HEADER    PROTEIN STRUCTURE ALIGNMENT                                           
COMPND    (A) USR1:_(230) [16-240] (B) USR2:_(240) [16-240]
REMARK   1 
REMARK   1 Alignment length=230 Sequence identity=220 Gaps=10(5%)
REMARK   1 
MODEL         1
ATOM      0  N   ILE A  11       3.502  38.724  59.242
ATOM      1  CA  ILE A  11       3.950  37.710  58.340
ATOM      2  C   ILE A  11       2.896  36.648  58.312
ATOM      3  O   ILE A  11       2.425  36.317  57.234
ATOM      4  CB  ILE A  11       5.288  37.180  58.766
ATOM      5  CG1 ILE A  11       6.368  38.264  58.725
ATOM      6  CG2 ILE A  11       5.714  36.066  57.898
ATOM      7  CD1 ILE A  11       6.584  38.932  57.350
ATOM      8  N   LEU A  12       2.486  36.146  59.489
ATOM      9  CA  LEU A  12       1.514  35.089  59.637
ATOM     10  C   LEU A  12       0.157  35.448  59.052
ATOM     11  O   LEU A  12      -0.486  34.585  58.451
ATOM     12  CB  LEU A  12       1.448  34.581  61.087
ATOM     13  CG  LEU A  12       0.695  33.254  61.263
ATOM     14  CD1 LEU A  12       0.854  32.760  62.696
ATOM     15  CD2 LEU A  12      -0.831  33.268  61.040
ATOM     16  N   PRO A  13      -0.347  36.662  59.255
ATOM     17  CA  PRO A  13      -1.633  36.993  58.618
ATOM     18  C   PRO A  13      -1.666  37.309  57.145
ATOM     19  O   PRO A  13      -2.758  37.380  56.588
ATOM     20  CB  PRO A  13      -2.184  38.181  59.458
ATOM     21  CG  PRO A  13      -1.292  38.312  60.724
ATOM     22  CD  PRO A  13      -0.452  37.039  60.683
ATOM     23  N   ARG A  14      -0.512  37.506  56.509
ATOM     24  CA  ARG A  14      -0.374  37.966  55.162
ATOM     25  C   ARG A  14       0.182  36.819  54.352
ATOM     26  O   ARG A  14       0.832  37.029  53.330
ATOM     27  CB  ARG A  14       0.668  39.099  55.162
ATOM     28  CG  ARG A  14       0.061  40.447  55.552
ATOM     29  CD  ARG A  14      -0.034  40.687  57.067
ATOM     30  NE  ARG A  14       1.342  40.732  57.641
ATOM     31  CZ  ARG A  14       2.061  41.905  57.673
ATOM     32  NH1 ARG A  14       1.528  43.059  57.131
ATOM     33  NH2 ARG A  14       3.314  41.907  58.243
ATOM     34  N   GLY A  15      -0.031  35.565  54.793
ATOM     35  CA  GLY A  15       0.391  34.437  54.008
ATOM     36  C   GLY A  15       1.761  33.932  54.373
ATOM     37  O   GLY A  15       1.995  32.734  54.260
ATOM     38  N   SER A  16       2.704  34.787  54.792
ATOM     39  CA  SER A  16       3.986  34.289  55.145
ATOM     40  C   SER A  16       3.741  33.600  56.471
ATOM     41  O   SER A  16       2.940  33.963  57.290
ATOM     42  CB  SER A  16       4.947  35.438  55.129
ATOM     43  OG  SER A  16       5.228  36.011  53.871
ATOM     44  N   ARG A  17       4.220  32.416  56.741
ATOM     45  CA  ARG A  17       4.450  32.085  58.089
ATOM     46  C   ARG A  17       5.911  31.999  58.138
ATOM     47  O   ARG A  17       6.484  32.376  59.125
ATOM     48  CB  ARG A  17       3.650  30.853  58.515
ATOM     49  CG  ARG A  17       3.779  30.501  59.989
ATOM     50  CD  ARG A  17       4.996  29.603  60.325
ATOM     51  NE  ARG A  17       6.160  30.459  60.708
ATOM     52  CZ  ARG A  17       7.491  30.129  60.495
ATOM     53  NH1 ARG A  17       7.768  28.791  60.533
ATOM     54  NH2 ARG A  17       8.542  31.017  60.432
ATOM     55  N   GLU A  18       6.628  31.644  57.103
ATOM     56  CA  GLU A  18       8.040  31.419  57.162
ATOM     57  C   GLU A  18       8.845  32.598  57.713
ATOM     58  O   GLU A  18       9.999  32.394  58.078
ATOM     59  CB  GLU A  18       8.639  31.000  55.779
ATOM     60  CG  GLU A  18       8.461  31.829  54.474
ATOM     61  CD  GLU A  18       7.102  31.862  53.917
ATOM     62  OE1 GLU A  18       6.056  31.775  54.590
ATOM     63  OE2 GLU A  18       7.143  32.007  52.689
ATOM     64  N   PRO A  19       8.349  33.825  57.682
ATOM     65  CA  PRO A  19       9.003  34.940  58.361
ATOM     66  C   PRO A  19       8.461  35.359  59.683
ATOM     67  O   PRO A  19       8.938  36.387  60.140
ATOM     68  CB  PRO A  19       8.961  36.120  57.320
ATOM     69  CG  PRO A  19       8.490  35.558  55.976
ATOM     70  CD  PRO A  19       8.418  34.113  56.282
ATOM     71  N   VAL A  20       7.504  34.651  60.314
ATOM     72  CA  VAL A  20       6.966  35.027  61.617
ATOM     73  C   VAL A  20       8.082  35.444  62.598
ATOM     74  O   VAL A  20       9.132  34.836  62.536
ATOM     75  CB  VAL A  20       6.245  33.827  62.220
ATOM     76  CG1 VAL A  20       7.229  32.749  62.578
ATOM     77  CG2 VAL A  20       5.564  34.187  63.532
ATOM     78  N   GLN A  21       7.982  36.402  63.560
ATOM     79  CA  GLN A  21       9.174  36.612  64.386
ATOM     80  C   GLN A  21       9.667  35.302  65.034
ATOM     81  O   GLN A  21      10.839  34.959  64.908
ATOM     82  CB  GLN A  21       9.021  37.716  65.442
ATOM     83  CG  GLN A  21      10.340  38.282  65.983
ATOM     84  CD  GLN A  21      10.948  37.443  67.131
ATOM     85  OE1 GLN A  21      10.923  37.742  68.310
ATOM     86  NE2 GLN A  21      11.644  36.330  66.886
ATOM     87  N   ARG A  22       8.814  34.461  65.634
ATOM     88  CA  ARG A  22       9.313  33.246  66.263
ATOM     89  C   ARG A  22       9.935  32.246  65.282
ATOM     90  O   ARG A  22       9.630  32.242  64.101
ATOM     91  CB  ARG A  22       8.176  32.512  66.987
ATOM     92  CG  ARG A  22       8.569  31.286  67.818
ATOM     93  CD  ARG A  22       9.240  31.655  69.138
ATOM     94  NE  ARG A  22      10.705  31.868  68.933
ATOM     95  CZ  ARG A  22      11.490  32.340  69.960
ATOM     96  NH1 ARG A  22      10.913  32.670  71.171
ATOM     97  NH2 ARG A  22      12.840  32.509  69.753
ATOM     98  N   SER A  23      10.841  31.347  65.738
ATOM     99  CA  SER A  23      11.348  30.257  64.946
ATOM    100  C   SER A  23      10.858  28.961  65.558
ATOM    101  O   SER A  23      10.915  28.805  66.777
ATOM    102  CB  SER A  23      12.883  30.250  64.985
ATOM    103  OG  SER A  23      13.349  30.007  66.307
ATOM    104  N   TRP A  24      10.374  27.990  64.751
ATOM    105  CA  TRP A  24       9.851  26.752  65.291
ATOM    106  C   TRP A  24      10.491  25.679  64.519
ATOM    107  O   TRP A  24      10.351  25.714  63.302
ATOM    108  CB  TRP A  24       8.365  26.587  64.988
ATOM    109  CG  TRP A  24       7.769  25.311  65.523
ATOM    110  CD1 TRP A  24       7.445  24.216  64.778
ATOM    111  CD2 TRP A  24       7.372  25.010  66.890
ATOM    112  NE1 TRP A  24       6.884  23.257  65.577
ATOM    113  CE2 TRP A  24       6.832  23.727  66.880
ATOM    114  CE3 TRP A  24       7.452  25.722  68.070
ATOM    115  CZ2 TRP A  24       6.361  23.147  68.033
ATOM    116  CZ3 TRP A  24       6.975  25.129  69.235
ATOM    117  CH2 TRP A  24       6.437  23.858  69.215
ATOM    118  N   LEU A  25      11.231  24.750  65.131
ATOM    119  CA  LEU A  25      11.968  23.878  64.274
ATOM    120  C   LEU A  25      11.680  22.644  64.702
ATOM    121  O   LEU A  25      11.270  22.638  65.841
ATOM    122  CB  LEU A  25      13.373  24.115  64.229
ATOM    123  CG  LEU A  25      13.703  25.063  63.056
ATOM    124  CD1 LEU A  25      13.006  26.404  63.032
ATOM    125  CD2 LEU A  25      15.113  25.589  63.008
ATOM    126  N   HIS A  26      11.490  21.945  63.579
ATOM    127  CA  HIS A  26      11.509  20.563  63.473
ATOM    128  C   HIS A  26      12.928  20.150  63.257
ATOM    129  O   HIS A  26      13.534  20.383  62.212
ATOM    130  CB  HIS A  26      10.586  20.059  62.365
ATOM    131  CG  HIS A  26       9.130  20.400  62.619
ATOM    132  ND1 HIS A  26       8.432  19.780  63.642
ATOM    133  CD2 HIS A  26       8.311  21.264  61.952
ATOM    134  CE1 HIS A  26       7.206  20.267  63.564
ATOM    135  NE2 HIS A  26       7.078  21.177  62.566
ATOM    136  N   GLY A  27      13.493  19.502  64.286
ATOM    137  CA  GLY A  27      14.802  18.917  64.204
ATOM    138  C   GLY A  27      15.884  19.936  64.410
ATOM    139  O   GLY A  27      17.038  19.677  64.067
ATOM    140  N   TYR A  28      15.553  21.114  64.979
ATOM    141  CA  TYR A  28      16.569  22.093  65.232
ATOM    142  C   TYR A  28      16.311  22.733  66.574
ATOM    143  O   TYR A  28      17.157  22.620  67.454
ATOM    144  CB  TYR A  28      16.654  23.156  64.166
ATOM    145  CG  TYR A  28      16.965  22.677  62.776
ATOM    146  CD1 TYR A  28      15.998  22.369  61.824
ATOM    147  CD2 TYR A  28      18.283  22.614  62.414
ATOM    148  CE1 TYR A  28      16.359  21.923  60.575
ATOM    149  CE2 TYR A  28      18.652  22.170  61.171
ATOM    150  CZ  TYR A  28      17.691  21.824  60.251
ATOM    151  OH  TYR A  28      18.075  21.363  58.974
ATOM    152  N   THR A  29      15.160  23.414  66.790
ATOM    153  CA  THR A  29      14.844  24.036  68.057
ATOM    154  C   THR A  29      13.872  23.146  68.827
ATOM    155  O   THR A  29      13.566  23.405  69.993
ATOM    156  CB  THR A  29      14.291  25.444  67.865
ATOM    157  OG1 THR A  29      15.253  26.251  67.194
ATOM    158  CG2 THR A  29      13.932  26.149  69.194
ATOM    159  N   ILE A  30      13.371  22.057  68.205
ATOM    160  CA  ILE A  30      12.501  21.106  68.866
ATOM    161  C   ILE A  30      12.920  19.800  68.255
ATOM    162  O   ILE A  30      13.534  19.790  67.188
ATOM    163  CB  ILE A  30      10.998  21.339  68.676
ATOM    164  CG1 ILE A  30      10.097  20.536  69.596
ATOM    165  CG2 ILE A  30      10.480  20.748  67.374
ATOM    166  CD1 ILE A  30       8.639  20.982  69.506
ATOM    167  N   ASP A  31      12.579  18.673  68.890
ATOM    168  CA  ASP A  31      12.908  17.370  68.374
ATOM    169  C   ASP A  31      12.199  17.075  67.069
ATOM    170  O   ASP A  31      11.074  17.506  66.829
ATOM    171  CB  ASP A  31      12.617  16.233  69.371
ATOM    172  CG  ASP A  31      11.135  16.117  69.749
ATOM    173  OD1 ASP A  31      10.274  16.890  69.262
ATOM    174  OD2 ASP A  31      10.844  15.239  70.601
ATOM    175  N   GLY A  32      12.874  16.330  66.164
ATOM    176  CA  GLY A  32      12.349  16.086  64.840
ATOM    177  C   GLY A  32      11.932  14.653  64.599
ATOM    178  O   GLY A  32      11.545  13.915  65.504
ATOM    179  N   GLY A  33      12.004  14.233  63.311
ATOM    180  CA  GLY A  33      11.477  12.968  62.875
ATOM    181  C   GLY A  33      12.459  11.821  62.875
ATOM    182  O   GLY A  33      12.109  10.736  62.411
ATOM    183  N   PHE A  34      13.690  11.994  63.407
ATOM    184  CA  PHE A  34      14.661  10.925  63.486
ATOM    185  C   PHE A  34      14.332  10.007  64.653
ATOM    186  O   PHE A  34      15.196   9.606  65.428
ATOM    187  CB  PHE A  34      16.121  11.453  63.623
ATOM    188  CG  PHE A  34      16.318  12.256  64.888
ATOM    189  CD1 PHE A  34      16.834  11.671  66.035
ATOM    190  CD2 PHE A  34      16.067  13.612  64.929
ATOM    191  CE1 PHE A  34      16.964  12.357  67.205
ATOM    192  CE2 PHE A  34      16.274  14.331  66.087
ATOM    193  CZ  PHE A  34      16.708  13.702  67.231
ATOM    194  N   ALA A  35      13.060   9.610  64.816
ATOM    195  CA  ALA A  35      12.686   8.821  65.938
ATOM    196  C   ALA A  35      11.379   8.176  65.662
ATOM    197  O   ALA A  35      10.660   8.503  64.714
ATOM    198  CB  ALA A  35      12.533   9.636  67.233
ATOM    199  N   ALA A  36      11.058   7.243  66.576
ATOM    200  CA  ALA A  36       9.925   6.387  66.470
ATOM    201  C   ALA A  36       8.686   7.238  66.536
ATOM    202  O   ALA A  36       7.644   6.836  66.019
ATOM    203  CB  ALA A  36       9.894   5.328  67.595
ATOM    204  N   HIS A  37       8.780   8.434  67.167
ATOM    205  CA  HIS A  37       7.645   9.236  67.501
ATOM    206  C   HIS A  37       8.085  10.657  67.621
ATOM    207  O   HIS A  37       9.238  10.937  67.954
ATOM    208  CB  HIS A  37       7.049   8.910  68.880
ATOM    209  CG  HIS A  37       7.999   9.190  70.030
ATOM    210  ND1 HIS A  37       9.017   8.295  70.337
ATOM    211  CD2 HIS A  37       8.026  10.243  70.896
ATOM    212  CE1 HIS A  37       9.643   8.835  71.368
ATOM    213  NE2 HIS A  37       9.080  10.006  71.753
ATOM    214  N   ALA A  38       7.131  11.588  67.392
ATOM    215  CA  ALA A  38       7.438  12.986  67.382
ATOM    216  C   ALA A  38       6.207  13.746  67.779
ATOM    217  O   ALA A  38       5.117  13.518  67.255
ATOM    218  CB  ALA A  38       7.888  13.462  65.999
ATOM    219  N   ALA A  39       6.367  14.674  68.736
ATOM    220  CA  ALA A  39       5.290  15.526  69.152
ATOM    221  C   ALA A  39       5.268  16.631  68.138
ATOM    222  O   ALA A  39       6.328  17.077  67.703
ATOM    223  CB  ALA A  39       5.525  16.102  70.557
ATOM    224  N   ALA A  40       4.061  17.081  67.712
ATOM    225  CA  ALA A  40       3.980  18.091  66.690
ATOM    226  C   ALA A  40       2.830  19.027  66.956
ATOM    227  O   ALA A  40       1.853  18.682  67.621
ATOM    228  CB  ALA A  40       3.828  17.494  65.282
ATOM    229  N   GLU A  41       2.943  20.262  66.426
ATOM    230  CA  GLU A  41       1.918  21.251  66.548
ATOM    231  C   GLU A  41       0.899  20.916  65.496
ATOM    232  O   GLU A  41       1.205  20.903  64.306
ATOM    233  CB  GLU A  41       2.455  22.683  66.327
ATOM    234  CG  GLU A  41       1.394  23.747  66.585
ATOM    235  CD  GLU A  41       1.983  25.121  66.368
ATOM    236  OE1 GLU A  41       2.985  25.464  67.047
ATOM    237  OE2 GLU A  41       1.414  25.857  65.520
ATOM    238  N   ALA A  42      -0.345  20.633  65.928
ATOM    239  CA  ALA A  42      -1.422  20.203  65.077
ATOM    240  C   ALA A  42      -1.702  21.131  63.920
ATOM    241  O   ALA A  42      -1.923  20.675  62.799
ATOM    242  CB  ALA A  42      -2.722  20.050  65.881
ATOM    243  N   GLY A  43      -1.694  22.458  64.155
ATOM    244  CA  GLY A  43      -2.003  23.415  63.127
ATOM    245  C   GLY A  43      -0.958  23.477  62.041
ATOM    246  O   GLY A  43      -1.248  23.992  60.961
ATOM    247  N   TYR A  44       0.280  22.979  62.283
ATOM    248  CA  TYR A  44       1.352  23.186  61.334
ATOM    249  C   TYR A  44       1.670  21.929  60.569
ATOM    250  O   TYR A  44       2.565  21.785  59.730
ATOM    251  CB  TYR A  44       2.573  23.844  61.942
ATOM    252  CG  TYR A  44       3.645  24.137  60.931
ATOM    253  CD1 TYR A  44       3.437  24.271  59.570
ATOM    254  CD2 TYR A  44       4.923  24.336  61.372
ATOM    255  CE1 TYR A  44       4.437  24.349  58.666
ATOM    256  CE2 TYR A  44       5.931  24.593  60.476
ATOM    257  CZ  TYR A  44       5.689  24.593  59.122
ATOM    258  OH  TYR A  44       6.710  24.844  58.194
ATOM    259  N   ALA A  45       0.794  20.980  60.733
ATOM    260  CA  ALA A  45       1.027  19.778  60.036
ATOM    261  C   ALA A  45       0.411  19.814  58.702
ATOM    262  O   ALA A  45      -0.516  20.577  58.431
ATOM    263  CB  ALA A  45       0.471  18.605  60.791
ATOM    264  N   PHE A  46       0.949  18.937  57.850
ATOM    265  CA  PHE A  46       0.451  18.824  56.519
ATOM    266  C   PHE A  46       0.046  17.421  56.147
ATOM    267  O   PHE A  46       0.788  16.445  56.225
ATOM    268  CB  PHE A  46       1.358  19.470  55.470
ATOM    269  CG  PHE A  46       2.651  18.745  55.272
ATOM    270  CD1 PHE A  46       3.139  17.732  56.091
ATOM    271  CD2 PHE A  46       3.497  19.235  54.327
ATOM    272  CE1 PHE A  46       4.191  16.946  55.794
ATOM    273  CE2 PHE A  46       4.733  18.668  54.272
ATOM    274  CZ  PHE A  46       4.919  17.397  54.762
ATOM    275  N   GLU A  47      -1.206  17.298  55.721
ATOM    276  CA  GLU A  47      -1.741  16.039  55.343
ATOM    277  C   GLU A  47      -1.096  15.534  54.123
ATOM    278  O   GLU A  47      -0.667  16.250  53.214
ATOM    279  CB  GLU A  47      -3.237  16.077  55.056
ATOM    280  CG  GLU A  47      -3.639  17.226  54.120
ATOM    281  CD  GLU A  47      -3.488  16.790  52.680
ATOM    282  OE1 GLU A  47      -4.022  15.701  52.361
ATOM    283  OE2 GLU A  47      -2.843  17.536  51.894
ATOM    284  N   LEU A  48      -1.063  14.218  54.127
ATOM    285  CA  LEU A  48      -0.414  13.504  53.111
ATOM    286  C   LEU A  48      -1.486  12.780  52.319
ATOM    287  O   LEU A  48      -2.180  11.918  52.813
ATOM    288  CB  LEU A  48       0.696  12.601  53.661
ATOM    289  CG  LEU A  48       0.312  11.589  54.781
ATOM    290  CD1 LEU A  48      -0.027  12.201  56.139
ATOM    291  CD2 LEU A  48      -0.797  10.570  54.561
ATOM    292  N   PRO A  49      -1.732  13.013  51.094
ATOM    293  CA  PRO A  49      -2.712  12.179  50.392
ATOM    294  C   PRO A  49      -2.567  10.671  50.489
ATOM    295  O   PRO A  49      -1.458  10.173  50.664
ATOM    296  CB  PRO A  49      -2.589  12.731  48.958
ATOM    297  CG  PRO A  49      -1.778  14.077  49.068
ATOM    298  CD  PRO A  49      -1.764  14.375  50.566
ATOM    299  N   GLU A  50      -3.705   9.955  50.445
ATOM    300  CA  GLU A  50      -3.778   8.534  50.631
ATOM    301  C   GLU A  50      -2.868   7.765  49.707
ATOM    302  O   GLU A  50      -2.067   6.946  50.154
ATOM    303  CB  GLU A  50      -5.214   8.018  50.407
ATOM    304  CG  GLU A  50      -6.197   8.433  51.511
ATOM    305  CD  GLU A  50      -6.502   9.916  51.418
ATOM    306  OE1 GLU A  50      -6.872  10.380  50.308
ATOM    307  OE2 GLU A  50      -6.334  10.610  52.452
ATOM    308  N   ASP A  51      -2.989   8.000  48.389
ATOM    309  CA  ASP A  51      -2.296   7.250  47.365
ATOM    310  C   ASP A  51      -0.797   7.474  47.336
ATOM    311  O   ASP A  51      -0.064   6.710  46.711
ATOM    312  CB  ASP A  51      -2.865   7.624  45.982
ATOM    313  CG  ASP A  51      -2.261   6.823  44.843
ATOM    314  OD1 ASP A  51      -2.373   5.567  44.864
ATOM    315  OD2 ASP A  51      -1.731   7.477  43.903
ATOM    316  N   ALA A  52      -0.280   8.508  48.027
ATOM    317  CA  ALA A  52       1.139   8.753  48.018
ATOM    318  C   ALA A  52       1.769   7.997  49.164
ATOM    319  O   ALA A  52       1.422   8.175  50.326
ATOM    320  CB  ALA A  52       1.473  10.245  48.153
ATOM    321  N   ASP A  53       2.741   7.135  48.863
ATOM    322  CA  ASP A  53       3.454   6.345  49.832
ATOM    323  C   ASP A  53       4.402   7.223  50.676
ATOM    324  O   ASP A  53       4.959   8.146  50.079
ATOM    325  CB  ASP A  53       4.216   5.244  49.058
ATOM    326  CG  ASP A  53       5.170   5.828  48.016
ATOM    327  OD1 ASP A  53       4.817   6.666  47.153
ATOM    328  OD2 ASP A  53       6.316   5.361  48.016
ATOM    329  N   PRO A  54       4.644   7.012  52.028
ATOM    330  CA  PRO A  54       5.532   7.854  52.857
ATOM    331  C   PRO A  54       6.916   8.085  52.350
ATOM    332  O   PRO A  54       7.419   9.194  52.533
ATOM    333  CB  PRO A  54       5.550   7.165  54.266
ATOM    334  CG  PRO A  54       4.416   6.091  54.241
ATOM    335  CD  PRO A  54       3.621   6.428  52.937
ATOM    336  N   VAL A  55       7.536   7.075  51.731
ATOM    337  CA  VAL A  55       8.859   7.193  51.184
ATOM    338  C   VAL A  55       8.918   8.292  50.140
ATOM    339  O   VAL A  55       9.895   9.040  50.082
ATOM    340  CB  VAL A  55       9.342   5.869  50.622
ATOM    341  CG1 VAL A  55       8.509   5.400  49.488
ATOM    342  CG2 VAL A  55      10.769   5.903  50.139
ATOM    343  N   ALA A  56       7.882   8.406  49.284
ATOM    344  CA  ALA A  56       7.843   9.353  48.213
ATOM    345  C   ALA A  56       7.531  10.713  48.759
ATOM    346  O   ALA A  56       8.028  11.712  48.248
ATOM    347  CB  ALA A  56       6.763   9.008  47.179
ATOM    348  N   THR A  57       6.689  10.789  49.808
ATOM    349  CA  THR A  57       6.245  12.037  50.352
ATOM    350  C   THR A  57       7.333  12.761  51.118
ATOM    351  O   THR A  57       7.436  13.984  51.031
ATOM    352  CB  THR A  57       5.037  11.814  51.231
ATOM    353  OG1 THR A  57       3.991  11.251  50.445
ATOM    354  CG2 THR A  57       4.579  13.148  51.869
ATOM    355  N   ALA A  58       8.147  12.037  51.908
ATOM    356  CA  ALA A  58       9.164  12.601  52.768
ATOM    357  C   ALA A  58      10.036  13.670  52.110
ATOM    358  O   ALA A  58      10.043  14.800  52.607
ATOM    359  CB  ALA A  58      10.005  11.496  53.454
ATOM    360  N   PRO A  59      10.747  13.397  51.015
ATOM    361  CA  PRO A  59      11.544  14.433  50.361
ATOM    362  C   PRO A  59      10.832  15.647  49.868
ATOM    363  O   PRO A  59      11.492  16.666  49.659
ATOM    364  CB  PRO A  59      12.299  13.655  49.244
ATOM    365  CG  PRO A  59      12.128  12.141  49.566
ATOM    366  CD  PRO A  59      11.527  12.144  50.958
ATOM    367  N   LEU A  60       9.514  15.585  49.713
ATOM    368  CA  LEU A  60       8.789  16.702  49.254
ATOM    369  C   LEU A  60       8.661  17.752  50.326
ATOM    370  O   LEU A  60       8.601  18.949  50.036
ATOM    371  CB  LEU A  60       7.394  16.291  48.727
ATOM    372  CG  LEU A  60       7.292  15.753  47.281
ATOM    373  CD1 LEU A  60       8.323  14.720  46.973
ATOM    374  CD2 LEU A  60       5.881  15.361  46.897
ATOM    375  N   LEU A  61       8.617  17.321  51.598
ATOM    376  CA  LEU A  61       8.418  18.196  52.719
ATOM    377  C   LEU A  61       9.511  19.237  52.836
ATOM    378  O   LEU A  61       9.407  20.201  53.565
ATOM    379  CB  LEU A  61       8.306  17.424  54.042
ATOM    380  CG  LEU A  61       7.801  18.259  55.261
ATOM    381  CD1 LEU A  61       7.402  17.375  56.445
ATOM    382  CD2 LEU A  61       8.760  19.208  55.964
ATOM    383  N   CYS A  62      10.620  19.173  52.114
ATOM    384  CA  CYS A  62      11.541  20.273  52.174
ATOM    385  C   CYS A  62      12.034  20.520  50.795
ATOM    386  O   CYS A  62      11.762  21.570  50.242
ATOM    387  CB  CYS A  62      12.693  20.000  53.139
ATOM    388  SG  CYS A  62      13.625  18.488  52.728
ATOM    389  N   ALA A  63      12.756  19.567  50.187
ATOM    390  CA  ALA A  63      13.439  19.732  48.948
ATOM    391  C   ALA A  63      12.419  20.037  47.931
ATOM    392  O   ALA A  63      12.508  20.915  47.077
ATOM    393  CB  ALA A  63      14.184  18.473  48.497
ATOM    394  N   GLY A  64      11.360  19.315  47.991
ATOM    395  CA  GLY A  64      10.473  19.646  47.014
ATOM    396  C   GLY A  64       9.685  20.939  47.143
ATOM    397  O   GLY A  64       9.571  21.694  46.174
ATOM    398  N   LEU A  65       9.089  21.214  48.304
ATOM    399  CA  LEU A  65       8.400  22.454  48.474
ATOM    400  C   LEU A  65       9.367  23.595  48.214
ATOM    401  O   LEU A  65       8.974  24.624  47.674
ATOM    402  CB  LEU A  65       7.718  22.547  49.839
ATOM    403  CG  LEU A  65       8.672  22.368  51.023
ATOM    404  CD1 LEU A  65       9.429  23.645  51.431
ATOM    405  CD2 LEU A  65       7.866  22.009  52.251
ATOM    406  N   ILE A  66      10.671  23.435  48.538
ATOM    407  CA  ILE A  66      11.656  24.482  48.419
ATOM    408  C   ILE A  66      11.781  24.879  46.990
ATOM    409  O   ILE A  66      11.806  26.056  46.641
ATOM    410  CB  ILE A  66      13.020  24.157  49.030
ATOM    411  CG1 ILE A  66      13.992  25.301  49.036
ATOM    412  CG2 ILE A  66      13.736  23.042  48.335
ATOM    413  CD1 ILE A  66      15.234  24.982  49.872
ATOM    414  N   GLY A  67      11.836  23.904  46.102
ATOM    415  CA  GLY A  67      12.003  24.223  44.762
ATOM    416  C   GLY A  67      10.814  24.731  44.053
ATOM    417  O   GLY A  67      10.898  25.569  43.155
ATOM    418  N   TRP A  68       9.667  24.186  44.438
ATOM    419  CA  TRP A  68       8.416  24.588  43.896
ATOM    420  C   TRP A  68       8.167  26.007  44.189
ATOM    421  O   TRP A  68       7.804  26.784  43.314
ATOM    422  CB  TRP A  68       7.310  23.729  44.471
ATOM    423  CG  TRP A  68       5.889  23.969  43.998
ATOM    424  CD1 TRP A  68       4.939  24.637  44.691
ATOM    425  CD2 TRP A  68       5.265  23.639  42.730
ATOM    426  NE1 TRP A  68       3.786  24.721  43.943
ATOM    427  CE2 TRP A  68       3.970  24.070  42.749
ATOM    428  CE3 TRP A  68       5.497  22.721  41.807
ATOM    429  CZ2 TRP A  68       3.107  23.835  41.687
ATOM    430  CZ3 TRP A  68       4.798  22.687  40.615
ATOM    431  CH2 TRP A  68       3.562  23.212  40.547
ATOM    432  N   GLN A  69       8.382  26.416  45.414
ATOM    433  CA  GLN A  69       8.147  27.781  45.599
ATOM    434  C   GLN A  69       9.172  28.698  45.098
ATOM    435  O   GLN A  69       8.846  29.825  44.738
ATOM    436  CB  GLN A  69       8.348  28.008  46.881
ATOM    437  CG  GLN A  69       8.178  29.503  47.351
ATOM    438  CD  GLN A  69       6.672  29.983  47.624
ATOM    439  OE1 GLN A  69       5.962  30.447  48.523
ATOM    440  NE2 GLN A  69       6.039  29.979  46.488
ATOM    441  N   SER A  70      10.434  28.261  45.027
ATOM    442  CA  SER A  70      11.444  29.034  44.377
ATOM    443  C   SER A  70      11.048  29.363  42.990
ATOM    444  O   SER A  70      11.273  30.477  42.519
ATOM    445  CB  SER A  70      12.786  28.292  44.434
ATOM    446  OG  SER A  70      13.785  29.018  43.766
ATOM    447  N   LEU A  71      10.418  28.402  42.312
ATOM    448  CA  LEU A  71      10.009  28.602  40.971
ATOM    449  C   LEU A  71       8.808  29.455  40.930
ATOM    450  O   LEU A  71       8.682  30.168  39.945
ATOM    451  CB  LEU A  71       9.691  27.281  40.263
ATOM    452  CG  LEU A  71      10.958  26.465  39.946
ATOM    453  CD1 LEU A  71      10.654  24.970  39.837
ATOM    454  CD2 LEU A  71      11.604  26.974  38.663
ATOM    455  N   LYS A  72       7.929  29.387  41.951
ATOM    456  CA  LYS A  72       6.772  30.211  42.050
ATOM    457  C   LYS A  72       6.908  31.672  41.595
ATOM    458  O   LYS A  72       6.493  32.791  41.773
ATOM    459  CB  LYS A  72       5.875  29.966  43.234
ATOM    460  CG  LYS A  72       5.192  28.596  43.197
ATOM    461  CD  LYS A  72       4.418  28.208  44.424
ATOM    462  CE  LYS A  72       3.176  29.082  44.586
ATOM    463  NZ  LYS A  72       2.405  28.688  45.770
ATOM    464  N   MET A  73       6.673  31.565  40.347
ATOM    465  CA  MET A  73       5.718  32.330  39.510
ATOM    466  C   MET A  73       6.086  31.907  38.108
ATOM    467  O   MET A  73       6.361  32.696  37.210
ATOM    468  CB  MET A  73       5.657  33.922  39.500
ATOM    469  CG  MET A  73       4.642  34.589  38.599
ATOM    470  SD  MET A  73       2.939  34.230  38.978
ATOM    471  CE  MET A  73       2.268  34.784  37.382
ATOM    472  N   ALA A  74       6.095  30.588  37.880
ATOM    473  CA  ALA A  74       6.465  29.988  36.639
ATOM    474  C   ALA A  74       5.751  30.497  35.436
ATOM    475  O   ALA A  74       6.341  30.580  34.366
ATOM    476  CB  ALA A  74       6.150  28.519  36.680
ATOM    477  N   GLY A  75       4.465  30.854  35.592
ATOM    478  CA  GLY A  75       3.635  31.362  34.532
ATOM    479  C   GLY A  75       4.097  32.707  34.044
ATOM    480  O   GLY A  75       3.653  33.194  33.007
ATOM    481  N   GLU A  76       5.006  33.358  34.772
ATOM    482  CA  GLU A  76       5.549  34.605  34.339
ATOM    483  C   GLU A  76       6.798  34.296  33.551
ATOM    484  O   GLU A  76       7.411  35.168  32.943
ATOM    485  CB  GLU A  76       5.852  35.471  35.551
ATOM    486  CG  GLU A  76       6.093  36.933  35.267
ATOM    487  CD  GLU A  76       7.551  37.143  34.936
ATOM    488  OE1 GLU A  76       8.381  36.239  35.228
ATOM    489  OE2 GLU A  76       7.833  38.224  34.363
ATOM    490  N   GLY A  77       7.178  33.007  33.507
ATOM    491  CA  GLY A  77       8.437  32.508  33.040
ATOM    492  C   GLY A  77       8.446  31.877  31.652
ATOM    493  O   GLY A  77       7.894  30.808  31.369
ATOM    494  N   ARG A  78       9.202  32.529  30.745
ATOM    495  CA  ARG A  78       9.358  32.096  29.382
ATOM    496  C   ARG A  78      10.347  30.977  29.281
ATOM    497  O   ARG A  78      10.235  30.081  28.441
ATOM    498  CB  ARG A  78       9.814  33.265  28.489
ATOM    499  CG  ARG A  78       9.779  32.906  27.006
ATOM    500  CD  ARG A  78      11.037  32.316  26.439
ATOM    501  NE  ARG A  78      11.916  33.399  26.303
ATOM    502  CZ  ARG A  78      13.094  33.273  26.851
ATOM    503  NH1 ARG A  78      13.154  32.763  28.228
ATOM    504  NH2 ARG A  78      13.575  34.323  26.256
ATOM    505  N   THR A  79      11.348  31.041  30.151
ATOM    506  CA  THR A  79      12.277  30.005  30.258
ATOM    507  C   THR A  79      12.891  30.192  31.618
ATOM    508  O   THR A  79      12.970  31.341  32.033
ATOM    509  CB  THR A  79      13.232  30.082  29.196
ATOM    510  OG1 THR A  79      12.884  29.927  27.842
ATOM    511  CG2 THR A  79      13.776  28.844  29.425
ATOM    512  N   ILE A  80      13.300  29.102  32.349
ATOM    513  CA  ILE A  80      14.033  29.106  33.610
ATOM    514  C   ILE A  80      15.244  28.162  33.543
ATOM    515  O   ILE A  80      15.285  27.236  32.740
ATOM    516  CB  ILE A  80      13.280  28.754  34.807
ATOM    517  CG1 ILE A  80      12.773  27.400  34.651
ATOM    518  CG2 ILE A  80      12.126  29.678  34.944
ATOM    519  CD1 ILE A  80      13.650  26.377  35.252
ATOM    520  N   GLY A  81      16.232  28.253  34.470
ATOM    521  CA  GLY A  81      17.537  27.673  34.278
ATOM    522  C   GLY A  81      17.722  27.254  35.611
ATOM    523  O   GLY A  81      17.512  28.020  36.548
ATOM    524  N   ILE A  82      18.042  25.981  35.692
ATOM    525  CA  ILE A  82      18.157  25.318  36.937
ATOM    526  C   ILE A  82      19.620  25.046  37.040
ATOM    527  O   ILE A  82      20.158  24.242  36.280
ATOM    528  CB  ILE A  82      17.404  24.009  37.008
ATOM    529  CG1 ILE A  82      15.910  24.233  37.043
ATOM    530  CG2 ILE A  82      17.726  23.227  38.276
ATOM    531  CD1 ILE A  82      15.466  24.138  35.688
ATOM    532  N   TYR A  83      20.297  25.694  37.999
ATOM    533  CA  TYR A  83      21.708  25.492  38.197
ATOM    534  C   TYR A  83      21.841  24.365  39.187
ATOM    535  O   TYR A  83      21.251  24.407  40.253
ATOM    536  CB  TYR A  83      22.404  26.782  38.680
ATOM    537  CG  TYR A  83      22.806  27.632  37.506
ATOM    538  CD1 TYR A  83      21.887  28.361  36.777
ATOM    539  CD2 TYR A  83      24.124  27.705  37.119
ATOM    540  CE1 TYR A  83      22.279  29.092  35.677
ATOM    541  CE2 TYR A  83      24.529  28.428  36.032
ATOM    542  CZ  TYR A  83      23.604  29.132  35.313
ATOM    543  OH  TYR A  83      24.016  29.874  34.192
ATOM    544  N   GLY A  84      22.536  23.269  38.831
ATOM    545  CA  GLY A  84      22.864  22.171  39.704
ATOM    546  C   GLY A  84      21.726  21.255  39.598
ATOM    547  O   GLY A  84      20.686  21.769  39.942
ATOM    548  N   PHE A  85      21.907  19.978  39.121
ATOM    549  CA  PHE A  85      20.928  18.911  39.016
ATOM    550  C   PHE A  85      21.144  17.840  40.037
ATOM    551  O   PHE A  85      21.406  16.705  39.677
ATOM    552  CB  PHE A  85      20.735  18.293  37.700
ATOM    553  CG  PHE A  85      19.669  17.309  37.514
ATOM    554  CD1 PHE A  85      18.373  17.701  37.282
ATOM    555  CD2 PHE A  85      20.053  16.002  37.385
ATOM    556  CE1 PHE A  85      17.483  16.724  36.930
ATOM    557  CE2 PHE A  85      19.141  15.033  37.294
ATOM    558  CZ  PHE A  85      17.904  15.425  37.038
ATOM    559  N   GLY A  86      21.066  18.151  41.341
ATOM    560  CA  GLY A  86      21.283  17.165  42.363
ATOM    561  C   GLY A  86      20.028  16.991  43.143
ATOM    562  O   GLY A  86      18.951  17.010  42.574
ATOM    563  N   ALA A  87      20.147  16.864  44.476
ATOM    564  CA  ALA A  87      19.055  16.601  45.374
ATOM    565  C   ALA A  87      17.856  17.467  45.089
ATOM    566  O   ALA A  87      16.745  16.969  44.926
ATOM    567  CB  ALA A  87      19.476  16.852  46.828
ATOM    568  N   ALA A  88      18.062  18.793  45.008
ATOM    569  CA  ALA A  88      16.981  19.709  44.778
ATOM    570  C   ALA A  88      16.757  19.883  43.313
ATOM    571  O   ALA A  88      15.641  19.846  42.819
ATOM    572  CB  ALA A  88      17.250  21.073  45.426
ATOM    573  N   ALA A  89      17.809  20.068  42.552
ATOM    574  CA  ALA A  89      17.612  20.329  41.188
ATOM    575  C   ALA A  89      16.892  19.372  40.318
ATOM    576  O   ALA A  89      16.105  19.823  39.501
ATOM    577  CB  ALA A  89      18.848  20.163  40.711
ATOM    578  N   HIS A  90      17.095  18.051  40.469
ATOM    579  CA  HIS A  90      16.351  17.108  39.715
ATOM    580  C   HIS A  90      14.889  17.184  39.900
ATOM    581  O   HIS A  90      14.120  16.893  38.982
ATOM    582  CB  HIS A  90      16.866  15.661  39.874
ATOM    583  CG  HIS A  90      16.734  15.100  41.233
ATOM    584  ND1 HIS A  90      15.555  14.539  41.644
ATOM    585  CD2 HIS A  90      17.677  14.958  42.194
ATOM    586  CE1 HIS A  90      15.773  14.235  42.907
ATOM    587  NE2 HIS A  90      17.019  14.534  43.322
ATOM    588  N   ILE A  91      14.483  17.646  41.081
ATOM    589  CA  ILE A  91      13.109  17.804  41.434
ATOM    590  C   ILE A  91      12.617  19.118  40.854
ATOM    591  O   ILE A  91      11.470  19.232  40.421
ATOM    592  CB  ILE A  91      12.947  17.759  42.947
ATOM    593  CG1 ILE A  91      13.375  16.397  43.527
ATOM    594  CG2 ILE A  91      11.500  18.037  43.372
ATOM    595  CD1 ILE A  91      13.445  16.378  45.055
ATOM    596  N   LEU A  92      13.472  20.152  40.823
ATOM    597  CA  LEU A  92      13.120  21.443  40.304
ATOM    598  C   LEU A  92      12.763  21.346  38.856
ATOM    599  O   LEU A  92      11.781  21.944  38.418
ATOM    600  CB  LEU A  92      14.289  22.436  40.423
ATOM    601  CG  LEU A  92      14.677  22.724  41.862
ATOM    602  CD1 LEU A  92      15.930  23.567  42.050
ATOM    603  CD2 LEU A  92      13.598  23.433  42.510
ATOM    604  N   VAL A  93      13.546  20.567  38.087
ATOM    605  CA  VAL A  93      13.334  20.369  36.676
ATOM    606  C   VAL A  93      11.912  19.929  36.448
ATOM    607  O   VAL A  93      11.247  20.412  35.534
ATOM    608  CB  VAL A  93      14.274  19.327  36.098
ATOM    609  CG1 VAL A  93      13.965  19.037  34.618
ATOM    610  CG2 VAL A  93      15.720  19.823  36.228
ATOM    611  N   GLN A  94      11.419  19.013  37.295
ATOM    612  CA  GLN A  94      10.134  18.424  37.131
ATOM    613  C   GLN A  94       9.013  19.378  37.472
ATOM    614  O   GLN A  94       7.991  19.408  36.785
ATOM    615  CB  GLN A  94      10.008  17.145  37.976
ATOM    616  CG  GLN A  94       8.667  16.442  37.874
ATOM    617  CD  GLN A  94       8.471  15.800  36.505
ATOM    618  OE1 GLN A  94       8.473  14.576  36.397
ATOM    619  NE2 GLN A  94       8.271  16.618  35.438
ATOM    620  N   VAL A  95       9.169  20.166  38.542
ATOM    621  CA  VAL A  95       8.190  21.114  38.943
ATOM    622  C   VAL A  95       8.035  22.139  37.840
ATOM    623  O   VAL A  95       6.926  22.500  37.475
ATOM    624  CB  VAL A  95       8.673  21.751  40.217
ATOM    625  CG1 VAL A  95       7.895  22.972  40.391
ATOM    626  CG2 VAL A  95       8.531  20.782  41.399
ATOM    627  N   CYS A  96       9.145  22.635  37.289
ATOM    628  CA  CYS A  96       9.138  23.648  36.276
ATOM    629  C   CYS A  96       8.349  23.198  35.068
ATOM    630  O   CYS A  96       7.556  23.956  34.514
ATOM    631  CB  CYS A  96      10.584  23.960  35.885
ATOM    632  SG  CYS A  96      10.703  25.203  34.638
ATOM    633  N   LYS A  97       8.517  21.936  34.643
ATOM    634  CA  LYS A  97       7.784  21.413  33.522
ATOM    635  C   LYS A  97       6.321  21.293  33.854
ATOM    636  O   LYS A  97       5.456  21.556  33.019
ATOM    637  CB  LYS A  97       8.312  20.027  33.096
ATOM    638  CG  LYS A  97       9.769  20.035  32.594
ATOM    639  CD  LYS A  97      10.031  21.024  31.468
ATOM    640  CE  LYS A  97       9.152  20.749  30.244
ATOM    641  NZ  LYS A  97       9.292  21.803  29.232
ATOM    642  N   HIS A  98       5.997  20.928  35.102
ATOM    643  CA  HIS A  98       4.625  20.808  35.523
ATOM    644  C   HIS A  98       3.997  22.183  35.598
ATOM    645  O   HIS A  98       2.777  22.336  35.583
ATOM    646  CB  HIS A  98       4.510  20.097  36.887
ATOM    647  CG  HIS A  98       3.098  19.766  37.296
ATOM    648  ND1 HIS A  98       2.320  20.711  37.948
ATOM    649  CD2 HIS A  98       2.402  18.603  37.149
ATOM    650  CE1 HIS A  98       1.158  20.116  38.145
ATOM    651  NE2 HIS A  98       1.162  18.836  37.702
ATOM    652  N   ARG A  99       4.833  23.236  35.638
ATOM    653  CA  ARG A  99       4.397  24.588  35.773
ATOM    654  C   ARG A  99       4.392  25.284  34.427
ATOM    655  O   ARG A  99       4.199  26.498  34.336
ATOM    656  CB  ARG A  99       5.307  25.342  36.738
ATOM    657  CG  ARG A  99       5.158  24.875  38.179
ATOM    658  CD  ARG A  99       6.122  25.550  39.158
ATOM    659  NE  ARG A  99       5.738  26.969  39.290
ATOM    660  CZ  ARG A  99       4.744  27.382  40.134
ATOM    661  NH1 ARG A  99       4.086  26.464  40.916
ATOM    662  NH2 ARG A  99       4.378  28.703  40.149
ATOM    663  N   GLY A 100       4.589  24.515  33.340
ATOM    664  CA  GLY A 100       4.474  25.014  31.994
ATOM    665  C   GLY A 100       5.704  25.737  31.507
ATOM    666  O   GLY A 100       5.635  26.466  30.518
ATOM    667  N   GLN A 101       6.872  25.548  32.149
ATOM    668  CA  GLN A 101       8.037  26.289  31.758
ATOM    669  C   GLN A 101       8.981  25.439  30.961
ATOM    670  O   GLN A 101       8.985  24.206  31.010
ATOM    671  CB  GLN A 101       8.756  26.800  32.966
ATOM    672  CG  GLN A 101       8.039  27.848  33.750
ATOM    673  CD  GLN A 101       8.799  28.242  35.012
ATOM    674  OE1 GLN A 101       8.872  27.586  36.053
ATOM    675  NE2 GLN A 101       9.297  29.490  34.948
ATOM    676  N   SER A 102       9.818  26.113  30.160
ATOM    677  CA  SER A 102      10.789  25.430  29.372
ATOM    678  C   SER A 102      12.052  25.509  30.179
ATOM    679  O   SER A 102      12.318  26.541  30.795
ATOM    680  CB  SER A 102      10.969  26.090  28.005
ATOM    681  OG  SER A 102      11.442  27.396  28.192
ATOM    682  N   VAL A 103      12.850  24.413  30.215
ATOM    683  CA  VAL A 103      13.959  24.333  31.132
ATOM    684  C   VAL A 103      15.319  24.147  30.505
ATOM    685  O   VAL A 103      15.499  23.435  29.511
ATOM    686  CB  VAL A 103      13.752  23.257  32.136
ATOM    687  CG1 VAL A 103      13.643  21.959  31.490
ATOM    688  CG2 VAL A 103      14.926  23.142  33.032
ATOM    689  N   TYR A 104      16.325  24.834  31.131
ATOM    690  CA  TYR A 104      17.694  24.729  30.812
ATOM    691  C   TYR A 104      18.397  24.202  31.941
ATOM    692  O   TYR A 104      18.478  24.894  32.941
ATOM    693  CB  TYR A 104      18.317  25.933  30.382
ATOM    694  CG  TYR A 104      17.336  25.808  29.097
ATOM    695  CD1 TYR A 104      15.908  26.474  29.023
ATOM    696  CD2 TYR A 104      18.016  25.689  27.765
ATOM    697  CE1 TYR A 104      15.311  27.042  27.783
ATOM    698  CE2 TYR A 104      17.373  26.252  26.487
ATOM    699  CZ  TYR A 104      15.965  26.876  26.535
ATOM    700  OH  TYR A 104      15.658  28.184  26.066
ATOM    701  N   ALA A 105      18.896  22.976  31.846
ATOM    702  CA  ALA A 105      19.569  22.422  32.970
ATOM    703  C   ALA A 105      21.028  22.612  32.887
ATOM    704  O   ALA A 105      21.629  22.376  31.842
ATOM    705  CB  ALA A 105      19.359  20.986  32.990
ATOM    706  N   PHE A 106      21.641  23.042  34.005
ATOM    707  CA  PHE A 106      23.019  23.440  33.981
ATOM    708  C   PHE A 106      23.713  23.023  35.200
ATOM    709  O   PHE A 106      23.143  22.922  36.272
ATOM    710  CB  PHE A 106      23.248  24.919  34.283
ATOM    711  CG  PHE A 106      22.756  25.758  33.194
ATOM    712  CD1 PHE A 106      21.544  26.386  33.248
ATOM    713  CD2 PHE A 106      23.603  26.074  32.204
ATOM    714  CE1 PHE A 106      21.149  27.215  32.238
ATOM    715  CE2 PHE A 106      23.221  26.882  31.184
ATOM    716  CZ  PHE A 106      21.966  27.433  31.178
ATOM    717  N   VAL A 107      25.023  22.890  35.158
ATOM    718  CA  VAL A 107      25.590  22.012  36.126
ATOM    719  C   VAL A 107      26.958  22.289  36.364
ATOM    720  O   VAL A 107      27.500  23.142  35.685
ATOM    721  CB  VAL A 107      25.648  20.663  35.738
ATOM    722  CG1 VAL A 107      24.306  20.364  36.612
ATOM    723  CG2 VAL A 107      26.205  20.672  34.162
ATOM    724  N   LEU A 108      27.548  21.564  37.327
ATOM    725  CA  LEU A 108      28.896  21.832  37.650
ATOM    726  C   LEU A 108      29.797  21.002  36.818
ATOM    727  O   LEU A 108      29.333  20.051  36.195
ATOM    728  CB  LEU A 108      29.219  21.570  39.118
ATOM    729  CG  LEU A 108      28.782  22.728  39.972
ATOM    730  CD1 LEU A 108      29.430  23.993  39.508
ATOM    731  CD2 LEU A 108      27.258  22.934  40.034
ATOM    732  N   PRO A 109      31.074  21.362  36.757
ATOM    733  CA  PRO A 109      31.952  20.535  35.956
ATOM    734  C   PRO A 109      32.000  19.098  36.366
ATOM    735  O   PRO A 109      31.826  18.755  37.533
ATOM    736  CB  PRO A 109      33.289  21.323  35.904
ATOM    737  CG  PRO A 109      32.966  22.762  36.430
ATOM    738  CD  PRO A 109      31.422  22.784  36.506
ATOM    739  N   GLY A 110      32.172  18.216  35.378
ATOM    740  CA  GLY A 110      32.275  16.843  35.737
ATOM    741  C   GLY A 110      30.969  16.131  35.601
ATOM    742  O   GLY A 110      30.957  14.907  35.630
ATOM    743  N   ASP A 111      29.828  16.801  35.441
ATOM    744  CA  ASP A 111      28.624  16.041  35.259
ATOM    745  C   ASP A 111      28.589  15.935  33.712
ATOM    746  O   ASP A 111      29.279  16.601  32.974
ATOM    747  CB  ASP A 111      27.424  16.962  35.650
ATOM    748  CG  ASP A 111      27.373  17.310  37.148
ATOM    749  OD1 ASP A 111      28.280  18.011  37.666
ATOM    750  OD2 ASP A 111      26.362  16.909  37.783
ATOM    751  N   GLU A 112      27.541  15.521  33.028
ATOM    752  CA  GLU A 112      27.167  14.685  31.915
ATOM    753  C   GLU A 112      26.168  13.727  32.373
ATOM    754  O   GLU A 112      25.121  13.548  31.753
ATOM    755  CB  GLU A 112      28.142  14.132  30.871
ATOM    756  CG  GLU A 112      27.431  13.474  29.670
ATOM    757  CD  GLU A 112      26.736  14.515  28.808
ATOM    758  OE1 GLU A 112      26.982  15.735  29.003
ATOM    759  OE2 GLU A 112      25.948  14.090  27.923
ATOM    760  N   ALA A 113      26.467  13.113  33.511
ATOM    761  CA  ALA A 113      25.594  12.143  34.083
ATOM    762  C   ALA A 113      24.324  12.845  34.473
ATOM    763  O   ALA A 113      23.228  12.429  34.099
ATOM    764  CB  ALA A 113      26.230  11.496  35.320
ATOM    765  N   GLY A 114      24.457  13.963  35.212
ATOM    766  CA  GLY A 114      23.337  14.719  35.697
ATOM    767  C   GLY A 114      22.545  15.338  34.582
ATOM    768  O   GLY A 114      21.325  15.429  34.656
ATOM    769  N   ARG A 115      23.210  15.796  33.511
ATOM    770  CA  ARG A 115      22.515  16.407  32.414
ATOM    771  C   ARG A 115      21.695  15.425  31.665
ATOM    772  O   ARG A 115      20.591  15.750  31.239
ATOM    773  CB  ARG A 115      23.454  17.056  31.387
ATOM    774  CG  ARG A 115      24.268  18.212  31.864
ATOM    775  CD  ARG A 115      23.372  19.502  32.142
ATOM    776  NE  ARG A 115      22.226  19.378  33.115
ATOM    777  CZ  ARG A 115      22.589  19.142  34.352
ATOM    778  NH1 ARG A 115      23.835  19.296  34.287
ATOM    779  NH2 ARG A 115      21.694  19.467  35.378
ATOM    780  N   LYS A 116      22.200  14.201  31.495
ATOM    781  CA  LYS A 116      21.461  13.191  30.809
ATOM    782  C   LYS A 116      20.228  12.875  31.612
ATOM    783  O   LYS A 116      19.156  12.644  31.055
ATOM    784  CB  LYS A 116      22.313  11.934  30.582
ATOM    785  CG  LYS A 116      21.710  10.966  29.569
ATOM    786  CD  LYS A 116      20.686  10.005  30.186
ATOM    787  CE  LYS A 116      20.097   9.027  29.189
ATOM    788  NZ  LYS A 116      19.283   9.732  28.174
ATOM    789  N   PHE A 117      20.353  12.876  32.946
ATOM    790  CA  PHE A 117      19.250  12.626  33.826
ATOM    791  C   PHE A 117      18.228  13.703  33.646
ATOM    792  O   PHE A 117      17.039  13.430  33.522
ATOM    793  CB  PHE A 117      19.697  12.600  35.301
ATOM    794  CG  PHE A 117      20.623  11.467  35.648
ATOM    795  CD1 PHE A 117      20.738  10.340  34.853
ATOM    796  CD2 PHE A 117      21.376  11.520  36.814
ATOM    797  CE1 PHE A 117      21.577   9.314  35.192
ATOM    798  CE2 PHE A 117      22.215  10.482  37.159
ATOM    799  CZ  PHE A 117      22.317   9.379  36.345
ATOM    800  N   THR A 118      18.665  14.964  33.606
ATOM    801  CA  THR A 118      17.785  16.053  33.427
ATOM    802  C   THR A 118      16.995  15.933  32.134
ATOM    803  O   THR A 118      15.833  16.341  32.088
ATOM    804  CB  THR A 118      18.583  17.312  33.458
ATOM    805  OG1 THR A 118      19.290  17.484  34.659
ATOM    806  CG2 THR A 118      17.589  18.389  33.358
ATOM    807  N   LEU A 119      17.604  15.439  31.054
ATOM    808  CA  LEU A 119      16.909  15.310  29.809
ATOM    809  C   LEU A 119      15.795  14.325  29.984
ATOM    810  O   LEU A 119      14.687  14.528  29.492
ATOM    811  CB  LEU A 119      17.837  14.831  28.689
ATOM    812  CG  LEU A 119      18.931  15.864  28.337
ATOM    813  CD1 LEU A 119      19.963  15.288  27.363
ATOM    814  CD2 LEU A 119      18.353  17.168  27.774
ATOM    815  N   ASP A 120      16.060  13.248  30.736
ATOM    816  CA  ASP A 120      15.102  12.206  30.980
ATOM    817  C   ASP A 120      13.983  12.731  31.853
ATOM    818  O   ASP A 120      12.842  12.277  31.768
ATOM    819  CB  ASP A 120      15.749  10.985  31.677
ATOM    820  CG  ASP A 120      16.657  10.191  30.730
ATOM    821  OD1 ASP A 120      16.614  10.392  29.483
ATOM    822  OD2 ASP A 120      17.440   9.353  31.254
ATOM    823  N   LEU A 121      14.266  13.727  32.713
ATOM    824  CA  LEU A 121      13.275  14.291  33.585
ATOM    825  C   LEU A 121      12.503  15.407  32.938
ATOM    826  O   LEU A 121      11.565  15.930  33.543
ATOM    827  CB  LEU A 121      13.907  14.824  34.870
ATOM    828  CG  LEU A 121      14.466  13.676  35.722
ATOM    829  CD1 LEU A 121      15.090  14.253  36.910
ATOM    830  CD2 LEU A 121      13.437  12.711  36.263
ATOM    831  N   GLY A 122      12.856  15.800  31.695
ATOM    832  CA  GLY A 122      12.053  16.754  30.967
ATOM    833  C   GLY A 122      12.775  17.993  30.526
ATOM    834  O   GLY A 122      12.150  18.865  29.916
ATOM    835  N   ALA A 123      14.087  18.105  30.799
ATOM    836  CA  ALA A 123      14.810  19.237  30.337
ATOM    837  C   ALA A 123      14.696  19.532  28.894
ATOM    838  O   ALA A 123      14.821  18.609  28.111
ATOM    839  CB  ALA A 123      16.246  19.354  30.706
ATOM    840  N   VAL A 124      14.454  20.804  28.499
ATOM    841  CA  VAL A 124      14.251  21.138  27.114
ATOM    842  C   VAL A 124      15.599  21.414  26.475
ATOM    843  O   VAL A 124      15.827  21.062  25.315
ATOM    844  CB  VAL A 124      13.315  22.326  26.964
ATOM    845  CG1 VAL A 124      13.146  22.732  25.503
ATOM    846  CG2 VAL A 124      11.926  21.950  27.491
ATOM    847  N   TRP A 125      16.523  22.074  27.202
ATOM    848  CA  TRP A 125      17.824  22.329  26.653
ATOM    849  C   TRP A 125      18.779  22.360  27.809
ATOM    850  O   TRP A 125      18.403  22.558  28.940
ATOM    851  CB  TRP A 125      17.820  23.601  25.936
ATOM    852  CG  TRP A 125      17.016  23.915  24.726
ATOM    853  CD1 TRP A 125      15.800  24.527  24.674
ATOM    854  CD2 TRP A 125      17.386  23.608  23.382
ATOM    855  NE1 TRP A 125      15.329  24.504  23.398
ATOM    856  CE2 TRP A 125      16.300  23.947  22.584
ATOM    857  CE3 TRP A 125      18.518  23.047  22.846
ATOM    858  CZ2 TRP A 125      16.330  23.727  21.232
ATOM    859  CZ3 TRP A 125      18.544  22.826  21.479
ATOM    860  CH2 TRP A 125      17.466  23.162  20.684
ATOM    861  N   ALA A 126      20.049  22.049  27.634
ATOM    862  CA  ALA A 126      20.947  21.939  28.802
ATOM    863  C   ALA A 126      22.195  22.403  28.341
ATOM    864  O   ALA A 126      22.132  22.203  27.190
ATOM    865  CB  ALA A 126      21.308  20.505  29.118
ATOM    866  N   GLY A 127      23.216  22.966  29.054
ATOM    867  CA  GLY A 127      24.636  22.975  28.736
ATOM    868  C   GLY A 127      25.030  24.267  29.221
ATOM    869  O   GLY A 127      24.839  24.699  30.348
ATOM    870  N   PHE A 128      25.179  24.926  28.100
ATOM    871  CA  PHE A 128      24.061  25.418  27.265
ATOM    872  C   PHE A 128      23.207  26.333  27.970
ATOM    873  O   PHE A 128      22.277  26.064  28.743
ATOM    874  CB  PHE A 128      23.107  24.595  26.308
ATOM    875  CG  PHE A 128      23.751  23.348  25.553
ATOM    876  CD1 PHE A 128      25.013  23.531  25.152
ATOM    877  CD2 PHE A 128      23.212  22.105  25.034
ATOM    878  CE1 PHE A 128      25.537  22.636  24.275
ATOM    879  CE2 PHE A 128      23.873  21.011  24.598
ATOM    880  CZ  PHE A 128      25.012  21.395  23.985
ATOM    881  N   SER A 129      23.626  27.483  27.539
ATOM    882  CA  SER A 129      23.174  28.637  28.006
ATOM    883  C   SER A 129      23.015  29.366  26.681
ATOM    884  O   SER A 129      22.986  29.105  25.522
ATOM    885  CB  SER A 129      24.148  29.664  28.666
ATOM    886  OG  SER A 129      24.509  29.243  29.920
ATOM    887  N   GLY A 130      23.186  30.614  26.620
ATOM    888  CA  GLY A 130      22.094  31.080  25.988
ATOM    889  C   GLY A 130      21.507  32.087  25.433
ATOM    890  O   GLY A 130      20.368  32.135  24.997
ATOM    891  N   GLU A 131      22.215  33.015  25.742
ATOM    892  CA  GLU A 131      21.870  34.147  25.118
ATOM    893  C   GLU A 131      21.664  33.784  23.648
ATOM    894  O   GLU A 131      20.682  34.218  23.065
ATOM    895  CB  GLU A 131      23.031  35.015  25.352
ATOM    896  CG  GLU A 131      23.144  35.489  26.809
ATOM    897  CD  GLU A 131      23.640  34.385  27.726
ATOM    898  OE1 GLU A 131      24.635  33.691  27.395
ATOM    899  OE2 GLU A 131      22.926  34.128  28.711
ATOM    900  N   LYS A 132      22.453  32.836  23.086
ATOM    901  CA  LYS A 132      22.287  32.347  21.774
ATOM    902  C   LYS A 132      21.099  31.401  21.543
ATOM    903  O   LYS A 132      20.388  31.668  20.571
ATOM    904  CB  LYS A 132      23.656  31.843  21.232
ATOM    905  CG  LYS A 132      24.346  30.583  21.751
ATOM    906  CD  LYS A 132      24.560  30.425  23.296
ATOM    907  CE  LYS A 132      24.916  28.972  23.764
ATOM    908  NZ  LYS A 132      25.500  29.054  25.149
ATOM    909  N   PRO A 133      20.866  30.294  22.303
ATOM    910  CA  PRO A 133      19.716  29.483  22.073
ATOM    911  C   PRO A 133      18.412  30.132  22.397
ATOM    912  O   PRO A 133      17.638  30.334  21.462
ATOM    913  CB  PRO A 133      20.170  27.958  22.602
ATOM    914  CG  PRO A 133      21.569  28.010  22.995
ATOM    915  CD  PRO A 133      21.909  29.283  22.351
ATOM    916  N   PRO A 134      18.041  30.123  23.598
ATOM    917  CA  PRO A 134      16.875  30.947  23.988
ATOM    918  C   PRO A 134      16.943  31.454  25.361
ATOM    919  O   PRO A 134      15.994  31.998  25.968
ATOM    920  CB  PRO A 134      15.761  29.936  23.921
ATOM    921  CG  PRO A 134      16.353  28.513  23.553
ATOM    922  CD  PRO A 134      17.621  28.752  23.220
ATOM    923  N   VAL A 135      18.206  31.248  25.720
ATOM    924  CA  VAL A 135      19.131  30.498  26.625
ATOM    925  C   VAL A 135      18.778  30.003  27.937
ATOM    926  O   VAL A 135      19.380  29.719  29.035
ATOM    927  CB  VAL A 135      19.893  31.205  27.757
ATOM    928  CG1 VAL A 135      19.705  32.650  27.800
ATOM    929  CG2 VAL A 135      21.335  30.725  28.598
ATOM    930  N   PRO A 136      17.679  30.111  27.704
ATOM    931  CA  PRO A 136      16.931  30.101  28.847
ATOM    932  C   PRO A 136      16.563  30.896  29.738
ATOM    933  O   PRO A 136      15.749  30.190  30.233
ATOM    934  CB  PRO A 136      17.154  28.835  29.587
ATOM    935  CG  PRO A 136      17.797  28.211  28.396
ATOM    936  CD  PRO A 136      17.982  28.826  27.234
ATOM    937  N   LEU A 137      16.807  32.123  30.033
ATOM    938  CA  LEU A 137      15.654  32.277  30.870
ATOM    939  C   LEU A 137      15.299  33.556  31.226
ATOM    940  O   LEU A 137      16.169  34.360  31.442
ATOM    941  CB  LEU A 137      15.745  31.588  32.252
ATOM    942  CG  LEU A 137      17.096  31.499  32.578
ATOM    943  CD1 LEU A 137      16.783  32.407  33.479
ATOM    944  CD2 LEU A 137      17.461  30.367  33.218
ATOM    945  N   ASP A 138      14.012  33.708  31.485
ATOM    946  CA  ASP A 138      13.549  34.874  32.174
ATOM    947  C   ASP A 138      13.886  34.814  33.661
ATOM    948  O   ASP A 138      13.843  35.801  34.379
ATOM    949  CB  ASP A 138      12.030  35.004  32.013
ATOM    950  CG  ASP A 138      11.532  36.397  32.371
ATOM    951  OD1 ASP A 138      11.726  36.860  33.516
ATOM    952  OD2 ASP A 138      10.924  37.018  31.463
ATOM    953  N   ALA A 139      14.266  33.651  34.201
ATOM    954  CA  ALA A 139      14.713  33.490  35.578
ATOM    955  C   ALA A 139      15.536  32.252  35.993
ATOM    956  O   ALA A 139      15.440  31.164  35.456
ATOM    957  CB  ALA A 139      13.507  33.272  36.423
ATOM    958  N   ALA A 140      16.417  32.315  36.975
ATOM    959  CA  ALA A 140      17.322  31.209  37.197
ATOM    960  C   ALA A 140      17.150  30.824  38.624
ATOM    961  O   ALA A 140      16.888  31.690  39.447
ATOM    962  CB  ALA A 140      18.767  31.598  36.923
ATOM    963  N   ILE A 141      17.263  29.515  38.938
ATOM    964  CA  ILE A 141      17.108  28.981  40.260
ATOM    965  C   ILE A 141      18.429  28.324  40.529
ATOM    966  O   ILE A 141      18.797  27.373  39.842
ATOM    967  CB  ILE A 141      15.978  27.971  40.391
ATOM    968  CG1 ILE A 141      14.613  28.644  40.175
ATOM    969  CG2 ILE A 141      15.987  27.307  41.778
ATOM    970  CD1 ILE A 141      14.233  28.794  38.705
ATOM    971  N   ILE A 142      19.170  28.834  41.529
ATOM    972  CA  ILE A 142      20.482  28.392  41.838
ATOM    973  C   ILE A 142      20.301  27.522  42.992
ATOM    974  O   ILE A 142      20.171  27.922  44.155
ATOM    975  CB  ILE A 142      21.488  29.473  42.143
ATOM    976  CG1 ILE A 142      21.771  30.265  40.867
ATOM    977  CG2 ILE A 142      22.825  28.919  42.681
ATOM    978  CD1 ILE A 142      20.740  31.349  40.602
ATOM    979  N   PHE A 143      20.413  26.255  42.655
ATOM    980  CA  PHE A 143      21.359  25.611  43.506
ATOM    981  C   PHE A 143      22.661  25.524  42.841
ATOM    982  O   PHE A 143      22.701  25.669  41.644
ATOM    983  CB  PHE A 143      20.854  24.292  44.000
ATOM    984  CG  PHE A 143      21.812  23.714  44.984
ATOM    985  CD1 PHE A 143      21.877  24.180  46.279
ATOM    986  CD2 PHE A 143      22.663  22.698  44.595
ATOM    987  CE1 PHE A 143      22.755  23.623  47.181
ATOM    988  CE2 PHE A 143      23.558  22.157  45.486
ATOM    989  CZ  PHE A 143      23.591  22.605  46.784
ATOM    990  N   ALA A 144      23.755  25.379  43.604
ATOM    991  CA  ALA A 144      25.039  25.135  43.068
ATOM    992  C   ALA A 144      26.078  25.742  43.987
ATOM    993  O   ALA A 144      25.713  26.511  44.878
ATOM    994  CB  ALA A 144      25.265  25.719  41.708
ATOM    995  N   PRO A 145      27.362  25.406  43.787
ATOM    996  CA  PRO A 145      28.387  25.936  44.681
ATOM    997  C   PRO A 145      28.587  27.420  44.714
ATOM    998  O   PRO A 145      28.141  28.152  43.834
ATOM    999  CB  PRO A 145      29.690  25.181  44.274
ATOM   1000  CG  PRO A 145      29.253  24.025  43.329
ATOM   1001  CD  PRO A 145      27.714  23.993  43.499
ATOM   1002  N   ALA A 146      29.283  27.888  45.757
ATOM   1003  CA  ALA A 146      29.546  29.281  45.909
ATOM   1004  C   ALA A 146      30.355  29.868  44.780
ATOM   1005  O   ALA A 146      31.318  29.295  44.269
ATOM   1006  CB  ALA A 146      30.384  29.567  47.155
ATOM   1007  N   GLY A 147      29.930  31.092  44.423
ATOM   1008  CA  GLY A 147      30.611  32.135  43.730
ATOM   1009  C   GLY A 147      30.533  31.894  42.291
ATOM   1010  O   GLY A 147      29.904  32.652  41.687
ATOM   1011  N   GLU A 148      31.087  30.925  41.607
ATOM   1012  CA  GLU A 148      31.040  30.850  40.163
ATOM   1013  C   GLU A 148      29.659  30.553  39.575
ATOM   1014  O   GLU A 148      29.299  30.994  38.485
ATOM   1015  CB  GLU A 148      32.046  29.762  39.855
ATOM   1016  CG  GLU A 148      32.507  29.680  38.444
ATOM   1017  CD  GLU A 148      31.537  28.864  37.720
ATOM   1018  OE1 GLU A 148      31.068  27.749  38.076
ATOM   1019  OE2 GLU A 148      31.323  29.477  36.670
ATOM   1020  N   LEU A 149      28.824  29.810  40.299
ATOM   1021  CA  LEU A 149      27.544  29.418  39.798
ATOM   1022  C   LEU A 149      26.629  30.590  39.771
ATOM   1023  O   LEU A 149      25.880  30.781  38.814
ATOM   1024  CB  LEU A 149      26.948  28.322  40.664
ATOM   1025  CG  LEU A 149      27.622  26.985  40.301
ATOM   1026  CD1 LEU A 149      27.217  26.499  38.894
ATOM   1027  CD2 LEU A 149      29.085  26.965  40.676
ATOM   1028  N   VAL A 150      26.692  31.422  40.821
ATOM   1029  CA  VAL A 150      25.903  32.618  40.917
ATOM   1030  C   VAL A 150      26.311  33.611  39.821
ATOM   1031  O   VAL A 150      25.397  34.180  39.221
ATOM   1032  CB  VAL A 150      25.974  33.256  42.306
ATOM   1033  CG1 VAL A 150      25.231  34.596  42.349
ATOM   1034  CG2 VAL A 150      25.467  32.307  43.386
ATOM   1035  N   PRO A 151      27.594  33.888  39.511
ATOM   1036  CA  PRO A 151      27.906  34.739  38.379
ATOM   1037  C   PRO A 151      27.428  34.248  37.122
ATOM   1038  O   PRO A 151      26.949  35.091  36.377
ATOM   1039  CB  PRO A 151      29.453  34.970  38.410
ATOM   1040  CG  PRO A 151      29.889  34.470  39.772
ATOM   1041  CD  PRO A 151      28.473  34.441  40.526
ATOM   1042  N   MET A 152      27.526  32.947  36.866
ATOM   1043  CA  MET A 152      27.067  32.431  35.624
ATOM   1044  C   MET A 152      25.592  32.662  35.491
ATOM   1045  O   MET A 152      25.126  33.151  34.469
ATOM   1046  CB  MET A 152      27.350  30.938  35.522
ATOM   1047  CG  MET A 152      28.834  30.630  35.376
ATOM   1048  SD  MET A 152      29.122  28.834  35.330
ATOM   1049  CE  MET A 152      28.644  28.476  33.653
ATOM   1050  N   ALA A 153      24.814  32.331  36.530
ATOM   1051  CA  ALA A 153      23.388  32.483  36.515
ATOM   1052  C   ALA A 153      22.996  33.921  36.319
ATOM   1053  O   ALA A 153      22.111  34.233  35.527
ATOM   1054  CB  ALA A 153      22.774  31.968  37.814
ATOM   1055  N   LEU A 154      23.674  34.844  37.014
ATOM   1056  CA  LEU A 154      23.413  36.248  36.920
ATOM   1057  C   LEU A 154      23.621  36.699  35.489
ATOM   1058  O   LEU A 154      22.918  37.568  34.978
ATOM   1059  CB  LEU A 154      24.317  37.018  37.902
ATOM   1060  CG  LEU A 154      23.838  38.428  38.254
ATOM   1061  CD1 LEU A 154      24.661  39.087  39.344
ATOM   1062  CD2 LEU A 154      24.020  39.342  37.140
ATOM   1063  N   ASP A 155      24.582  36.105  34.781
ATOM   1064  CA  ASP A 155      24.912  36.496  33.439
ATOM   1065  C   ASP A 155      24.023  35.872  32.391
ATOM   1066  O   ASP A 155      23.981  36.371  31.265
ATOM   1067  CB  ASP A 155      26.379  36.177  33.118
ATOM   1068  CG  ASP A 155      27.269  37.271  33.731
ATOM   1069  OD1 ASP A 155      28.498  37.035  33.863
ATOM   1070  OD2 ASP A 155      26.750  38.370  34.082
ATOM   1071  N   VAL A 156      23.268  34.798  32.723
ATOM   1072  CA  VAL A 156      22.478  34.096  31.748
ATOM   1073  C   VAL A 156      21.044  34.608  31.642
ATOM   1074  O   VAL A 156      20.299  34.343  30.693
ATOM   1075  CB  VAL A 156      22.504  32.607  32.000
ATOM   1076  CG1 VAL A 156      21.557  31.907  31.119
ATOM   1077  CG2 VAL A 156      23.909  32.052  31.703
ATOM   1078  N   VAL A 157      20.594  35.358  32.642
ATOM   1079  CA  VAL A 157      19.239  35.829  32.723
ATOM   1080  C   VAL A 157      19.085  37.066  31.854
ATOM   1081  O   VAL A 157      20.003  37.875  31.693
ATOM   1082  CB  VAL A 157      18.862  36.149  34.138
ATOM   1083  CG1 VAL A 157      18.897  34.932  35.057
ATOM   1084  CG2 VAL A 157      19.942  37.050  34.603
ATOM   1085  N   ARG A 158      17.885  37.253  31.275
ATOM   1086  CA  ARG A 158      17.644  38.387  30.427
ATOM   1087  C   ARG A 158      17.288  39.559  31.288
ATOM   1088  O   ARG A 158      16.982  39.405  32.465
ATOM   1089  CB  ARG A 158      16.528  38.123  29.417
ATOM   1090  CG  ARG A 158      16.989  37.114  28.364
ATOM   1091  CD  ARG A 158      16.011  37.014  27.190
ATOM   1092  NE  ARG A 158      14.736  36.623  27.803
ATOM   1093  CZ  ARG A 158      14.669  35.451  28.470
ATOM   1094  NH1 ARG A 158      15.636  34.453  27.927
ATOM   1095  NH2 ARG A 158      13.393  35.306  28.884
ATOM   1096  N   LYS A 159      17.352  40.772  30.711
ATOM   1097  CA  LYS A 159      17.084  41.986  31.428
ATOM   1098  C   LYS A 159      15.740  41.917  32.077
ATOM   1099  O   LYS A 159      14.801  41.367  31.510
ATOM   1100  CB  LYS A 159      17.122  43.190  30.478
ATOM   1101  CG  LYS A 159      18.524  43.405  29.882
ATOM   1102  CD  LYS A 159      19.567  43.824  30.920
ATOM   1103  CE  LYS A 159      19.323  45.240  31.445
ATOM   1104  NZ  LYS A 159      20.328  45.612  32.458
ATOM   1105  N   GLY A 160      15.633  42.422  33.321
ATOM   1106  CA  GLY A 160      14.372  42.326  34.001
ATOM   1107  C   GLY A 160      14.140  41.018  34.627
ATOM   1108  O   GLY A 160      13.090  40.811  35.226
ATOM   1109  N   GLY A 161      15.136  40.127  34.576
ATOM   1110  CA  GLY A 161      14.926  38.801  35.053
ATOM   1111  C   GLY A 161      15.191  38.653  36.525
ATOM   1112  O   GLY A 161      15.689  39.559  37.203
ATOM   1113  N   THR A 162      14.894  37.442  37.050
ATOM   1114  CA  THR A 162      15.027  37.149  38.448
ATOM   1115  C   THR A 162      16.003  36.014  38.633
ATOM   1116  O   THR A 162      16.006  35.042  37.887
ATOM   1117  CB  THR A 162      13.699  36.843  39.095
ATOM   1118  OG1 THR A 162      13.840  36.704  40.497
ATOM   1119  CG2 THR A 162      13.082  35.570  38.533
ATOM   1120  N   VAL A 163      16.876  36.125  39.647
ATOM   1121  CA  VAL A 163      17.840  35.122  39.996
ATOM   1122  C   VAL A 163      17.438  34.684  41.386
ATOM   1123  O   VAL A 163      17.651  35.418  42.349
ATOM   1124  CB  VAL A 163      19.248  35.696  39.999
ATOM   1125  CG1 VAL A 163      20.266  34.660  40.456
ATOM   1126  CG2 VAL A 163      19.635  36.156  38.593
ATOM   1127  N   VAL A 164      16.840  33.481  41.512
ATOM   1128  CA  VAL A 164      16.332  32.973  42.756
ATOM   1129  C   VAL A 164      17.294  31.928  43.331
ATOM   1130  O   VAL A 164      17.793  31.071  42.614
ATOM   1131  CB  VAL A 164      14.957  32.359  42.604
ATOM   1132  CG1 VAL A 164      14.482  31.802  43.945
ATOM   1133  CG2 VAL A 164      13.889  33.347  42.118
ATOM   1134  N   CYS A 165      17.554  31.938  44.661
ATOM   1135  CA  CYS A 165      18.345  30.948  45.407
ATOM   1136  C   CYS A 165      17.341  30.317  46.445
ATOM   1137  O   CYS A 165      16.525  31.006  46.953
ATOM   1138  CB  CYS A 165      19.347  31.806  46.241
ATOM   1139  SG  CYS A 165      20.226  33.096  45.272
ATOM   1140  N   GLY A 166      17.039  29.167  47.044
ATOM   1141  CA  GLY A 166      17.545  27.906  47.116
ATOM   1142  C   GLY A 166      18.628  27.985  48.123
ATOM   1143  O   GLY A 166      18.556  28.620  49.182
ATOM   1144  N   GLY A 167      19.690  27.271  47.758
ATOM   1145  CA  GLY A 167      20.823  27.123  48.612
ATOM   1146  C   GLY A 167      21.804  28.218  48.314
ATOM   1147  O   GLY A 167      21.942  28.643  47.165
ATOM   1148  N   ILE A 168      22.504  28.689  49.376
ATOM   1149  CA  ILE A 168      23.512  29.710  49.281
ATOM   1150  C   ILE A 168      24.643  29.290  50.189
ATOM   1151  O   ILE A 168      24.417  28.637  51.209
ATOM   1152  CB  ILE A 168      22.993  31.086  49.671
ATOM   1153  CG1 ILE A 168      23.993  32.207  49.346
ATOM   1154  CG2 ILE A 168      22.615  31.138  51.166
ATOM   1155  CD1 ILE A 168      23.380  33.599  49.457
ATOM   1156  N   ASP A 169      25.889  29.665  49.833
ATOM   1157  CA  ASP A 169      27.062  29.293  50.574
ATOM   1158  C   ASP A 169      27.506  30.473  51.423
ATOM   1159  O   ASP A 169      27.440  31.631  51.013
ATOM   1160  CB  ASP A 169      28.203  28.913  49.634
ATOM   1161  CG  ASP A 169      27.996  27.580  48.887
ATOM   1162  OD1 ASP A 169      27.059  27.500  48.047
ATOM   1163  OD2 ASP A 169      28.821  26.648  49.095
ATOM   1164  N   MET A 170      27.960  30.200  52.660
ATOM   1165  CA  MET A 170      28.432  31.189  53.602
ATOM   1166  C   MET A 170      29.880  31.574  53.340
ATOM   1167  O   MET A 170      30.770  30.740  53.339
ATOM   1168  CB  MET A 170      28.344  30.685  55.065
ATOM   1169  CG  MET A 170      29.330  29.563  55.462
ATOM   1170  SD  MET A 170      29.087  27.993  54.569
ATOM   1171  CE  MET A 170      30.272  28.045  53.182
ATOM   1172  N   SER A 171      30.185  32.872  53.143
ATOM   1173  CA  SER A 171      31.498  33.430  52.868
ATOM   1174  C   SER A 171      30.988  34.882  52.595
ATOM   1175  O   SER A 171      30.000  35.358  53.090
ATOM   1176  CB  SER A 171      32.036  32.959  51.491
ATOM   1177  OG  SER A 171      32.229  31.556  51.392
ATOM   1178  N   ASP A 172      31.341  35.670  51.592
ATOM   1179  CA  ASP A 172      30.387  36.813  51.271
ATOM   1180  C   ASP A 172      30.052  36.779  49.809
ATOM   1181  O   ASP A 172      30.804  36.155  49.072
ATOM   1182  CB  ASP A 172      30.920  38.185  51.692
ATOM   1183  CG  ASP A 172      32.336  38.324  51.181
ATOM   1184  OD1 ASP A 172      32.538  38.225  49.943
ATOM   1185  OD2 ASP A 172      33.243  38.560  52.022
ATOM   1186  N   ILE A 173      28.917  37.395  49.346
ATOM   1187  CA  ILE A 173      28.541  37.371  47.941
ATOM   1188  C   ILE A 173      28.568  38.781  47.366
ATOM   1189  O   ILE A 173      27.760  39.605  47.807
ATOM   1190  CB  ILE A 173      27.167  36.770  47.713
ATOM   1191  CG1 ILE A 173      27.105  35.320  48.229
ATOM   1192  CG2 ILE A 173      26.780  36.798  46.216
ATOM   1193  CD1 ILE A 173      28.078  34.370  47.513
ATOM   1194  N   PRO A 174      29.434  39.125  46.400
ATOM   1195  CA  PRO A 174      29.512  40.483  45.894
ATOM   1196  C   PRO A 174      28.582  40.549  44.696
ATOM   1197  O   PRO A 174      28.522  39.613  43.895
ATOM   1198  CB  PRO A 174      30.990  40.604  45.450
ATOM   1199  CG  PRO A 174      31.459  39.153  45.094
ATOM   1200  CD  PRO A 174      30.366  38.218  45.687
ATOM   1201  N   SER A 175      27.841  41.660  44.536
ATOM   1202  CA  SER A 175      26.927  41.778  43.431
ATOM   1203  C   SER A 175      27.209  43.066  42.760
ATOM   1204  O   SER A 175      27.509  44.011  43.455
ATOM   1205  CB  SER A 175      25.468  41.782  43.900
ATOM   1206  OG  SER A 175      25.147  40.510  44.443
ATOM   1207  N   MET A 176      27.145  43.122  41.420
ATOM   1208  CA  MET A 176      27.428  44.279  40.629
ATOM   1209  C   MET A 176      26.308  45.297  40.793
ATOM   1210  O   MET A 176      25.215  45.022  40.318
ATOM   1211  CB  MET A 176      27.567  43.792  39.161
ATOM   1212  CG  MET A 176      28.933  43.129  38.883
ATOM   1213  SD  MET A 176      29.290  41.605  39.829
ATOM   1214  CE  MET A 176      28.183  40.479  38.934
ATOM   1215  N   PRO A 177      26.466  46.478  41.423
ATOM   1216  CA  PRO A 177      25.331  47.396  41.426
ATOM   1217  C   PRO A 177      25.052  48.038  40.125
ATOM   1218  O   PRO A 177      23.874  48.188  39.810
ATOM   1219  CB  PRO A 177      25.658  48.463  42.515
ATOM   1220  CG  PRO A 177      26.909  47.966  43.287
ATOM   1221  CD  PRO A 177      27.044  46.537  42.782
ATOM   1222  N   TYR A 178      26.092  48.437  39.383
ATOM   1223  CA  TYR A 178      25.937  49.118  38.133
ATOM   1224  C   TYR A 178      25.117  48.280  37.176
ATOM   1225  O   TYR A 178      24.189  48.768  36.537
ATOM   1226  CB  TYR A 178      27.315  49.404  37.500
ATOM   1227  CG  TYR A 178      28.107  50.396  38.319
ATOM   1228  CD1 TYR A 178      29.084  49.974  39.207
ATOM   1229  CD2 TYR A 178      27.922  51.755  38.149
ATOM   1230  CE1 TYR A 178      29.827  50.883  39.926
ATOM   1231  CE2 TYR A 178      28.665  52.669  38.863
ATOM   1232  CZ  TYR A 178      29.622  52.231  39.750
ATOM   1233  OH  TYR A 178      30.385  53.160  40.489
ATOM   1234  N   ARG A 179      25.431  46.978  37.070
ATOM   1235  CA  ARG A 179      24.760  46.098  36.161
ATOM   1236  C   ARG A 179      23.328  45.869  36.572
ATOM   1237  O   ARG A 179      22.431  45.838  35.726
ATOM   1238  CB  ARG A 179      25.499  44.748  36.075
ATOM   1239  CG  ARG A 179      24.955  43.813  35.004
ATOM   1240  CD  ARG A 179      23.777  42.962  35.518
ATOM   1241  NE  ARG A 179      23.308  42.031  34.472
ATOM   1242  CZ  ARG A 179      23.925  40.821  34.297
ATOM   1243  NH1 ARG A 179      25.135  40.601  34.935
ATOM   1244  NH2 ARG A 179      23.489  39.931  33.366
ATOM   1245  N   LEU A 180      23.101  45.631  37.871
ATOM   1246  CA  LEU A 180      21.813  45.319  38.407
ATOM   1247  C   LEU A 180      20.811  46.417  38.148
ATOM   1248  O   LEU A 180      19.669  46.156  37.769
ATOM   1249  CB  LEU A 180      21.940  45.094  39.926
ATOM   1250  CG  LEU A 180      22.391  43.684  40.277
ATOM   1251  CD1 LEU A 180      23.412  42.908  39.420
ATOM   1252  CD2 LEU A 180      22.420  43.306  41.755
ATOM   1253  N   LEU A 181      21.238  47.672  38.348
ATOM   1254  CA  LEU A 181      20.397  48.814  38.198
ATOM   1255  C   LEU A 181      20.076  49.012  36.775
ATOM   1256  O   LEU A 181      18.917  49.256  36.510
ATOM   1257  CB  LEU A 181      21.057  50.098  38.729
ATOM   1258  CG  LEU A 181      20.099  51.302  38.890
ATOM   1259  CD1 LEU A 181      20.755  52.432  39.690
ATOM   1260  CD2 LEU A 181      19.623  51.945  37.573
ATOM   1261  N   TRP A 182      21.078  48.968  35.877
ATOM   1262  CA  TRP A 182      20.964  49.201  34.454
ATOM   1263  C   TRP A 182      19.699  48.716  33.632
ATOM   1264  O   TRP A 182      19.514  48.629  32.436
ATOM   1265  CB  TRP A 182      22.345  49.064  33.741
ATOM   1266  CG  TRP A 182      23.365  50.169  34.079
ATOM   1267  CD1 TRP A 182      23.136  51.281  34.846
ATOM   1268  CD2 TRP A 182      24.775  50.246  33.692
ATOM   1269  NE1 TRP A 182      24.274  52.032  34.950
ATOM   1270  CE2 TRP A 182      25.291  51.418  34.245
ATOM   1271  CE3 TRP A 182      25.589  49.429  32.932
ATOM   1272  CZ2 TRP A 182      26.602  51.786  34.051
ATOM   1273  CZ3 TRP A 182      26.915  49.807  32.737
ATOM   1274  CH2 TRP A 182      27.415  50.970  33.289
ATOM   1275  N   GLY A 183      18.525  48.755  34.130
ATOM   1276  CA  GLY A 183      17.411  47.996  33.674
ATOM   1277  C   GLY A 183      16.821  47.486  34.930
ATOM   1278  O   GLY A 183      16.523  48.266  35.828
ATOM   1279  N   GLU A 184      16.655  46.149  35.020
ATOM   1280  CA  GLU A 184      16.113  45.540  36.201
ATOM   1281  C   GLU A 184      16.955  44.360  36.575
ATOM   1282  O   GLU A 184      17.547  43.686  35.722
ATOM   1283  CB  GLU A 184      14.704  45.049  35.948
ATOM   1284  CG  GLU A 184      13.647  46.067  35.598
ATOM   1285  CD  GLU A 184      13.178  46.716  36.860
ATOM   1286  OE1 GLU A 184      14.018  47.353  37.544
ATOM   1287  OE2 GLU A 184      11.966  46.591  37.158
ATOM   1288  N   ARG A 185      17.036  44.106  37.894
ATOM   1289  CA  ARG A 185      17.743  42.973  38.353
ATOM   1290  C   ARG A 185      17.047  42.501  39.531
ATOM   1291  O   ARG A 185      16.792  43.254  40.473
ATOM   1292  CB  ARG A 185      19.183  43.198  38.752
ATOM   1293  CG  ARG A 185      19.848  41.865  39.166
ATOM   1294  CD  ARG A 185      20.432  41.140  38.007
ATOM   1295  NE  ARG A 185      19.379  40.149  37.784
ATOM   1296  CZ  ARG A 185      19.425  39.361  36.695
ATOM   1297  NH1 ARG A 185      20.503  39.555  35.839
ATOM   1298  NH2 ARG A 185      18.364  38.509  36.508
ATOM   1299  N   ARG A 186      16.738  41.205  39.513
ATOM   1300  CA  ARG A 186      16.260  40.797  40.765
ATOM   1301  C   ARG A 186      17.020  39.684  41.299
ATOM   1302  O   ARG A 186      17.244  38.709  40.603
ATOM   1303  CB  ARG A 186      14.771  40.607  40.719
ATOM   1304  CG  ARG A 186      14.204  40.514  42.111
ATOM   1305  CD  ARG A 186      13.981  41.852  42.801
ATOM   1306  NE  ARG A 186      15.222  42.229  43.544
ATOM   1307  CZ  ARG A 186      15.338  43.473  44.120
ATOM   1308  NH1 ARG A 186      14.301  44.375  44.019
ATOM   1309  NH2 ARG A 186      16.490  43.791  44.808
ATOM   1310  N   VAL A 187      17.452  39.843  42.570
ATOM   1311  CA  VAL A 187      18.094  38.803  43.320
ATOM   1312  C   VAL A 187      17.178  38.473  44.473
ATOM   1313  O   VAL A 187      16.901  39.320  45.324
ATOM   1314  CB  VAL A 187      19.477  39.220  43.791
ATOM   1315  CG1 VAL A 187      19.453  40.394  44.794
ATOM   1316  CG2 VAL A 187      20.222  38.024  44.398
ATOM   1317  N   VAL A 188      16.644  37.235  44.511
ATOM   1318  CA  VAL A 188      15.685  36.866  45.523
ATOM   1319  C   VAL A 188      16.031  35.496  46.067
ATOM   1320  O   VAL A 188      16.679  34.692  45.409
ATOM   1321  CB  VAL A 188      14.258  36.838  45.030
ATOM   1322  CG1 VAL A 188      13.787  38.196  44.557
ATOM   1323  CG2 VAL A 188      14.180  35.930  43.843
ATOM   1324  N   SER A 189      15.574  35.181  47.293
ATOM   1325  CA  SER A 189      15.747  33.871  47.901
ATOM   1326  C   SER A 189      14.390  33.128  47.857
ATOM   1327  O   SER A 189      13.407  33.820  47.684
ATOM   1328  CB  SER A 189      16.030  34.089  49.399
ATOM   1329  OG  SER A 189      16.249  32.850  50.047
ATOM   1330  N   VAL A 190      14.182  31.782  48.061
ATOM   1331  CA  VAL A 190      13.156  31.240  48.966
ATOM   1332  C   VAL A 190      13.722  29.967  49.579
ATOM   1333  O   VAL A 190      14.078  29.025  48.871
ATOM   1334  CB  VAL A 190      11.806  30.886  48.349
ATOM   1335  CG1 VAL A 190      11.107  32.114  47.735
ATOM   1336  CG2 VAL A 190      11.980  29.868  47.264
ATOM   1337  N   ALA A 191      13.847  29.914  50.924
ATOM   1338  CA  ALA A 191      14.439  28.796  51.619
ATOM   1339  C   ALA A 191      13.395  27.885  52.222
ATOM   1340  O   ALA A 191      13.727  26.771  52.633
ATOM   1341  CB  ALA A 191      15.331  29.267  52.780
ATOM   1342  N   ASN A 192      12.119  28.337  52.316
ATOM   1343  CA  ASN A 192      11.040  27.524  52.835
ATOM   1344  C   ASN A 192       9.783  28.150  52.390
ATOM   1345  O   ASN A 192       9.784  29.333  52.016
ATOM   1346  CB  ASN A 192      10.967  27.491  54.365
ATOM   1347  CG  ASN A 192       9.937  26.499  54.909
ATOM   1348  OD1 ASN A 192      10.032  25.292  54.698
ATOM   1349  ND2 ASN A 192       8.944  27.025  55.680
ATOM   1350  N   LEU A 193       8.733  27.290  52.309
ATOM   1351  CA  LEU A 193       7.449  27.701  51.968
ATOM   1352  C   LEU A 193       6.404  27.348  52.818
ATOM   1353  O   LEU A 193       6.446  26.237  53.304
ATOM   1354  CB  LEU A 193       7.064  26.976  50.708
ATOM   1355  CG  LEU A 193       7.733  27.683  49.685
ATOM   1356  CD1 LEU A 193       7.580  29.102  50.136
ATOM   1357  CD2 LEU A 193       9.259  27.375  49.496
ATOM   1358  N   THR A 194       5.489  28.301  53.073
ATOM   1359  CA  THR A 194       4.478  27.995  53.974
ATOM   1360  C   THR A 194       3.182  27.929  53.278
ATOM   1361  O   THR A 194       2.739  28.819  52.532
ATOM   1362  CB  THR A 194       4.305  28.976  55.104
ATOM   1363  OG1 THR A 194       3.952  30.242  54.578
ATOM   1364  CG2 THR A 194       5.608  29.006  55.889
ATOM   1365  N   ARG A 195       2.469  27.132  54.097
ATOM   1366  CA  ARG A 195       2.023  25.771  54.251
ATOM   1367  C   ARG A 195       1.242  25.328  53.071
ATOM   1368  O   ARG A 195       1.300  24.165  52.675
ATOM   1369  CB  ARG A 195       1.085  25.683  55.501
ATOM   1370  CG  ARG A 195       1.803  25.919  56.841
ATOM   1371  CD  ARG A 195       0.894  25.880  58.079
ATOM   1372  NE  ARG A 195       0.307  24.510  58.191
ATOM   1373  CZ  ARG A 195      -0.992  24.248  57.836
ATOM   1374  NH1 ARG A 195      -1.781  25.230  57.297
ATOM   1375  NH2 ARG A 195      -1.499  22.984  57.976
ATOM   1376  N   SER A 196       0.506  26.274  52.476
ATOM   1377  CA  SER A 196      -0.241  26.047  51.277
ATOM   1378  C   SER A 196       0.685  25.583  50.190
ATOM   1379  O   SER A 196       0.351  24.692  49.412
ATOM   1380  CB  SER A 196      -0.926  27.343  50.835
ATOM   1381  OG  SER A 196      -1.842  27.763  51.841
ATOM   1382  N   ASP A 197       1.891  26.162  50.133
ATOM   1383  CA  ASP A 197       2.842  25.779  49.137
ATOM   1384  C   ASP A 197       3.191  24.328  49.227
ATOM   1385  O   ASP A 197       3.333  23.676  48.198
ATOM   1386  CB  ASP A 197       4.131  26.487  49.323
ATOM   1387  CG  ASP A 197       3.976  27.936  49.032
ATOM   1388  OD1 ASP A 197       3.095  28.451  48.315
ATOM   1389  OD2 ASP A 197       4.740  28.605  49.713
ATOM   1390  N   GLY A 198       3.315  23.766  50.446
ATOM   1391  CA  GLY A 198       3.628  22.370  50.627
ATOM   1392  C   GLY A 198       2.514  21.467  50.161
ATOM   1393  O   GLY A 198       2.777  20.421  49.575
ATOM   1394  N   ALA A 199       1.244  21.840  50.407
ATOM   1395  CA  ALA A 199       0.111  21.060  49.971
ATOM   1396  C   ALA A 199       0.069  21.024  48.463
ATOM   1397  O   ALA A 199      -0.186  19.987  47.850
ATOM   1398  CB  ALA A 199      -1.217  21.646  50.484
ATOM   1399  N   GLU A 200       0.333  22.176  47.823
ATOM   1400  CA  GLU A 200       0.359  22.299  46.392
ATOM   1401  C   GLU A 200       1.479  21.465  45.823
ATOM   1402  O   GLU A 200       1.331  20.844  44.775
ATOM   1403  CB  GLU A 200       0.551  23.770  45.960
ATOM   1404  CG  GLU A 200      -0.744  24.598  46.031
ATOM   1405  CD  GLU A 200      -0.424  26.093  46.016
ATOM   1406  OE1 GLU A 200       0.688  26.474  45.552
ATOM   1407  OE2 GLU A 200      -1.299  26.889  46.449
ATOM   1408  N   PHE A 201       2.634  21.422  46.498
ATOM   1409  CA  PHE A 201       3.773  20.678  46.045
ATOM   1410  C   PHE A 201       3.494  19.200  46.174
ATOM   1411  O   PHE A 201       3.902  18.384  45.368
ATOM   1412  CB  PHE A 201       5.018  21.048  46.872
ATOM   1413  CG  PHE A 201       6.209  20.312  46.409
ATOM   1414  CD1 PHE A 201       6.918  20.699  45.304
ATOM   1415  CD2 PHE A 201       6.685  19.320  47.154
ATOM   1416  CE1 PHE A 201       7.974  19.979  44.780
ATOM   1417  CE2 PHE A 201       7.705  18.662  46.618
ATOM   1418  CZ  PHE A 201       8.292  18.839  45.399
ATOM   1419  N   PHE A 202       2.788  18.755  47.212
ATOM   1420  CA  PHE A 202       2.469  17.354  47.377
ATOM   1421  C   PHE A 202       1.489  16.931  46.354
ATOM   1422  O   PHE A 202       1.480  15.790  45.888
ATOM   1423  CB  PHE A 202       1.885  17.079  48.767
ATOM   1424  CG  PHE A 202       2.913  17.258  49.834
ATOM   1425  CD1 PHE A 202       4.267  17.313  49.572
ATOM   1426  CD2 PHE A 202       2.472  17.383  51.125
ATOM   1427  CE1 PHE A 202       5.155  17.482  50.563
ATOM   1428  CE2 PHE A 202       3.401  17.319  52.096
ATOM   1429  CZ  PHE A 202       4.734  17.379  51.780
ATOM   1430  N   SER A 203       0.671  17.905  45.956
ATOM   1431  CA  SER A 203      -0.266  17.745  44.930
ATOM   1432  C   SER A 203       0.245  17.241  43.607
ATOM   1433  O   SER A 203      -0.266  16.363  42.902
ATOM   1434  CB  SER A 203      -1.246  19.046  44.717
ATOM   1435  OG  SER A 203      -2.202  19.036  43.617
ATOM   1436  N   ILE A 204       1.281  17.907  43.195
ATOM   1437  CA  ILE A 204       1.879  17.629  41.953
ATOM   1438  C   ILE A 204       2.417  16.282  42.050
ATOM   1439  O   ILE A 204       2.423  15.580  41.079
ATOM   1440  CB  ILE A 204       2.964  18.587  41.620
ATOM   1441  CG1 ILE A 204       4.037  18.632  42.670
ATOM   1442  CG2 ILE A 204       2.340  19.989  41.575
ATOM   1443  CD1 ILE A 204       5.239  19.442  42.410
ATOM   1444  N   GLY A 205       2.815  15.874  43.234
ATOM   1445  CA  GLY A 205       3.169  14.566  43.420
ATOM   1446  C   GLY A 205       2.389  13.424  43.284
ATOM   1447  O   GLY A 205       2.713  12.443  42.600
ATOM   1448  N   LYS A 206       1.315  13.600  43.963
ATOM   1449  CA  LYS A 206       0.276  12.679  43.950
ATOM   1450  C   LYS A 206      -0.215  12.433  42.562
ATOM   1451  O   LYS A 206      -0.896  11.442  42.327
ATOM   1452  CB  LYS A 206      -0.876  13.170  44.815
ATOM   1453  CG  LYS A 206      -1.517  14.418  44.314
ATOM   1454  CD  LYS A 206      -2.659  14.933  45.142
ATOM   1455  CE  LYS A 206      -3.546  15.895  44.437
ATOM   1456  NZ  LYS A 206      -2.732  16.754  44.586
ATOM   1457  N   ALA A 207       0.104  13.312  41.601
ATOM   1458  CA  ALA A 207      -0.423  13.152  40.322
ATOM   1459  C   ALA A 207       0.343  12.180  39.600
ATOM   1460  O   ALA A 207      -0.004  12.227  38.428
ATOM   1461  CB  ALA A 207      -0.442  14.486  39.478
ATOM   1462  N   ALA A 208       1.416  11.521  40.154
ATOM   1463  CA  ALA A 208       2.430  11.472  39.183
ATOM   1464  C   ALA A 208       2.833  12.908  38.935
ATOM   1465  O   ALA A 208       2.335  13.852  39.491
ATOM   1466  CB  ALA A 208       2.038  10.612  37.926
ATOM   1467  N   GLY A 209       3.860  13.124  38.132
ATOM   1468  CA  GLY A 209       4.406  14.422  37.858
ATOM   1469  C   GLY A 209       5.358  14.902  38.917
ATOM   1470  O   GLY A 209       5.957  15.957  38.730
ATOM   1471  N   VAL A 210       5.533  14.191  40.053
ATOM   1472  CA  VAL A 210       6.492  14.648  41.029
ATOM   1473  C   VAL A 210       7.509  13.585  41.178
ATOM   1474  O   VAL A 210       7.269  12.412  41.478
ATOM   1475  CB  VAL A 210       5.960  14.973  42.362
ATOM   1476  CG1 VAL A 210       5.751  13.641  43.149
ATOM   1477  CG2 VAL A 210       6.862  15.769  43.263
ATOM   1478  N   ARG A 211       8.739  13.989  40.908
ATOM   1479  CA  ARG A 211       9.810  13.060  40.932
ATOM   1480  C   ARG A 211      10.436  13.063  42.307
ATOM   1481  O   ARG A 211      10.502  14.085  42.982
ATOM   1482  CB  ARG A 211      10.842  13.402  39.855
ATOM   1483  CG  ARG A 211      11.997  12.410  39.738
ATOM   1484  CD  ARG A 211      11.601  11.129  39.002
ATOM   1485  NE  ARG A 211      11.056  10.148  39.984
ATOM   1486  CZ  ARG A 211      10.497   8.964  39.561
ATOM   1487  NH1 ARG A 211      10.415   8.684  38.212
ATOM   1488  NH2 ARG A 211      10.027   8.068  40.497
ATOM   1489  N   CYS A 212      10.910  11.873  42.739
ATOM   1490  CA  CYS A 212      11.687  11.567  43.934
ATOM   1491  C   CYS A 212      13.080  11.061  43.400
ATOM   1492  O   CYS A 212      13.017  10.261  42.533
ATOM   1493  CB  CYS A 212      11.041  10.211  44.423
ATOM   1494  SG  CYS A 212       9.255  10.196  44.820
ATOM   1495  N   PHE A 213      14.421  11.193  43.570
ATOM   1496  CA  PHE A 213      15.165   9.880  43.335
ATOM   1497  C   PHE A 213      15.590   9.538  44.679
ATOM   1498  O   PHE A 213      16.244  10.400  45.243
ATOM   1499  CB  PHE A 213      16.360   9.979  42.317
ATOM   1500  CG  PHE A 213      17.155   8.711  42.100
ATOM   1501  CD1 PHE A 213      16.623   7.441  42.267
ATOM   1502  CD2 PHE A 213      18.475   8.810  41.689
ATOM   1503  CE1 PHE A 213      17.389   6.321  42.077
ATOM   1504  CE2 PHE A 213      19.240   7.684  41.485
ATOM   1505  CZ  PHE A 213      18.697   6.437  41.682
ATOM   1506  N   THR A 214      15.171   8.375  45.259
ATOM   1507  CA  THR A 214      15.460   8.145  46.645
ATOM   1508  C   THR A 214      16.174   6.845  46.922
ATOM   1509  O   THR A 214      16.074   5.863  46.181
ATOM   1510  CB  THR A 214      14.257   8.197  47.546
ATOM   1511  OG1 THR A 214      13.310   7.219  47.153
ATOM   1512  CG2 THR A 214      13.601   9.585  47.486
ATOM   1513  N   SER A 215      16.907   6.841  48.059
ATOM   1514  CA  SER A 215      17.611   5.716  48.576
ATOM   1515  C   SER A 215      17.108   5.540  49.991
ATOM   1516  O   SER A 215      17.154   6.471  50.794
ATOM   1517  CB  SER A 215      19.115   6.017  48.587
ATOM   1518  OG  SER A 215      19.377   7.133  49.424
ATOM   1519  N   VAL A 216      16.578   4.346  50.329
ATOM   1520  CA  VAL A 216      16.036   4.084  51.640
ATOM   1521  C   VAL A 216      17.114   3.478  52.510
ATOM   1522  O   VAL A 216      17.810   2.554  52.087
ATOM   1523  CB  VAL A 216      14.807   3.188  51.595
ATOM   1524  CG1 VAL A 216      15.137   1.792  51.034
ATOM   1525  CG2 VAL A 216      14.156   3.054  52.983
ATOM   1526  N   TYR A 217      17.268   3.982  53.760
ATOM   1527  CA  TYR A 217      18.267   3.484  54.670
ATOM   1528  C   TYR A 217      17.661   3.422  56.063
ATOM   1529  O   TYR A 217      16.873   4.292  56.408
ATOM   1530  CB  TYR A 217      19.523   4.370  54.731
ATOM   1531  CG  TYR A 217      20.265   4.332  53.420
ATOM   1532  CD1 TYR A 217      20.134   5.360  52.508
ATOM   1533  CD2 TYR A 217      21.180   3.331  53.148
ATOM   1534  CE1 TYR A 217      20.868   5.350  51.346
ATOM   1535  CE2 TYR A 217      21.887   3.305  51.966
ATOM   1536  CZ  TYR A 217      21.725   4.324  51.061
ATOM   1537  OH  TYR A 217      22.467   4.347  49.859
ATOM   1538  N   PRO A 218      17.954   2.413  56.863
ATOM   1539  CA  PRO A 218      17.483   2.388  58.253
ATOM   1540  C   PRO A 218      18.086   3.437  59.133
ATOM   1541  O   PRO A 218      19.167   3.936  58.833
ATOM   1542  CB  PRO A 218      17.790   0.932  58.713
ATOM   1543  CG  PRO A 218      18.168   0.137  57.421
ATOM   1544  CD  PRO A 218      17.751   1.077  56.282
ATOM   1545  N   LEU A 219      17.390   3.780  60.231
ATOM   1546  CA  LEU A 219      17.810   4.818  61.127
ATOM   1547  C   LEU A 219      19.238   4.637  61.597
ATOM   1548  O   LEU A 219      19.998   5.601  61.683
ATOM   1549  CB  LEU A 219      16.885   4.885  62.352
ATOM   1550  CG  LEU A 219      17.257   5.986  63.357
ATOM   1551  CD1 LEU A 219      17.196   7.384  62.724
ATOM   1552  CD2 LEU A 219      16.366   5.942  64.599
ATOM   1553  N   GLU A 220      19.647   3.394  61.894
ATOM   1554  CA  GLU A 220      20.948   3.064  62.407
ATOM   1555  C   GLU A 220      22.084   3.500  61.507
ATOM   1556  O   GLU A 220      23.204   3.713  61.976
ATOM   1557  CB  GLU A 220      21.074   1.548  62.646
ATOM   1558  CG  GLU A 220      20.205   1.042  63.811
ATOM   1559  CD  GLU A 220      18.735   1.074  63.432
ATOM   1560  OE1 GLU A 220      18.385   0.530  62.353
ATOM   1561  OE2 GLU A 220      17.949   1.693  64.194
ATOM   1562  N   HIS A 221      21.833   3.670  60.195
ATOM   1563  CA  HIS A 221      22.856   4.048  59.254
ATOM   1564  C   HIS A 221      22.956   5.551  59.082
ATOM   1565  O   HIS A 221      23.594   6.033  58.151
ATOM   1566  CB  HIS A 221      22.621   3.397  57.876
ATOM   1567  CG  HIS A 221      22.844   1.899  57.891
ATOM   1568  ND1 HIS A 221      22.438   1.125  56.813
ATOM   1569  CD2 HIS A 221      23.411   1.106  58.849
ATOM   1570  CE1 HIS A 221      22.790  -0.109  57.129
ATOM   1571  NE2 HIS A 221      23.361  -0.179  58.356
ATOM   1572  N   ALA A 222      22.366   6.360  59.984
ATOM   1573  CA  ALA A 222      22.359   7.796  59.837
ATOM   1574  C   ALA A 222      23.743   8.397  59.749
ATOM   1575  O   ALA A 222      23.990   9.271  58.923
ATOM   1576  CB  ALA A 222      21.602   8.495  60.981
ATOM   1577  N   ASN A 223      24.687   7.936  60.585
ATOM   1578  CA  ASN A 223      26.043   8.437  60.591
ATOM   1579  C   ASN A 223      26.771   8.090  59.316
ATOM   1580  O   ASN A 223      27.639   8.840  58.866
ATOM   1581  CB  ASN A 223      26.871   7.935  61.797
ATOM   1582  CG  ASN A 223      27.153   6.431  61.738
ATOM   1583  OD1 ASN A 223      28.275   6.029  61.438
ATOM   1584  ND2 ASN A 223      26.145   5.577  62.079
ATOM   1585  N   GLU A 224      26.405   6.956  58.695
ATOM   1586  CA  GLU A 224      26.963   6.535  57.444
ATOM   1587  C   GLU A 224      26.524   7.530  56.413
ATOM   1588  O   GLU A 224      27.316   8.039  55.630
ATOM   1589  CB  GLU A 224      26.460   5.139  57.019
ATOM   1590  CG  GLU A 224      27.095   4.667  55.721
ATOM   1591  CD  GLU A 224      26.619   3.271  55.403
ATOM   1592  OE1 GLU A 224      25.381   3.077  55.276
ATOM   1593  OE2 GLU A 224      27.495   2.377  55.269
ATOM   1594  N   ALA A 225      25.220   7.842  56.401
ATOM   1595  CA  ALA A 225      24.628   8.740  55.454
ATOM   1596  C   ALA A 225      25.269  10.098  55.511
ATOM   1597  O   ALA A 225      25.618  10.660  54.479
ATOM   1598  CB  ALA A 225      23.111   8.889  55.677
ATOM   1599  N   LEU A 226      25.454  10.667  56.714
ATOM   1600  CA  LEU A 226      26.071  11.960  56.852
ATOM   1601  C   LEU A 226      27.461  11.962  56.275
ATOM   1602  O   LEU A 226      27.889  12.938  55.665
ATOM   1603  CB  LEU A 226      26.168  12.388  58.325
ATOM   1604  CG  LEU A 226      24.787  12.616  58.978
ATOM   1605  CD1 LEU A 226      24.904  12.853  60.488
ATOM   1606  CD2 LEU A 226      24.019  13.778  58.333
ATOM   1607  N   ASP A 227      28.189  10.854  56.452
ATOM   1608  CA  ASP A 227      29.532  10.647  55.965
ATOM   1609  C   ASP A 227      29.558  10.760  54.463
ATOM   1610  O   ASP A 227      30.339  11.519  53.885
ATOM   1611  CB  ASP A 227      30.025   9.250  56.400
ATOM   1612  CG  ASP A 227      31.471   8.974  56.111
ATOM   1613  OD1 ASP A 227      32.169   9.874  55.582
ATOM   1614  OD2 ASP A 227      31.911   7.850  56.473
ATOM   1615  N   ASP A 228      28.653  10.031  53.795
ATOM   1616  CA  ASP A 228      28.581   9.989  52.363
ATOM   1617  C   ASP A 228      28.085  11.316  51.847
ATOM   1618  O   ASP A 228      28.342  11.706  50.712
ATOM   1619  CB  ASP A 228      27.605   8.879  51.912
ATOM   1620  CG  ASP A 228      28.211   7.480  52.089
ATOM   1621  OD1 ASP A 228      29.446   7.350  52.304
ATOM   1622  OD2 ASP A 228      27.416   6.510  51.967
ATOM   1623  N   LEU A 229      27.360  12.069  52.682
ATOM   1624  CA  LEU A 229      26.803  13.338  52.337
ATOM   1625  C   LEU A 229      27.918  14.335  52.183
ATOM   1626  O   LEU A 229      27.997  15.051  51.183
ATOM   1627  CB  LEU A 229      25.816  13.805  53.428
ATOM   1628  CG  LEU A 229      24.901  14.964  53.031
ATOM   1629  CD1 LEU A 229      23.789  15.171  54.065
ATOM   1630  CD2 LEU A 229      25.637  16.304  52.878
ATOM   1631  N   ARG A 230      28.798  14.411  53.192
ATOM   1632  CA  ARG A 230      29.896  15.334  53.219
ATOM   1633  C   ARG A 230      30.800  15.148  52.030
ATOM   1634  O   ARG A 230      31.372  16.116  51.527
ATOM   1635  CB  ARG A 230      30.728  15.144  54.493
ATOM   1636  CG  ARG A 230      29.962  15.583  55.746
ATOM   1637  CD  ARG A 230      30.767  15.403  57.028
ATOM   1638  NE  ARG A 230      30.951  13.944  57.266
ATOM   1639  CZ  ARG A 230      31.764  13.490  58.281
ATOM   1640  NH1 ARG A 230      32.421  14.390  59.094
ATOM   1641  NH2 ARG A 230      31.885  12.131  58.490
ATOM   1642  N   ALA A 231      30.950  13.904  51.545
ATOM   1643  CA  ALA A 231      31.862  13.638  50.472
ATOM   1644  C   ALA A 231      31.138  13.502  49.153
ATOM   1645  O   ALA A 231      31.661  12.903  48.214
ATOM   1646  CB  ALA A 231      32.684  12.379  50.761
ATOM   1647  N   GLY A 232      29.923  14.079  49.040
ATOM   1648  CA  GLY A 232      29.157  14.094  47.819
ATOM   1649  C   GLY A 232      29.005  12.730  47.206
ATOM   1650  O   GLY A 232      29.045  12.574  45.986
ATOM   1651  N   ARG A 233      28.810  11.701  48.034
ATOM   1652  CA  ARG A 233      28.675  10.378  47.559
ATOM   1653  C   ARG A 233      27.190  10.207  47.531
ATOM   1654  O   ARG A 233      26.692   9.188  47.862
ATOM   1655  CB  ARG A 233      29.306   9.347  48.539
ATOM   1656  CG  ARG A 233      29.487   7.914  47.995
ATOM   1657  CD  ARG A 233      28.269   6.941  48.110
ATOM   1658  NE  ARG A 233      27.407   6.994  46.842
ATOM   1659  CZ  ARG A 233      26.025   6.810  46.927
ATOM   1660  NH1 ARG A 233      25.523   6.100  47.988
ATOM   1661  NH2 ARG A 233      25.162   7.409  46.009
ATOM   1662  N   VAL A 234      26.285  11.130  47.246
ATOM   1663  CA  VAL A 234      24.873  10.759  47.262
ATOM   1664  C   VAL A 234      24.265  11.282  46.005
ATOM   1665  O   VAL A 234      24.333  12.473  45.724
ATOM   1666  CB  VAL A 234      24.139  11.280  48.479
ATOM   1667  CG1 VAL A 234      24.258  12.811  48.600
ATOM   1668  CG2 VAL A 234      22.660  10.854  48.458
ATOM   1669  N   SER A 235      23.626  10.397  45.216
ATOM   1670  CA  SER A 235      22.936  10.800  44.026
ATOM   1671  C   SER A 235      21.468  10.747  44.347
ATOM   1672  O   SER A 235      20.900   9.661  44.460
ATOM   1673  CB  SER A 235      23.242   9.849  42.856
ATOM   1674  OG  SER A 235      22.539  10.245  41.689
ATOM   1675  N   GLY A 236      20.817  11.919  44.511
ATOM   1676  CA  GLY A 236      19.410  11.954  44.808
ATOM   1677  C   GLY A 236      19.242  12.246  46.271
ATOM   1678  O   GLY A 236      20.025  13.005  46.843
ATOM   1679  N   ALA A 237      18.196  11.673  46.910
ATOM   1680  CA  ALA A 237      17.917  11.957  48.293
ATOM   1681  C   ALA A 237      17.823  10.689  49.097
ATOM   1682  O   ALA A 237      17.457   9.637  48.587
ATOM   1683  CB  ALA A 237      16.624  12.760  48.475
ATOM   1684  N   ALA A 238      18.160  10.777  50.400
ATOM   1685  CA  ALA A 238      18.138   9.644  51.290
ATOM   1686  C   ALA A 238      16.979   9.779  52.241
ATOM   1687  O   ALA A 238      16.749  10.851  52.801
ATOM   1688  CB  ALA A 238      19.437   9.498  52.099
ATOM   1689  N   VAL A 239      16.221   8.675  52.435
ATOM   1690  CA  VAL A 239      15.070   8.645  53.296
ATOM   1691  C   VAL A 239      15.302   7.557  54.307
ATOM   1692  O   VAL A 239      15.552   6.401  53.979
ATOM   1693  CB  VAL A 239      13.779   8.401  52.545
ATOM   1694  CG1 VAL A 239      13.774   7.034  51.857
ATOM   1695  CG2 VAL A 239      12.556   8.541  53.466
ATOM   1696  N   ILE A 240      15.220   7.917  55.589
ATOM   1697  CA  ILE A 240      15.379   7.004  56.667
ATOM   1698  C   ILE A 240      14.071   6.310  56.912
ATOM   1699  O   ILE A 240      13.009   6.936  56.937
ATOM   1700  CB  ILE A 240      15.861   7.649  57.938
ATOM   1701  CG1 ILE A 240      14.886   8.715  58.475
ATOM   1702  CG2 ILE A 240      17.249   8.288  57.704
ATOM   1703  CD1 ILE A 240      14.928  10.066  57.742
ENDMDL
MODEL         2
ATOM      0  N   MET B   1      10.874  15.643  58.614
ATOM      1  CA  MET B   1      10.186  14.357  58.835
ATOM      2  CB  MET B   1      10.400  13.890  60.276
ATOM      3  CG  MET B   1      11.822  13.351  60.472
ATOM      4  SD  MET B   1      13.166  14.565  60.266
ATOM      5  CE  MET B   1      12.535  15.749  61.490
ATOM      6  C   MET B   1       8.778  14.617  58.509
ATOM      7  O   MET B   1       8.437  15.795  58.400
ATOM      8  N   ALA B   2       7.971  13.547  58.277
ATOM      9  CA  ALA B   2       6.588  13.768  57.978
ATOM     10  CB  ALA B   2       5.752  12.479  57.895
ATOM     11  C   ALA B   2       6.188  14.510  59.191
ATOM     12  O   ALA B   2       6.048  13.861  60.220
ATOM     13  N   GLY B   3       5.982  15.853  59.074
ATOM     14  CA  GLY B   3       5.954  16.719  60.239
ATOM     15  C   GLY B   3       6.047  18.269  59.929
ATOM     16  O   GLY B   3       6.260  18.554  58.745
ATOM     17  N   PRO B   4       5.836  19.197  60.999
ATOM     18  CA  PRO B   4       5.716  20.731  61.146
ATOM     19  CD  PRO B   4       4.965  18.580  61.992
ATOM     20  CB  PRO B   4       4.456  20.945  61.989
ATOM     21  CG  PRO B   4       4.392  19.699  62.873
ATOM     22  C   PRO B   4       6.754  21.848  61.605
ATOM     23  O   PRO B   4       7.956  21.599  61.574
ATOM     24  N   TYR B   5       6.253  23.092  62.051
ATOM     25  CA  TYR B   5       6.774  24.424  62.516
ATOM     26  CB  TYR B   5       6.338  25.533  61.510
ATOM     27  CG  TYR B   5       6.202  26.858  62.180
ATOM     28  CD1 TYR B   5       7.273  27.607  62.621
ATOM     29  CD2 TYR B   5       4.934  27.370  62.315
ATOM     30  CE1 TYR B   5       7.061  28.813  63.259
ATOM     31  CE2 TYR B   5       4.720  28.567  62.942
ATOM     32  CZ  TYR B   5       5.779  29.291  63.421
ATOM     33  OH  TYR B   5       5.522  30.512  64.078
ATOM     34  C   TYR B   5       6.239  24.783  63.925
ATOM     35  O   TYR B   5       5.260  24.203  64.375
ATOM     36  N   LEU B   6       6.856  25.749  64.681
ATOM     37  CA  LEU B   6       6.527  26.116  66.063
ATOM     38  CB  LEU B   6       7.456  27.127  66.754
ATOM     39  CG  LEU B   6       8.567  26.461  67.568
ATOM     40  CD2 LEU B   6       8.022  25.224  68.294
ATOM     41  CD1 LEU B   6       9.203  27.466  68.540
ATOM     42  C   LEU B   6       5.146  26.633  66.356
ATOM     43  O   LEU B   6       4.582  26.209  67.359
ATOM     44  N   ARG B   7       4.614  27.577  65.550
ATOM     45  CA  ARG B   7       3.302  28.204  65.558
ATOM     46  CB  ARG B   7       2.119  27.219  65.682
ATOM     47  CG  ARG B   7       1.934  26.635  67.088
ATOM     48  CD  ARG B   7       0.912  25.513  67.241
ATOM     49  NE  ARG B   7       1.135  24.900  68.581
ATOM     50  CZ  ARG B   7       0.565  25.450  69.693
ATOM     51  NH1 ARG B   7      -0.206  26.571  69.585
ATOM     52  NH2 ARG B   7       0.777  24.885  70.918
ATOM     53  C   ARG B   7       3.083  29.110  66.727
ATOM     54  O   ARG B   7       1.950  29.527  66.968
ATOM     55  N   ALA B   8       4.124  29.422  67.509
ATOM     56  CA  ALA B   8       3.900  30.264  68.649
ATOM     57  CB  ALA B   8       5.097  30.277  69.615
ATOM     58  C   ALA B   8       3.612  31.689  68.281
ATOM     59  O   ALA B   8       2.642  32.277  68.757
ATOM     60  N   LEU B   9       4.427  32.262  67.377
ATOM     61  CA  LEU B   9       4.381  33.669  67.101
ATOM     62  CB  LEU B   9       5.644  34.228  66.424
ATOM     63  CG  LEU B   9       6.853  34.345  67.368
ATOM     64  CD2 LEU B   9       6.498  35.172  68.617
ATOM     65  CD1 LEU B   9       8.074  34.910  66.625
ATOM     66  C   LEU B   9       3.232  34.005  66.236
ATOM     67  O   LEU B   9       2.618  33.124  65.648
ATOM     68  N   ARG B  10       2.928  35.314  66.158
ATOM     69  CA  ARG B  10       1.844  35.854  65.394
ATOM     70  CB  ARG B  10       1.727  37.383  65.520
ATOM     71  CG  ARG B  10       2.981  38.127  65.058
ATOM     72  CD  ARG B  10       3.012  39.605  65.456
ATOM     73  NE  ARG B  10       4.287  40.177  64.937
ATOM     74  CZ  ARG B  10       4.345  40.673  63.666
ATOM     75  NH1 ARG B  10       3.216  40.700  62.897
ATOM     76  NH2 ARG B  10       5.527  41.125  63.155
ATOM     77  C   ARG B  10       2.104  35.536  63.962
ATOM     78  O   ARG B  10       1.174  35.335  63.185
ATOM     79  N   ILE B  11       3.393  35.468  63.585
ATOM     80  CA  ILE B  11       3.769  35.223  62.228
ATOM     81  CB  ILE B  11       5.257  35.174  62.070
ATOM     82  CG2 ILE B  11       5.550  35.034  60.576
ATOM     83  CG1 ILE B  11       5.875  36.465  62.632
ATOM     84  CD1 ILE B  11       5.383  37.726  61.920
ATOM     85  C   ILE B  11       3.145  33.920  61.840
ATOM     86  O   ILE B  11       2.704  33.750  60.706
ATOM     87  N   LEU B  12       3.095  32.947  62.770
ATOM     88  CA  LEU B  12       2.418  31.732  62.436
ATOM     89  CB  LEU B  12       2.357  30.667  63.527
ATOM     90  CG  LEU B  12       1.305  29.632  63.082
ATOM     91  CD2 LEU B  12       0.443  29.148  64.246
ATOM     92  CD1 LEU B  12       1.881  28.558  62.149
ATOM     93  C   LEU B  12       0.965  32.002  62.143
ATOM     94  O   LEU B  12       0.474  31.453  61.162
ATOM     95  N   PRO B  13       0.199  32.750  62.912
ATOM     96  CA  PRO B  13      -1.148  32.993  62.468
ATOM     97  CD  PRO B  13       0.207  32.603  64.360
ATOM     98  CB  PRO B  13      -1.932  33.490  63.677
ATOM     99  CG  PRO B  13      -1.237  32.788  64.847
ATOM    100  C   PRO B  13      -1.229  33.913  61.292
ATOM    101  O   PRO B  13      -2.276  33.959  60.650
ATOM    102  N   ARG B  14      -0.151  34.671  61.025
ATOM    103  CA  ARG B  14      -0.058  35.635  59.964
ATOM    104  CB  ARG B  14       1.231  36.470  60.029
ATOM    105  CG  ARG B  14       1.248  37.436  61.214
ATOM    106  CD  ARG B  14       0.579  38.777  60.912
ATOM    107  NE  ARG B  14      -0.758  38.484  60.325
ATOM    108  CZ  ARG B  14      -1.081  38.988  59.100
ATOM    109  NH1 ARG B  14      -0.187  39.768  58.425
ATOM    110  NH2 ARG B  14      -2.301  38.715  58.551
ATOM    111  C   ARG B  14      -0.082  34.939  58.644
ATOM    112  O   ARG B  14      -0.520  35.508  57.648
ATOM    113  N   GLY B  15       0.409  33.692  58.575
ATOM    114  CA  GLY B  15       0.399  33.047  57.299
ATOM    115  C   GLY B  15       1.792  33.032  56.770
ATOM    116  O   GLY B  15       2.017  32.610  55.639
ATOM    117  N   SER B  16       2.763  33.539  57.553
ATOM    118  CA  SER B  16       4.123  33.414  57.115
ATOM    119  CB  SER B  16       4.868  34.758  57.091
ATOM    120  OG  SER B  16       4.274  35.630  56.143
ATOM    121  C   SER B  16       4.797  32.563  58.144
ATOM    122  O   SER B  16       5.746  32.981  58.799
ATOM    123  N   ARG B  17       4.362  31.301  58.262
ATOM    124  CA  ARG B  17       4.890  30.427  59.265
ATOM    125  CB  ARG B  17       4.086  29.114  59.416
ATOM    126  CG  ARG B  17       3.901  28.283  58.146
ATOM    127  CD  ARG B  17       2.750  27.284  58.288
ATOM    128  NE  ARG B  17       1.507  28.085  58.481
ATOM    129  CZ  ARG B  17       0.761  28.462  57.403
ATOM    130  NH1 ARG B  17       1.089  28.015  56.156
ATOM    131  NH2 ARG B  17      -0.312  29.288  57.571
ATOM    132  C   ARG B  17       6.333  30.170  59.001
ATOM    133  O   ARG B  17       7.109  29.924  59.924
ATOM    134  N   GLU B  18       6.734  30.188  57.724
ATOM    135  CA  GLU B  18       8.112  29.971  57.401
ATOM    136  CB  GLU B  18       8.358  29.830  55.887
ATOM    137  CG  GLU B  18       9.605  29.010  55.532
ATOM    138  CD  GLU B  18      10.854  29.761  55.968
ATOM    139  OE1 GLU B  18      10.992  30.952  55.583
ATOM    140  OE2 GLU B  18      11.688  29.156  56.694
ATOM    141  C   GLU B  18       8.965  31.105  57.926
ATOM    142  O   GLU B  18      10.092  30.868  58.359
ATOM    143  N   PRO B  19       8.490  32.329  57.873
ATOM    144  CA  PRO B  19       9.271  33.451  58.353
ATOM    145  CD  PRO B  19       7.691  32.720  56.716
ATOM    146  CB  PRO B  19       8.668  34.697  57.708
ATOM    147  CG  PRO B  19       8.069  34.172  56.397
ATOM    148  C   PRO B  19       9.416  33.597  59.832
ATOM    149  O   PRO B  19      10.153  34.487  60.255
ATOM    150  N   VAL B  20       8.741  32.761  60.632
ATOM    151  CA  VAL B  20       8.715  32.980  62.043
ATOM    152  CB  VAL B  20       7.909  31.939  62.721
ATOM    153  CG1 VAL B  20       7.892  32.178  64.241
ATOM    154  CG2 VAL B  20       6.545  32.011  62.010
ATOM    155  C   VAL B  20      10.102  33.062  62.592
ATOM    156  O   VAL B  20      10.956  32.207  62.368
ATOM    157  N   GLN B  21      10.318  34.170  63.329
ATOM    158  CA  GLN B  21      11.555  34.584  63.920
ATOM    159  CB  GLN B  21      11.413  35.979  64.559
ATOM    160  CG  GLN B  21      12.641  36.466  65.328
ATOM    161  CD  GLN B  21      12.405  36.182  66.806
ATOM    162  OE1 GLN B  21      11.266  36.131  67.270
ATOM    163  NE2 GLN B  21      13.515  35.995  67.571
ATOM    164  C   GLN B  21      11.988  33.604  64.955
ATOM    165  O   GLN B  21      13.163  33.245  65.010
ATOM    166  N   ARG B  22      11.053  33.115  65.793
ATOM    167  CA  ARG B  22      11.486  32.204  66.808
ATOM    168  CB  ARG B  22      10.456  31.891  67.910
ATOM    169  CG  ARG B  22      11.007  30.923  68.960
ATOM    170  CD  ARG B  22      10.305  31.012  70.316
ATOM    171  NE  ARG B  22       8.851  31.237  70.093
ATOM    172  CZ  ARG B  22       8.356  32.507  70.077
ATOM    173  NH1 ARG B  22       9.197  33.577  70.181
ATOM    174  NH2 ARG B  22       7.012  32.703  69.973
ATOM    175  C   ARG B  22      11.876  30.949  66.120
ATOM    176  O   ARG B  22      11.497  30.735  64.968
ATOM    177  N   SER B  23      12.697  30.121  66.802
ATOM    178  CA  SER B  23      13.143  28.890  66.220
ATOM    179  CB  SER B  23      13.951  28.016  67.198
ATOM    180  OG  SER B  23      13.185  27.743  68.362
ATOM    181  C   SER B  23      11.920  28.165  65.777
ATOM    182  O   SER B  23      11.088  27.742  66.574
ATOM    183  N   TRP B  24      11.799  28.033  64.445
ATOM    184  CA  TRP B  24      10.632  27.504  63.819
ATOM    185  CB  TRP B  24      10.135  28.510  62.748
ATOM    186  CG  TRP B  24      11.123  28.822  61.629
ATOM    187  CD2 TRP B  24      12.419  29.446  61.769
ATOM    188  CD1 TRP B  24      11.009  28.487  60.311
ATOM    189  NE1 TRP B  24      12.144  28.850  59.626
ATOM    190  CE2 TRP B  24      13.022  29.439  60.510
ATOM    191  CE3 TRP B  24      13.064  29.972  62.853
ATOM    192  CZ2 TRP B  24      14.274  29.954  60.317
ATOM    193  CZ3 TRP B  24      14.323  30.493  62.656
ATOM    194  CH2 TRP B  24      14.919  30.484  61.412
ATOM    195  C   TRP B  24      11.006  26.209  63.172
ATOM    196  O   TRP B  24      11.560  26.180  62.073
ATOM    197  N   LEU B  25      10.751  25.074  63.852
ATOM    198  CA  LEU B  25      11.027  23.862  63.150
ATOM    199  CB  LEU B  25      12.480  23.683  62.664
ATOM    200  CG  LEU B  25      12.655  22.435  61.779
ATOM    201  CD2 LEU B  25      14.137  22.101  61.568
ATOM    202  CD1 LEU B  25      11.882  22.578  60.456
ATOM    203  C   LEU B  25      10.793  22.719  64.049
ATOM    204  O   LEU B  25      11.146  22.744  65.228
ATOM    205  N   HIS B  26      10.170  21.666  63.508
ATOM    206  CA  HIS B  26      10.150  20.535  64.354
ATOM    207  ND1 HIS B  26       9.184  17.554  62.069
ATOM    208  CG  HIS B  26       9.678  18.755  62.529
ATOM    209  CB  HIS B  26       9.285  19.356  63.851
ATOM    210  NE2 HIS B  26      10.562  18.310  60.498
ATOM    211  CD2 HIS B  26      10.519  19.203  61.554
ATOM    212  CE1 HIS B  26       9.745  17.337  60.853
ATOM    213  C   HIS B  26      11.591  20.142  64.406
ATOM    214  O   HIS B  26      12.302  20.250  63.409
ATOM    215  N   GLY B  27      12.085  19.756  65.595
ATOM    216  CA  GLY B  27      13.446  19.321  65.701
ATOM    217  C   GLY B  27      14.273  20.332  66.439
ATOM    218  O   GLY B  27      15.079  19.973  67.297
ATOM    219  N   TYR B  28      14.178  21.626  66.087
ATOM    220  CA  TYR B  28      14.966  22.545  66.856
ATOM    221  CB  TYR B  28      15.234  23.875  66.135
ATOM    222  CG  TYR B  28      16.165  23.517  65.037
ATOM    223  CD1 TYR B  28      17.469  23.191  65.330
ATOM    224  CD2 TYR B  28      15.752  23.508  63.727
ATOM    225  CE1 TYR B  28      18.351  22.848  64.334
ATOM    226  CE2 TYR B  28      16.630  23.167  62.726
ATOM    227  CZ  TYR B  28      17.928  22.834  63.028
ATOM    228  OH  TYR B  28      18.821  22.484  61.993
ATOM    229  C   TYR B  28      14.354  22.835  68.194
ATOM    230  O   TYR B  28      14.994  22.678  69.232
ATOM    231  N   THR B  29      13.081  23.277  68.193
ATOM    232  CA  THR B  29      12.391  23.651  69.397
ATOM    233  CB  THR B  29      11.110  24.367  69.103
ATOM    234  OG1 THR B  29      10.210  23.516  68.409
ATOM    235  CG2 THR B  29      11.448  25.577  68.225
ATOM    236  C   THR B  29      12.027  22.455  70.208
ATOM    237  O   THR B  29      12.284  22.400  71.409
ATOM    238  N   ILE B  30      11.430  21.449  69.545
ATOM    239  CA  ILE B  30      10.929  20.285  70.207
ATOM    240  CB  ILE B  30       9.422  20.272  70.231
ATOM    241  CG2 ILE B  30       8.911  18.991  70.915
ATOM    242  CG1 ILE B  30       8.932  21.548  70.937
ATOM    243  CD1 ILE B  30       7.432  21.798  70.784
ATOM    244  C   ILE B  30      11.443  19.128  69.415
ATOM    245  O   ILE B  30      11.977  19.323  68.323
ATOM    246  N   ASP B  31      11.314  17.896  69.949
ATOM    247  CA  ASP B  31      11.870  16.757  69.283
ATOM    248  CB  ASP B  31      11.573  15.410  69.965
ATOM    249  CG  ASP B  31      10.079  15.157  69.864
ATOM    250  OD1 ASP B  31       9.302  16.148  69.921
ATOM    251  OD2 ASP B  31       9.695  13.966  69.719
ATOM    252  C   ASP B  31      11.294  16.698  67.909
ATOM    253  O   ASP B  31      10.163  17.123  67.672
ATOM    254  N   GLY B  32      12.107  16.187  66.962
ATOM    255  CA  GLY B  32      11.747  16.147  65.579
ATOM    256  C   GLY B  32      11.468  14.749  65.156
ATOM    257  O   GLY B  32      10.957  13.932  65.921
ATOM    258  N   GLY B  33      11.834  14.439  63.895
ATOM    259  CA  GLY B  33      11.451  13.168  63.374
ATOM    260  C   GLY B  33      12.622  12.254  63.180
ATOM    261  O   GLY B  33      12.537  11.330  62.373
ATOM    262  N   PHE B  34      13.739  12.436  63.914
ATOM    263  CA  PHE B  34      14.768  11.442  63.766
ATOM    264  CB  PHE B  34      16.156  11.910  64.243
ATOM    265  CG  PHE B  34      16.743  12.922  63.318
ATOM    266  CD1 PHE B  34      16.272  14.214  63.287
ATOM    267  CD2 PHE B  34      17.799  12.584  62.502
ATOM    268  CE1 PHE B  34      16.826  15.145  62.439
ATOM    269  CE2 PHE B  34      18.359  13.510  61.652
ATOM    270  CZ  PHE B  34      17.871  14.794  61.618
ATOM    271  C   PHE B  34      14.368  10.380  64.741
ATOM    272  O   PHE B  34      15.173   9.975  65.581
ATOM    273  N   ALA B  35      13.112   9.889  64.634
ATOM    274  CA  ALA B  35      12.610   8.906  65.551
ATOM    275  CB  ALA B  35      12.174   9.496  66.905
ATOM    276  C   ALA B  35      11.394   8.286  64.936
ATOM    277  O   ALA B  35      10.842   8.783  63.954
ATOM    278  N   ALA B  36      10.948   7.163  65.526
ATOM    279  CA  ALA B  36       9.825   6.416  65.043
ATOM    280  CB  ALA B  36       9.562   5.148  65.874
ATOM    281  C   ALA B  36       8.588   7.251  65.104
ATOM    282  O   ALA B  36       7.773   7.222  64.183
ATOM    283  N   HIS B  37       8.407   8.020  66.194
ATOM    284  CA  HIS B  37       7.198   8.779  66.303
ATOM    285  ND1 HIS B  37       4.438   6.858  65.798
ATOM    286  CG  HIS B  37       5.574   6.870  66.574
ATOM    287  CB  HIS B  37       6.143   8.108  67.194
ATOM    288  NE2 HIS B  37       5.177   4.762  65.875
ATOM    289  CD2 HIS B  37       6.013   5.583  66.612
ATOM    290  CE1 HIS B  37       4.246   5.575  65.406
ATOM    291  C   HIS B  37       7.521  10.098  66.918
ATOM    292  O   HIS B  37       8.570  10.276  67.534
ATOM    293  N   ALA B  38       6.626  11.081  66.720
ATOM    294  CA  ALA B  38       6.829  12.359  67.328
ATOM    295  CB  ALA B  38       7.646  13.331  66.459
ATOM    296  C   ALA B  38       5.482  12.974  67.540
ATOM    297  O   ALA B  38       4.558  12.765  66.756
ATOM    298  N   ALA B  39       5.333  13.753  68.626
ATOM    299  CA  ALA B  39       4.071  14.385  68.884
ATOM    300  CB  ALA B  39       3.952  14.968  70.303
ATOM    301  C   ALA B  39       3.947  15.515  67.915
ATOM    302  O   ALA B  39       4.938  16.165  67.583
ATOM    303  N   ALA B  40       2.717  15.782  67.432
ATOM    304  CA  ALA B  40       2.587  16.834  66.473
ATOM    305  CB  ALA B  40       2.551  16.334  65.020
ATOM    306  C   ALA B  40       1.337  17.617  66.694
ATOM    307  O   ALA B  40       0.342  17.134  67.232
ATOM    308  N   GLU B  41       1.373  18.882  66.238
ATOM    309  CA  GLU B  41       0.273  19.773  66.423
ATOM    310  CB  GLU B  41       0.694  21.251  66.490
ATOM    311  CG  GLU B  41       1.597  21.577  67.680
ATOM    312  CD  GLU B  41       0.832  21.268  68.958
ATOM    313  OE1 GLU B  41      -0.411  21.473  68.980
ATOM    314  OE2 GLU B  41       1.493  20.820  69.933
ATOM    315  C   GLU B  41      -0.646  19.626  65.259
ATOM    316  O   GLU B  41      -0.232  19.661  64.101
ATOM    317  N   ALA B  42      -1.945  19.458  65.557
ATOM    318  CA  ALA B  42      -2.905  19.386  64.504
ATOM    319  CB  ALA B  42      -4.343  19.128  64.985
ATOM    320  C   ALA B  42      -2.871  20.739  63.868
ATOM    321  O   ALA B  42      -2.341  21.688  64.429
ATOM    322  N   GLY B  43      -3.320  20.865  62.618
ATOM    323  CA  GLY B  43      -3.414  22.182  62.054
ATOM    324  C   GLY B  43      -2.186  22.496  61.274
ATOM    325  O   GLY B  43      -2.244  23.091  60.202
ATOM    326  N   TYR B  44      -1.024  22.163  61.844
ATOM    327  CA  TYR B  44       0.222  22.358  61.184
ATOM    328  CB  TYR B  44       1.403  22.411  62.155
ATOM    329  CG  TYR B  44       0.930  23.565  62.946
ATOM    330  CD1 TYR B  44       1.162  24.852  62.521
ATOM    331  CD2 TYR B  44       0.200  23.336  64.084
ATOM    332  CE1 TYR B  44       0.677  25.913  63.245
ATOM    333  CE2 TYR B  44      -0.286  24.384  64.805
ATOM    334  CZ  TYR B  44      -0.043  25.668  64.390
ATOM    335  OH  TYR B  44      -0.562  26.727  65.157
ATOM    336  C   TYR B  44       0.355  21.273  60.212
ATOM    337  O   TYR B  44       0.989  21.438  59.174
ATOM    338  N   ALA B  45      -0.228  20.114  60.561
ATOM    339  CA  ALA B  45      -0.063  19.015  59.682
ATOM    340  CB  ALA B  45      -0.700  17.712  60.196
ATOM    341  C   ALA B  45      -0.722  19.364  58.393
ATOM    342  O   ALA B  45      -1.800  19.964  58.350
ATOM    343  N   PHE B  46      -0.023  19.038  57.292
ATOM    344  CA  PHE B  46      -0.656  19.131  56.022
ATOM    345  CB  PHE B  46       0.088  19.857  54.893
ATOM    346  CG  PHE B  46      -0.987  20.011  53.869
ATOM    347  CD1 PHE B  46      -1.860  21.072  53.950
ATOM    348  CD2 PHE B  46      -1.145  19.093  52.855
ATOM    349  CE1 PHE B  46      -2.866  21.226  53.026
ATOM    350  CE2 PHE B  46      -2.151  19.242  51.927
ATOM    351  CZ  PHE B  46      -3.013  20.308  52.015
ATOM    352  C   PHE B  46      -0.794  17.716  55.629
ATOM    353  O   PHE B  46       0.164  16.939  55.692
ATOM    354  N   GLU B  47      -2.021  17.357  55.226
ATOM    355  CA  GLU B  47      -2.275  15.989  54.943
ATOM    356  CB  GLU B  47      -3.722  15.662  54.527
ATOM    357  CG  GLU B  47      -4.163  16.296  53.207
ATOM    358  CD  GLU B  47      -5.492  15.660  52.821
ATOM    359  OE1 GLU B  47      -5.876  14.656  53.478
ATOM    360  OE2 GLU B  47      -6.138  16.163  51.862
ATOM    361  C   GLU B  47      -1.381  15.564  53.849
ATOM    362  O   GLU B  47      -1.109  16.303  52.903
ATOM    363  N   LEU B  48      -0.851  14.349  54.019
ATOM    364  CA  LEU B  48      -0.051  13.734  53.026
ATOM    365  CB  LEU B  48       0.764  12.585  53.630
ATOM    366  CG  LEU B  48       1.930  12.223  52.730
ATOM    367  CD2 LEU B  48       2.756  13.501  52.532
ATOM    368  CD1 LEU B  48       1.458  11.593  51.413
ATOM    369  C   LEU B  48      -1.047  13.163  52.064
ATOM    370  O   LEU B  48      -2.111  12.714  52.488
ATOM    371  N   PRO B  49      -0.770  13.150  50.792
ATOM    372  CA  PRO B  49      -1.735  12.605  49.876
ATOM    373  CD  PRO B  49       0.046  14.183  50.176
ATOM    374  CB  PRO B  49      -1.236  12.981  48.483
ATOM    375  CG  PRO B  49      -0.466  14.295  48.728
ATOM    376  C   PRO B  49      -1.867  11.143  50.128
ATOM    377  O   PRO B  49      -0.919  10.521  50.593
ATOM    378  N   GLU B  50      -3.042  10.577  49.823
ATOM    379  CA  GLU B  50      -3.337   9.210  50.118
ATOM    380  CB  GLU B  50      -4.789   8.857  49.769
ATOM    381  CG  GLU B  50      -5.785   9.625  50.642
ATOM    382  CD  GLU B  50      -7.188   9.388  50.110
ATOM    383  OE1 GLU B  50      -7.422   8.314  49.493
ATOM    384  OE2 GLU B  50      -8.050  10.283  50.321
ATOM    385  C   GLU B  50      -2.427   8.294  49.361
ATOM    386  O   GLU B  50      -2.008   7.269  49.893
ATOM    387  N   ASP B  51      -2.095   8.629  48.099
ATOM    388  CA  ASP B  51      -1.293   7.715  47.335
ATOM    389  CB  ASP B  51      -1.661   7.717  45.838
ATOM    390  CG  ASP B  51      -1.404   9.104  45.253
ATOM    391  OD1 ASP B  51      -1.104  10.048  46.033
ATOM    392  OD2 ASP B  51      -1.516   9.236  44.006
ATOM    393  C   ASP B  51       0.161   8.070  47.447
ATOM    394  O   ASP B  51       0.927   7.818  46.518
ATOM    395  N   ALA B  52       0.594   8.644  48.591
ATOM    396  CA  ALA B  52       1.991   8.944  48.750
ATOM    397  CB  ALA B  52       2.326  10.441  48.621
ATOM    398  C   ALA B  52       2.407   8.507  50.128
ATOM    399  O   ALA B  52       1.736   8.779  51.122
ATOM    400  N   ASP B  53       3.551   7.807  50.227
ATOM    401  CA  ASP B  53       3.997   7.314  51.500
ATOM    402  CB  ASP B  53       4.865   6.044  51.363
ATOM    403  CG  ASP B  53       5.074   5.392  52.723
ATOM    404  OD1 ASP B  53       5.974   5.855  53.471
ATOM    405  OD2 ASP B  53       4.333   4.419  53.032
ATOM    406  C   ASP B  53       4.795   8.396  52.156
ATOM    407  O   ASP B  53       5.189   9.353  51.498
ATOM    408  N   PRO B  54       5.046   8.293  53.435
ATOM    409  CA  PRO B  54       5.857   9.281  54.069
ATOM    410  CD  PRO B  54       4.061   7.737  54.352
ATOM    411  CB  PRO B  54       5.774   8.982  55.562
ATOM    412  CG  PRO B  54       4.359   8.387  55.716
ATOM    413  C   PRO B  54       7.235   9.301  53.485
ATOM    414  O   PRO B  54       7.874  10.348  53.524
ATOM    415  N   VAL B  55       7.727   8.165  52.958
ATOM    416  CA  VAL B  55       9.043   8.118  52.377
ATOM    417  CB  VAL B  55       9.436   6.734  51.953
ATOM    418  CG1 VAL B  55      10.821   6.799  51.287
ATOM    419  CG2 VAL B  55       9.364   5.810  53.182
ATOM    420  C   VAL B  55       9.096   8.993  51.155
ATOM    421  O   VAL B  55      10.015   9.796  50.998
ATOM    422  N   ALA B  56       8.111   8.848  50.244
ATOM    423  CA  ALA B  56       8.078   9.605  49.019
ATOM    424  CB  ALA B  56       6.958   9.150  48.067
ATOM    425  C   ALA B  56       7.850  11.049  49.331
ATOM    426  O   ALA B  56       8.438  11.944  48.724
ATOM    427  N   THR B  57       6.953  11.298  50.295
ATOM    428  CA  THR B  57       6.536  12.609  50.668
ATOM    429  CB  THR B  57       5.337  12.548  51.523
ATOM    430  OG1 THR B  57       5.610  11.850  52.731
ATOM    431  CG2 THR B  57       4.292  11.801  50.687
ATOM    432  C   THR B  57       7.603  13.378  51.379
ATOM    433  O   THR B  57       7.687  14.594  51.222
ATOM    434  N   ALA B  58       8.463  12.694  52.152
ATOM    435  CA  ALA B  58       9.400  13.360  53.017
ATOM    436  CB  ALA B  58      10.315  12.372  53.763
ATOM    437  C   ALA B  58      10.289  14.318  52.270
ATOM    438  O   ALA B  58      10.527  15.422  52.760
ATOM    439  N   PRO B  59      10.806  13.984  51.128
ATOM    440  CA  PRO B  59      11.681  14.907  50.449
ATOM    441  CD  PRO B  59      11.114  12.599  50.820
ATOM    442  CB  PRO B  59      12.352  14.092  49.348
ATOM    443  CG  PRO B  59      12.343  12.654  49.902
ATOM    444  C   PRO B  59      10.977  16.139  49.957
ATOM    445  O   PRO B  59      11.631  17.154  49.721
ATOM    446  N   LEU B  60       9.656  16.050  49.749
ATOM    447  CA  LEU B  60       8.781  17.088  49.281
ATOM    448  CB  LEU B  60       7.491  16.423  48.770
ATOM    449  CG  LEU B  60       6.134  16.811  49.362
ATOM    450  CD2 LEU B  60       5.074  15.947  48.658
ATOM    451  CD1 LEU B  60       5.822  18.312  49.298
ATOM    452  C   LEU B  60       8.586  18.172  50.308
ATOM    453  O   LEU B  60       8.393  19.341  49.975
ATOM    454  N   LEU B  61       8.674  17.804  51.595
ATOM    455  CA  LEU B  61       8.427  18.640  52.741
ATOM    456  CB  LEU B  61       8.667  17.882  54.059
ATOM    457  CG  LEU B  61       7.847  16.588  54.200
ATOM    458  CD2 LEU B  61       6.352  16.840  53.956
ATOM    459  CD1 LEU B  61       8.134  15.884  55.536
ATOM    460  C   LEU B  61       9.365  19.804  52.782
ATOM    461  O   LEU B  61       9.025  20.841  53.351
ATOM    462  N   CYS B  62      10.597  19.638  52.262
ATOM    463  CA  CYS B  62      11.549  20.706  52.315
ATOM    464  CB  CYS B  62      12.784  20.367  53.165
ATOM    465  SG  CYS B  62      13.964  21.748  53.266
ATOM    466  C   CYS B  62      12.029  20.978  50.919
ATOM    467  O   CYS B  62      11.776  22.045  50.364
ATOM    468  N   ALA B  63      12.750  20.015  50.308
ATOM    469  CA  ALA B  63      13.320  20.219  49.005
ATOM    470  CB  ALA B  63      14.151  19.016  48.524
ATOM    471  C   ALA B  63      12.248  20.459  47.979
ATOM    472  O   ALA B  63      12.360  21.381  47.173
ATOM    473  N   GLY B  64      11.169  19.658  47.973
ATOM    474  CA  GLY B  64      10.169  19.822  46.949
ATOM    475  C   GLY B  64       9.483  21.156  47.033
ATOM    476  O   GLY B  64       9.361  21.865  46.034
ATOM    477  N   LEU B  65       9.034  21.545  48.240
ATOM    478  CA  LEU B  65       8.285  22.758  48.424
ATOM    479  CB  LEU B  65       7.833  22.962  49.881
ATOM    480  CG  LEU B  65       7.002  21.801  50.459
ATOM    481  CD2 LEU B  65       5.899  21.356  49.491
ATOM    482  CD1 LEU B  65       6.467  22.144  51.856
ATOM    483  C   LEU B  65       9.164  23.926  48.090
ATOM    484  O   LEU B  65       8.709  24.897  47.487
ATOM    485  N   ILE B  66      10.453  23.864  48.487
ATOM    486  CA  ILE B  66      11.341  24.974  48.289
ATOM    487  CB  ILE B  66      12.705  24.805  48.899
ATOM    488  CG2 ILE B  66      12.529  24.679  50.418
ATOM    489  CG1 ILE B  66      13.467  23.640  48.254
ATOM    490  CD1 ILE B  66      14.954  23.618  48.604
ATOM    491  C   ILE B  66      11.539  25.237  46.828
ATOM    492  O   ILE B  66      11.555  26.385  46.392
ATOM    493  N   GLY B  67      11.743  24.185  46.022
ATOM    494  CA  GLY B  67      11.944  24.392  44.616
ATOM    495  C   GLY B  67      10.692  24.895  43.968
ATOM    496  O   GLY B  67      10.739  25.746  43.081
ATOM    497  N   TRP B  68       9.534  24.347  44.380
ATOM    498  CA  TRP B  68       8.272  24.696  43.790
ATOM    499  CB  TRP B  68       7.104  23.900  44.396
ATOM    500  CG  TRP B  68       5.768  24.154  43.743
ATOM    501  CD2 TRP B  68       4.928  25.290  44.004
ATOM    502  CD1 TRP B  68       5.119  23.401  42.809
ATOM    503  NE1 TRP B  68       3.926  23.991  42.473
ATOM    504  CE2 TRP B  68       3.795  25.155  43.201
ATOM    505  CE3 TRP B  68       5.087  26.353  44.846
ATOM    506  CZ2 TRP B  68       2.799  26.091  43.226
ATOM    507  CZ3 TRP B  68       4.083  27.295  44.868
ATOM    508  CH2 TRP B  68       2.964  27.164  44.074
ATOM    509  C   TRP B  68       8.007  26.146  44.044
ATOM    510  O   TRP B  68       7.612  26.892  43.148
ATOM    511  N   GLN B  69       8.223  26.575  45.297
ATOM    512  CA  GLN B  69       7.974  27.922  45.713
ATOM    513  CB  GLN B  69       8.178  28.059  47.220
ATOM    514  CG  GLN B  69       9.596  27.780  47.691
ATOM    515  CD  GLN B  69      10.364  29.088  47.650
ATOM    516  OE1 GLN B  69      11.560  29.085  47.372
ATOM    517  NE2 GLN B  69       9.669  30.222  47.937
ATOM    518  C   GLN B  69       8.908  28.862  45.006
ATOM    519  O   GLN B  69       8.495  29.931  44.560
ATOM    520  N   SER B  70      10.192  28.479  44.866
ATOM    521  CA  SER B  70      11.171  29.337  44.255
ATOM    522  CB  SER B  70      12.582  28.721  44.236
ATOM    523  OG  SER B  70      12.612  27.576  43.396
ATOM    524  C   SER B  70      10.781  29.592  42.834
ATOM    525  O   SER B  70      10.955  30.695  42.316
ATOM    526  N   LEU B  71      10.240  28.565  42.158
ATOM    527  CA  LEU B  71       9.857  28.732  40.789
ATOM    528  CB  LEU B  71       9.384  27.431  40.118
ATOM    529  CG  LEU B  71      10.504  26.390  39.942
ATOM    530  CD2 LEU B  71      11.763  27.014  39.316
ATOM    531  CD1 LEU B  71      10.000  25.172  39.154
ATOM    532  C   LEU B  71       8.749  29.730  40.717
ATOM    533  O   LEU B  71       8.710  30.555  39.808
ATOM    534  N   LYS B  72       7.812  29.685  41.682
ATOM    535  CA  LYS B  72       6.698  30.589  41.657
ATOM    536  CB  LYS B  72       5.681  30.331  42.782
ATOM    537  CG  LYS B  72       4.385  31.136  42.638
ATOM    538  CD  LYS B  72       3.219  30.583  43.463
ATOM    539  CE  LYS B  72       3.387  30.753  44.973
ATOM    540  NZ  LYS B  72       2.214  30.184  45.676
ATOM    541  C   LYS B  72       7.206  31.989  41.787
ATOM    542  O   LYS B  72       6.720  32.899  41.115
ATOM    543  N   MET B  73       8.221  32.205  42.645
ATOM    544  CA  MET B  73       8.706  33.542  42.833
ATOM    545  CB  MET B  73       9.748  33.700  43.954
ATOM    546  CG  MET B  73      10.204  35.158  44.086
ATOM    547  SD  MET B  73      11.026  35.613  45.645
ATOM    548  CE  MET B  73       9.484  35.893  46.567
ATOM    549  C   MET B  73       9.300  34.062  41.550
ATOM    550  O   MET B  73       9.201  35.251  41.252
ATOM    551  N   ALA B  74       9.976  33.194  40.773
ATOM    552  CA  ALA B  74      10.610  33.600  39.545
ATOM    553  CB  ALA B  74      11.466  32.479  38.930
ATOM    554  C   ALA B  74       9.627  34.025  38.480
ATOM    555  O   ALA B  74       9.845  35.047  37.828
ATOM    556  N   GLY B  75       8.511  33.273  38.298
ATOM    557  CA  GLY B  75       7.557  33.496  37.228
ATOM    558  C   GLY B  75       7.637  32.296  36.287
ATOM    559  O   GLY B  75       8.671  31.635  36.249
ATOM    560  N   GLU B  76       6.557  31.984  35.503
ATOM    561  CA  GLU B  76       6.494  30.814  34.651
ATOM    562  CB  GLU B  76       5.523  29.766  35.212
ATOM    563  CG  GLU B  76       5.963  29.252  36.584
ATOM    564  CD  GLU B  76       4.745  28.690  37.301
ATOM    565  OE1 GLU B  76       3.678  28.554  36.644
ATOM    566  OE2 GLU B  76       4.866  28.409  38.523
ATOM    567  C   GLU B  76       6.002  31.195  33.281
ATOM    568  O   GLU B  76       5.619  32.337  33.040
ATOM    569  N   GLY B  77       6.018  30.219  32.339
ATOM    570  CA  GLY B  77       5.560  30.423  30.989
ATOM    571  C   GLY B  77       6.710  30.888  30.165
ATOM    572  O   GLY B  77       6.550  31.307  29.021
ATOM    573  N   ARG B  78       7.918  30.796  30.732
ATOM    574  CA  ARG B  78       9.081  31.290  30.071
ATOM    575  CB  ARG B  78       9.585  32.571  30.740
ATOM    576  CG  ARG B  78       9.889  32.351  32.226
ATOM    577  CD  ARG B  78       9.963  33.637  33.048
ATOM    578  NE  ARG B  78       8.699  34.385  32.802
ATOM    579  CZ  ARG B  78       8.542  35.639  33.312
ATOM    580  NH1 ARG B  78       9.542  36.204  34.049
ATOM    581  NH2 ARG B  78       7.386  36.331  33.090
ATOM    582  C   ARG B  78      10.147  30.257  30.228
ATOM    583  O   ARG B  78       9.875  29.118  30.606
ATOM    584  N   THR B  79      11.397  30.638  29.904
ATOM    585  CA  THR B  79      12.503  29.737  30.021
ATOM    586  CB  THR B  79      13.501  29.894  28.913
ATOM    587  OG1 THR B  79      14.018  31.218  28.912
ATOM    588  CG2 THR B  79      12.807  29.593  27.572
ATOM    589  C   THR B  79      13.208  30.043  31.304
ATOM    590  O   THR B  79      13.456  31.205  31.627
ATOM    591  N   ILE B  80      13.524  28.995  32.094
ATOM    592  CA  ILE B  80      14.218  29.217  33.329
ATOM    593  CB  ILE B  80      13.403  29.005  34.574
ATOM    594  CG2 ILE B  80      12.250  30.021  34.544
ATOM    595  CG1 ILE B  80      12.948  27.545  34.724
ATOM    596  CD1 ILE B  80      12.428  27.236  36.128
ATOM    597  C   ILE B  80      15.392  28.298  33.383
ATOM    598  O   ILE B  80      15.375  27.209  32.811
ATOM    599  N   GLY B  81      16.465  28.735  34.072
ATOM    600  CA  GLY B  81      17.640  27.922  34.148
ATOM    601  C   GLY B  81      17.750  27.382  35.537
ATOM    602  O   GLY B  81      17.590  28.108  36.517
ATOM    603  N   ILE B  82      18.058  26.074  35.643
ATOM    604  CA  ILE B  82      18.189  25.431  36.918
ATOM    605  CB  ILE B  82      17.471  24.104  36.968
ATOM    606  CG2 ILE B  82      17.747  23.440  38.328
ATOM    607  CG1 ILE B  82      15.972  24.284  36.666
ATOM    608  CD1 ILE B  82      15.247  25.206  37.647
ATOM    609  C   ILE B  82      19.650  25.141  37.079
ATOM    610  O   ILE B  82      20.209  24.336  36.335
ATOM    611  N   TYR B  83      20.311  25.776  38.070
ATOM    612  CA  TYR B  83      21.722  25.567  38.239
ATOM    613  CB  TYR B  83      22.510  26.819  38.679
ATOM    614  CG  TYR B  83      22.725  27.770  37.546
ATOM    615  CD1 TYR B  83      21.705  28.545  37.046
ATOM    616  CD2 TYR B  83      23.982  27.906  37.003
ATOM    617  CE1 TYR B  83      21.937  29.423  36.009
ATOM    618  CE2 TYR B  83      24.221  28.781  35.970
ATOM    619  CZ  TYR B  83      23.194  29.542  35.468
ATOM    620  OH  TYR B  83      23.432  30.443  34.406
ATOM    621  C   TYR B  83      21.955  24.549  39.313
ATOM    622  O   TYR B  83      21.595  24.752  40.473
ATOM    623  N   GLY B  84      22.563  23.411  38.915
ATOM    624  CA  GLY B  84      22.986  22.373  39.814
ATOM    625  C   GLY B  84      21.896  21.388  39.996
ATOM    626  O   GLY B  84      21.097  21.576  40.904
ATOM    627  N   PHE B  85      21.905  20.296  39.190
ATOM    628  CA  PHE B  85      20.912  19.253  39.158
ATOM    629  CB  PHE B  85      20.916  18.584  37.769
ATOM    630  CG  PHE B  85      19.944  17.459  37.670
ATOM    631  CD1 PHE B  85      18.611  17.684  37.407
ATOM    632  CD2 PHE B  85      20.385  16.163  37.808
ATOM    633  CE1 PHE B  85      17.734  16.630  37.310
ATOM    634  CE2 PHE B  85      19.514  15.105  37.712
ATOM    635  CZ  PHE B  85      18.186  15.340  37.462
ATOM    636  C   PHE B  85      21.283  18.234  40.183
ATOM    637  O   PHE B  85      21.868  17.199  39.871
ATOM    638  N   GLY B  86      20.875  18.471  41.441
ATOM    639  CA  GLY B  86      21.248  17.587  42.499
ATOM    640  C   GLY B  86      20.014  17.252  43.258
ATOM    641  O   GLY B  86      18.952  17.042  42.672
ATOM    642  N   ALA B  87      20.129  17.200  44.599
ATOM    643  CA  ALA B  87      19.000  16.796  45.374
ATOM    644  CB  ALA B  87      19.260  16.873  46.889
ATOM    645  C   ALA B  87      17.851  17.712  45.081
ATOM    646  O   ALA B  87      16.753  17.243  44.787
ATOM    647  N   ALA B  88      18.055  19.040  45.175
ATOM    648  CA  ALA B  88      16.989  19.947  44.846
ATOM    649  CB  ALA B  88      17.180  21.361  45.406
ATOM    650  C   ALA B  88      16.761  20.072  43.362
ATOM    651  O   ALA B  88      15.622  20.058  42.905
ATOM    652  N   ALA B  89      17.828  20.186  42.543
ATOM    653  CA  ALA B  89      17.538  20.515  41.168
ATOM    654  CB  ALA B  89      18.658  20.805  40.208
ATOM    655  C   ALA B  89      16.782  19.489  40.421
ATOM    656  O   ALA B  89      15.977  19.853  39.566
ATOM    657  N   HIS B  90      17.046  18.197  40.659
ATOM    658  CA  HIS B  90      16.375  17.218  39.857
ATOM    659  ND1 HIS B  90      16.608  15.486  42.742
ATOM    660  CG  HIS B  90      16.114  15.257  41.477
ATOM    661  CB  HIS B  90      16.747  15.765  40.216
ATOM    662  NE2 HIS B  90      14.776  14.249  42.989
ATOM    663  CD2 HIS B  90      14.996  14.500  41.646
ATOM    664  CE1 HIS B  90      15.770  14.861  43.607
ATOM    665  C   HIS B  90      14.894  17.384  40.047
ATOM    666  O   HIS B  90      14.119  17.130  39.128
ATOM    667  N   ILE B  91      14.453  17.745  41.269
ATOM    668  CA  ILE B  91      13.052  17.966  41.530
ATOM    669  CB  ILE B  91      12.687  17.986  43.001
ATOM    670  CG2 ILE B  91      13.088  19.342  43.596
ATOM    671  CG1 ILE B  91      11.186  17.710  43.212
ATOM    672  CD1 ILE B  91      10.265  18.829  42.729
ATOM    673  C   ILE B  91      12.615  19.243  40.870
ATOM    674  O   ILE B  91      11.508  19.339  40.344
ATOM    675  N   LEU B  92      13.492  20.265  40.880
ATOM    676  CA  LEU B  92      13.176  21.566  40.357
ATOM    677  CB  LEU B  92      14.384  22.518  40.427
ATOM    678  CG  LEU B  92      14.968  22.693  41.840
ATOM    679  CD2 LEU B  92      13.886  23.098  42.840
ATOM    680  CD1 LEU B  92      16.159  23.664  41.840
ATOM    681  C   LEU B  92      12.830  21.432  38.904
ATOM    682  O   LEU B  92      11.909  22.081  38.413
ATOM    683  N   VAL B  93      13.568  20.587  38.160
ATOM    684  CA  VAL B  93      13.285  20.471  36.757
ATOM    685  CB  VAL B  93      14.262  19.627  35.985
ATOM    686  CG1 VAL B  93      15.601  20.371  35.942
ATOM    687  CG2 VAL B  93      14.380  18.247  36.637
ATOM    688  C   VAL B  93      11.899  19.944  36.536
ATOM    689  O   VAL B  93      11.203  20.415  35.639
ATOM    690  N   GLN B  94      11.459  18.952  37.335
ATOM    691  CA  GLN B  94      10.166  18.349  37.150
ATOM    692  CB  GLN B  94       9.991  17.089  38.015
ATOM    693  CG  GLN B  94      11.005  16.003  37.637
ATOM    694  CD  GLN B  94      10.789  14.782  38.517
ATOM    695  OE1 GLN B  94       9.707  14.197  38.523
ATOM    696  NE2 GLN B  94      11.841  14.387  39.285
ATOM    697  C   GLN B  94       9.057  19.315  37.452
ATOM    698  O   GLN B  94       8.073  19.380  36.717
ATOM    699  N   VAL B  95       9.178  20.098  38.541
ATOM    700  CA  VAL B  95       8.146  21.027  38.905
ATOM    701  CB  VAL B  95       8.424  21.712  40.214
ATOM    702  CG1 VAL B  95       8.350  20.658  41.335
ATOM    703  CG2 VAL B  95       9.794  22.402  40.130
ATOM    704  C   VAL B  95       8.021  22.062  37.828
ATOM    705  O   VAL B  95       6.916  22.429  37.427
ATOM    706  N   CYS B  96       9.165  22.525  37.296
ATOM    707  CA  CYS B  96       9.208  23.563  36.307
ATOM    708  CB  CYS B  96      10.652  23.844  35.855
ATOM    709  SG  CYS B  96      10.780  25.145  34.599
ATOM    710  C   CYS B  96       8.425  23.120  35.113
ATOM    711  O   CYS B  96       7.656  23.893  34.543
ATOM    712  N   LYS B  97       8.601  21.855  34.699
ATOM    713  CA  LYS B  97       7.910  21.359  33.549
ATOM    714  CB  LYS B  97       8.396  19.966  33.132
ATOM    715  CG  LYS B  97       7.947  19.610  31.722
ATOM    716  CD  LYS B  97       8.531  20.540  30.657
ATOM    717  CE  LYS B  97       7.940  20.288  29.270
ATOM    718  NZ  LYS B  97       8.326  21.379  28.348
ATOM    719  C   LYS B  97       6.436  21.300  33.833
ATOM    720  O   LYS B  97       5.620  21.638  32.979
ATOM    721  N   HIS B  98       6.057  20.886  35.057
ATOM    722  CA  HIS B  98       4.670  20.777  35.423
ATOM    723  ND1 HIS B  98       2.292  18.976  36.937
ATOM    724  CG  HIS B  98       3.040  20.090  37.249
ATOM    725  CB  HIS B  98       4.479  20.273  36.865
ATOM    726  NE2 HIS B  98       0.955  20.342  38.075
ATOM    727  CD2 HIS B  98       2.208  20.913  37.943
ATOM    728  CE1 HIS B  98       1.053  19.179  37.456
ATOM    729  C   HIS B  98       4.072  22.148  35.332
ATOM    730  O   HIS B  98       2.904  22.314  34.987
ATOM    731  N   ARG B  99       4.886  23.162  35.665
ATOM    732  CA  ARG B  99       4.548  24.559  35.682
ATOM    733  CB  ARG B  99       5.614  25.433  36.366
ATOM    734  CG  ARG B  99       5.728  25.157  37.865
ATOM    735  CD  ARG B  99       4.375  24.914  38.536
ATOM    736  NE  ARG B  99       3.539  26.123  38.312
ATOM    737  CZ  ARG B  99       2.203  26.089  38.580
ATOM    738  NH1 ARG B  99       1.637  24.942  39.049
ATOM    739  NH2 ARG B  99       1.436  27.200  38.373
ATOM    740  C   ARG B  99       4.335  25.093  34.299
ATOM    741  O   ARG B  99       3.777  26.177  34.140
ATOM    742  N   GLY B 100       4.827  24.412  33.250
ATOM    743  CA  GLY B 100       4.589  24.981  31.958
ATOM    744  C   GLY B 100       5.721  25.898  31.644
ATOM    745  O   GLY B 100       5.539  26.966  31.062
ATOM    746  N   GLN B 101       6.933  25.511  32.068
ATOM    747  CA  GLN B 101       8.062  26.320  31.732
ATOM    748  CB  GLN B 101       8.836  26.839  32.949
ATOM    749  CG  GLN B 101       8.052  27.791  33.848
ATOM    750  CD  GLN B 101       8.993  28.179  34.976
ATOM    751  OE1 GLN B 101       9.317  27.365  35.840
ATOM    752  NE2 GLN B 101       9.469  29.453  34.956
ATOM    753  C   GLN B 101       9.016  25.475  30.953
ATOM    754  O   GLN B 101       8.958  24.246  31.015
ATOM    755  N   SER B 102       9.900  26.131  30.170
ATOM    756  CA  SER B 102      10.916  25.447  29.413
ATOM    757  CB  SER B 102      11.269  26.136  28.079
ATOM    758  OG  SER B 102      12.280  25.403  27.403
ATOM    759  C   SER B 102      12.143  25.483  30.267
ATOM    760  O   SER B 102      12.454  26.511  30.865
ATOM    761  N   VAL B 103      12.890  24.359  30.333
ATOM    762  CA  VAL B 103      13.970  24.301  31.280
ATOM    763  CB  VAL B 103      13.828  23.143  32.228
ATOM    764  CG1 VAL B 103      15.019  23.145  33.202
ATOM    765  CG2 VAL B 103      12.446  23.208  32.901
ATOM    766  C   VAL B 103      15.313  24.121  30.632
ATOM    767  O   VAL B 103      15.484  23.334  29.703
ATOM    768  N   TYR B 104      16.318  24.857  31.157
ATOM    769  CA  TYR B 104      17.682  24.723  30.737
ATOM    770  CB  TYR B 104      18.314  26.073  30.343
ATOM    771  CG  TYR B 104      19.719  25.862  29.889
ATOM    772  CD1 TYR B 104      19.970  25.405  28.617
ATOM    773  CD2 TYR B 104      20.781  26.136  30.722
ATOM    774  CE1 TYR B 104      21.260  25.213  28.183
ATOM    775  CE2 TYR B 104      22.074  25.946  30.293
ATOM    776  CZ  TYR B 104      22.312  25.481  29.023
ATOM    777  OH  TYR B 104      23.637  25.284  28.578
ATOM    778  C   TYR B 104      18.375  24.229  31.970
ATOM    779  O   TYR B 104      18.349  24.891  33.006
ATOM    780  N   ALA B 105      19.003  23.039  31.898
ATOM    781  CA  ALA B 105      19.622  22.493  33.071
ATOM    782  CB  ALA B 105      19.420  20.972  33.216
ATOM    783  C   ALA B 105      21.090  22.761  32.987
ATOM    784  O   ALA B 105      21.703  22.610  31.932
ATOM    785  N   PHE B 106      21.688  23.196  34.114
ATOM    786  CA  PHE B 106      23.087  23.510  34.123
ATOM    787  CB  PHE B 106      23.362  24.992  34.422
ATOM    788  CG  PHE B 106      24.804  25.082  34.760
ATOM    789  CD1 PHE B 106      25.758  24.889  33.793
ATOM    790  CD2 PHE B 106      25.198  25.367  36.047
ATOM    791  CE1 PHE B 106      27.086  24.969  34.120
ATOM    792  CE2 PHE B 106      26.530  25.451  36.373
ATOM    793  CZ  PHE B 106      27.482  25.248  35.405
ATOM    794  C   PHE B 106      23.783  22.717  35.183
ATOM    795  O   PHE B 106      23.387  22.742  36.348
ATOM    796  N   VAL B 107      24.849  21.983  34.794
ATOM    797  CA  VAL B 107      25.623  21.234  35.745
ATOM    798  CB  VAL B 107      25.083  19.855  35.990
ATOM    799  CG1 VAL B 107      26.023  19.123  36.965
ATOM    800  CG2 VAL B 107      23.631  19.977  36.484
ATOM    801  C   VAL B 107      27.001  21.059  35.180
ATOM    802  O   VAL B 107      27.163  20.840  33.981
ATOM    803  N   LEU B 108      28.036  21.199  36.035
ATOM    804  CA  LEU B 108      29.389  20.990  35.605
ATOM    805  CB  LEU B 108      30.409  21.543  36.635
ATOM    806  CG  LEU B 108      31.900  21.564  36.220
ATOM    807  CD2 LEU B 108      32.417  20.193  35.759
ATOM    808  CD1 LEU B 108      32.769  22.142  37.349
ATOM    809  C   LEU B 108      29.580  19.514  35.383
ATOM    810  O   LEU B 108      30.137  19.107  34.365
ATOM    811  N   PRO B 109      29.145  18.686  36.296
ATOM    812  CA  PRO B 109      29.250  17.261  36.129
ATOM    813  CD  PRO B 109      29.081  19.055  37.703
ATOM    814  CB  PRO B 109      29.223  16.656  37.534
ATOM    815  CG  PRO B 109      28.657  17.769  38.428
ATOM    816  C   PRO B 109      28.124  16.800  35.277
ATOM    817  O   PRO B 109      27.978  15.600  35.068
ATOM    818  N   GLY B 110      27.339  17.735  34.734
ATOM    819  CA  GLY B 110      26.089  17.383  34.143
ATOM    820  C   GLY B 110      26.206  16.311  33.105
ATOM    821  O   GLY B 110      25.357  15.425  33.104
ATOM    822  N   ASP B 111      27.262  16.301  32.261
ATOM    823  CA  ASP B 111      27.249  15.479  31.073
ATOM    824  CB  ASP B 111      28.612  15.455  30.358
ATOM    825  CG  ASP B 111      28.416  14.935  28.936
ATOM    826  OD1 ASP B 111      27.577  14.019  28.731
ATOM    827  OD2 ASP B 111      29.106  15.470  28.026
ATOM    828  C   ASP B 111      26.871  14.062  31.376
ATOM    829  O   ASP B 111      25.813  13.619  30.937
ATOM    830  N   GLU B 112      27.672  13.319  32.153
ATOM    831  CA  GLU B 112      27.193  12.012  32.500
ATOM    832  CB  GLU B 112      28.278  11.092  33.077
ATOM    833  CG  GLU B 112      27.736   9.707  33.437
ATOM    834  CD  GLU B 112      28.865   8.887  34.042
ATOM    835  OE1 GLU B 112      29.965   9.463  34.256
ATOM    836  OE2 GLU B 112      28.640   7.674  34.297
ATOM    837  C   GLU B 112      26.176  12.155  33.565
ATOM    838  O   GLU B 112      25.104  11.551  33.540
ATOM    839  N   ALA B 113      26.503  13.045  34.507
ATOM    840  CA  ALA B 113      25.777  13.196  35.717
ATOM    841  CB  ALA B 113      26.475  14.074  36.771
ATOM    842  C   ALA B 113      24.450  13.786  35.452
ATOM    843  O   ALA B 113      23.687  13.362  34.587
ATOM    844  N   GLY B 114      24.157  14.818  36.237
ATOM    845  CA  GLY B 114      22.849  15.358  36.314
ATOM    846  C   GLY B 114      22.303  15.728  34.981
ATOM    847  O   GLY B 114      21.118  15.522  34.749
ATOM    848  N   ARG B 115      23.114  16.267  34.062
ATOM    849  CA  ARG B 115      22.599  16.686  32.787
ATOM    850  CB  ARG B 115      23.695  17.182  31.831
ATOM    851  CG  ARG B 115      23.209  17.489  30.418
ATOM    852  CD  ARG B 115      24.347  17.732  29.426
ATOM    853  NE  ARG B 115      23.732  18.017  28.100
ATOM    854  CZ  ARG B 115      23.338  16.993  27.286
ATOM    855  NH1 ARG B 115      23.463  15.698  27.704
ATOM    856  NH2 ARG B 115      22.826  17.266  26.050
ATOM    857  C   ARG B 115      21.922  15.529  32.127
ATOM    858  O   ARG B 115      20.816  15.672  31.610
ATOM    859  N   LYS B 116      22.545  14.340  32.155
ATOM    860  CA  LYS B 116      21.968  13.193  31.512
ATOM    861  CB  LYS B 116      22.825  11.932  31.738
ATOM    862  CG  LYS B 116      22.178  10.617  31.295
ATOM    863  CD  LYS B 116      22.022  10.461  29.784
ATOM    864  CE  LYS B 116      21.407   9.117  29.388
ATOM    865  NZ  LYS B 116      22.276   8.010  29.848
ATOM    866  C   LYS B 116      20.626  12.921  32.110
ATOM    867  O   LYS B 116      19.646  12.712  31.396
ATOM    868  N   PHE B 117      20.548  12.942  33.450
ATOM    869  CA  PHE B 117      19.328  12.618  34.125
ATOM    870  CB  PHE B 117      19.506  12.431  35.642
ATOM    871  CG  PHE B 117      18.306  11.699  36.136
ATOM    872  CD1 PHE B 117      18.183  10.350  35.898
ATOM    873  CD2 PHE B 117      17.321  12.337  36.849
ATOM    874  CE1 PHE B 117      17.088   9.649  36.343
ATOM    875  CE2 PHE B 117      16.224  11.636  37.296
ATOM    876  CZ  PHE B 117      16.100  10.291  37.045
ATOM    877  C   PHE B 117      18.317  13.697  33.878
ATOM    878  O   PHE B 117      17.121  13.432  33.784
ATOM    879  N   THR B 118      18.777  14.954  33.775
ATOM    880  CA  THR B 118      17.907  16.081  33.614
ATOM    881  CB  THR B 118      18.661  17.378  33.567
ATOM    882  OG1 THR B 118      19.477  17.508  34.720
ATOM    883  CG2 THR B 118      17.647  18.527  33.561
ATOM    884  C   THR B 118      17.146  15.917  32.335
ATOM    885  O   THR B 118      15.960  16.243  32.274
ATOM    886  N   LEU B 119      17.800  15.410  31.270
ATOM    887  CA  LEU B 119      17.082  15.240  30.036
ATOM    888  CB  LEU B 119      17.923  14.712  28.856
ATOM    889  CG  LEU B 119      18.828  15.755  28.169
ATOM    890  CD2 LEU B 119      19.953  16.259  29.080
ATOM    891  CD1 LEU B 119      17.993  16.889  27.554
ATOM    892  C   LEU B 119      15.966  14.260  30.233
ATOM    893  O   LEU B 119      14.860  14.474  29.741
ATOM    894  N   ASP B 120      16.213  13.147  30.949
ATOM    895  CA  ASP B 120      15.148  12.196  31.103
ATOM    896  CB  ASP B 120      15.561  10.833  31.701
ATOM    897  CG  ASP B 120      16.100  10.986  33.111
ATOM    898  OD1 ASP B 120      15.276  11.178  34.045
ATOM    899  OD2 ASP B 120      17.346  10.912  33.278
ATOM    900  C   ASP B 120      14.065  12.821  31.926
ATOM    901  O   ASP B 120      12.886  12.526  31.739
ATOM    902  N   LEU B 121      14.451  13.712  32.857
ATOM    903  CA  LEU B 121      13.541  14.411  33.720
ATOM    904  CB  LEU B 121      14.220  15.180  34.865
ATOM    905  CG  LEU B 121      14.840  14.236  35.908
ATOM    906  CD2 LEU B 121      13.887  13.066  36.206
ATOM    907  CD1 LEU B 121      15.273  15.001  37.169
ATOM    908  C   LEU B 121      12.691  15.361  32.929
ATOM    909  O   LEU B 121      11.647  15.797  33.416
ATOM    910  N   GLY B 122      13.123  15.754  31.711
ATOM    911  CA  GLY B 122      12.275  16.631  30.950
ATOM    912  C   GLY B 122      12.950  17.928  30.615
ATOM    913  O   GLY B 122      12.327  18.799  30.009
ATOM    914  N   ALA B 123      14.229  18.118  30.989
ATOM    915  CA  ALA B 123      14.856  19.363  30.632
ATOM    916  CB  ALA B 123      16.296  19.508  31.141
ATOM    917  C   ALA B 123      14.908  19.466  29.138
ATOM    918  O   ALA B 123      15.262  18.509  28.451
ATOM    919  N   VAL B 124      14.517  20.642  28.598
ATOM    920  CA  VAL B 124      14.545  20.848  27.177
ATOM    921  CB  VAL B 124      13.783  22.057  26.705
ATOM    922  CG1 VAL B 124      12.325  21.926  27.171
ATOM    923  CG2 VAL B 124      14.495  23.339  27.156
ATOM    924  C   VAL B 124      15.964  20.976  26.706
ATOM    925  O   VAL B 124      16.335  20.414  25.678
ATOM    926  N   TRP B 125      16.800  21.729  27.453
ATOM    927  CA  TRP B 125      18.159  21.929  27.033
ATOM    928  CB  TRP B 125      18.454  23.358  26.546
ATOM    929  CG  TRP B 125      17.866  23.711  25.204
ATOM    930  CD2 TRP B 125      18.586  23.583  23.971
ATOM    931  CD1 TRP B 125      16.631  24.193  24.885
ATOM    932  NE1 TRP B 125      16.536  24.372  23.524
ATOM    933  CE2 TRP B 125      17.734  24.000  22.948
ATOM    934  CE3 TRP B 125      19.855  23.153  23.710
ATOM    935  CZ2 TRP B 125      18.141  23.995  21.646
ATOM    936  CZ3 TRP B 125      20.263  23.146  22.395
ATOM    937  CH2 TRP B 125      19.421  23.559  21.382
ATOM    938  C   TRP B 125      19.067  21.703  28.201
ATOM    939  O   TRP B 125      18.677  21.861  29.356
ATOM    940  N   ALA B 126      20.329  21.322  27.912
ATOM    941  CA  ALA B 126      21.285  21.088  28.951
ATOM    942  CB  ALA B 126      21.556  19.598  29.205
ATOM    943  C   ALA B 126      22.565  21.710  28.504
ATOM    944  O   ALA B 126      22.816  21.833  27.305
ATOM    945  N   GLY B 127      23.409  22.134  29.466
ATOM    946  CA  GLY B 127      24.647  22.739  29.085
ATOM    947  C   GLY B 127      25.625  22.583  30.202
ATOM    948  O   GLY B 127      25.289  22.694  31.381
ATOM    949  N   PHE B 128      26.888  22.349  29.815
ATOM    950  CA  PHE B 128      28.012  22.148  30.677
ATOM    951  CB  PHE B 128      28.971  21.145  30.003
ATOM    952  CG  PHE B 128      30.199  20.837  30.789
ATOM    953  CD1 PHE B 128      31.153  21.804  31.014
ATOM    954  CD2 PHE B 128      30.395  19.577  31.305
ATOM    955  CE1 PHE B 128      32.287  21.512  31.738
ATOM    956  CE2 PHE B 128      31.527  19.281  32.023
ATOM    957  CZ  PHE B 128      32.478  20.246  32.239
ATOM    958  C   PHE B 128      28.732  23.458  30.696
ATOM    959  O   PHE B 128      29.304  23.856  29.681
ATOM    960  N   SER B 129      28.738  24.192  31.827
ATOM    961  CA  SER B 129      29.500  25.402  31.732
ATOM    962  CB  SER B 129      29.337  26.396  32.896
ATOM    963  OG  SER B 129      30.133  27.550  32.671
ATOM    964  C   SER B 129      30.910  24.949  31.718
ATOM    965  O   SER B 129      31.310  24.106  32.509
ATOM    966  N   GLY B 130      31.729  25.508  30.828
ATOM    967  CA  GLY B 130      33.075  25.043  30.744
ATOM    968  C   GLY B 130      33.201  24.409  29.404
ATOM    969  O   GLY B 130      34.183  24.632  28.699
ATOM    970  N   GLU B 131      32.210  23.585  29.015
ATOM    971  CA  GLU B 131      32.246  23.094  27.673
ATOM    972  CB  GLU B 131      31.155  22.054  27.366
ATOM    973  CG  GLU B 131      31.370  20.704  28.051
ATOM    974  CD  GLU B 131      30.215  19.797  27.652
ATOM    975  OE1 GLU B 131      29.137  20.333  27.275
ATOM    976  OE2 GLU B 131      30.397  18.552  27.720
ATOM    977  C   GLU B 131      31.974  24.289  26.826
ATOM    978  O   GLU B 131      32.649  24.536  25.830
ATOM    979  N   LYS B 132      30.967  25.083  27.239
ATOM    980  CA  LYS B 132      30.614  26.272  26.523
ATOM    981  CB  LYS B 132      29.616  26.050  25.378
ATOM    982  CG  LYS B 132      30.200  25.275  24.195
ATOM    983  CD  LYS B 132      29.147  24.844  23.173
ATOM    984  CE  LYS B 132      28.612  26.006  22.333
ATOM    985  NZ  LYS B 132      27.730  26.864  23.156
ATOM    986  C   LYS B 132      29.955  27.182  27.501
ATOM    987  O   LYS B 132      29.586  26.780  28.601
ATOM    988  N   PRO B 133      29.814  28.417  27.129
ATOM    989  CA  PRO B 133      29.191  29.323  28.045
ATOM    990  CD  PRO B 133      30.844  29.072  26.335
ATOM    991  CB  PRO B 133      29.552  30.725  27.557
ATOM    992  CG  PRO B 133      30.906  30.519  26.853
ATOM    993  C   PRO B 133      27.720  29.069  28.191
ATOM    994  O   PRO B 133      27.052  28.772  27.201
ATOM    995  N   PRO B 134      27.224  29.199  29.392
ATOM    996  CA  PRO B 134      25.823  29.073  29.725
ATOM    997  CD  PRO B 134      28.063  29.393  30.560
ATOM    998  CB  PRO B 134      25.769  29.050  31.252
ATOM    999  CG  PRO B 134      27.075  29.742  31.684
ATOM   1000  C   PRO B 134      25.189  30.315  29.148
ATOM   1001  O   PRO B 134      25.967  31.129  28.673
ATOM   1002  N   VAL B 135      23.841  30.527  29.164
ATOM   1003  CA  VAL B 135      23.327  31.654  28.385
ATOM   1004  CB  VAL B 135      23.229  31.282  26.921
ATOM   1005  CG1 VAL B 135      24.605  30.960  26.321
ATOM   1006  CG2 VAL B 135      22.203  30.143  26.793
ATOM   1007  C   VAL B 135      21.882  32.092  28.736
ATOM   1008  O   VAL B 135      21.301  31.515  29.647
ATOM   1009  N   PRO B 136      21.262  33.061  27.986
ATOM   1010  CA  PRO B 136      19.984  33.720  28.341
ATOM   1011  CD  PRO B 136      22.105  34.026  27.279
ATOM   1012  CB  PRO B 136      19.866  34.942  27.436
ATOM   1013  CG  PRO B 136      21.324  35.343  27.188
ATOM   1014  C   PRO B 136      18.637  33.084  28.559
ATOM   1015  O   PRO B 136      18.071  32.519  27.632
ATOM   1016  N   LEU B 137      18.050  33.283  29.765
ATOM   1017  CA  LEU B 137      16.737  32.794  30.100
ATOM   1018  CB  LEU B 137      16.728  31.522  30.966
ATOM   1019  CG  LEU B 137      17.304  30.285  30.255
ATOM   1020  CD2 LEU B 137      18.786  30.470  29.918
ATOM   1021  CD1 LEU B 137      16.459  29.891  29.034
ATOM   1022  C   LEU B 137      16.014  33.865  30.867
ATOM   1023  O   LEU B 137      16.599  34.868  31.272
ATOM   1024  N   ASP B 138      14.689  33.695  31.045
ATOM   1025  CA  ASP B 138      13.886  34.658  31.746
ATOM   1026  CB  ASP B 138      12.382  34.428  31.572
ATOM   1027  CG  ASP B 138      12.021  34.764  30.131
ATOM   1028  OD1 ASP B 138      12.964  34.943  29.313
ATOM   1029  OD2 ASP B 138      10.802  34.852  29.830
ATOM   1030  C   ASP B 138      14.207  34.675  33.215
ATOM   1031  O   ASP B 138      14.148  35.729  33.846
ATOM   1032  N   ALA B 139      14.522  33.511  33.820
ATOM   1033  CA  ALA B 139      14.810  33.511  35.231
ATOM   1034  CB  ALA B 139      13.556  33.344  36.108
ATOM   1035  C   ALA B 139      15.718  32.356  35.526
ATOM   1036  O   ALA B 139      15.866  31.444  34.714
ATOM   1037  N   ALA B 140      16.377  32.380  36.703
ATOM   1038  CA  ALA B 140      17.247  31.293  37.053
ATOM   1039  CB  ALA B 140      18.742  31.624  36.894
ATOM   1040  C   ALA B 140      17.023  30.948  38.490
ATOM   1041  O   ALA B 140      16.687  31.807  39.304
ATOM   1042  N   ILE B 141      17.182  29.652  38.825
ATOM   1043  CA  ILE B 141      17.058  29.211  40.183
ATOM   1044  CB  ILE B 141      15.985  28.179  40.373
ATOM   1045  CG2 ILE B 141      16.051  27.691  41.830
ATOM   1046  CG1 ILE B 141      14.616  28.759  39.978
ATOM   1047  CD1 ILE B 141      14.208  29.969  40.816
ATOM   1048  C   ILE B 141      18.369  28.576  40.524
ATOM   1049  O   ILE B 141      18.791  27.620  39.873
ATOM   1050  N   ILE B 142      19.049  29.090  41.569
ATOM   1051  CA  ILE B 142      20.343  28.573  41.909
ATOM   1052  CB  ILE B 142      21.337  29.664  42.222
ATOM   1053  CG2 ILE B 142      20.747  30.593  43.301
ATOM   1054  CG1 ILE B 142      22.709  29.057  42.567
ATOM   1055  CD1 ILE B 142      23.393  28.379  41.380
ATOM   1056  C   ILE B 142      20.222  27.669  43.102
ATOM   1057  O   ILE B 142      20.076  28.112  44.241
ATOM   1058  N   PHE B 143      20.246  26.348  42.836
ATOM   1059  CA  PHE B 143      20.181  25.329  43.848
ATOM   1060  CB  PHE B 143      19.901  23.928  43.280
ATOM   1061  CG  PHE B 143      20.200  22.956  44.370
ATOM   1062  CD1 PHE B 143      19.566  23.048  45.584
ATOM   1063  CD2 PHE B 143      21.095  21.932  44.167
ATOM   1064  CE1 PHE B 143      19.837  22.144  46.586
ATOM   1065  CE2 PHE B 143      21.368  21.027  45.165
ATOM   1066  CZ  PHE B 143      20.740  21.129  46.382
ATOM   1067  C   PHE B 143      21.445  25.243  44.634
ATOM   1068  O   PHE B 143      21.411  25.062  45.850
ATOM   1069  N   ALA B 144      22.609  25.309  43.962
ATOM   1070  CA  ALA B 144      23.816  25.246  44.727
ATOM   1071  CB  ALA B 144      24.808  24.188  44.212
ATOM   1072  C   ALA B 144      24.461  26.581  44.588
ATOM   1073  O   ALA B 144      25.103  26.883  43.585
ATOM   1074  N   PRO B 145      24.310  27.397  45.588
ATOM   1075  CA  PRO B 145      24.904  28.693  45.485
ATOM   1076  CD  PRO B 145      23.044  27.443  46.298
ATOM   1077  CB  PRO B 145      24.194  29.580  46.502
ATOM   1078  CG  PRO B 145      22.804  28.932  46.603
ATOM   1079  C   PRO B 145      26.379  28.612  45.643
ATOM   1080  O   PRO B 145      26.847  27.892  46.523
ATOM   1081  N   ALA B 146      27.113  29.360  44.799
ATOM   1082  CA  ALA B 146      28.540  29.400  44.826
ATOM   1083  CB  ALA B 146      29.209  28.204  44.127
ATOM   1084  C   ALA B 146      28.904  30.623  44.054
ATOM   1085  O   ALA B 146      28.080  31.168  43.320
ATOM   1086  N   GLY B 147      30.150  31.094  44.216
ATOM   1087  CA  GLY B 147      30.574  32.284  43.546
ATOM   1088  C   GLY B 147      30.568  32.071  42.065
ATOM   1089  O   GLY B 147      30.223  32.969  41.311
ATOM   1090  N   GLU B 148      31.005  30.907  41.568
ATOM   1091  CA  GLU B 148      31.014  30.773  40.137
ATOM   1092  CB  GLU B 148      31.773  29.517  39.687
ATOM   1093  CG  GLU B 148      33.263  29.589  40.026
ATOM   1094  CD  GLU B 148      33.918  28.283  39.610
ATOM   1095  OE1 GLU B 148      33.310  27.209  39.864
ATOM   1096  OE2 GLU B 148      35.038  28.342  39.036
ATOM   1097  C   GLU B 148      29.617  30.678  39.607
ATOM   1098  O   GLU B 148      29.265  31.322  38.620
ATOM   1099  N   LEU B 149      28.769  29.878  40.276
ATOM   1100  CA  LEU B 149      27.457  29.599  39.763
ATOM   1101  CB  LEU B 149      26.706  28.557  40.612
ATOM   1102  CG  LEU B 149      27.389  27.173  40.616
ATOM   1103  CD2 LEU B 149      27.725  26.712  39.190
ATOM   1104  CD1 LEU B 149      26.568  26.134  41.395
ATOM   1105  C   LEU B 149      26.620  30.837  39.708
ATOM   1106  O   LEU B 149      25.933  31.079  38.716
ATOM   1107  N   VAL B 150      26.644  31.661  40.774
ATOM   1108  CA  VAL B 150      25.787  32.814  40.768
ATOM   1109  CB  VAL B 150      25.732  33.535  42.093
ATOM   1110  CG1 VAL B 150      24.869  34.798  41.925
ATOM   1111  CG2 VAL B 150      25.198  32.568  43.167
ATOM   1112  C   VAL B 150      26.200  33.750  39.661
ATOM   1113  O   VAL B 150      25.339  34.211  38.919
ATOM   1114  N   PRO B 151      27.455  34.077  39.500
ATOM   1115  CA  PRO B 151      27.788  34.871  38.353
ATOM   1116  CD  PRO B 151      28.127  34.649  40.650
ATOM   1117  CB  PRO B 151      29.217  35.345  38.584
ATOM   1118  CG  PRO B 151      29.214  35.596  40.101
ATOM   1119  C   PRO B 151      27.477  34.273  37.019
ATOM   1120  O   PRO B 151      27.217  35.029  36.085
ATOM   1121  N   MET B 152      27.527  32.944  36.848
ATOM   1122  CA  MET B 152      27.084  32.491  35.563
ATOM   1123  CB  MET B 152      27.304  30.989  35.325
ATOM   1124  CG  MET B 152      28.696  30.654  34.780
ATOM   1125  SD  MET B 152      30.092  30.951  35.903
ATOM   1126  CE  MET B 152      30.115  32.746  35.627
ATOM   1127  C   MET B 152      25.624  32.786  35.452
ATOM   1128  O   MET B 152      25.164  33.295  34.433
ATOM   1129  N   ALA B 153      24.860  32.507  36.528
ATOM   1130  CA  ALA B 153      23.435  32.693  36.505
ATOM   1131  CB  ALA B 153      22.750  32.231  37.804
ATOM   1132  C   ALA B 153      23.094  34.143  36.318
ATOM   1133  O   ALA B 153      22.192  34.473  35.551
ATOM   1134  N   LEU B 154      23.789  35.073  36.996
ATOM   1135  CA  LEU B 154      23.382  36.441  36.850
ATOM   1136  CB  LEU B 154      24.014  37.427  37.869
ATOM   1137  CG  LEU B 154      25.222  38.296  37.448
ATOM   1138  CD2 LEU B 154      24.840  39.376  36.421
ATOM   1139  CD1 LEU B 154      26.436  37.460  37.043
ATOM   1140  C   LEU B 154      23.640  36.875  35.438
ATOM   1141  O   LEU B 154      22.932  37.732  34.916
ATOM   1142  N   ASP B 155      24.692  36.322  34.802
ATOM   1143  CA  ASP B 155      25.035  36.654  33.444
ATOM   1144  CB  ASP B 155      26.386  36.079  32.987
ATOM   1145  CG  ASP B 155      27.491  36.918  33.611
ATOM   1146  OD1 ASP B 155      27.171  37.829  34.420
ATOM   1147  OD2 ASP B 155      28.679  36.657  33.283
ATOM   1148  C   ASP B 155      24.013  36.163  32.475
ATOM   1149  O   ASP B 155      23.760  36.826  31.472
ATOM   1150  N   VAL B 156      23.446  34.969  32.730
ATOM   1151  CA  VAL B 156      22.518  34.316  31.843
ATOM   1152  CB  VAL B 156      22.313  32.856  32.146
ATOM   1153  CG1 VAL B 156      23.662  32.133  32.000
ATOM   1154  CG2 VAL B 156      21.658  32.704  33.527
ATOM   1155  C   VAL B 156      21.156  34.968  31.803
ATOM   1156  O   VAL B 156      20.450  34.869  30.808
ATOM   1157  N   VAL B 157      20.682  35.624  32.870
ATOM   1158  CA  VAL B 157      19.317  36.083  32.792
ATOM   1159  CB  VAL B 157      18.756  36.494  34.123
ATOM   1160  CG1 VAL B 157      17.327  37.020  33.909
ATOM   1161  CG2 VAL B 157      18.843  35.294  35.079
ATOM   1162  C   VAL B 157      19.176  37.256  31.866
ATOM   1163  O   VAL B 157      20.061  38.104  31.756
ATOM   1164  N   ARG B 158      18.019  37.314  31.172
ATOM   1165  CA  ARG B 158      17.688  38.380  30.270
ATOM   1166  CB  ARG B 158      16.416  38.092  29.458
ATOM   1167  CG  ARG B 158      16.143  39.096  28.341
ATOM   1168  CD  ARG B 158      14.697  39.056  27.840
ATOM   1169  NE  ARG B 158      14.391  37.659  27.422
ATOM   1170  CZ  ARG B 158      13.121  37.334  27.044
ATOM   1171  NH1 ARG B 158      12.153  38.296  27.025
ATOM   1172  NH2 ARG B 158      12.817  36.052  26.688
ATOM   1173  C   ARG B 158      17.403  39.569  31.130
ATOM   1174  O   ARG B 158      17.151  39.425  32.325
ATOM   1175  N   LYS B 159      17.454  40.782  30.549
ATOM   1176  CA  LYS B 159      17.224  41.963  31.328
ATOM   1177  CB  LYS B 159      17.351  43.260  30.508
ATOM   1178  CG  LYS B 159      16.420  43.307  29.295
ATOM   1179  CD  LYS B 159      16.402  44.659  28.578
ATOM   1180  CE  LYS B 159      15.486  45.699  29.228
ATOM   1181  NZ  LYS B 159      14.067  45.361  28.972
ATOM   1182  C   LYS B 159      15.842  41.885  31.890
ATOM   1183  O   LYS B 159      14.929  41.358  31.258
ATOM   1184  N   GLY B 160      15.681  42.370  33.138
ATOM   1185  CA  GLY B 160      14.402  42.400  33.786
ATOM   1186  C   GLY B 160      14.095  41.038  34.324
ATOM   1187  O   GLY B 160      12.994  40.797  34.820
ATOM   1188  N   GLY B 161      15.066  40.108  34.253
ATOM   1189  CA  GLY B 161      14.825  38.769  34.714
ATOM   1190  C   GLY B 161      15.056  38.688  36.191
ATOM   1191  O   GLY B 161      15.457  39.660  36.828
ATOM   1192  N   THR B 162      14.808  37.493  36.774
ATOM   1193  CA  THR B 162      14.978  37.338  38.194
ATOM   1194  CB  THR B 162      13.682  37.100  38.915
ATOM   1195  OG1 THR B 162      13.885  37.123  40.319
ATOM   1196  CG2 THR B 162      13.122  35.738  38.476
ATOM   1197  C   THR B 162      15.881  36.176  38.485
ATOM   1198  O   THR B 162      15.808  35.130  37.841
ATOM   1199  N   VAL B 163      16.781  36.350  39.478
ATOM   1200  CA  VAL B 163      17.650  35.281  39.886
ATOM   1201  CB  VAL B 163      19.099  35.673  39.947
ATOM   1202  CG1 VAL B 163      19.902  34.503  40.543
ATOM   1203  CG2 VAL B 163      19.548  36.091  38.538
ATOM   1204  C   VAL B 163      17.237  34.903  41.273
ATOM   1205  O   VAL B 163      17.350  35.697  42.204
ATOM   1206  N   VAL B 164      16.758  33.655  41.449
ATOM   1207  CA  VAL B 164      16.297  33.244  42.745
ATOM   1208  CB  VAL B 164      15.004  32.481  42.706
ATOM   1209  CG1 VAL B 164      14.681  31.966  44.121
ATOM   1210  CG2 VAL B 164      13.921  33.399  42.110
ATOM   1211  C   VAL B 164      17.324  32.355  43.368
ATOM   1212  O   VAL B 164      17.783  31.387  42.764
ATOM   1213  N   CYS B 165      17.702  32.670  44.624
ATOM   1214  CA  CYS B 165      18.708  31.902  45.300
ATOM   1215  CB  CYS B 165      19.782  32.782  45.959
ATOM   1216  SG  CYS B 165      19.057  34.021  47.072
ATOM   1217  C   CYS B 165      18.071  31.061  46.368
ATOM   1218  O   CYS B 165      17.410  31.568  47.273
ATOM   1219  N   GLY B 166      18.145  29.727  46.182
ATOM   1220  CA  GLY B 166      17.704  28.720  47.111
ATOM   1221  C   GLY B 166      18.696  28.385  48.194
ATOM   1222  O   GLY B 166      18.314  28.108  49.330
ATOM   1223  N   GLY B 167      20.002  28.353  47.855
ATOM   1224  CA  GLY B 167      20.995  27.815  48.752
ATOM   1225  C   GLY B 167      21.336  28.769  49.850
ATOM   1226  O   GLY B 167      21.024  29.957  49.789
ATOM   1227  N   ILE B 168      21.992  28.239  50.909
ATOM   1228  CA  ILE B 168      22.421  29.066  51.999
ATOM   1229  CB  ILE B 168      21.791  28.697  53.321
ATOM   1230  CG2 ILE B 168      20.290  29.019  53.236
ATOM   1231  CG1 ILE B 168      22.101  27.242  53.721
ATOM   1232  CD1 ILE B 168      21.771  26.928  55.179
ATOM   1233  C   ILE B 168      23.918  28.978  52.117
ATOM   1234  O   ILE B 168      24.473  27.994  52.603
ATOM   1235  N   ASP B 169      24.620  30.036  51.669
ATOM   1236  CA  ASP B 169      26.050  30.059  51.761
ATOM   1237  CB  ASP B 169      26.776  30.302  50.427
ATOM   1238  CG  ASP B 169      26.763  29.013  49.627
ATOM   1239  OD1 ASP B 169      25.900  28.140  49.911
ATOM   1240  OD2 ASP B 169      27.627  28.884  48.720
ATOM   1241  C   ASP B 169      26.441  31.183  52.662
ATOM   1242  O   ASP B 169      25.822  32.245  52.663
ATOM   1243  N   MET B 170      27.473  30.935  53.484
ATOM   1244  CA  MET B 170      28.026  31.879  54.409
ATOM   1245  CB  MET B 170      29.014  31.212  55.374
ATOM   1246  CG  MET B 170      30.159  30.498  54.655
ATOM   1247  SD  MET B 170      31.146  29.423  55.734
ATOM   1248  CE  MET B 170      29.771  28.284  56.072
ATOM   1249  C   MET B 170      28.732  32.985  53.678
ATOM   1250  O   MET B 170      28.732  34.127  54.134
ATOM   1251  N   SER B 171      29.356  32.670  52.523
ATOM   1252  CA  SER B 171      30.163  33.620  51.798
ATOM   1253  CB  SER B 171      30.948  32.997  50.631
ATOM   1254  OG  SER B 171      30.052  32.558  49.622
ATOM   1255  C   SER B 171      29.314  34.713  51.227
ATOM   1256  O   SER B 171      28.086  34.646  51.247
ATOM   1257  N   ASP B 172      29.980  35.780  50.729
ATOM   1258  CA  ASP B 172      29.311  36.916  50.159
ATOM   1259  CB  ASP B 172      29.896  38.264  50.617
ATOM   1260  CG  ASP B 172      31.342  38.360  50.145
ATOM   1261  OD1 ASP B 172      31.970  37.291  49.924
ATOM   1262  OD2 ASP B 172      31.839  39.508  50.004
ATOM   1263  C   ASP B 172      29.444  36.856  48.668
ATOM   1264  O   ASP B 172      30.439  36.367  48.133
ATOM   1265  N   ILE B 173      28.410  37.340  47.950
ATOM   1266  CA  ILE B 173      28.450  37.350  46.518
ATOM   1267  CB  ILE B 173      27.307  36.616  45.873
ATOM   1268  CG2 ILE B 173      27.414  35.140  46.287
ATOM   1269  CG1 ILE B 173      25.954  37.259  46.225
ATOM   1270  CD1 ILE B 173      25.600  37.195  47.710
ATOM   1271  C   ILE B 173      28.397  38.776  46.075
ATOM   1272  O   ILE B 173      27.506  39.537  46.451
ATOM   1273  N   PRO B 174      29.367  39.162  45.296
ATOM   1274  CA  PRO B 174      29.389  40.508  44.805
ATOM   1275  CD  PRO B 174      30.705  38.620  45.435
ATOM   1276  CB  PRO B 174      30.838  40.804  44.404
ATOM   1277  CG  PRO B 174      31.538  39.432  44.432
ATOM   1278  C   PRO B 174      28.412  40.649  43.691
ATOM   1279  O   PRO B 174      28.167  39.668  42.991
ATOM   1280  N   SER B 175      27.839  41.852  43.510
ATOM   1281  CA  SER B 175      26.926  42.066  42.428
ATOM   1282  CB  SER B 175      25.465  42.222  42.879
ATOM   1283  OG  SER B 175      24.628  42.432  41.753
ATOM   1284  C   SER B 175      27.334  43.346  41.777
ATOM   1285  O   SER B 175      27.793  44.264  42.453
ATOM   1286  N   MET B 176      27.186  43.439  40.441
ATOM   1287  CA  MET B 176      27.582  44.637  39.752
ATOM   1288  CB  MET B 176      27.772  44.411  38.244
ATOM   1289  CG  MET B 176      28.933  43.479  37.896
ATOM   1290  SD  MET B 176      30.580  44.233  38.021
ATOM   1291  CE  MET B 176      30.483  45.081  36.418
ATOM   1292  C   MET B 176      26.487  45.647  39.898
ATOM   1293  O   MET B 176      25.337  45.375  39.556
ATOM   1294  N   PRO B 177      26.802  46.799  40.431
ATOM   1295  CA  PRO B 177      25.809  47.833  40.538
ATOM   1296  CD  PRO B 177      27.813  46.906  41.471
ATOM   1297  CB  PRO B 177      26.383  48.872  41.499
ATOM   1298  CG  PRO B 177      27.349  48.058  42.379
ATOM   1299  C   PRO B 177      25.477  48.393  39.196
ATOM   1300  O   PRO B 177      24.330  48.778  38.967
ATOM   1301  N   TYR B 178      26.468  48.444  38.292
ATOM   1302  CA  TYR B 178      26.276  49.024  36.998
ATOM   1303  CB  TYR B 178      27.593  48.978  36.197
ATOM   1304  CG  TYR B 178      27.435  49.562  34.834
ATOM   1305  CD1 TYR B 178      27.434  50.928  34.655
ATOM   1306  CD2 TYR B 178      27.327  48.746  33.733
ATOM   1307  CE1 TYR B 178      27.305  51.472  33.397
ATOM   1308  CE2 TYR B 178      27.197  49.283  32.474
ATOM   1309  CZ  TYR B 178      27.186  50.646  32.305
ATOM   1310  OH  TYR B 178      27.055  51.191  31.010
ATOM   1311  C   TYR B 178      25.262  48.193  36.289
ATOM   1312  O   TYR B 178      24.293  48.701  35.729
ATOM   1313  N   ARG B 179      25.471  46.869  36.335
ATOM   1314  CA  ARG B 179      24.647  45.923  35.650
ATOM   1315  CB  ARG B 179      25.167  44.488  35.824
ATOM   1316  CG  ARG B 179      26.526  44.223  35.183
ATOM   1317  CD  ARG B 179      26.456  43.219  34.033
ATOM   1318  NE  ARG B 179      27.834  43.053  33.494
ATOM   1319  CZ  ARG B 179      28.243  43.849  32.463
ATOM   1320  NH1 ARG B 179      27.379  44.763  31.933
ATOM   1321  NH2 ARG B 179      29.509  43.739  31.967
ATOM   1322  C   ARG B 179      23.257  45.898  36.205
ATOM   1323  O   ARG B 179      22.284  45.958  35.454
ATOM   1324  N   LEU B 180      23.129  45.837  37.544
ATOM   1325  CA  LEU B 180      21.846  45.605  38.148
ATOM   1326  CB  LEU B 180      21.897  45.546  39.684
ATOM   1327  CG  LEU B 180      22.659  44.340  40.256
ATOM   1328  CD2 LEU B 180      22.143  43.016  39.666
ATOM   1329  CD1 LEU B 180      22.627  44.365  41.793
ATOM   1330  C   LEU B 180      20.882  46.690  37.812
ATOM   1331  O   LEU B 180      19.744  46.406  37.442
ATOM   1332  N   LEU B 181      21.301  47.959  37.941
ATOM   1333  CA  LEU B 181      20.386  49.041  37.714
ATOM   1334  CB  LEU B 181      20.983  50.411  38.076
ATOM   1335  CG  LEU B 181      21.167  50.642  39.590
ATOM   1336  CD2 LEU B 181      22.024  49.545  40.235
ATOM   1337  CD1 LEU B 181      19.815  50.803  40.299
ATOM   1338  C   LEU B 181      19.961  49.104  36.282
ATOM   1339  O   LEU B 181      18.769  49.201  35.988
ATOM   1340  N   TRP B 182      20.923  49.029  35.346
ATOM   1341  CA  TRP B 182      20.595  49.177  33.957
ATOM   1342  CB  TRP B 182      21.850  49.200  33.067
ATOM   1343  CG  TRP B 182      21.587  49.395  31.593
ATOM   1344  CD2 TRP B 182      22.418  50.214  30.755
ATOM   1345  CD1 TRP B 182      20.584  48.922  30.798
ATOM   1346  NE1 TRP B 182      20.741  49.391  29.514
ATOM   1347  CE2 TRP B 182      21.865  50.191  29.474
ATOM   1348  CE3 TRP B 182      23.544  50.936  31.034
ATOM   1349  CZ2 TRP B 182      22.434  50.890  28.448
ATOM   1350  CZ3 TRP B 182      24.119  51.633  29.994
ATOM   1351  CH2 TRP B 182      23.575  51.610  28.727
ATOM   1352  C   TRP B 182      19.713  48.042  33.527
ATOM   1353  O   TRP B 182      18.680  48.249  32.893
ATOM   1354  N   GLY B 183      20.116  46.812  33.892
ATOM   1355  CA  GLY B 183      19.468  45.573  33.551
ATOM   1356  C   GLY B 183      18.120  45.438  34.201
ATOM   1357  O   GLY B 183      17.245  44.750  33.676
ATOM   1358  N   GLU B 184      17.928  46.044  35.389
ATOM   1359  CA  GLU B 184      16.690  45.905  36.105
ATOM   1360  CB  GLU B 184      15.466  46.385  35.300
ATOM   1361  CG  GLU B 184      15.482  47.892  35.023
ATOM   1362  CD  GLU B 184      15.347  48.628  36.350
ATOM   1363  OE1 GLU B 184      14.396  48.300  37.109
ATOM   1364  OE2 GLU B 184      16.187  49.528  36.618
ATOM   1365  C   GLU B 184      16.508  44.466  36.472
ATOM   1366  O   GLU B 184      15.398  43.935  36.459
ATOM   1367  N   ARG B 185      17.626  43.804  36.827
ATOM   1368  CA  ARG B 185      17.609  42.430  37.235
ATOM   1369  CB  ARG B 185      18.970  41.737  37.071
ATOM   1370  CG  ARG B 185      19.441  41.736  35.616
ATOM   1371  CD  ARG B 185      20.807  41.088  35.384
ATOM   1372  NE  ARG B 185      21.086  41.188  33.923
ATOM   1373  CZ  ARG B 185      22.332  40.923  33.431
ATOM   1374  NH1 ARG B 185      23.328  40.517  34.269
ATOM   1375  NH2 ARG B 185      22.584  41.069  32.097
ATOM   1376  C   ARG B 185      17.230  42.376  38.682
ATOM   1377  O   ARG B 185      17.474  43.318  39.437
ATOM   1378  N   ARG B 186      16.597  41.259  39.098
ATOM   1379  CA  ARG B 186      16.188  41.124  40.468
ATOM   1380  CB  ARG B 186      14.684  40.869  40.665
ATOM   1381  CG  ARG B 186      13.780  42.029  40.253
ATOM   1382  CD  ARG B 186      12.419  41.987  40.955
ATOM   1383  NE  ARG B 186      12.563  42.791  42.202
ATOM   1384  CZ  ARG B 186      12.228  44.114  42.190
ATOM   1385  NH1 ARG B 186      11.628  44.648  41.085
ATOM   1386  NH2 ARG B 186      12.479  44.899  43.279
ATOM   1387  C   ARG B 186      16.871  39.942  41.077
ATOM   1388  O   ARG B 186      17.041  38.903  40.436
ATOM   1389  N   VAL B 187      17.291  40.089  42.349
ATOM   1390  CA  VAL B 187      17.884  38.998  43.069
ATOM   1391  CB  VAL B 187      19.214  39.335  43.685
ATOM   1392  CG1 VAL B 187      19.701  38.122  44.497
ATOM   1393  CG2 VAL B 187      20.184  39.776  42.575
ATOM   1394  C   VAL B 187      16.951  38.714  44.203
ATOM   1395  O   VAL B 187      16.717  39.581  45.043
ATOM   1396  N   VAL B 188      16.383  37.493  44.263
ATOM   1397  CA  VAL B 188      15.474  37.236  45.341
ATOM   1398  CB  VAL B 188      14.045  37.107  44.907
ATOM   1399  CG1 VAL B 188      13.597  38.459  44.327
ATOM   1400  CG2 VAL B 188      13.932  35.932  43.920
ATOM   1401  C   VAL B 188      15.867  35.964  46.018
ATOM   1402  O   VAL B 188      16.370  35.036  45.384
ATOM   1403  N   SER B 189      15.644  35.900  47.346
ATOM   1404  CA  SER B 189      15.986  34.711  48.069
ATOM   1405  CB  SER B 189      16.801  34.962  49.347
ATOM   1406  OG  SER B 189      17.089  33.724  49.983
ATOM   1407  C   SER B 189      14.705  34.073  48.480
ATOM   1408  O   SER B 189      13.749  34.756  48.846
ATOM   1409  N   VAL B 190      14.643  32.730  48.406
ATOM   1410  CA  VAL B 190      13.428  32.070  48.776
ATOM   1411  CB  VAL B 190      12.588  31.745  47.585
ATOM   1412  CG1 VAL B 190      12.129  33.073  46.973
ATOM   1413  CG2 VAL B 190      13.437  30.924  46.596
ATOM   1414  C   VAL B 190      13.763  30.784  49.449
ATOM   1415  O   VAL B 190      14.699  30.092  49.055
ATOM   1416  N   ALA B 191      12.997  30.434  50.502
ATOM   1417  CA  ALA B 191      13.247  29.198  51.181
ATOM   1418  CB  ALA B 191      14.061  29.372  52.475
ATOM   1419  C   ALA B 191      11.921  28.625  51.573
ATOM   1420  O   ALA B 191      11.022  29.363  51.973
ATOM   1421  N   ASN B 192      11.794  27.281  51.470
ATOM   1422  CA  ASN B 192      10.609  26.541  51.834
ATOM   1423  CB  ASN B 192      10.449  26.324  53.351
ATOM   1424  CG  ASN B 192      11.516  25.355  53.834
ATOM   1425  OD1 ASN B 192      11.961  24.479  53.094
ATOM   1426  ND2 ASN B 192      11.938  25.508  55.119
ATOM   1427  C   ASN B 192       9.386  27.272  51.366
ATOM   1428  O   ASN B 192       9.439  28.035  50.405
ATOM   1429  N   LEU B 193       8.226  26.958  51.977
ATOM   1430  CA  LEU B 193       7.014  27.709  51.791
ATOM   1431  CB  LEU B 193       6.371  27.827  50.402
ATOM   1432  CG  LEU B 193       6.911  29.068  49.671
ATOM   1433  CD2 LEU B 193       7.186  30.209  50.659
ATOM   1434  CD1 LEU B 193       5.987  29.496  48.521
ATOM   1435  C   LEU B 193       5.974  27.344  52.802
ATOM   1436  O   LEU B 193       6.182  26.509  53.681
ATOM   1437  N   THR B 194       4.812  28.016  52.695
ATOM   1438  CA  THR B 194       3.738  27.858  53.633
ATOM   1439  CB  THR B 194       2.688  28.922  53.517
ATOM   1440  OG1 THR B 194       2.092  28.878  52.230
ATOM   1441  CG2 THR B 194       3.346  30.292  53.756
ATOM   1442  C   THR B 194       3.060  26.539  53.423
ATOM   1443  O   THR B 194       3.431  25.763  52.546
ATOM   1444  N   ARG B 195       2.049  26.246  54.268
ATOM   1445  CA  ARG B 195       1.324  25.011  54.188
ATOM   1446  CB  ARG B 195       0.300  24.824  55.328
ATOM   1447  CG  ARG B 195       0.966  24.708  56.703
ATOM   1448  CD  ARG B 195       0.137  23.960  57.751
ATOM   1449  NE  ARG B 195      -0.999  24.821  58.187
ATOM   1450  CZ  ARG B 195      -0.852  25.627  59.278
ATOM   1451  NH1 ARG B 195       0.360  25.711  59.898
ATOM   1452  NH2 ARG B 195      -1.917  26.326  59.764
ATOM   1453  C   ARG B 195       0.610  24.957  52.876
ATOM   1454  O   ARG B 195       0.506  23.895  52.267
ATOM   1455  N   SER B 196       0.092  26.106  52.402
ATOM   1456  CA  SER B 196      -0.612  26.108  51.154
ATOM   1457  CB  SER B 196      -1.177  27.491  50.786
ATOM   1458  OG  SER B 196      -1.859  27.420  49.542
ATOM   1459  C   SER B 196       0.326  25.707  50.053
ATOM   1460  O   SER B 196      -0.017  24.907  49.184
ATOM   1461  N   ASP B 197       1.553  26.256  50.075
ATOM   1462  CA  ASP B 197       2.530  26.010  49.054
ATOM   1463  CB  ASP B 197       3.808  26.811  49.319
ATOM   1464  CG  ASP B 197       3.415  28.280  49.266
ATOM   1465  OD1 ASP B 197       2.679  28.667  48.319
ATOM   1466  OD2 ASP B 197       3.847  29.035  50.176
ATOM   1467  C   ASP B 197       2.879  24.556  49.072
ATOM   1468  O   ASP B 197       3.016  23.917  48.028
ATOM   1469  N   GLY B 198       3.029  23.997  50.283
ATOM   1470  CA  GLY B 198       3.409  22.625  50.428
ATOM   1471  C   GLY B 198       2.344  21.749  49.865
ATOM   1472  O   GLY B 198       2.640  20.768  49.185
ATOM   1473  N   ALA B 199       1.072  22.094  50.130
ATOM   1474  CA  ALA B 199      -0.026  21.271  49.720
ATOM   1475  CB  ALA B 199      -1.377  21.880  50.130
ATOM   1476  C   ALA B 199      -0.004  21.164  48.235
ATOM   1477  O   ALA B 199      -0.191  20.086  47.673
ATOM   1478  N   GLU B 200       0.240  22.300  47.563
ATOM   1479  CA  GLU B 200       0.260  22.315  46.136
ATOM   1480  CB  GLU B 200       0.399  23.741  45.577
ATOM   1481  CG  GLU B 200      -0.867  24.567  45.814
ATOM   1482  CD  GLU B 200      -0.593  26.013  45.430
ATOM   1483  OE1 GLU B 200       0.600  26.352  45.198
ATOM   1484  OE2 GLU B 200      -1.573  26.799  45.364
ATOM   1485  C   GLU B 200       1.399  21.470  45.655
ATOM   1486  O   GLU B 200       1.250  20.707  44.703
ATOM   1487  N   PHE B 201       2.566  21.558  46.319
ATOM   1488  CA  PHE B 201       3.717  20.801  45.904
ATOM   1489  CB  PHE B 201       4.994  21.121  46.695
ATOM   1490  CG  PHE B 201       6.106  20.353  46.059
ATOM   1491  CD1 PHE B 201       6.739  20.830  44.936
ATOM   1492  CD2 PHE B 201       6.522  19.152  46.580
ATOM   1493  CE1 PHE B 201       7.763  20.118  44.352
ATOM   1494  CE2 PHE B 201       7.543  18.434  46.006
ATOM   1495  CZ  PHE B 201       8.171  18.918  44.886
ATOM   1496  C   PHE B 201       3.437  19.333  46.061
ATOM   1497  O   PHE B 201       3.865  18.532  45.234
ATOM   1498  N   PHE B 202       2.726  18.942  47.142
ATOM   1499  CA  PHE B 202       2.408  17.565  47.428
ATOM   1500  CB  PHE B 202       1.481  17.344  48.655
ATOM   1501  CG  PHE B 202       2.077  17.675  49.985
ATOM   1502  CD1 PHE B 202       3.041  16.879  50.554
ATOM   1503  CD2 PHE B 202       1.623  18.753  50.711
ATOM   1504  CE1 PHE B 202       3.580  17.171  51.785
ATOM   1505  CE2 PHE B 202       2.154  19.057  51.944
ATOM   1506  CZ  PHE B 202       3.139  18.267  52.483
ATOM   1507  C   PHE B 202       1.560  17.023  46.316
ATOM   1508  O   PHE B 202       1.755  15.893  45.872
ATOM   1509  N   SER B 203       0.578  17.824  45.858
ATOM   1510  CA  SER B 203      -0.391  17.391  44.892
ATOM   1511  CB  SER B 203      -1.401  18.494  44.528
ATOM   1512  OG  SER B 203      -2.330  18.005  43.572
ATOM   1513  C   SER B 203       0.285  16.989  43.626
ATOM   1514  O   SER B 203      -0.117  16.021  42.983
ATOM   1515  N   ILE B 204       1.343  17.716  43.232
ATOM   1516  CA  ILE B 204       2.009  17.401  42.005
ATOM   1517  CB  ILE B 204       3.156  18.323  41.700
ATOM   1518  CG2 ILE B 204       3.937  17.748  40.505
ATOM   1519  CG1 ILE B 204       2.647  19.758  41.480
ATOM   1520  CD1 ILE B 204       3.766  20.798  41.420
ATOM   1521  C   ILE B 204       2.566  16.016  42.119
ATOM   1522  O   ILE B 204       2.504  15.237  41.168
ATOM   1523  N   GLY B 205       3.144  15.688  43.289
ATOM   1524  CA  GLY B 205       3.750  14.404  43.502
ATOM   1525  C   GLY B 205       2.727  13.309  43.438
ATOM   1526  O   GLY B 205       2.969  12.262  42.838
ATOM   1527  N   LYS B 206       1.550  13.522  44.056
ATOM   1528  CA  LYS B 206       0.538  12.503  44.098
ATOM   1529  CB  LYS B 206      -0.705  12.915  44.904
ATOM   1530  CG  LYS B 206      -1.533  14.017  44.243
ATOM   1531  CD  LYS B 206      -2.909  14.203  44.882
ATOM   1532  CE  LYS B 206      -3.764  12.933  44.865
ATOM   1533  NZ  LYS B 206      -3.990  12.495  43.471
ATOM   1534  C   LYS B 206       0.110  12.226  42.690
ATOM   1535  O   LYS B 206      -0.248  11.102  42.343
ATOM   1536  N   ALA B 207       0.132  13.288  41.863
ATOM   1537  CA  ALA B 207      -0.211  13.329  40.468
ATOM   1538  CB  ALA B 207      -0.156  14.752  39.889
ATOM   1539  C   ALA B 207       0.749  12.482  39.685
ATOM   1540  O   ALA B 207       0.400  11.982  38.616
ATOM   1541  N   ALA B 208       1.984  12.301  40.203
ATOM   1542  CA  ALA B 208       3.045  11.595  39.530
ATOM   1543  CB  ALA B 208       2.575  10.327  38.791
ATOM   1544  C   ALA B 208       3.718  12.494  38.532
ATOM   1545  O   ALA B 208       4.445  12.028  37.655
ATOM   1546  N   GLY B 209       3.473  13.816  38.639
ATOM   1547  CA  GLY B 209       4.151  14.814  37.856
ATOM   1548  C   GLY B 209       5.577  14.907  38.319
ATOM   1549  O   GLY B 209       6.480  15.186  37.529
ATOM   1550  N   VAL B 210       5.803  14.733  39.641
ATOM   1551  CA  VAL B 210       7.124  14.873  40.190
ATOM   1552  CB  VAL B 210       7.260  16.087  41.065
ATOM   1553  CG1 VAL B 210       8.670  16.103  41.677
ATOM   1554  CG2 VAL B 210       6.931  17.337  40.231
ATOM   1555  C   VAL B 210       7.451  13.681  41.039
ATOM   1556  O   VAL B 210       6.612  13.164  41.776
ATOM   1557  N   ARG B 211       8.712  13.212  40.952
ATOM   1558  CA  ARG B 211       9.117  12.081  41.730
ATOM   1559  CB  ARG B 211       9.113  10.787  40.905
ATOM   1560  CG  ARG B 211      10.034  10.873  39.689
ATOM   1561  CD  ARG B 211       9.683   9.879  38.581
ATOM   1562  NE  ARG B 211      10.780   9.920  37.574
ATOM   1563  CZ  ARG B 211      10.802  10.879  36.604
ATOM   1564  NH1 ARG B 211       9.821  11.828  36.548
ATOM   1565  NH2 ARG B 211      11.813  10.885  35.688
ATOM   1566  C   ARG B 211      10.511  12.347  42.187
ATOM   1567  O   ARG B 211      11.325  12.896  41.448
ATOM   1568  N   CYS B 212      10.823  11.966  43.438
ATOM   1569  CA  CYS B 212      12.137  12.206  43.945
ATOM   1570  CB  CYS B 212      12.133  12.694  45.403
ATOM   1571  SG  CYS B 212      11.260  11.540  46.503
ATOM   1572  C   CYS B 212      12.875  10.916  43.901
ATOM   1573  O   CYS B 212      12.334   9.862  44.234
ATOM   1574  N   PHE B 213      14.146  10.969  43.465
ATOM   1575  CA  PHE B 213      14.915   9.765  43.440
ATOM   1576  CB  PHE B 213      16.108   9.835  42.471
ATOM   1577  CG  PHE B 213      16.737   8.486  42.415
ATOM   1578  CD1 PHE B 213      16.254   7.527  41.553
ATOM   1579  CD2 PHE B 213      17.810   8.178  43.219
ATOM   1580  CE1 PHE B 213      16.829   6.280  41.496
ATOM   1581  CE2 PHE B 213      18.390   6.932  43.167
ATOM   1582  CZ  PHE B 213      17.900   5.982  42.304
ATOM   1583  C   PHE B 213      15.451   9.644  44.828
ATOM   1584  O   PHE B 213      16.249  10.474  45.258
ATOM   1585  N   THR B 214      15.013   8.613  45.580
ATOM   1586  CA  THR B 214      15.472   8.552  46.936
ATOM   1587  CB  THR B 214      14.433   8.964  47.941
ATOM   1588  OG1 THR B 214      15.011   9.067  49.234
ATOM   1589  CG2 THR B 214      13.306   7.916  47.939
ATOM   1590  C   THR B 214      15.907   7.168  47.290
ATOM   1591  O   THR B 214      15.485   6.180  46.690
ATOM   1592  N   SER B 215      16.811   7.085  48.286
ATOM   1593  CA  SER B 215      17.262   5.824  48.786
ATOM   1594  CB  SER B 215      18.762   5.566  48.569
ATOM   1595  OG  SER B 215      19.039   5.454  47.181
ATOM   1596  C   SER B 215      17.021   5.866  50.258
ATOM   1597  O   SER B 215      17.265   6.883  50.905
ATOM   1598  N   VAL B 216      16.526   4.754  50.829
ATOM   1599  CA  VAL B 216      16.232   4.753  52.232
ATOM   1600  CB  VAL B 216      14.977   4.026  52.596
ATOM   1601  CG1 VAL B 216      13.776   4.834  52.090
ATOM   1602  CG2 VAL B 216      15.061   2.613  52.002
ATOM   1603  C   VAL B 216      17.347   4.101  52.973
ATOM   1604  O   VAL B 216      17.921   3.108  52.530
ATOM   1605  N   TYR B 217      17.690   4.683  54.138
ATOM   1606  CA  TYR B 217      18.735   4.156  54.964
ATOM   1607  CB  TYR B 217      20.025   4.997  54.961
ATOM   1608  CG  TYR B 217      20.658   4.953  53.614
ATOM   1609  CD1 TYR B 217      20.298   5.856  52.639
ATOM   1610  CD2 TYR B 217      21.618   4.009  53.332
ATOM   1611  CE1 TYR B 217      20.893   5.815  51.401
ATOM   1612  CE2 TYR B 217      22.215   3.963  52.095
ATOM   1613  CZ  TYR B 217      21.851   4.867  51.129
ATOM   1614  OH  TYR B 217      22.463   4.824  49.859
ATOM   1615  C   TYR B 217      18.249   4.188  56.377
ATOM   1616  O   TYR B 217      17.308   4.899  56.713
ATOM   1617  N   PRO B 218      18.889   3.408  57.204
ATOM   1618  CA  PRO B 218      18.530   3.360  58.597
ATOM   1619  CD  PRO B 218      19.453   2.151  56.743
ATOM   1620  CB  PRO B 218      19.172   2.094  59.153
ATOM   1621  CG  PRO B 218      19.306   1.181  57.925
ATOM   1622  C   PRO B 218      18.991   4.598  59.299
ATOM   1623  O   PRO B 218      19.924   5.246  58.830
ATOM   1624  N   LEU B 219      18.367   4.923  60.446
ATOM   1625  CA  LEU B 219      18.676   6.120  61.175
ATOM   1626  CB  LEU B 219      17.768   6.314  62.407
ATOM   1627  CG  LEU B 219      17.896   7.692  63.095
ATOM   1628  CD2 LEU B 219      17.545   8.832  62.119
ATOM   1629  CD1 LEU B 219      19.261   7.895  63.774
ATOM   1630  C   LEU B 219      20.097   6.045  61.639
ATOM   1631  O   LEU B 219      20.808   7.051  61.665
ATOM   1632  N   GLU B 220      20.557   4.833  61.987
ATOM   1633  CA  GLU B 220      21.854   4.672  62.571
ATOM   1634  CB  GLU B 220      22.224   3.205  62.849
ATOM   1635  CG  GLU B 220      21.351   2.544  63.914
ATOM   1636  CD  GLU B 220      20.005   2.243  63.273
ATOM   1637  OE1 GLU B 220      19.105   3.120  63.331
ATOM   1638  OE2 GLU B 220      19.862   1.126  62.708
ATOM   1639  C   GLU B 220      22.895   5.193  61.643
ATOM   1640  O   GLU B 220      23.863   5.804  62.097
ATOM   1641  N   HIS B 221      22.736   4.984  60.324
ATOM   1642  CA  HIS B 221      23.816   5.369  59.463
ATOM   1643  ND1 HIS B 221      23.390   2.105  58.885
ATOM   1644  CG  HIS B 221      24.288   3.072  58.489
ATOM   1645  CB  HIS B 221      23.916   4.495  58.201
ATOM   1646  NE2 HIS B 221      25.382   1.120  58.784
ATOM   1647  CD2 HIS B 221      25.499   2.454  58.434
ATOM   1648  CE1 HIS B 221      24.097   0.958  59.046
ATOM   1649  C   HIS B 221      23.680   6.789  58.998
ATOM   1650  O   HIS B 221      24.040   7.097  57.863
ATOM   1651  N   ALA B 222      23.219   7.710  59.865
ATOM   1652  CA  ALA B 222      23.105   9.079  59.442
ATOM   1653  CB  ALA B 222      22.521  10.002  60.528
ATOM   1654  C   ALA B 222      24.482   9.580  59.121
ATOM   1655  O   ALA B 222      24.706  10.253  58.116
ATOM   1656  N   ASN B 223      25.456   9.230  59.974
ATOM   1657  CA  ASN B 223      26.796   9.710  59.808
ATOM   1658  CB  ASN B 223      27.713   9.297  60.965
ATOM   1659  CG  ASN B 223      28.954  10.166  60.885
ATOM   1660  OD1 ASN B 223      29.675  10.174  59.888
ATOM   1661  ND2 ASN B 223      29.204  10.940  61.974
ATOM   1662  C   ASN B 223      27.373   9.178  58.532
ATOM   1663  O   ASN B 223      28.123   9.876  57.852
ATOM   1664  N   GLU B 224      27.049   7.920  58.182
ATOM   1665  CA  GLU B 224      27.573   7.314  56.991
ATOM   1666  CB  GLU B 224      27.122   5.853  56.824
ATOM   1667  CG  GLU B 224      27.711   4.909  57.874
ATOM   1668  CD  GLU B 224      29.182   4.706  57.540
ATOM   1669  OE1 GLU B 224      29.616   5.207  56.469
ATOM   1670  OE2 GLU B 224      29.889   4.047  58.349
ATOM   1671  C   GLU B 224      27.064   8.077  55.810
ATOM   1672  O   GLU B 224      27.785   8.293  54.839
ATOM   1673  N   ALA B 225      25.794   8.514  55.877
ATOM   1674  CA  ALA B 225      25.180   9.222  54.796
ATOM   1675  CB  ALA B 225      23.721   9.603  55.094
ATOM   1676  C   ALA B 225      25.937  10.488  54.562
ATOM   1677  O   ALA B 225      26.180  10.874  53.420
ATOM   1678  N   LEU B 226      26.352  11.163  55.648
ATOM   1679  CA  LEU B 226      27.021  12.422  55.508
ATOM   1680  CB  LEU B 226      27.379  13.050  56.875
ATOM   1681  CG  LEU B 226      27.994  14.468  56.829
ATOM   1682  CD2 LEU B 226      27.044  15.463  56.141
ATOM   1683  CD1 LEU B 226      29.413  14.482  56.236
ATOM   1684  C   LEU B 226      28.294  12.214  54.739
ATOM   1685  O   LEU B 226      28.599  12.979  53.825
ATOM   1686  N   ASP B 227      29.077  11.170  55.084
ATOM   1687  CA  ASP B 227      30.335  10.971  54.416
ATOM   1688  CB  ASP B 227      31.276   9.930  55.065
ATOM   1689  CG  ASP B 227      30.654   8.543  55.064
ATOM   1690  OD1 ASP B 227      30.827   7.810  54.055
ATOM   1691  OD2 ASP B 227      30.002   8.197  56.083
ATOM   1692  C   ASP B 227      30.102  10.595  52.988
ATOM   1693  O   ASP B 227      30.880  10.955  52.109
ATOM   1694  N   ASP B 228      29.008   9.859  52.728
ATOM   1695  CA  ASP B 228      28.648   9.406  51.419
ATOM   1696  CB  ASP B 228      27.310   8.642  51.483
ATOM   1697  CG  ASP B 228      27.186   7.678  50.317
ATOM   1698  OD1 ASP B 228      28.232   7.119  49.899
ATOM   1699  OD2 ASP B 228      26.037   7.480  49.837
ATOM   1700  C   ASP B 228      28.441  10.646  50.609
ATOM   1701  O   ASP B 228      28.767  10.696  49.423
ATOM   1702  N   LEU B 229      27.878  11.685  51.258
ATOM   1703  CA  LEU B 229      27.608  12.948  50.633
ATOM   1704  CB  LEU B 229      26.850  13.918  51.570
ATOM   1705  CG  LEU B 229      26.315  15.233  50.941
ATOM   1706  CD2 LEU B 229      27.386  16.069  50.222
ATOM   1707  CD1 LEU B 229      25.593  16.070  52.009
ATOM   1708  C   LEU B 229      28.917  13.569  50.257
ATOM   1709  O   LEU B 229      29.048  14.147  49.179
ATOM   1710  N   ARG B 230      29.929  13.463  51.136
ATOM   1711  CA  ARG B 230      31.204  14.072  50.878
ATOM   1712  CB  ARG B 230      32.213  13.798  52.008
ATOM   1713  CG  ARG B 230      33.672  13.992  51.594
ATOM   1714  CD  ARG B 230      34.472  12.688  51.630
ATOM   1715  NE  ARG B 230      33.496  11.562  51.591
ATOM   1716  CZ  ARG B 230      33.912  10.303  51.266
ATOM   1717  NH1 ARG B 230      35.206  10.088  50.890
ATOM   1718  NH2 ARG B 230      33.036   9.257  51.323
ATOM   1719  C   ARG B 230      31.756  13.498  49.616
ATOM   1720  O   ARG B 230      32.301  14.215  48.778
ATOM   1721  N   ALA B 231      31.615  12.173  49.454
ATOM   1722  CA  ALA B 231      32.097  11.496  48.291
ATOM   1723  CB  ALA B 231      31.890   9.972  48.350
ATOM   1724  C   ALA B 231      31.350  12.013  47.102
ATOM   1725  O   ALA B 231      31.905  12.119  46.012
ATOM   1726  N   GLY B 232      30.058  12.354  47.271
ATOM   1727  CA  GLY B 232      29.286  12.760  46.131
ATOM   1728  C   GLY B 232      28.784  11.477  45.572
ATOM   1729  O   GLY B 232      28.417  11.356  44.404
ATOM   1730  N   ARG B 233      28.799  10.476  46.463
ATOM   1731  CA  ARG B 233      28.428   9.118  46.239
ATOM   1732  CB  ARG B 233      28.749   8.244  47.460
ATOM   1733  CG  ARG B 233      28.846   6.738  47.204
ATOM   1734  CD  ARG B 233      27.548   6.066  46.767
ATOM   1735  NE  ARG B 233      27.697   5.733  45.324
ATOM   1736  CZ  ARG B 233      28.322   4.571  44.971
ATOM   1737  NH1 ARG B 233      28.777   3.722  45.938
ATOM   1738  NH2 ARG B 233      28.499   4.262  43.653
ATOM   1739  C   ARG B 233      26.959   9.042  45.977
ATOM   1740  O   ARG B 233      26.503   8.129  45.298
ATOM   1741  N   VAL B 234      26.145   9.968  46.514
ATOM   1742  CA  VAL B 234      24.743   9.728  46.334
ATOM   1743  CB  VAL B 234      23.942   9.855  47.600
ATOM   1744  CG1 VAL B 234      23.910  11.333  48.025
ATOM   1745  CG2 VAL B 234      22.555   9.237  47.361
ATOM   1746  C   VAL B 234      24.110  10.607  45.303
ATOM   1747  O   VAL B 234      24.308  11.822  45.235
ATOM   1748  N   SER B 235      23.297   9.967  44.447
ATOM   1749  CA  SER B 235      22.546  10.718  43.500
ATOM   1750  CB  SER B 235      22.448  10.073  42.106
ATOM   1751  OG  SER B 235      21.678  10.904  41.249
ATOM   1752  C   SER B 235      21.167  10.746  44.058
ATOM   1753  O   SER B 235      20.636   9.716  44.472
ATOM   1754  N   GLY B 236      20.547  11.938  44.093
ATOM   1755  CA  GLY B 236      19.210  12.005  44.601
ATOM   1756  C   GLY B 236      19.215  12.340  46.058
ATOM   1757  O   GLY B 236      20.142  12.966  46.571
ATOM   1758  N   ALA B 237      18.134  11.942  46.757
ATOM   1759  CA  ALA B 237      17.976  12.279  48.140
ATOM   1760  CB  ALA B 237      16.670  13.034  48.441
ATOM   1761  C   ALA B 237      17.945  11.031  48.953
ATOM   1762  O   ALA B 237      17.592   9.952  48.477
ATOM   1763  N   ALA B 238      18.353  11.165  50.227
ATOM   1764  CA  ALA B 238      18.334  10.047  51.111
ATOM   1765  CB  ALA B 238      19.662   9.830  51.857
ATOM   1766  C   ALA B 238      17.281  10.319  52.128
ATOM   1767  O   ALA B 238      17.113  11.449  52.587
ATOM   1768  N   VAL B 239      16.511   9.275  52.479
ATOM   1769  CA  VAL B 239      15.513   9.457  53.481
ATOM   1770  CB  VAL B 239      14.118   9.230  52.971
ATOM   1771  CG1 VAL B 239      13.935   7.739  52.645
ATOM   1772  CG2 VAL B 239      13.121   9.781  53.999
ATOM   1773  C   VAL B 239      15.799   8.451  54.546
ATOM   1774  O   VAL B 239      16.108   7.295  54.262
ATOM   1775  N   ILE B 240      15.724   8.882  55.815
ATOM   1776  CA  ILE B 240      15.974   7.967  56.885
ATOM   1777  CB  ILE B 240      16.140   8.659  58.215
ATOM   1778  CG2 ILE B 240      14.803   9.318  58.590
ATOM   1779  CG1 ILE B 240      16.703   7.706  59.287
ATOM   1780  CD1 ILE B 240      15.778   6.547  59.658
ATOM   1781  C   ILE B 240      14.759   7.043  56.940
ATOM   1782  O   ILE B 240      14.962   5.804  57.051
ATOM   1783  OXT ILE B 240      13.611   7.557  56.858
ENDMDL