File: 1A8O.asa

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python-biopython 1.68%2Bdfsg-3
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ATOM      9  N   ASP A 152      21.554  34.953  27.691  37.371  1.65
ATOM     10  CA  ASP A 152      21.835  36.306  28.144  10.829  1.87
ATOM     11  C   ASP A 152      21.947  37.322  27.000    .490  1.76
ATOM     12  O   ASP A 152      21.678  38.510  27.187   9.320  1.40
ATOM     13  CB  ASP A 152      23.126  36.292  28.966  26.086  1.87
ATOM     14  CG  ASP A 152      23.098  37.275  30.112  11.885  1.76
ATOM     15  OD1 ASP A 152      23.433  38.456  29.884  34.529  1.40
ATOM     16  OD2 ASP A 152      22.749  36.865  31.241  40.969  1.40
ATOM     17  N   ILE A 153      22.322  36.838  25.818   1.042  1.65
ATOM     18  CA  ILE A 153      22.498  37.681  24.632    .729  1.87
ATOM     19  C   ILE A 153      21.220  38.389  24.164    .000  1.76
ATOM     20  O   ILE A 153      20.214  37.743  23.876    .294  1.40
ATOM     21  CB  ILE A 153      23.062  36.854  23.441   1.882  1.87
ATOM     22  CG1 ILE A 153      24.282  36.029  23.879   1.880  1.87
ATOM     23  CG2 ILE A 153      23.423  37.769  22.280    .000  1.87
ATOM     24  CD1 ILE A 153      25.429  36.840  24.455  26.201  1.87
ATOM     25  N   ARG A 154      21.280  39.719  24.101   2.027  1.65
ATOM     26  CA  ARG A 154      20.173  40.563  23.646    .000  1.87
ATOM     27  C   ARG A 154      20.766  41.644  22.751    .003  1.76
ATOM     28  O   ARG A 154      21.804  42.216  23.075   8.796  1.40
ATOM     29  CB  ARG A 154      19.444  41.206  24.830  18.323  1.87
ATOM     30  CG  ARG A 154      18.724  40.196  25.695    .092  1.87
ATOM     31  CD  ARG A 154      18.011  40.824  26.869  32.364  1.87
ATOM     32  NE  ARG A 154      17.416  39.777  27.690  13.390  1.65
ATOM     33  CZ  ARG A 154      16.221  39.234  27.476   4.926  1.76
ATOM     34  NH1 ARG A 154      15.459  39.650  26.470  25.516  1.65
ATOM     35  NH2 ARG A 154      15.824  38.211  28.222  53.311  1.65
ATOM     36  N   GLN A 155      20.116  41.917  21.623    .000  1.65
ATOM     37  CA  GLN A 155      20.613  42.918  20.680    .000  1.87
ATOM     38  C   GLN A 155      20.546  44.344  21.203    .000  1.76
ATOM     39  O   GLN A 155      19.488  44.804  21.635   9.720  1.40
ATOM     40  CB  GLN A 155      19.837  42.841  19.368    .000  1.87
ATOM     41  CG  GLN A 155      20.385  43.751  18.271    .000  1.87
ATOM     42  CD  GLN A 155      19.526  43.736  17.022    .000  1.76
ATOM     43  OE1 GLN A 155      18.365  43.322  17.058    .000  1.40
ATOM     44  NE2 GLN A 155      20.090  44.190  15.909   3.991  1.65
ATOM     45  N   GLY A 156      21.675  45.045  21.155    .303  1.65
ATOM     46  CA  GLY A 156      21.698  46.427  21.598  22.923  1.87
ATOM     47  C   GLY A 156      20.859  47.278  20.654    .000  1.76
ATOM     48  O   GLY A 156      20.729  46.935  19.475    .000  1.40
ATOM     49  N   PRO A 157      20.260  48.380  21.137    .000  1.65
ATOM     50  CA  PRO A 157      19.435  49.249  20.287    .776  1.87
ATOM     51  C   PRO A 157      20.158  49.801  19.054    .000  1.76
ATOM     52  O   PRO A 157      19.512  50.154  18.068   7.332  1.40
ATOM     53  CB  PRO A 157      18.993  50.357  21.249  26.396  1.87
ATOM     54  CG  PRO A 157      20.056  50.358  22.317  35.649  1.87
ATOM     55  CD  PRO A 157      20.300  48.887  22.519  30.627  1.87
ATOM     56  N   LYS A 158      21.486  49.867  19.109   1.292  1.65
ATOM     57  CA  LYS A 158      22.285  50.358  17.985   3.534  1.87
ATOM     58  C   LYS A 158      23.286  49.318  17.478   5.076  1.76
ATOM     59  O   LYS A 158      24.155  49.627  16.659  20.075  1.40
ATOM     60  CB  LYS A 158      23.025  51.649  18.358  27.393  1.87
ATOM     61  CG  LYS A 158      22.117  52.841  18.584  24.659  1.87
ATOM     62  CD  LYS A 158      21.236  53.111  17.369  20.931  1.87
ATOM     63  CE  LYS A 158      20.159  54.136  17.694  37.362  1.87
ATOM     64  NZ  LYS A 158      19.231  54.379  16.560  42.639  1.50
ATOM     65  N   GLU A 159      23.152  48.085  17.961   1.054  1.65
ATOM     66  CA  GLU A 159      24.037  46.996  17.561   4.111  1.87
ATOM     67  C   GLU A 159      23.563  46.364  16.255   1.016  1.76
ATOM     68  O   GLU A 159      22.398  45.994  16.132   3.126  1.40
ATOM     69  CB  GLU A 159      24.086  45.924  18.653   8.581  1.87
ATOM     70  CG  GLU A 159      25.003  44.744  18.321   9.289  1.87
ATOM     71  CD  GLU A 159      24.858  43.575  19.284   4.912  1.76
ATOM     72  OE1 GLU A 159      23.861  43.516  20.039    .547  1.40
ATOM     73  OE2 GLU A 159      25.748  42.701  19.277   3.382  1.40
ATOM     74  N   PRO A 160      24.459  46.247  15.256    .026  1.65
ATOM     75  CA  PRO A 160      24.089  45.645  13.969   7.316  1.87
ATOM     76  C   PRO A 160      23.580  44.224  14.212    .000  1.76
ATOM     77  O   PRO A 160      24.111  43.515  15.070    .000  1.40
ATOM     78  CB  PRO A 160      25.415  45.639  13.207   7.426  1.87
ATOM     79  CG  PRO A 160      26.116  46.856  13.749  30.220  1.87
ATOM     80  CD  PRO A 160      25.852  46.732  15.231  12.036  1.87
ATOM     81  N   PHE A 161      22.544  43.824  13.480   2.677  1.65
ATOM     82  CA  PHE A 161      21.960  42.494  13.639    .000  1.87
ATOM     83  C   PHE A 161      22.965  41.346  13.502    .000  1.76
ATOM     84  O   PHE A 161      22.928  40.397  14.283    .000  1.40
ATOM     85  CB  PHE A 161      20.793  42.292  12.666   1.403  1.87
ATOM     86  CG  PHE A 161      19.999  41.042  12.927    .000  1.76
ATOM     87  CD1 PHE A 161      19.234  40.918  14.085    .000  1.76
ATOM     88  CD2 PHE A 161      20.019  39.985  12.021  10.723  1.76
ATOM     89  CE1 PHE A 161      18.495  39.758  14.340    .000  1.76
ATOM     90  CE2 PHE A 161      19.286  38.821  12.263   8.557  1.76
ATOM     91  CZ  PHE A 161      18.523  38.708  13.427   1.900  1.76
ATOM     92  N   ARG A 162      23.861  41.443  12.522   2.294  1.65
ATOM     93  CA  ARG A 162      24.870  40.411  12.294    .617  1.87
ATOM     94  C   ARG A 162      25.788  40.216  13.509    .000  1.76
ATOM     95  O   ARG A 162      26.158  39.090  13.835    .000  1.40
ATOM     96  CB  ARG A 162      25.684  40.732  11.032  25.347  1.87
ATOM     97  CG  ARG A 162      26.777  39.725  10.715  17.281  1.87
ATOM     98  CD  ARG A 162      26.215  38.321  10.515  18.082  1.87
ATOM     99  NE  ARG A 162      27.235  37.297  10.736   2.717  1.65
ATOM    100  CZ  ARG A 162      28.136  36.918   9.833   6.269  1.76
ATOM    101  NH1 ARG A 162      28.155  37.473   8.628  47.024  1.65
ATOM    102  NH2 ARG A 162      29.030  35.992  10.145  44.980  1.65
ATOM    103  N   ASP A 163      26.137  41.309  14.185    .000  1.65
ATOM    104  CA  ASP A 163      26.994  41.247  15.373   2.277  1.87
ATOM    105  C   ASP A 163      26.279  40.526  16.517    .000  1.76
ATOM    106  O   ASP A 163      26.880  39.735  17.245   1.209  1.40
ATOM    107  CB  ASP A 163      27.408  42.658  15.805   9.604  1.87
ATOM    108  CG  ASP A 163      28.345  43.328  14.804   8.361  1.76
ATOM    109  OD1 ASP A 163      28.814  42.655  13.859  24.745  1.40
ATOM    110  OD2 ASP A 163      28.620  44.532  14.968  23.848  1.40
ATOM    111  N   TYR A 164      24.992  40.818  16.662    .000  1.65
ATOM    112  CA  TYR A 164      24.151  40.196  17.672    .000  1.87
ATOM    113  C   TYR A 164      24.025  38.704  17.350    .000  1.76
ATOM    114  O   TYR A 164      24.139  37.861  18.238    .000  1.40
ATOM    115  CB  TYR A 164      22.787  40.897  17.684    .000  1.87
ATOM    116  CG  TYR A 164      21.629  40.095  18.244    .000  1.76
ATOM    117  CD1 TYR A 164      21.657  39.583  19.543    .000  1.76
ATOM    118  CD2 TYR A 164      20.489  39.874  17.474    .000  1.76
ATOM    119  CE1 TYR A 164      20.571  38.872  20.056    .000  1.76
ATOM    120  CE2 TYR A 164      19.408  39.171  17.972    .000  1.76
ATOM    121  CZ  TYR A 164      19.450  38.673  19.258    .000  1.76
ATOM    122  OH  TYR A 164      18.365  37.977  19.732    .000  1.40
ATOM    123  N   VAL A 165      23.839  38.388  16.069    .000  1.65
ATOM    124  CA  VAL A 165      23.720  37.002  15.614    .000  1.87
ATOM    125  C   VAL A 165      24.962  36.204  15.999    .000  1.76
ATOM    126  O   VAL A 165      24.853  35.084  16.498    .000  1.40
ATOM    127  CB  VAL A 165      23.502  36.931  14.077    .000  1.87
ATOM    128  CG1 VAL A 165      23.661  35.501  13.570   8.189  1.87
ATOM    129  CG2 VAL A 165      22.120  37.444  13.733   2.131  1.87
ATOM    130  N   ASP A 166      26.137  36.796  15.797    .000  1.65
ATOM    131  CA  ASP A 166      27.387  36.126  16.139   2.281  1.87
ATOM    132  C   ASP A 166      27.511  35.879  17.644   1.302  1.76
ATOM    133  O   ASP A 166      27.925  34.804  18.060   1.514  1.40
ATOM    134  CB  ASP A 166      28.595  36.912  15.612  21.675  1.87
ATOM    135  CG  ASP A 166      28.723  36.860  14.085   6.903  1.76
ATOM    136  OD1 ASP A 166      28.016  36.066  13.422   9.424  1.40
ATOM    137  OD2 ASP A 166      29.545  37.627  13.543  23.179  1.40
ATOM    138  N   ARG A 167      27.136  36.859  18.461    .074  1.65
ATOM    139  CA  ARG A 167      27.202  36.685  19.913   1.500  1.87
ATOM    140  C   ARG A 167      26.238  35.580  20.335    .000  1.76
ATOM    141  O   ARG A 167      26.585  34.701  21.120    .732  1.40
ATOM    142  CB  ARG A 167      26.850  37.988  20.638   1.573  1.87
ATOM    143  CG  ARG A 167      27.835  39.118  20.394  18.541  1.87
ATOM    144  CD  ARG A 167      27.667  40.246  21.404  31.735  1.87
ATOM    145  NE  ARG A 167      26.352  40.877  21.333   1.345  1.65
ATOM    146  CZ  ARG A 167      25.494  40.940  22.345   4.223  1.76
ATOM    147  NH1 ARG A 167      25.797  40.401  23.519  25.855  1.65
ATOM    148  NH2 ARG A 167      24.325  41.539  22.181   6.135  1.65
ATOM    149  N   PHE A 168      25.037  35.622  19.769    .000  1.65
ATOM    150  CA  PHE A 168      23.984  34.649  20.039    .025  1.87
ATOM    151  C   PHE A 168      24.456  33.232  19.729    .000  1.76
ATOM    152  O   PHE A 168      24.305  32.327  20.552   1.954  1.40
ATOM    153  CB  PHE A 168      22.761  34.993  19.186    .000  1.87
ATOM    154  CG  PHE A 168      21.538  34.184  19.504    .073  1.76
ATOM    155  CD1 PHE A 168      21.301  32.973  18.859    .107  1.76
ATOM    156  CD2 PHE A 168      20.586  34.664  20.397   2.400  1.76
ATOM    157  CE1 PHE A 168      20.130  32.254  19.094   2.318  1.76
ATOM    158  CE2 PHE A 168      19.415  33.954  20.639   6.121  1.76
ATOM    159  CZ  PHE A 168      19.186  32.747  19.985   9.534  1.76
ATOM    160  N   TYR A 169      25.033  33.048  18.544    .000  1.65
ATOM    161  CA  TYR A 169      25.526  31.738  18.123    .000  1.87
ATOM    162  C   TYR A 169      26.755  31.256  18.875    .000  1.76
ATOM    163  O   TYR A 169      27.015  30.057  18.949    .000  1.40
ATOM    164  CB  TYR A 169      25.771  31.709  16.616   6.316  1.87
ATOM    165  CG  TYR A 169      24.608  31.119  15.869   2.343  1.76
ATOM    166  CD1 TYR A 169      23.508  31.900  15.519    .715  1.76
ATOM    167  CD2 TYR A 169      24.583  29.762  15.555  11.177  1.76
ATOM    168  CE1 TYR A 169      22.406  31.340  14.877    .000  1.76
ATOM    169  CE2 TYR A 169      23.490  29.193  14.913   9.956  1.76
ATOM    170  CZ  TYR A 169      22.406  29.985  14.577    .682  1.76
ATOM    171  OH  TYR A 169      21.326  29.415  13.941   9.814  1.40
ATOM    172  N   LYS A 170      27.508  32.195  19.432    .000  1.65
ATOM    173  CA  LYS A 170      28.691  31.859  20.208    .000  1.87
ATOM    174  C   LYS A 170      28.183  31.155  21.468    .665  1.76
ATOM    175  O   LYS A 170      28.705  30.117  21.859   5.086  1.40
ATOM    176  CB  LYS A 170      29.455  33.137  20.556    .997  1.87
ATOM    177  CG  LYS A 170      30.787  32.942  21.242  16.562  1.87
ATOM    178  CD  LYS A 170      31.428  34.297  21.496  25.560  1.87
ATOM    179  CE  LYS A 170      32.618  34.194  22.436  45.068  1.87
ATOM    180  NZ  LYS A 170      33.153  35.536  22.820  48.641  1.50
ATOM    181  N   THR A 171      27.116  31.695  22.055    .000  1.65
ATOM    182  CA  THR A 171      26.508  31.110  23.247   5.215  1.87
ATOM    183  C   THR A 171      25.826  29.789  22.889    .000  1.76
ATOM    184  O   THR A 171      25.827  28.840  23.676    .062  1.40
ATOM    185  CB  THR A 171      25.475  32.075  23.876   1.098  1.87
ATOM    186  OG1 THR A 171      26.150  33.240  24.357  13.388  1.40
ATOM    187  CG2 THR A 171      24.741  31.417  25.045  48.926  1.87
ATOM    188  N   LEU A 172      25.264  29.727  21.687    .164  1.65
ATOM    189  CA  LEU A 172      24.587  28.528  21.224   1.718  1.87
ATOM    190  C   LEU A 172      25.587  27.392  20.984    .589  1.76
ATOM    191  O   LEU A 172      25.302  26.236  21.301    .000  1.40
ATOM    192  CB  LEU A 172      23.789  28.840  19.955    .750  1.87
ATOM    193  CG  LEU A 172      22.707  27.854  19.514    .720  1.87
ATOM    194  CD1 LEU A 172      21.787  27.515  20.682  26.378  1.87
ATOM    195  CD2 LEU A 172      21.910  28.464  18.375   1.741  1.87
ATOM    196  N   ARG A 173      26.767  27.727  20.462    .122  1.65
ATOM    197  CA  ARG A 173      27.806  26.728  20.202   4.512  1.87
ATOM    198  C   ARG A 173      28.299  26.044  21.468    .904  1.76
ATOM    199  O   ARG A 173      28.656  24.864  21.443   4.779  1.40
ATOM    200  CB  ARG A 173      29.006  27.352  19.492   8.983  1.87
ATOM    201  CG  ARG A 173      28.944  27.266  17.984  17.930  1.87
ATOM    202  CD  ARG A 173      30.295  27.583  17.356  37.282  1.87
ATOM    203  NE  ARG A 173      30.744  28.937  17.662  14.045  1.65
ATOM    204  CZ  ARG A 173      30.326  30.032  17.033   4.464  1.76
ATOM    205  NH1 ARG A 173      29.441  29.954  16.046  27.568  1.65
ATOM    206  NH2 ARG A 173      30.787  31.215  17.406  29.995  1.65
ATOM    207  N   ALA A 174      28.332  26.793  22.568    .406  1.65
ATOM    208  CA  ALA A 174      28.789  26.276  23.854   9.822  1.87
ATOM    209  C   ALA A 174      27.943  25.109  24.350    .000  1.76
ATOM    210  O   ALA A 174      28.374  24.348  25.215  16.269  1.40
ATOM    211  CB  ALA A 174      28.803  27.388  24.888  41.450  1.87
ATOM    212  N   GLU A 175      26.740  24.973  23.801    .000  1.65
ATOM    213  CA  GLU A 175      25.833  23.899  24.186   2.332  1.87
ATOM    214  C   GLU A 175      25.775  22.791  23.139    .030  1.76
ATOM    215  O   GLU A 175      24.998  21.847  23.280  18.956  1.40
ATOM    216  CB  GLU A 175      24.425  24.456  24.418  12.362  1.87
ATOM    217  CG  GLU A 175      24.354  25.596  25.435  19.466  1.87
ATOM    218  CD  GLU A 175      24.816  25.190  26.824   9.282  1.76
ATOM    219  OE1 GLU A 175      24.535  24.049  27.243  34.463  1.40
ATOM    220  OE2 GLU A 175      25.454  26.018  27.506  32.000  1.40
ATOM    221  N   GLN A 176      26.601  22.907  22.098    .000  1.65
ATOM    222  CA  GLN A 176      26.645  21.930  21.007   7.972  1.87
ATOM    223  C   GLN A 176      25.240  21.583  20.533   1.073  1.76
ATOM    224  O   GLN A 176      24.885  20.411  20.389  20.005  1.40
ATOM    225  CB  GLN A 176      27.391  20.655  21.422  22.169  1.87
ATOM    226  CG  GLN A 176      28.884  20.833  21.646  35.203  1.87
ATOM    227  CD  GLN A 176      29.200  21.479  22.977   5.521  1.76
ATOM    228  OE1 GLN A 176      28.729  21.028  24.025  26.283  1.40
ATOM    229  NE2 GLN A 176      29.998  22.543  22.947  29.649  1.65
ATOM    230  N   ALA A 177      24.438  22.619  20.314   1.422  1.65
ATOM    231  CA  ALA A 177      23.066  22.454  19.863   5.561  1.87
ATOM    232  C   ALA A 177      23.001  21.782  18.498    .065  1.76
ATOM    233  O   ALA A 177      23.824  22.046  17.620   9.176  1.40
ATOM    234  CB  ALA A 177      22.370  23.806  19.817   2.348  1.87
ATOM    235  N   SER A 178      22.035  20.886  18.339   2.057  1.65
ATOM    236  CA  SER A 178      21.831  20.180  17.080  11.528  1.87
ATOM    237  C   SER A 178      21.174  21.137  16.090    .144  1.76
ATOM    238  O   SER A 178      20.852  22.271  16.441    .000  1.40
ATOM    239  CB  SER A 178      20.917  18.979  17.305  43.136  1.87
ATOM    240  OG  SER A 178      19.638  19.408  17.741   6.205  1.40
ATOM    241  N   GLN A 179      20.949  20.675  14.865   7.634  1.65
ATOM    242  CA  GLN A 179      20.315  21.512  13.851    .440  1.87
ATOM    243  C   GLN A 179      18.908  21.923  14.284    .000  1.76
ATOM    244  O   GLN A 179      18.539  23.095  14.184    .000  1.40
ATOM    245  CB  GLN A 179      20.262  20.791  12.500  28.119  1.87
ATOM    246  CG  GLN A 179      19.688  21.641  11.372  25.453  1.87
ATOM    247  CD  GLN A 179      20.414  22.968  11.212   4.860  1.76
ATOM    248  OE1 GLN A 179      21.592  23.004  10.860  29.416  1.40
ATOM    249  NE2 GLN A 179      19.714  24.065  11.484  17.669  1.65
ATOM    250  N   GLU A 180      18.136  20.955  14.773    .833  1.65
ATOM    251  CA  GLU A 180      16.775  21.211  15.233    .000  1.87
ATOM    252  C   GLU A 180      16.738  22.240  16.354    .000  1.76
ATOM    253  O   GLU A 180      15.875  23.117  16.360    .000  1.40
ATOM    254  CB  GLU A 180      16.101  19.916  15.692   7.079  1.87
ATOM    255  CG  GLU A 180      15.478  19.100  14.569  35.598  1.87
ATOM    256  CD  GLU A 180      14.341  19.832  13.879   8.939  1.76
ATOM    257  OE1 GLU A 180      13.247  19.935  14.473  20.971  1.40
ATOM    258  OE2 GLU A 180      14.542  20.307  12.743  23.306  1.40
ATOM    259  N   VAL A 181      17.668  22.133  17.300    .000  1.65
ATOM    260  CA  VAL A 181      17.730  23.079  18.412    .000  1.87
ATOM    261  C   VAL A 181      18.064  24.477  17.897    .000  1.76
ATOM    262  O   VAL A 181      17.491  25.467  18.352   4.823  1.40
ATOM    263  CB  VAL A 181      18.754  22.639  19.484    .000  1.87
ATOM    264  CG1 VAL A 181      18.932  23.733  20.530  29.246  1.87
ATOM    265  CG2 VAL A 181      18.279  21.357  20.158  30.227  1.87
ATOM    266  N   LYS A 182      18.971  24.552  16.929    .000  1.65
ATOM    267  CA  LYS A 182      19.343  25.835  16.344    .000  1.87
ATOM    268  C   LYS A 182      18.126  26.477  15.685    .140  1.76
ATOM    269  O   LYS A 182      17.905  27.680  15.830    .294  1.40
ATOM    270  CB  LYS A 182      20.444  25.660  15.306    .676  1.87
ATOM    271  CG  LYS A 182      21.777  25.239  15.874    .000  1.87
ATOM    272  CD  LYS A 182      22.756  25.055  14.742   5.860  1.87
ATOM    273  CE  LYS A 182      24.069  24.517  15.226  13.422  1.87
ATOM    274  NZ  LYS A 182      24.913  24.222  14.047  43.920  1.50
ATOM    275  N   ASN A 183      17.344  25.672  14.964    .000  1.65
ATOM    276  CA  ASN A 183      16.136  26.161  14.297   2.092  1.87
ATOM    277  C   ASN A 183      15.146  26.712  15.308    .000  1.76
ATOM    278  O   ASN A 183      14.599  27.791  15.108    .301  1.40
ATOM    279  CB  ASN A 183      15.468  25.055  13.475  10.678  1.87
ATOM    280  CG  ASN A 183      16.242  24.712  12.220   5.564  1.76
ATOM    281  OD1 ASN A 183      17.164  25.430  11.828  17.046  1.40
ATOM    282  ND2 ASN A 183      15.865  23.613  11.576  28.105  1.65
ATOM    283  N   TRP A 184      14.932  25.976  16.397    .000  1.65
ATOM    284  CA  TRP A 184      14.017  26.406  17.450    .270  1.87
ATOM    285  C   TRP A 184      14.495  27.713  18.072   6.652  1.76
ATOM    286  O   TRP A 184      13.700  28.624  18.299    .000  1.40
ATOM    287  CB  TRP A 184      13.904  25.342  18.545  16.576  1.87
ATOM    288  CG  TRP A 184      13.254  24.076  18.112   2.177  1.76
ATOM    289  CD1 TRP A 184      12.332  23.924  17.121  11.448  1.76
ATOM    290  CD2 TRP A 184      13.484  22.772  18.655   2.579  1.76
ATOM    291  NE1 TRP A 184      11.975  22.601  17.007  20.144  1.65
ATOM    292  CE2 TRP A 184      12.666  21.873  17.937   3.275  1.76
ATOM    293  CE3 TRP A 184      14.303  22.276  19.678  13.098  1.76
ATOM    294  CZ2 TRP A 184      12.641  20.502  18.209  22.067  1.76
ATOM    295  CZ3 TRP A 184      14.280  20.914  19.948  20.803  1.76
ATOM    296  CH2 TRP A 184      13.452  20.042  19.213  29.151  1.76
ATOM    305  N   THR A 186      16.438  29.964  16.716   3.674  1.65
ATOM    306  CA  THR A 186      16.375  31.015  15.695    .000  1.87
ATOM    307  C   THR A 186      14.950  31.585  15.557    .000  1.76
ATOM    308  O   THR A 186      14.778  32.797  15.378   1.326  1.40
ATOM    309  CB  THR A 186      16.869  30.474  14.331   2.345  1.87
ATOM    310  OG1 THR A 186      18.228  30.039  14.461   1.920  1.40
ATOM    311  CG2 THR A 186      16.791  31.544  13.245  12.538  1.87
ATOM    312  N   GLU A 187      13.947  30.705  15.643    .000  1.65
ATOM    313  CA  GLU A 187      12.529  31.082  15.544   8.546  1.87
ATOM    314  C   GLU A 187      12.045  31.815  16.785    .021  1.76
ATOM    315  O   GLU A 187      11.151  32.654  16.700  14.381  1.40
ATOM    316  CB  GLU A 187      11.625  29.849  15.408  13.346  1.87
ATOM    317  CG  GLU A 187      11.950  28.866  14.305  11.888  1.87
ATOM    318  CD  GLU A 187      11.054  27.634  14.345   8.127  1.76
ATOM    319  OE1 GLU A 187      11.086  26.907  15.364  12.687  1.40
ATOM    320  OE2 GLU A 187      10.326  27.392  13.357  30.194  1.40
ATOM    321  N   THR A 188      12.589  31.444  17.942    .000  1.65
ATOM    322  CA  THR A 188      12.177  32.030  19.212    .126  1.87
ATOM    323  C   THR A 188      13.076  33.117  19.787    .000  1.76
ATOM    324  O   THR A 188      12.888  34.301  19.504    .000  1.40
ATOM    325  CB  THR A 188      11.978  30.936  20.287   4.548  1.87
ATOM    326  OG1 THR A 188      13.202  30.210  20.469  10.198  1.40
ATOM    327  CG2 THR A 188      10.883  29.970  19.861  46.233  1.87
ATOM    328  N   LEU A 189      14.054  32.705  20.590    .074  1.65
ATOM    329  CA  LEU A 189      14.963  33.627  21.252    .000  1.87
ATOM    330  C   LEU A 189      15.702  34.645  20.392    .000  1.76
ATOM    331  O   LEU A 189      15.846  35.795  20.805    .000  1.40
ATOM    332  CB  LEU A 189      15.935  32.864  22.153   3.615  1.87
ATOM    333  CG  LEU A 189      15.286  32.289  23.417   5.355  1.87
ATOM    334  CD1 LEU A 189      16.327  31.647  24.304  62.618  1.87
ATOM    335  CD2 LEU A 189      14.580  33.396  24.183  27.594  1.87
ATOM    336  N   LEU A 190      16.162  34.254  19.205    .000  1.65
ATOM    337  CA  LEU A 190      16.876  35.211  18.356    .000  1.87
ATOM    338  C   LEU A 190      15.961  36.378  17.999    .000  1.76
ATOM    339  O   LEU A 190      16.391  37.528  17.968    .000  1.40
ATOM    340  CB  LEU A 190      17.402  34.552  17.078    .000  1.87
ATOM    341  CG  LEU A 190      18.238  35.486  16.188    .000  1.87
ATOM    342  CD1 LEU A 190      19.553  35.825  16.881    .000  1.87
ATOM    343  CD2 LEU A 190      18.506  34.834  14.842   4.339  1.87
ATOM    344  N   VAL A 191      14.695  36.068  17.738    .000  1.65
ATOM    345  CA  VAL A 191      13.703  37.080  17.395    .000  1.87
ATOM    346  C   VAL A 191      13.270  37.854  18.643    .000  1.76
ATOM    347  O   VAL A 191      13.262  39.086  18.649    .000  1.40
ATOM    348  CB  VAL A 191      12.460  36.438  16.718    .000  1.87
ATOM    349  CG1 VAL A 191      11.372  37.479  16.491   1.342  1.87
ATOM    350  CG2 VAL A 191      12.854  35.806  15.394  17.375  1.87
ATOM    351  N   GLN A 192      12.954  37.119  19.706    .000  1.65
ATOM    352  CA  GLN A 192      12.503  37.705  20.967    .000  1.87
ATOM    353  C   GLN A 192      13.541  38.565  21.682    .000  1.76
ATOM    354  O   GLN A 192      13.184  39.453  22.453   9.338  1.40
ATOM    355  CB  GLN A 192      12.008  36.602  21.902   6.312  1.87
ATOM    356  CG  GLN A 192      10.830  35.818  21.343   7.400  1.87
ATOM    357  CD  GLN A 192      10.505  34.578  22.155   5.545  1.76
ATOM    358  OE1 GLN A 192      10.626  34.568  23.385  26.944  1.40
ATOM    359  NE2 GLN A 192      10.093  33.520  21.466  22.469  1.65
ATOM    360  N   ASN A 193      14.820  38.291  21.445    .000  1.65
ATOM    361  CA  ASN A 193      15.887  39.056  22.080   1.008  1.87
ATOM    362  C   ASN A 193      16.443  40.164  21.189   1.045  1.76
ATOM    363  O   ASN A 193      17.416  40.823  21.548   1.966  1.40
ATOM    364  CB  ASN A 193      17.014  38.130  22.538    .000  1.87
ATOM    365  CG  ASN A 193      16.627  37.286  23.738    .000  1.76
ATOM    366  OD1 ASN A 193      15.451  37.192  24.094   3.798  1.40
ATOM    367  ND2 ASN A 193      17.619  36.681  24.378   9.884  1.65
ATOM    368  N   ALA A 194      15.830  40.353  20.023    .000  1.65
ATOM    369  CA  ALA A 194      16.248  41.392  19.084    .000  1.87
ATOM    370  C   ALA A 194      15.758  42.759  19.582    .331  1.76
ATOM    371  O   ALA A 194      14.809  42.834  20.368   8.554  1.40
ATOM    372  CB  ALA A 194      15.689  41.097  17.701    .000  1.87
ATOM    373  N   ASN A 195      16.404  43.837  19.140    .000  1.65
ATOM    374  CA  ASN A 195      16.005  45.172  19.582   3.232  1.87
ATOM    375  C   ASN A 195      14.639  45.580  19.015    .000  1.76
ATOM    376  O   ASN A 195      14.122  44.928  18.111    .000  1.40
ATOM    377  CB  ASN A 195      17.109  46.213  19.295    .321  1.87
ATOM    378  CG  ASN A 195      17.396  46.399  17.818    .563  1.76
ATOM    379  OD1 ASN A 195      16.559  46.131  16.960    .293  1.40
ATOM    380  ND2 ASN A 195      18.588  46.890  17.519   7.084  1.65
ATOM    381  N   PRO A 196      14.018  46.635  19.574    .392  1.65
ATOM    382  CA  PRO A 196      12.706  47.128  19.133   7.844  1.87
ATOM    383  C   PRO A 196      12.516  47.250  17.620   1.908  1.76
ATOM    384  O   PRO A 196      11.536  46.743  17.073   4.213  1.40
ATOM    385  CB  PRO A 196      12.617  48.485  19.822  31.414  1.87
ATOM    386  CG  PRO A 196      13.288  48.219  21.117  43.377  1.87
ATOM    387  CD  PRO A 196      14.522  47.454  20.693  17.291  1.87
ATOM    388  N   ASP A 197      13.454  47.913  16.952    .123  1.65
ATOM    389  CA  ASP A 197      13.383  48.098  15.506   6.388  1.87
ATOM    390  C   ASP A 197      13.351  46.786  14.733    .000  1.76
ATOM    391  O   ASP A 197      12.406  46.515  13.991   2.939  1.40
ATOM    392  CB  ASP A 197      14.564  48.939  15.018  20.609  1.87
ATOM    393  CG  ASP A 197      14.482  50.380  15.475  12.470  1.76
ATOM    394  OD1 ASP A 197      13.353  50.889  15.662  33.551  1.40
ATOM    395  OD2 ASP A 197      15.552  51.007  15.637  28.804  1.40
ATOM    396  N   CYS A 198      14.378  45.967  14.932    .227  1.65
ATOM    397  CA  CYS A 198      14.488  44.687  14.241    .963  1.87
ATOM    398  C   CYS A 198      13.443  43.638  14.633    .000  1.76
ATOM    399  O   CYS A 198      12.968  42.886  13.783    .000  1.40
ATOM    400  CB  CYS A 198      15.902  44.124  14.411   5.598  1.87
ATOM    401  SG  CYS A 198      16.144  42.477  13.674    .000  1.85
ATOM    402  N   LYS A 199      13.061  43.612  15.907    .000  1.65
ATOM    403  CA  LYS A 199      12.087  42.641  16.402    .000  1.87
ATOM    404  C   LYS A 199      10.746  42.686  15.673    .000  1.76
ATOM    405  O   LYS A 199      10.157  41.641  15.386    .000  1.40
ATOM    406  CB  LYS A 199      11.879  42.818  17.907   1.211  1.87
ATOM    407  CG  LYS A 199      11.014  41.753  18.541   4.192  1.87
ATOM    408  CD  LYS A 199      11.003  41.892  20.045  16.083  1.87
ATOM    409  CE  LYS A 199      10.171  40.797  20.670  16.832  1.87
ATOM    410  NZ  LYS A 199      10.269  40.823  22.154  33.658  1.50
ATOM    411  N   THR A 200      10.273  43.892  15.369    .165  1.65
ATOM    412  CA  THR A 200       9.002  44.065  14.665   5.526  1.87
ATOM    413  C   THR A 200       9.101  43.494  13.251    .000  1.76
ATOM    414  O   THR A 200       8.227  42.753  12.799   1.128  1.40
ATOM    415  CB  THR A 200       8.612  45.551  14.577   5.538  1.87
ATOM    416  OG1 THR A 200       8.611  46.122  15.892  23.213  1.40
ATOM    417  CG2 THR A 200       7.224  45.702  13.961  60.295  1.87
ATOM    418  N   ILE A 201      10.191  43.835  12.574    .000  1.65
ATOM    419  CA  ILE A 201      10.458  43.373  11.221   4.163  1.87
ATOM    420  C   ILE A 201      10.518  41.848  11.161    .000  1.76
ATOM    421  O   ILE A 201       9.916  41.229  10.284   1.180  1.40
ATOM    422  CB  ILE A 201      11.791  43.960  10.721    .000  1.87
ATOM    423  CG1 ILE A 201      11.677  45.481  10.620  18.988  1.87
ATOM    424  CG2 ILE A 201      12.184  43.356   9.389  15.109  1.87
ATOM    425  CD1 ILE A 201      12.967  46.169  10.250  38.939  1.87
ATOM    426  N   LEU A 202      11.222  41.249  12.117    .000  1.65
ATOM    427  CA  LEU A 202      11.377  39.801  12.170    .000  1.87
ATOM    428  C   LEU A 202      10.082  39.036  12.412    .000  1.76
ATOM    429  O   LEU A 202       9.885  37.956  11.855   7.535  1.40
ATOM    430  CB  LEU A 202      12.416  39.416  13.221    .586  1.87
ATOM    431  CG  LEU A 202      13.824  39.939  12.950    .000  1.87
ATOM    432  CD1 LEU A 202      14.764  39.438  14.027   1.240  1.87
ATOM    433  CD2 LEU A 202      14.287  39.491  11.575  10.066  1.87
ATOM    434  N   LYS A 203       9.214  39.575  13.261    .000  1.65
ATOM    435  CA  LYS A 203       7.937  38.927  13.546   2.544  1.87
ATOM    436  C   LYS A 203       7.048  38.954  12.303   1.381  1.76
ATOM    437  O   LYS A 203       6.294  38.011  12.044  17.022  1.40
ATOM    438  CB  LYS A 203       7.230  39.620  14.712  18.502  1.87
ATOM    439  CG  LYS A 203       7.828  39.324  16.085  10.831  1.87
ATOM    440  CD  LYS A 203       7.618  37.867  16.471  21.409  1.87
ATOM    441  CE  LYS A 203       8.090  37.590  17.889  14.257  1.87
ATOM    442  NZ  LYS A 203       7.916  36.158  18.262  27.636  1.50
ATOM    443  N   ALA A 204       7.189  40.020  11.516    .159  1.65
ATOM    444  CA  ALA A 204       6.419  40.213  10.290  12.085  1.87
ATOM    445  C   ALA A 204       6.871  39.332   9.117   1.702  1.76
ATOM    446  O   ALA A 204       6.391  39.495   7.991  27.103  1.40
ATOM    447  CB  ALA A 204       6.449  41.683   9.885  45.475  1.87
ATOM    448  N   LEU A 205       7.815  38.428   9.369    .000  1.65
ATOM    449  CA  LEU A 205       8.305  37.528   8.328   1.824  1.87
ATOM    450  C   LEU A 205       7.481  36.243   8.312   1.850  1.76
ATOM    451  O   LEU A 205       7.371  35.579   7.281  26.753  1.40
ATOM    452  CB  LEU A 205       9.788  37.196   8.539    .633  1.87
ATOM    453  CG  LEU A 205      10.832  38.299   8.323    .000  1.87
ATOM    454  CD1 LEU A 205      12.217  37.767   8.660   4.692  1.87
ATOM    455  CD2 LEU A 205      10.789  38.797   6.888  38.970  1.87
ATOM    456  N   GLY A 206       6.886  35.909   9.455    .865  1.65
ATOM    457  CA  GLY A 206       6.080  34.704   9.548  22.542  1.87
ATOM    458  C   GLY A 206       6.922  33.478   9.835   4.345  1.76
ATOM    459  O   GLY A 206       8.149  33.569   9.881   7.444  1.40
ATOM    460  N   PRO A 207       6.294  32.310  10.042    .343  1.65
ATOM    461  CA  PRO A 207       7.024  31.068  10.328  10.674  1.87
ATOM    462  C   PRO A 207       7.912  30.540   9.197   1.266  1.76
ATOM    463  O   PRO A 207       7.680  30.812   8.017  20.161  1.40
ATOM    464  CB  PRO A 207       5.901  30.083  10.675  36.106  1.87
ATOM    465  CG  PRO A 207       4.734  30.601   9.890  39.896  1.87
ATOM    466  CD  PRO A 207       4.839  32.090  10.112  31.688  1.87
ATOM    467  N   GLY A 208       8.952  29.808   9.585   4.177  1.65
ATOM    468  CA  GLY A 208       9.861  29.227   8.617  35.704  1.87
ATOM    469  C   GLY A 208      10.886  30.161   8.004   4.118  1.76
ATOM    470  O   GLY A 208      11.642  29.736   7.130  17.956  1.40
ATOM    471  N   ALA A 209      10.910  31.423   8.429   1.610  1.65
ATOM    472  CA  ALA A 209      11.884  32.382   7.900   3.789  1.87
ATOM    473  C   ALA A 209      13.285  31.936   8.311    .067  1.76
ATOM    474  O   ALA A 209      13.524  31.614   9.478  14.483  1.40
ATOM    475  CB  ALA A 209      11.599  33.779   8.428  14.143  1.87
ATOM    476  N   THR A 210      14.199  31.887   7.347    .000  1.65
ATOM    477  CA  THR A 210      15.563  31.458   7.625   6.924  1.87
ATOM    478  C   THR A 210      16.391  32.562   8.265    .411  1.76
ATOM    479  O   THR A 210      16.022  33.735   8.212   5.286  1.40
ATOM    480  CB  THR A 210      16.290  31.000   6.345   3.512  1.87
ATOM    481  OG1 THR A 210      16.498  32.124   5.479   2.619  1.40
ATOM    482  CG2 THR A 210      15.473  29.943   5.616  51.918  1.87
ATOM    483  N   LEU A 211      17.509  32.169   8.871   3.623  1.65
ATOM    484  CA  LEU A 211      18.426  33.111   9.499   3.156  1.87
ATOM    485  C   LEU A 211      18.875  34.122   8.447    .000  1.76
ATOM    486  O   LEU A 211      19.012  35.308   8.739   9.136  1.40
ATOM    487  CB  LEU A 211      19.645  32.369  10.045   8.519  1.87
ATOM    488  CG  LEU A 211      20.773  33.233  10.603   5.634  1.87
ATOM    489  CD1 LEU A 211      20.264  34.065  11.765   1.659  1.87
ATOM    490  CD2 LEU A 211      21.920  32.342  11.045  27.920  1.87
ATOM    491  N   GLU A 212      19.082  33.643   7.221    .000  1.65
ATOM    492  CA  GLU A 212      19.510  34.489   6.111   8.516  1.87
ATOM    493  C   GLU A 212      18.471  35.569   5.808    .000  1.76
ATOM    494  O   GLU A 212      18.816  36.740   5.636   2.850  1.40
ATOM    495  CB  GLU A 212      19.784  33.638   4.863  20.774  1.87
ATOM    496  CG  GLU A 212      21.035  32.751   4.953  39.133  1.87
ATOM    497  CD  GLU A 212      20.954  31.668   6.033   8.049  1.76
ATOM    498  OE1 GLU A 212      19.902  30.999   6.155  15.404  1.40
ATOM    499  OE2 GLU A 212      21.955  31.483   6.762  27.553  1.40
ATOM    500  N   GLU A 213      17.199  35.173   5.771    .000  1.65
ATOM    501  CA  GLU A 213      16.109  36.113   5.512   3.614  1.87
ATOM    502  C   GLU A 213      16.001  37.117   6.660   4.742  1.76
ATOM    503  O   GLU A 213      15.690  38.289   6.438   2.378  1.40
ATOM    504  CB  GLU A 213      14.787  35.364   5.300   5.119  1.87
ATOM    505  CG  GLU A 213      14.776  34.514   4.026  23.353  1.87
ATOM    506  CD  GLU A 213      13.539  33.638   3.893   9.592  1.76
ATOM    507  OE1 GLU A 213      13.220  32.890   4.838   5.575  1.40
ATOM    508  OE2 GLU A 213      12.888  33.683   2.829  41.810  1.40
ATOM    525  N   THR A 216      18.915  39.521   6.253  18.181  1.65
ATOM    526  CA  THR A 216      18.636  40.413   5.133   4.541  1.87
ATOM    527  C   THR A 216      17.640  41.485   5.571    .000  1.76
ATOM    528  O   THR A 216      17.807  42.666   5.263   4.862  1.40
ATOM    529  CB  THR A 216      18.050  39.641   3.929   2.891  1.87
ATOM    530  OG1 THR A 216      18.998  38.664   3.483  24.330  1.40
ATOM    531  CG2 THR A 216      17.730  40.596   2.778  50.916  1.87
ATOM    532  N   ALA A 217      16.631  41.064   6.328    .490  1.65
ATOM    533  CA  ALA A 217      15.593  41.963   6.816  11.315  1.87
ATOM    534  C   ALA A 217      16.104  43.052   7.759    .000  1.76
ATOM    535  O   ALA A 217      15.685  44.202   7.659  17.373  1.40
ATOM    536  CB  ALA A 217      14.486  41.158   7.488   7.550  1.87
ATOM    537  N   CYS A 218      17.033  42.701   8.645   1.066  1.65
ATOM    538  CA  CYS A 218      17.572  43.657   9.613   4.675  1.87
ATOM    539  C   CYS A 218      18.985  44.159   9.339    .904  1.76
ATOM    540  O   CYS A 218      19.634  44.683  10.245  10.457  1.40
ATOM    541  CB  CYS A 218      17.525  43.060  11.021   1.695  1.87
ATOM    542  SG  CYS A 218      15.855  42.777  11.680    .071  1.85
ATOM    543  N   GLN A 219      19.451  44.037   8.099    .778  1.65
ATOM    544  CA  GLN A 219      20.802  44.479   7.755   8.175  1.87
ATOM    545  C   GLN A 219      21.001  45.986   7.940    .000  1.76
ATOM    546  O   GLN A 219      20.066  46.772   7.786  21.956  1.40
ATOM    547  CB  GLN A 219      21.152  44.074   6.323  20.279  1.87
ATOM    548  CG  GLN A 219      20.421  44.863   5.251  16.063  1.87
ATOM    549  CD  GLN A 219      20.725  44.362   3.860   7.981  1.76
ATOM    550  OE1 GLN A 219      21.768  44.673   3.288  39.145  1.40
ATOM    551  NE2 GLN A 219      19.817  43.572   3.311  25.197  1.65
ATOM    552  N   GLY A 220      22.226  46.374   8.287   6.948  1.65
ATOM    553  CA  GLY A 220      22.536  47.781   8.491  35.358  1.87
ATOM    554  C   GLY A 220      23.683  48.032   9.461  12.927  1.76
ATOM    555  O   GLY A 220      24.328  47.057   9.907  15.193  1.40
ATOM    556  OXT GLY A 220      23.949  49.212   9.776  39.147  1.40