -116.450  49.989   7.483  1.00 50.66           O
ANISOU 4236  OD1 ASP B 184     6004   4898   8348   -253    789    193       O
ATOM   4237  OD2 ASP B 184    -118.009  48.649   8.256  1.00 55.21           O
ANISOU 4237  OD2 ASP B 184     6146   5586   9246    -55    794   -201       O
ATOM   4238  N   GLY B 185    -117.684  54.427   9.780  1.00 38.50           N
ANISOU 4238  N   GLY B 185     4868   3132   6626     32    170    577       N
ATOM   4239  CA  GLY B 185    -118.362  55.645  10.164  1.00 33.27           C
ANISOU 4239  CA  GLY B 185     4420   2375   5845      2     77    612       C
ATOM   4240  C   GLY B 185    -119.185  55.561  11.430  1.00 32.07           C
ANISOU 4240  C   GLY B 185     4386   2078   5722    120    -92    593       C
ATOM   4241  O   GLY B 185    -119.817  56.558  11.802  1.00 44.22           O
ANISOU 4241  O   GLY B 185     6208   3485   7110     55   -167    621       O
ATOM   4242  N   VAL B 186    -119.200  54.416  12.106  1.00 32.34           N
ANISOU 4242  N   VAL B 186     4257   2115   5914    272   -164    536       N
ATOM   4243  CA  VAL B 186    -119.983  54.217  13.320  1.00 37.79           C
ANISOU 4243  CA  VAL B 186     5087   2645   6626    430   -385    504       C
ATOM   4244  C   VAL B 186    -119.025  54.021  14.486  1.00 37.34           C
ANISOU 4244  C   VAL B 186     4975   2647   6564    355   -436    595       C
ATOM   4245  O   VAL B 186    -118.114  53.187  14.417  1.00 39.09           O
ANISOU 4245  O   VAL B 186     4926   3025   6903    341   -344    590       O
ATOM   4246  CB  VAL B 186    -120.937  53.018  13.186  1.00 40.60           C
ANISOU 4246  CB  VAL B 186     5267   2973   7188    714   -474    290       C
ATOM   4247  CG1 VAL B 186    -121.774  52.861  14.447  1.00 37.36           C
ANISOU 4247  CG1 VAL B 186     5056   2360   6779    937   -788    243       C
ATOM   4248  CG2 VAL B 186    -121.824  53.183  11.963  1.00 42.11           C
ANISOU 4248  CG2 VAL B 186     5477   3129   7394    776   -389    161       C
ATOM   4249  N   VAL B 187    -119.232  54.788  15.556  1.00 37.43           N
ANISOU 4249  N   VAL B 187     5290   2517   6414    275   -568    669       N
ATOM   4250  CA  VAL B 187    -118.393  54.668  16.741  1.00 33.50           C
ANISOU 4250  CA  VAL B 187     4774   2064   5889    179   -609    736       C
ATOM   4251  C   VAL B 187    -118.674  53.341  17.430  1.00 40.09           C
ANISOU 4251  C   VAL B 187     5468   2865   6898    417   -772    663       C
ATOM   4252  O   VAL B 187    -119.829  53.005  17.722  1.00 51.18           O
ANISOU 4252  O   VAL B 187     7024   4091   8330    645   -989    572       O
ATOM   4253  CB  VAL B 187    -118.633  55.848  17.693  1.00 33.27           C
ANISOU 4253  CB  VAL B 187     5165   1880   5596    -36   -675    798       C
ATOM   4254  CG1 VAL B 187    -117.799  55.690  18.956  1.00 32.83           C
ANISOU 4254  CG1 VAL B 187     5098   1872   5505   -157   -700    840       C
ATOM   4255  CG2 VAL B 187    -118.316  57.161  16.999  1.00 34.66           C
ANISOU 4255  CG2 VAL B 187     5410   2151   5608   -306   -492    806       C
ATOM   4256  N  AGLN B 188    -117.615  52.576  17.677  0.73 42.21           N
ANISOU 4256  N  AGLN B 188     5452   3304   7282    382   -688    674       N
ATOM   4257  N  BGLN B 188    -117.620  52.578  17.703  0.27 41.82           N
ANISOU 4257  N  BGLN B 188     5406   3252   7231    383   -692    675       N
ATOM   4258  CA AGLN B 188    -117.710  51.316  18.394  0.73 43.79           C
ANISOU 4258  CA AGLN B 188     5480   3519   7638    554   -818    586       C
ATOM   4259  CA BGLN B 188    -117.748  51.296  18.380  0.27 44.06           C
ANISOU 4259  CA BGLN B 188     5513   3552   7677    562   -822    581       C
ATOM   4260  C  AGLN B 188    -117.517  51.556  19.883  0.73 45.84           C
ANISOU 4260  C  AGLN B 188     5970   3670   7778    491   -980    670       C
ATOM   4261  C  BGLN B 188    -117.428  51.439  19.862  0.27 45.65           C
ANISOU 4261  C  BGLN B 188     5903   3667   7774    494   -968    665       C
ATOM   4262  O  AGLN B 188    -116.733  52.418  20.289  0.73 47.72           O
ANISOU 4262  O  AGLN B 188     6334   3935   7864    248   -880    781       O
ATOM   4263  O  BGLN B 188    -116.468  52.117  20.240  0.27 45.91           O
ANISOU 4263  O  BGLN B 188     5995   3761   7689    261   -851    772       O
ATOM   4264  CB AGLN B 188    -116.654  50.328  17.893  0.73 44.20           C
ANISOU 4264  CB AGLN B 188     5167   3787   7838    498   -623    550       C
ATOM   4265  CB BGLN B 188    -116.833  50.242  17.753  0.27 44.87           C
ANISOU 4265  CB BGLN B 188     5236   3871   7943    528   -626    523       C
ATOM   4266  CG AGLN B 188    -116.789  49.947  16.431  0.73 47.14           C
ANISOU 4266  CG AGLN B 188     5361   4257   8292    502   -438    450       C
ATOM   4267  CG BGLN B 188    -117.451  49.506  16.577  0.27 49.05           C
ANISOU 4267  CG BGLN B 188     5549   4476   8612    630   -526    340       C
ATOM   4268  CD AGLN B 188    -117.946  49.003  16.181  0.73 51.41           C
ANISOU 4268  CD AGLN B 188     5725   4807   9002    717   -514    203       C
ATOM   4269  CD BGLN B 188    -116.828  48.142  16.356  0.27 49.94           C
ANISOU 4269  CD BGLN B 188     5339   4765   8869    582   -377    210       C
ATOM   4270  OE1AGLN B 188    -119.060  49.432  15.885  0.73 54.37           O
ANISOU 4270  OE1AGLN B 188     6224   5068   9368    866   -623    126       O
ATOM   4271  OE1BGLN B 188    -115.799  47.815  16.946  0.27 47.58           O
ANISOU 4271  OE1BGLN B 188     5002   4521   8556    472   -339    298       O
ATOM   4272  NE2AGLN B 188    -117.686  47.705  16.300  0.73 52.26           N
ANISOU 4272  NE2AGLN B 188     5532   5061   9262    732   -456     38       N
ATOM   4273  NE2BGLN B 188    -117.455  47.335  15.508  0.27 52.56           N
ANISOU 4273  NE2BGLN B 188     5449   5193   9327    637   -274    -30       N
ATOM   4274  N   GLN B 189    -118.238  50.791  20.696  1.00 43.97           N
ANISOU 4274  N   GLN B 189     5781   3321   7604    708  -1238    581       N
ATOM   4275  CA  GLN B 189    -118.022  50.793  22.136  1.00 44.21           C
ANISOU 4275  CA  GLN B 189     6028   3283   7488    639  -1384    639       C
ATOM   4276  C   GLN B 189    -116.932  49.779  22.461  1.00 45.84           C
ANISOU 4276  C   GLN B 189     5874   3663   7882    608  -1299    631       C
ATOM   4277  O   GLN B 189    -117.084  48.586  22.180  1.00 47.43           O
ANISOU 4277  O   GLN B 189     5743   3982   8294    785  -1325    475       O
ATOM   4278  CB  GLN B 189    -119.307  50.462  22.889  1.00 45.73           C
ANISOU 4278  CB  GLN B 189     6473   3340   7563    876  -1696    520       C
ATOM   4279  CG  GLN B 189    -119.137  50.497  24.399  1.00 52.31           C
ANISOU 4279  CG  GLN B 189     7597   4078   8202    781  -1854    583       C
ATOM   4280  CD  GLN B 189    -120.238  49.762  25.134  1.00 69.49           C
ANISOU 4280  CD  GLN B 189     9900   6166  10337   1069  -2205    426       C
ATOM   4281  OE1 GLN B 189    -121.308  49.505  24.581  1.00 75.40           O
ANISOU 4281  OE1 GLN B 189    10618   6892  11139   1327  -2345    268       O
ATOM   4282  NE2 GLN B 189    -119.977  49.412  26.388  1.00 75.85           N
ANISOU 4282  NE2 GLN B 189    10848   6922  11048   1029  -2364    447       N
ATOM   4283  N   LEU B 190    -115.835  50.252  23.040  1.00 43.63           N
ANISOU 4283  N   LEU B 190     5644   3440   7492    357  -1165    752       N
ATOM   4284  CA  LEU B 190    -114.723  49.366  23.344  1.00 36.98           C
ANISOU 4284  CA  LEU B 190     4509   2769   6772    305  -1058    744       C
ATOM   4285  C   LEU B 190    -115.073  48.474  24.533  1.00 39.13           C
ANISOU 4285  C   LEU B 190     4815   2972   7082    429  -1301    685       C
ATOM   4286  O   LEU B 190    -115.722  48.926  25.482  1.00 41.22           O
ANISOU 4286  O   LEU B 190     5452   3028   7180    442  -1530    722       O
ATOM   4287  CB  LEU B 190    -113.459  50.174  23.633  1.00 34.63           C
ANISOU 4287  CB  LEU B 190     4249   2554   6357     43   -872    844       C
ATOM   4288  CG  LEU B 190    -112.892  50.902  22.412  1.00 38.88           C
ANISOU 4288  CG  LEU B 190     4680   3206   6888    -38   -664    861       C
ATOM   4289  CD1 LEU B 190    -111.590  51.618  22.738  1.00 40.67           C
ANISOU 4289  CD1 LEU B 190     4871   3548   7034   -230   -530    878       C
ATOM   4290  CD2 LEU B 190    -112.693  49.923  21.264  1.00 37.98           C
ANISOU 4290  CD2 LEU B 190     4295   3192   6946     82   -565    812       C
ATOM   4291  N   PRO B 191    -114.664  47.209  24.514  1.00 39.11           N
ANISOU 4291  N   PRO B 191     4471   3124   7264    499  -1266    580       N
ATOM   4292  CA  PRO B 191    -115.093  46.274  25.556  1.00 42.22           C
ANISOU 4292  CA  PRO B 191     4841   3485   7718    650  -1528    472       C
ATOM   4293  C   PRO B 191    -114.322  46.458  26.854  1.00 40.76           C
ANISOU 4293  C   PRO B 191     4853   3243   7389    470  -1560    595       C
ATOM   4294  O   PRO B 191    -113.210  46.988  26.887  1.00 40.20           O
ANISOU 4294  O   PRO B 191     4793   3237   7244    232  -1327    712       O
ATOM   4295  CB  PRO B 191    -114.799  44.905  24.935  1.00 43.77           C
ANISOU 4295  CB  PRO B 191     4565   3917   8147    698  -1392    280       C
ATOM   4296  CG  PRO B 191    -113.625  45.162  24.054  1.00 32.49           C
ANISOU 4296  CG  PRO B 191     3046   2599   6701    466  -1039    393       C
ATOM   4297  CD  PRO B 191    -113.816  46.553  23.501  1.00 31.49           C
ANISOU 4297  CD  PRO B 191     3166   2361   6436    422   -991    534       C
ATOM   4298  N   GLU B 192    -114.949  46.007  27.939  1.00 44.89           N
ANISOU 4298  N   GLU B 192     5540   3641   7873    607  -1879    537       N
ATOM   4299  CA  GLU B 192    -114.270  45.934  29.225  1.00 47.10           C
ANISOU 4299  CA  GLU B 192     5988   3878   8029    439  -1924    619       C
ATOM   4300  C   GLU B 192    -113.096  44.970  29.119  1.00 45.41           C
ANISOU 4300  C   GLU B 192     5366   3906   7981    334  -1692    575       C
ATOM   4301  O   GLU B 192    -113.251  43.837  28.657  1.00 50.70           O
ANISOU 4301  O   GLU B 192     5675   4733   8856    470  -1694    402       O
ATOM   4302  CB  GLU B 192    -115.245  45.473  30.308  1.00 59.21           C
ANISOU 4302  CB  GLU B 192     7782   5222   9493    653  -2366    539       C
ATOM   4303  CG  GLU B 192    -115.027  46.104  31.672  1.00 71.91           C
ANISOU 4303  CG  GLU B 192     9904   6615  10802    434  -2478    683       C
ATOM   4304  CD  GLU B 192    -115.829  47.378  31.860  1.00 83.26           C
ANISOU 4304  CD  GLU B 192    11886   7879  11871    324  -2512    740       C
ATOM   4305  OE1 GLU B 192    -116.145  48.043  30.850  1.00 84.79           O
ANISOU 4305  OE1 GLU B 192    12046   8098  12070    332  -2364    749       O
ATOM   4306  OE2 GLU B 192    -116.152  47.710  33.020  1.00 88.96           O
ANISOU 4306  OE2 GLU B 192    13085   8436  12282    212  -2684    766       O
ATOM   4307  N   THR B 193    -111.917  45.420  29.538  1.00 41.54           N
ANISOU 4307  N   THR B 193     4944   3448   7390     76  -1482    697       N
ATOM   4308  CA  THR B 193    -110.698  44.672  29.276  1.00 41.29           C
ANISOU 4308  CA  THR B 193     4608   3600   7481    -28  -1242    676       C
ATOM   4309  C   THR B 193    -109.726  44.795  30.440  1.00 41.99           C
ANISOU 4309  C   THR B 193     4830   3670   7455   -227  -1195    744       C
ATOM   4310  O   THR B 193    -109.737  45.779  31.184  1.00 31.49           O
ANISOU 4310  O   THR B 193     3807   2226   5933   -366  -1228    818       O
ATOM   4311  CB  THR B 193    -110.011  45.156  27.989  1.00 40.50           C
ANISOU 4311  CB  THR B 193     4382   3588   7420    -92   -964    719       C
ATOM   4312  OG1 THR B 193    -108.789  44.436  27.793  1.00 44.49           O
ANISOU 4312  OG1 THR B 193     4711   4201   7992   -190   -771    706       O
ATOM   4313  CG2 THR B 193    -109.708  46.643  28.071  1.00 39.54           C
ANISOU 4313  CG2 THR B 193     4488   3403   7131   -227   -888    821       C
ATOM   4314  N   TYR B 194    -108.896  43.767  30.595  1.00 41.49           N
ANISOU 4314  N   TYR B 194     4552   3721   7493   -274  -1097    693       N
ATOM   4315  CA  TYR B 194    -107.688  43.847  31.397  1.00 38.95           C
ANISOU 4315  CA  TYR B 194     4293   3412   7094   -462   -972    741       C
ATOM   4316  C   TYR B 194    -106.555  44.412  30.545  1.00 35.70           C
ANISOU 4316  C   TYR B 194     3806   3064   6695   -530   -713    777       C
ATOM   4317  O   TYR B 194    -106.640  44.480  29.317  1.00 33.21           O
ANISOU 4317  O   TYR B 194     3384   2785   6450   -446   -627    774       O
ATOM   4318  CB  TYR B 194    -107.292  42.472  31.941  1.00 38.45           C
ANISOU 4318  CB  TYR B 194     4071   3421   7116   -484   -993    660       C
ATOM   4319  CG  TYR B 194    -108.252  41.866  32.943  1.00 41.73           C
ANISOU 4319  CG  TYR B 194     4550   3789   7516   -395  -1300    588       C
ATOM   4320  CD1 TYR B 194    -108.201  42.219  34.286  1.00 44.57           C
ANISOU 4320  CD1 TYR B 194     5204   4028   7703   -504  -1439    648       C
ATOM   4321  CD2 TYR B 194    -109.189  40.918  32.551  1.00 43.18           C
ANISOU 4321  CD2 TYR B 194     4501   4054   7850   -201  -1464    421       C
ATOM   4322  CE1 TYR B 194    -109.070  41.660  35.207  1.00 45.00           C
ANISOU 4322  CE1 TYR B 194     5380   4004   7715   -394  -1780    580       C
ATOM   4323  CE2 TYR B 194    -110.061  40.353  33.465  1.00 45.19           C
ANISOU 4323  CE2 TYR B 194     4799   4270   8101    -55  -1813    308       C
ATOM   4324  CZ  TYR B 194    -109.998  40.727  34.792  1.00 46.07           C
ANISOU 4324  CZ  TYR B 194     5264   4221   8019   -138  -1993    406       C
ATOM   4325  OH  TYR B 194    -110.865  40.168  35.705  1.00 49.14           O
ANISOU 4325  OH  TYR B 194     5759   4536   8375     34  -2398    295       O
ATOM   4326  N   PHE B 195    -105.476  44.813  31.209  1.00 35.33           N
ANISOU 4326  N   PHE B 195     3824   3026   6572   -667   -608    784       N
ATOM   4327  CA  PHE B 195    -104.292  45.301  30.520  1.00 34.78           C
ANISOU 4327  CA  PHE B 195     3685   3011   6520   -670   -430    767       C
ATOM   4328  C   PHE B 195    -103.058  44.588  31.047  1.00 38.67           C
ANISOU 4328  C   PHE B 195     4150   3512   7029   -727   -349    732       C
ATOM   4329  O   PHE B 195    -102.911  44.393  32.257  1.00 40.32           O
ANISOU 4329  O   PHE B 195     4429   3708   7182   -844   -382    714       O
ATOM   4330  CB  PHE B 195    -104.122  46.815  30.684  1.00 31.84           C
ANISOU 4330  CB  PHE B 195     3391   2668   6039   -755   -377    728       C
ATOM   4331  CG  PHE B 195    -105.163  47.621  29.965  1.00 32.24           C
ANISOU 4331  CG  PHE B 195     3495   2701   6055   -716   -420    758       C
ATOM   4332  CD1 PHE B 195    -105.268  47.566  28.585  1.00 30.99           C
ANISOU 4332  CD1 PHE B 195     3225   2564   5984   -565   -390    779       C
ATOM   4333  CD2 PHE B 195    -106.030  48.442  30.667  1.00 30.86           C
ANISOU 4333  CD2 PHE B 195     3542   2461   5724   -856   -487    762       C
ATOM   4334  CE1 PHE B 195    -106.224  48.309  27.919  1.00 32.43           C
ANISOU 4334  CE1 PHE B 195     3464   2728   6132   -534   -424    801       C
ATOM   4335  CE2 PHE B 195    -106.987  49.189  30.008  1.00 32.15           C
ANISOU 4335  CE2 PHE B 195     3803   2580   5833   -832   -526    788       C
ATOM   4336  CZ  PHE B 195    -107.084  49.123  28.631  1.00 35.39           C
ANISOU 4336  CZ  PHE B 195     4047   3036   6363   -660   -493    805       C
ATOM   4337  N   THR B 196    -102.180  44.192  30.131  1.00 39.12           N
ANISOU 4337  N   THR B 196     4164   3563   7139   -651   -254    722       N
ATOM   4338  CA  THR B 196    -100.890  43.658  30.534  1.00 35.12           C
ANISOU 4338  CA  THR B 196     3701   3021   6620   -684   -184    682       C
ATOM   4339  C   THR B 196    -100.028  44.771  31.119  1.00 32.12           C
ANISOU 4339  C   THR B 196     3329   2682   6194   -687   -156    586       C
ATOM   4340  O   THR B 196    -100.196  45.951  30.800  1.00 27.70           O
ANISOU 4340  O   THR B 196     2722   2189   5615   -651   -157    533       O
ATOM   4341  CB  THR B 196    -100.181  42.997  29.351  1.00 37.05           C
ANISOU 4341  CB  THR B 196     4016   3187   6876   -608   -116    694       C
ATOM   4342  OG1 THR B 196    -100.135  43.905  28.243  1.00 40.27           O
ANISOU 4342  OG1 THR B 196     4436   3589   7276   -467   -132    698       O
ATOM   4343  CG2 THR B 196    -100.914  41.737  28.931  1.00 28.27           C
ANISOU 4343  CG2 THR B 196     2864   2078   5798   -696    -79    710       C
ATOM   4344  N   GLN B 197     -99.103  44.385  31.994  1.00 32.07           N
ANISOU 4344  N   GLN B 197     3362   2655   6168   -750   -118    525       N
ATOM   4345  CA  GLN B 197     -98.301  45.359  32.721  1.00 32.18           C
ANISOU 4345  CA  GLN B 197     3338   2743   6147   -782    -70    364       C
ATOM   4346  C   GLN B 197     -97.047  45.789  31.972  1.00 36.96           C
ANISOU 4346  C   GLN B 197     3910   3342   6793   -561    -73    228       C
ATOM   4347  O   GLN B 197     -96.438  46.798  32.348  1.00 42.36           O
ANISOU 4347  O   GLN B 197     4474   4143   7477   -542    -43     15       O
ATOM   4348  CB  GLN B 197     -97.921  44.799  34.093  1.00 37.32           C
ANISOU 4348  CB  GLN B 197     4051   3377   6750   -954    -32    330       C
ATOM   4349  CG  GLN B 197     -99.124  44.474  34.965  1.00 36.87           C
ANISOU 4349  CG  GLN B 197     4073   3310   6624  -1143    -94    432       C
ATOM   4350  CD  GLN B 197     -99.990  45.689  35.236  1.00 44.78           C
ANISOU 4350  CD  GLN B 197     5122   4364   7528  -1261   -106    407       C
ATOM   4351  OE1 GLN B 197     -99.499  46.733  35.665  1.00 49.27           O
ANISOU 4351  OE1 GLN B 197     5670   5021   8028  -1379      3    245       O
ATOM   4352  NE2 GLN B 197    -101.287  45.561  34.979  1.00 46.83           N
ANISOU 4352  NE2 GLN B 197     5454   4570   7768  -1244   -232    532       N
ATOM   4353  N   SER B 198     -96.647  45.049  30.935  1.00 35.41           N
ANISOU 4353  N   SER B 198     3835   3006   6613   -402   -120    312       N
ATOM   4354  CA  SER B 198     -95.552  45.447  30.045  1.00 35.86           C
ANISOU 4354  CA  SER B 198     3955   2993   6675   -134   -204    200       C
ATOM   4355  C   SER B 198     -94.234  45.620  30.799  1.00 36.89           C
ANISOU 4355  C   SER B 198     4084   3117   6816    -34   -223    -10       C
ATOM   4356  O   SER B 198     -93.457  46.537  30.526  1.00 39.66           O
ANISOU 4356  O   SER B 198     4332   3534   7204    194   -314   -237       O
ATOM   4357  CB  SER B 198     -95.902  46.724  29.276  1.00 40.00           C
ANISOU 4357  CB  SER B 198     4324   3647   7226    -11   -260    114       C
ATOM   4358  OG  SER B 198     -97.077  46.548  28.504  1.00 43.82           O
ANISOU 4358  OG  SER B 198     4834   4115   7700    -79   -247    297       O
ATOM   4359  N   ARG B 199     -93.973  44.733  31.751  1.00 36.27           N
ANISOU 4359  N   ARG B 199     4097   2972   6710   -191   -151     28       N
ATOM   4360  CA  ARG B 199     -92.700  44.732  32.454  1.00 40.86           C
ANISOU 4360  CA  ARG B 199     4713   3515   7296    -95   -163   -169       C
ATOM   4361  C   ARG B 199     -91.710  43.810  31.750  1.00 45.21           C
ANISOU 4361  C   ARG B 199     5615   3780   7784     95   -262   -117       C
ATOM   4362  O   ARG B 199     -92.081  42.969  30.929  1.00 49.45           O
ANISOU 4362  O   ARG B 199     6380   4160   8249     37   -259     87       O
ATOM   4363  CB  ARG B 199     -92.887  44.304  33.910  1.00 40.56           C
ANISOU 4363  CB  ARG B 199     4636   3540   7234   -385    -31   -166       C
ATOM   4364  CG  ARG B 199     -93.543  45.365  34.776  1.00 44.85           C
ANISOU 4364  CG  ARG B 199     4946   4317   7776   -588     61   -287       C
ATOM   4365  CD  ARG B 199     -94.004  44.805  36.110  1.00 44.38           C
ANISOU 4365  CD  ARG B 199     4951   4268   7644   -906    153   -211       C
ATOM   4366  NE  ARG B 199     -95.164  43.932  35.962  1.00 43.24           N
ANISOU 4366  NE  ARG B 199     4904   4054   7472  -1026    108     55       N
ATOM   4367  CZ  ARG B 199     -95.903  43.493  36.975  1.00 45.31           C
ANISOU 4367  CZ  ARG B 199     5230   4324   7663  -1266    111    140       C
ATOM   4368  NH1 ARG B 199     -95.605  43.845  38.219  1.00 44.91           N
ANISOU 4368  NH1 ARG B 199     5208   4325   7531  -1464    188     16       N
ATOM   4369  NH2 ARG B 199     -96.942  42.701  36.746  1.00 44.47           N
ANISOU 4369  NH2 ARG B 199     5161   4176   7561  -1303     24    318       N
ATOM   4370  N   ASN B 200     -90.434  43.991  32.069  1.00 43.37           N
ANISOU 4370  N   ASN B 200     5451   3470   7558    312   -348   -335       N
ATOM   4371  CA  ASN B 200     -89.379  43.145  31.538  1.00 47.66           C
ANISOU 4371  CA  ASN B 200     6432   3680   7995    497   -470   -306       C
ATOM   4372  C   ASN B 200     -88.800  42.280  32.649  1.00 47.67           C
ANISOU 4372  C   ASN B 200     6569   3590   7955    331   -365   -324       C
ATOM   4373  O   ASN B 200     -88.969  42.557  33.840  1.00 46.35           O
ANISOU 4373  O   ASN B 200     6127   3628   7857    157   -239   -428       O
ATOM   4374  CB  ASN B 200     -88.274  43.977  30.876  1.00 56.19           C
ANISOU 4374  CB  ASN B 200     7578   4672   9098    973   -736   -563       C
ATOM   4375  CG  ASN B 200     -87.592  44.916  31.844  1.00 64.53           C
ANISOU 4375  CG  ASN B 200     8272   5956  10291   1123   -752   -944       C
ATOM   4376  OD1 ASN B 200     -86.676  44.523  32.564  1.00 67.87           O
ANISOU 4376  OD1 ASN B 200     8817   6270  10703   1186   -762  -1082       O
ATOM   4377  ND2 ASN B 200     -88.030  46.169  31.860  1.00 67.71           N
ANISOU 4377  ND2 ASN B 200     8230   6687  10812   1151   -734  -1149       N
ATOM   4378  N   LEU B 201     -88.108  41.216  32.237  1.00 45.26           N
ANISOU 4378  N   LEU B 201     6743   2952   7501    351   -410   -224       N
ATOM   4379  CA  LEU B 201     -87.646  40.222  33.198  1.00 52.07           C
ANISOU 4379  CA  LEU B 201     7785   3704   8294    134   -290   -207       C
ATOM   4380  C   LEU B 201     -86.508  40.761  34.054  1.00 60.75           C
ANISOU 4380  C   LEU B 201     8817   4807   9458    370   -368   -500       C
ATOM   4381  O   LEU B 201     -86.457  40.506  35.263  1.00 62.12           O
ANISOU 4381  O   LEU B 201     8857   5087   9657    152   -220   -557       O
ATOM   4382  CB  LEU B 201     -87.211  38.956  32.465  1.00 54.70           C
ANISOU 4382  CB  LEU B 201     8706   3666   8410     37   -290    -46       C
ATOM   4383  CG  LEU B 201     -87.283  37.699  33.323  1.00 56.80           C
ANISOU 4383  CG  LEU B 201     9093   3898   8592   -365    -82     40       C
ATOM   4384  CD1 LEU B 201     -88.683  37.579  33.891  1.00 56.85           C
ANISOU 4384  CD1 LEU B 201     8642   4244   8713   -690     86    139       C
ATOM   4385  CD2 LEU B 201     -86.916  36.471  32.512  1.00 59.23           C
ANISOU 4385  CD2 LEU B 201    10001   3857   8648   -548    -32    167       C
ATOM   4386  N   GLN B 202     -85.587  41.504  33.441  1.00 65.57           N
ANISOU 4386  N   GLN B 202     9513   5306  10093    827   -615   -720       N
ATOM   4387  CA  GLN B 202     -84.450  42.052  34.171  1.00 72.81           C
ANISOU 4387  CA  GLN B 202    10325   6244  11094   1115   -717  -1083       C
ATOM   4388  C   GLN B 202     -84.904  43.055  35.226  1.00 73.54           C
ANISOU 4388  C   GLN B 202     9798   6780  11362    961   -543  -1315       C
ATOM   4389  O   GLN B 202     -84.610  42.904  36.417  1.00 74.91           O
ANISOU 4389  O   GLN B 202     9865   7041  11556    782   -390  -1444       O
ATOM   4390  CB  GLN B 202     -83.476  42.702  33.188  1.00 83.74           C
ANISOU 4390  CB  GLN B 202    11890   7443  12484   1697  -1082  -1318       C
ATOM   4391  CG  GLN B 202     -82.519  43.700  33.818  1.00 96.98           C
ANISOU 4391  CG  GLN B 202    13215   9300  14332   2071  -1216  -1824       C
ATOM   4392  CD  GLN B 202     -81.963  44.680  32.805  1.00108.06           C
ANISOU 4392  CD  GLN B 202    14541  10753  15764   2592  -1560  -2070       C
ATOM   4393  OE1 GLN B 202     -81.227  45.604  33.153  1.00115.29           O
ANISOU 4393  OE1 GLN B 202    15078  11944  16784   2862  -1668  -2490       O
ATOM   4394  NE2 GLN B 202     -82.317  44.484  31.540  1.00107.94           N
ANISOU 4394  NE2 GLN B 202    14836  10604  15572   2609  -1677  -1761       N
ATOM   4395  N   GLU B 203     -85.632  44.088  34.804  1.00 73.47           N
ANISOU 4395  N   GLU B 203     9420   7045  11452    987   -548  -1376       N
ATOM   4396  CA  GLU B 203     -86.039  45.185  35.680  1.00 72.46           C
ANISOU 4396  CA  GLU B 203     8763   7325  11442    812   -377  -1641       C
ATOM   4397  C   GLU B 203     -87.466  45.020  36.184  1.00 60.16           C
ANISOU 4397  C   GLU B 203     7095   5928   9836    314   -139  -1353       C
ATOM   4398  O   GLU B 203     -88.227  45.989  36.240  1.00 62.07           O
ANISOU 4398  O   GLU B 203     7026   6439  10120    176    -54  -1435       O
ATOM   4399  CB  GLU B 203     -85.879  46.517  34.953  1.00 85.70           C
ANISOU 4399  CB  GLU B 203    10108   9215  13237   1138   -534  -1962       C
ATOM   4400  CG  GLU B 203     -84.479  46.768  34.414  1.00100.14           C
ANISOU 4400  CG  GLU B 203    12032  10892  15125   1722   -857  -2307       C
ATOM   4401  CD  GLU B 203     -84.450  47.850  33.352  1.00107.62           C
ANISOU 4401  CD  GLU B 203    12746  11982  16161   2088  -1094  -2535       C
ATOM   4402  OE1 GLU B 203     -84.361  47.509  32.153  1.00109.17           O
ANISOU 4402  OE1 GLU B 203    13319  11889  16273   2363  -1354  -2325       O
ATOM   4403  OE2 GLU B 203     -84.527  49.042  33.717  1.00110.90           O
ANISOU 4403  OE2 GLU B 203    12618  12809  16711   2064  -1007  -2942       O
ATOM   4404  N   PHE B 204     -87.860  43.806  36.561  1.00 44.12           N
ANISOU 4404  N   PHE B 204     5201   4851   6712   -209    660    -45       N
ATOM   4405  CA  PHE B 204     -89.218  43.583  37.035  1.00 38.92           C
ANISOU 4405  CA  PHE B 204     4711   4233   5843   -290    635     56       C
ATOM   4406  C   PHE B 204     -89.414  44.207  38.410  1.00 41.45           C
ANISOU 4406  C   PHE B 204     5137   4591   6021   -379    852     34       C
ATOM   4407  O   PHE B 204     -88.567  44.080  39.299  1.00 46.27           O
ANISOU 4407  O   PHE B 204     5796   5207   6576   -380   1001    -74       O
ATOM   4408  CB  PHE B 204     -89.532  42.089  37.094  1.00 39.65           C
ANISOU 4408  CB  PHE B 204     4955   4326   5784   -268    480     86       C
ATOM   4409  CG  PHE B 204     -90.976  41.786  37.383  1.00 42.21           C
ANISOU 4409  CG  PHE B 204     5416   4675   5947   -326    401    201       C
ATOM   4410  CD1 PHE B 204     -91.873  41.583  36.348  1.00 42.68           C
ANISOU 4410  CD1 PHE B 204     5436   4717   6063   -310    252    286       C
ATOM   4411  CD2 PHE B 204     -91.439  41.708  38.688  1.00 42.64           C
ANISOU 4411  CD2 PHE B 204     5647   4758   5795   -396    473    223       C
ATOM   4412  CE1 PHE B 204     -93.202  41.306  36.607  1.00 42.66           C
ANISOU 4412  CE1 PHE B 204     5538   4717   5953   -344    179    385       C
ATOM   4413  CE2 PHE B 204     -92.767  41.434  38.954  1.00 40.98           C
ANISOU 4413  CE2 PHE B 204     5558   4551   5462   -436    370    342       C
ATOM   4414  CZ  PHE B 204     -93.649  41.231  37.911  1.00 42.71           C
ANISOU 4414  CZ  PHE B 204     5707   4744   5778   -400    223    421       C
ATOM   4415  N   LYS B 205     -90.548  44.885  38.584  1.00 43.44           N
ANISOU 4415  N   LYS B 205     5443   4858   6204   -465    876    136       N
ATOM   4416  CA  LYS B 205     -90.879  45.543  39.840  1.00 50.92           C
ANISOU 4416  CA  LYS B 205     6520   5834   6992   -577   1077    144       C
ATOM   4417  C   LYS B 205     -92.351  45.288  40.152  1.00 46.05           C
ANISOU 4417  C   LYS B 205     6096   5213   6187   -642    965    294       C
ATOM   4418  O   LYS B 205     -93.220  45.572  39.306  1.00 41.21           O
ANISOU 4418  O   LYS B 205     5422   4569   5665   -637    846    386       O
ATOM   4419  CB  LYS B 205     -90.590  47.047  39.769  1.00 61.10           C
ANISOU 4419  CB  LYS B 205     7634   7125   8456   -633   1276    108       C
ATOM   4420  CG  LYS B 205     -89.119  47.377  39.536  1.00 69.35           C
ANISOU 4420  CG  LYS B 205     8460   8161   9727   -557   1390    -45       C
ATOM   4421  CD  LYS B 205     -88.899  48.854  39.257  1.00 75.95           C
ANISOU 4421  CD  LYS B 205     9063   8996  10797   -604   1540    -72       C
ATOM   4422  CE  LYS B 205     -87.440  49.136  38.926  1.00 80.69           C
ANISOU 4422  CE  LYS B 205     9411   9572  11676   -502   1611   -218       C
ATOM   4423  NZ  LYS B 205     -87.203  50.571  38.606  1.00 86.87           N
ANISOU 4423  NZ  LYS B 205     9924  10353  12729   -546   1732   -248       N
ATOM   4424  N   PRO B 206     -92.666  44.762  41.333  1.00 48.50           N
ANISOU 4424  N   PRO B 206     6644   5542   6242   -704    987    322       N
ATOM   4425  CA  PRO B 206     -94.062  44.453  41.658  1.00 48.68           C
ANISOU 4425  CA  PRO B 206     6848   5544   6104   -752    842    478       C
ATOM   4426  C   PRO B 206     -94.902  45.715  41.793  1.00 53.84           C
ANISOU 4426  C   PRO B 206     7523   6168   6766   -853    946    574       C
ATOM   4427  O   PRO B 206     -94.399  46.813  42.038  1.00 58.37           O
ANISOU 4427  O   PRO B 206     8024   6756   7397   -926   1174    518       O
ATOM   4428  CB  PRO B 206     -93.961  43.708  42.993  1.00 47.86           C
ANISOU 4428  CB  PRO B 206     7000   5469   5718   -811    850    470       C
ATOM   4429  CG  PRO B 206     -92.691  44.201  43.598  1.00 49.95           C
ANISOU 4429  CG  PRO B 206     7245   5768   5965   -848   1116    314       C
ATOM   4430  CD  PRO B 206     -91.754  44.440  42.445  1.00 49.74           C
ANISOU 4430  CD  PRO B 206     6925   5731   6242   -737   1140    209       C
ATOM   4431  N   ARG B 207     -96.216  45.538  41.626  1.00 52.80           N
ANISOU 4431  N   ARG B 207     7484   5983   6595   -857    777    718       N
ATOM   4432  CA  ARG B 207     -97.150  46.658  41.631  1.00 51.05           C
ANISOU 4432  CA  ARG B 207     7293   5704   6398   -949    838    824       C
ATOM   4433  C   ARG B 207     -98.361  46.399  42.522  1.00 50.10           C
ANISOU 4433  C   ARG B 207     7441   5530   6065  -1012    732    985       C
ATOM   4434  O   ARG B 207     -99.376  47.091  42.392  1.00 49.16           O
ANISOU 4434  O   ARG B 207     7367   5330   5981  -1064    712   1100       O
ATOM   4435  CB  ARG B 207     -97.599  46.987  40.205  1.00 48.91           C
ANISOU 4435  CB  ARG B 207     6827   5384   6374   -882    734    836       C
ATOM   4436  CG  ARG B 207     -96.469  47.482  39.316  1.00 50.36           C
ANISOU 4436  CG  ARG B 207     6756   5605   6772   -843    821    703       C
ATOM   4437  CD  ARG B 207     -96.912  47.676  37.878  1.00 51.68           C
ANISOU 4437  CD  ARG B 207     6772   5725   7140   -789    686    714       C
ATOM   4438  NE  ARG B 207     -95.814  48.164  37.048  1.00 53.23           N
ANISOU 4438  NE  ARG B 207     6741   5952   7533   -758    732    603       N
ATOM   4439  CZ  ARG B 207     -95.893  48.356  35.735  1.00 50.31           C
ANISOU 4439  CZ  ARG B 207     6235   5552   7330   -720    616    588       C
ATOM   4440  NH1 ARG B 207     -97.023  48.100  35.091  1.00 47.54           N
ANISOU 4440  NH1 ARG B 207     5949   5141   6974   -708    480    658       N
ATOM   4441  NH2 ARG B 207     -94.839  48.803  35.066  1.00 50.59           N
ANISOU 4441  NH2 ARG B 207     6074   5610   7537   -696    631    501       N
ATOM   4442  N   SER B 208     -98.276  45.424  43.423  1.00 49.05           N
ANISOU 4442  N   SER B 208     7493   5427   5716  -1013    647   1000       N
ATOM   4443  CA  SER B 208     -99.346  45.170  44.376  1.00 47.05           C
ANISOU 4443  CA  SER B 208     7513   5119   5244  -1080    519   1163       C
ATOM   4444  C   SER B 208     -98.769  44.416  45.563  1.00 48.10           C
ANISOU 4444  C   SER B 208     7860   5316   5101  -1135    520   1128       C
ATOM   4445  O   SER B 208     -97.717  43.779  45.465  1.00 48.77           O
ANISOU 4445  O   SER B 208     7860   5470   5202  -1080    551    982       O
ATOM   4446  CB  SER B 208    -100.495  44.378  43.745  1.00 45.44           C
ANISOU 4446  CB  SER B 208     7277   4838   5151   -965    225   1271       C
ATOM   4447  OG  SER B 208    -100.135  43.021  43.552  1.00 44.63           O
ANISOU 4447  OG  SER B 208     7115   4782   5059   -860     56   1209       O
ATOM   4448  N   GLN B 209     -99.478  44.500  46.693  1.00 49.34           N
ANISOU 4448  N   GLN B 209     8316   5436   4995  -1252    475   1266       N
ATOM   4449  CA  GLN B 209     -99.052  43.775  47.886  1.00 50.68           C
ANISOU 4449  CA  GLN B 209     8742   5658   4858  -1328    446   1246       C
ATOM   4450  C   GLN B 209     -98.998  42.276  47.626  1.00 50.19           C
ANISOU 4450  C   GLN B 209     8621   5615   4833  -1202    163   1216       C
ATOM   4451  O   GLN B 209     -98.114  41.579  48.138  1.00 49.79           O
ANISOU 4451  O   GLN B 209     8644   5630   4643  -1220    181   1099       O
ATOM   4452  CB  GLN B 209     -99.989  44.087  49.053  1.00 55.61           C
ANISOU 4452  CB  GLN B 209     9722   6221   5187  -1479    387   1435       C
ATOM   4453  CG  GLN B 209     -99.703  43.282  50.313  1.00 63.01           C
ANISOU 4453  CG  GLN B 209    10972   7203   5768  -1574    302   1435       C
ATOM   4454  CD  GLN B 209     -98.291  43.485  50.827  1.00 70.17           C
ANISOU 4454  CD  GLN B 209    11915   8208   6537  -1657    619   1224       C
ATOM   4455  OE1 GLN B 209     -97.737  44.581  50.742  1.00 70.93           O
ANISOU 4455  OE1 GLN B 209    11925   8328   6698  -1721    954   1136       O
ATOM   4456  NE2 GLN B 209     -97.698  42.423  51.362  1.00 74.72           N
ANISOU 4456  NE2 GLN B 209    12610   8836   6943  -1655    515   1134       N
ATOM   4457  N   MET B 210     -99.934  41.763  46.825  1.00 46.65           N
ANISOU 4457  N   MET B 210     8037   5104   4583  -1080    -88   1311       N
ATOM   4458  CA  MET B 210     -99.889  40.356  46.446  1.00 45.45           C
ANISOU 4458  CA  MET B 210     7779   4972   4517   -963   -334   1274       C
ATOM   4459  C   MET B 210     -98.626  40.043  45.654  1.00 51.11           C
ANISOU 4459  C   MET B 210     8269   5761   5390   -889   -207   1076       C
ATOM   4460  O   MET B 210     -97.979  39.015  45.884  1.00 49.21           O
ANISOU 4460  O   MET B 210     8043   5566   5086   -872   -292    989       O
ATOM   4461  CB  MET B 210    -101.134  39.993  45.639  1.00 45.76           C
ANISOU 4461  CB  MET B 210     7682   4925   4782   -844   -570   1394       C
ATOM   4462  CG  MET B 210    -101.157  38.558  45.149  1.00 48.27           C
ANISOU 4462  CG  MET B 210     7849   5261   5231   -728   -802   1353       C
ATOM   4463  SD  MET B 210    -102.599  38.204  44.129  1.00 54.70           S
ANISOU 4463  SD  MET B 210     8468   5967   6348   -582  -1015   1460       S
ATOM   4464  CE  MET B 210    -103.928  38.502  45.292  1.00 56.48           C
ANISOU 4464  CE  MET B 210     8972   6080   6408   -643  -1211   1693       C
ATOM   4465  N   GLU B 211     -98.254  40.924  44.721  1.00 46.63           N
ANISOU 4465  N   GLU B 211     7497   5193   5028   -853    -19   1008       N
ATOM   4466  CA  GLU B 211     -97.027  40.713  43.961  1.00 43.48           C
ANISOU 4466  CA  GLU B 211     6893   4845   4781   -783     88    836       C
ATOM   4467  C   GLU B 211     -95.798  40.844  44.852  1.00 48.82           C
ANISOU 4467  C   GLU B 211     7682   5579   5289   -860    289    703       C
ATOM   4468  O   GLU B 211     -94.805  40.134  44.655  1.00 52.19           O
ANISOU 4468  O   GLU B 211     8036   6035   5757   -808    291    571       O
ATOM   4469  CB  GLU B 211     -96.954  41.694  42.792  1.00 43.22           C
ANISOU 4469  CB  GLU B 211     6632   4792   5000   -737    212    808       C
ATOM   4470  CG  GLU B 211     -97.991  41.445  41.712  1.00 49.19           C
ANISOU 4470  CG  GLU B 211     7257   5488   5943   -649     35    891       C
ATOM   4471  CD  GLU B 211     -97.676  42.176  40.422  1.00 57.45           C
ANISOU 4471  CD  GLU B 211     8080   6524   7225   -603    129    828       C
ATOM   4472  OE1 GLU B 211     -96.849  43.111  40.451  1.00 60.31           O
ANISOU 4472  OE1 GLU B 211     8382   6913   7620   -649    324    752       O
ATOM   4473  OE2 GLU B 211     -98.253  41.809  39.377  1.00 60.62           O
ANISOU 4473  OE2 GLU B 211     8363   6888   7781   -526      5    848       O
ATOM   4474  N   ILE B 212     -95.844  41.748  45.833  1.00 49.04           N
ANISOU 4474  N   ILE B 212     7894   5612   5125   -990    473    729       N
ATOM   4475  CA  ILE B 212     -94.751  41.850  46.796  1.00 50.81           C
ANISOU 4475  CA  ILE B 212     8257   5885   5162  -1076    690    590       C
ATOM   4476  C   ILE B 212     -94.621  40.555  47.586  1.00 54.33           C
ANISOU 4476  C   ILE B 212     8911   6350   5381  -1098    509    572       C
ATOM   4477  O   ILE B 212     -93.513  40.055  47.814  1.00 54.72           O
ANISOU 4477  O   ILE B 212     8969   6429   5395  -1089    592    408       O
ATOM   4478  CB  ILE B 212     -94.966  43.061  47.723  1.00 48.18           C
ANISOU 4478  CB  ILE B 212     8107   5553   4644  -1236    937    635       C
ATOM   4479  CG1 ILE B 212     -94.900  44.364  46.923  1.00 49.95           C
ANISOU 4479  CG1 ILE B 212     8090   5763   5125  -1224   1136    621       C
ATOM   4480  CG2 ILE B 212     -93.941  43.065  48.847  1.00 50.52           C
ANISOU 4480  CG2 ILE B 212     8596   5898   4701  -1341   1172    486       C
ATOM   4481  CD1 ILE B 212     -95.143  45.604  47.757  1.00 52.59           C
ANISOU 4481  CD1 ILE B 212     8577   6095   5311  -1397   1397    667       C
ATOM   4482  N   ASP B 213     -95.754  39.986  48.004  1.00 54.54           N
ANISOU 4482  N   ASP B 213     9104   6350   5269  -1127    244    738       N
ATOM   4483  CA  ASP B 213     -95.727  38.731  48.747  1.00 53.54           C
ANISOU 4483  CA  ASP B 213     9166   6239   4938  -1159     23    735       C
ATOM   4484  C   ASP B 213     -95.195  37.592  47.885  1.00 54.61           C
ANISOU 4484  C   ASP B 213     9082   6385   5284  -1032   -125    636       C
ATOM   4485  O   ASP B 213     -94.370  36.792  48.340  1.00 59.87           O
ANISOU 4485  O   ASP B 213     9835   7076   5838  -1058   -144    514       O
ATOM   4486  CB  ASP B 213     -97.126  38.404  49.270  1.00 54.80           C
ANISOU 4486  CB  ASP B 213     9507   6354   4961  -1200   -267    953       C
ATOM   4487  CG  ASP B 213     -97.616  39.408  50.296  1.00 62.45           C
ANISOU 4487  CG  ASP B 213    10768   7302   5658  -1358   -141   1065       C
ATOM   4488  OD1 ASP B 213     -96.808  40.249  50.741  1.00 65.16           O
ANISOU 4488  OD1 ASP B 213    11194   7682   5884  -1455    189    954       O
ATOM   4489  OD2 ASP B 213     -98.812  39.359  50.656  1.00 65.02           O
ANISOU 4489  OD2 ASP B 213    11241   7567   5899  -1387   -366   1266       O
ATOM   4490  N   PHE B 214     -95.652  37.512  46.632  1.00 53.04           N
ANISOU 4490  N   PHE B 214     8612   6159   5382   -905   -221    683       N
ATOM   4491  CA  PHE B 214     -95.259  36.408  45.759  1.00 49.84           C
ANISOU 4491  CA  PHE B 214     8009   5758   5171   -801   -362    610       C
ATOM   4492  C   PHE B 214     -93.746  36.326  45.608  1.00 52.09           C
ANISOU 4492  C   PHE B 214     8234   6064   5494   -787   -176    414       C
ATOM   4493  O   PHE B 214     -93.172  35.231  45.607  1.00 53.74           O
ANISOU 4493  O   PHE B 214     8440   6276   5701   -773   -284    331       O
ATOM   4494  CB  PHE B 214     -95.922  36.563  44.390  1.00 45.57           C
ANISOU 4494  CB  PHE B 214     7207   5184   4924   -687   -422    674       C
ATOM   4495  CG  PHE B 214     -95.495  35.529  43.384  1.00 44.18           C
ANISOU 4495  CG  PHE B 214     6829   5010   4946   -597   -524    600       C
ATOM   4496  CD1 PHE B 214     -94.457  35.782  42.500  1.00 43.83           C
ANISOU 4496  CD1 PHE B 214     6624   4968   5061   -544   -372    480       C
ATOM   4497  CD2 PHE B 214     -96.139  34.306  43.317  1.00 43.29           C
ANISOU 4497  CD2 PHE B 214     6687   4891   4872   -571   -777    655       C
ATOM   4498  CE1 PHE B 214     -94.067  34.831  41.573  1.00 45.11           C
ANISOU 4498  CE1 PHE B 214     6632   5123   5384   -480   -463    426       C
ATOM   4499  CE2 PHE B 214     -95.755  33.354  42.392  1.00 40.50           C
ANISOU 4499  CE2 PHE B 214     6153   4539   4696   -511   -846    587       C
ATOM   4500  CZ  PHE B 214     -94.718  33.616  41.521  1.00 40.49           C
ANISOU 4500  CZ  PHE B 214     6026   4537   4821   -471   -685    476       C
ATOM   4501  N   LEU B 215     -93.085  37.477  45.476  1.00 55.45           N
ANISOU 4501  N   LEU B 215     8601   6493   5975   -790    100    337       N
ATOM   4502  CA  LEU B 215     -91.634  37.496  45.332  1.00 55.84           C
ANISOU 4502  CA  LEU B 215     8576   6541   6100   -759    282    150       C
ATOM   4503  C   LEU B 215     -90.934  37.206  46.653  1.00 62.96           C
ANISOU 4503  C   LEU B 215     9736   7458   6729   -861    382     35       C
ATOM   4504  O   LEU B 215     -89.887  36.551  46.671  1.00 66.08           O
ANISOU 4504  O   LEU B 215    10125   7835   7148   -834    408   -114       O
ATOM   4505  CB  LEU B 215     -91.183  38.847  44.781  1.00 52.73           C
ANISOU 4505  CB  LEU B 215     8007   6141   5887   -725    531    104       C
ATOM   4506  CG  LEU B 215     -91.758  39.227  43.416  1.00 46.51           C
ANISOU 4506  CG  LEU B 215     6977   5332   5360   -637    446    195       C
ATOM   4507  CD1 LEU B 215     -91.310  40.621  43.003  1.00 45.81           C
ANISOU 4507  CD1 LEU B 215     6730   5239   5436   -628    675    150       C
ATOM   4508  CD2 LEU B 215     -91.354  38.197  42.376  1.00 41.66           C
ANISOU 4508  CD2 LEU B 215     6213   4696   4921   -536    282    157       C
ATOM   4509  N   GLU B 216     -91.490  37.691  47.764  1.00 67.87           N
ANISOU 4509  N   GLU B 216    10606   8104   7079   -988    444    101       N
ATOM   4510  CA  GLU B 216     -90.853  37.481  49.059  1.00 74.52           C
ANISOU 4510  CA  GLU B 216    11735   8962   7619  -1109    561    -16       C
ATOM   4511  C   GLU B 216     -91.159  36.100  49.624  1.00 73.69           C
ANISOU 4511  C   GLU B 216    11820   8858   7320  -1159    260     16       C
ATOM   4512  O   GLU B 216     -90.264  35.430  50.152  1.00 75.23           O
ANISOU 4512  O   GLU B 216    12142   9047   7397  -1198    288   -140       O
ATOM   4513  CB  GLU B 216     -91.296  38.560  50.046  1.00 85.31           C
ANISOU 4513  CB  GLU B 216    13326  10351   8738  -1252    760     44       C
ATOM   4514  CG  GLU B 216     -90.152  39.313  50.710  1.00 97.41           C
ANISOU 4514  CG  GLU B 216    14935  11894  10182  -1321   1152   -155       C
ATOM   4515  CD  GLU B 216     -89.658  40.486  49.880  1.00106.62           C
ANISOU 4515  CD  GLU B 216    15792  13052  11667  -1236   1415   -217       C
ATOM   4516  OE1 GLU B 216     -88.941  40.263  48.880  1.00107.35           O
ANISOU 4516  OE1 GLU B 216    15608  13116  12064  -1088   1394   -306       O
ATOM   4517  OE2 GLU B 216     -89.997  41.637  50.228  1.00110.97           O
ANISOU 4517  OE2 GLU B 216    16380  13620  12163  -1327   1631   -170       O
ATOM   4518  N   LEU B 217     -92.408  35.655  49.517  1.00 72.59           N
ANISOU 4518  N   LEU B 217    11694   8719   7167  -1157    -35    208       N
ATOM   4519  CA  LEU B 217     -92.858  34.462  50.218  1.00 73.16           C
ANISOU 4519  CA  LEU B 217    11960   8796   7042  -1226   -344    264       C
ATOM   4520  C   LEU B 217     -92.507  33.192  49.449  1.00 74.67           C
ANISOU 4520  C   LEU B 217    11954   8973   7444  -1135   -545    202       C
ATOM   4521  O   LEU B 217     -92.277  33.203  48.238  1.00 73.29           O
ANISOU 4521  O   LEU B 217    11488   8781   7577  -1009   -506    177       O
ATOM   4522  CB  LEU B 217     -94.368  34.517  50.454  1.00 68.80           C
ANISOU 4522  CB  LEU B 217    11488   8232   6420  -1252   -592    503       C
ATOM   4523  CG  LEU B 217     -94.880  34.973  51.821  1.00 71.10           C
ANISOU 4523  CG  LEU B 217    12161   8529   6325  -1420   -596    601       C
ATOM   4524  CD1 LEU B 217     -93.874  35.866  52.534  1.00 73.13           C
ANISOU 4524  CD1 LEU B 217    12605   8812   6371  -1531   -205    443       C
ATOM   4525  CD2 LEU B 217     -96.206  35.692  51.649  1.00 70.56           C
ANISOU 4525  CD2 LEU B 217    12077   8422   6311  -1403   -684    826       C
ATOM   4526  N   ALA B 218     -92.470  32.085  50.183  1.00 76.05           N
ANISOU 4526  N   ALA B 218    12306   9152   7437  -1218   -767    179       N
ATOM   4527  CA  ALA B 218     -92.301  30.779  49.574  1.00 71.70           C
ANISOU 4527  CA  ALA B 218    11587   8586   7068  -1164   -993    142       C
ATOM   4528  C   ALA B 218     -93.617  30.320  48.955  1.00 70.18           C
ANISOU 4528  C   ALA B 218    11208   8393   7063  -1093  -1278    331       C
ATOM   4529  O   ALA B 218     -94.688  30.871  49.223  1.00 71.30           O
ANISOU 4529  O   ALA B 218    11410   8534   7146  -1100  -1354    495       O
ATOM   4530  CB  ALA B 218     -91.809  29.758  50.602  1.00 70.48           C
ANISOU 4530  CB  ALA B 218    11686   8433   6661  -1294  -1142     44       C
ATOM   4531  N   MET B 219     -93.521  29.293  48.110  1.00 66.86           N
ANISOU 4531  N   MET B 219    10559   7962   6884  -1027  -1423    303       N
ATOM   4532  CA  MET B 219     -94.684  28.842  47.352  1.00 65.22           C
ANISOU 4532  CA  MET B 219    10121   7747   6913   -943  -1641    448       C
ATOM   4533  C   MET B 219     -95.795  28.358  48.276  1.00 65.81           C
ANISOU 4533  C   MET B 219    10339   7824   6843  -1007  -1959    598       C
ATOM   4534  O   MET B 219     -96.952  28.776  48.148  1.00 67.15           O
ANISOU 4534  O   MET B 219    10455   7973   7087   -952  -2055    759       O
ATOM   4535  CB  MET B 219     -94.272  27.739  46.379  1.00 67.57           C
ANISOU 4535  CB  MET B 219    10174   8035   7466   -893  -1714    371       C
ATOM   4536  CG  MET B 219     -95.392  27.262  45.480  1.00 69.77           C
ANISOU 4536  CG  MET B 219    10184   8306   8019   -804  -1881    489       C
ATOM   4537  SD  MET B 219     -94.856  25.978  44.337  1.00 72.94           S
ANISOU 4537  SD  MET B 219    10318   8698   8699   -778  -1921    393       S
ATOM   4538  CE  MET B 219     -94.593  24.610  45.462  1.00 75.88           C
ANISOU 4538  CE  MET B 219    10836   9080   8916   -917  -2201    344       C
ATOM   4539  N   ASP B 220     -95.460  27.478  49.221  1.00 68.68           N
ANISOU 4539  N   ASP B 220    10893   8199   7001  -1125  -2143    548       N
ATOM   4540  CA  ASP B 220     -96.473  26.949  50.127  1.00 72.59           C
ANISOU 4540  CA  ASP B 220    11533   8692   7357  -1194  -2495    696       C
ATOM   4541  C   ASP B 220     -97.000  28.019  51.074  1.00 70.74           C
ANISOU 4541  C   ASP B 220    11599   8450   6829  -1262  -2452    816       C
ATOM   4542  O   ASP B 220     -98.164  27.961  51.485  1.00 69.01           O
ANISOU 4542  O   ASP B 220    11436   8204   6582  -1263  -2719   1003       O
ATOM   4543  CB  ASP B 220     -95.905  25.769  50.913  1.00 80.38           C
ANISOU 4543  CB  ASP B 220    12672   9693   8176  -1326  -2708    601       C
ATOM   4544  CG  ASP B 220     -95.432  24.646  50.010  1.00 86.18           C
ANISOU 4544  CG  ASP B 220    13117  10425   9204  -1282  -2765    495       C
ATOM   4545  OD1 ASP B 220     -96.095  24.390  48.982  1.00 86.61           O
ANISOU 4545  OD1 ASP B 220    12848  10471   9591  -1162  -2818    567       O
ATOM   4546  OD2 ASP B 220     -94.395  24.025  50.323  1.00 88.91           O
ANISOU 4546  OD2 ASP B 220    13568  10769   9444  -1375  -2741    336       O
ATOM   4547  N   GLU B 221     -96.170  29.000  51.431  1.00 72.11           N
ANISOU 4547  N   GLU B 221    11964   8640   6796  -1320  -2119    715       N
ATOM   4548  CA  GLU B 221     -96.651  30.077  52.289  1.00 75.79           C
ANISOU 4548  CA  GLU B 221    12716   9097   6983  -1404  -2033    827       C
ATOM   4549  C   GLU B 221     -97.565  31.024  51.522  1.00 70.02           C
ANISOU 4549  C   GLU B 221    11800   8331   6473  -1286  -1951    972       C
ATOM   4550  O   GLU B 221     -98.579  31.488  52.057  1.00 71.29           O
ANISOU 4550  O   GLU B 221    12119   8454   6513  -1322  -2080   1158       O
ATOM   4551  CB  GLU B 221     -95.469  30.835  52.889  1.00 85.93           C
ANISOU 4551  CB  GLU B 221    14235  10409   8005  -1508  -1665    654       C
ATOM   4552  CG  GLU B 221     -94.612  29.997  53.820  1.00100.47           C
ANISOU 4552  CG  GLU B 221    16334  12269   9569  -1648  -1732    503       C
ATOM   4553  CD  GLU B 221     -93.157  30.412  53.791  1.00108.57           C
ANISOU 4553  CD  GLU B 221    17391  13305  10558  -1664  -1339    255       C
ATOM   4554  OE1 GLU B 221     -92.292  29.580  54.135  1.00111.43           O
ANISOU 4554  OE1 GLU B 221    17850  13662  10827  -1726  -1371     89       O
ATOM   4555  OE2 GLU B 221     -92.879  31.569  53.410  1.00109.89           O
ANISOU 4555  OE2 GLU B 221    17472  13473  10809  -1610  -1003    223       O
ATOM   4556  N   PHE B 222     -97.231  31.309  50.262  1.00 63.73           N
ANISOU 4556  N   PHE B 222    10685   7534   5994  -1153  -1752    894       N
ATOM   4557  CA  PHE B 222     -98.026  32.249  49.477  1.00 61.21           C
ANISOU 4557  CA  PHE B 222    10198   7178   5883  -1052  -1655   1007       C
ATOM   4558  C   PHE B 222     -99.382  31.661  49.108  1.00 61.21           C
ANISOU 4558  C   PHE B 222    10044   7124   6088   -961  -1979   1178       C
ATOM   4559  O   PHE B 222    -100.402  32.358  49.164  1.00 61.84           O
ANISOU 4559  O   PHE B 222    10165   7146   6188   -937  -2022   1337       O
ATOM   4560  CB  PHE B 222     -97.253  32.656  48.222  1.00 57.91           C
ANISOU 4560  CB  PHE B 222     9500   6773   5731   -948  -1382    871       C
ATOM   4561  CG  PHE B 222     -97.992  33.619  47.336  1.00 58.21           C
ANISOU 4561  CG  PHE B 222     9365   6771   5982   -856  -1278    962       C
ATOM   4562  CD1 PHE B 222     -97.964  34.980  47.592  1.00 59.99           C
ANISOU 4562  CD1 PHE B 222     9701   6987   6104   -907  -1035    987       C
ATOM   4563  CD2 PHE B 222     -98.706  33.164  46.239  1.00 56.45           C
ANISOU 4563  CD2 PHE B 222     8869   6516   6065   -730  -1409   1012       C
ATOM   4564  CE1 PHE B 222     -98.639  35.868  46.775  1.00 58.35           C
ANISOU 4564  CE1 PHE B 222     9342   6735   6094   -836   -951   1064       C
ATOM   4565  CE2 PHE B 222     -99.384  34.046  45.420  1.00 54.81           C
ANISOU 4565  CE2 PHE B 222     8524   6261   6040   -654  -1311   1080       C
ATOM   4566  CZ  PHE B 222     -99.350  35.400  45.688  1.00 55.44           C
ANISOU 4566  CZ  PHE B 222     8722   6328   6014   -708  -1094   1108       C
ATOM   4567  N   ILE B 223     -99.414  30.381  48.731  1.00 60.08           N
ANISOU 4567  N   ILE B 223     9718   6991   6118   -911  -2201   1142       N
ATOM   4568  CA  ILE B 223    -100.658  29.767  48.277  1.00 59.86           C
ANISOU 4568  CA  ILE B 223     9484   6910   6350   -806  -2482   1277       C
ATOM   4569  C   ILE B 223    -101.663  29.670  49.420  1.00 65.80           C
ANISOU 4569  C   ILE B 223    10472   7613   6916   -867  -2795   1467       C
ATOM   4570  O   ILE B 223    -102.861  29.916  49.234  1.00 68.52           O
ANISOU 4570  O   ILE B 223    10742   7876   7415   -781  -2938   1627       O
ATOM   4571  CB  ILE B 223    -100.366  28.394  47.645  1.00 55.62           C
ANISOU 4571  CB  ILE B 223     8687   6402   6045   -761  -2620   1179       C
ATOM   4572  CG1 ILE B 223     -99.599  28.576  46.332  1.00 54.13           C
ANISOU 4572  CG1 ILE B 223     8257   6237   6074   -685  -2329   1034       C
ATOM   4573  CG2 ILE B 223    -101.651  27.614  47.415  1.00 55.74           C
ANISOU 4573  CG2 ILE B 223     8498   6364   6315   -670  -2937   1309       C
ATOM   4574  CD1 ILE B 223     -99.241  27.282  45.643  1.00 57.45           C
ANISOU 4574  CD1 ILE B 223     8438   6680   6711   -661  -2419    936       C
ATOM   4575  N   GLU B 224    -101.195  29.323  50.621  1.00 70.05           N
ANISOU 4575  N   GLU B 224    11315   8187   7115  -1018  -2914   1454       N
ATOM   4576  CA  GLU B 224    -102.094  29.290  51.769  1.00 74.80           C
ANISOU 4576  CA  GLU B 224    12195   8737   7487  -1099  -3226   1648       C
ATOM   4577  C   GLU B 224    -102.510  30.693  52.195  1.00 75.01           C
ANISOU 4577  C   GLU B 224    12468   8715   7316  -1148  -3050   1771       C
ATOM   4578  O   GLU B 224    -103.636  30.887  52.668  1.00 78.69           O
ANISOU 4578  O   GLU B 224    13058   9094   7746  -1144  -3292   1983       O
ATOM   4579  CB  GLU B 224    -101.435  28.553  52.936  1.00 79.96           C
ANISOU 4579  CB  GLU B 224    13145   9444   7794  -1273  -3394   1589       C
ATOM   4580  CG  GLU B 224    -102.297  28.482  54.189  1.00 89.50           C
ANISOU 4580  CG  GLU B 224    14690  10600   8714  -1383  -3750   1796       C
ATOM   4581  CD  GLU B 224    -101.622  27.741  55.325  1.00 98.34           C
ANISOU 4581  CD  GLU B 224    16080  11769   9513  -1559  -3869   1698       C
ATOM   4582  OE1 GLU B 224    -100.779  26.863  55.047  1.00100.84           O
ANISOU 4582  OE1 GLU B 224    16292  12146   9876  -1580  -3899   1535       O
ATOM   4583  OE2 GLU B 224    -101.934  28.039  56.498  1.00103.12           O
ANISOU 4583  OE2 GLU B 224    16997  12346   9838  -1681  -3913   1771       O
ATOM   4584  N   ARG B 225    -101.626  31.678  52.026  1.00 72.36           N
ANISOU 4584  N   ARG B 225    12196   8424   6872  -1193  -2637   1645       N
ATOM   4585  CA  ARG B 225    -101.941  33.043  52.438  1.00 73.97           C
ANISOU 4585  CA  ARG B 225    12626   8587   6891  -1264  -2434   1747       C
ATOM   4586  C   ARG B 225    -103.116  33.600  51.645  1.00 72.58           C
ANISOU 4586  C   ARG B 225    12252   8312   7015  -1126  -2477   1899       C
ATOM   4587  O   ARG B 225    -104.086  34.106  52.220  1.00 76.79           O
ANISOU 4587  O   ARG B 225    12987   8754   7436  -1166  -2614   2100       O
ATOM   4588  CB  ARG B 225    -100.712  33.937  52.270  1.00 76.06           C
ANISOU 4588  CB  ARG B 225    12915   8922   7063  -1322  -1972   1557       C
ATOM   4589  CG  ARG B 225    -100.882  35.344  52.819  1.00 78.44           C
ANISOU 4589  CG  ARG B 225    13463   9195   7144  -1435  -1721   1637       C
ATOM   4590  CD  ARG B 225     -99.777  36.257  52.315  1.00 79.85           C
ANISOU 4590  CD  ARG B 225    13525   9432   7384  -1438  -1266   1445       C
ATOM   4591  NE  ARG B 225     -99.670  37.487  53.094  1.00 84.27           N
ANISOU 4591  NE  ARG B 225    14360   9989   7670  -1597   -988   1476       N
ATOM   4592  CZ  ARG B 225     -98.803  37.666  54.085  1.00 89.04           C
ANISOU 4592  CZ  ARG B 225    15249  10651   7933  -1760   -786   1363       C
ATOM   4593  NH1 ARG B 225     -97.966  36.693  54.419  1.00 85.96           N
ANISOU 4593  NH1 ARG B 225    14913  10316   7433  -1782   -850   1209       N
ATOM   4594  NH2 ARG B 225     -98.771  38.818  54.742  1.00 95.99           N
ANISOU 4594  NH2 ARG B 225    16363  11527   8584  -1912   -505   1394       N
ATOM   4595  N   TYR B 226    -103.046  33.517  50.317  1.00 68.21           N
ANISOU 4595  N   TYR B 226    11321   7763   6835   -970  -2361   1804       N
ATOM   4596  CA  TYR B 226    -104.100  34.019  49.448  1.00 65.93           C
ANISOU 4596  CA  TYR B 226    10829   7374   6847   -836  -2373   1910       C
ATOM   4597  C   TYR B 226    -105.086  32.931  49.037  1.00 64.86           C
ANISOU 4597  C   TYR B 226    10465   7174   7005   -695  -2722   1992       C
ATOM   4598  O   TYR B 226    -105.794  33.093  48.037  1.00 61.44           O
ANISOU 4598  O   TYR B 226     9779   6670   6896   -554  -2700   2012       O
ATOM   4599  CB  TYR B 226    -103.492  34.695  48.219  1.00 60.86           C
ANISOU 4599  CB  TYR B 226     9936   6766   6421   -764  -2024   1759       C
ATOM   4600  CG  TYR B 226    -102.795  35.998  48.542  1.00 58.85           C
ANISOU 4600  CG  TYR B 226     9858   6544   5958   -881  -1680   1710       C
ATOM   4601  CD1 TYR B 226    -103.508  37.187  48.625  1.00 57.85           C
ANISOU 4601  CD1 TYR B 226     9837   6335   5810   -914  -1578   1836       C
ATOM   4602  CD2 TYR B 226    -101.427  36.039  48.775  1.00 56.68           C
ANISOU 4602  CD2 TYR B 226     9636   6372   5527   -961  -1452   1532       C
ATOM   4603  CE1 TYR B 226    -102.878  38.379  48.925  1.00 59.31           C
ANISOU 4603  CE1 TYR B 226    10156   6552   5827  -1034  -1251   1787       C
ATOM   4604  CE2 TYR B 226    -100.788  37.227  49.076  1.00 55.50           C
ANISOU 4604  CE2 TYR B 226     9613   6250   5223  -1063  -1123   1474       C
ATOM   4605  CZ  TYR B 226    -101.518  38.393  49.150  1.00 58.43           C
ANISOU 4605  CZ  TYR B 226    10070   6552   5580  -1105  -1020   1603       C
ATOM   4606  OH  TYR B 226    -100.885  39.578  49.450  1.00 61.84           O
ANISOU 4606  OH  TYR B 226    10602   7013   5880  -1218   -679   1541       O
ATOM   4607  N   LYS B 227    -105.149  31.838  49.797  1.00 70.61           N
ANISOU 4607  N   LYS B 227    11276   7922   7632   -737  -3041   2030       N
ATOM   4608  CA  LYS B 227    -106.169  30.797  49.657  1.00 76.50           C
ANISOU 4608  CA  LYS B 227    11826   8597   8643   -621  -3422   2133       C
ATOM   4609  C   LYS B 227    -106.273  30.305  48.212  1.00 73.12           C
ANISOU 4609  C   LYS B 227    10959   8173   8652   -454  -3328   2013       C
ATOM   4610  O   LYS B 227    -107.325  30.372  47.573  1.00 75.00           O
ANISOU 4610  O   LYS B 227    10997   8306   9192   -313  -3400   2091       O
ATOM   4611  CB  LYS B 227    -107.527  31.295  50.164  1.00 84.37           C
ANISOU 4611  CB  LYS B 227    12969   9442   9645   -587  -3652   2378       C
ATOM   4612  CG  LYS B 227    -107.455  32.233  51.366  1.00 92.28           C
ANISOU 4612  CG  LYS B 227    14406  10433  10224   -761  -3579   2475       C
ATOM   4613  CD  LYS B 227    -107.679  33.681  50.941  1.00 96.42           C
ANISOU 4613  CD  LYS B 227    15007  10884  10744   -761  -3293   2537       C
ATOM   4614  CE  LYS B 227    -107.273  34.661  52.029  1.00100.45           C
ANISOU 4614  CE  LYS B 227    15929  11419  10816   -967  -3110   2579       C
ATOM   4615  NZ  LYS B 227    -107.242  36.063  51.522  1.00 98.67           N
ANISOU 4615  NZ  LYS B 227    15726  11153  10610   -988  -2759   2584       N
ATOM   4616  N   LEU B 228    -105.151  29.796  47.702  1.00 65.75           N
ANISOU 4616  N   LEU B 228     9891   7352   7740   -478  -3156   1818       N
ATOM   4617  CA  LEU B 228    -105.054  29.362  46.314  1.00 60.70           C
ANISOU 4617  CA  LEU B 228     8880   6729   7455   -357  -3019   1690       C
ATOM   4618  C   LEU B 228    -104.936  27.848  46.175  1.00 64.30           C
ANISOU 4618  C   LEU B 228     9120   7229   8083   -340  -3236   1623       C
ATOM   4619  O   LEU B 228    -104.418  27.363  45.164  1.00 67.48           O
ANISOU 4619  O   LEU B 228     9277   7680   8683   -300  -3080   1480       O
ATOM   4620  CB  LEU B 228    -103.874  30.050  45.628  1.00 53.53           C
ANISOU 4620  CB  LEU B 228     7961   5896   6482   -391  -2632   1526       C
ATOM   4621  CG  LEU B 228    -104.081  31.512  45.232  1.00 51.33           C
ANISOU 4621  CG  LEU B 228     7743   5570   6190   -370  -2375   1559       C
ATOM   4622  CD1 LEU B 228    -102.769  32.141  44.798  1.00 46.82           C
ANISOU 4622  CD1 LEU B 228     7186   5080   5524   -425  -2041   1401       C
ATOM   4623  CD2 LEU B 228    -105.112  31.613  44.122  1.00 52.90           C
ANISOU 4623  CD2 LEU B 228     7684   5680   6734   -223  -2370   1592       C
ATOM   4624  N   GLU B 229    -105.403  27.091  47.165  1.00 62.70           N
ANISOU 4624  N   GLU B 229     9009   7006   7807   -382  -3600   1729       N
ATOM   4625  CA  GLU B 229    -105.371  25.639  47.065  1.00 63.98           C
ANISOU 4625  CA  GLU B 229     8942   7204   8162   -376  -3832   1673       C
ATOM   4626  C   GLU B 229    -106.295  25.163  45.951  1.00 62.10           C
ANISOU 4626  C   GLU B 229     8299   6905   8390   -207  -3854   1671       C
ATOM   4627  O   GLU B 229    -107.407  25.671  45.782  1.00 64.72           O
ANISOU 4627  O   GLU B 229     8576   7129   8887    -90  -3910   1791       O
ATOM   4628  CB  GLU B 229    -105.779  24.995  48.391  1.00 73.05           C
ANISOU 4628  CB  GLU B 229    10279   8334   9144   -459  -4260   1804       C
ATOM   4629  CG  GLU B 229    -104.800  25.215  49.534  1.00 81.78           C
ANISOU 4629  CG  GLU B 229    11792   9508   9772   -652  -4252   1774       C
ATOM   4630  CD  GLU B 229    -105.048  26.512  50.281  1.00 91.64           C
ANISOU 4630  CD  GLU B 229    13407  10710  10702   -708  -4169   1902       C
ATOM   4631  OE1 GLU B 229    -105.853  27.337  49.799  1.00 93.15           O
ANISOU 4631  OE1 GLU B 229    13530  10817  11046   -597  -4074   2000       O
ATOM   4632  OE2 GLU B 229    -104.440  26.703  51.355  1.00 96.69           O
ANISOU 4632  OE2 GLU B 229    14413  11391  10932   -874  -4188   1901       O
ATOM   4633  N   GLY B 230    -105.825  24.182  45.185  1.00 59.20           N
ANISOU 4633  N   GLY B 230     7655   6599   8237   -202  -3793   1527       N
ATOM   4634  CA  GLY B 230    -106.605  23.634  44.097  1.00 58.21           C
ANISOU 4634  CA  GLY B 230     7139   6430   8549    -63  -3770   1494       C
ATOM   4635  C   GLY B 230    -106.620  24.459  42.833  1.00 57.27           C
ANISOU 4635  C   GLY B 230     6913   6289   8557     23  -3397   1417       C
ATOM   4636  O   GLY B 230    -107.449  24.198  41.953  1.00 60.18           O
ANISOU 4636  O   GLY B 230     6996   6598   9271    147  -3356   1399       O
ATOM   4637  N   TYR B 231    -105.734  25.447  42.707  1.00 54.22           N
ANISOU 4637  N   TYR B 231     6744   5946   7911    -42  -3125   1363       N
ATOM   4638  CA  TYR B 231    -105.681  26.285  41.516  1.00 53.25           C
ANISOU 4638  CA  TYR B 231     6542   5806   7885     22  -2794   1292       C
ATOM   4639  C   TYR B 231    -104.386  26.115  40.731  1.00 49.75           C
ANISOU 4639  C   TYR B 231     6059   5455   7388    -49  -2537   1128       C
ATOM   4640  O   TYR B 231    -104.134  26.890  39.800  1.00 50.26           O
ANISOU 4640  O   TYR B 231     6107   5517   7474    -22  -2271   1067       O
ATOM   4641  CB  TYR B 231    -105.893  27.754  41.891  1.00 54.45           C
ANISOU 4641  CB  TYR B 231     6947   5904   7837     22  -2694   1384       C
ATOM   4642  CG  TYR B 231    -107.329  28.060  42.247  1.00 55.38           C
ANISOU 4642  CG  TYR B 231     7064   5890   8087    123  -2888   1544       C
ATOM   4643  CD1 TYR B 231    -108.289  28.209  41.255  1.00 56.40           C
ANISOU 4643  CD1 TYR B 231     6972   5925   8535    260  -2808   1535       C
ATOM   4644  CD2 TYR B 231    -107.728  28.188  43.571  1.00 57.94           C
ANISOU 4644  CD2 TYR B 231     7625   6173   8217     77  -3155   1704       C
ATOM   4645  CE1 TYR B 231    -109.606  28.483  41.570  1.00 59.36           C
ANISOU 4645  CE1 TYR B 231     7343   6153   9059    365  -2989   1678       C
ATOM   4646  CE2 TYR B 231    -109.045  28.463  43.896  1.00 60.92           C
ANISOU 4646  CE2 TYR B 231     8014   6406   8726    173  -3357   1868       C
ATOM   4647  CZ  TYR B 231    -109.980  28.609  42.891  1.00 59.69           C
ANISOU 4647  CZ  TYR B 231     7617   6145   8918    325  -3274   1853       C
ATOM   4648  OH  TYR B 231    -111.292  28.882  43.205  1.00 57.94           O
ANISOU 4648  OH  TYR B 231     7405   5756   8854    434  -3476   2012       O
ATOM   4649  N   ALA B 232    -103.565  25.123  41.082  1.00 47.32           N
ANISOU 4649  N   ALA B 232     5746   5219   7014   -143  -2628   1059       N
ATOM   4650  CA  ALA B 232    -102.408  24.716  40.281  1.00 47.36           C
ANISOU 4650  CA  ALA B 232     5682   5288   7024   -204  -2426    911       C
ATOM   4651  C   ALA B 232    -101.424  25.863  40.064  1.00 45.35           C
ANISOU 4651  C   ALA B 232     5621   5056   6554   -238  -2165    859       C
ATOM   4652  O   ALA B 232    -100.813  25.987  39.001  1.00 45.44           O
ANISOU 4652  O   ALA B 232     5550   5082   6631   -235  -1948    767       O
ATOM   4653  CB  ALA B 232    -102.849  24.124  38.940  1.00 41.91           C
ANISOU 4653  CB  ALA B 232     4684   4583   6655   -140  -2310    844       C
ATOM   4654  N   PHE B 233    -101.262  26.712  41.080  1.00 47.45           N
ANISOU 4654  N   PHE B 233     6146   5320   6562   -275  -2189    920       N
ATOM   4655  CA  PHE B 233    -100.278  27.783  40.974  1.00 48.77           C
ANISOU 4655  CA  PHE B 233     6473   5510   6549   -310  -1942    861       C
ATOM   4656  C   PHE B 233     -98.857  27.240  40.990  1.00 48.57           C
ANISOU 4656  C   PHE B 233     6495   5535   6426   -393  -1868    731       C
ATOM   4657  O   PHE B 233     -97.961  27.842  40.387  1.00 46.23           O
ANISOU 4657  O   PHE B 233     6214   5247   6105   -393  -1648    651       O
ATOM   4658  CB  PHE B 233    -100.481  28.801  42.094  1.00 53.37           C
ANISOU 4658  CB  PHE B 233     7316   6077   6886   -347  -1959    952       C
ATOM   4659  CG  PHE B 233    -101.172  30.054  41.646  1.00 53.26           C
ANISOU 4659  CG  PHE B 233     7302   6010   6926   -282  -1823   1022       C
ATOM   4660  CD1 PHE B 233    -102.366  29.988  40.948  1.00 56.68           C
ANISOU 4660  CD1 PHE B 233     7557   6376   7602   -181  -1882   1086       C
ATOM   4661  CD2 PHE B 233    -100.630  31.298  41.921  1.00 51.07           C
ANISOU 4661  CD2 PHE B 233     7194   5741   6471   -328  -1626   1013       C
ATOM   4662  CE1 PHE B 233    -103.007  31.140  40.529  1.00 55.93           C
ANISOU 4662  CE1 PHE B 233     7476   6217   7557   -131  -1760   1141       C
ATOM   4663  CE2 PHE B 233    -101.266  32.454  41.507  1.00 51.29           C
ANISOU 4663  CE2 PHE B 233     7217   5714   6556   -286  -1507   1075       C
ATOM   4664  CZ  PHE B 233    -102.456  32.375  40.810  1.00 52.39           C
ANISOU 4664  CZ  PHE B 233     7202   5781   6924   -190  -1581   1140       C
ATOM   4665  N   GLU B 234     -98.635  26.103  41.657  1.00 52.64           N
ANISOU 4665  N   GLU B 234     7030   6072   6898   -463  -2063    708       N
ATOM   4666  CA  GLU B 234     -97.324  25.462  41.621  1.00 56.16           C
ANISOU 4666  CA  GLU B 234     7514   6544   7282   -543  -2005    578       C
ATOM   4667  C   GLU B 234     -96.906  25.133  40.195  1.00 52.12           C
ANISOU 4667  C   GLU B 234     6795   6025   6983   -511  -1848    503       C
ATOM   4668  O   GLU B 234     -95.708  25.055  39.899  1.00 55.81           O
ANISOU 4668  O   GLU B 234     7312   6490   7404   -552  -1721    403       O
ATOM   4669  CB  GLU B 234     -97.331  24.188  42.468  1.00 67.20           C
ANISOU 4669  CB  GLU B 234     8936   7958   8640   -632  -2270    569       C
ATOM   4670  CG  GLU B 234     -98.008  24.319  43.825  1.00 75.86           C
ANISOU 4670  CG  GLU B 234    10226   9056   9542   -670  -2498    673       C
ATOM   4671  CD  GLU B 234     -99.483  23.965  43.782  1.00 80.50           C
ANISOU 4671  CD  GLU B 234    10641   9616  10328   -596  -2726    808       C
ATOM   4672  OE1 GLU B 234    -100.067  23.969  42.678  1.00 80.63           O
ANISOU 4672  OE1 GLU B 234    10408   9612  10617   -496  -2637    818       O
ATOM   4673  OE2 GLU B 234    -100.056  23.676  44.854  1.00 84.20           O
ANISOU 4673  OE2 GLU B 234    11231  10078  10683   -639  -3000    901       O
ATOM   4674  N   HIS B 235     -97.875  24.937  39.304  1.00 46.72           N
ANISOU 4674  N   HIS B 235     5895   5327   6530   -440  -1851    548       N
ATOM   4675  CA  HIS B 235     -97.627  24.618  37.905  1.00 41.98           C
ANISOU 4675  CA  HIS B 235     5118   4720   6115   -424  -1696    486       C
ATOM   4676  C   HIS B 235     -97.774  25.831  36.995  1.00 42.38           C
ANISOU 4676  C   HIS B 235     5163   4749   6191   -351  -1490    499       C
ATOM   4677  O   HIS B 235     -96.877  26.123  36.200  1.00 43.37           O
ANISOU 4677  O   HIS B 235     5304   4869   6304   -367  -1329    436       O
ATOM   4678  CB  HIS B 235     -98.582  23.507  37.455  1.00 40.41           C
ANISOU 4678  CB  HIS B 235     4670   4518   6164   -411  -1807    502       C
ATOM   4679  CG  HIS B 235     -98.462  23.155  36.006  1.00 44.54           C
ANISOU 4679  CG  HIS B 235     5025   5035   6863   -412  -1628    440       C
ATOM   4680  ND1 HIS B 235     -97.464  22.339  35.519  1.00 47.21           N
ANISOU 4680  ND1 HIS B 235     5343   5380   7214   -506  -1569    359       N
ATOM   4681  CD2 HIS B 235     -99.215  23.508  34.937  1.00 45.80           C
ANISOU 4681  CD2 HIS B 235     5053   5172   7176   -344  -1489    445       C
ATOM   4682  CE1 HIS B 235     -97.608  22.203  34.212  1.00 47.74           C
ANISOU 4682  CE1 HIS B 235     5282   5436   7421   -503  -1402    328       C
ATOM   4683  NE2 HIS B 235     -98.662  22.903  33.835  1.00 45.93           N
ANISOU 4683  NE2 HIS B 235     4985   5193   7274   -406  -1346    371       N
ATOM   4684  N   ILE B 236     -98.890  26.553  37.109  1.00 46.18           N
ANISOU 4684  N   ILE B 236     5630   5207   6710   -277  -1511    583       N
ATOM   4685  CA  ILE B 236     -99.187  27.633  36.173  1.00 44.13           C
ANISOU 4685  CA  ILE B 236     5347   4918   6501   -217  -1333    591       C
ATOM   4686  C   ILE B 236     -98.202  28.783  36.345  1.00 42.64           C
ANISOU 4686  C   ILE B 236     5327   4739   6137   -238  -1198    568       C
ATOM   4687  O   ILE B 236     -97.610  29.266  35.373  1.00 39.28           O
ANISOU 4687  O   ILE B 236     4879   4306   5738   -236  -1046    518       O
ATOM   4688  CB  ILE B 236    -100.639  28.109  36.352  1.00 39.89           C
ANISOU 4688  CB  ILE B 236     4769   4333   6055   -136  -1401    686       C
ATOM   4689  CG1 ILE B 236    -101.615  26.963  36.079  1.00 38.21           C
ANISOU 4689  CG1 ILE B 236     4342   4100   6075    -95  -1521    693       C
ATOM   4690  CG2 ILE B 236    -100.925  29.291  35.442  1.00 37.55           C
ANISOU 4690  CG2 ILE B 236     4474   3999   5796    -90  -1221    685       C
ATOM   4691  CD1 ILE B 236    -103.045  27.282  36.454  1.00 39.74           C
ANISOU 4691  CD1 ILE B 236     4495   4224   6381     -2  -1639    794       C
ATOM   4692  N   VAL B 237     -98.016  29.242  37.576  1.00 42.51           N
ANISOU 4692  N   VAL B 237     5480   4734   5940   -265  -1252    602       N
ATOM   4693  CA  VAL B 237     -97.222  30.432  37.854  1.00 40.14           C
ANISOU 4693  CA  VAL B 237     5319   4438   5495   -283  -1104    579       C
ATOM   4694  C   VAL B 237     -95.787  30.079  38.218  1.00 43.83           C
ANISOU 4694  C   VAL B 237     5871   4928   5854   -339  -1061    480       C
ATOM   4695  O   VAL B 237     -94.843  30.669  37.692  1.00 45.38           O
ANISOU 4695  O   VAL B 237     6068   5116   6058   -332   -913    416       O
ATOM   4696  CB  VAL B 237     -97.893  31.272  38.963  1.00 39.10           C
ANISOU 4696  CB  VAL B 237     5339   4297   5221   -292  -1141    672       C
ATOM   4697  CG1 VAL B 237     -97.137  32.570  39.175  1.00 40.83           C
ANISOU 4697  CG1 VAL B 237     5668   4523   5323   -316   -950    640       C
ATOM   4698  CG2 VAL B 237     -99.344  31.547  38.605  1.00 38.80           C
ANISOU 4698  CG2 VAL B 237     5218   4209   5315   -227  -1202    772       C
ATOM   4699  N   TYR B 238     -95.602  29.116  39.123  1.00 42.89           N
ANISOU 4699  N   TYR B 238     5826   4826   5644   -395  -1202    462       N
ATOM   4700  CA  TYR B 238     -94.257  28.769  39.567  1.00 40.36           C
ANISOU 4700  CA  TYR B 238     5612   4508   5214   -453  -1161    355       C
ATOM   4701  C   TYR B 238     -93.513  27.913  38.550  1.00 41.62           C
ANISOU 4701  C   TYR B 238     5651   4646   5516   -459  -1141    281       C
ATOM   4702  O   TYR B 238     -92.294  28.054  38.405  1.00 40.48           O
ANISOU 4702  O   TYR B 238     5559   4474   5347   -469  -1036    194       O
ATOM   4703  CB  TYR B 238     -94.319  28.054  40.918  1.00 41.16           C
ANISOU 4703  CB  TYR B 238     5866   4628   5144   -530  -1329    355       C
ATOM   4704  CG  TYR B 238     -94.746  28.949  42.060  1.00 47.99           C
ANISOU 4704  CG  TYR B 238     6925   5507   5801   -556  -1325    417       C
ATOM   4705  CD1 TYR B 238     -93.809  29.666  42.791  1.00 50.99           C
ANISOU 4705  CD1 TYR B 238     7489   5891   5994   -601  -1166    338       C
ATOM   4706  CD2 TYR B 238     -96.084  29.079  42.405  1.00 50.20           C
ANISOU 4706  CD2 TYR B 238     7208   5786   6080   -538  -1469    553       C
ATOM   4707  CE1 TYR B 238     -94.193  30.486  43.836  1.00 50.64           C
ANISOU 4707  CE1 TYR B 238     7641   5861   5740   -648  -1134    394       C
ATOM   4708  CE2 TYR B 238     -96.479  29.897  43.447  1.00 52.56           C
ANISOU 4708  CE2 TYR B 238     7713   6086   6171   -579  -1467    626       C
ATOM   4709  CZ  TYR B 238     -95.529  30.595  44.160  1.00 54.28           C
ANISOU 4709  CZ  TYR B 238     8126   6320   6178   -644  -1291    547       C
ATOM   4710  OH  TYR B 238     -95.916  31.411  45.198  1.00 58.58           O
ANISOU 4710  OH  TYR B 238     8893   6866   6497   -707  -1262    619       O
ATOM   4711  N   GLY B 239     -94.211  27.034  37.847  1.00 44.40           N
ANISOU 4711  N   GLY B 239     5845   5001   6025   -455  -1230    314       N
ATOM   4712  CA  GLY B 239     -93.564  26.228  36.822  1.00 42.90           C
ANISOU 4712  CA  GLY B 239     5554   4786   5959   -482  -1193    256       C
ATOM   4713  C   GLY B 239     -92.973  24.947  37.374  1.00 43.39           C
ANISOU 4713  C   GLY B 239     5650   4842   5994   -571  -1314    196       C
ATOM   4714  O   GLY B 239     -92.526  24.868  38.518  1.00 44.89           O
ANISOU 4714  O   GLY B 239     5993   5034   6029   -614  -1379    158       O
ATOM   4715  N   ASP B 240     -92.969  23.918  36.530  1.00 42.12           N
ANISOU 4715  N   ASP B 240     5353   4668   5982   -614  -1333    179       N
ATOM   4716  CA  ASP B 240     -92.453  22.601  36.879  1.00 46.10           C
ANISOU 4716  CA  ASP B 240     5858   5157   6499   -717  -1448    122       C
ATOM   4717  C   ASP B 240     -91.179  22.343  36.085  1.00 43.79           C
ANISOU 4717  C   ASP B 240     5604   4798   6236   -759  -1337     55       C
ATOM   4718  O   ASP B 240     -91.197  22.368  34.849  1.00 40.28           O
ANISOU 4718  O   ASP B 240     5068   4336   5902   -749  -1232     75       O
ATOM   4719  CB  ASP B 240     -93.493  21.515  36.600  1.00 52.02           C
ANISOU 4719  CB  ASP B 240     6403   5939   7424   -752  -1565    158       C
ATOM   4720  CG  ASP B 240     -93.040  20.139  37.054  1.00 56.99           C
ANISOU 4720  CG  ASP B 240     7017   6556   8080   -876  -1707    101       C
ATOM   4721  OD1 ASP B 240     -92.047  20.048  37.806  1.00 60.41           O
ANISOU 4721  OD1 ASP B 240     7633   6958   8364   -932  -1744     36       O
ATOM   4722  OD2 ASP B 240     -93.679  19.144  36.653  1.00 59.67           O
ANISOU 4722  OD2 ASP B 240     7156   6913   8601   -923  -1774    112       O
ATOM   4723  N   PHE B 241     -90.081  22.089  36.795  1.00 45.57           N
ANISOU 4723  N   PHE B 241     5983   4975   6355   -810  -1363    -26       N
ATOM   4724  CA  PHE B 241     -88.785  21.837  36.182  1.00 44.79           C
ANISOU 4724  CA  PHE B 241     5947   4784   6288   -844  -1282    -88       C
ATOM   4725  C   PHE B 241     -88.289  20.420  36.432  1.00 48.49           C
ANISOU 4725  C   PHE B 241     6431   5207   6788   -975  -1391   -149       C
ATOM   4726  O   PHE B 241     -87.156  20.095  36.060  1.00 49.67           O
ANISOU 4726  O   PHE B 241     6658   5256   6958  -1016  -1344   -203       O
ATOM   4727  CB  PHE B 241     -87.754  22.844  36.694  1.00 43.56           C
ANISOU 4727  CB  PHE B 241     5957   4576   6017   -779  -1187   -151       C
ATOM   4728  CG  PHE B 241     -88.207  24.271  36.611  1.00 44.23           C
ANISOU 4728  CG  PHE B 241     6028   4707   6070   -668  -1084   -100       C
ATOM   4729  CD1 PHE B 241     -87.969  25.021  35.472  1.00 43.95           C
ANISOU 4729  CD1 PHE B 241     5932   4642   6125   -602   -973    -63       C
ATOM   4730  CD2 PHE B 241     -88.868  24.865  37.674  1.00 50.53           C
ANISOU 4730  CD2 PHE B 241     6887   5572   6741   -645  -1108    -83       C
ATOM   4731  CE1 PHE B 241     -88.384  26.337  35.393  1.00 44.54           C
ANISOU 4731  CE1 PHE B 241     5986   4756   6182   -516   -888    -21       C
ATOM   4732  CE2 PHE B 241     -89.287  26.180  37.601  1.00 50.51           C
ANISOU 4732  CE2 PHE B 241     6873   5603   6716   -562  -1006    -34       C
ATOM   4733  CZ  PHE B 241     -89.044  26.917  36.459  1.00 47.26           C
ANISOU 4733  CZ  PHE B 241     6380   5164   6414   -497   -895     -8       C
ATOM   4734  N   SER B 242     -89.107  19.570  37.055  1.00 50.08           N
ANISOU 4734  N   SER B 242     6555   5468   7006  -1044  -1549   -137       N
ATOM   4735  CA  SER B 242     -88.661  18.230  37.414  1.00 46.96           C
ANISOU 4735  CA  SER B 242     6171   5032   6640  -1186  -1675   -201       C
ATOM   4736  C   SER B 242     -88.506  17.319  36.204  1.00 45.71           C
ANISOU 4736  C   SER B 242     5874   4832   6662  -1271  -1620   -188       C
ATOM   4737  O   SER B 242     -87.758  16.339  36.276  1.00 49.23           O
ANISOU 4737  O   SER B 242     6366   5205   7136  -1396  -1672   -250       O
ATOM   4738  CB  SER B 242     -89.639  17.606  38.410  1.00 47.98           C
ANISOU 4738  CB  SER B 242     6237   5238   6754  -1238  -1892   -181       C
ATOM   4739  OG  SER B 242     -90.965  17.642  37.909  1.00 49.69           O
ANISOU 4739  OG  SER B 242     6233   5532   7114  -1182  -1910    -86       O
ATOM   4740  N   HIS B 243     -89.185  17.617  35.102  1.00 41.94           N
ANISOU 4740  N   HIS B 243     5247   4392   6296  -1220  -1508   -116       N
ATOM   4741  CA  HIS B 243     -89.174  16.774  33.917  1.00 41.01           C
ANISOU 4741  CA  HIS B 243     5005   4247   6331  -1316  -1427   -100       C
ATOM   4742  C   HIS B 243     -88.387  17.445  32.798  1.00 39.80           C
ANISOU 4742  C   HIS B 243     4952   4018   6151  -1280  -1259    -77       C
ATOM   4743  O   HIS B 243     -88.060  18.632  32.858  1.00 38.53           O
ANISOU 4743  O   HIS B 243     4900   3844   5894  -1160  -1205    -66       O
ATOM   4744  CB  HIS B 243     -90.604  16.469  33.457  1.00 51.62           C
ANISOU 4744  CB  HIS B 243     6100   5685   7830  -1306  -1418    -49       C
ATOM   4745  CG  HIS B 243     -91.420  15.732  34.473  1.00 67.72           C
ANISOU 4745  CG  HIS B 243     8008   7786   9936  -1340  -1619    -57       C
ATOM   4746  ND1 HIS B 243     -91.677  16.237  35.730  1.00 71.35           N
ANISOU 4746  ND1 HIS B 243     8562   8280  10266  -1272  -1773    -51       N
ATOM   4747  CD2 HIS B 243     -92.036  14.528  34.419  1.00 73.63           C
ANISOU 4747  CD2 HIS B 243     8538   8566  10872  -1442  -1701    -67       C
ATOM   4748  CE1 HIS B 243     -92.416  15.375  36.406  1.00 73.89           C
ANISOU 4748  CE1 HIS B 243     8743   8647  10683  -1328  -1970    -47       C
ATOM   4749  NE2 HIS B 243     -92.648  14.329  35.633  1.00 75.12           N
ANISOU 4749  NE2 HIS B 243     8689   8804  11051  -1425  -1934    -60       N
ATOM   4750  N   SER B 244     -88.084  16.655  31.764  1.00 38.88           N
ANISOU 4750  N   SER B 244     4798   3849   6124  -1396  -1183    -65       N
ATOM   4751  CA  SER B 244     -87.336  17.182  30.627  1.00 39.33           C
ANISOU 4751  CA  SER B 244     4969   3824   6150  -1384  -1054    -25       C
ATOM   4752  C   SER B 244     -88.111  18.291  29.931  1.00 41.43           C
ANISOU 4752  C   SER B 244     5184   4159   6398  -1267   -952     34       C
ATOM   4753  O   SER B 244     -87.527  19.291  29.498  1.00 40.30           O
ANISOU 4753  O   SER B 244     5160   3967   6185  -1186   -904     62       O
ATOM   4754  CB  SER B 244     -87.011  16.060  29.642  1.00 40.21           C
ANISOU 4754  CB  SER B 244     5064   3872   6344  -1558   -988    -10       C
ATOM   4755  OG  SER B 244     -88.166  15.673  28.916  1.00 44.48           O
ANISOU 4755  OG  SER B 244     5413   4504   6983  -1607   -891     17       O
ATOM   4756  N   GLN B 245     -89.426  18.133  29.816  1.00 42.57           N
ANISOU 4756  N   GLN B 245     5145   4407   6623  -1257   -926     49       N
ATOM   4757  CA  GLN B 245     -90.279  19.153  29.226  1.00 39.32           C
ANISOU 4757  CA  GLN B 245     4684   4053   6203  -1150   -832     92       C
ATOM   4758  C   GLN B 245     -90.762  20.090  30.326  1.00 37.24           C
ANISOU 4758  C   GLN B 245     4424   3844   5883  -1011   -918     94       C
ATOM   4759  O   GLN B 245     -91.364  19.645  31.310  1.00 39.69           O
ANISOU 4759  O   GLN B 245     4648   4204   6227  -1007  -1033     79       O
ATOM   4760  CB  GLN B 245     -91.459  18.519  28.493  1.00 42.86           C
ANISOU 4760  CB  GLN B 245     4937   4563   6786  -1204   -737     95       C
ATOM   4761  CG  GLN B 245     -92.212  19.479  27.582  1.00 50.82           C
ANISOU 4761  CG  GLN B 245     5929   5601   7778  -1126   -604    125       C
ATOM   4762  CD  GLN B 245     -91.397  19.909  26.372  1.00 56.51           C
ANISOU 4762  CD  GLN B 245     6820   6255   8396  -1176   -497    155       C
ATOM   4763  OE1 GLN B 245     -90.335  19.351  26.089  1.00 57.30           O
ANISOU 4763  OE1 GLN B 245     7033   6279   8459  -1278   -507    162       O
ATOM   4764  NE2 GLN B 245     -91.895  20.905  25.649  1.00 57.84           N
ANISOU 4764  NE2 GLN B 245     7018   6441   8518  -1110   -410    178       N
ATOM   4765  N   LEU B 246     -90.485  21.380  30.161  1.00 36.79           N
ANISOU 4765  N   LEU B 246     4469   3773   5737   -908   -871    118       N
ATOM   4766  CA  LEU B 246     -90.892  22.371  31.146  1.00 38.55           C
ANISOU 4766  CA  LEU B 246     4714   4041   5894   -793   -921    126       C
ATOM   4767  C   LEU B 246     -92.412  22.465  31.203  1.00 44.47           C
ANISOU 4767  C   LEU B 246     5312   4866   6718   -745   -926    159       C
ATOM   4768  O   LEU B 246     -93.090  22.459  30.172  1.00 48.58           O
ANISOU 4768  O   LEU B 246     5741   5398   7318   -749   -827    177       O
ATOM   4769  CB  LEU B 246     -90.282  23.730  30.801  1.00 36.16           C
ANISOU 4769  CB  LEU B 246     4520   3703   5516   -708   -851    142       C
ATOM   4770  CG  LEU B 246     -89.994  24.699  31.949  1.00 37.38           C
ANISOU 4770  CG  LEU B 246     4758   3867   5576   -622   -881    125       C
ATOM   4771  CD1 LEU B 246     -88.933  25.701  31.530  1.00 40.13           C
ANISOU 4771  CD1 LEU B 246     5197   4151   5899   -567   -816    118       C
ATOM   4772  CD2 LEU B 246     -91.252  25.424  32.396  1.00 34.18           C
ANISOU 4772  CD2 LEU B 246     4291   3536   5159   -552   -884    167       C
ATOM   4773  N   GLY B 247     -92.947  22.544  32.418  1.00 44.44           N
ANISOU 4773  N   GLY B 247     5298   4903   6685   -701  -1044    167       N
ATOM   4774  CA  GLY B 247     -94.382  22.564  32.641  1.00 42.73           C
ANISOU 4774  CA  GLY B 247     4942   4736   6558   -646  -1091    209       C
ATOM   4775  C   GLY B 247     -94.834  23.898  33.215  1.00 46.14           C
ANISOU 4775  C   GLY B 247     5455   5181   6896   -541  -1094    256       C
ATOM   4776  O   GLY B 247     -94.260  24.392  34.186  1.00 48.99           O
ANISOU 4776  O   GLY B 247     5958   5541   7115   -530  -1144    251       O
ATOM   4777  N   GLY B 248     -95.867  24.465  32.594  1.00 44.94           N
ANISOU 4777  N   GLY B 248     5216   5034   6826   -474  -1024    293       N
ATOM   4778  CA  GLY B 248     -96.466  25.686  33.110  1.00 44.66           C
ANISOU 4778  CA  GLY B 248     5244   5001   6725   -387  -1030    346       C
ATOM   4779  C   GLY B 248     -95.596  26.909  32.887  1.00 41.75           C
ANISOU 4779  C   GLY B 248     5013   4615   6236   -368   -922    338       C
ATOM   4780  O   GLY B 248     -95.010  27.100  31.815  1.00 37.89           O
ANISOU 4780  O   GLY B 248     4530   4104   5763   -388   -816    312       O
ATOM   4781  N   LEU B 249     -95.522  27.759  33.916  1.00 43.49           N
ANISOU 4781  N   LEU B 249     5345   4843   6337   -336   -952    365       N
ATOM   4782  CA  LEU B 249     -94.744  29.000  33.894  1.00 44.27           C
ANISOU 4782  CA  LEU B 249     5547   4929   6345   -315   -849    353       C
ATOM   4783  C   LEU B 249     -95.250  29.938  32.792  1.00 46.36           C
ANISOU 4783  C   LEU B 249     5760   5175   6679   -276   -746    378       C
ATOM   4784  O   LEU B 249     -94.597  30.173  31.773  1.00 43.33           O
ANISOU 4784  O   LEU B 249     5372   4770   6322   -289   -672    350       O
ATOM   4785  CB  LEU B 249     -93.249  28.699  33.727  1.00 42.52           C
ANISOU 4785  CB  LEU B 249     5386   4683   6088   -354   -815    283       C
ATOM   4786  CG  LEU B 249     -92.260  29.786  34.159  1.00 41.98           C
ANISOU 4786  CG  LEU B 249     5417   4598   5938   -328   -735    250       C
ATOM   4787  CD1 LEU B 249     -92.244  29.938  35.674  1.00 43.08           C
ANISOU 4787  CD1 LEU B 249     5667   4762   5940   -339   -767    239       C
ATOM   4788  CD2 LEU B 249     -90.869  29.477  33.631  1.00 40.59           C
ANISOU 4788  CD2 LEU B 249     5266   4367   5790   -344   -706    188       C
ATOM   4789  N   HIS B 250     -96.444  30.482  33.035  1.00 44.63           N
ANISOU 4789  N   HIS B 250     5519   4955   6484   -233   -759    435       N
ATOM   4790  CA  HIS B 250     -97.123  31.314  32.052  1.00 41.58           C
ANISOU 4790  CA  HIS B 250     5090   4541   6168   -203   -673    452       C
ATOM   4791  C   HIS B 250     -97.305  32.762  32.488  1.00 38.14           C
ANISOU 4791  C   HIS B 250     4727   4091   5672   -180   -627    492       C
ATOM   4792  O   HIS B 250     -97.844  33.559  31.712  1.00 32.57           O
ANISOU 4792  O   HIS B 250     4000   3355   5020   -166   -563    501       O
ATOM   4793  CB  HIS B 250     -98.492  30.713  31.706  1.00 40.25           C
ANISOU 4793  CB  HIS B 250     4812   4353   6129   -171   -703    472       C
ATOM   4794  CG  HIS B 250     -98.414  29.337  31.126  1.00 41.31           C
ANISOU 4794  CG  HIS B 250     4843   4500   6353   -207   -713    425       C
ATOM   4795  ND1 HIS B 250     -98.047  29.101  29.819  1.00 40.44           N
ANISOU 4795  ND1 HIS B 250     4706   4381   6276   -251   -606    374       N
ATOM   4796  CD2 HIS B 250     -98.648  28.122  31.677  1.00 40.74           C
ANISOU 4796  CD2 HIS B 250     4690   4446   6342   -220   -817    424       C
ATOM   4797  CE1 HIS B 250     -98.059  27.800  29.588  1.00 39.57           C
ANISOU 4797  CE1 HIS B 250     4504   4285   6246   -295   -619    341       C
ATOM   4798  NE2 HIS B 250     -98.421  27.184  30.699  1.00 41.76           N
ANISOU 4798  NE2 HIS B 250     4731   4581   6556   -274   -751    367       N
ATOM   4799  N   LEU B 251     -96.878  33.129  33.692  1.00 38.25           N
ANISOU 4799  N   LEU B 251     4835   4125   5572   -190   -647    508       N
ATOM   4800  CA  LEU B 251     -96.963  34.504  34.166  1.00 39.87           C
ANISOU 4800  CA  LEU B 251     5110   4321   5718   -191   -576    541       C
ATOM   4801  C   LEU B 251     -95.561  35.068  34.338  1.00 43.18           C
ANISOU 4801  C   LEU B 251     5567   4758   6081   -213   -489    480       C
ATOM   4802  O   LEU B 251     -94.696  34.418  34.935  1.00 49.28           O
ANISOU 4802  O   LEU B 251     6385   5550   6788   -229   -510    432       O
ATOM   4803  CB  LEU B 251     -97.736  34.593  35.482  1.00 40.85           C
ANISOU 4803  CB  LEU B 251     5329   4445   5748   -196   -645    617       C
ATOM   4804  CG  LEU B 251     -99.225  34.907  35.333  1.00 44.38           C
ANISOU 4804  CG  LEU B 251     5753   4837   6274   -160   -689    700       C
ATOM   4805  CD1 LEU B 251     -99.994  33.693  34.831  1.00 43.17           C
ANISOU 4805  CD1 LEU B 251     5484   4666   6252   -115   -792    700       C
ATOM   4806  CD2 LEU B 251     -99.800  35.420  36.643  1.00 51.87           C
ANISOU 4806  CD2 LEU B 251     6840   5768   7099   -181   -738    794       C
ATOM   4807  N   LEU B 252     -95.350  36.283  33.823  1.00 40.39           N
ANISOU 4807  N   LEU B 252     5186   4389   5770   -213   -397    476       N
ATOM   4808  CA  LEU B 252     -94.019  36.882  33.829  1.00 41.67           C
ANISOU 4808  CA  LEU B 252     5340   4557   5938   -217   -317    412       C
ATOM   4809  C   LEU B 252     -93.462  37.026  35.238  1.00 44.49           C
ANISOU 4809  C   LEU B 252     5789   4938   6178   -237   -259    384       C
ATOM   4810  O   LEU B 252     -92.247  36.915  35.438  1.00 47.33           O
ANISOU 4810  O   LEU B 252     6150   5294   6537   -229   -213    305       O
ATOM   4811  CB  LEU B 252     -94.057  38.243  33.136  1.00 38.31           C
ANISOU 4811  CB  LEU B 252     4851   4111   5595   -221   -246    422       C
ATOM   4812  CG  LEU B 252     -92.711  38.951  32.977  1.00 40.34           C
ANISOU 4812  CG  LEU B 252     5050   4362   5916   -212   -180    358       C
ATOM   4813  CD1 LEU B 252     -91.830  38.203  31.989  1.00 42.04           C
ANISOU 4813  CD1 LEU B 252     5227   4550   6196   -187   -256    321       C
ATOM   4814  CD2 LEU B 252     -92.908  40.390  32.544  1.00 41.44           C
ANISOU 4814  CD2 LEU B 252     5118   4488   6140   -233   -122    375       C
ATOM   4815  N   ILE B 253     -94.326  37.279  36.225  1.00 42.48           N
ANISOU 4815  N   ILE B 253     5627   4696   5816   -267   -257    445       N
ATOM   4816  CA  ILE B 253     -93.850  37.409  37.598  1.00 41.34           C
ANISOU 4816  CA  ILE B 253     5611   4577   5518   -310   -190    416       C
ATOM   4817  C   ILE B 253     -93.265  36.091  38.088  1.00 37.92           C
ANISOU 4817  C   ILE B 253     5242   4157   5007   -315   -277    361       C
ATOM   4818  O   ILE B 253     -92.322  36.079  38.887  1.00 36.99           O
ANISOU 4818  O   ILE B 253     5209   4049   4798   -340   -198    279       O
ATOM   4819  CB  ILE B 253     -94.986  37.917  38.511  1.00 40.82           C
ANISOU 4819  CB  ILE B 253     5666   4512   5331   -358   -195    517       C
ATOM   4820  CG1 ILE B 253     -94.457  38.211  39.916  1.00 47.22           C
ANISOU 4820  CG1 ILE B 253     6642   5351   5949   -428    -92    484       C
ATOM   4821  CG2 ILE B 253     -96.138  36.922  38.553  1.00 36.08           C
ANISOU 4821  CG2 ILE B 253     5091   3897   4719   -340   -385    603       C
ATOM   4822  CD1 ILE B 253     -95.490  38.813  40.843  1.00 50.06           C
ANISOU 4822  CD1 ILE B 253     7156   5702   6163   -498    -86    597       C
ATOM   4823  N   GLY B 254     -93.797  34.964  37.609  1.00 36.66           N
ANISOU 4823  N   GLY B 254     5040   3993   4895   -297   -428    392       N
ATOM   4824  CA  GLY B 254     -93.195  33.684  37.926  1.00 34.38           C
ANISOU 4824  CA  GLY B 254     4790   3711   4564   -315   -518    334       C
ATOM   4825  C   GLY B 254     -91.822  33.517  37.312  1.00 38.49           C
ANISOU 4825  C   GLY B 254     5258   4203   5164   -294   -453    233       C
ATOM   4826  O   GLY B 254     -90.943  32.891  37.910  1.00 44.37           O
ANISOU 4826  O   GLY B 254     6081   4937   5842   -318   -458    153       O
ATOM   4827  N   LEU B 255     -91.615  34.075  36.116  1.00 36.10           N
ANISOU 4827  N   LEU B 255     4839   3875   5003   -254   -405    237       N
ATOM   4828  CA  LEU B 255     -90.291  34.038  35.507  1.00 32.46           C
ANISOU 4828  CA  LEU B 255     4335   3369   4630   -227   -365    161       C
ATOM   4829  C   LEU B 255     -89.319  34.941  36.253  1.00 36.79           C
ANISOU 4829  C   LEU B 255     4916   3903   5158   -212   -227     83       C
ATOM   4830  O   LEU B 255     -88.146  34.593  36.424  1.00 39.11           O
ANISOU 4830  O   LEU B 255     5233   4152   5476   -194   -200     -8       O
ATOM   4831  CB  LEU B 255     -90.370  34.445  34.035  1.00 31.43           C
ANISOU 4831  CB  LEU B 255     4092   3213   4637   -200   -376    198       C
ATOM   4832  CG  LEU B 255     -90.896  33.460  32.988  1.00 35.72           C
ANISOU 4832  CG  LEU B 255     4596   3748   5227   -219   -470    238       C
ATOM   4833  CD1 LEU B 255     -92.407  33.320  33.054  1.00 34.35           C
ANISOU 4833  CD1 LEU B 255     4405   3613   5035   -230   -505    305       C
ATOM   4834  CD2 LEU B 255     -90.459  33.890  31.594  1.00 36.44           C
ANISOU 4834  CD2 LEU B 255     4630   3799   5419   -207   -469    248       C
ATOM   4835  N   ALA B 256     -89.790  36.108  36.702  1.00 38.73           N
ANISOU 4835  N   ALA B 256     5162   4181   5374   -221   -125    110       N
ATOM   4836  CA  ALA B 256     -88.919  37.031  37.420  1.00 40.60           C
ANISOU 4836  CA  ALA B 256     5409   4410   5608   -216     44     26       C
ATOM   4837  C   ALA B 256     -88.450  36.432  38.737  1.00 41.76           C
ANISOU 4837  C   ALA B 256     5717   4564   5586   -256     91    -56       C
ATOM   4838  O   ALA B 256     -87.311  36.659  39.162  1.00 46.35           O
ANISOU 4838  O   ALA B 256     6308   5110   6193   -235    217   -175       O
ATOM   4839  CB  ALA B 256     -89.642  38.357  37.656  1.00 42.72           C
ANISOU 4839  CB  ALA B 256     5652   4713   5868   -245    152     82       C
ATOM   4840  N   LYS B 257     -89.315  35.661  39.398  1.00 39.33           N
ANISOU 4840  N   LYS B 257     5539   4294   5111   -315    -16      0       N
ATOM   4841  CA  LYS B 257     -88.921  35.014  40.643  1.00 42.24           C
ANISOU 4841  CA  LYS B 257     6091   4669   5290   -373     -6    -76       C
ATOM   4842  C   LYS B 257     -87.852  33.957  40.397  1.00 46.17           C
ANISOU 4842  C   LYS B 257     6588   5109   5846   -350    -64   -177       C
ATOM   4843  O   LYS B 257     -86.868  33.875  41.140  1.00 48.60           O
ANISOU 4843  O   LYS B 257     6994   5384   6090   -364     40   -306       O
ATOM   4844  CB  LYS B 257     -90.144  34.399  41.321  1.00 40.87           C
ANISOU 4844  CB  LYS B 257     6045   4540   4944   -441   -162     27       C
ATOM   4845  CG  LYS B 257     -89.877  33.849  42.708  1.00 41.41           C
ANISOU 4845  CG  LYS B 257     6341   4623   4771   -528   -173    -36       C
ATOM   4846  CD  LYS B 257     -91.154  33.331  43.346  1.00 43.84           C
ANISOU 4846  CD  LYS B 257     6766   4968   4923   -591   -367     91       C
ATOM   4847  CE  LYS B 257     -90.909  32.874  44.774  1.00 51.83           C
ANISOU 4847  CE  LYS B 257     8042   5995   5657   -698   -394     35       C
ATOM   4848  NZ  LYS B 257     -90.393  33.980  45.627  1.00 58.53           N
ANISOU 4848  NZ  LYS B 257     9039   6853   6348   -752   -137    -37       N
ATOM   4849  N   ARG B 258     -88.025  33.145  39.352  1.00 46.96           N
ANISOU 4849  N   ARG B 258     6586   5187   6068   -324   -214   -127       N
ATOM   4850  CA  ARG B 258     -87.039  32.119  39.035  1.00 47.17           C
ANISOU 4850  CA  ARG B 258     6618   5145   6159   -317   -274   -207       C
ATOM   4851  C   ARG B 258     -85.727  32.727  38.554  1.00 45.83           C
ANISOU 4851  C   ARG B 258     6375   4893   6144   -240   -153   -297       C
ATOM   4852  O   ARG B 258     -84.655  32.169  38.813  1.00 47.35           O
ANISOU 4852  O   ARG B 258     6629   5007   6354   -233   -136   -406       O
ATOM   4853  CB  ARG B 258     -87.604  31.166  37.980  1.00 48.70           C
ANISOU 4853  CB  ARG B 258     6719   5337   6446   -324   -438   -123       C
ATOM   4854  CG  ARG B 258     -86.630  30.105  37.478  1.00 57.12           C
ANISOU 4854  CG  ARG B 258     7788   6323   7593   -334   -502   -184       C
ATOM   4855  CD  ARG B 258     -86.526  28.925  38.434  1.00 63.10           C
ANISOU 4855  CD  ARG B 258     8674   7077   8224   -417   -594   -244       C
ATOM   4856  NE  ARG B 258     -85.695  27.856  37.885  1.00 64.81           N
ANISOU 4856  NE  ARG B 258     8890   7206   8529   -444   -662   -290       N
ATOM   4857  CZ  ARG B 258     -85.522  26.670  38.461  1.00 69.27           C
ANISOU 4857  CZ  ARG B 258     9544   7751   9026   -530   -766   -343       C
ATOM   4858  NH1 ARG B 258     -86.124  26.395  39.610  1.00 71.79           N
ANISOU 4858  NH1 ARG B 258     9965   8135   9177   -595   -833   -354       N
ATOM   4859  NH2 ARG B 258     -84.748  25.759  37.889  1.00 70.52           N
ANISOU 4859  NH2 ARG B 258     9700   7816   9278   -564   -816   -380       N
ATOM   4860  N   PHE B 259     -85.789  33.873  37.873  1.00 48.35           N
ANISOU 4860  N   PHE B 259     6561   5217   6591   -182    -78   -255       N
ATOM   4861  CA  PHE B 259     -84.588  34.429  37.258  1.00 53.71           C
ANISOU 4861  CA  PHE B 259     7135   5809   7462    -98    -11   -320       C
ATOM   4862  C   PHE B 259     -83.611  34.954  38.303  1.00 56.46           C
ANISOU 4862  C   PHE B 259     7530   6119   7801    -73    175   -467       C
ATOM   4863  O   PHE B 259     -82.393  34.800  38.152  1.00 58.17           O
ANISOU 4863  O   PHE B 259     7721   6229   8151     -8    205   -565       O
ATOM   4864  CB  PHE B 259     -84.965  35.536  36.276  1.00 58.33           C
ANISOU 4864  CB  PHE B 259     7561   6413   8187    -56     -5   -235       C
ATOM   4865  CG  PHE B 259     -83.816  36.012  35.439  1.00 69.87           C
ANISOU 4865  CG  PHE B 259     8899   7779   9870     31     -6   -271       C
ATOM   4866  CD1 PHE B 259     -83.442  35.322  34.298  1.00 72.78           C
ANISOU 4866  CD1 PHE B 259     9248   8075  10328     49   -160   -222       C
ATOM   4867  CD2 PHE B 259     -83.105  37.145  35.796  1.00 76.77           C
ANISOU 4867  CD2 PHE B 259     9673   8628  10869     90    144   -351       C
ATOM   4868  CE1 PHE B 259     -82.382  35.753  33.526  1.00 74.98           C
ANISOU 4868  CE1 PHE B 259     9429   8250  10808    130   -197   -236       C
ATOM   4869  CE2 PHE B 259     -82.043  37.583  35.028  1.00 81.26           C
ANISOU 4869  CE2 PHE B 259    10106   9096  11674    182    112   -378       C
ATOM   4870  CZ  PHE B 259     -81.682  36.885  33.891  1.00 80.58           C
ANISOU 4870  CZ  PHE B 259    10020   8930  11665    205    -76   -312       C
ATOM   4871  N   LYS B 260     -84.121  35.584  39.365  1.00 58.05           N
ANISOU 4871  N   LYS B 260     7809   6397   7852   -126    312   -487       N
ATOM   4872  CA  LYS B 260     -83.239  36.088  40.412  1.00 65.76           C
ANISOU 4872  CA  LYS B 260     8846   7343   8796   -121    531   -644       C
ATOM   4873  C   LYS B 260     -82.496  34.959  41.111  1.00 71.19           C
ANISOU 4873  C   LYS B 260     9706   7966   9377   -147    513   -768       C
ATOM   4874  O   LYS B 260     -81.404  35.174  41.653  1.00 73.72           O
ANISOU 4874  O   LYS B 260    10051   8211   9748   -108    680   -930       O
ATOM   4875  CB  LYS B 260     -84.039  36.907  41.425  1.00 67.07           C
ANISOU 4875  CB  LYS B 260     9103   7608   8774   -206    681   -625       C
ATOM   4876  CG  LYS B 260     -84.291  38.338  40.989  1.00 70.63           C
ANISOU 4876  CG  LYS B 260     9374   8090   9374   -178    801   -576       C
ATOM   4877  CD  LYS B 260     -82.995  39.134  40.966  1.00 72.83           C
ANISOU 4877  CD  LYS B 260     9500   8296   9876    -92    997   -722       C
ATOM   4878  CE  LYS B 260     -83.150  40.426  40.182  1.00 71.36           C
ANISOU 4878  CE  LYS B 260     9075   8125   9914    -52   1042   -661       C
ATOM   4879  NZ  LYS B 260     -83.409  40.158  38.740  1.00 67.46           N
ANISOU 4879  NZ  LYS B 260     8458   7605   9569      5    794   -537       N
ATOM   4880  N   GLU B 261     -83.063  33.753  41.103  1.00 76.27           N
ANISOU 4880  N   GLU B 261    10459   8630   9890   -214    316   -704       N
ATOM   4881  CA  GLU B 261     -82.412  32.608  41.730  1.00 79.63           C
ANISOU 4881  CA  GLU B 261    11051   8991  10214   -260    270   -817       C
ATOM   4882  C   GLU B 261     -81.385  31.979  40.792  1.00 77.87           C
ANISOU 4882  C   GLU B 261    10745   8634  10208   -185    188   -856       C
ATOM   4883  O   GLU B 261     -80.183  31.980  41.076  1.00 84.38           O
ANISOU 4883  O   GLU B 261    11602   9343  11117   -133    296  -1007       O
ATOM   4884  CB  GLU B 261     -83.466  31.581  42.147  1.00 86.35           C
ANISOU 4884  CB  GLU B 261    12035   9919  10855   -374     77   -730       C
ATOM   4885  CG  GLU B 261     -84.658  32.191  42.867  1.00 95.13           C
ANISOU 4885  CG  GLU B 261    13221  11150  11774   -441    100   -639       C
ATOM   4886  CD  GLU B 261     -85.815  31.222  43.004  1.00100.82           C
ANISOU 4886  CD  GLU B 261    14005  11935  12366   -522   -140   -517       C
ATOM   4887  OE1 GLU B 261     -86.673  31.444  43.883  1.00103.67           O
ANISOU 4887  OE1 GLU B 261    14498  12369  12524   -596   -161   -458       O
ATOM   4888  OE2 GLU B 261     -85.865  30.240  42.233  1.00101.27           O
ANISOU 4888  OE2 GLU B 261    13978  11964  12537   -514   -308   -478       O
ATOM   4889  N   SER B 262     -81.846  31.435  39.669  1.00 65.71           N
ANISOU 4889  N   SER B 262     9109   7098   8760   -182      4   -723       N
ATOM   4890  CA  SER B 262     -80.981  30.827  38.673  1.00 62.05           C
ANISOU 4890  CA  SER B 262     8588   6507   8483   -132    -92   -725       C
ATOM   4891  C   SER B 262     -81.375  31.318  37.286  1.00 56.57           C
ANISOU 4891  C   SER B 262     7722   5829   7944    -80   -169   -580       C
ATOM   4892  O   SER B 262     -82.567  31.365  36.956  1.00 54.35           O
ANISOU 4892  O   SER B 262     7399   5657   7593   -126   -234   -461       O
ATOM   4893  CB  SER B 262     -81.064  29.295  38.726  1.00 63.97           C
ANISOU 4893  CB  SER B 262     8945   6721   8640   -230   -253   -722       C
ATOM   4894  OG  SER B 262     -82.391  28.851  38.502  1.00 65.16           O
ANISOU 4894  OG  SER B 262     9069   6993   8697   -307   -378   -591       O
ATOM   4895  N   PRO B 263     -80.404  31.684  36.456  1.00 57.44           N
ANISOU 4895  N   PRO B 263     7739   5822   8263     13   -174   -589       N
ATOM   4896  CA  PRO B 263     -80.724  32.221  35.129  1.00 57.02           C
ANISOU 4896  CA  PRO B 263     7548   5780   8336     50   -259   -456       C
ATOM   4897  C   PRO B 263     -81.220  31.135  34.185  1.00 52.99           C
ANISOU 4897  C   PRO B 263     7074   5271   7789    -28   -424   -345       C
ATOM   4898  O   PRO B 263     -81.127  29.936  34.452  1.00 53.62           O
ANISOU 4898  O   PRO B 263     7258   5320   7795   -101   -483   -372       O
ATOM   4899  CB  PRO B 263     -79.390  32.803  34.655  1.00 61.24           C
ANISOU 4899  CB  PRO B 263     7998   6166   9105    169   -244   -507       C
ATOM   4900  CG  PRO B 263     -78.364  31.983  35.364  1.00 63.17           C
ANISOU 4900  CG  PRO B 263     8364   6284   9354    178   -212   -642       C
ATOM   4901  CD  PRO B 263     -78.954  31.649  36.707  1.00 61.80           C
ANISOU 4901  CD  PRO B 263     8316   6213   8952     92   -110   -725       C
ATOM   4902  N   PHE B 264     -81.755  31.588  33.055  1.00 49.51           N
ANISOU 4902  N   PHE B 264     6543   4866   7402    -24   -488   -227       N
ATOM   4903  CA  PHE B 264     -82.241  30.701  32.006  1.00 44.98           C
ANISOU 4903  CA  PHE B 264     5994   4294   6801   -102   -608   -124       C
ATOM   4904  C   PHE B 264     -82.242  31.473  30.694  1.00 41.89           C
ANISOU 4904  C   PHE B 264     5527   3883   6506    -70   -667    -28       C
ATOM   4905  O   PHE B 264     -82.012  32.684  30.663  1.00 43.30           O
ANISOU 4905  O   PHE B 264     5614   4062   6777      8   -629    -35       O
ATOM   4906  CB  PHE B 264     -83.633  30.152  32.333  1.00 43.86           C
ANISOU 4906  CB  PHE B 264     5863   4287   6516   -190   -611    -85       C
ATOM   4907  CG  PHE B 264     -84.591  31.191  32.835  1.00 48.90           C
ANISOU 4907  CG  PHE B 264     6440   5039   7100   -164   -534    -68       C
ATOM   4908  CD1 PHE B 264     -85.299  31.986  31.950  1.00 49.74           C
ANISOU 4908  CD1 PHE B 264     6464   5192   7243   -152   -539     16       C
ATOM   4909  CD2 PHE B 264     -84.787  31.369  34.195  1.00 53.89           C
ANISOU 4909  CD2 PHE B 264     7122   5724   7631   -166   -458   -135       C
ATOM   4910  CE1 PHE B 264     -86.183  32.943  32.412  1.00 53.13           C
ANISOU 4910  CE1 PHE B 264     6848   5708   7631   -138   -469     35       C
ATOM   4911  CE2 PHE B 264     -85.670  32.322  34.663  1.00 57.25           C
ANISOU 4911  CE2 PHE B 264     7514   6240   7998   -158   -386   -105       C
ATOM   4912  CZ  PHE B 264     -86.368  33.111  33.771  1.00 57.12           C
ANISOU 4912  CZ  PHE B 264     7402   6260   8041   -141   -392    -19       C
ATOM   4913  N   GLU B 265     -82.507  30.754  29.608  1.00 39.55           N
ANISOU 4913  N   GLU B 265     5274   3569   6184   -146   -758     59       N
ATOM   4914  CA  GLU B 265     -82.407  31.300  28.262  1.00 42.46           C
ANISOU 4914  CA  GLU B 265     5623   3900   6610   -143   -839    154       C
ATOM   4915  C   GLU B 265     -83.798  31.496  27.677  1.00 41.38           C
ANISOU 4915  C   GLU B 265     5457   3887   6380   -209   -819    219       C
ATOM   4916  O   GLU B 265     -84.616  30.571  27.688  1.00 38.39           O
ANISOU 4916  O   GLU B 265     5108   3568   5910   -292   -795    229       O
ATOM   4917  CB  GLU B 265     -81.580  30.379  27.362  1.00 48.45           C
ANISOU 4917  CB  GLU B 265     6492   4525   7392   -196   -947    206       C
ATOM   4918  CG  GLU B 265     -80.823  31.100  26.258  1.00 57.00           C
ANISOU 4918  CG  GLU B 265     7580   5503   8574   -152  -1069    284       C
ATOM   4919  CD  GLU B 265     -79.646  31.901  26.784  1.00 68.98           C
ANISOU 4919  CD  GLU B 265     9022   6912  10275     -9  -1088    222       C
ATOM   4920  OE1 GLU B 265     -79.238  31.677  27.944  1.00 72.77           O
ANISOU 4920  OE1 GLU B 265     9488   7372  10788     42   -995    110       O
ATOM   4921  OE2 GLU B 265     -79.126  32.754  26.035  1.00 74.90           O
ANISOU 4921  OE2 GLU B 265     9724   7594  11142     51  -1198    281       O
ATOM   4922  N   LEU B 266     -84.057  32.697  27.168  1.00 46.66           N
ANISOU 4922  N   LEU B 266     6057   4582   7088   -171   -830    256       N
ATOM   4923  CA  LEU B 266     -85.307  33.030  26.496  1.00 47.17           C
ANISOU 4923  CA  LEU B 266     6105   4738   7078   -228   -812    309       C
ATOM   4924  C   LEU B 266     -85.015  33.310  25.030  1.00 47.14           C
ANISOU 4924  C   LEU B 266     6156   4674   7081   -269   -921    388       C
ATOM   4925  O   LEU B 266     -84.277  34.249  24.709  1.00 58.41           O
ANISOU 4925  O   LEU B 266     7543   6042   8608   -211  -1003    406       O
ATOM   4926  CB  LEU B 266     -85.977  34.245  27.136  1.00 55.74           C
ANISOU 4926  CB  LEU B 266     7089   5905   8184   -177   -737    286       C
ATOM   4927  CG  LEU B 266     -86.491  34.130  28.566  1.00 64.20           C
ANISOU 4927  CG  LEU B 266     8137   7048   9208   -156   -633    228       C
ATOM   4928  CD1 LEU B 266     -87.087  35.459  28.989  1.00 70.47           C
ANISOU 4928  CD1 LEU B 266     8851   7902  10024   -125   -562    226       C
ATOM   4929  CD2 LEU B 266     -87.519  33.024  28.676  1.00 63.61           C
ANISOU 4929  CD2 LEU B 266     8104   7031   9033   -224   -621    242       C
ATOM   4930  N   GLU B 267     -85.599  32.509  24.147  1.00 39.62           N
ANISOU 4930  N   GLU B 267     5294   3735   6024   -376   -921    432       N
ATOM   4931  CA  GLU B 267     -85.467  32.691  22.707  1.00 43.19           C
ANISOU 4931  CA  GLU B 267     5846   4139   6427   -448  -1013    508       C
ATOM   4932  C   GLU B 267     -86.798  33.221  22.185  1.00 39.15           C
ANISOU 4932  C   GLU B 267     5319   3719   5836   -499   -948    510       C
ATOM   4933  O   GLU B 267     -87.796  32.494  22.158  1.00 38.64           O
ANISOU 4933  O   GLU B 267     5265   3718   5699   -560   -840    487       O
ATOM   4934  CB  GLU B 267     -85.071  31.384  22.022  1.00 53.38           C
ANISOU 4934  CB  GLU B 267     7279   5362   7641   -555  -1036    549       C
ATOM   4935  CG  GLU B 267     -84.205  31.559  20.779  1.00 65.05           C
ANISOU 4935  CG  GLU B 267     8899   6726   9091   -607  -1189    643       C
ATOM   4936  CD  GLU B 267     -85.007  31.933  19.549  1.00 76.69           C
ANISOU 4936  CD  GLU B 267    10466   8243  10429   -713  -1192    688       C
ATOM   4937  OE1 GLU B 267     -86.245  31.779  19.579  1.00 81.19           O
ANISOU 4937  OE1 GLU B 267    11000   8919  10931   -758  -1047    640       O
ATOM   4938  OE2 GLU B 267     -84.400  32.379  18.552  1.00 79.65           O
ANISOU 4938  OE2 GLU B 267    10958   8537  10768   -752  -1347    770       O
ATOM   4939  N   ASP B 268     -86.810  34.493  21.785  1.00 38.54           N
ANISOU 4939  N   ASP B 268     5208   3641   5793   -471  -1016    530       N
ATOM   4940  CA  ASP B 268     -88.017  35.156  21.293  1.00 35.01           C
ANISOU 4940  CA  ASP B 268     4757   3262   5284   -517   -964    523       C
ATOM   4941  C   ASP B 268     -88.055  35.010  19.775  1.00 31.20           C
ANISOU 4941  C   ASP B 268     4440   2739   4675   -639  -1034    575       C
ATOM   4942  O   ASP B 268     -87.660  35.899  19.019  1.00 34.03           O
ANISOU 4942  O   ASP B 268     4842   3056   5033   -658  -1172    619       O
ATOM   4943  CB  ASP B 268     -88.029  36.616  21.733  1.00 41.33           C
ANISOU 4943  CB  ASP B 268     5433   4081   6190   -443   -995    509       C
ATOM   4944  CG  ASP B 268     -89.314  37.331  21.369  1.00 47.00           C
ANISOU 4944  CG  ASP B 268     6147   4855   6857   -490   -935    493       C
ATOM   4945  OD1 ASP B 268     -90.285  36.660  20.957  1.00 50.75           O
ANISOU 4945  OD1 ASP B 268     6695   5360   7229   -557   -844    476       O
ATOM   4946  OD2 ASP B 268     -89.351  38.573  21.497  1.00 47.97           O
ANISOU 4946  OD2 ASP B 268     6184   4983   7059   -462   -973    490       O
ATOM   4947  N   PHE B 269     -88.551  33.855  19.322  1.00 30.99           N
ANISOU 4947  N   PHE B 269     4512   2727   4537   -734   -935    568       N
ATOM   4948  CA  PHE B 269     -88.516  33.548  17.896  1.00 33.90           C
ANISOU 4948  CA  PHE B 269     5075   3054   4752   -874   -972    614       C
ATOM   4949  C   PHE B 269     -89.517  34.359  17.085  1.00 37.39           C
ANISOU 4949  C   PHE B 269     5573   3532   5102   -939   -941    589       C
ATOM   4950  O   PHE B 269     -89.496  34.276  15.852  1.00 40.56           O
ANISOU 4950  O   PHE B 269     6164   3899   5347  -1069   -978    622       O
ATOM   4951  CB  PHE B 269     -88.732  32.046  17.658  1.00 37.11           C
ANISOU 4951  CB  PHE B 269     5560   3464   5075   -974   -841    603       C
ATOM   4952  CG  PHE B 269     -89.912  31.460  18.388  1.00 40.85           C
ANISOU 4952  CG  PHE B 269     5899   4026   5596   -948   -652    518       C
ATOM   4953  CD1 PHE B 269     -91.127  31.288  17.744  1.00 41.91           C
ANISOU 4953  CD1 PHE B 269     6062   4206   5655  -1025   -502    466       C
ATOM   4954  CD2 PHE B 269     -89.798  31.046  19.707  1.00 42.37           C
ANISOU 4954  CD2 PHE B 269     5944   4245   5910   -850   -632    489       C
ATOM   4955  CE1 PHE B 269     -92.210  30.738  18.406  1.00 42.06           C
ANISOU 4955  CE1 PHE B 269     5937   4289   5753   -986   -349    394       C
ATOM   4956  CE2 PHE B 269     -90.878  30.496  20.376  1.00 42.58           C
ANISOU 4956  CE2 PHE B 269     5850   4344   5986   -827   -499    427       C
ATOM   4957  CZ  PHE B 269     -92.086  30.341  19.723  1.00 40.79           C
ANISOU 4957  CZ  PHE B 269     5626   4155   5717   -887   -365    383       C
ATOM   4958  N   ILE B 270     -90.382  35.135  17.732  1.00 38.04           N
ANISOU 4958  N   ILE B 270     5517   3672   5263   -865   -874    532       N
ATOM   4959  CA  ILE B 270     -91.231  36.097  17.034  1.00 36.06           C
ANISOU 4959  CA  ILE B 270     5316   3436   4951   -918   -870    504       C
ATOM   4960  C   ILE B 270     -91.020  37.457  17.686  1.00 33.32           C
ANISOU 4960  C   ILE B 270     4826   3093   4743   -823   -971    511       C
ATOM   4961  O   ILE B 270     -91.874  37.910  18.463  1.00 31.65           O
ANISOU 4961  O   ILE B 270     4494   2924   4606   -763   -871    462       O
ATOM   4962  CB  ILE B 270     -92.711  35.684  17.069  1.00 41.04           C
ANISOU 4962  CB  ILE B 270     5927   4115   5550   -941   -659    419       C
ATOM   4963  CG1 ILE B 270     -92.869  34.202  16.728  1.00 44.55           C
ANISOU 4963  CG1 ILE B 270     6440   4567   5920  -1015   -524    400       C
ATOM   4964  CG2 ILE B 270     -93.516  36.524  16.089  1.00 37.58           C
ANISOU 4964  CG2 ILE B 270     5599   3664   5014  -1027   -648    380       C
ATOM   4965  CD1 ILE B 270     -94.303  33.716  16.761  1.00 47.41           C
ANISOU 4965  CD1 ILE B 270     6749   4968   6298  -1022   -312    308       C
ATOM   4966  N   PRO B 271     -89.901  38.139  17.413  1.00 37.30           N
ANISOU 4966  N   PRO B 271     5331   3544   5298   -808  -1169    572       N
ATOM   4967  CA  PRO B 271     -89.619  39.403  18.108  1.00 35.60           C
ANISOU 4967  CA  PRO B 271     4941   3335   5252   -718  -1243    569       C
ATOM   4968  C   PRO B 271     -90.564  40.522  17.702  1.00 37.22           C
ANISOU 4968  C   PRO B 271     5143   3560   5439   -775  -1242    536       C
ATOM   4969  O   PRO B 271     -90.322  41.235  16.723  1.00 41.12           O
ANISOU 4969  O   PRO B 271     5717   4016   5890   -853  -1405    566       O
ATOM   4970  CB  PRO B 271     -88.173  39.710  17.700  1.00 34.35           C
ANISOU 4970  CB  PRO B 271     4787   3097   5166   -696  -1469    643       C
ATOM   4971  CG  PRO B 271     -88.006  39.031  16.387  1.00 35.19           C
ANISOU 4971  CG  PRO B 271     5135   3156   5082   -825  -1556    698       C
ATOM   4972  CD  PRO B 271     -88.840  37.782  16.457  1.00 35.15           C
ANISOU 4972  CD  PRO B 271     5215   3196   4946   -876  -1337    652       C
ATOM   4973  N   MET B 272     -91.646  40.682  18.459  1.00 36.36           N
ANISOU 4973  N   MET B 272     4952   3500   5364   -741  -1075    478       N
ATOM   4974  CA  MET B 272     -92.634  41.713  18.182  1.00 35.06           C
ANISOU 4974  CA  MET B 272     4787   3338   5196   -793  -1054    440       C
ATOM   4975  C   MET B 272     -93.419  41.988  19.453  1.00 31.81           C
ANISOU 4975  C   MET B 272     4237   2964   4887   -713   -903    407       C
ATOM   4976  O   MET B 272     -93.404  41.195  20.399  1.00 35.80           O
ANISOU 4976  O   MET B 272     4684   3500   5420   -635   -805    406       O
ATOM   4977  CB  MET B 272     -93.579  41.300  17.051  1.00 33.76           C
ANISOU 4977  CB  MET B 272     4816   3158   4853   -910   -991    398       C
ATOM   4978  CG  MET B 272     -94.404  40.069  17.376  1.00 39.81           C
ANISOU 4978  CG  MET B 272     5602   3951   5572   -885   -788    353       C
ATOM   4979  SD  MET B 272     -95.731  39.792  16.193  1.00 48.21           S
ANISOU 4979  SD  MET B 272     6850   4990   6479  -1006   -650    265       S
ATOM   4980  CE  MET B 272     -96.669  41.308  16.372  1.00 48.29           C
ANISOU 4980  CE  MET B 272     6809   4970   6569  -1007   -658    222       C
ATOM   4981  N   ASP B 273     -94.110  43.122  19.460  1.00 33.11           N
ANISOU 4981  N   ASP B 273     4364   3118   5098   -746   -897    385       N
ATOM   4982  CA  ASP B 273     -94.957  43.491  20.586  1.00 37.62           C
ANISOU 4982  CA  ASP B 273     4838   3706   5749   -693   -763    368       C
ATOM   4983  C   ASP B 273     -96.296  42.774  20.458  1.00 35.88           C
ANISOU 4983  C   ASP B 273     4709   3473   5450   -701   -626    326       C
ATOM   4984  O   ASP B 273     -96.990  42.921  19.446  1.00 34.83           O
ANISOU 4984  O   ASP B 273     4694   3301   5241   -782   -618    282       O
ATOM   4985  CB  ASP B 273     -95.154  45.005  20.631  1.00 41.65           C
ANISOU 4985  CB  ASP B 273     5274   4195   6355   -739   -809    365       C
ATOM   4986  CG  ASP B 273     -95.532  45.503  22.012  1.00 42.35           C
ANISOU 4986  CG  ASP B 273     5242   4302   6545   -683   -691    374       C
ATOM   4987  OD1 ASP B 273     -95.359  44.741  22.988  1.00 43.67           O
ANISOU 4987  OD1 ASP B 273     5376   4506   6712   -600   -608    389       O
ATOM   4988  OD2 ASP B 273     -96.003  46.654  22.122  1.00 40.43           O
ANISOU 4988  OD2 ASP B 273     4954   4034   6372   -737   -683    369       O
ATOM   4989  N   SER B 274     -96.653  41.991  21.473  1.00 28.14           N
ANISOU 4989  N   SER B 274     3676   2519   4496   -618   -522    332       N
ATOM   4990  CA  SER B 274     -97.928  41.291  21.474  1.00 38.55           C
ANISOU 4990  CA  SER B 274     5039   3818   5792   -602   -402    295       C
ATOM   4991  C   SER B 274     -98.366  41.054  22.911  1.00 31.75           C
ANISOU 4991  C   SER B 274     4088   2974   5001   -510   -341    327       C
ATOM   4992  O   SER B 274     -97.538  40.977  23.823  1.00 29.25           O
ANISOU 4992  O   SER B 274     3705   2702   4707   -465   -368    366       O
ATOM   4993  CB  SER B 274     -97.849  39.964  20.708  1.00 43.25           C
ANISOU 4993  CB  SER B 274     5708   4424   6302   -626   -366    265       C
ATOM   4994  OG  SER B 274     -96.858  39.112  21.251  1.00 50.57           O
ANISOU 4994  OG  SER B 274     6587   5396   7230   -582   -400    303       O
ATOM   4995  N   THR B 275     -99.684  40.944  23.100  1.00 31.31           N
ANISOU 4995  N   THR B 275     4044   2873   4978   -485   -262    310       N
ATOM   4996  CA  THR B 275    -100.234  40.746  24.438  1.00 31.57           C
ANISOU 4996  CA  THR B 275     4019   2908   5067   -405   -232    356       C
ATOM   4997  C   THR B 275     -99.732  39.447  25.058  1.00 31.73           C
ANISOU 4997  C   THR B 275     3996   2989   5071   -350   -244    373       C
ATOM   4998  O   THR B 275     -99.388  39.410  26.246  1.00 34.70           O
ANISOU 4998  O   THR B 275     4337   3399   5447   -310   -266    420       O
ATOM   4999  CB  THR B 275    -101.764  40.767  24.380  1.00 34.88           C
ANISOU 4999  CB  THR B 275     4463   3243   5548   -378   -169    337       C
ATOM   5000  OG1 THR B 275    -102.210  42.065  23.966  1.00 35.36           O
ANISOU 5000  OG1 THR B 275     4572   3235   5626   -439   -163    323       O
ATOM   5001  CG2 THR B 275    -102.366  40.442  25.740  1.00 33.10           C
ANISOU 5001  CG2 THR B 275     4194   3007   5374   -296   -174    404       C
ATOM   5002  N   VAL B 276     -99.676  38.375  24.273  1.00 32.64           N
ANISOU 5002  N   VAL B 276     4123   3115   5162   -364   -222    329       N
ATOM   5003  CA  VAL B 276     -99.122  37.097  24.706  1.00 33.39           C
ANISOU 5003  CA  VAL B 276     4176   3262   5247   -336   -238    336       C
ATOM   5004  C   VAL B 276     -97.833  36.851  23.935  1.00 32.44           C
ANISOU 5004  C   VAL B 276     4101   3168   5056   -395   -278    326       C
ATOM   5005  O   VAL B 276     -97.800  36.994  22.706  1.00 31.39           O
ANISOU 5005  O   VAL B 276     4041   3011   4873   -465   -264    294       O
ATOM   5006  CB  VAL B 276    -100.118  35.943  24.496  1.00 34.09           C
ANISOU 5006  CB  VAL B 276     4223   3336   5396   -310   -174    299       C
ATOM   5007  CG1 VAL B 276     -99.477  34.613  24.866  1.00 37.71           C
ANISOU 5007  CG1 VAL B 276     4631   3848   5850   -306   -200    303       C
ATOM   5008  CG2 VAL B 276    -101.375  36.173  25.317  1.00 32.26           C
ANISOU 5008  CG2 VAL B 276     3944   3056   5257   -234   -170    325       C
ATOM   5009  N   LYS B 277     -96.775  36.487  24.654  1.00 32.95           N
ANISOU 5009  N   LYS B 277     4140   3270   5110   -372   -333    353       N
ATOM   5010  CA  LYS B 277     -95.470  36.228  24.065  1.00 35.97           C
ANISOU 5010  CA  LYS B 277     4565   3655   5448   -413   -390    356       C
ATOM   5011  C   LYS B 277     -95.141  34.744  24.147  1.00 36.75           C
ANISOU 5011  C   LYS B 277     4661   3771   5532   -424   -381    346       C
ATOM   5012  O   LYS B 277     -95.390  34.097  25.170  1.00 40.02           O
ANISOU 5012  O   LYS B 277     5016   4211   5978   -379   -376    348       O
ATOM   5013  CB  LYS B 277     -94.379  37.042  24.768  1.00 34.03           C
ANISOU 5013  CB  LYS B 277     4286   3414   5228   -377   -453    380       C
ATOM   5014  CG  LYS B 277     -94.466  38.538  24.529  1.00 30.74           C
ANISOU 5014  CG  LYS B 277     3855   2979   4845   -389   -472    388       C
ATOM   5015  CD  LYS B 277     -94.227  38.876  23.068  1.00 30.68           C
ANISOU 5015  CD  LYS B 277     3920   2938   4801   -463   -536    384       C
ATOM   5016  CE  LYS B 277     -92.855  38.412  22.604  1.00 29.86           C
ANISOU 5016  CE  LYS B 277     3848   2815   4682   -474   -632    404       C
ATOM   5017  NZ  LYS B 277     -92.615  38.749  21.172  1.00 29.75           N
ANISOU 5017  NZ  LYS B 277     3936   2762   4606   -560   -724    418       N
ATOM   5018  N   ASN B 278     -94.582  34.211  23.066  1.00 34.31           N
ANISOU 5018  N   ASN B 278     4427   3442   5168   -498   -390    340       N
ATOM   5019  CA  ASN B 278     -94.153  32.821  22.994  1.00 38.77           C
ANISOU 5019  CA  ASN B 278     5000   4011   5718   -536   -376    334       C
ATOM   5020  C   ASN B 278     -92.632  32.766  23.014  1.00 42.11           C
ANISOU 5020  C   ASN B 278     5477   4403   6120   -544   -475    366       C
ATOM   5021  O   ASN B 278     -91.972  33.463  22.234  1.00 42.94           O
ANISOU 5021  O   ASN B 278     5657   4468   6191   -572   -544    394       O
ATOM   5022  CB  ASN B 278     -94.693  32.144  21.733  1.00 46.61           C
ANISOU 5022  CB  ASN B 278     6057   4993   6659   -634   -284    304       C
ATOM   5023  CG  ASN B 278     -96.197  31.968  21.765  1.00 54.77           C
ANISOU 5023  CG  ASN B 278     7012   6042   7755   -611   -168    253       C
ATOM   5024  OD1 ASN B 278     -96.770  31.602  22.793  1.00 57.75           O
ANISOU 5024  OD1 ASN B 278     7273   6443   8226   -537   -166    250       O
ATOM   5025  ND2 ASN B 278     -96.848  32.232  20.639  1.00 58.46           N
ANISOU 5025  ND2 ASN B 278     7554   6486   8173   -674    -78    210       N
ATOM   5026  N   TYR B 279     -92.082  31.939  23.901  1.00 43.55           N
ANISOU 5026  N   TYR B 279     5624   4591   6332   -519   -496    362       N
ATOM   5027  CA  TYR B 279     -90.641  31.836  24.077  1.00 39.72           C
ANISOU 5027  CA  TYR B 279     5184   4054   5852   -509   -582    379       C
ATOM   5028  C   TYR B 279     -90.200  30.381  24.038  1.00 36.52           C
ANISOU 5028  C   TYR B 279     4813   3627   5435   -574   -578    373       C
ATOM   5029  O   TYR B 279     -90.916  29.489  24.502  1.00 32.46           O
ANISOU 5029  O   TYR B 279     4237   3157   4940   -592   -524    345       O
ATOM   5030  CB  TYR B 279     -90.185  32.456  25.406  1.00 37.78           C
ANISOU 5030  CB  TYR B 279     4876   3820   5660   -412   -607    361       C
ATOM   5031  CG  TYR B 279     -90.452  33.937  25.538  1.00 39.40           C
ANISOU 5031  CG  TYR B 279     5035   4040   5894   -360   -603    368       C
ATOM   5032  CD1 TYR B 279     -89.742  34.861  24.784  1.00 41.65           C
ANISOU 5032  CD1 TYR B 279     5337   4279   6208   -359   -671    392       C
ATOM   5033  CD2 TYR B 279     -91.401  34.412  26.433  1.00 39.64           C
ANISOU 5033  CD2 TYR B 279     5007   4124   5931   -322   -544    357       C
ATOM   5034  CE1 TYR B 279     -89.981  36.218  24.908  1.00 43.58           C
ANISOU 5034  CE1 TYR B 279     5520   4538   6500   -326   -669    393       C
ATOM   5035  CE2 TYR B 279     -91.644  35.764  26.566  1.00 38.17           C
ANISOU 5035  CE2 TYR B 279     4782   3945   5775   -294   -528    366       C
ATOM   5036  CZ  TYR B 279     -90.933  36.663  25.801  1.00 40.18           C
ANISOU 5036  CZ  TYR B 279     5034   4161   6072   -299   -585    378       C
ATOM   5037  OH  TYR B 279     -91.174  38.012  25.929  1.00 46.50           O
ANISOU 5037  OH  TYR B 279     5777   4970   6923   -286   -570    382       O
ATOM   5038  N   PHE B 280     -89.013  30.158  23.480  1.00 38.40           N
ANISOU 5038  N   PHE B 280     5148   3787   5657   -611   -650    404       N
ATOM   5039  CA  PHE B 280     -88.299  28.894  23.614  1.00 35.36           C
ANISOU 5039  CA  PHE B 280     4807   3353   5274   -669   -666    401       C
ATOM   5040  C   PHE B 280     -87.421  29.016  24.855  1.00 36.15           C
ANISOU 5040  C   PHE B 280     4876   3422   5437   -579   -722    368       C
ATOM   5041  O   PHE B 280     -86.430  29.754  24.852  1.00 37.25           O
ANISOU 5041  O   PHE B 280     5044   3492   5617   -516   -794    380       O
ATOM   5042  CB  PHE B 280     -87.477  28.608  22.358  1.00 37.29           C
ANISOU 5042  CB  PHE B 280     5201   3505   5462   -763   -718    462       C
ATOM   5043  CG  PHE B 280     -87.044  27.168  22.208  1.00 41.47           C
ANISOU 5043  CG  PHE B 280     5794   3986   5977   -872   -699    467       C
ATOM   5044  CD1 PHE B 280     -86.808  26.365  23.314  1.00 43.15           C
ANISOU 5044  CD1 PHE B 280     5941   4200   6253   -854   -699    418       C
ATOM   5045  CD2 PHE B 280     -86.864  26.623  20.947  1.00 42.54           C
ANISOU 5045  CD2 PHE B 280     6069   4070   6023  -1011   -680    522       C
ATOM   5046  CE1 PHE B 280     -86.405  25.049  23.164  1.00 40.54           C
ANISOU 5046  CE1 PHE B 280     5664   3817   5922   -970   -686    420       C
ATOM   5047  CE2 PHE B 280     -86.463  25.307  20.791  1.00 39.10           C
ANISOU 5047  CE2 PHE B 280     5694   3583   5578  -1132   -649    531       C
ATOM   5048  CZ  PHE B 280     -86.233  24.520  21.901  1.00 39.53           C
ANISOU 5048  CZ  PHE B 280     5661   3636   5721  -1110   -654    479       C
ATOM   5049  N   ILE B 281     -87.789  28.305  25.917  1.00 40.02           N
ANISOU 5049  N   ILE B 281     5306   3959   5941   -573   -693    319       N
ATOM   5050  CA  ILE B 281     -87.167  28.458  27.226  1.00 40.89           C
ANISOU 5050  CA  ILE B 281     5402   4056   6078   -498   -720    268       C
ATOM   5051  C   ILE B 281     -86.287  27.250  27.512  1.00 37.37           C
ANISOU 5051  C   ILE B 281     5020   3536   5644   -556   -761    238       C
ATOM   5052  O   ILE B 281     -86.668  26.109  27.226  1.00 37.28           O
ANISOU 5052  O   ILE B 281     5006   3536   5622   -656   -750    244       O
ATOM   5053  CB  ILE B 281     -88.230  28.639  28.327  1.00 45.23           C
ANISOU 5053  CB  ILE B 281     5872   4707   6608   -458   -683    238       C
ATOM   5054  CG1 ILE B 281     -89.080  29.876  28.039  1.00 54.68           C
ANISOU 5054  CG1 ILE B 281     7018   5956   7803   -408   -641    269       C
ATOM   5055  CG2 ILE B 281     -87.579  28.750  29.696  1.00 45.07           C
ANISOU 5055  CG2 ILE B 281     5876   4675   6575   -406   -696    177       C
ATOM   5056  CD1 ILE B 281     -90.021  30.247  29.161  1.00 61.07           C
ANISOU 5056  CD1 ILE B 281     7775   6839   8590   -363   -616    258       C
ATOM   5057  N   THR B 282     -85.106  27.507  28.074  1.00 34.99           N
ANISOU 5057  N   THR B 282     4769   3149   5379   -495   -798    199       N
ATOM   5058  CA  THR B 282     -84.185  26.463  28.514  1.00 36.32           C
ANISOU 5058  CA  THR B 282     5012   3224   5564   -540   -838    153       C
ATOM   5059  C   THR B 282     -83.681  26.836  29.902  1.00 38.29           C
ANISOU 5059  C   THR B 282     5267   3465   5817   -457   -821     58       C
ATOM   5060  O   THR B 282     -82.950  27.820  30.054  1.00 39.63           O
ANISOU 5060  O   THR B 282     5434   3581   6042   -356   -806     33       O
ATOM   5061  CB  THR B 282     -83.016  26.299  27.541  1.00 36.39           C
ANISOU 5061  CB  THR B 282     5120   3082   5623   -560   -900    200       C
ATOM   5062  OG1 THR B 282     -83.513  25.957  26.242  1.00 39.60           O
ANISOU 5062  OG1 THR B 282     5555   3502   5988   -661   -899    287       O
ATOM   5063  CG2 THR B 282     -82.075  25.202  28.021  1.00 32.87           C
ANISOU 5063  CG2 THR B 282     4764   2521   5206   -612   -939    148       C
ATOM   5064  N   ASP B 283     -84.070  26.058  30.910  1.00 37.95           N
ANISOU 5064  N   ASP B 283     5231   3472   5716   -506   -824      1       N
ATOM   5065  CA  ASP B 283     -83.616  26.304  32.272  1.00 35.60           C
ANISOU 5065  CA  ASP B 283     4980   3168   5380   -456   -799    -99       C
ATOM   5066  C   ASP B 283     -82.189  25.799  32.439  1.00 39.71           C
ANISOU 5066  C   ASP B 283     5604   3528   5954   -456   -822   -173       C
ATOM   5067  O   ASP B 283     -81.899  24.630  32.169  1.00 43.63           O
ANISOU 5067  O   ASP B 283     6156   3960   6464   -554   -884   -172       O
ATOM   5068  CB  ASP B 283     -84.543  25.627  33.280  1.00 38.66           C
ANISOU 5068  CB  ASP B 283     5364   3657   5667   -522   -828   -126       C
ATOM   5069  CG  ASP B 283     -84.121  25.878  34.714  1.00 45.73           C
ANISOU 5069  CG  ASP B 283     6350   4550   6476   -494   -799   -232       C
ATOM   5070  OD1 ASP B 283     -84.169  27.046  35.155  1.00 46.65           O
ANISOU 5070  OD1 ASP B 283     6459   4703   6564   -413   -713   -248       O
ATOM   5071  OD2 ASP B 283     -83.740  24.907  35.402  1.00 48.85           O
ANISOU 5071  OD2 ASP B 283     6832   4905   6824   -568   -855   -304       O
ATOM   5072  N   ALA B 284     -81.300  26.685  32.891  1.00 43.73           N
ANISOU 5072  N   ALA B 284     6134   3968   6513   -348   -765   -244       N
ATOM   5073  CA  ALA B 284     -79.880  26.359  32.943  1.00 43.73           C
ANISOU 5073  CA  ALA B 284     6222   3787   6606   -318   -781   -317       C
ATOM   5074  C   ALA B 284     -79.533  25.434  34.103  1.00 48.79           C
ANISOU 5074  C   ALA B 284     6978   4388   7170   -383   -779   -442       C
ATOM   5075  O   ALA B 284     -78.567  24.668  34.008  1.00 53.21           O
ANISOU 5075  O   ALA B 284     7633   4791   7792   -414   -824   -488       O
ATOM   5076  CB  ALA B 284     -79.053  27.641  33.036  1.00 44.42           C
ANISOU 5076  CB  ALA B 284     6260   3803   6812   -167   -708   -365       C
ATOM   5077  N   GLN B 285     -80.296  25.483  35.196  1.00 47.31           N
ANISOU 5077  N   GLN B 285     6804   4330   6841   -415   -741   -494       N
ATOM   5078  CA  GLN B 285     -79.935  24.697  36.370  1.00 49.72           C
ANISOU 5078  CA  GLN B 285     7245   4599   7047   -485   -751   -623       C
ATOM   5079  C   GLN B 285     -80.338  23.235  36.221  1.00 46.81           C
ANISOU 5079  C   GLN B 285     6903   4237   6644   -638   -883   -590       C
ATOM   5080  O   GLN B 285     -79.561  22.338  36.566  1.00 48.09           O
ANISOU 5080  O   GLN B 285     7180   4281   6813   -708   -928   -678       O
ATOM   5081  CB  GLN B 285     -80.576  25.297  37.622  1.00 53.54           C
ANISOU 5081  CB  GLN B 285     7764   5211   7367   -479   -678   -682       C
ATOM   5082  CG  GLN B 285     -80.067  24.699  38.926  1.00 61.21           C
ANISOU 5082  CG  GLN B 285     8915   6136   8206   -548   -670   -838       C
ATOM   5083  CD  GLN B 285     -78.621  25.062  39.211  1.00 72.03           C
ANISOU 5083  CD  GLN B 285    10369   7337   9664   -464   -547   -989       C
ATOM   5084  OE1 GLN B 285     -77.695  24.481  38.641  1.00 71.90           O
ANISOU 5084  OE1 GLN B 285    10378   7157   9785   -457   -592  -1014       O
ATOM   5085  NE2 GLN B 285     -78.419  26.031  40.097  1.00 78.94           N
ANISOU 5085  NE2 GLN B 285    11287   8238  10468   -400   -382  -1092       N
ATOM   5086  N   THR B 286     -81.539  22.976  35.708  1.00 47.74           N
ANISOU 5086  N   THR B 286     6908   4485   6744   -693   -941   -474       N
ATOM   5087  CA  THR B 286     -82.078  21.623  35.654  1.00 49.31           C
ANISOU 5087  CA  THR B 286     7089   4715   6932   -840  -1054   -448       C
ATOM   5088  C   THR B 286     -82.031  20.999  34.269  1.00 44.77           C
ANISOU 5088  C   THR B 286     6448   4087   6476   -902  -1077   -353       C
ATOM   5089  O   THR B 286     -82.003  19.769  34.160  1.00 48.00           O
ANISOU 5089  O   THR B 286     6864   4460   6912  -1038  -1148   -360       O
ATOM   5090  CB  THR B 286     -83.529  21.612  36.144  1.00 37.05           C
ANISOU 5090  CB  THR B 286     5443   3338   5295   -867  -1105   -396       C
ATOM   5091  OG1 THR B 286     -84.350  22.332  35.214  1.00 35.47           O
ANISOU 5091  OG1 THR B 286     5109   3218   5151   -801  -1053   -283       O
ATOM   5092  CG2 THR B 286     -83.630  22.270  37.508  1.00 37.65           C
ANISOU 5092  CG2 THR B 286     5619   3469   5219   -826  -1083   -471       C
ATOM   5093  N   GLY B 287     -82.025  21.804  33.213  1.00 40.65           N
ANISOU 5093  N   GLY B 287     5871   3558   6015   -823  -1018   -267       N
ATOM   5094  CA  GLY B 287     -82.103  21.284  31.866  1.00 36.96           C
ANISOU 5094  CA  GLY B 287     5368   3055   5619   -899  -1026   -168       C
ATOM   5095  C   GLY B 287     -83.505  21.099  31.335  1.00 38.53           C
ANISOU 5095  C   GLY B 287     5426   3404   5811   -949  -1010    -89       C
ATOM   5096  O   GLY B 287     -83.667  20.535  30.246  1.00 36.98           O
ANISOU 5096  O   GLY B 287     5203   3189   5658  -1040   -992    -21       O
ATOM   5097  N   SER B 288     -84.522  21.543  32.069  1.00 38.91           N
ANISOU 5097  N   SER B 288     5390   3588   5807   -898  -1009    -98       N
ATOM   5098  CA  SER B 288     -85.895  21.468  31.595  1.00 37.40           C
ANISOU 5098  CA  SER B 288     5052   3521   5635   -919   -990    -30       C
ATOM   5099  C   SER B 288     -86.144  22.559  30.561  1.00 36.16           C
ANISOU 5099  C   SER B 288     4871   3382   5489   -839   -907     41       C
ATOM   5100  O   SER B 288     -85.638  23.677  30.687  1.00 39.34           O
ANISOU 5100  O   SER B 288     5324   3756   5868   -734   -882     36       O
ATOM   5101  CB  SER B 288     -86.869  21.612  32.764  1.00 34.90           C
ANISOU 5101  CB  SER B 288     4675   3318   5265   -884  -1043    -52       C
ATOM   5102  OG  SER B 288     -88.178  21.226  32.389  1.00 40.20           O
ANISOU 5102  OG  SER B 288     5190   4084   5999   -914  -1049      1       O
ATOM   5103  N   SER B 289     -86.924  22.230  29.533  1.00 33.02           N
ANISOU 5103  N   SER B 289     4390   3027   5130   -899   -859     99       N
ATOM   5104  CA  SER B 289     -87.132  23.156  28.430  1.00 32.69           C
ANISOU 5104  CA  SER B 289     4352   2989   5079   -853   -789    161       C
ATOM   5105  C   SER B 289     -88.505  22.924  27.814  1.00 34.05           C
ANISOU 5105  C   SER B 289     4400   3256   5282   -891   -719    189       C
ATOM   5106  O   SER B 289     -89.197  21.953  28.126  1.00 40.66           O
ANISOU 5106  O   SER B 289     5130   4143   6175   -955   -726    166       O
ATOM   5107  CB  SER B 289     -86.036  23.011  27.369  1.00 35.98           C
ANISOU 5107  CB  SER B 289     4892   3283   5495   -910   -788    200       C
ATOM   5108  OG  SER B 289     -86.113  21.752  26.725  1.00 40.56           O
ANISOU 5108  OG  SER B 289     5474   3839   6097  -1063   -759    216       O
ATOM   5109  N   LYS B 290     -88.888  23.841  26.927  1.00 31.02           N
ANISOU 5109  N   LYS B 290     4024   2888   4873   -851   -655    230       N
ATOM   5110  CA  LYS B 290     -90.143  23.746  26.192  1.00 33.32           C
ANISOU 5110  CA  LYS B 290     4219   3248   5192   -881   -561    242       C
ATOM   5111  C   LYS B 290     -90.075  24.699  25.008  1.00 29.99           C
ANISOU 5111  C   LYS B 290     3884   2801   4708   -873   -506    284       C
ATOM   5112  O   LYS B 290     -89.672  25.855  25.166  1.00 29.65           O
ANISOU 5112  O   LYS B 290     3893   2740   4632   -782   -554    302       O
ATOM   5113  CB  LYS B 290     -91.340  24.074  27.093  1.00 35.55           C
ANISOU 5113  CB  LYS B 290     4370   3616   5519   -791   -576    224       C
ATOM   5114  CG  LYS B 290     -92.676  24.099  26.370  1.00 40.33           C
ANISOU 5114  CG  LYS B 290     4869   4272   6183   -793   -473    224       C
ATOM   5115  CD  LYS B 290     -93.836  24.007  27.349  1.00 43.08           C
ANISOU 5115  CD  LYS B 290     5073   4681   6616   -719   -521    214       C
ATOM   5116  CE  LYS B 290     -93.762  25.096  28.406  1.00 45.91           C
ANISOU 5116  CE  LYS B 290     5487   5050   6908   -610   -606    236       C
ATOM   5117  NZ  LYS B 290     -94.870  24.989  29.395  1.00 49.99           N
ANISOU 5117  NZ  LYS B 290     5898   5611   7487   -548   -680    247       N
ATOM   5118  N   CYS B 291     -90.469  24.212  23.829  1.00 33.65           N
ANISOU 5118  N   CYS B 291     4367   3264   5156   -979   -405    294       N
ATOM   5119  CA  CYS B 291     -90.297  24.991  22.606  1.00 36.60           C
ANISOU 5119  CA  CYS B 291     4868   3603   5437  -1007   -371    336       C
ATOM   5120  C   CYS B 291     -91.211  26.209  22.580  1.00 37.09           C
ANISOU 5120  C   CYS B 291     4882   3717   5493   -909   -347    327       C
ATOM   5121  O   CYS B 291     -90.779  27.314  22.233  1.00 41.84           O
ANISOU 5121  O   CYS B 291     5569   4289   6041   -866   -406    361       O
ATOM   5122  CB  CYS B 291     -90.549  24.109  21.383  1.00 40.47           C
ANISOU 5122  CB  CYS B 291     5415   4081   5882  -1169   -242    339       C
ATOM   5123  SG  CYS B 291     -89.316  22.826  21.127  1.00 49.03           S
ANISOU 5123  SG  CYS B 291     6612   5070   6945  -1320   -270    374       S
ATOM   5124  N   VAL B 292     -92.481  26.027  22.929  1.00 40.12           N
ANISOU 5124  N   VAL B 292     5126   4169   5950   -876   -271    283       N
ATOM   5125  CA  VAL B 292     -93.476  27.092  22.872  1.00 39.91           C
ANISOU 5125  CA  VAL B 292     5059   4175   5931   -794   -236    272       C
ATOM   5126  C   VAL B 292     -94.004  27.297  24.284  1.00 39.08           C
ANISOU 5126  C   VAL B 292     4830   4110   5908   -679   -301    264       C
ATOM   5127  O   VAL B 292     -94.829  26.515  24.770  1.00 41.50           O
ANISOU 5127  O   VAL B 292     5007   4450   6309   -670   -279    237       O
ATOM   5128  CB  VAL B 292     -94.616  26.772  21.899  1.00 43.48           C
ANISOU 5128  CB  VAL B 292     5476   4644   6400   -855    -77    226       C
ATOM   5129  CG1 VAL B 292     -95.603  27.931  21.844  1.00 29.53           C
ANISOU 5129  CG1 VAL B 292     3688   2886   4645   -770    -49    210       C
ATOM   5130  CG2 VAL B 292     -94.065  26.465  20.522  1.00 42.71           C
ANISOU 5130  CG2 VAL B 292     5538   4507   6183   -999     -3    236       C
ATOM   5131  N  ACYS B 293     -93.532  28.350  24.945  0.58 39.04           N
ANISOU 5131  N  ACYS B 293     4865   4098   5870   -597   -383    290       N
ATOM   5132  N  BCYS B 293     -93.539  28.348  24.951  0.42 39.01           N
ANISOU 5132  N  BCYS B 293     4861   4095   5867   -597   -383    290       N
ATOM   5133  CA ACYS B 293     -93.984  28.726  26.280  0.58 38.80           C
ANISOU 5133  CA ACYS B 293     4765   4101   5874   -504   -438    293       C
ATOM   5134  CA BCYS B 293     -94.005  28.694  26.290  0.42 38.79           C
ANISOU 5134  CA BCYS B 293     4762   4102   5876   -505   -437    293       C
ATOM   5135  C  ACYS B 293     -94.751  30.036  26.163  0.58 37.40           C
ANISOU 5135  C  ACYS B 293     4588   3928   5694   -443   -408    308       C
ATOM   5136  C  BCYS B 293     -94.742  30.025  26.206  0.42 37.39           C
ANISOU 5136  C  BCYS B 293     4585   3927   5693   -442   -411    308       C
ATOM   5137  O  ACYS B 293     -94.161  31.081  25.866  0.58 34.53           O
ANISOU 5137  O  ACYS B 293     4292   3543   5286   -431   -423    324       O
ATOM   5138  O  BCYS B 293     -94.125  31.070  25.972  0.42 34.94           O
ANISOU 5138  O  BCYS B 293     4342   3596   5338   -427   -428    325       O
ATOM   5139  CB ACYS B 293     -92.806  28.868  27.239  0.58 39.29           C
ANISOU 5139  CB ACYS B 293     4882   4150   5898   -476   -522    297       C
ATOM   5140  CB BCYS B 293     -92.842  28.764  27.277  0.42 39.44           C
ANISOU 5140  CB BCYS B 293     4895   4170   5919   -479   -523    295       C
ATOM   5141  SG ACYS B 293     -91.580  27.556  27.111  0.58 46.22           S
ANISOU 5141  SG ACYS B 293     5810   4982   6768   -562   -561    278       S
ATOM   5142  SG BCYS B 293     -93.354  28.844  29.009  0.42 37.11           S
ANISOU 5142  SG BCYS B 293     4556   3921   5623   -409   -589    295       S
ATOM   5143  N   SER B 294     -96.060  29.982  26.390  1.00 39.54           N
ANISOU 5143  N   SER B 294     4775   4215   6032   -405   -376    303       N
ATOM   5144  CA  SER B 294     -96.885  31.181  26.330  1.00 37.77           C
ANISOU 5144  CA  SER B 294     4558   3976   5817   -353   -348    317       C
ATOM   5145  C   SER B 294     -96.769  31.941  27.645  1.00 32.19           C
ANISOU 5145  C   SER B 294     3864   3283   5085   -290   -418    357       C
ATOM   5146  O   SER B 294     -97.004  31.378  28.720  1.00 30.81           O
ANISOU 5146  O   SER B 294     3654   3129   4924   -261   -480    374       O
ATOM   5147  CB  SER B 294     -98.336  30.813  26.037  1.00 44.78           C
ANISOU 5147  CB  SER B 294     5358   4851   6807   -329   -282    292       C
ATOM   5148  OG  SER B 294     -98.447  30.180  24.776  1.00 52.72           O
ANISOU 5148  OG  SER B 294     6363   5846   7822   -402   -176    240       O
ATOM   5149  N   VAL B 295     -96.392  33.215  27.560  1.00 36.67           N
ANISOU 5149  N   VAL B 295     4486   3836   5611   -280   -408    372       N
ATOM   5150  CA  VAL B 295     -96.198  34.068  28.725  1.00 35.90           C
ANISOU 5150  CA  VAL B 295     4409   3749   5480   -241   -434    403       C
ATOM   5151  C   VAL B 295     -97.033  35.328  28.546  1.00 35.39           C
ANISOU 5151  C   VAL B 295     4352   3658   5437   -228   -394    426       C
ATOM   5152  O   VAL B 295     -97.189  35.827  27.426  1.00 34.99           O
ANISOU 5152  O   VAL B 295     4312   3579   5404   -257   -360    408       O
ATOM   5153  CB  VAL B 295     -94.709  34.425  28.930  1.00 33.24           C
ANISOU 5153  CB  VAL B 295     4110   3417   5103   -249   -448    386       C
ATOM   5154  CG1 VAL B 295     -94.503  35.153  30.254  1.00 32.76           C
ANISOU 5154  CG1 VAL B 295     4071   3375   5002   -221   -437    398       C
ATOM   5155  CG2 VAL B 295     -93.845  33.174  28.870  1.00 31.39           C
ANISOU 5155  CG2 VAL B 295     3887   3184   4857   -275   -487    358       C
ATOM   5156  N   ILE B 296     -97.578  35.833  29.649  1.00 32.91           N
ANISOU 5156  N   ILE B 296     4052   3344   5110   -198   -403    469       N
ATOM   5157  CA  ILE B 296     -98.339  37.076  29.654  1.00 36.03           C
ANISOU 5157  CA  ILE B 296     4465   3700   5524   -197   -365    501       C
ATOM   5158  C   ILE B 296     -98.050  37.809  30.957  1.00 35.02           C
ANISOU 5158  C   ILE B 296     4384   3590   5333   -199   -356    542       C
ATOM   5159  O   ILE B 296     -97.928  37.188  32.019  1.00 32.43           O
ANISOU 5159  O   ILE B 296     4090   3291   4942   -188   -396    562       O
ATOM   5160  CB  ILE B 296     -99.851  36.817  29.473  1.00 37.50           C
ANISOU 5160  CB  ILE B 296     4633   3832   5783   -164   -369    521       C
ATOM   5161  CG1 ILE B 296    -100.617  38.139  29.391  1.00 35.07           C
ANISOU 5161  CG1 ILE B 296     4362   3463   5501   -173   -329    550       C
ATOM   5162  CG2 ILE B 296    -100.393  35.939  30.595  1.00 33.52           C
ANISOU 5162  CG2 ILE B 296     4119   3337   5281   -119   -447    568       C
ATOM   5163  CD1 ILE B 296    -102.070  37.978  29.008  1.00 35.65           C
ANISOU 5163  CD1 ILE B 296     4420   3453   5672   -133   -321    553       C
ATOM   5164  N   ASP B 297     -97.922  39.135  30.874  1.00 35.51           N
ANISOU 5164  N   ASP B 297     4452   3635   5404   -230   -298    549       N
ATOM   5165  CA  ASP B 297     -97.578  39.957  32.034  1.00 37.51           C
ANISOU 5165  CA  ASP B 297     4746   3907   5599   -253   -246    576       C
ATOM   5166  C   ASP B 297     -98.832  40.666  32.536  1.00 36.76           C
ANISOU 5166  C   ASP B 297     4709   3760   5500   -269   -230    651       C
ATOM   5167  O   ASP B 297     -99.051  41.854  32.302  1.00 38.20           O
ANISOU 5167  O   ASP B 297     4885   3908   5722   -313   -171    663       O
ATOM   5168  CB  ASP B 297     -96.473  40.949  31.686  1.00 36.72           C
ANISOU 5168  CB  ASP B 297     4589   3822   5542   -282   -183    531       C
ATOM   5169  CG  ASP B 297     -96.060  41.803  32.873  1.00 39.60           C
ANISOU 5169  CG  ASP B 297     4977   4209   5860   -315    -85    539       C
ATOM   5170  OD1 ASP B 297     -96.371  41.426  34.023  1.00 41.24           O
ANISOU 5170  OD1 ASP B 297     5279   4432   5958   -320    -75    574       O
ATOM   5171  OD2 ASP B 297     -95.432  42.858  32.655  1.00 43.51           O
ANISOU 5171  OD2 ASP B 297     5397   4705   6428   -344    -18    509       O
ATOM   5172  N   LEU B 298     -99.661  39.916  33.248  1.00 35.69           N
ANISOU 5172  N   LEU B 298     4630   3607   5323   -238   -299    708       N
ATOM   5173  CA  LEU B 298    -100.805  40.484  33.941  1.00 36.79           C
ANISOU 5173  CA  LEU B 298     4852   3681   5444   -250   -310    801       C
ATOM   5174  C   LEU B 298    -100.432  40.810  35.381  1.00 36.23           C
ANISOU 5174  C   LEU B 298     4897   3645   5225   -301   -279    850       C
ATOM   5175  O   LEU B 298     -99.506  40.232  35.954  1.00 40.14           O
ANISOU 5175  O   LEU B 298     5413   4210   5630   -307   -279    810       O
ATOM   5176  CB  LEU B 298    -101.992  39.519  33.923  1.00 36.68           C
ANISOU 5176  CB  LEU B 298     4834   3610   5491   -181   -426    846       C
ATOM   5177  CG  LEU B 298    -102.694  39.266  32.590  1.00 38.89           C
ANISOU 5177  CG  LEU B 298     5023   3833   5921   -135   -424    796       C
ATOM   5178  CD1 LEU B 298    -103.736  38.172  32.743  1.00 39.10           C
ANISOU 5178  CD1 LEU B 298     5010   3811   6034    -55   -530    828       C
ATOM   5179  CD2 LEU B 298    -103.334  40.544  32.071  1.00 41.40           C
ANISOU 5179  CD2 LEU B 298     5370   4065   6296   -168   -354    807       C
ATOM   5180  N   LEU B 299    -101.159  41.760  35.961  1.00 34.84           N
ANISOU 5180  N   LEU B 299     4815   3410   5014   -351   -242    934       N
ATOM   5181  CA  LEU B 299    -101.088  41.952  37.401  1.00 40.32           C
ANISOU 5181  CA  LEU B 299     5664   4122   5534   -413   -222   1003       C
ATOM   5182  C   LEU B 299    -101.550  40.675  38.089  1.00 44.14           C
ANISOU 5182  C   LEU B 299     6223   4607   5943   -366   -394   1058       C
ATOM   5183  O   LEU B 299    -102.579  40.101  37.723  1.00 48.97           O
ANISOU 5183  O   LEU B 299     6798   5151   6658   -294   -525   1108       O
ATOM   5184  CB  LEU B 299    -101.955  43.135  37.830  1.00 34.87           C
ANISOU 5184  CB  LEU B 299     5080   3347   4822   -486   -165   1104       C
ATOM   5185  CG  LEU B 299    -101.901  43.504  39.314  1.00 39.59           C
ANISOU 5185  CG  LEU B 299     5876   3957   5210   -583   -114   1186       C
ATOM   5186  CD1 LEU B 299    -100.538  44.073  39.674  1.00 38.08           C
ANISOU 5186  CD1 LEU B 299     5662   3862   4944   -658     82   1086       C
ATOM   5187  CD2 LEU B 299    -103.009  44.482  39.671  1.00 38.13           C
ANISOU 5187  CD2 LEU B 299     5817   3658   5012   -653    -98   1315       C
ATOM   5188  N   LEU B 300    -100.773  40.218  39.073  1.00 42.82           N
ANISOU 5188  N   LEU B 300     6150   4511   5607   -405   -394   1039       N
ATOM   5189  CA  LEU B 300    -101.079  38.943  39.716  1.00 43.58           C
ANISOU 5189  CA  LEU B 300     6309   4618   5632   -374   -582   1080       C
ATOM   5190  C   LEU B 300    -102.473  38.953  40.328  1.00 43.61           C
ANISOU 5190  C   LEU B 300     6430   4529   5612   -366   -734   1235       C
ATOM   5191  O   LEU B 300    -103.172  37.933  40.316  1.00 46.50           O
ANISOU 5191  O   LEU B 300     6752   4862   6054   -295   -929   1280       O
ATOM   5192  CB  LEU B 300    -100.028  38.621  40.776  1.00 45.80           C
ANISOU 5192  CB  LEU B 300     6719   4980   5704   -443   -546   1030       C
ATOM   5193  CG  LEU B 300    -100.110  37.218  41.378  1.00 45.17           C
ANISOU 5193  CG  LEU B 300     6692   4924   5548   -427   -752   1044       C
ATOM   5194  CD1 LEU B 300    -100.042  36.165  40.283  1.00 37.49           C
ANISOU 5194  CD1 LEU B 300     5509   3961   4776   -336   -838    975       C
ATOM   5195  CD2 LEU B 300     -99.003  37.008  42.397  1.00 48.67           C
ANISOU 5195  CD2 LEU B 300     7287   5438   5769   -511   -691    971       C
ATOM   5196  N   ASP B 301    -102.900  40.102  40.856  1.00 41.58           N
ANISOU 5196  N   ASP B 301     6313   4217   5270   -442   -651   1323       N
ATOM   5197  CA  ASP B 301    -104.250  40.210  41.396  1.00 39.86           C
ANISOU 5197  CA  ASP B 301     6222   3881   5041   -435   -804   1488       C
ATOM   5198  C   ASP B 301    -105.294  40.005  40.307  1.00 39.67           C
ANISOU 5198  C   ASP B 301     6034   3755   5284   -315   -890   1500       C
ATOM   5199  O   ASP B 301    -106.351  39.411  40.552  1.00 42.79           O
ANISOU 5199  O   ASP B 301     6448   4059   5752   -243  -1091   1600       O
ATOM   5200  CB  ASP B 301    -104.433  41.570  42.067  1.00 44.06           C
ANISOU 5200  CB  ASP B 301     6939   4365   5435   -559   -664   1574       C
ATOM   5201  CG  ASP B 301    -103.283  41.921  42.987  1.00 52.29           C
ANISOU 5201  CG  ASP B 301     8118   5515   6235   -685   -499   1521       C
ATOM   5202  OD1 ASP B 301    -102.128  41.930  42.513  1.00 55.11           O
ANISOU 5202  OD1 ASP B 301     8338   5968   6633   -680   -351   1368       O
ATOM   5203  OD2 ASP B 301    -103.531  42.193  44.180  1.00 58.12           O
ANISOU 5203  OD2 ASP B 301     9107   6232   6742   -792   -513   1630       O
ATOM   5204  N   ASP B 302    -105.014  40.489  39.095  1.00 40.23           N
ANISOU 5204  N   ASP B 302     5945   3832   5507   -292   -743   1392       N
ATOM   5205  CA  ASP B 302    -105.940  40.288  37.985  1.00 44.42           C
ANISOU 5205  CA  ASP B 302     6334   4269   6277   -189   -789   1373       C
ATOM   5206  C   ASP B 302    -106.043  38.814  37.622  1.00 44.73           C
ANISOU 5206  C   ASP B 302     6229   4338   6427    -85   -925   1323       C
ATOM   5207  O   ASP B 302    -107.146  38.283  37.448  1.00 49.17           O
ANISOU 5207  O   ASP B 302     6732   4801   7149      9  -1055   1371       O
ATOM   5208  CB  ASP B 302    -105.499  41.111  36.773  1.00 46.80           C
ANISOU 5208  CB  ASP B 302     6524   4581   6675   -212   -609   1260       C
ATOM   5209  CG  ASP B 302    -105.728  42.598  36.962  1.00 52.98           C
ANISOU 5209  CG  ASP B 302     7410   5298   7422   -309   -492   1314       C
ATOM   5210  OD1 ASP B 302    -106.310  42.988  37.995  1.00 57.68           O
ANISOU 5210  OD1 ASP B 302     8174   5825   7916   -357   -537   1446       O
ATOM   5211  OD2 ASP B 302    -105.325  43.378  36.073  1.00 54.62           O
ANISOU 5211  OD2 ASP B 302     7534   5517   7700   -348   -363   1229       O
ATOM   5212  N   PHE B 303    -104.900  38.134  37.509  1.00 42.84           N
ANISOU 5212  N   PHE B 303     5924   4227   6126   -103   -893   1224       N
ATOM   5213  CA  PHE B 303    -104.914  36.718  37.158  1.00 43.13           C
ANISOU 5213  CA  PHE B 303     5819   4298   6270    -29  -1006   1172       C
ATOM   5214  C   PHE B 303    -105.632  35.894  38.219  1.00 44.94           C
ANISOU 5214  C   PHE B 303     6105   4492   6477      4  -1238   1283       C
ATOM   5215  O   PHE B 303    -106.339  34.933  37.895  1.00 45.22           O
ANISOU 5215  O   PHE B 303     5997   4487   6696     94  -1364   1282       O
ATOM   5216  CB  PHE B 303    -103.486  36.215  36.955  1.00 42.62           C
ANISOU 5216  CB  PHE B 303     5709   4361   6123    -73   -933   1057       C
ATOM   5217  CG  PHE B 303    -103.401  34.753  36.622  1.00 41.86           C
ANISOU 5217  CG  PHE B 303     5474   4303   6126    -26  -1034   1002       C
ATOM   5218  CD1 PHE B 303    -103.808  34.286  35.383  1.00 42.20           C
ANISOU 5218  CD1 PHE B 303     5347   4320   6369     34   -992    933       C
ATOM   5219  CD2 PHE B 303    -102.907  33.846  37.545  1.00 41.03           C
ANISOU 5219  CD2 PHE B 303     5418   4260   5912    -57  -1162   1010       C
ATOM   5220  CE1 PHE B 303    -103.729  32.940  35.073  1.00 44.78           C
ANISOU 5220  CE1 PHE B 303     5535   4683   6798     60  -1061    879       C
ATOM   5221  CE2 PHE B 303    -102.824  32.500  37.241  1.00 41.46           C
ANISOU 5221  CE2 PHE B 303     5332   4347   6074    -30  -1256    958       C
ATOM   5222  CZ  PHE B 303    -103.236  32.047  36.003  1.00 44.32           C
ANISOU 5222  CZ  PHE B 303     5506   4685   6650     27  -1198    895       C
ATOM   5223  N   VAL B 304    -105.464  36.256  39.493  1.00 44.22           N
ANISOU 5223  N   VAL B 304     6223   4414   6166    -74  -1298   1378       N
ATOM   5224  CA  VAL B 304    -106.200  35.581  40.558  1.00 44.06           C
ANISOU 5224  CA  VAL B 304     6296   4346   6098    -57  -1554   1508       C
ATOM   5225  C   VAL B 304    -107.696  35.811  40.394  1.00 46.79           C
ANISOU 5225  C   VAL B 304     6614   4530   6635     37  -1670   1622       C
ATOM   5226  O   VAL B 304    -108.502  34.883  40.537  1.00 50.00           O
ANISOU 5226  O   VAL B 304     6926   4876   7196    128  -1890   1677       O
ATOM   5227  CB  VAL B 304    -105.699  36.052  41.935  1.00 47.07           C
ANISOU 5227  CB  VAL B 304     6956   4768   6160   -186  -1568   1586       C
ATOM   5228  CG1 VAL B 304    -106.620  35.555  43.037  1.00 44.52           C
ANISOU 5228  CG1 VAL B 304     6779   4371   5767   -182  -1860   1754       C
ATOM   5229  CG2 VAL B 304    -104.280  35.567  42.172  1.00 46.77           C
ANISOU 5229  CG2 VAL B 304     6933   4872   5965   -258  -1487   1459       C
ATOM   5230  N   GLU B 305    -108.089  37.048  40.085  1.00 48.02           N
ANISOU 5230  N   GLU B 305     6841   4601   6804     18  -1529   1654       N
ATOM   5231  CA  GLU B 305    -109.496  37.340  39.834  1.00 48.21           C
ANISOU 5231  CA  GLU B 305     6843   4444   7029    111  -1616   1746       C
ATOM   5232  C   GLU B 305    -110.020  36.538  38.650  1.00 43.77           C
ANISOU 5232  C   GLU B 305     6009   3844   6778    250  -1620   1639       C
ATOM   5233  O   GLU B 305    -111.172  36.089  38.653  1.00 48.27           O
ANISOU 5233  O   GLU B 305     6501   4280   7560    367  -1782   1705       O
ATOM   5234  CB  GLU B 305    -109.680  38.840  39.599  1.00 54.61           C
ANISOU 5234  CB  GLU B 305     7774   5177   7800     42  -1434   1772       C
ATOM   5235  CG  GLU B 305    -111.078  39.248  39.161  1.00 64.20           C
ANISOU 5235  CG  GLU B 305     8967   6185   9241    135  -1485   1839       C
ATOM   5236  CD  GLU B 305    -111.229  40.753  39.033  1.00 72.39           C
ANISOU 5236  CD  GLU B 305    10143   7139  10221     39  -1316   1872       C
ATOM   5237  OE1 GLU B 305    -110.470  41.487  39.701  1.00 75.58           O
ANISOU 5237  OE1 GLU B 305    10706   7624  10385   -106  -1213   1905       O
ATOM   5238  OE2 GLU B 305    -112.104  41.204  38.264  1.00 75.36           O
ANISOU 5238  OE2 GLU B 305    10466   7366  10801    101  -1276   1854       O
ATOM   5239  N   ILE B 306    -109.181  36.333  37.634  1.00 42.01           N
ANISOU 5239  N   ILE B 306     5641   3730   6591    237  -1439   1473       N
ATOM   5240  CA  ILE B 306    -109.600  35.578  36.458  1.00 44.10           C
ANISOU 5240  CA  ILE B 306     5666   3969   7120    341  -1398   1356       C
ATOM   5241  C   ILE B 306    -109.771  34.103  36.801  1.00 51.20           C
ANISOU 5241  C   ILE B 306     6419   4904   8132    409  -1591   1361       C
ATOM   5242  O   ILE B 306    -110.816  33.502  36.525  1.00 56.57           O
ANISOU 5242  O   ILE B 306     6942   5479   9074    530  -1687   1368       O
ATOM   5243  CB  ILE B 306    -108.593  35.771  35.310  1.00 43.60           C
ANISOU 5243  CB  ILE B 306     5529   4013   7025    284  -1166   1194       C
ATOM   5244  CG1 ILE B 306    -108.576  37.228  34.846  1.00 42.59           C
ANISOU 5244  CG1 ILE B 306     5508   3833   6841    224  -1000   1183       C
ATOM   5245  CG2 ILE B 306    -108.921  34.842  34.152  1.00 37.53           C
ANISOU 5245  CG2 ILE B 306     4538   3236   6484    364  -1110   1070       C
ATOM   5246  CD1 ILE B 306    -107.460  37.541  33.873  1.00 34.98           C
ANISOU 5246  CD1 ILE B 306     4502   2977   5812    152   -817   1050       C
ATOM   5247  N   ILE B 307    -108.747  33.500  37.411  1.00 49.48           N
ANISOU 5247  N   ILE B 307     6239   4824   7735    331  -1649   1350       N
ATOM   5248  CA  ILE B 307    -108.762  32.059  37.641  1.00 48.93           C
ANISOU 5248  CA  ILE B 307     6013   4803   7775    370  -1822   1333       C
ATOM   5249  C   ILE B 307    -109.843  31.672  38.644  1.00 49.17           C
ANISOU 5249  C   ILE B 307     6065   4727   7889    441  -2120   1489       C
ATOM   5250  O   ILE B 307    -110.407  30.574  38.565  1.00 53.00           O
ANISOU 5250  O   ILE B 307     6342   5187   8609    527  -2276   1481       O
ATOM   5251  CB  ILE B 307    -107.366  31.578  38.090  1.00 51.60           C
ANISOU 5251  CB  ILE B 307     6419   5299   7887    256  -1814   1278       C
ATOM   5252  CG1 ILE B 307    -107.311  30.051  38.168  1.00 54.91           C
ANISOU 5252  CG1 ILE B 307     6655   5771   8438    276  -1975   1238       C
ATOM   5253  CG2 ILE B 307    -106.984  32.187  39.430  1.00 53.27           C
ANISOU 5253  CG2 ILE B 307     6909   5533   7800    162  -1902   1388       C
ATOM   5254  CD1 ILE B 307    -107.395  29.363  36.826  1.00 54.57           C
ANISOU 5254  CD1 ILE B 307     6349   5738   8647    328  -1831   1102       C
ATOM   5255  N   LYS B 308    -110.170  32.559  39.583  1.00 49.41           N
ANISOU 5255  N   LYS B 308     6342   4686   7744    404  -2210   1638       N
ATOM   5256  CA  LYS B 308    -111.126  32.232  40.634  1.00 53.21           C
ANISOU 5256  CA  LYS B 308     6895   5059   8262    454  -2529   1814       C
ATOM   5257  C   LYS B 308    -112.577  32.419  40.213  1.00 59.21           C
ANISOU 5257  C   LYS B 308     7540   5619   9337    610  -2600   1877       C
ATOM   5258  O   LYS B 308    -113.472  32.203  41.037  1.00 66.94           O
ANISOU 5258  O   LYS B 308     8574   6476  10384    671  -2888   2040       O
ATOM   5259  CB  LYS B 308    -110.843  33.069  41.884  1.00 54.99           C
ANISOU 5259  CB  LYS B 308     7474   5288   8132    326  -2596   1960       C
ATOM   5260  CG  LYS B 308    -109.653  32.583  42.694  1.00 56.68           C
ANISOU 5260  CG  LYS B 308     7819   5666   8051    191  -2638   1929       C
ATOM   5261  CD  LYS B 308    -109.570  33.292  44.034  1.00 60.71           C
ANISOU 5261  CD  LYS B 308     8692   6161   8214     64  -2727   2082       C
ATOM   5262  CE  LYS B 308    -108.523  32.650  44.929  1.00 65.35           C
ANISOU 5262  CE  LYS B 308     9421   6892   8518    -64  -2806   2046       C
ATOM   5263  NZ  LYS B 308    -108.434  33.316  46.257  1.00 72.43           N
ANISOU 5263  NZ  LYS B 308    10700   7776   9044   -207  -2871   2184       N
ATOM   5264  N   SER B 309    -112.839  32.806  38.966  1.00 56.70           N
ANISOU 5264  N   SER B 309     7078   5252   9214    673  -2357   1752       N
ATOM   5265  CA  SER B 309    -114.201  32.966  38.474  1.00 60.39           C
ANISOU 5265  CA  SER B 309     7428   5515  10003    827  -2390   1776       C
ATOM   5266  C   SER B 309    -114.583  31.896  37.458  1.00 60.55           C
ANISOU 5266  C   SER B 309     7099   5531  10377    952  -2333   1622       C
ATOM   5267  O   SER B 309    -115.599  32.040  36.771  1.00 63.36           O
ANISOU 5267  O   SER B 309     7327   5726  11022   1081  -2270   1580       O
ATOM   5268  CB  SER B 309    -114.384  34.359  37.867  1.00 60.05           C
ANISOU 5268  CB  SER B 309     7522   5382   9912    796  -2152   1752       C
ATOM   5269  OG  SER B 309    -113.466  34.584  36.814  1.00 59.81           O
ANISOU 5269  OG  SER B 309     7430   5483   9812    722  -1859   1570       O
ATOM   5270  N   GLN B 310    -113.803  30.825  37.355  1.00 59.53           N
ANISOU 5270  N   GLN B 310     6817   5564  10237    910  -2340   1531       N
ATOM   5271  CA  GLN B 310    -114.031  29.780  36.370  1.00 60.61           C
ANISOU 5271  CA  GLN B 310     6624   5720  10687    993  -2244   1373       C
ATOM   5272  C   GLN B 310    -114.788  28.611  36.989  1.00 62.14           C
ANISOU 5272  C   GLN B 310     6601   5855  11154   1104  -2552   1446       C
ATOM   5273  O   GLN B 310    -114.710  28.364  38.195  1.00 61.78           O
ANISOU 5273  O   GLN B 310     6683   5842  10950   1056  -2827   1583       O
ATOM   5274  CB  GLN B 310    -112.704  29.288  35.789  1.00 60.19           C
ANISOU 5274  CB  GLN B 310     6523   5869  10476    866  -2052   1227       C
ATOM   5275  CG  GLN B 310    -111.834  30.395  35.220  1.00 60.30           C
ANISOU 5275  CG  GLN B 310     6737   5949  10225    754  -1787   1163       C
ATOM   5276  CD  GLN B 310    -112.500  31.123  34.070  1.00 64.24           C
ANISOU 5276  CD  GLN B 310     7200   6334  10874    814  -1557   1071       C
ATOM   5277  OE1 GLN B 310    -113.210  30.519  33.265  1.00 70.04           O
ANISOU 5277  OE1 GLN B 310     7712   7002  11898    911  -1476    968       O
ATOM   5278  NE2 GLN B 310    -112.278  32.429  33.988  1.00 60.08           N
ANISOU 5278  NE2 GLN B 310     6892   5780  10156    749  -1443   1097       N
ATOM   5279  N   ASP B 311    -115.528  27.894  36.144  1.00 64.51           N
ANISOU 5279  N   ASP B 311     6594   6099  11820   1220  -2458   1318       N
ATOM   5280  CA  ASP B 311    -116.226  26.688  36.571  1.00 67.52           C
ANISOU 5280  CA  ASP B 311     6747   6483  12424   1275  -2648   1312       C
ATOM   5281  C   ASP B 311    -115.261  25.511  36.503  1.00 67.41           C
ANISOU 5281  C   ASP B 311     6557   6640  12416   1190  -2673   1236       C
ATOM   5282  O   ASP B 311    -114.759  25.172  35.425  1.00 63.72           O
ANISOU 5282  O   ASP B 311     5914   6233  12064   1176  -2427   1083       O
ATOM   5283  CB  ASP B 311    -117.451  26.435  35.694  1.00 68.48           C
ANISOU 5283  CB  ASP B 311     6619   6475  12925   1418  -2497   1190       C
ATOM   5284  CG  ASP B 311    -118.465  25.522  36.358  1.00 76.36           C
ANISOU 5284  CG  ASP B 311     7444   7418  14152   1496  -2741   1234       C
ATOM   5285  OD1 ASP B 311    -119.660  25.880  36.392  1.00 81.15           O
ANISOU 5285  OD1 ASP B 311     8042   7862  14928   1611  -2773   1263       O
ATOM   5286  OD2 ASP B 311    -118.064  24.454  36.865  1.00 78.72           O
ANISOU 5286  OD2 ASP B 311     7621   7826  14464   1439  -2911   1244       O
ATOM   5287  N   LEU B 312    -115.003  24.886  37.651  1.00 71.37           N
ANISOU 5287  N   LEU B 312     7120   7214  12783   1119  -2965   1337       N
ATOM   5288  CA  LEU B 312    -114.017  23.820  37.759  1.00 71.04           C
ANISOU 5288  CA  LEU B 312     6962   7332  12699   1010  -3023   1279       C
ATOM   5289  C   LEU B 312    -114.615  22.432  37.546  1.00 72.93           C
ANISOU 5289  C   LEU B 312     6852   7577  13280   1052  -3071   1185       C
ATOM   5290  O   LEU B 312    -113.967  21.433  37.880  1.00 74.87           O
ANISOU 5290  O   LEU B 312     7010   7939  13500    953  -3185   1159       O
ATOM   5291  CB  LEU B 312    -113.324  23.883  39.123  1.00 72.94           C
ANISOU 5291  CB  LEU B 312     7485   7648  12581    887  -3300   1420       C
ATOM   5292  CG  LEU B 312    -112.097  24.787  39.292  1.00 72.00           C
ANISOU 5292  CG  LEU B 312     7668   7610  12077    770  -3213   1456       C
ATOM   5293  CD1 LEU B 312    -112.391  26.239  38.947  1.00 73.99           C
ANISOU 5293  CD1 LEU B 312     8128   7771  12213    806  -3008   1488       C
ATOM   5294  CD2 LEU B 312    -111.545  24.680  40.706  1.00 72.54           C
ANISOU 5294  CD2 LEU B 312     8001   7743  11817    649  -3499   1582       C
ATOM   5295  N   SER B 313    -115.826  22.344  36.995  1.00 77.35           N
ANISOU 5295  N   SER B 313     7216   8012  14162   1189  -2979   1128       N
ATOM   5296  CA  SER B 313    -116.534  21.077  36.866  1.00 83.06           C
ANISOU 5296  CA  SER B 313     7608   8720  15231   1240  -3032   1050       C
ATOM   5297  C   SER B 313    -116.458  20.490  35.462  1.00 85.04           C
ANISOU 5297  C   SER B 313     7562   9005  15745   1251  -2682    841       C
ATOM   5298  O   SER B 313    -117.207  19.559  35.153  1.00 91.08           O
ANISOU 5298  O   SER B 313     8035   9732  16839   1310  -2652    754       O
ATOM   5299  CB  SER B 313    -118.000  21.248  37.274  1.00 87.54           C
ANISOU 5299  CB  SER B 313     8140   9116  16008   1385  -3183   1125       C
ATOM   5300  OG  SER B 313    -118.747  21.884  36.251  1.00 88.46           O
ANISOU 5300  OG  SER B 313     8185   9112  16315   1503  -2907   1029       O
ATOM   5301  N   VAL B 314    -115.579  21.006  34.609  1.00 81.77           N
ANISOU 5301  N   VAL B 314     7217   8657  15193   1188  -2412    758       N
ATOM   5302  CA  VAL B 314    -115.424  20.526  33.241  1.00 81.88           C
ANISOU 5302  CA  VAL B 314     6996   8710  15406   1171  -2050    558       C
ATOM   5303  C   VAL B 314    -113.981  20.092  33.034  1.00 75.92           C
ANISOU 5303  C   VAL B 314     6252   8126  14469   1003  -1982    513       C
ATOM   5304  O   VAL B 314    -113.053  20.713  33.563  1.00 73.81           O
ANISOU 5304  O   VAL B 314     6234   7921  13891    928  -2097    612       O
ATOM   5305  CB  VAL B 314    -115.819  21.598  32.205  1.00 86.74           C
ANISOU 5305  CB  VAL B 314     7683   9221  16052   1252  -1743    475       C
ATOM   5306  CG1 VAL B 314    -117.113  21.211  31.508  1.00 88.17           C
ANISOU 5306  CG1 VAL B 314     7626   9282  16593   1371  -1571    347       C
ATOM   5307  CG2 VAL B 314    -115.946  22.963  32.870  1.00 89.60           C
ANISOU 5307  CG2 VAL B 314     8372   9495  16177   1299  -1892    634       C
ATOM   5308  N   VAL B 315    -113.796  19.031  32.246  1.00 74.45           N
ANISOU 5308  N   VAL B 315     5804   8009  14472    935  -1779    361       N
ATOM   5309  CA  VAL B 315    -112.458  18.491  32.016  1.00 70.96           C
ANISOU 5309  CA  VAL B 315     5359   7723  13881    754  -1708    312       C
ATOM   5310  C   VAL B 315    -111.619  19.466  31.198  1.00 64.67           C
ANISOU 5310  C   VAL B 315     4864   6972  12735    661  -1407    259       C
ATOM   5311  O   VAL B 315    -110.458  19.739  31.528  1.00 61.64           O
ANISOU 5311  O   VAL B 315     4746   6684  11991    527  -1448    307       O
ATOM   5312  CB  VAL B 315    -112.546  17.113  31.336  1.00 74.90           C
ANISOU 5312  CB  VAL B 315     5550   8276  14632    679  -1526    161       C
ATOM   5313  CG1 VAL B 315    -111.167  16.645  30.899  1.00 73.54           C
ANISOU 5313  CG1 VAL B 315     5397   8247  14299    473  -1392     98       C
ATOM   5314  CG2 VAL B 315    -113.187  16.103  32.273  1.00 78.16           C
ANISOU 5314  CG2 VAL B 315     5807   8670  15220    714  -1821    218       C
ATOM   5315  N   SER B 316    -112.183  19.994  30.115  1.00 62.82           N
ANISOU 5315  N   SER B 316     4612   6663  12592    723  -1099    151       N
ATOM   5316  CA  SER B 316    -111.465  20.938  29.269  1.00 60.70           C
ANISOU 5316  CA  SER B 316     4642   6430  11992    628   -826     99       C
ATOM   5317  C   SER B 316    -112.455  21.943  28.702  1.00 59.25           C
ANISOU 5317  C   SER B 316     4513   6106  11892    761   -672     60       C
ATOM   5318  O   SER B 316    -113.493  21.555  28.159  1.00 58.30           O
ANISOU 5318  O   SER B 316     4139   5891  12122    870   -539    -43       O
ATOM   5319  CB  SER B 316    -110.723  20.221  28.136  1.00 65.97           C
ANISOU 5319  CB  SER B 316     5250   7195  12620    465   -517    -49       C
ATOM   5320  OG  SER B 316    -111.625  19.734  27.159  1.00 74.74           O
ANISOU 5320  OG  SER B 316     6100   8245  14053    519   -251   -202       O
ATOM   5321  N   LYS B 317    -112.132  23.227  28.837  1.00 56.59           N
ANISOU 5321  N   LYS B 317     4500   5749  11252    749   -683    135       N
ATOM   5322  CA  LYS B 317    -112.972  24.305  28.336  1.00 57.39           C
ANISOU 5322  CA  LYS B 317     4703   5712  11390    850   -551    106       C
ATOM   5323  C   LYS B 317    -112.089  25.430  27.820  1.00 55.98           C
ANISOU 5323  C   LYS B 317     4856   5584  10828    730   -403    101       C
ATOM   5324  O   LYS B 317    -111.071  25.759  28.436  1.00 56.35           O
ANISOU 5324  O   LYS B 317     5097   5726  10589    638   -534    199       O
ATOM   5325  CB  LYS B 317    -113.909  24.849  29.423  1.00 59.67           C
ANISOU 5325  CB  LYS B 317     5012   5863  11798   1010   -839    257       C
ATOM   5326  CG  LYS B 317    -114.835  25.955  28.935  1.00 65.04           C
ANISOU 5326  CG  LYS B 317     5798   6375  12542   1113   -711    228       C
ATOM   5327  CD  LYS B 317    -115.115  26.981  30.021  1.00 70.90           C
ANISOU 5327  CD  LYS B 317     6762   7026  13152   1172   -972    419       C
ATOM   5328  CE  LYS B 317    -115.809  26.356  31.219  1.00 76.14           C
ANISOU 5328  CE  LYS B 317     7270   7618  14043   1296  -1326    563       C
ATOM   5329  NZ  LYS B 317    -116.100  27.370  32.272  1.00 76.26           N
ANISOU 5329  NZ  LYS B 317     7539   7534  13901   1332  -1570    761       N
ATOM   5330  N   VAL B 318    -112.479  26.014  26.690  1.00 55.38           N
ANISOU 5330  N   VAL B 318     4842   5440  10760    731   -133    -22       N
ATOM   5331  CA  VAL B 318    -111.825  27.221  26.201  1.00 53.68           C
ANISOU 5331  CA  VAL B 318     4931   5245  10220    634    -27    -20       C
ATOM   5332  C   VAL B 318    -112.429  28.427  26.906  1.00 54.35           C
ANISOU 5332  C   VAL B 318     5167   5209  10274    729   -180     95       C
ATOM   5333  O   VAL B 318    -113.648  28.507  27.109  1.00 59.57           O
ANISOU 5333  O   VAL B 318     5720   5718  11196    876   -226    101       O
ATOM   5334  CB  VAL B 318    -111.948  27.336  24.669  1.00 57.54           C
ANISOU 5334  CB  VAL B 318     5453   5713  10695    566    312   -202       C
ATOM   5335  CG1 VAL B 318    -111.253  26.164  23.992  1.00 56.98           C
ANISOU 5335  CG1 VAL B 318     5271   5765  10614    441    471   -299       C
ATOM   5336  CG2 VAL B 318    -113.409  27.417  24.240  1.00 67.61           C
ANISOU 5336  CG2 VAL B 318     6592   6818  12281    710    440   -306       C
ATOM   5337  N   VAL B 319    -111.573  29.362  27.307  1.00 50.96           N
ANISOU 5337  N   VAL B 319     4984   4839   9540    643   -259    191       N
ATOM   5338  CA  VAL B 319    -111.986  30.546  28.051  1.00 47.54           C
ANISOU 5338  CA  VAL B 319     4718   4307   9037    696   -397    314       C
ATOM   5339  C   VAL B 319    -111.438  31.769  27.333  1.00 41.19           C
ANISOU 5339  C   VAL B 319     4142   3515   7995    590   -247    275       C
ATOM   5340  O   VAL B 319    -110.218  31.912  27.187  1.00 42.18           O
ANISOU 5340  O   VAL B 319     4374   3772   7883    467   -221    278       O
ATOM   5341  CB  VAL B 319    -111.497  30.511  29.509  1.00 48.11           C
ANISOU 5341  CB  VAL B 319     4859   4442   8981    687   -670    488       C
ATOM   5342  CG1 VAL B 319    -111.856  31.804  30.218  1.00 51.76           C
ANISOU 5342  CG1 VAL B 319     5524   4806   9335    708   -772    615       C
ATOM   5343  CG2 VAL B 319    -112.091  29.316  30.239  1.00 47.93           C
ANISOU 5343  CG2 VAL B 319     4614   4399   9200    786   -863    535       C
ATOM   5344  N   LYS B 320    -112.333  32.645  26.885  1.00 42.26           N
ANISOU 5344  N   LYS B 320     4346   3501   8208    639   -162    238       N
ATOM   5345  CA  LYS B 320    -111.958  33.874  26.198  1.00 42.37           C
ANISOU 5345  CA  LYS B 320     4567   3505   8025    538    -43    199       C
ATOM   5346  C   LYS B 320    -111.995  35.030  27.188  1.00 43.82           C
ANISOU 5346  C   LYS B 320     4911   3636   8103    535   -198    351       C
ATOM   5347  O   LYS B 320    -113.029  35.284  27.814  1.00 52.54           O
ANISOU 5347  O   LYS B 320     6009   4593   9362    640   -299    428       O
ATOM   5348  CB  LYS B 320    -112.891  34.148  25.019  1.00 46.39           C
ANISOU 5348  CB  LYS B 320     5077   3880   8671    565    164     42       C
ATOM   5349  CG  LYS B 320    -112.833  33.102  23.919  1.00 53.69           C
ANISOU 5349  CG  LYS B 320     5874   4858   9667    536    372   -127       C
ATOM   5350  CD  LYS B 320    -113.795  33.440  22.790  1.00 65.66           C
ANISOU 5350  CD  LYS B 320     7421   6229  11299    556    597   -298       C
ATOM   5351  CE  LYS B 320    -113.770  32.379  21.701  1.00 73.51           C
ANISOU 5351  CE  LYS B 320     8301   7276  12354    511    840   -475       C
ATOM   5352  NZ  LYS B 320    -114.729  32.688  20.603  1.00 78.50           N
ANISOU 5352  NZ  LYS B 320     8978   7760  13087    524   1087   -664       N
ATOM   5353  N   VAL B 321    -110.868  35.723  27.329  1.00 41.02           N
ANISOU 5353  N   VAL B 321     4697   3392   7495    414   -211    397       N
ATOM   5354  CA  VAL B 321    -110.749  36.880  28.207  1.00 40.50           C
ANISOU 5354  CA  VAL B 321     4786   3296   7307    379   -312    527       C
ATOM   5355  C   VAL B 321    -110.272  38.059  27.372  1.00 38.68           C
ANISOU 5355  C   VAL B 321     4687   3070   6938    262   -191    465       C
ATOM   5356  O   VAL B 321    -109.349  37.918  26.561  1.00 36.64           O
ANISOU 5356  O   VAL B 321     4433   2922   6567    178   -107    381       O
ATOM   5357  CB  VAL B 321    -109.783  36.613  29.376  1.00 41.10           C
ANISOU 5357  CB  VAL B 321     4888   3505   7225    341   -453    643       C
ATOM   5358  CG1 VAL B 321    -109.755  37.803  30.325  1.00 40.71           C
ANISOU 5358  CG1 VAL B 321     5000   3415   7051    295   -525    773       C
ATOM   5359  CG2 VAL B 321    -110.179  35.345  30.114  1.00 44.09           C
ANISOU 5359  CG2 VAL B 321     5131   3891   7731    437   -596    693       C
ATOM   5360  N   THR B 322    -110.903  39.214  27.566  1.00 40.64           N
ANISOU 5360  N   THR B 322     5048   3192   7202    251   -199    513       N
ATOM   5361  CA  THR B 322    -110.523  40.422  26.844  1.00 37.71           C
ANISOU 5361  CA  THR B 322     4794   2814   6721    132   -112    461       C
ATOM   5362  C   THR B 322    -109.365  41.087  27.578  1.00 37.99           C
ANISOU 5362  C   THR B 322     4890   2970   6573     35   -171    555       C
ATOM   5363  O   THR B 322    -109.530  41.583  28.697  1.00 38.81           O
ANISOU 5363  O   THR B 322     5054   3042   6651     36   -250    682       O
ATOM   5364  CB  THR B 322    -111.711  41.369  26.715  1.00 37.08           C
ANISOU 5364  CB  THR B 322     4803   2533   6754    148    -87    461       C
ATOM   5365  OG1 THR B 322    -112.804  40.679  26.096  1.00 38.58           O
ANISOU 5365  OG1 THR B 322     4918   2596   7144    258    -19    360       O
ATOM   5366  CG2 THR B 322    -111.337  42.572  25.862  1.00 39.10           C
ANISOU 5366  CG2 THR B 322     5168   2780   6907      8     -6    390       C
ATOM   5367  N   ILE B 323    -108.190  41.083  26.953  1.00 34.59           N
ANISOU 5367  N   ILE B 323     4450   2672   6019    -48   -128    492       N
ATOM   5368  CA  ILE B 323    -106.982  41.677  27.511  1.00 34.57           C
ANISOU 5368  CA  ILE B 323     4476   2784   5875   -130   -163    552       C
ATOM   5369  C   ILE B 323    -106.369  42.571  26.444  1.00 33.55           C
ANISOU 5369  C   ILE B 323     4384   2676   5686   -240   -108    474       C
ATOM   5370  O   ILE B 323    -106.214  42.148  25.294  1.00 35.64           O
ANISOU 5370  O   ILE B 323     4643   2958   5941   -260    -63    372       O
ATOM   5371  CB  ILE B 323    -105.971  40.606  27.964  1.00 30.98           C
ANISOU 5371  CB  ILE B 323     3952   2472   5347   -107   -208    566       C
ATOM   5372  CG1 ILE B 323    -106.632  39.620  28.929  1.00 31.72           C
ANISOU 5372  CG1 ILE B 323     4002   2543   5507     -7   -292    635       C
ATOM   5373  CG2 ILE B 323    -104.758  41.254  28.614  1.00 30.21           C
ANISOU 5373  CG2 ILE B 323     3881   2471   5125   -177   -226    615       C
ATOM   5374  CD1 ILE B 323    -105.748  38.457  29.312  1.00 38.66           C
ANISOU 5374  CD1 ILE B 323     4813   3547   6328      8   -343    634       C
ATOM   5375  N   ASP B 324    -106.023  43.803  26.824  1.00 33.32           N
ANISOU 5375  N   ASP B 324     4398   2644   5619   -320   -116    524       N
ATOM   5376  CA  ASP B 324    -105.487  44.791  25.886  1.00 34.74           C
ANISOU 5376  CA  ASP B 324     4599   2833   5768   -431    -99    461       C
ATOM   5377  C   ASP B 324    -106.430  44.994  24.701  1.00 34.40           C
ANISOU 5377  C   ASP B 324     4623   2672   5776   -456    -54    362       C
ATOM   5378  O   ASP B 324    -105.996  45.124  23.555  1.00 32.18           O
ANISOU 5378  O   ASP B 324     4369   2417   5442   -527    -50    274       O
ATOM   5379  CB  ASP B 324    -104.088  44.401  25.402  1.00 37.08           C
ANISOU 5379  CB  ASP B 324     4842   3265   5983   -460   -128    424       C
ATOM   5380  CG  ASP B 324    -103.060  44.404  26.515  1.00 38.28           C
ANISOU 5380  CG  ASP B 324     4935   3517   6092   -449   -154    497       C
ATOM   5381  OD1 ASP B 324    -103.236  45.167  27.487  1.00 38.18           O
ANISOU 5381  OD1 ASP B 324     4933   3482   6090   -471   -136    567       O
ATOM   5382  OD2 ASP B 324    -102.072  43.647  26.412  1.00 37.99           O
ANISOU 5382  OD2 ASP B 324     4854   3573   6007   -427   -180    479       O
ATOM   5383  N   TYR B 325    -107.733  45.006  24.985  1.00 33.33           N
ANISOU 5383  N   TYR B 325     4528   2396   5741   -397    -26    375       N
ATOM   5384  CA  TYR B 325    -108.816  45.207  24.024  1.00 34.54           C
ANISOU 5384  CA  TYR B 325     4753   2402   5967   -403     38    272       C
ATOM   5385  C   TYR B 325    -108.965  44.067  23.026  1.00 37.50           C
ANISOU 5385  C   TYR B 325     5109   2797   6343   -357    109    151       C
ATOM   5386  O   TYR B 325    -109.690  44.218  22.035  1.00 37.17           O
ANISOU 5386  O   TYR B 325     5142   2649   6332   -383    190     31       O
ATOM   5387  CB  TYR B 325    -108.666  46.521  23.248  1.00 35.03           C
ANISOU 5387  CB  TYR B 325     4899   2421   5991   -550     37    217       C
ATOM   5388  CG  TYR B 325    -108.777  47.762  24.098  1.00 42.05           C
ANISOU 5388  CG  TYR B 325     5810   3254   6914   -617      3    317       C
ATOM   5389  CD1 TYR B 325    -109.987  48.129  24.670  1.00 41.71           C
ANISOU 5389  CD1 TYR B 325     5831   3040   6978   -581     21    368       C
ATOM   5390  CD2 TYR B 325    -107.675  48.578  24.315  1.00 43.11           C
ANISOU 5390  CD2 TYR B 325     5896   3494   6988   -721    -41    360       C
ATOM   5391  CE1 TYR B 325    -110.094  49.268  25.445  1.00 45.64           C
ANISOU 5391  CE1 TYR B 325     6366   3479   7494   -666      5    466       C
ATOM   5392  CE2 TYR B 325    -107.772  49.720  25.087  1.00 44.77           C
ANISOU 5392  CE2 TYR B 325     6115   3657   7237   -801    -42    443       C
ATOM   5393  CZ  TYR B 325    -108.983  50.061  25.650  1.00 44.56           C
ANISOU 5393  CZ  TYR B 325     6175   3465   7291   -783    -14    499       C
ATOM   5394  OH  TYR B 325    -109.084  51.196  26.420  1.00 47.02           O
ANISOU 5394  OH  TYR B 325     6513   3723   7630   -884     -1    590       O
ATOM   5395  N   THR B 326    -108.307  42.931  23.248  1.00 30.90           N
ANISOU 5395  N   THR B 326     3007   3047   5687    394   -206    553       N
ATOM   5396  CA  THR B 326    -108.455  41.778  22.375  1.00 31.53           C
ANISOU 5396  CA  THR B 326     3098   3228   5654    330   -150    488       C
ATOM   5397  C   THR B 326    -108.820  40.557  23.208  1.00 35.93           C
ANISOU 5397  C   THR B 326     3632   3701   6318    414   -102    468       C
ATOM   5398  O   THR B 326    -108.472  40.462  24.389  1.00 36.79           O
ANISOU 5398  O   THR B 326     3762   3704   6511    506   -146    564       O
ATOM   5399  CB  THR B 326    -107.176  41.512  21.556  1.00 40.22           C
ANISOU 5399  CB  THR B 326     4251   4445   6586    227   -237    666       C
ATOM   5400  OG1 THR B 326    -107.477  40.631  20.467  1.00 44.12           O
ANISOU 5400  OG1 THR B 326     4771   5128   6864     38   -156    610       O
ATOM   5401  CG2 THR B 326    -106.091  40.883  22.417  1.00 31.58           C
ANISOU 5401  CG2 THR B 326     3173   3214   5613    330   -304    824       C
ATOM   5402  N  AGLU B 327    -109.541  39.627  22.586  0.49 37.14           N
ANISOU 5402  N  AGLU B 327     3714   3944   6456    358     -2    301       N
ATOM   5403  N  BGLU B 327    -109.530  39.623  22.581  0.51 37.12           N
ANISOU 5403  N  BGLU B 327     3711   3942   6450    357     -2    302       N
ATOM   5404  CA AGLU B 327    -109.959  38.408  23.267  0.49 38.89           C
ANISOU 5404  CA AGLU B 327     3852   4109   6816    426     21    250       C
ATOM   5405  CA BGLU B 327    -109.959  38.403  23.254  0.51 38.91           C
ANISOU 5405  CA BGLU B 327     3854   4114   6817    424     22    249       C
ATOM   5406  C  AGLU B 327    -108.818  37.399  23.260  0.49 38.30           C
ANISOU 5406  C  AGLU B 327     3825   4095   6631    329     22    417       C
ATOM   5407  C  BGLU B 327    -108.821  37.390  23.258  0.51 38.31           C
ANISOU 5407  C  BGLU B 327     3826   4098   6633    328     22    416       C
ATOM   5408  O  AGLU B 327    -108.352  36.984  22.194  0.49 37.97           O
ANISOU 5408  O  AGLU B 327     3807   4222   6397    132     83    461       O
ATOM   5409  O  BGLU B 327    -108.359  36.962  22.194  0.51 37.98           O
ANISOU 5409  O  BGLU B 327     3806   4224   6398    131     85    460       O
ATOM   5410  CB AGLU B 327    -111.204  37.817  22.608  0.49 42.17           C
ANISOU 5410  CB AGLU B 327     4080   4608   7333    413    144    -70       C
ATOM   5411  CB BGLU B 327    -111.196  37.824  22.569  0.51 42.18           C
ANISOU 5411  CB BGLU B 327     4082   4617   7328    407    148    -73       C
ATOM   5412  CG AGLU B 327    -112.515  38.345  23.169  0.49 45.19           C
ANISOU 5412  CG AGLU B 327     4375   4750   8045    598     43   -238       C
ATOM   5413  CG BGLU B 327    -112.478  37.904  23.391  0.51 44.72           C
ANISOU 5413  CG BGLU B 327     4286   4693   8012    613     38   -220       C
ATOM   5414  CD AGLU B 327    -113.691  37.441  22.849  0.49 49.87           C
ANISOU 5414  CD AGLU B 327     4692   5354   8901    674    119   -602       C
ATOM   5415  CD BGLU B 327    -113.163  39.258  23.305  0.51 46.58           C
ANISOU 5415  CD BGLU B 327     4573   4751   8375    669    -46   -291       C
ATOM   5416  OE1AGLU B 327    -113.591  36.650  21.887  0.49 53.10           O
ANISOU 5416  OE1AGLU B 327     4965   6062   9147    519    344   -808       O
ATOM   5417  OE1BGLU B 327    -112.466  40.287  23.184  0.51 45.97           O
ANISOU 5417  OE1BGLU B 327     4649   4703   8114    585    -66   -125       O
ATOM   5418  OE2AGLU B 327    -114.711  37.516  23.565  0.49 51.48           O
ANISOU 5418  OE2AGLU B 327     4797   5272   9489    872    -62   -680       O
ATOM   5419  OE2BGLU B 327    -114.411  39.291  23.354  0.51 50.27           O
ANISOU 5419  OE2BGLU B 327     4900   5018   9180    797   -117   -528       O
ATOM   5420  N   ILE B 328    -108.371  37.006  24.450  1.00 37.69           N
ANISOU 5420  N   ILE B 328     3780   3880   6662    427    -66    513       N
ATOM   5421  CA  ILE B 328    -107.311  36.020  24.614  1.00 37.25           C
ANISOU 5421  CA  ILE B 328     3768   3792   6591    351   -103    631       C
ATOM   5422  C   ILE B 328    -107.943  34.701  25.036  1.00 41.11           C
ANISOU 5422  C   ILE B 328     4131   4302   7188    327    -74    522       C
ATOM   5423  O   ILE B 328    -108.685  34.647  26.025  1.00 40.80           O
ANISOU 5423  O   ILE B 328     4031   4192   7279    461   -145    445       O
ATOM   5424  CB  ILE B 328    -106.269  36.485  25.645  1.00 39.33           C
ANISOU 5424  CB  ILE B 328     4121   3904   6917    466   -211    713       C
ATOM   5425  CG1 ILE B 328    -105.635  37.805  25.203  1.00 42.99           C
ANISOU 5425  CG1 ILE B 328     4624   4365   7343    502   -249    783       C
ATOM   5426  CG2 ILE B 328    -105.198  35.424  25.830  1.00 38.42           C
ANISOU 5426  CG2 ILE B 328     4047   3675   6877    404   -283    776       C
ATOM   5427  CD1 ILE B 328    -104.842  37.699  23.919  1.00 42.09           C
ANISOU 5427  CD1 ILE B 328     4563   4269   7159    369   -326    941       C
ATOM   5428  N   SER B 329    -107.655  33.641  24.286  1.00 43.78           N
ANISOU 5428  N   SER B 329     4421   4747   7465    120      3    543       N
ATOM   5429  CA  SER B 329    -108.196  32.321  24.575  1.00 42.56           C
ANISOU 5429  CA  SER B 329     4083   4653   7434     53     46    417       C
ATOM   5430  C   SER B 329    -107.283  31.584  25.545  1.00 43.89           C
ANISOU 5430  C   SER B 329     4332   4648   7697     42    -99    521       C
ATOM   5431  O   SER B 329    -106.059  31.581  25.379  1.00 38.71           O
ANISOU 5431  O   SER B 329     3842   3864   7002    -47   -170    694       O
ATOM   5432  CB  SER B 329    -108.365  31.512  23.288  1.00 44.86           C
ANISOU 5432  CB  SER B 329     4249   5211   7583   -248    249    359       C
ATOM   5433  OG  SER B 329    -109.374  32.070  22.464  1.00 49.46           O
ANISOU 5433  OG  SER B 329     4702   5994   8097   -235    414    125       O
ATOM   5434  N   PHE B 330    -107.883  30.966  26.558  1.00 48.38           N
ANISOU 5434  N   PHE B 330     4774   5187   8419    135   -185    399       N
ATOM   5435  CA  PHE B 330    -107.165  30.162  27.533  1.00 47.12           C
ANISOU 5435  CA  PHE B 330     4667   4902   8337     97   -325    415       C
ATOM   5436  C   PHE B 330    -107.678  28.731  27.496  1.00 52.46           C
ANISOU 5436  C   PHE B 330     5099   5681   9151    -59   -313    305       C
ATOM   5437  O   PHE B 330    -108.849  28.481  27.194  1.00 60.81           O
ANISOU 5437  O   PHE B 330     5899   6895  10312    -21   -245    152       O
ATOM   5438  CB  PHE B 330    -107.324  30.722  28.952  1.00 43.35           C
ANISOU 5438  CB  PHE B 330     4273   4350   7848    288   -487    375       C
ATOM   5439  CG  PHE B 330    -106.561  31.989  29.198  1.00 41.74           C
ANISOU 5439  CG  PHE B 330     4266   4073   7520    387   -474    436       C
ATOM   5440  CD1 PHE B 330    -107.039  33.204  28.735  1.00 42.92           C
ANISOU 5440  CD1 PHE B 330     4441   4268   7600    475   -404    490       C
ATOM   5441  CD2 PHE B 330    -105.372  31.968  29.907  1.00 42.71           C
ANISOU 5441  CD2 PHE B 330     4506   4084   7639    388   -528    383       C
ATOM   5442  CE1 PHE B 330    -106.340  34.373  28.966  1.00 31.21           C
ANISOU 5442  CE1 PHE B 330     3074   2753   6030    544   -382    523       C
ATOM   5443  CE2 PHE B 330    -104.668  33.133  30.141  1.00 41.12           C
ANISOU 5443  CE2 PHE B 330     4397   3851   7375    490   -488    364       C
ATOM   5444  CZ  PHE B 330    -105.153  34.338  29.669  1.00 39.02           C
ANISOU 5444  CZ  PHE B 330     4133   3666   7026    558   -412    450       C
ATOM   5445  N   MET B 331    -106.791  27.791  27.804  1.00 48.05           N
ANISOU 5445  N   MET B 331     4588   5019   8651   -232   -389    344       N
ATOM   5446  CA  MET B 331    -107.161  26.391  27.958  1.00 49.42           C
ANISOU 5446  CA  MET B 331     4514   5284   8979   -412   -410    233       C
ATOM   5447  C   MET B 331    -107.291  26.085  29.443  1.00 45.56           C
ANISOU 5447  C   MET B 331     4018   4711   8580   -282   -663    122       C
ATOM   5448  O   MET B 331    -106.311  26.182  30.188  1.00 44.48           O
ANISOU 5448  O   MET B 331     4104   4398   8398   -277   -784    130       O
ATOM   5449  CB  MET B 331    -106.133  25.469  27.304  1.00 57.97           C
ANISOU 5449  CB  MET B 331     5659   6294  10074   -772   -361    370       C
ATOM   5450  CG  MET B 331    -106.352  25.257  25.816  1.00 66.39           C
ANISOU 5450  CG  MET B 331     6624   7602  10998  -1059   -105    461       C
ATOM   5451  SD  MET B 331    -108.017  24.667  25.444  1.00 75.15           S
ANISOU 5451  SD  MET B 331     7229   9124  12202  -1071    120    127       S
ATOM   5452  CE  MET B 331    -108.098  23.181  26.442  1.00 74.00           C
ANISOU 5452  CE  MET B 331     6819   8946  12354  -1189    -51    -10       C
ATOM   5453  N   LEU B 332    -108.497  25.723  29.868  1.00 48.59           N
ANISOU 5453  N   LEU B 332     4134   5227   9101   -180   -766     -7       N
ATOM   5454  CA  LEU B 332    -108.781  25.391  31.259  1.00 50.22           C
ANISOU 5454  CA  LEU B 332     4326   5407   9347    -98  -1074    -70       C
ATOM   5455  C   LEU B 332    -108.960  23.882  31.370  1.00 52.13           C
ANISOU 5455  C   LEU B 332     4260   5732   9814   -297  -1163   -205       C
ATOM   5456  O   LEU B 332    -109.949  23.330  30.876  1.00 54.87           O
ANISOU 5456  O   LEU B 332     4222   6232  10395   -291  -1119   -323       O
ATOM   5457  CB  LEU B 332    -110.024  26.125  31.757  1.00 50.54           C
ANISOU 5457  CB  LEU B 332     4300   5475   9427    160  -1251    -47       C
ATOM   5458  CG  LEU B 332    -110.484  25.740  33.164  1.00 54.25           C
ANISOU 5458  CG  LEU B 332     4753   5957   9903    196  -1650    -40       C
ATOM   5459  CD1 LEU B 332    -109.423  26.099  34.196  1.00 52.43           C
ANISOU 5459  CD1 LEU B 332     4889   5708   9326    104  -1722     -6       C
ATOM   5460  CD2 LEU B 332    -111.815  26.395  33.500  1.00 58.32           C
ANISOU 5460  CD2 LEU B 332     5188   6429  10543    424  -1896     60       C
ATOM   5461  N   TRP B 333    -108.005  23.222  32.014  1.00 50.51           N
ANISOU 5461  N   TRP B 333     4189   5427   9576   -476  -1283   -238       N
ATOM   5462  CA  TRP B 333    -108.082  21.796  32.296  1.00 54.72           C
ANISOU 5462  CA  TRP B 333     4450   6021  10319   -703  -1418   -372       C
ATOM   5463  C   TRP B 333    -108.359  21.604  33.779  1.00 54.88           C
ANISOU 5463  C   TRP B 333     4500   6066  10286   -624  -1807   -459       C
ATOM   5464  O   TRP B 333    -107.636  22.143  34.623  1.00 54.51           O
ANISOU 5464  O   TRP B 333     4794   5930   9986   -594  -1903   -469       O
ATOM   5465  CB  TRP B 333    -106.789  21.084  31.899  1.00 58.89           C
ANISOU 5465  CB  TRP B 333     5112   6379  10884  -1030  -1316   -350       C
ATOM   5466  CG  TRP B 333    -106.567  21.029  30.422  1.00 60.44           C
ANISOU 5466  CG  TRP B 333     5265   6609  11093  -1231   -996   -200       C
ATOM   5467  CD1 TRP B 333    -105.917  21.951  29.655  1.00 59.44           C
ANISOU 5467  CD1 TRP B 333     5425   6358  10802  -1194   -831     -7       C
ATOM   5468  CD2 TRP B 333    -106.996  19.995  29.529  1.00 64.98           C
ANISOU 5468  CD2 TRP B 333     5476   7406  11809  -1551   -808   -230       C
ATOM   5469  NE1 TRP B 333    -105.914  21.555  28.340  1.00 62.60           N
ANISOU 5469  NE1 TRP B 333     5714   6895  11177  -1495   -583    125       N
ATOM   5470  CE2 TRP B 333    -106.570  20.357  28.236  1.00 65.63           C
ANISOU 5470  CE2 TRP B 333     5695   7516  11726  -1738   -526    -23       C
ATOM   5471  CE3 TRP B 333    -107.698  18.797  29.697  1.00 70.31           C
ANISOU 5471  CE3 TRP B 333     5693   8297  12724  -1726   -851   -424       C
ATOM   5472  CZ2 TRP B 333    -106.824  19.565  27.118  1.00 70.87           C
ANISOU 5472  CZ2 TRP B 333     6086   8462  12380  -2142   -245     -4       C
ATOM   5473  CZ3 TRP B 333    -107.949  18.012  28.586  1.00 73.58           C
ANISOU 5473  CZ3 TRP B 333     5779   8979  13200  -2094   -546   -447       C
ATOM   5474  CH2 TRP B 333    -107.513  18.400  27.313  1.00 73.92           C
ANISOU 5474  CH2 TRP B 333     5999   9089  12998  -2323   -226   -237       C
ATOM   5475  N   CYS B 334    -109.407  20.848  34.093  1.00 56.14           N
ANISOU 5475  N   CYS B 334     4280   6375  10677   -604  -2038   -544       N
ATOM   5476  CA  CYS B 334    -109.784  20.585  35.472  1.00 58.51           C
ANISOU 5476  CA  CYS B 334     4589   6734  10908   -570  -2492   -578       C
ATOM   5477  C   CYS B 334    -109.965  19.091  35.682  1.00 72.11           C
ANISOU 5477  C   CYS B 334     5920   8555  12925   -793  -2693   -754       C
ATOM   5478  O   CYS B 334    -110.259  18.344  34.745  1.00 75.93           O
ANISOU 5478  O   CYS B 334     6005   9116  13730   -905  -2489   -848       O
ATOM   5479  CB  CYS B 334    -111.069  21.324  35.861  1.00 58.75           C
ANISOU 5479  CB  CYS B 334     4547   6807  10969   -274  -2756   -435       C
ATOM   5480  SG  CYS B 334    -110.977  23.116  35.681  1.00 65.04           S
ANISOU 5480  SG  CYS B 334     5772   7501  11440    -62  -2551   -217       S
ATOM   5481  N   LYS B 335    -109.790  18.666  36.931  1.00 73.64           N
ANISOU 5481  N   LYS B 335     6215   8792  12973   -896  -3086   -822       N
ATOM   5482  CA  LYS B 335    -109.882  17.255  37.288  1.00 79.09           C
ANISOU 5482  CA  LYS B 335     6553   9577  13921  -1139  -3344  -1006       C
ATOM   5483  C   LYS B 335    -110.286  17.163  38.750  1.00 81.09           C
ANISOU 5483  C   LYS B 335     6892   9954  13964  -1128  -3913   -998       C
ATOM   5484  O   LYS B 335    -109.557  17.646  39.620  1.00 81.78           O
ANISOU 5484  O   LYS B 335     7432  10042  13597  -1209  -3992  -1020       O
ATOM   5485  CB  LYS B 335    -108.549  16.542  37.052  1.00 84.45           C
ANISOU 5485  CB  LYS B 335     7370  10113  14603  -1492  -3134  -1159       C
ATOM   5486  CG  LYS B 335    -108.646  15.029  36.930  1.00 93.96           C
ANISOU 5486  CG  LYS B 335     8163  11408  16129  -1794  -3209  -1318       C
ATOM   5487  CD  LYS B 335    -108.937  14.614  35.496  1.00 99.58           C
ANISOU 5487  CD  LYS B 335     8549  12198  17090  -1882  -2762  -1269       C
ATOM   5488  CE  LYS B 335    -108.696  13.127  35.290  1.00108.31           C
ANISOU 5488  CE  LYS B 335     9402  13399  18352  -2268  -2691  -1385       C
ATOM   5489  NZ  LYS B 335    -108.788  12.744  33.853  1.00111.09           N
ANISOU 5489  NZ  LYS B 335     9503  13882  18825  -2478  -2216  -1328       N
ATOM   5490  N   ASP B 336    -111.446  16.558  39.011  1.00 84.07           N
ANISOU 5490  N   ASP B 336     6956  10468  14519  -1002  -4162   -948       N
ATOM   5491  CA  ASP B 336    -111.920  16.302  40.372  1.00 87.37           C
ANISOU 5491  CA  ASP B 336     7473  11031  14693  -1024  -4698   -875       C
ATOM   5492  C   ASP B 336    -112.039  17.594  41.181  1.00 84.28           C
ANISOU 5492  C   ASP B 336     7521  10650  13852   -921  -4956   -625       C
ATOM   5493  O   ASP B 336    -111.504  17.717  42.285  1.00 85.01           O
ANISOU 5493  O   ASP B 336     7948  10886  13466  -1140  -5232   -652       O
ATOM   5494  CB  ASP B 336    -111.017  15.290  41.084  1.00 90.83           C
ANISOU 5494  CB  ASP B 336     7971  11565  14976  -1395  -4842  -1123       C
ATOM   5495  CG  ASP B 336    -110.990  13.942  40.389  1.00 92.93           C
ANISOU 5495  CG  ASP B 336     7803  11849  15655  -1558  -4636  -1312       C
ATOM   5496  OD1 ASP B 336    -111.782  13.742  39.445  1.00 92.96           O
ANISOU 5496  OD1 ASP B 336     7431  11866  16024  -1384  -4406  -1275       O
ATOM   5497  OD2 ASP B 336    -110.175  13.083  40.786  1.00 94.46           O
ANISOU 5497  OD2 ASP B 336     8040  12061  15789  -1887  -4686  -1524       O
ATOM   5498  N   GLY B 337    -112.750  18.569  40.618  1.00 81.26           N
ANISOU 5498  N   GLY B 337     7150  10140  13584   -624  -4837   -400       N
ATOM   5499  CA  GLY B 337    -113.062  19.793  41.325  1.00 81.58           C
ANISOU 5499  CA  GLY B 337     7585  10186  13225   -546  -5078    -88       C
ATOM   5500  C   GLY B 337    -111.940  20.802  41.431  1.00 76.74           C
ANISOU 5500  C   GLY B 337     7432   9601  12123   -673  -4781   -113       C
ATOM   5501  O   GLY B 337    -112.128  21.841  42.075  1.00 72.56           O
ANISOU 5501  O   GLY B 337     7269   9144  11158   -680  -4903    143       O
ATOM   5502  N   HIS B 338    -110.783  20.535  40.834  1.00 72.93           N
ANISOU 5502  N   HIS B 338     6998   9057  11656   -778  -4296   -402       N
ATOM   5503  CA  HIS B 338    -109.678  21.480  40.810  1.00 70.95           C
ANISOU 5503  CA  HIS B 338     7169   8781  11007   -821  -3871   -481       C
ATOM   5504  C   HIS B 338    -109.125  21.561  39.395  1.00 64.27           C
ANISOU 5504  C   HIS B 338     6214   7705  10500   -712  -3352   -561       C
ATOM   5505  O   HIS B 338    -109.343  20.669  38.572  1.00 62.78           O
ANISOU 5505  O   HIS B 338     5665   7440  10748   -725  -3282   -628       O
ATOM   5506  CB  HIS B 338    -108.564  21.083  41.791  1.00 78.04           C
ANISOU 5506  CB  HIS B 338     8321   9814  11518  -1112  -3910   -802       C
ATOM   5507  CG  HIS B 338    -107.965  19.738  41.517  1.00 84.43           C
ANISOU 5507  CG  HIS B 338     8895  10508  12677  -1286  -3903  -1104       C
ATOM   5508  ND1 HIS B 338    -108.233  18.632  42.294  1.00 90.36           N
ANISOU 5508  ND1 HIS B 338     9473  11409  13449  -1500  -4348  -1232       N
ATOM   5509  CD2 HIS B 338    -107.109  19.321  40.553  1.00 84.35           C
ANISOU 5509  CD2 HIS B 338     8803  10236  13009  -1321  -3541  -1267       C
ATOM   5510  CE1 HIS B 338    -107.569  17.592  41.822  1.00 91.24           C
ANISOU 5510  CE1 HIS B 338     9394  11354  13920  -1666  -4227  -1490       C
ATOM   5511  NE2 HIS B 338    -106.881  17.983  40.765  1.00 87.07           N
ANISOU 5511  NE2 HIS B 338     8932  10563  13587  -1574  -3746  -1488       N
ATOM   5512  N   VAL B 339    -108.401  22.639  39.118  1.00 62.92           N
ANISOU 5512  N   VAL B 339     6345   7461  10101   -641  -2998   -548       N
ATOM   5513  CA  VAL B 339    -107.832  22.838  37.791  1.00 63.73           C
ANISOU 5513  CA  VAL B 339     6401   7353  10459   -560  -2568   -561       C
ATOM   5514  C   VAL B 339    -106.534  22.052  37.672  1.00 65.19           C
ANISOU 5514  C   VAL B 339     6638   7378  10753   -764  -2441   -819       C
ATOM   5515  O   VAL B 339    -105.781  21.899  38.642  1.00 63.53           O
ANISOU 5515  O   VAL B 339     6620   7193  10325   -897  -2549  -1061       O
ATOM   5516  CB  VAL B 339    -107.608  24.335  37.500  1.00 61.68           C
ANISOU 5516  CB  VAL B 339     6401   7058   9977   -390  -2301   -429       C
ATOM   5517  CG1 VAL B 339    -108.860  25.132  37.800  1.00 67.04           C
ANISOU 5517  CG1 VAL B 339     7082   7843  10545   -242  -2494   -162       C
ATOM   5518  CG2 VAL B 339    -106.429  24.877  38.284  1.00 59.16           C
ANISOU 5518  CG2 VAL B 339     6395   6769   9313   -474  -2194   -639       C
ATOM   5519  N   GLU B 340    -106.286  21.525  36.475  1.00 70.81           N
ANISOU 5519  N   GLU B 340     7178   7924  11804   -824  -2225   -778       N
ATOM   5520  CA  GLU B 340    -104.995  20.941  36.130  1.00 74.33           C
ANISOU 5520  CA  GLU B 340     7720   8104  12417  -1023  -2108   -920       C
ATOM   5521  C   GLU B 340    -104.031  22.026  35.658  1.00 66.02           C
ANISOU 5521  C   GLU B 340     6951   6839  11296   -884  -1859   -878       C
ATOM   5522  O   GLU B 340    -102.961  22.220  36.244  1.00 63.72           O
ANISOU 5522  O   GLU B 340     6872   6376  10964   -891  -1875  -1114       O
ATOM   5523  CB  GLU B 340    -105.170  19.870  35.047  1.00 85.41           C
ANISOU 5523  CB  GLU B 340     8825   9458  14170  -1244  -2012   -825       C
ATOM   5524  CG  GLU B 340    -105.695  18.532  35.542  1.00 97.07           C
ANISOU 5524  CG  GLU B 340     9978  11075  15830  -1464  -2266   -967       C
ATOM   5525  CD  GLU B 340    -104.586  17.517  35.750  1.00108.73           C
ANISOU 5525  CD  GLU B 340    11523  12303  17487  -1799  -2353  -1146       C
ATOM   5526  OE1 GLU B 340    -104.189  17.295  36.913  1.00113.76           O
ANISOU 5526  OE1 GLU B 340    12296  12917  18010  -1847  -2607  -1406       O
ATOM   5527  OE2 GLU B 340    -104.104  16.949  34.747  1.00112.98           O
ANISOU 5527  OE2 GLU B 340    11995  12667  18266  -2051  -2177  -1028       O
ATOM   5528  N   THR B 341    -104.405  22.741  34.600  1.00 58.76           N
ANISOU 5528  N   THR B 341     6002   5933  10392   -749  -1643   -626       N
ATOM   5529  CA  THR B 341    -103.615  23.851  34.093  1.00 57.53           C
ANISOU 5529  CA  THR B 341     6068   5607  10184   -600  -1453   -552       C
ATOM   5530  C   THR B 341    -104.562  24.900  33.530  1.00 57.39           C
ANISOU 5530  C   THR B 341     6011   5776  10018   -400  -1311   -339       C
ATOM   5531  O   THR B 341    -105.746  24.642  33.298  1.00 58.43           O
ANISOU 5531  O   THR B 341     5926   6095  10179   -384  -1337   -255       O
ATOM   5532  CB  THR B 341    -102.614  23.394  33.026  1.00 59.10           C
ANISOU 5532  CB  THR B 341     6315   5481  10658   -767  -1374   -437       C
ATOM   5533  OG1 THR B 341    -101.847  24.518  32.577  1.00 60.20           O
ANISOU 5533  OG1 THR B 341     6644   5442  10789   -588  -1269   -359       O
ATOM   5534  CG2 THR B 341    -103.344  22.781  31.841  1.00 56.64           C
ANISOU 5534  CG2 THR B 341     5786   5306  10427   -955  -1252   -195       C
ATOM   5535  N   PHE B 342    -104.019  26.099  33.313  1.00 53.74           N
ANISOU 5535  N   PHE B 342     5728   5237   9452   -239  -1177   -294       N
ATOM   5536  CA  PHE B 342    -104.807  27.206  32.774  1.00 50.27           C
ANISOU 5536  CA  PHE B 342     5279   4936   8884    -71  -1049   -114       C
ATOM   5537  C   PHE B 342    -103.823  28.184  32.134  1.00 53.00           C
ANISOU 5537  C   PHE B 342     5775   5118   9243     22   -908    -56       C
ATOM   5538  O   PHE B 342    -103.251  29.030  32.826  1.00 58.64           O
ANISOU 5538  O   PHE B 342     6605   5824   9852    139   -888   -192       O
ATOM   5539  CB  PHE B 342    -105.641  27.869  33.857  1.00 48.08           C
ANISOU 5539  CB  PHE B 342     5040   4865   8362     38  -1157   -135       C
ATOM   5540  CG  PHE B 342    -106.490  29.001  33.361  1.00 47.26           C
ANISOU 5540  CG  PHE B 342     4934   4839   8183    187  -1066     47       C
ATOM   5541  CD1 PHE B 342    -107.641  28.752  32.634  1.00 49.84           C
ANISOU 5541  CD1 PHE B 342     5059   5208   8670    230  -1075    143       C
ATOM   5542  CD2 PHE B 342    -106.139  30.313  33.625  1.00 46.43           C
ANISOU 5542  CD2 PHE B 342     4993   4766   7884    273   -965     68       C
ATOM   5543  CE1 PHE B 342    -108.427  29.794  32.177  1.00 51.22           C
ANISOU 5543  CE1 PHE B 342     5234   5401   8827    365  -1013    255       C
ATOM   5544  CE2 PHE B 342    -106.920  31.358  33.171  1.00 44.35           C
ANISOU 5544  CE2 PHE B 342     4730   4543   7577    373   -904    232       C
ATOM   5545  CZ  PHE B 342    -108.065  31.099  32.447  1.00 47.73           C
ANISOU 5545  CZ  PHE B 342     4995   4960   8182    424   -942    325       C
ATOM   5546  N   TYR B 343    -103.638  28.059  30.824  1.00 49.19           N
ANISOU 5546  N   TYR B 343     5268   4544   8878    -59   -819    136       N
ATOM   5547  CA  TYR B 343    -102.619  28.814  30.117  1.00 46.23           C
ANISOU 5547  CA  TYR B 343     5023   3970   8573     -1   -784    242       C
ATOM   5548  C   TYR B 343    -103.214  29.524  28.913  1.00 42.85           C
ANISOU 5548  C   TYR B 343     4570   3688   8024      7   -654    462       C
ATOM   5549  O   TYR B 343    -104.242  29.096  28.378  1.00 42.06           O
ANISOU 5549  O   TYR B 343     4334   3793   7855    -94   -562    509       O
ATOM   5550  CB  TYR B 343    -101.481  27.891  29.656  1.00 48.65           C
ANISOU 5550  CB  TYR B 343     5398   3946   9140   -191   -906    314       C
ATOM   5551  CG  TYR B 343    -101.927  26.762  28.754  1.00 46.96           C
ANISOU 5551  CG  TYR B 343     5093   3810   8938   -511   -870    512       C
ATOM   5552  CD1 TYR B 343    -102.372  25.558  29.286  1.00 48.19           C
ANISOU 5552  CD1 TYR B 343     5106   4044   9160   -682   -906    382       C
ATOM   5553  CD2 TYR B 343    -101.893  26.895  27.371  1.00 46.10           C
ANISOU 5553  CD2 TYR B 343     5022   3747   8748   -686   -795    813       C
ATOM   5554  CE1 TYR B 343    -102.775  24.521  28.468  1.00 48.52           C
ANISOU 5554  CE1 TYR B 343     5000   4214   9222  -1012   -828    518       C
ATOM   5555  CE2 TYR B 343    -102.295  25.862  26.545  1.00 48.52           C
ANISOU 5555  CE2 TYR B 343     5221   4215   8999  -1052   -700    958       C
ATOM   5556  CZ  TYR B 343    -102.734  24.677  27.100  1.00 48.66           C
ANISOU 5556  CZ  TYR B 343     5053   4315   9121  -1211   -696    796       C
ATOM   5557  OH  TYR B 343    -103.136  23.643  26.287  1.00 51.87           O
ANISOU 5557  OH  TYR B 343     5289   4937   9483  -1610   -558    897       O
ATOM   5558  N   PRO B 344    -102.593  30.614  28.466  1.00 44.93           N
ANISOU 5558  N   PRO B 344     4927   3863   8281    127   -647    546       N
ATOM   5559  CA  PRO B 344    -103.055  31.265  27.238  1.00 48.07           C
ANISOU 5559  CA  PRO B 344     5321   4405   8540     87   -552    741       C
ATOM   5560  C   PRO B 344    -102.568  30.517  26.009  1.00 58.13           C
ANISOU 5560  C   PRO B 344     6648   5611   9826   -198   -592    991       C
ATOM   5561  O   PRO B 344    -101.456  29.987  25.979  1.00 60.12           O
ANISOU 5561  O   PRO B 344     7003   5564  10276   -294   -765   1098       O
ATOM   5562  CB  PRO B 344    -102.432  32.663  27.325  1.00 42.06           C
ANISOU 5562  CB  PRO B 344     4619   3568   7795    296   -585    732       C
ATOM   5563  CG  PRO B 344    -101.193  32.459  28.119  1.00 38.13           C
ANISOU 5563  CG  PRO B 344     4158   2788   7541    387   -717    586       C
ATOM   5564  CD  PRO B 344    -101.501  31.367  29.114  1.00 39.43           C
ANISOU 5564  CD  PRO B 344     4298   2973   7712    312   -719    402       C
ATOM   5565  N   LYS B 345    -103.422  30.465  24.993  1.00 70.14           N
ANISOU 5565  N   LYS B 345     8102   7415  11134   -366   -436   1072       N
ATOM   5566  CA  LYS B 345    -103.003  29.883  23.731  1.00 79.48           C
ANISOU 5566  CA  LYS B 345     9360   8641  12196   -728   -443   1347       C
ATOM   5567  C   LYS B 345    -101.988  30.785  23.037  1.00 86.51           C
ANISOU 5567  C   LYS B 345    10447   9352  13070   -713   -644   1620       C
ATOM   5568  O   LYS B 345    -101.936  32.001  23.252  1.00 85.30           O
ANISOU 5568  O   LYS B 345    10299   9174  12936   -434   -681   1544       O
ATOM   5569  CB  LYS B 345    -104.200  29.646  22.810  1.00 81.21           C
ANISOU 5569  CB  LYS B 345     9421   9296  12140   -939   -171   1266       C
ATOM   5570  CG  LYS B 345    -105.034  28.429  23.161  1.00 81.66           C
ANISOU 5570  CG  LYS B 345     9224   9528  12277  -1061    -13   1049       C
ATOM   5571  CD  LYS B 345    -105.518  27.736  21.897  1.00 85.09           C
ANISOU 5571  CD  LYS B 345     9525  10356  12448  -1490    238   1065       C
ATOM   5572  CE  LYS B 345    -106.912  27.155  22.067  1.00 83.54           C
ANISOU 5572  CE  LYS B 345     8932  10465  12342  -1443    482    658       C
ATOM   5573  NZ  LYS B 345    -107.405  26.540  20.802  1.00 85.33           N
ANISOU 5573  NZ  LYS B 345     8967  11166  12289  -1880    808    563       N
ATOM   5574  N   LEU B 346    -101.175  30.160  22.182  1.00 91.34           N
ANISOU 5574  N   LEU B 346    11211   9837  13658  -1053   -806   1969       N
ATOM   5575  CA  LEU B 346    -100.136  30.887  21.462  1.00 93.01           C
ANISOU 5575  CA  LEU B 346    11611   9823  13904  -1068  -1110   2305       C
ATOM   5576  C   LEU B 346    -100.718  31.922  20.504  1.00 91.43           C
ANISOU 5576  C   LEU B 346    11419   9990  13331  -1104  -1018   2356       C
ATOM   5577  O   LEU B 346    -100.089  32.960  20.269  1.00 92.45           O
ANISOU 5577  O   LEU B 346    11613   9971  13543   -932  -1255   2482       O
ATOM   5578  CB  LEU B 346     -99.237  29.899  20.709  1.00 98.04           C
ANISOU 5578  CB  LEU B 346    12446  10233  14570  -1509  -1361   2756       C
ATOM   5579  CG  LEU B 346     -99.774  28.498  20.381  1.00100.95           C
ANISOU 5579  CG  LEU B 346    12774  10855  14726  -1989  -1138   2814       C
ATOM   5580  CD1 LEU B 346     -99.171  28.010  19.073  1.00105.49           C
ANISOU 5580  CD1 LEU B 346    13588  11465  15027  -2563  -1324   3365       C
ATOM   5581  CD2 LEU B 346     -99.480  27.504  21.505  1.00102.19           C
ANISOU 5581  CD2 LEU B 346    12856  10683  15287  -1919  -1181   2625       C
ATOM   5582  N   GLN B 347    -101.910  31.660  19.958  1.00 91.54           N
ANISOU 5582  N   GLN B 347    11329  10477  12976  -1318   -686   2206       N
ATOM   5583  CA  GLN B 347    -102.623  32.533  19.010  1.00 93.10           C
ANISOU 5583  CA  GLN B 347    11514  11068  12792  -1399   -549   2148       C
ATOM   5584  C   GLN B 347    -102.272  34.014  19.075  1.00 90.49           C
ANISOU 5584  C   GLN B 347    11224  10605  12554  -1084   -746   2156       C
ATOM   5585  O   GLN B 347    -102.552  34.762  18.142  1.00 91.27           O
ANISOU 5585  O   GLN B 347    11366  10971  12341  -1213   -745   2196       O
ATOM   5586  CB  GLN B 347    -104.134  32.396  19.216  1.00 94.22           C
ANISOU 5586  CB  GLN B 347    11406  11556  12836  -1326   -155   1691       C
ATOM   5587  CG  GLN B 347    -104.821  31.517  18.196  1.00 97.71           C
ANISOU 5587  CG  GLN B 347    11757  12463  12904  -1785    134   1619       C
ATOM   5588  CD  GLN B 347    -106.250  31.205  18.579  1.00 95.05           C
ANISOU 5588  CD  GLN B 347    11089  12357  12667  -1632    472   1104       C
ATOM   5589  OE1 GLN B 347    -106.645  31.368  19.734  1.00 89.17           O
ANISOU 5589  OE1 GLN B 347    10226  11368  12286  -1232    429    906       O
ATOM   5590  NE2 GLN B 347    -107.036  30.753  17.610  1.00 99.15           N
ANISOU 5590  NE2 GLN B 347    11443  13358  12872  -1965    791    872       N
TER    5591      GLN B 347
HETATM 5592  C1  GOL A 401     -84.903  36.516 -16.457  1.00 61.23           C
HETATM 5593  O1  GOL A 401     -84.602  35.194 -16.136  1.00 65.57           O
HETATM 5594  C2  GOL A 401     -84.868  37.318 -15.134  1.00 59.32           C
HETATM 5595  O2  GOL A 401     -83.585  37.415 -14.616  1.00 50.98           O
HETATM 5596  C3  GOL A 401     -85.465  38.701 -15.488  1.00 67.18           C
HETATM 5597  O3  GOL A 401     -85.226  39.532 -14.395  1.00 70.21           O
HETATM 5598  C1  GOL A 402    -113.490  36.978 -25.759  1.00 61.54           C
HETATM 5599  O1  GOL A 402    -112.296  36.471 -26.271  1.00 58.12           O
HETATM 5600  C2  GOL A 402    -113.342  38.517 -25.699  1.00 59.84           C
HETATM 5601  O2  GOL A 402    -112.417  38.918 -24.746  1.00 56.28           O
HETATM 5602  C3  GOL A 402    -114.765  39.048 -25.398  1.00 60.57           C
HETATM 5603  O3  GOL A 402    -115.284  39.514 -26.604  1.00 61.32           O
HETATM 5604 MG    MG A 403     -73.914  59.912 -36.300  1.00 49.76          MG
HETATM 5605  C1  GOL A 404    -106.503  56.666  -9.689  1.00 79.85           C
HETATM 5606  O1  GOL A 404    -105.747  55.697 -10.351  1.00 79.48           O
HETATM 5607  C2  GOL A 404    -106.136  56.594  -8.186  1.00 80.65           C
HETATM 5608  O2  GOL A 404    -106.928  55.683  -7.502  1.00 78.07           O
HETATM 5609  C3  GOL A 404    -104.640  56.200  -8.161  1.00 84.17           C
HETATM 5610  O3  GOL A 404    -103.999  56.989  -9.115  1.00 85.24           O
HETATM 5611  C1  GOL A 405     -89.954  48.000 -28.620  1.00 77.67           C
HETATM 5612  O1  GOL A 405     -90.445  47.561 -29.848  1.00 77.81           O
HETATM 5613  C2  GOL A 405     -91.061  48.867 -27.976  1.00 75.76           C
HETATM 5614  O2  GOL A 405     -91.629  48.248 -26.872  1.00 74.89           O
HETATM 5615  C3  GOL A 405     -90.362  50.201 -27.613  1.00 73.76           C
HETATM 5616  O3  GOL A 405     -91.365  51.163 -27.491  1.00 69.40           O
HETATM 5617  C   ACY A 406     -84.687  52.611 -29.533  1.00 62.72           C
HETATM 5618  O   ACY A 406     -85.202  52.379 -30.618  1.00 62.59           O
HETATM 5619  OXT ACY A 406     -85.083  53.506 -28.701  1.00 61.39           O
HETATM 5620  CH3 ACY A 406     -83.467  51.826 -29.038  1.00 61.36           C
HETATM 5621  C1  GOL B 401    -102.708  38.609  19.263  1.00 65.38           C
HETATM 5622  O1  GOL B 401    -104.092  38.712  19.389  1.00 66.88           O
HETATM 5623  C2  GOL B 401    -102.093  39.462  20.395  1.00 60.28           C
HETATM 5624  O2  GOL B 401    -101.313  38.700  21.256  1.00 53.91           O
HETATM 5625  C3  GOL B 401    -101.275  40.554  19.665  1.00 59.16           C
HETATM 5626  O3  GOL B 401    -101.035  41.573  20.590  1.00 50.58           O
HETATM 5627  C1  GOL B 402     -92.149  45.152  27.149  1.00 81.03           C
HETATM 5628  O1  GOL B 402     -92.918  44.130  27.697  1.00 79.72           O
HETATM 5629  C2  GOL B 402     -91.067  45.521  28.189  1.00 82.30           C
HETATM 5630  O2  GOL B 402     -90.071  44.559  28.263  1.00 81.86           O
HETATM 5631  C3  GOL B 402     -90.523  46.893  27.725  1.00 82.86           C
HETATM 5632  O3  GOL B 402     -91.628  47.665  27.374  1.00 83.39           O
HETATM 5633  C1  GOL B 403    -108.092  46.921   9.926  1.00 75.79           C
HETATM 5634  O1  GOL B 403    -109.027  46.893  10.956  1.00 73.13           O
HETATM 5635  C2  GOL B 403    -108.876  46.920   8.591  1.00 81.11           C
HETATM 5636  O2  GOL B 403    -108.096  46.473   7.536  1.00 80.59           O
HETATM 5637  C3  GOL B 403    -109.341  48.385   8.391  1.00 85.66           C
HETATM 5638  O3  GOL B 403    -110.636  48.476   8.889  1.00 89.22           O
HETATM 5639 CL    CL B 404    -118.837  64.011  27.265  1.00 49.72          CL
HETATM 5640  C1  GOL B 405     -81.071  53.921  15.303  1.00 69.26           C
HETATM 5641  O1  GOL B 405     -80.463  54.935  14.564  1.00 70.29           O
HETATM 5642  C2  GOL B 405     -80.538  52.577  14.752  1.00 69.69           C
HETATM 5643  O2  GOL B 405     -79.409  52.752  13.964  1.00 67.55           O
HETATM 5644  C3  GOL B 405     -81.722  51.965  13.959  1.00 68.65           C
HETATM 5645  O3  GOL B 405     -82.833  51.980  14.801  1.00 67.28           O
HETATM 5646  C1 AGOL B 406    -113.732  39.181  29.278  0.58 60.14           C
HETATM 5647  C1 BGOL B 406    -114.975  39.539  28.330  0.42 63.68           C
HETATM 5648  O1 AGOL B 406    -113.565  39.994  30.386  0.58 54.46           O
HETATM 5649  O1 BGOL B 406    -114.771  40.789  27.747  0.42 64.71           O
HETATM 5650  C2 AGOL B 406    -114.936  39.731  28.493  0.58 63.89           C
HETATM 5651  C2 BGOL B 406    -115.175  38.531  27.175  0.42 63.75           C
HETATM 5652  O2 AGOL B 406    -114.721  41.030  28.051  0.58 65.10           O
HETATM 5653  O2 BGOL B 406    -113.980  38.223  26.542  0.42 61.86           O
HETATM 5654  C3 AGOL B 406    -115.101  38.735  27.331  0.58 63.97           C
HETATM 5655  C3 BGOL B 406    -116.182  39.216  26.222  0.42 64.13           C
HETATM 5656  O3 AGOL B 406    -116.196  39.154  26.592  0.58 64.60           O
HETATM 5657  O3 BGOL B 406    -117.390  39.305  26.911  0.42 63.71           O
HETATM 5658  C   ACY B 407    -107.662  59.230  31.232  1.00 63.74           C
HETATM 5659  O   ACY B 407    -107.970  58.200  30.647  1.00 64.31           O
HETATM 5660  OXT ACY B 407    -106.916  60.160  30.752  1.00 64.45           O
HETATM 5661  CH3 ACY B 407    -108.153  59.526  32.656  1.00 57.87           C
HETATM 5662  C   ACY B 408    -113.789  17.769  36.474  1.00 92.05           C
HETATM 5663  O   ACY B 408    -113.059  17.752  35.493  1.00 94.87           O
HETATM 5664  OXT ACY B 408    -113.562  18.426  37.554  1.00 93.60           O
HETATM 5665  CH3 ACY B 408    -115.104  16.976  36.514  1.00 90.75           C
HETATM 5666  O   HOH A 501    -112.637  49.052  -7.815  1.00 45.47           O
HETATM 5667  O   HOH A 502     -99.477  49.981 -27.418  1.00 32.27           O
HETATM 5668  O   HOH A 503    -103.954  74.414 -39.714  1.00 41.10           O
HETATM 5669  O   HOH A 504    -103.341  47.593 -26.378  1.00 35.23           O
HETATM 5670  O   HOH A 505    -105.553  38.161 -27.762  1.00 37.08           O
HETATM 5671  O   HOH A 506    -109.373  63.591 -28.404  1.00 38.33           O
HETATM 5672  O   HOH A 507     -95.518  41.445 -22.256  1.00 31.32           O
HETATM 5673  O   HOH A 508    -115.097  37.643 -18.558  1.00 52.63           O
HETATM 5674  O   HOH A 509     -85.553  58.528 -20.714  1.00 30.89           O
HETATM 5675  O   HOH A 510     -94.083  47.461 -41.852  1.00 54.85           O
HETATM 5676  O   HOH A 511     -82.900  21.943  -9.423  1.00 40.29           O
HETATM 5677  O   HOH A 512     -73.961  72.997 -27.191  1.00 46.33           O
HETATM 5678  O   HOH A 513     -86.839  61.610 -46.757  1.00 34.81           O
HETATM 5679  O   HOH A 514     -92.774  51.672 -17.725  1.00 34.63           O
HETATM 5680  O   HOH A 515    -103.585  59.898 -18.741  1.00 34.90           O
HETATM 5681  O   HOH A 516     -84.232  24.735  -1.356  1.00 36.13           O
HETATM 5682  O   HOH A 517    -102.814  41.381  -9.645  1.00 39.82           O
HETATM 5683  O   HOH A 518    -102.562  55.945 -10.995  1.00 45.65           O
HETATM 5684  O   HOH A 519     -94.845  37.656 -20.290  1.00 26.51           O
HETATM 5685  O   HOH A 520     -86.749  48.169 -12.073  1.00 37.93           O
HETATM 5686  O   HOH A 521    -119.074  47.039 -27.381  1.00 46.99           O
HETATM 5687  O   HOH A 522     -91.814  53.560 -24.094  1.00 36.54           O
HETATM 5688  O   HOH A 523    -104.829  46.704 -28.682  1.00 30.82           O
HETATM 5689  O   HOH A 524     -99.400  56.853 -34.971  1.00 37.75           O
HETATM 5690  O   HOH A 525     -86.980  45.412  -1.072  1.00 33.14           O
HETATM 5691  O   HOH A 526    -111.399  44.891   1.624  1.00 60.32           O
HETATM 5692  O   HOH A 527     -72.448  68.959 -28.598  1.00 32.32           O
HETATM 5693  O   HOH A 528     -84.138  44.011 -19.627  1.00 49.21           O
HETATM 5694  O   HOH A 529     -72.209  69.505 -38.174  1.00 37.10           O
HETATM 5695  O   HOH A 530    -100.841  67.339 -21.364  1.00 50.20           O
HETATM 5696  O   HOH A 531     -86.395  42.888 -20.296  1.00 48.05           O
HETATM 5697  O   HOH A 532     -99.707  79.585 -33.464  1.00 41.16           O
HETATM 5698  O   HOH A 533     -77.783  71.913 -34.568  1.00 31.00           O
HETATM 5699  O   HOH A 534    -105.537  43.378   2.519  1.00 47.33           O
HETATM 5700  O   HOH A 535     -88.073  48.583  -1.394  1.00 43.18           O
HETATM 5701  O   HOH A 536    -102.522  80.387 -33.193  1.00 48.43           O
HETATM 5702  O   HOH A 537     -90.499  48.304 -36.751  1.00 47.31           O
HETATM 5703  O   HOH A 538     -78.937  26.776  -6.060  1.00 48.11           O
HETATM 5704  O   HOH A 539     -96.910  50.709 -14.365  1.00 69.58           O
HETATM 5705  O   HOH A 540     -92.982  54.627 -26.216  1.00 36.77           O
HETATM 5706  O   HOH A 541     -99.927  73.062 -46.734  1.00 55.23           O
HETATM 5707  O   HOH A 542     -93.599  50.896 -25.874  1.00 39.14           O
HETATM 5708  O   HOH A 543     -96.174  55.552 -18.890  1.00 25.26           O
HETATM 5709  O   HOH A 544    -101.529  74.161 -42.479  1.00 48.51           O
HETATM 5710  O   HOH A 545     -73.753  67.060 -24.619  1.00 32.26           O
HETATM 5711  O   HOH A 546     -71.644  35.206  -4.272  1.00 39.50           O
HETATM 5712  O   HOH A 547     -91.226  53.051 -29.392  1.00 50.26           O
HETATM 5713  O   HOH A 548     -97.352  39.029 -22.294  1.00 30.08           O
HETATM 5714  O   HOH A 549    -107.122  67.861 -40.010  1.00 34.57           O
HETATM 5715  O   HOH A 550    -108.285  34.603  -5.716  1.00 54.04           O
HETATM 5716  O   HOH A 551     -98.844  56.931 -46.694  1.00 54.37           O
HETATM 5717  O   HOH A 552     -84.419  40.815  -1.716  1.00 29.75           O
HETATM 5718  O   HOH A 553    -106.205  72.878 -33.970  1.00 28.35           O
HETATM 5719  O   HOH A 554     -97.382  45.069 -21.296  1.00 35.45           O
HETATM 5720  O   HOH A 555     -91.322  46.631 -32.231  1.00 50.81           O
HETATM 5721  O   HOH A 556     -85.683  53.138 -25.511  1.00 51.03           O
HETATM 5722  O   HOH A 557     -98.099  33.272  -2.421  1.00 37.39           O
HETATM 5723  O   HOH A 558    -101.411  62.886 -43.212  1.00 42.50           O
HETATM 5724  O   HOH A 559     -83.648  50.151 -38.806  1.00 40.44           O
HETATM 5725  O   HOH A 560     -96.329  42.559 -20.027  1.00 27.39           O
HETATM 5726  O   HOH A 561     -99.613  44.806  -1.512  1.00 36.64           O
HETATM 5727  O   HOH A 562     -97.096  32.889 -15.591  1.00 46.89           O
HETATM 5728  O   HOH A 563    -100.211  43.709 -12.516  1.00 25.13           O
HETATM 5729  O   HOH A 564     -86.453  41.759 -11.893  1.00 27.47           O
HETATM 5730  O   HOH A 565     -93.340  56.973 -28.748  1.00 27.24           O
HETATM 5731  O   HOH A 566    -118.306  37.972 -17.605  1.00 57.14           O
HETATM 5732  O   HOH A 567     -95.310  24.959 -19.932  1.00 48.48           O
HETATM 5733  O   HOH A 568    -102.781  34.432  -3.519  1.00 41.53           O
HETATM 5734  O   HOH A 569     -97.189  78.909 -32.257  1.00 43.75           O
HETATM 5735  O   HOH A 570    -103.749  75.464 -33.415  1.00 36.80           O
HETATM 5736  O   HOH A 571     -90.743  70.950 -44.057  1.00 37.02           O
HETATM 5737  O   HOH A 572     -85.571  27.481   1.407  1.00 28.11           O
HETATM 5738  O   HOH A 573     -92.320  47.967  -9.980  1.00 36.74           O
HETATM 5739  O   HOH A 574     -88.247  58.910 -21.310  1.00 38.60           O
HETATM 5740  O   HOH A 575     -87.692  41.014 -16.995  1.00 36.85           O
HETATM 5741  O   HOH A 576     -76.691  37.990  -0.244  1.00 43.45           O
HETATM 5742  O   HOH A 577    -101.591  60.114 -45.365  1.00 52.18           O
HETATM 5743  O   HOH A 578     -89.836  47.696  -8.184  1.00 24.71           O
HETATM 5744  O   HOH A 579    -102.219  35.380 -15.726  1.00 48.63           O
HETATM 5745  O   HOH A 580    -111.168  56.153 -28.872  1.00 42.87           O
HETATM 5746  O   HOH A 581     -90.836  32.222 -15.577  1.00 57.08           O
HETATM 5747  O   HOH A 582     -97.121  40.489 -18.333  1.00 30.03           O
HETATM 5748  O   HOH A 583    -103.413  59.396 -40.916  1.00 50.01           O
HETATM 5749  O   HOH A 584    -108.629  61.356 -39.992  1.00 46.39           O
HETATM 5750  O   HOH A 585    -103.045  56.780 -34.287  1.00 44.40           O
HETATM 5751  O   HOH A 586    -101.305  48.140  -7.017  1.00 45.50           O
HETATM 5752  O   HOH A 587     -90.134  74.307 -43.622  1.00 46.72           O
HETATM 5753  O   HOH A 588     -99.228  57.959 -17.857  1.00 53.79           O
HETATM 5754  O   HOH A 589     -86.898  71.675 -31.554  1.00 41.32           O
HETATM 5755  O   HOH A 590    -101.173  54.056  -9.418  1.00 63.72           O
HETATM 5756  O   HOH A 591     -86.742  75.731 -38.114  1.00 47.71           O
HETATM 5757  O   HOH A 592    -121.030  49.895 -11.080  1.00 57.71           O
HETATM 5758  O   HOH A 593    -100.835  48.004 -26.639  1.00 28.50           O
HETATM 5759  O   HOH A 594     -96.781  83.461 -37.155  1.00 38.59           O
HETATM 5760  O   HOH A 595     -78.941  70.411 -24.232  1.00 54.84           O
HETATM 5761  O   HOH A 596    -100.982  50.862 -15.078  1.00 26.63           O
HETATM 5762  O   HOH A 597     -99.526  31.426 -14.014  1.00 62.08           O
HETATM 5763  O   HOH A 598     -80.561  65.797 -40.821  1.00 44.10           O
HETATM 5764  O   HOH A 599     -96.958  66.408 -22.174  1.00 38.03           O
HETATM 5765  O   HOH A 600     -92.167  61.791 -20.575  1.00 39.22           O
HETATM 5766  O   HOH A 601     -80.904  72.747 -27.798  1.00 52.06           O
HETATM 5767  O   HOH A 602     -91.825  57.710 -35.952  1.00 42.33           O
HETATM 5768  O   HOH A 603     -82.850  62.232 -39.915  1.00 37.55           O
HETATM 5769  O   HOH A 604    -101.127  73.957 -39.965  1.00 47.80           O
HETATM 5770  O   HOH A 605    -101.402  43.684 -10.064  1.00 28.39           O
HETATM 5771  O   HOH A 606     -93.881  54.261 -29.108  1.00 30.95           O
HETATM 5772  O   HOH A 607    -103.629  36.746 -39.595  1.00 49.57           O
HETATM 5773  O   HOH A 608     -77.473  68.693 -40.173  1.00 43.06           O
HETATM 5774  O   HOH A 609     -81.123  73.985 -34.687  1.00 41.48           O
HETATM 5775  O   HOH A 610    -107.232  58.544 -17.973  1.00 46.10           O
HETATM 5776  O   HOH A 611     -99.633  50.417  -9.092  1.00 39.45           O
HETATM 5777  O   HOH A 612     -99.903  52.732 -28.716  1.00 31.97           O
HETATM 5778  O   HOH A 613     -97.817  44.068 -11.696  1.00 29.18           O
HETATM 5779  O   HOH A 614     -99.551  19.046 -10.982  1.00 37.06           O
HETATM 5780  O   HOH A 615     -72.203  37.166  -1.196  1.00 37.04           O
HETATM 5781  O   HOH A 616     -85.270  46.409 -19.835  1.00 42.74           O
HETATM 5782  O   HOH A 617    -108.170  58.798 -20.735  1.00 65.27           O
HETATM 5783  O   HOH A 618    -109.758  57.547 -31.502  1.00 64.25           O
HETATM 5784  O   HOH A 619     -77.129  54.236 -27.612  1.00 51.68           O
HETATM 5785  O   HOH A 620    -100.132  78.363 -24.600  1.00 41.82           O
HETATM 5786  O   HOH A 621     -94.123  31.195  -2.465  1.00 48.41           O
HETATM 5787  O   HOH A 622     -97.203  45.090  -2.893  1.00 45.59           O
HETATM 5788  O   HOH A 623     -82.829  40.643 -15.752  1.00 58.47           O
HETATM 5789  O   HOH A 624     -94.794  47.641 -32.512  1.00 49.74           O
HETATM 5790  O   HOH A 625     -96.151  20.352  -4.553  1.00 49.30           O
HETATM 5791  O   HOH A 626     -93.497  45.471 -20.910  1.00 37.26           O
HETATM 5792  O   HOH A 627     -75.995  30.196 -13.836  1.00 32.39           O
HETATM 5793  O   HOH A 628     -95.300  60.313 -21.928  1.00 35.38           O
HETATM 5794  O   HOH A 629     -75.454  60.492 -25.244  1.00 37.88           O
HETATM 5795  O   HOH A 630    -105.418  66.488 -36.030  1.00 35.94           O
HETATM 5796  O   HOH A 631     -75.592  27.685  -2.972  1.00 38.90           O
HETATM 5797  O   HOH A 632    -105.982  51.550 -34.060  1.00 43.93           O
HETATM 5798  O   HOH A 633     -94.109  47.892 -24.073  1.00 49.83           O
HETATM 5799  O   HOH A 634    -101.124  50.711 -34.555  1.00 42.20           O
HETATM 5800  O   HOH A 635    -113.013  53.610 -31.314  1.00 54.58           O
HETATM 5801  O   HOH A 636     -86.489  68.160 -27.138  1.00 35.33           O
HETATM 5802  O   HOH A 637     -84.215  71.678 -30.454  1.00 39.85           O
HETATM 5803  O   HOH A 638     -86.414  73.936 -40.901  1.00 45.93           O
HETATM 5804  O   HOH A 639     -87.577  52.319 -21.773  1.00 55.25           O
HETATM 5805  O   HOH A 640     -96.948  57.111 -20.776  1.00 28.37           O
HETATM 5806  O   HOH A 641     -90.142  45.246 -23.544  1.00 68.79           O
HETATM 5807  O   HOH A 642    -115.385  52.703 -23.781  1.00 30.44           O
HETATM 5808  O   HOH A 643    -104.339  41.244 -34.176  1.00 43.08           O
HETATM 5809  O   HOH A 644    -101.022  34.066 -18.731  1.00 38.98           O
HETATM 5810  O   HOH A 645     -74.676  53.412 -38.068  1.00 55.07           O
HETATM 5811  O   HOH A 646    -105.805  38.256 -17.571  1.00 65.03           O
HETATM 5812  O   HOH A 647    -109.811  55.020 -30.946  1.00 49.20           O
HETATM 5813  O   HOH A 648     -85.643  70.704 -28.304  1.00 53.90           O
HETATM 5814  O   HOH A 649     -91.069  32.945  -2.261  1.00 48.73           O
HETATM 5815  O   HOH A 650     -81.610  69.928 -23.731  1.00 35.40           O
HETATM 5816  O   HOH A 651     -79.447  53.944 -22.074  1.00 39.19           O
HETATM 5817  O   HOH A 652    -101.525  14.566  -6.295  1.00 56.34           O
HETATM 5818  O   HOH A 653     -80.348  73.854 -32.180  1.00 46.98           O
HETATM 5819  O   HOH A 654     -72.324  25.899  -7.797  1.00 42.13           O
HETATM 5820  O   HOH A 655    -103.899  43.986 -35.105  1.00 52.06           O
HETATM 5821  O   HOH A 656    -121.318  40.110 -21.206  1.00 56.54           O
HETATM 5822  O   HOH A 657     -81.810  39.984  -1.055  1.00 34.57           O
HETATM 5823  O   HOH A 658     -90.337  44.689 -28.463  1.00 57.68           O
HETATM 5824  O   HOH A 659    -119.446  55.327  -6.655  1.00 71.65           O
HETATM 5825  O   HOH A 660     -94.258  52.405 -15.713  1.00 51.34           O
HETATM 5826  O   HOH A 661    -117.333  60.366 -20.216  1.00 54.19           O
HETATM 5827  O   HOH A 662    -100.140  53.622 -47.312  1.00 56.66           O
HETATM 5828  O   HOH A 663     -87.322  19.176 -11.980  1.00 52.80           O
HETATM 5829  O   HOH A 664    -112.049  30.099 -21.150  1.00 63.92           O
HETATM 5830  O   HOH A 665    -112.423  39.630 -33.185  1.00 59.93           O
HETATM 5831  O   HOH A 666    -115.700  55.043 -26.121  1.00 45.84           O
HETATM 5832  O   HOH A 667    -110.894  31.591 -18.962  1.00 43.58           O
HETATM 5833  O   HOH A 668     -99.051  24.350  -6.674  1.00 55.41           O
HETATM 5834  O   HOH A 669     -98.995  34.250 -40.090  1.00 52.64           O
HETATM 5835  O   HOH A 670     -73.346  29.608  -9.977  1.00 42.69           O
HETATM 5836  O   HOH A 671     -84.700  50.090 -16.383  1.00 49.09           O
HETATM 5837  O   HOH A 672     -94.917  46.950 -22.111  1.00 43.25           O
HETATM 5838  O   HOH A 673     -84.478  43.729  -1.912  1.00 36.02           O
HETATM 5839  O   HOH A 674    -104.925  63.452 -19.585  1.00 50.63           O
HETATM 5840  O   HOH A 675     -81.676  66.800 -49.678  1.00 44.22           O
HETATM 5841  O   HOH A 676     -81.385  33.523 -15.731  1.00 40.82           O
HETATM 5842  O   HOH A 677     -80.904  62.444 -42.198  1.00 61.01           O
HETATM 5843  O   HOH A 678    -101.270  55.031 -13.114  1.00 52.38           O
HETATM 5844  O   HOH A 679     -88.989  52.509 -23.967  1.00 47.51           O
HETATM 5845  O   HOH A 680     -89.403  56.137 -28.542  1.00 74.02           O
HETATM 5846  O   HOH A 681     -87.663  43.159 -23.276  1.00 60.77           O
HETATM 5847  O   HOH A 682    -121.857  49.044 -16.337  1.00 44.46           O
HETATM 5848  O   HOH A 683     -71.150  70.201 -26.869  1.00 35.75           O
HETATM 5849  O   HOH A 684     -84.717  77.306 -35.885  1.00 54.15           O
HETATM 5850  O   HOH A 685     -86.402  73.266 -29.218  1.00 52.60           O
HETATM 5851  O   HOH A 686     -83.946  20.227 -11.952  1.00 46.48           O
HETATM 5852  O   HOH B 501     -93.976  42.603  29.084  1.00 36.02           O
HETATM 5853  O   HOH B 502    -101.899  53.575  26.098  1.00 46.98           O
HETATM 5854  O   HOH B 503     -78.074  58.385  15.041  1.00 50.70           O
HETATM 5855  O   HOH B 504     -92.829  47.962  19.941  1.00 50.92           O
HETATM 5856  O   HOH B 505    -100.047  48.991   8.726  1.00 59.54           O
HETATM 5857  O   HOH B 506     -82.152  70.239   1.381  1.00 68.24           O
HETATM 5858  O   HOH B 507    -115.183  54.198  20.844  1.00 31.54           O
HETATM 5859  O   HOH B 508     -92.455  47.861   9.435  1.00 31.29           O
HETATM 5860  O   HOH B 509    -113.073  48.343   9.198  1.00 35.16           O
HETATM 5861  O   HOH B 510     -87.393  44.736  11.942  1.00 36.70           O
HETATM 5862  O   HOH B 511     -85.542  21.947  24.340  1.00 44.77           O
HETATM 5863  O   HOH B 512     -94.284  44.563  17.453  1.00 48.16           O
HETATM 5864  O   HOH B 513     -84.908  51.192  16.638  1.00 39.13           O
HETATM 5865  O   HOH B 514     -81.934  27.837  35.962  1.00 42.80           O
HETATM 5866  O   HOH B 515    -102.911  54.947  28.088  1.00 29.05           O
HETATM 5867  O   HOH B 516     -84.516  49.287  19.737  1.00 43.32           O
HETATM 5868  O   HOH B 517     -66.225  60.538   4.013  1.00 48.41           O
HETATM 5869  O   HOH B 518    -102.885  43.133  34.708  1.00 39.69           O
HETATM 5870  O   HOH B 519     -85.292  19.580  28.295  1.00 28.18           O
HETATM 5871  O   HOH B 520     -94.818  42.319  23.611  1.00 37.74           O
HETATM 5872  O   HOH B 521     -94.893  45.341  25.435  1.00 77.41           O
HETATM 5873  O   HOH B 522    -115.193  51.225   5.622  1.00 55.06           O
HETATM 5874  O   HOH B 523    -106.594  51.428  32.794  1.00 51.48           O
HETATM 5875  O   HOH B 524     -89.246  63.043  15.531  1.00 31.25           O
HETATM 5876  O   HOH B 525     -84.148  50.254  11.638  1.00 31.77           O
HETATM 5877  O   HOH B 526    -115.112  61.264  26.225  1.00 33.21           O
HETATM 5878  O   HOH B 527     -86.831  69.583  18.944  1.00 51.30           O
HETATM 5879  O   HOH B 528     -86.244  47.446   0.843  1.00 28.40           O
HETATM 5880  O   HOH B 529     -98.296  58.309   8.971  1.00 26.24           O
HETATM 5881  O   HOH B 530     -99.410  42.831  18.465  1.00 31.82           O
HETATM 5882  O   HOH B 531     -89.684  58.029  19.838  1.00 44.55           O
HETATM 5883  O   HOH B 532     -94.349  40.393  51.635  1.00 47.07           O
HETATM 5884  O   HOH B 533    -107.503  67.651  18.218  1.00 33.56           O
HETATM 5885  O   HOH B 534    -119.777  49.771  12.269  1.00 43.26           O
HETATM 5886  O   HOH B 535     -97.662  40.158  28.466  1.00 28.73           O
HETATM 5887  O   HOH B 536     -91.692  51.030  24.444  1.00 54.56           O
HETATM 5888  O   HOH B 537     -73.687  49.220  -0.073  1.00 37.17           O
HETATM 5889  O   HOH B 538    -102.280  43.010  46.562  1.00 59.67           O
HETATM 5890  O   HOH B 539    -104.258  33.217  22.695  1.00 49.34           O
HETATM 5891  O   HOH B 540     -90.865  46.470  36.260  1.00 39.56           O
HETATM 5892  O   HOH B 541    -112.907  49.459  27.886  1.00 33.84           O
HETATM 5893  O   HOH B 542     -99.930  51.371   6.575  1.00 32.12           O
HETATM 5894  O   HOH B 543    -100.015  49.008  26.886  1.00 40.15           O
HETATM 5895  O   HOH B 544    -110.543  56.239   7.654  1.00 28.65           O
HETATM 5896  O   HOH B 545     -83.945  69.287  19.500  1.00 45.73           O
HETATM 5897  O   HOH B 546    -112.209  68.050  27.490  1.00 34.84           O
HETATM 5898  O   HOH B 547    -102.336  26.473  43.550  1.00 41.07           O
HETATM 5899  O   HOH B 548     -81.965  50.118   1.301  1.00 23.78           O
HETATM 5900  O   HOH B 549     -99.263  62.806  26.918  1.00 31.77           O
HETATM 5901  O   HOH B 550     -97.015  53.437   1.019  1.00 37.92           O
HETATM 5902  O   HOH B 551    -112.469  58.947  30.491  1.00 44.67           O
HETATM 5903  O   HOH B 552     -93.029  54.545  19.404  1.00 34.01           O
HETATM 5904  O   HOH B 553     -90.499  63.098   1.943  1.00 40.30           O
HETATM 5905  O   HOH B 554     -97.116  54.901  11.917  1.00 22.16           O
HETATM 5906  O   HOH B 555     -92.504  57.893  21.830  1.00 20.64           O
HETATM 5907  O   HOH B 556     -83.567  24.438  39.989  1.00 59.11           O
HETATM 5908  O   HOH B 557    -105.930  45.194  33.893  1.00 42.28           O
HETATM 5909  O   HOH B 558     -86.391  63.150   2.175  1.00 53.42           O
HETATM 5910  O   HOH B 559     -89.536  40.050  25.052  1.00 52.59           O
HETATM 5911  O   HOH B 560    -101.147  49.093  14.562  1.00 26.73           O
HETATM 5912  O   HOH B 561    -104.459  67.438  25.222  1.00 57.06           O
HETATM 5913  O   HOH B 562     -68.053  48.963   3.724  1.00 39.44           O
HETATM 5914  O   HOH B 563     -99.155  62.705  17.251  1.00 48.52           O
HETATM 5915  O   HOH B 564     -83.916  28.566  25.005  1.00 32.71           O
HETATM 5916  O   HOH B 565    -115.223  67.643  19.691  1.00 37.86           O
HETATM 5917  O   HOH B 566     -69.680  55.484  13.332  1.00 28.53           O
HETATM 5918  O   HOH B 567     -95.260  64.306   3.086  1.00 47.31           O
HETATM 5919  O   HOH B 568     -98.184  55.334   9.560  1.00 30.95           O
HETATM 5920  O   HOH B 569     -92.087  55.275  21.645  1.00 25.28           O
HETATM 5921  O   HOH B 570    -117.570  48.304  27.510  1.00 41.91           O
HETATM 5922  O   HOH B 571    -107.355  43.273  40.593  1.00 52.66           O
HETATM 5923  O   HOH B 572    -112.806  36.141  40.945  1.00 46.75           O
HETATM 5924  O   HOH B 573    -101.305  47.032  28.334  1.00 25.59           O
HETATM 5925  O   HOH B 574     -93.901  48.700  23.775  1.00 50.21           O
HETATM 5926  O   HOH B 575    -106.030  65.162  24.366  1.00 39.46           O
HETATM 5927  O   HOH B 576     -83.774  44.455  15.491  1.00 42.40           O
HETATM 5928  O   HOH B 577    -115.903  52.485  24.766  1.00 41.44           O
HETATM 5929  O   HOH B 578    -114.730  54.433  23.243  1.00 27.68           O
HETATM 5930  O   HOH B 579     -99.905  51.737  26.097  1.00 25.22           O
HETATM 5931  O   HOH B 580     -91.421  19.596  34.140  1.00 34.95           O
HETATM 5932  O   HOH B 581     -74.571  64.426   0.806  1.00 34.27           O
HETATM 5933  O   HOH B 582     -86.102  73.484  18.412  1.00 50.22           O
HETATM 5934  O   HOH B 583     -92.818  56.670  17.927  1.00 22.72           O
HETATM 5935  O   HOH B 584    -108.181  70.714  17.959  1.00 46.32           O
HETATM 5936  O   HOH B 585     -78.759  49.909   0.610  1.00 45.08           O
HETATM 5937  O   HOH B 586     -96.936  42.728  28.792  1.00 35.15           O
HETATM 5938  O   HOH B 587     -67.483  57.029   2.480  1.00 48.40           O
HETATM 5939  O   HOH B 588     -89.060  45.003   0.954  1.00 46.22           O
HETATM 5940  O   HOH B 589     -85.475  16.045  38.000  1.00 48.44           O
HETATM 5941  O   HOH B 590     -95.260  53.561  11.225  1.00 37.83           O
HETATM 5942  O   HOH B 591    -110.844  50.083  30.516  1.00 38.80           O
HETATM 5943  O   HOH B 592     -96.516  20.381  37.468  1.00 55.15           O
HETATM 5944  O   HOH B 593     -90.790  47.636  30.987  1.00 58.83           O
HETATM 5945  O   HOH B 594     -94.828  63.362  14.971  1.00 53.98           O
HETATM 5946  O   HOH B 595     -99.450  47.714  11.289  1.00 61.79           O
HETATM 5947  O   HOH B 596     -95.218  52.666  20.610  1.00 31.26           O
HETATM 5948  O   HOH B 597    -117.320  44.422  27.215  1.00 49.83           O
HETATM 5949  O   HOH B 598     -82.163  48.867  18.488  1.00 60.59           O
HETATM 5950  O   HOH B 599     -93.199  63.816  17.987  1.00 35.36           O
HETATM 5951  O   HOH B 600    -100.773  57.078  34.087  1.00 41.82           O
HETATM 5952  O   HOH B 601    -113.435  52.902  30.411  1.00 53.78           O
HETATM 5953  O   HOH B 602     -92.557  26.134  49.371  1.00 42.95           O
HETATM 5954  O   HOH B 603     -97.109  63.382  38.925  1.00 39.07           O
HETATM 5955  O   HOH B 604    -105.421  45.246  10.788  1.00 48.71           O
HETATM 5956  O   HOH B 605     -94.174  35.922  20.686  1.00 32.17           O
HETATM 5957  O   HOH B 606     -96.786  38.871  35.477  1.00 39.37           O
HETATM 5958  O   HOH B 607    -103.455  41.676  17.422  1.00 43.11           O
HETATM 5959  O   HOH B 608     -84.075  76.551  10.577  1.00 51.17           O
HETATM 5960  O   HOH B 609     -77.832  32.147  30.520  1.00 57.14           O
HETATM 5961  O   HOH B 610     -90.732  65.182  13.419  1.00 48.07           O
HETATM 5962  O   HOH B 611     -82.837  73.289   4.192  1.00 41.18           O
HETATM 5963  O   HOH B 612    -105.347  38.345  51.869  1.00 55.78           O
HETATM 5964  O   HOH B 613     -89.780  46.722   8.208  1.00 34.22           O
HETATM 5965  O   HOH B 614    -101.251  71.127  18.116  1.00 49.16           O
HETATM 5966  O   HOH B 615     -64.209  66.054  15.177  1.00 38.08           O
HETATM 5967  O   HOH B 616     -92.065  50.806  20.479  1.00 43.96           O
HETATM 5968  O   HOH B 617     -99.271  24.109  31.059  1.00 39.27           O
HETATM 5969  O   HOH B 618     -97.194  27.193  26.725  1.00 53.12           O
HETATM 5970  O   HOH B 619     -87.661  42.231  15.669  1.00 36.98           O
HETATM 5971  O   HOH B 620     -90.883  41.216  28.752  1.00 57.76           O
HETATM 5972  O   HOH B 621    -109.842  68.797  16.799  1.00 31.07           O
HETATM 5973  O   HOH B 622     -84.521  46.381  19.421  1.00 54.35           O
HETATM 5974  O   HOH B 623    -113.036  61.546  30.046  1.00 48.94           O
HETATM 5975  O   HOH B 624     -90.685  26.580  40.544  1.00 49.41           O
HETATM 5976  O   HOH B 625     -64.293  57.374   7.587  1.00 48.82           O
HETATM 5977  O   HOH B 626     -81.814  75.747  11.340  1.00 56.35           O
HETATM 5978  O   HOH B 627    -107.332  59.856  -2.291  1.00 43.44           O
HETATM 5979  O   HOH B 628     -90.174  41.556  21.022  1.00 74.25           O
HETATM 5980  O   HOH B 629    -100.439  59.326  33.454  1.00 61.79           O
HETATM 5981  O   HOH B 630    -115.293  39.294  20.370  1.00 56.42           O
HETATM 5982  O   HOH B 631    -118.242  59.039   9.618  1.00 49.50           O
HETATM 5983  O   HOH B 632    -119.968  47.001  18.304  1.00 42.37           O
HETATM 5984  O   HOH B 633     -74.635  71.079  11.072  1.00 50.44           O
HETATM 5985  O   HOH B 634    -101.895  46.488  47.047  1.00 52.93           O
HETATM 5986  O   HOH B 635     -94.902  51.945   2.222  1.00 48.17           O
HETATM 5987  O   HOH B 636     -92.712  54.038  35.232  1.00 40.88           O
HETATM 5988  O   HOH B 637     -89.671  48.900  23.427  1.00 52.47           O
HETATM 5989  O   HOH B 638     -67.596  68.843  10.852  1.00 42.85           O
HETATM 5990  O   HOH B 639     -67.044  54.629   9.675  1.00 34.37           O
HETATM 5991  O   HOH B 640    -111.392  46.253  13.020  1.00 53.68           O
HETATM 5992  O   HOH B 641     -93.299  39.070  28.109  1.00 53.52           O
HETATM 5993  O   HOH B 642     -87.168  71.417   6.631  1.00 50.33           O
HETATM 5994  O   HOH B 643     -92.818  66.095   7.631  1.00 46.36           O
HETATM 5995  O   HOH B 644    -105.582  69.671  20.845  1.00 53.60           O
HETATM 5996  O   HOH B 645    -112.050  44.342  39.434  1.00 56.01           O
HETATM 5997  O   HOH B 646     -83.495  47.776   1.511  1.00 37.64           O
HETATM 5998  O   HOH B 647    -114.777  24.533  24.830  1.00 57.50           O
HETATM 5999  O   HOH B 648     -83.948  36.144  21.195  1.00 38.63           O
HETATM 6000  O   HOH B 649    -111.311  67.234  29.992  1.00 46.76           O
HETATM 6001  O   HOH B 650     -76.068  55.554  15.526  1.00 43.97           O
HETATM 6002  O   HOH B 651    -112.052  48.321  31.283  1.00 38.01           O
HETATM 6003  O   HOH B 652    -108.647  46.800  34.227  1.00 57.26           O
HETATM 6004  O   HOH B 653     -93.372  49.452  39.128  1.00 54.46           O
HETATM 6005  O   HOH B 654     -74.272  72.186   8.696  1.00 52.73           O
HETATM 6006  O   HOH B 655    -119.953  60.725  11.726  1.00 42.37           O
HETATM 6007  O   HOH B 656    -103.862  45.168  12.729  1.00 50.09           O
HETATM 6008  O   HOH B 657    -100.743  71.259  15.484  1.00 76.60           O
HETATM 6009  O   HOH B 658    -115.559  61.557  28.538  1.00 31.13           O
HETATM 6010  O   HOH B 659    -111.349  37.372  43.333  1.00 52.93           O
HETATM 6011  O   HOH B 660     -93.403  65.083   9.891  1.00 45.05           O
ENDMDL
MASTER        8    0    0   20   50    0   24    6 5912    2    0   58
END
