CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: EXAMPLE2

Input data for this run:

HEADER Maltodextrin bp

HEADER Maltodextrin binding protein
ATOM      1  N   LYS A   1     -12.621  27.691  51.154  1.00 87.40
ATOM      2  CA  LYS A   1     -12.341  26.198  51.153  1.00 87.46
ATOM      3  C   LYS A   1     -12.865  25.547  49.864  1.00 86.45
ATOM      4  O   LYS A   1     -12.310  24.601  49.210  1.00 86.78
ATOM      5  CB  LYS A   1     -12.846  25.664  52.487  1.00 87.70
ATOM      6  N   ILE A   2     -13.989  26.145  49.466  1.00 85.10
ATOM      7  CA  ILE A   2     -14.831  25.957  48.307  1.00 82.24
ATOM      8  C   ILE A   2     -15.288  24.505  48.119  1.00 80.03
ATOM      9  O   ILE A   2     -16.020  23.932  48.985  1.00 79.86
ATOM     10  CB  ILE A   2     -14.071  26.497  47.059  1.00 81.04
ATOM     11  N   GLU A   3     -14.808  24.006  46.994  1.00 75.95
ATOM     12  CA  GLU A   3     -15.046  22.628  46.522  1.00 72.52
ATOM     13  C   GLU A   3     -16.516  22.334  46.292  1.00 69.04
ATOM     14  O   GLU A   3     -17.058  22.773  45.193  1.00 69.11
ATOM     15  CB  GLU A   3     -14.129  21.719  47.409  1.00 71.61
ATOM     16  N   GLU A   4     -17.299  21.618  47.069  1.00 65.36
ATOM     17  CA  GLU A   4     -18.714  21.389  46.782  1.00 61.45
ATOM     18  C   GLU A   4     -19.341  20.296  47.651  1.00 59.14
ATOM     19  O   GLU A   4     -19.659  20.537  48.853  1.00 58.76
ATOM     20  CB  GLU A   4     -18.813  20.983  45.297  1.00 63.88
ATOM     21  N   GLY A   5     -19.530  19.202  46.959  1.00 55.20
ATOM     22  CA  GLY A   5     -19.972  17.870  47.059  1.00 52.46
ATOM     23  C   GLY A   5     -19.601  16.960  45.855  1.00 51.64
ATOM     24  O   GLY A   5     -20.237  16.004  45.374  1.00 51.78
ATOM     25  N   LYS A   6     -18.451  17.258  45.287  1.00 50.87
ATOM     26  CA  LYS A   6     -17.744  16.609  44.186  1.00 47.41
ATOM     27  C   LYS A   6     -16.265  16.450  44.595  1.00 44.94
ATOM     28  O   LYS A   6     -15.984  16.785  45.788  1.00 43.59
ATOM     29  CB  LYS A   6     -17.920  17.463  42.947  1.00 49.52
ATOM     30  CG  LYS A   6     -16.885  18.598  42.990  1.00 52.46
ATOM     31  CD  LYS A   6     -16.480  18.938  41.561  1.00 55.20
ATOM     32  CE  LYS A   6     -17.132  20.225  41.086  1.00 56.45
ATOM     33  NZ  LYS A   6     -16.020  21.174  40.677  1.00 58.97
ATOM     34  N   LEU A   7     -15.433  15.892  43.728  1.00 42.30
ATOM     35  CA  LEU A   7     -13.991  15.630  43.823  1.00 39.10
ATOM     36  C   LEU A   7     -13.205  16.243  42.650  1.00 36.75
ATOM     37  O   LEU A   7     -13.505  16.057  41.481  1.00 36.60
ATOM     38  CB  LEU A   7     -13.634  14.136  43.943  1.00 37.45
ATOM     39  CG  LEU A   7     -14.166  13.362  45.106  1.00 39.28
ATOM     40  CD1 LEU A   7     -13.737  11.918  45.219  1.00 38.12
ATOM     41  CD2 LEU A   7     -13.664  14.066  46.403  1.00 41.04
ATOM     42  N   VAL A   8     -12.187  17.031  42.859  1.00 34.90
ATOM     43  CA  VAL A   8     -11.288  17.626  41.815  1.00 31.67
ATOM     44  C   VAL A   8      -9.882  17.091  42.169  1.00 31.15
ATOM     45  O   VAL A   8      -9.462  17.109  43.371  1.00 28.51
ATOM     46  CB  VAL A   8     -11.578  19.114  41.813  1.00 31.66
ATOM     47  CG1 VAL A   8     -10.646  20.020  41.013  1.00 29.62
ATOM     48  CG2 VAL A   8     -13.007  19.352  41.412  1.00 33.16
ATOM     49  N   ILE A   9      -9.209  16.495  41.229  1.00 29.62
ATOM     50  CA  ILE A   9      -7.899  15.891  41.393  1.00 28.07
ATOM     51  C   ILE A   9      -6.925  16.579  40.475  1.00 25.92
ATOM     52  O   ILE A   9      -7.226  16.877  39.358  1.00 25.70
ATOM     53  CB  ILE A   9      -7.856  14.357  41.062  1.00 29.29
ATOM     54  CG1 ILE A   9      -8.904  13.659  41.998  1.00 31.89
ATOM     55  CG2 ILE A   9      -6.440  13.757  41.181  1.00 25.82
ATOM     56  CD1 ILE A   9      -9.486  12.274  41.659  1.00 29.23
ATOM     57  N   TRP A  10      -5.764  16.816  41.028  1.00 24.98
ATOM     58  CA  TRP A  10      -4.622  17.406  40.266  1.00 26.18
ATOM     59  C   TRP A  10      -3.477  16.376  40.225  1.00 25.37
ATOM     60  O   TRP A  10      -3.146  15.838  41.332  1.00 22.91
ATOM     61  CB  TRP A  10      -4.127  18.682  40.851  1.00 27.81
ATOM     62  CG  TRP A  10      -5.026  19.871  40.629  1.00 31.09
ATOM     63  CD1 TRP A  10      -6.343  20.013  40.219  1.00 29.15
ATOM     64  CD2 TRP A  10      -4.518  21.183  40.962  1.00 30.43
ATOM     65  NE1 TRP A  10      -6.664  21.356  40.229  1.00 32.09
ATOM     66  CE2 TRP A  10      -5.578  22.077  40.648  1.00 32.07
ATOM     67  CE3 TRP A  10      -3.311  21.602  41.524  1.00 30.41
ATOM     68  CZ2 TRP A  10      -5.379  23.434  40.869  1.00 34.46
ATOM     69  CZ3 TRP A  10      -3.101  22.952  41.739  1.00 28.99
ATOM     70  CH2 TRP A  10      -4.088  23.834  41.363  1.00 31.93
ATOM     71  N   ILE A  11      -3.012  16.060  39.014  1.00 22.92
ATOM     72  CA  ILE A  11      -1.912  15.068  38.860  1.00 20.90
ATOM     73  C   ILE A  11      -1.049  15.651  37.758  1.00 21.05
ATOM     74  O   ILE A  11      -1.514  16.506  37.026  1.00 23.35
ATOM     75  CB  ILE A  11      -2.545  13.679  38.583  1.00 19.59
ATOM     76  CG1 ILE A  11      -1.444  12.650  38.426  1.00 21.24
ATOM     77  CG2 ILE A  11      -3.380  13.755  37.310  1.00 24.06
ATOM     78  CD1 ILE A  11      -1.834  11.172  38.530  1.00 23.01
ATOM     79  N   ASN A  12       0.207  15.395  37.691  1.00 22.27
ATOM     80  CA  ASN A  12       1.192  15.821  36.714  1.00 21.93
ATOM     81  C   ASN A  12       0.771  15.179  35.360  1.00 23.41
ATOM     82  O   ASN A  12       0.235  14.074  35.194  1.00 24.07
ATOM     83  CB  ASN A  12       2.636  15.476  37.061  1.00 20.71
ATOM     84  CG  ASN A  12       3.544  16.517  36.370  1.00 23.03
ATOM     85  OD1 ASN A  12       3.174  17.701  36.311  1.00 26.41
ATOM     86  ND2 ASN A  12       4.723  16.170  35.940  1.00 23.71
ATOM     87  N   GLY A  13       1.121  15.974  34.373  1.00 22.90
ATOM     88  CA  GLY A  13       0.873  15.748  32.971  1.00 25.54
ATOM     89  C   GLY A  13       1.610  14.531  32.429  1.00 25.45
ATOM     90  O   GLY A  13       1.055  14.041  31.415  1.00 25.69
ATOM     91  N   ASP A  14       2.724  14.120  33.075  1.00 22.83
ATOM     92  CA  ASP A  14       3.387  12.920  32.595  1.00 22.35
ATOM     93  C   ASP A  14       2.817  11.618  33.199  1.00 22.69
ATOM     94  O   ASP A  14       3.325  10.556  32.783  1.00 24.80
ATOM     95  CB  ASP A  14       4.919  13.055  32.811  1.00 23.85
ATOM     96  CG  ASP A  14       5.269  13.270  34.283  1.00 25.78
ATOM     97  OD1 ASP A  14       4.326  13.325  35.094  1.00 21.27
ATOM     98  OD2 ASP A  14       6.468  13.454  34.625  1.00 27.63
ATOM     99  N   LYS A  15       1.748  11.621  33.974  1.00 20.08
ATOM    100  CA  LYS A  15       1.187  10.437  34.615  1.00 21.33
ATOM    101  C   LYS A  15      -0.058   9.987  33.887  1.00 20.90
ATOM    102  O   LYS A  15      -0.584  10.797  33.113  1.00 19.17
ATOM    103  CB  LYS A  15       0.916  10.766  36.160  1.00 16.97
ATOM    104  CG  LYS A  15       2.112  11.574  36.829  1.00 16.21
ATOM    105  CD  LYS A  15       3.294  10.615  36.574  1.00 18.66
ATOM    106  CE  LYS A  15       4.338  10.472  37.605  1.00 19.34
ATOM    107  NZ  LYS A  15       5.097  11.684  37.729  1.00 23.84
ATOM    108  N   GLY A  16      -0.632   8.797  34.189  1.00 22.97
ATOM    109  CA  GLY A  16      -1.825   8.421  33.448  1.00 24.44
ATOM    110  C   GLY A  16      -3.110   8.966  34.013  1.00 26.25
ATOM    111  O   GLY A  16      -3.995   8.283  34.640  1.00 26.82
ATOM    112  N   TYR A  17      -3.301  10.272  33.730  1.00 28.41
ATOM    113  CA  TYR A  17      -4.499  11.014  34.121  1.00 27.27
ATOM    114  C   TYR A  17      -5.729  10.473  33.399  1.00 29.24
ATOM    115  O   TYR A  17      -6.861  10.615  33.954  1.00 32.36
ATOM    116  CB  TYR A  17      -4.311  12.515  33.900  1.00 28.29
ATOM    117  CG  TYR A  17      -3.775  12.958  32.579  1.00 26.73
ATOM    118  CD1 TYR A  17      -4.721  13.135  31.554  1.00 30.37
ATOM    119  CD2 TYR A  17      -2.488  13.347  32.321  1.00 29.24
ATOM    120  CE1 TYR A  17      -4.357  13.643  30.309  1.00 27.34
ATOM    121  CE2 TYR A  17      -2.074  13.825  31.060  1.00 30.71
ATOM    122  CZ  TYR A  17      -3.031  13.938  30.057  1.00 30.99
ATOM    123  OH  TYR A  17      -2.749  14.415  28.771  1.00 33.39
ATOM    124  N   ASN A  18      -5.581   9.852  32.216  1.00 28.96
ATOM    125  CA  ASN A  18      -6.817   9.297  31.595  1.00 29.37
ATOM    126  C   ASN A  18      -7.081   8.001  32.377  1.00 29.76
ATOM    127  O   ASN A  18      -8.272   7.779  32.633  1.00 31.92
ATOM    128  CB  ASN A  18      -6.738   9.196  30.080  1.00 29.90
ATOM    129  CG  ASN A  18      -6.781  10.499  29.351  1.00 30.67
ATOM    130  OD1 ASN A  18      -6.031  10.844  28.439  1.00 33.03
ATOM    131  ND2 ASN A  18      -7.597  11.464  29.807  1.00 35.38
ATOM    132  N   GLY A  19      -6.146   7.157  32.816  1.00 27.54
ATOM    133  CA  GLY A  19      -6.523   6.007  33.584  1.00 26.01
ATOM    134  C   GLY A  19      -7.258   6.452  34.844  1.00 25.64
ATOM    135  O   GLY A  19      -8.164   5.768  35.373  1.00 25.49
ATOM    136  N   LEU A  20      -6.754   7.525  35.399  1.00 25.51
ATOM    137  CA  LEU A  20      -7.281   8.121  36.667  1.00 27.47
ATOM    138  C   LEU A  20      -8.708   8.566  36.419  1.00 28.32
ATOM    139  O   LEU A  20      -9.512   8.237  37.285  1.00 30.79
ATOM    140  CB  LEU A  20      -6.335   9.204  37.314  1.00 25.82
ATOM    141  CG  LEU A  20      -6.772   9.764  38.717  1.00 27.48
ATOM    142  CD1 LEU A  20      -6.867   8.694  39.754  1.00 24.39
ATOM    143  CD2 LEU A  20      -5.797  10.844  39.144  1.00 26.48
ATOM    144  N   ALA A  21      -8.985   9.269  35.378  1.00 31.50
ATOM    145  CA  ALA A  21     -10.320   9.674  34.936  1.00 33.85
ATOM    146  C   ALA A  21     -11.226   8.452  34.762  1.00 37.10
ATOM    147  O   ALA A  21     -12.414   8.612  35.224  1.00 38.89
ATOM    148  CB  ALA A  21     -10.253  10.485  33.655  1.00 34.38
ATOM    149  N   GLU A  22     -10.835   7.290  34.265  1.00 37.84
ATOM    150  CA  GLU A  22     -11.620   6.057  34.117  1.00 38.63
ATOM    151  C   GLU A  22     -11.995   5.543  35.496  1.00 39.37
ATOM    152  O   GLU A  22     -13.028   4.851  35.781  1.00 38.99
ATOM    153  CB  GLU A  22     -10.933   4.924  33.358  1.00 44.36
ATOM    154  CG  GLU A  22     -10.322   5.082  31.972  1.00 52.64
ATOM    155  CD  GLU A  22      -9.165   4.213  31.486  1.00 57.81
ATOM    156  OE1 GLU A  22      -9.075   3.012  31.846  1.00 61.61
ATOM    157  OE2 GLU A  22      -8.277   4.705  30.656  1.00 56.89
ATOM    158  N   VAL A  23     -11.077   5.791  36.448  1.00 37.01
ATOM    159  CA  VAL A  23     -11.375   5.411  37.822  1.00 37.32
ATOM    160  C   VAL A  23     -12.341   6.425  38.421  1.00 38.16
ATOM    161  O   VAL A  23     -13.289   6.027  39.139  1.00 40.42
ATOM    162  CB  VAL A  23     -10.088   5.170  38.645  1.00 36.43
ATOM    163  CG1 VAL A  23     -10.510   4.728  40.081  1.00 34.87
ATOM    164  CG2 VAL A  23      -9.195   4.304  37.828  1.00 31.98
ATOM    165  N   GLY A  24     -12.275   7.706  38.171  1.00 38.13
ATOM    166  CA  GLY A  24     -13.301   8.585  38.731  1.00 39.86
ATOM    167  C   GLY A  24     -14.716   8.186  38.304  1.00 41.89
ATOM    168  O   GLY A  24     -15.716   8.293  39.023  1.00 41.79
ATOM    169  N   LYS A  25     -14.778   7.749  37.062  1.00 44.67
ATOM    170  CA  LYS A  25     -15.980   7.351  36.343  1.00 46.41
ATOM    171  C   LYS A  25     -16.765   6.249  37.009  1.00 45.92
ATOM    172  O   LYS A  25     -17.992   6.367  36.983  1.00 46.99
ATOM    173  CB  LYS A  25     -15.739   6.897  34.879  1.00 47.96
ATOM    174  CG  LYS A  25     -15.733   8.202  34.069  1.00 50.20
ATOM    175  CD  LYS A  25     -15.846   7.994  32.583  1.00 55.40
ATOM    176  CE  LYS A  25     -16.630   6.820  32.052  1.00 57.98
ATOM    177  NZ  LYS A  25     -16.646   6.784  30.534  1.00 58.56
ATOM    178  N   LYS A  26     -16.096   5.278  37.536  1.00 45.84
ATOM    179  CA  LYS A  26     -16.853   4.214  38.198  1.00 47.97
ATOM    180  C   LYS A  26     -16.894   4.634  39.649  1.00 50.69
ATOM    181  O   LYS A  26     -17.203   3.780  40.539  1.00 54.70
ATOM    182  CB  LYS A  26     -16.322   2.822  37.883  1.00 46.57
ATOM    183  CG  LYS A  26     -15.234   2.281  38.738  1.00 47.35
ATOM    184  CD  LYS A  26     -15.127   0.818  38.861  1.00 51.79
ATOM    185  CE  LYS A  26     -16.078   0.118  39.827  1.00 54.95
ATOM    186  NZ  LYS A  26     -17.525   0.505  39.603  1.00 58.04
ATOM    187  N   PHE A  27     -16.518   5.884  39.968  1.00 49.17
ATOM    188  CA  PHE A  27     -16.617   6.193  41.436  1.00 47.47
ATOM    189  C   PHE A  27     -18.061   6.734  41.520  1.00 49.79
ATOM    190  O   PHE A  27     -18.953   6.417  42.314  1.00 48.83
ATOM    191  CB  PHE A  27     -15.540   7.136  41.940  1.00 42.14
ATOM    192  CG  PHE A  27     -15.792   7.593  43.366  1.00 37.02
ATOM    193  CD1 PHE A  27     -15.649   6.690  44.410  1.00 36.81
ATOM    194  CD2 PHE A  27     -16.157   8.897  43.633  1.00 35.18
ATOM    195  CE1 PHE A  27     -15.929   7.034  45.743  1.00 36.23
ATOM    196  CE2 PHE A  27     -16.366   9.281  44.953  1.00 32.89
ATOM    197  CZ  PHE A  27     -16.274   8.381  45.982  1.00 31.41
ATOM    198  N   GLU A  28     -18.199   7.594  40.510  1.00 51.63
ATOM    199  CA  GLU A  28     -19.358   8.408  40.199  1.00 55.22
ATOM    200  C   GLU A  28     -20.653   7.741  39.722  1.00 56.05
ATOM    201  O   GLU A  28     -21.822   8.128  39.972  1.00 54.35
ATOM    202  CB  GLU A  28     -18.945   9.386  39.104  1.00 54.62
ATOM    203  CG  GLU A  28     -20.074   9.733  38.122  1.00 59.09
ATOM    204  CD  GLU A  28     -19.576  10.855  37.273  1.00 62.34
ATOM    205  OE1 GLU A  28     -18.358  11.034  37.600  1.00 68.34
ATOM    206  OE2 GLU A  28     -20.132  11.497  36.445  1.00 65.27
ATOM    207  N   LYS A  29     -20.411   6.693  38.990  1.00 57.70
ATOM    208  CA  LYS A  29     -21.423   5.799  38.394  1.00 59.47
ATOM    209  C   LYS A  29     -21.898   4.951  39.573  1.00 59.49
ATOM    210  O   LYS A  29     -23.021   4.392  39.530  1.00 61.64
ATOM    211  CB  LYS A  29     -20.793   5.003  37.267  1.00 59.69
ATOM    212  CG  LYS A  29     -21.508   4.249  36.202  1.00 60.83
ATOM    213  CD  LYS A  29     -20.691   3.104  35.571  1.00 62.02
ATOM    214  CE  LYS A  29     -21.596   2.158  34.772  1.00 62.52
ATOM    215  NZ  LYS A  29     -20.805   1.224  33.938  1.00 62.32
ATOM    216  N   ASP A  30     -21.071   4.947  40.613  1.00 58.71
ATOM    217  CA  ASP A  30     -21.409   4.047  41.801  1.00 58.37
ATOM    218  C   ASP A  30     -21.657   4.907  43.016  1.00 57.60
ATOM    219  O   ASP A  30     -21.922   4.458  44.175  1.00 58.59
ATOM    220  CB  ASP A  30     -20.373   2.947  41.776  1.00 59.61
ATOM    221  CG  ASP A  30     -19.648   2.188  42.790  1.00 59.90
ATOM    222  OD1 ASP A  30     -19.749   2.631  43.971  1.00 63.11
ATOM    223  OD2 ASP A  30     -18.905   1.165  42.629  1.00 59.45
ATOM    224  N   THR A  31     -21.696   6.212  42.735  1.00 54.82
ATOM    225  CA  THR A  31     -21.886   7.060  43.910  1.00 53.63
ATOM    226  C   THR A  31     -22.646   8.330  43.732  1.00 53.55
ATOM    227  O   THR A  31     -23.122   8.854  44.778  1.00 56.25
ATOM    228  CB  THR A  31     -20.358   7.462  44.317  1.00 51.55
ATOM    229  OG1 THR A  31     -20.272   7.452  45.740  1.00 49.91
ATOM    230  CG2 THR A  31     -20.003   8.781  43.626  1.00 47.77
ATOM    231  N   GLY A  32     -22.666   8.868  42.542  1.00 51.51
ATOM    232  CA  GLY A  32     -23.250  10.163  42.263  1.00 51.98
ATOM    233  C   GLY A  32     -22.287  11.347  42.432  1.00 52.91
ATOM    234  O   GLY A  32     -22.644  12.559  42.128  1.00 54.34
ATOM    235  N   ILE A  33     -21.061  11.065  42.966  1.00 50.58
ATOM    236  CA  ILE A  33     -20.121  12.160  43.122  1.00 48.58
ATOM    237  C   ILE A  33     -19.304  12.135  41.824  1.00 46.88
ATOM    238  O   ILE A  33     -18.671  11.081  41.699  1.00 48.28
ATOM    239  CB  ILE A  33     -19.039  12.115  44.221  1.00 50.17
ATOM    240  CG1 ILE A  33     -19.630  12.085  45.653  1.00 50.93
ATOM    241  CG2 ILE A  33     -18.071  13.314  44.021  1.00 51.02
ATOM    242  CD1 ILE A  33     -20.086  10.599  45.995  1.00 51.53
ATOM    243  N   LYS A  34     -19.361  13.185  41.080  1.00 45.92
ATOM    244  CA  LYS A  34     -18.547  13.180  39.865  1.00 45.89
ATOM    245  C   LYS A  34     -17.117  13.674  40.216  1.00 44.95
ATOM    246  O   LYS A  34     -16.806  14.678  40.920  1.00 41.15
ATOM    247  CB  LYS A  34     -19.117  14.059  38.767  1.00 49.13
ATOM    248  CG  LYS A  34     -18.367  15.403  38.760  1.00 56.49
ATOM    249  CD  LYS A  34     -19.062  16.564  38.093  1.00 61.90
ATOM    250  CE  LYS A  34     -20.029  17.360  38.985  1.00 65.71
ATOM    251  NZ  LYS A  34     -21.411  16.740  39.074  1.00 66.82
ATOM    252  N   VAL A  35     -16.205  12.938  39.551  1.00 43.61
ATOM    253  CA  VAL A  35     -14.776  13.307  39.734  1.00 42.37
ATOM    254  C   VAL A  35     -14.243  14.043  38.531  1.00 42.66
ATOM    255  O   VAL A  35     -14.602  13.449  37.468  1.00 47.18
ATOM    256  CB  VAL A  35     -14.016  12.007  40.007  1.00 40.92
ATOM    257  CG1 VAL A  35     -12.548  12.383  40.292  1.00 40.88
ATOM    258  CG2 VAL A  35     -14.746  11.250  41.091  1.00 37.39
ATOM    259  N   THR A  36     -13.519  15.116  38.629  1.00 39.49
ATOM    260  CA  THR A  36     -12.892  15.922  37.634  1.00 38.66
ATOM    261  C   THR A  36     -11.333  15.794  37.753  1.00 39.37
ATOM    262  O   THR A  36     -10.790  16.204  38.801  1.00 39.74
ATOM    263  CB  THR A  36     -13.203  17.469  37.696  1.00 39.53
ATOM    264  OG1 THR A  36     -14.639  17.672  37.533  1.00 41.87
ATOM    265  CG2 THR A  36     -12.385  18.279  36.675  1.00 38.81
ATOM    266  N   VAL A  37     -10.588  15.348  36.773  1.00 38.11
ATOM    267  CA  VAL A  37      -9.151  15.159  36.795  1.00 37.21
ATOM    268  C   VAL A  37      -8.405  16.224  36.071  1.00 37.58
ATOM    269  O   VAL A  37      -8.695  16.308  34.862  1.00 40.64
ATOM    270  CB  VAL A  37      -8.803  13.772  36.187  1.00 36.33
ATOM    271  CG1 VAL A  37      -7.342  13.628  35.835  1.00 34.76
ATOM    272  CG2 VAL A  37      -9.260  12.703  37.160  1.00 35.47
ATOM    273  N   GLU A  38      -7.536  17.008  36.705  1.00 37.81
ATOM    274  CA  GLU A  38      -6.822  18.046  35.929  1.00 37.54
ATOM    275  C   GLU A  38      -5.322  17.851  36.109  1.00 36.54
ATOM    276  O   GLU A  38      -5.004  17.236  37.161  1.00 35.30
ATOM    277  CB  GLU A  38      -7.100  19.475  36.410  1.00 42.10
ATOM    278  CG  GLU A  38      -8.606  19.621  36.652  1.00 48.97
ATOM    279  CD  GLU A  38      -9.090  21.021  36.748  1.00 54.04
ATOM    280  OE1 GLU A  38      -8.351  21.948  37.040  1.00 58.98
ATOM    281  OE2 GLU A  38     -10.310  21.134  36.486  1.00 57.77
ATOM    282  N   HIS A  39      -4.620  18.377  35.132  1.00 32.21
ATOM    283  CA  HIS A  39      -3.146  18.326  35.153  1.00 31.14
ATOM    284  C   HIS A  39      -2.525  19.664  34.788  1.00 31.86
ATOM    285  O   HIS A  39      -1.823  19.795  33.737  1.00 31.29
ATOM    286  CB  HIS A  39      -2.518  17.196  34.289  1.00 30.01
ATOM    287  CG  HIS A  39      -3.069  17.208  32.920  1.00 31.38
ATOM    288  ND1 HIS A  39      -2.422  17.787  31.844  1.00 32.40
ATOM    289  CD2 HIS A  39      -4.303  16.792  32.483  1.00 32.92
ATOM    290  CE1 HIS A  39      -3.228  17.663  30.781  1.00 33.89
ATOM    291  NE2 HIS A  39      -4.353  17.064  31.106  1.00 31.74
ATOM    292  N   PRO A  40      -2.695  20.635  35.698  1.00 32.50
ATOM    293  CA  PRO A  40      -2.128  21.967  35.495  1.00 32.60
ATOM    294  C   PRO A  40      -0.641  21.868  35.449  1.00 33.22
ATOM    295  O   PRO A  40      -0.036  21.008  36.085  1.00 32.04
ATOM    296  CB  PRO A  40      -2.633  22.838  36.644  1.00 33.52
ATOM    297  CG  PRO A  40      -3.333  21.912  37.615  1.00 32.90
ATOM    298  CD  PRO A  40      -3.486  20.572  36.954  1.00 33.56
ATOM    299  N   ASP A  41      -0.059  22.802  34.710  1.00 36.01
ATOM    300  CA  ASP A  41       1.436  22.944  34.589  1.00 38.31
ATOM    301  C   ASP A  41       2.053  23.408  35.910  1.00 35.17
ATOM    302  O   ASP A  41       1.324  24.217  36.593  1.00 35.53
ATOM    303  CB  ASP A  41       1.641  23.960  33.450  1.00 47.84
ATOM    304  CG  ASP A  41       1.500  23.440  32.047  1.00 54.62
ATOM    305  OD1 ASP A  41       0.434  23.106  31.476  1.00 59.16
ATOM    306  OD2 ASP A  41       2.641  23.384  31.484  1.00 58.65
ATOM    307  N   LYS A  42       3.232  23.082  36.370  1.00 33.34
ATOM    308  CA  LYS A  42       3.651  23.612  37.691  1.00 32.73
ATOM    309  C   LYS A  42       2.669  23.350  38.796  1.00 32.19
ATOM    310  O   LYS A  42       2.411  24.250  39.676  1.00 32.46
ATOM    311  CB  LYS A  42       3.597  25.175  37.666  1.00 33.24
ATOM    312  CG  LYS A  42       5.012  25.630  37.477  1.00 36.74
ATOM    313  CD  LYS A  42       5.446  25.265  36.082  1.00 39.35
ATOM    314  CE  LYS A  42       6.976  25.289  36.013  1.00 43.17
ATOM    315  NZ  LYS A  42       7.392  25.944  34.660  1.00 49.31
ATOM    316  N   LEU A  43       1.997  22.222  38.782  1.00 31.74
ATOM    317  CA  LEU A  43       0.944  22.136  39.861  1.00 31.34
ATOM    318  C   LEU A  43       1.543  22.124  41.272  1.00 31.59
ATOM    319  O   LEU A  43       0.815  22.450  42.205  1.00 31.22
ATOM    320  CB  LEU A  43       0.128  20.886  39.547  1.00 31.10
ATOM    321  CG  LEU A  43       0.703  19.526  39.869  1.00 27.90
ATOM    322  CD1 LEU A  43       0.281  19.177  41.272  1.00 29.18
ATOM    323  CD2 LEU A  43       0.048  18.543  38.915  1.00 29.24
ATOM    324  N   GLU A  44       2.776  21.635  41.296  1.00 32.19
ATOM    325  CA  GLU A  44       3.448  21.420  42.587  1.00 33.24
ATOM    326  C   GLU A  44       3.793  22.736  43.264  1.00 34.27
ATOM    327  O   GLU A  44       4.055  22.890  44.405  1.00 30.98
ATOM    328  CB  GLU A  44       4.752  20.666  42.401  1.00 33.70
ATOM    329  CG  GLU A  44       5.962  21.332  41.808  1.00 33.18
ATOM    330  CD  GLU A  44       6.067  21.554  40.329  1.00 35.04
ATOM    331  OE1 GLU A  44       4.969  21.525  39.685  1.00 34.36
ATOM    332  OE2 GLU A  44       7.190  21.792  39.879  1.00 37.69
ATOM    333  N   GLU A  45       3.796  23.692  42.374  1.00 35.93
ATOM    334  CA  GLU A  45       4.027  25.119  42.646  1.00 36.94
ATOM    335  C   GLU A  45       2.709  25.833  42.796  1.00 36.65
ATOM    336  O   GLU A  45       2.489  26.624  43.737  1.00 36.65
ATOM    337  CB  GLU A  45       4.782  25.472  41.402  1.00 41.66
ATOM    338  CG  GLU A  45       4.826  26.869  40.956  1.00 46.66
ATOM    339  CD  GLU A  45       6.322  27.206  40.772  1.00 51.81
ATOM    340  OE1 GLU A  45       7.034  26.156  40.908  1.00 50.62
ATOM    341  OE2 GLU A  45       6.426  28.432  40.554  1.00 54.95
ATOM    342  N   LYS A  46       1.758  25.547  41.913  1.00 36.02
ATOM    343  CA  LYS A  46       0.466  26.160  41.953  1.00 35.83
ATOM    344  C   LYS A  46      -0.230  25.690  43.197  1.00 36.24
ATOM    345  O   LYS A  46      -0.981  26.527  43.707  1.00 38.78
ATOM    346  CB  LYS A  46      -0.459  25.800  40.789  1.00 41.42
ATOM    347  CG  LYS A  46      -0.207  26.535  39.472  1.00 48.85
ATOM    348  CD  LYS A  46       1.097  27.346  39.521  1.00 55.09
ATOM    349  CE  LYS A  46       1.573  28.134  38.286  1.00 56.83
ATOM    350  NZ  LYS A  46       2.666  29.121  38.737  1.00 56.90
ATOM    351  N   PHE A  47      -0.127  24.451  43.673  1.00 34.63
ATOM    352  CA  PHE A  47      -0.920  24.037  44.822  1.00 32.93
ATOM    353  C   PHE A  47      -0.864  24.921  46.075  1.00 35.37
ATOM    354  O   PHE A  47      -1.919  25.259  46.679  1.00 33.33
ATOM    355  CB  PHE A  47      -0.636  22.545  45.199  1.00 30.79
ATOM    356  CG  PHE A  47      -1.468  22.035  46.357  1.00 26.75
ATOM    357  CD1 PHE A  47      -2.843  21.842  46.245  1.00 27.45
ATOM    358  CD2 PHE A  47      -0.892  21.852  47.596  1.00 26.34
ATOM    359  CE1 PHE A  47      -3.539  21.447  47.382  1.00 28.71
ATOM    360  CE2 PHE A  47      -1.587  21.417  48.716  1.00 26.08
ATOM    361  CZ  PHE A  47      -2.950  21.244  48.641  1.00 26.87
ATOM    362  N   PRO A  48       0.366  25.197  46.525  1.00 37.90
ATOM    363  CA  PRO A  48       0.557  25.929  47.799  1.00 39.27
ATOM    364  C   PRO A  48      -0.070  27.308  47.664  1.00 41.00
ATOM    365  O   PRO A  48      -0.597  27.836  48.650  1.00 39.75
ATOM    366  CB  PRO A  48       2.056  25.901  48.093  1.00 38.29
ATOM    367  CG  PRO A  48       2.745  25.218  46.947  1.00 37.27
ATOM    368  CD  PRO A  48       1.675  24.829  45.930  1.00 37.84
ATOM    369  N   GLN A  49       0.040  27.797  46.397  1.00 42.28
ATOM    370  CA  GLN A  49      -0.524  29.123  46.160  1.00 44.96
ATOM    371  C   GLN A  49      -2.040  29.116  46.316  1.00 45.74
ATOM    372  O   GLN A  49      -2.540  29.957  47.116  1.00 48.98
ATOM    373  CB  GLN A  49      -0.176  29.734  44.839  1.00 48.52
ATOM    374  CG  GLN A  49       1.298  29.811  44.468  1.00 55.95
ATOM    375  CD  GLN A  49       1.394  30.293  43.003  1.00 61.29
ATOM    376  OE1 GLN A  49       2.474  30.719  42.552  1.00 65.13
ATOM    377  NE2 GLN A  49       0.248  30.249  42.275  1.00 61.81
ATOM    378  N   VAL A  50      -2.797  28.357  45.579  1.00 45.27
ATOM    379  CA  VAL A  50      -4.250  28.352  45.668  1.00 43.59
ATOM    380  C   VAL A  50      -4.740  27.665  46.926  1.00 43.02
ATOM    381  O   VAL A  50      -5.836  28.142  47.309  1.00 43.66
ATOM    382  CB  VAL A  50      -4.903  27.652  44.448  1.00 44.15
ATOM    383  CG1 VAL A  50      -4.205  27.955  43.145  1.00 44.46
ATOM    384  CG2 VAL A  50      -4.979  26.143  44.744  1.00 46.50
ATOM    385  N   ALA A  51      -4.031  26.669  47.469  1.00 41.85
ATOM    386  CA  ALA A  51      -4.557  25.966  48.663  1.00 41.49
ATOM    387  C   ALA A  51      -4.499  26.832  49.931  1.00 43.35
ATOM    388  O   ALA A  51      -5.193  26.649  50.964  1.00 41.26
ATOM    389  CB  ALA A  51      -3.825  24.629  48.879  1.00 39.05
ATOM    390  N   ALA A  52      -3.510  27.721  49.817  1.00 44.99
ATOM    391  CA  ALA A  52      -3.177  28.647  50.913  1.00 48.40
ATOM    392  C   ALA A  52      -4.415  29.494  51.168  1.00 51.82
ATOM    393  O   ALA A  52      -4.794  29.746  52.330  1.00 54.18
ATOM    394  CB  ALA A  52      -1.914  29.364  50.473  1.00 48.76
ATOM    395  N   THR A  53      -5.111  29.848  50.063  1.00 53.18
ATOM    396  CA  THR A  53      -6.349  30.628  50.036  1.00 51.99
ATOM    397  C   THR A  53      -7.531  29.712  50.391  1.00 51.61
ATOM    398  O   THR A  53      -8.669  30.191  50.286  1.00 53.19
ATOM    399  CB  THR A  53      -6.767  31.313  48.685  1.00 48.21
ATOM    400  OG1 THR A  53      -7.591  30.242  48.096  1.00 48.17
ATOM    401  CG2 THR A  53      -5.718  31.667  47.652  1.00 50.73
ATOM    402  N   GLY A  54      -7.262  28.490  50.767  1.00 51.76
ATOM    403  CA  GLY A  54      -8.430  27.652  51.115  1.00 52.79
ATOM    404  C   GLY A  54      -9.058  27.081  49.864  1.00 54.12
ATOM    405  O   GLY A  54     -10.132  26.463  50.058  1.00 54.17
ATOM    406  N   ASP A  55      -8.423  27.250  48.662  1.00 53.96
ATOM    407  CA  ASP A  55      -9.126  26.518  47.503  1.00 52.44
ATOM    408  C   ASP A  55      -8.201  25.438  46.912  1.00 50.08
ATOM    409  O   ASP A  55      -7.499  24.726  47.732  1.00 49.50
ATOM    410  CB  ASP A  55      -9.852  27.522  46.690  1.00 56.84
ATOM    411  CG  ASP A  55      -9.174  28.495  45.803  1.00 59.58
ATOM    412  OD1 ASP A  55      -8.186  28.203  45.105  1.00 63.13
ATOM    413  OD2 ASP A  55      -9.687  29.644  45.769  1.00 62.01
ATOM    414  N   GLY A  56      -8.221  25.180  45.595  1.00 46.98
ATOM    415  CA  GLY A  56      -7.368  24.152  44.925  1.00 42.30
ATOM    416  C   GLY A  56      -8.096  22.848  44.742  1.00 38.39
ATOM    417  O   GLY A  56      -9.339  22.935  44.812  1.00 39.81
ATOM    418  N   PRO A  57      -7.415  21.707  44.517  1.00 35.33
ATOM    419  CA  PRO A  57      -8.074  20.424  44.333  1.00 32.90
ATOM    420  C   PRO A  57      -8.468  19.832  45.643  1.00 31.43
ATOM    421  O   PRO A  57      -7.997  20.229  46.732  1.00 32.83
ATOM    422  CB  PRO A  57      -6.988  19.527  43.613  1.00 31.23
ATOM    423  CG  PRO A  57      -5.701  20.038  44.158  1.00 29.61
ATOM    424  CD  PRO A  57      -5.945  21.517  44.373  1.00 33.32
ATOM    425  N   ASP A  58      -9.340  18.884  45.696  1.00 30.53
ATOM    426  CA  ASP A  58      -9.684  18.125  46.900  1.00 31.94
ATOM    427  C   ASP A  58      -8.448  17.222  47.212  1.00 30.94
ATOM    428  O   ASP A  58      -8.072  16.970  48.366  1.00 28.83
ATOM    429  CB  ASP A  58     -10.971  17.287  46.759  1.00 35.52
ATOM    430  CG  ASP A  58     -12.234  18.155  46.643  1.00 36.53
ATOM    431  OD1 ASP A  58     -12.636  18.580  45.549  1.00 38.16
ATOM    432  OD2 ASP A  58     -12.712  18.421  47.788  1.00 40.41
ATOM    433  N   ILE A  59      -7.895  16.663  46.090  1.00 30.61
ATOM    434  CA  ILE A  59      -6.739  15.737  46.132  1.00 29.60
ATOM    435  C   ILE A  59      -5.663  16.128  45.108  1.00 27.63
ATOM    436  O   ILE A  59      -5.849  16.574  43.998  1.00 27.14
ATOM    437  CB  ILE A  59      -7.159  14.233  46.233  1.00 30.99
ATOM    438  CG1 ILE A  59      -6.049  13.418  45.499  1.00 27.52
ATOM    439  CG2 ILE A  59      -8.547  13.567  45.913  1.00 30.80
ATOM    440  CD1 ILE A  59      -6.401  11.914  45.668  1.00 32.51
ATOM    441  N   ILE A  60      -4.409  16.076  45.613  1.00 26.46
ATOM    442  CA  ILE A  60      -3.167  16.380  44.990  1.00 24.02
ATOM    443  C   ILE A  60      -2.205  15.196  45.019  1.00 22.46
ATOM    444  O   ILE A  60      -1.895  14.549  45.997  1.00 21.01
ATOM    445  CB  ILE A  60      -2.509  17.640  45.680  1.00 27.12
ATOM    446  CG1 ILE A  60      -1.269  18.093  44.857  1.00 27.26
ATOM    447  CG2 ILE A  60      -2.139  17.412  47.152  1.00 24.57
ATOM    448  CD1 ILE A  60      -1.800  18.935  43.613  1.00 32.92
ATOM    449  N   PHE A  61      -1.676  14.951  43.817  1.00 21.00
ATOM    450  CA  PHE A  61      -0.695  13.891  43.581  1.00 22.36
ATOM    451  C   PHE A  61       0.680  14.554  43.161  1.00 21.10
ATOM    452  O   PHE A  61       0.655  15.414  42.242  1.00 21.30
ATOM    453  CB  PHE A  61      -1.009  12.930  42.438  1.00 20.87
ATOM    454  CG  PHE A  61      -2.182  12.051  42.634  1.00 19.64
ATOM    455  CD1 PHE A  61      -3.472  12.472  42.634  1.00 18.74
ATOM    456  CD2 PHE A  61      -1.883  10.653  42.762  1.00 25.39
ATOM    457  CE1 PHE A  61      -4.523  11.573  42.824  1.00 21.61
ATOM    458  CE2 PHE A  61      -2.985   9.743  42.957  1.00 26.29
ATOM    459  CZ  PHE A  61      -4.304  10.189  42.993  1.00 21.81
ATOM    460  N   TRP A  62       1.697  14.114  43.902  1.00 18.91
ATOM    461  CA  TRP A  62       3.065  14.518  43.584  1.00 16.85
ATOM    462  C   TRP A  62       3.960  13.459  44.244  1.00 18.31
ATOM    463  O   TRP A  62       3.397  12.618  45.002  1.00 18.36
ATOM    464  CB  TRP A  62       3.347  16.007  43.934  1.00 17.63
ATOM    465  CG  TRP A  62       4.719  16.469  43.306  1.00 17.52
ATOM    466  CD1 TRP A  62       5.937  16.436  43.813  1.00 15.19
ATOM    467  CD2 TRP A  62       4.888  16.968  41.952  1.00 16.34
ATOM    468  NE1 TRP A  62       6.865  16.898  42.917  1.00 17.65
ATOM    469  CE2 TRP A  62       6.236  17.202  41.761  1.00 18.48
ATOM    470  CE3 TRP A  62       3.946  17.170  40.925  1.00 20.09
ATOM    471  CZ2 TRP A  62       6.790  17.735  40.576  1.00 18.35
ATOM    472  CZ3 TRP A  62       4.463  17.729  39.753  1.00 19.41
ATOM    473  CH2 TRP A  62       5.852  17.938  39.606  1.00 20.02
ATOM    474  N   ALA A  63       5.291  13.431  43.885  1.00 16.89
ATOM    475  CA  ALA A  63       6.322  12.663  44.574  1.00 14.19
ATOM    476  C   ALA A  63       6.303  13.135  46.061  1.00 15.79
ATOM    477  O   ALA A  63       5.928  14.359  46.283  1.00 14.46
ATOM    478  CB  ALA A  63       7.692  12.709  43.993  1.00 15.58
ATOM    479  N   HIS A  64       6.698  12.342  47.008  1.00 15.17
ATOM    480  CA  HIS A  64       6.574  12.744  48.441  1.00 16.39
ATOM    481  C   HIS A  64       7.488  13.836  48.860  1.00 18.44
ATOM    482  O   HIS A  64       7.202  14.477  49.952  1.00 17.46
ATOM    483  CB  HIS A  64       6.767  11.437  49.343  1.00 13.90
ATOM    484  CG  HIS A  64       8.221  11.007  49.194  1.00 16.61
ATOM    485  ND1 HIS A  64       9.264  11.216  50.076  1.00 17.21
ATOM    486  CD2 HIS A  64       8.795  10.378  48.140  1.00 12.50
ATOM    487  CE1 HIS A  64      10.399  10.741  49.657  1.00 14.10
ATOM    488  NE2 HIS A  64      10.077  10.260  48.424  1.00 17.83
ATOM    489  N   ASP A  65       8.622  14.139  48.128  1.00 17.03
ATOM    490  CA  ASP A  65       9.569  15.208  48.572  1.00 16.25
ATOM    491  C   ASP A  65       8.892  16.576  48.792  1.00 18.46
ATOM    492  O   ASP A  65       9.390  17.402  49.581  1.00 17.41
ATOM    493  CB  ASP A  65      10.795  15.320  47.622  1.00 16.52
ATOM    494  CG  ASP A  65      10.426  15.767  46.252  1.00 14.74
ATOM    495  OD1 ASP A  65       9.470  15.193  45.559  1.00 14.91
ATOM    496  OD2 ASP A  65      10.911  16.789  45.762  1.00 17.68
ATOM    497  N   ARG A  66       7.788  16.876  48.117  1.00 18.75
ATOM    498  CA  ARG A  66       7.104  18.181  48.226  1.00 17.77
ATOM    499  C   ARG A  66       6.153  18.168  49.444  1.00 18.83
ATOM    500  O   ARG A  66       5.840  19.328  49.880  1.00 18.58
ATOM    501  CB  ARG A  66       6.281  18.501  47.015  1.00 18.07
ATOM    502  CG  ARG A  66       7.025  18.710  45.705  1.00 18.34
ATOM    503  CD  ARG A  66       7.571  20.107  45.776  1.00 25.02
ATOM    504  NE  ARG A  66       8.625  20.265  44.789  1.00 28.36
ATOM    505  CZ  ARG A  66       9.183  21.434  44.466  1.00 30.88
ATOM    506  NH1 ARG A  66       8.715  22.643  44.971  1.00 30.46
ATOM    507  NH2 ARG A  66      10.222  21.471  43.589  1.00 29.38
ATOM    508  N   PHE A  67       5.746  17.028  49.959  1.00 19.04
ATOM    509  CA  PHE A  67       4.720  16.943  51.044  1.00 20.67
ATOM    510  C   PHE A  67       5.144  17.518  52.410  1.00 21.00
ATOM    511  O   PHE A  67       4.171  18.084  53.030  1.00 22.00
ATOM    512  CB  PHE A  67       4.141  15.523  51.113  1.00 18.36
ATOM    513  CG  PHE A  67       3.156  15.301  49.944  1.00 25.38
ATOM    514  CD1 PHE A  67       3.558  15.486  48.644  1.00 28.86
ATOM    515  CD2 PHE A  67       1.858  14.925  50.140  1.00 30.02
ATOM    516  CE1 PHE A  67       2.715  15.238  47.550  1.00 31.55
ATOM    517  CE2 PHE A  67       0.926  14.766  49.113  1.00 33.42
ATOM    518  CZ  PHE A  67       1.361  14.935  47.788  1.00 32.81
ATOM    519  N   GLY A  68       6.324  17.425  52.920  1.00 20.33
ATOM    520  CA  GLY A  68       6.770  18.004  54.198  1.00 21.17
ATOM    521  C   GLY A  68       6.485  19.494  54.187  1.00 22.44
ATOM    522  O   GLY A  68       6.000  20.150  55.116  1.00 22.77
ATOM    523  N   GLY A  69       6.738  20.187  53.112  1.00 20.54
ATOM    524  CA  GLY A  69       6.556  21.613  52.999  1.00 19.84
ATOM    525  C   GLY A  69       5.093  21.939  52.985  1.00 21.77
ATOM    526  O   GLY A  69       4.747  22.902  53.622  1.00 23.06
ATOM    527  N   TYR A  70       4.241  21.181  52.312  1.00 20.33
ATOM    528  CA  TYR A  70       2.831  21.430  52.245  1.00 19.86
ATOM    529  C   TYR A  70       2.291  21.298  53.663  1.00 20.89
ATOM    530  O   TYR A  70       1.468  22.121  53.999  1.00 22.64
ATOM    531  CB  TYR A  70       2.097  20.449  51.302  1.00 20.32
ATOM    532  CG  TYR A  70       2.386  20.531  49.821  1.00 22.15
ATOM    533  CD1 TYR A  70       2.986  21.674  49.250  1.00 19.96
ATOM    534  CD2 TYR A  70       2.152  19.373  49.004  1.00 19.73
ATOM    535  CE1 TYR A  70       3.286  21.768  47.893  1.00 20.82
ATOM    536  CE2 TYR A  70       2.474  19.453  47.625  1.00 20.55
ATOM    537  CZ  TYR A  70       3.058  20.620  47.126  1.00 21.69
ATOM    538  OH  TYR A  70       3.345  20.694  45.775  1.00 27.96
ATOM    539  N   ALA A  71       2.611  20.267  54.362  1.00 21.93
ATOM    540  CA  ALA A  71       2.203  19.924  55.711  1.00 23.56
ATOM    541  C   ALA A  71       2.621  21.041  56.691  1.00 25.83
ATOM    542  O   ALA A  71       1.766  21.468  57.457  1.00 27.05
ATOM    543  CB  ALA A  71       2.841  18.597  56.147  1.00 21.93
ATOM    544  N   GLN A  72       3.849  21.505  56.665  1.00 26.16
ATOM    545  CA  GLN A  72       4.324  22.585  57.526  1.00 29.69
ATOM    546  C   GLN A  72       3.581  23.915  57.325  1.00 31.89
ATOM    547  O   GLN A  72       3.529  24.731  58.266  1.00 33.87
ATOM    548  CB  GLN A  72       5.799  22.891  57.299  1.00 30.81
ATOM    549  CG  GLN A  72       6.335  24.087  58.014  1.00 28.04
ATOM    550  CD  GLN A  72       7.666  24.544  57.541  1.00 28.24
ATOM    551  OE1 GLN A  72       8.688  24.420  58.263  1.00 31.26
ATOM    552  NE2 GLN A  72       7.787  25.220  56.406  1.00 27.87
ATOM    553  N   SER A  73       3.125  24.182  56.132  1.00 30.29
ATOM    554  CA  SER A  73       2.352  25.347  55.800  1.00 30.44
ATOM    555  C   SER A  73       0.858  25.159  56.164  1.00 30.34
ATOM    556  O   SER A  73       0.023  26.082  55.871  1.00 32.61
ATOM    557  CB  SER A  73       2.461  25.609  54.288  1.00 30.38
ATOM    558  OG  SER A  73       3.816  25.858  54.030  1.00 32.28
ATOM    559  N   GLY A  74       0.540  24.016  56.679  1.00 28.77
ATOM    560  CA  GLY A  74      -0.750  23.452  57.039  1.00 30.04
ATOM    561  C   GLY A  74      -1.695  23.126  55.876  1.00 30.20
ATOM    562  O   GLY A  74      -2.925  23.338  56.115  1.00 31.87
ATOM    563  N   LEU A  75      -1.351  22.593  54.725  1.00 27.25
ATOM    564  CA  LEU A  75      -2.211  22.448  53.532  1.00 25.25
ATOM    565  C   LEU A  75      -2.814  21.088  53.298  1.00 25.97
ATOM    566  O   LEU A  75      -3.709  20.888  52.431  1.00 25.21
ATOM    567  CB  LEU A  75      -1.440  23.007  52.308  1.00 22.09
ATOM    568  CG  LEU A  75      -0.908  24.426  52.310  1.00 24.87
ATOM    569  CD1 LEU A  75       0.044  24.670  51.156  1.00 24.34
ATOM    570  CD2 LEU A  75      -2.032  25.491  52.287  1.00 22.85
ATOM    571  N   LEU A  76      -2.380  20.196  54.193  1.00 26.85
ATOM    572  CA  LEU A  76      -2.867  18.844  54.069  1.00 30.07
ATOM    573  C   LEU A  76      -3.517  18.346  55.355  1.00 32.12
ATOM    574  O   LEU A  76      -2.967  18.629  56.442  1.00 33.59
ATOM    575  CB  LEU A  76      -1.603  17.915  53.801  1.00 26.99
ATOM    576  CG  LEU A  76      -0.826  18.255  52.507  1.00 24.65
ATOM    577  CD1 LEU A  76       0.412  17.426  52.545  1.00 24.67
ATOM    578  CD2 LEU A  76      -1.736  17.975  51.314  1.00 25.03
ATOM    579  N   ALA A  77      -4.477  17.498  55.197  1.00 32.30
ATOM    580  CA  ALA A  77      -5.144  16.805  56.272  1.00 32.92
ATOM    581  C   ALA A  77      -4.357  15.537  56.609  1.00 34.17
ATOM    582  O   ALA A  77      -3.839  14.863  55.730  1.00 31.63
ATOM    583  CB  ALA A  77      -6.604  16.393  55.908  1.00 31.57
ATOM    584  N   GLU A  78      -4.388  15.224  57.907  1.00 35.96
ATOM    585  CA  GLU A  78      -3.802  14.005  58.469  1.00 38.34
ATOM    586  C   GLU A  78      -4.831  12.913  58.065  1.00 37.65
ATOM    587  O   GLU A  78      -6.035  13.018  58.167  1.00 37.24
ATOM    588  CB  GLU A  78      -3.524  14.013  59.946  1.00 40.69
ATOM    589  CG  GLU A  78      -3.506  12.672  60.714  1.00 47.32
ATOM    590  CD  GLU A  78      -3.186  12.745  62.197  1.00 51.54
ATOM    591  OE1 GLU A  78      -3.437  13.814  62.818  1.00 55.15
ATOM    592  OE2 GLU A  78      -2.630  11.729  62.729  1.00 51.80
ATOM    593  N   ILE A  79      -4.274  11.857  57.515  1.00 38.37
ATOM    594  CA  ILE A  79      -5.082  10.730  57.083  1.00 39.14
ATOM    595  C   ILE A  79      -4.895   9.711  58.212  1.00 41.86
ATOM    596  O   ILE A  79      -3.893   9.659  58.961  1.00 39.15
ATOM    597  CB  ILE A  79      -4.646  10.246  55.654  1.00 37.05
ATOM    598  CG1 ILE A  79      -3.221   9.669  55.737  1.00 33.87
ATOM    599  CG2 ILE A  79      -4.665  11.286  54.489  1.00 35.74
ATOM    600  CD1 ILE A  79      -2.836   8.543  54.811  1.00 33.96
ATOM    601  N   THR A  80      -5.870   8.815  58.253  1.00 48.00
ATOM    602  CA  THR A  80      -5.966   7.696  59.217  1.00 52.57
ATOM    603  C   THR A  80      -6.479   6.372  58.681  1.00 53.84
ATOM    604  O   THR A  80      -7.673   5.962  58.756  1.00 54.91
ATOM    605  CB  THR A  80      -6.917   8.170  60.409  1.00 55.23
ATOM    606  OG1 THR A  80      -8.044   8.810  59.662  1.00 58.54
ATOM    607  CG2 THR A  80      -6.330   9.099  61.448  1.00 55.39
ATOM    608  N   PRO A  81      -5.583   5.595  58.139  1.00 54.92
ATOM    609  CA  PRO A  81      -5.991   4.260  57.629  1.00 56.00
ATOM    610  C   PRO A  81      -5.798   3.336  58.818  1.00 55.47
ATOM    611  O   PRO A  81      -4.863   3.577  59.635  1.00 56.08
ATOM    612  CB  PRO A  81      -5.069   4.062  56.456  1.00 55.59
ATOM    613  CG  PRO A  81      -4.109   5.231  56.475  1.00 55.50
ATOM    614  CD  PRO A  81      -4.136   5.757  57.920  1.00 55.00
ATOM    615  N   ASP A  82      -6.608   2.319  58.946  1.00 55.71
ATOM    616  CA  ASP A  82      -6.325   1.423  60.098  1.00 56.52
ATOM    617  C   ASP A  82      -5.334   0.378  59.580  1.00 54.60
ATOM    618  O   ASP A  82      -5.275   0.112  58.398  1.00 54.20
ATOM    619  CB  ASP A  82      -7.533   0.779  60.713  1.00 62.77
ATOM    620  CG  ASP A  82      -8.510   0.203  59.684  1.00 66.06
ATOM    621  OD1 ASP A  82      -8.551   0.728  58.551  1.00 67.70
ATOM    622  OD2 ASP A  82      -9.232  -0.756  60.123  1.00 68.32
ATOM    623  N   LYS A  83      -4.683  -0.133  60.566  1.00 54.31
ATOM    624  CA  LYS A  83      -3.648  -1.162  60.479  1.00 54.60
ATOM    625  C   LYS A  83      -4.000  -2.220  59.437  1.00 51.81
ATOM    626  O   LYS A  83      -3.114  -2.932  58.965  1.00 50.29
ATOM    627  CB  LYS A  83      -3.361  -1.858  61.832  1.00 58.99
ATOM    628  CG  LYS A  83      -4.129  -3.155  62.039  1.00 63.00
ATOM    629  CD  LYS A  83      -3.495  -4.192  62.931  1.00 67.55
ATOM    630  CE  LYS A  83      -2.110  -4.711  62.605  1.00 70.95
ATOM    631  NZ  LYS A  83      -1.943  -6.219  62.769  1.00 72.56
ATOM    632  N   ALA A  84      -5.313  -2.323  59.170  1.00 50.22
ATOM    633  CA  ALA A  84      -5.685  -3.361  58.194  1.00 48.69
ATOM    634  C   ALA A  84      -5.360  -2.663  56.859  1.00 46.75
ATOM    635  O   ALA A  84      -4.632  -3.329  56.150  1.00 48.64
ATOM    636  CB  ALA A  84      -7.075  -3.972  58.102  1.00 47.82
ATOM    637  N   PHE A  85      -5.893  -1.498  56.680  1.00 44.73
ATOM    638  CA  PHE A  85      -5.592  -0.877  55.383  1.00 42.93
ATOM    639  C   PHE A  85      -4.103  -0.652  55.251  1.00 43.08
ATOM    640  O   PHE A  85      -3.555  -0.878  54.129  1.00 44.12
ATOM    641  CB  PHE A  85      -6.298   0.407  55.166  1.00 42.44
ATOM    642  CG  PHE A  85      -5.926   0.984  53.819  1.00 42.40
ATOM    643  CD1 PHE A  85      -4.763   1.697  53.693  1.00 40.81
ATOM    644  CD2 PHE A  85      -6.785   0.724  52.723  1.00 43.10
ATOM    645  CE1 PHE A  85      -4.413   2.219  52.454  1.00 40.45
ATOM    646  CE2 PHE A  85      -6.448   1.220  51.476  1.00 43.41
ATOM    647  CZ  PHE A  85      -5.229   1.961  51.384  1.00 41.49
ATOM    648  N   GLN A  86      -3.486  -0.239  56.338  1.00 41.40
ATOM    649  CA  GLN A  86      -2.055   0.037  56.321  1.00 40.67
ATOM    650  C   GLN A  86      -1.199  -1.130  55.858  1.00 41.37
ATOM    651  O   GLN A  86      -0.095  -0.987  55.275  1.00 41.02
ATOM    652  CB  GLN A  86      -1.576   0.502  57.733  1.00 42.75
ATOM    653  CG  GLN A  86      -1.367   1.945  57.878  1.00 44.12
ATOM    654  CD  GLN A  86      -0.889   2.594  59.145  1.00 45.08
ATOM    655  OE1 GLN A  86       0.263   2.976  59.394  1.00 45.97
ATOM    656  NE2 GLN A  86      -1.976   2.843  59.916  1.00 46.63
ATOM    657  N   ASP A  87      -1.659  -2.305  56.203  1.00 40.74
ATOM    658  CA  ASP A  87      -1.148  -3.659  56.041  1.00 40.77
ATOM    659  C   ASP A  87      -1.014  -4.095  54.581  1.00 36.12
ATOM    660  O   ASP A  87      -0.106  -4.841  54.178  1.00 36.45
ATOM    661  CB  ASP A  87      -2.078  -4.539  56.904  1.00 45.46
ATOM    662  CG  ASP A  87      -1.348  -5.368  57.935  1.00 50.80
ATOM    663  OD1 ASP A  87      -0.195  -5.011  58.289  1.00 52.85
ATOM    664  OD2 ASP A  87      -2.095  -6.334  58.365  1.00 54.43
ATOM    665  N   LYS A  88      -1.855  -3.553  53.783  1.00 34.25
ATOM    666  CA  LYS A  88      -1.866  -3.768  52.329  1.00 32.57
ATOM    667  C   LYS A  88      -0.695  -3.118  51.592  1.00 32.53
ATOM    668  O   LYS A  88      -0.388  -3.479  50.417  1.00 36.26
ATOM    669  CB  LYS A  88      -3.158  -3.208  51.839  1.00 31.00
ATOM    670  CG  LYS A  88      -4.348  -4.082  52.148  1.00 33.05
ATOM    671  CD  LYS A  88      -5.585  -3.624  51.509  1.00 36.47
ATOM    672  CE  LYS A  88      -6.801  -3.153  52.223  1.00 40.72
ATOM    673  NZ  LYS A  88      -8.041  -3.430  51.410  1.00 39.71
ATOM    674  N   LEU A  89      -0.001  -2.180  52.182  1.00 31.86
ATOM    675  CA  LEU A  89       1.078  -1.438  51.592  1.00 30.68
ATOM    676  C   LEU A  89       2.424  -1.743  52.188  1.00 31.20
ATOM    677  O   LEU A  89       2.580  -2.021  53.398  1.00 33.15
ATOM    678  CB  LEU A  89       0.754   0.058  51.818  1.00 28.91
ATOM    679  CG  LEU A  89      -0.396   0.724  51.217  1.00 28.89
ATOM    680  CD1 LEU A  89       0.033   2.105  50.669  1.00 31.33
ATOM    681  CD2 LEU A  89      -0.967  -0.023  50.028  1.00 28.02
ATOM    682  N   TYR A  90       3.420  -1.623  51.328  1.00 28.21
ATOM    683  CA  TYR A  90       4.762  -1.772  51.877  1.00 30.92
ATOM    684  C   TYR A  90       4.976  -0.644  52.893  1.00 34.34
ATOM    685  O   TYR A  90       4.765   0.612  52.670  1.00 34.67
ATOM    686  CB  TYR A  90       5.778  -1.665  50.766  1.00 30.58
ATOM    687  CG  TYR A  90       5.730  -2.788  49.775  1.00 33.53
ATOM    688  CD1 TYR A  90       6.343  -3.997  50.125  1.00 32.52
ATOM    689  CD2 TYR A  90       5.136  -2.674  48.483  1.00 32.65
ATOM    690  CE1 TYR A  90       6.375  -5.034  49.184  1.00 32.72
ATOM    691  CE2 TYR A  90       5.194  -3.704  47.543  1.00 31.58
ATOM    692  CZ  TYR A  90       5.806  -4.873  47.909  1.00 33.65
ATOM    693  OH  TYR A  90       5.894  -6.027  47.128  1.00 38.81
ATOM    694  N   PRO A  91       5.472  -1.021  54.054  1.00 35.71
ATOM    695  CA  PRO A  91       5.743  -0.054  55.147  1.00 34.70
ATOM    696  C   PRO A  91       6.789   0.986  54.825  1.00 31.44
ATOM    697  O   PRO A  91       6.625   2.093  55.315  1.00 29.86
ATOM    698  CB  PRO A  91       6.145  -0.898  56.366  1.00 36.66
ATOM    699  CG  PRO A  91       6.858  -2.068  55.646  1.00 39.29
ATOM    700  CD  PRO A  91       5.751  -2.407  54.507  1.00 37.31
ATOM    701  N   PHE A  92       7.812   0.692  54.062  1.00 31.09
ATOM    702  CA  PHE A  92       8.761   1.798  53.816  1.00 30.13
ATOM    703  C   PHE A  92       7.980   2.873  53.054  1.00 29.72
ATOM    704  O   PHE A  92       8.452   4.065  53.135  1.00 31.00
ATOM    705  CB  PHE A  92       9.994   1.312  53.066  1.00 32.57
ATOM    706  CG  PHE A  92       9.795   1.229  51.575  1.00 35.45
ATOM    707  CD1 PHE A  92       9.274   0.051  51.017  1.00 34.58
ATOM    708  CD2 PHE A  92      10.154   2.353  50.737  1.00 35.83
ATOM    709  CE1 PHE A  92       9.068  -0.024  49.621  1.00 35.83
ATOM    710  CE2 PHE A  92       9.954   2.238  49.346  1.00 34.23
ATOM    711  CZ  PHE A  92       9.423   1.049  48.762  1.00 32.68
ATOM    712  N   THR A  93       6.878   2.550  52.376  1.00 26.97
ATOM    713  CA  THR A  93       6.114   3.577  51.626  1.00 25.83
ATOM    714  C   THR A  93       5.303   4.485  52.544  1.00 26.16
ATOM    715  O   THR A  93       5.187   5.711  52.244  1.00 22.40
ATOM    716  CB  THR A  93       5.312   3.002  50.376  1.00 23.01
ATOM    717  OG1 THR A  93       4.140   2.345  50.911  1.00 24.85
ATOM    718  CG2 THR A  93       6.136   2.118  49.477  1.00 23.30
ATOM    719  N   TRP A  94       4.851   3.960  53.741  1.00 26.08
ATOM    720  CA  TRP A  94       4.115   4.857  54.703  1.00 23.12
ATOM    721  C   TRP A  94       5.129   5.776  55.365  1.00 21.53
ATOM    722  O   TRP A  94       4.807   6.960  55.720  1.00 24.87
ATOM    723  CB  TRP A  94       3.406   4.023  55.736  1.00 22.26
ATOM    724  CG  TRP A  94       2.208   3.297  55.299  1.00 18.12
ATOM    725  CD1 TRP A  94       2.068   1.941  55.159  1.00 19.30
ATOM    726  CD2 TRP A  94       0.951   3.873  54.963  1.00 21.74
ATOM    727  NE1 TRP A  94       0.792   1.662  54.712  1.00 23.67
ATOM    728  CE2 TRP A  94       0.060   2.833  54.640  1.00 21.25
ATOM    729  CE3 TRP A  94       0.467   5.175  54.836  1.00 22.59
ATOM    730  CZ2 TRP A  94      -1.244   3.066  54.237  1.00 24.60
ATOM    731  CZ3 TRP A  94      -0.838   5.426  54.475  1.00 23.57
ATOM    732  CH2 TRP A  94      -1.705   4.370  54.147  1.00 24.10
ATOM    733  N   ASP A  95       6.337   5.471  55.555  1.00 21.02
ATOM    734  CA  ASP A  95       7.382   6.192  56.184  1.00 24.72
ATOM    735  C   ASP A  95       7.741   7.457  55.390  1.00 27.52
ATOM    736  O   ASP A  95       8.259   8.423  55.970  1.00 29.97
ATOM    737  CB  ASP A  95       8.645   5.336  56.324  1.00 31.58
ATOM    738  CG  ASP A  95       8.676   4.295  57.449  1.00 37.85
ATOM    739  OD1 ASP A  95       7.891   4.520  58.384  1.00 38.66
ATOM    740  OD2 ASP A  95       9.482   3.292  57.276  1.00 41.90
ATOM    741  N   ALA A  96       7.610   7.281  54.071  1.00 24.95
ATOM    742  CA  ALA A  96       7.892   8.354  53.110  1.00 22.68
ATOM    743  C   ALA A  96       6.867   9.442  53.266  1.00 21.80
ATOM    744  O   ALA A  96       7.222  10.619  52.975  1.00 22.63
ATOM    745  CB  ALA A  96       7.917   7.754  51.666  1.00 22.45
ATOM    746  N   VAL A  97       5.668   9.140  53.809  1.00 21.20
ATOM    747  CA  VAL A  97       4.588  10.128  53.863  1.00 21.68
ATOM    748  C   VAL A  97       4.260  10.533  55.320  1.00 20.10
ATOM    749  O   VAL A  97       3.113  10.963  55.469  1.00 23.68
ATOM    750  CB  VAL A  97       3.406   9.711  52.984  1.00 20.81
ATOM    751  CG1 VAL A  97       3.849   9.699  51.476  1.00 22.95
ATOM    752  CG2 VAL A  97       2.806   8.361  53.305  1.00 22.42
ATOM    753  N   ARG A  98       5.221  10.425  56.118  1.00 20.47
ATOM    754  CA  ARG A  98       5.092  10.782  57.541  1.00 24.25
ATOM    755  C   ARG A  98       5.812  12.070  57.734  1.00 25.01
ATOM    756  O   ARG A  98       6.961  12.267  57.356  1.00 28.96
ATOM    757  CB  ARG A  98       5.688   9.779  58.522  1.00 28.60
ATOM    758  CG  ARG A  98       4.894   9.002  59.504  1.00 28.40
ATOM    759  CD  ARG A  98       5.836   7.995  60.108  1.00 31.71
ATOM    760  NE  ARG A  98       5.260   6.648  59.970  1.00 37.22
ATOM    761  CZ  ARG A  98       4.000   6.314  60.322  1.00 38.13
ATOM    762  NH1 ARG A  98       3.127   7.156  60.885  1.00 39.75
ATOM    763  NH2 ARG A  98       3.559   5.083  59.956  1.00 41.00
ATOM    764  N   TYR A  99       5.160  13.006  58.346  1.00 26.30
ATOM    765  CA  TYR A  99       5.801  14.269  58.627  1.00 26.67
ATOM    766  C   TYR A  99       5.519  14.525  60.134  1.00 27.16
ATOM    767  O   TYR A  99       4.373  14.753  60.435  1.00 26.89
ATOM    768  CB  TYR A  99       5.307  15.360  57.701  1.00 24.28
ATOM    769  CG  TYR A  99       5.961  16.706  57.982  1.00 25.20
ATOM    770  CD1 TYR A  99       7.269  17.038  57.673  1.00 24.46
ATOM    771  CD2 TYR A  99       5.163  17.655  58.601  1.00 25.88
ATOM    772  CE1 TYR A  99       7.777  18.288  57.850  1.00 26.00
ATOM    773  CE2 TYR A  99       5.666  18.875  58.900  1.00 26.79
ATOM    774  CZ  TYR A  99       6.935  19.203  58.489  1.00 26.99
ATOM    775  OH  TYR A  99       7.299  20.493  58.794  1.00 28.07
ATOM    776  N   ASN A 100       6.581  14.571  60.907  1.00 28.54
ATOM    777  CA  ASN A 100       6.527  14.796  62.348  1.00 32.41
ATOM    778  C   ASN A 100       5.685  13.700  62.989  1.00 31.57
ATOM    779  O   ASN A 100       4.853  13.941  63.858  1.00 33.49
ATOM    780  CB  ASN A 100       6.140  16.247  62.680  1.00 36.49
ATOM    781  CG  ASN A 100       7.183  17.309  62.280  1.00 41.17
ATOM    782  OD1 ASN A 100       6.758  18.431  61.850  1.00 41.34
ATOM    783  ND2 ASN A 100       8.541  17.155  62.334  1.00 39.92
ATOM    784  N   GLY A 101       5.851  12.476  62.548  1.00 30.13
ATOM    785  CA  GLY A 101       5.180  11.273  62.933  1.00 29.61
ATOM    786  C   GLY A 101       3.781  11.076  62.418  1.00 31.93
ATOM    787  O   GLY A 101       3.243   9.899  62.509  1.00 35.22
ATOM    788  N   LYS A 102       3.051  12.005  61.854  1.00 32.67
ATOM    789  CA  LYS A 102       1.670  11.907  61.342  1.00 32.94
ATOM    790  C   LYS A 102       1.656  11.447  59.839  1.00 32.17
ATOM    791  O   LYS A 102       2.573  11.834  59.150  1.00 28.00
ATOM    792  CB  LYS A 102       0.934  13.256  61.235  1.00 37.09
ATOM    793  CG  LYS A 102       0.784  14.097  62.538  1.00 40.86
ATOM    794  CD  LYS A 102       0.394  13.064  63.638  1.00 44.14
ATOM    795  CE  LYS A 102      -0.338  13.701  64.823  1.00 46.57
ATOM    796  NZ  LYS A 102      -0.755  12.588  65.782  1.00 46.78
ATOM    797  N   LEU A 103       0.651  10.772  59.416  1.00 29.20
ATOM    798  CA  LEU A 103       0.647  10.414  57.981  1.00 29.95
ATOM    799  C   LEU A 103      -0.024  11.544  57.260  1.00 28.33
ATOM    800  O   LEU A 103      -1.064  11.961  57.805  1.00 26.73
ATOM    801  CB  LEU A 103       0.057   9.038  57.935  1.00 27.56
ATOM    802  CG  LEU A 103       0.944   7.980  58.543  1.00 28.99
ATOM    803  CD1 LEU A 103      -0.150   6.846  58.571  1.00 31.26
ATOM    804  CD2 LEU A 103       2.117   7.496  57.758  1.00 27.09
ATOM    805  N   ILE A 104       0.541  12.052  56.160  1.00 25.90
ATOM    806  CA  ILE A 104      -0.093  13.204  55.454  1.00 24.57
ATOM    807  C   ILE A 104      -0.491  12.985  53.991  1.00 23.58
ATOM    808  O   ILE A 104      -0.848  13.939  53.305  1.00 22.61
ATOM    809  CB  ILE A 104       0.911  14.399  55.422  1.00 26.59
ATOM    810  CG1 ILE A 104       2.225  13.846  54.747  1.00 25.94
ATOM    811  CG2 ILE A 104       1.146  14.944  56.807  1.00 30.88
ATOM    812  CD1 ILE A 104       3.358  14.822  54.795  1.00 30.36
ATOM    813  N   ALA A 105      -0.335  11.666  53.675  1.00 23.69
ATOM    814  CA  ALA A 105      -0.716  11.218  52.310  1.00 20.89
ATOM    815  C   ALA A 105      -0.708   9.698  52.197  1.00 20.42
ATOM    816  O   ALA A 105      -0.234   8.960  53.070  1.00 20.81
ATOM    817  CB  ALA A 105       0.229  11.869  51.295  1.00 21.61
ATOM    818  N   TYR A 106      -1.336   9.241  51.108  1.00 20.25
ATOM    819  CA  TYR A 106      -1.406   7.840  50.689  1.00 21.08
ATOM    820  C   TYR A 106      -0.307   7.633  49.587  1.00 20.59
ATOM    821  O   TYR A 106      -0.359   8.425  48.619  1.00 19.76
ATOM    822  CB  TYR A 106      -2.718   7.479  50.009  1.00 23.92
ATOM    823  CG  TYR A 106      -3.876   7.430  51.002  1.00 28.83
ATOM    824  CD1 TYR A 106      -4.573   8.611  51.259  1.00 26.50
ATOM    825  CD2 TYR A 106      -4.262   6.222  51.592  1.00 29.20
ATOM    826  CE1 TYR A 106      -5.639   8.582  52.167  1.00 29.58
ATOM    827  CE2 TYR A 106      -5.306   6.180  52.510  1.00 30.48
ATOM    828  CZ  TYR A 106      -5.965   7.379  52.777  1.00 31.74
ATOM    829  OH  TYR A 106      -7.020   7.383  53.717  1.00 38.89
ATOM    830  N   PRO A 107       0.534   6.704  49.826  1.00 22.27
ATOM    831  CA  PRO A 107       1.638   6.329  48.917  1.00 21.19
ATOM    832  C   PRO A 107       1.011   5.510  47.810  1.00 23.25
ATOM    833  O   PRO A 107       0.141   4.688  48.173  1.00 23.73
ATOM    834  CB  PRO A 107       2.586   5.492  49.685  1.00 23.35
ATOM    835  CG  PRO A 107       1.966   5.419  51.123  1.00 25.03
ATOM    836  CD  PRO A 107       0.528   5.833  51.049  1.00 21.59
ATOM    837  N   ILE A 108       1.388   5.744  46.566  1.00 20.48
ATOM    838  CA  ILE A 108       0.812   5.081  45.397  1.00 19.11
ATOM    839  C   ILE A 108       1.842   4.209  44.688  1.00 20.39
ATOM    840  O   ILE A 108       1.619   2.986  44.489  1.00 20.35
ATOM    841  CB  ILE A 108       0.203   6.157  44.376  1.00 17.76
ATOM    842  CG1 ILE A 108      -0.820   7.134  44.985  1.00 19.36
ATOM    843  CG2 ILE A 108      -0.363   5.481  43.115  1.00 22.68
ATOM    844  CD1 ILE A 108      -2.163   6.666  45.614  1.00 20.72
ATOM    845  N   ALA A 109       3.045   4.788  44.414  1.00 17.12
ATOM    846  CA  ALA A 109       4.029   3.991  43.618  1.00 18.16
ATOM    847  C   ALA A 109       5.391   4.510  43.851  1.00 16.34
ATOM    848  O   ALA A 109       5.536   5.681  44.292  1.00 19.36
ATOM    849  CB  ALA A 109       3.693   4.114  42.090  1.00 19.32
ATOM    850  N   VAL A 110       6.392   3.757  43.616  1.00 16.63
ATOM    851  CA  VAL A 110       7.815   3.914  43.813  1.00 19.47
ATOM    852  C   VAL A 110       8.466   4.093  42.441  1.00 19.31
ATOM    853  O   VAL A 110       8.361   3.235  41.575  1.00 19.56
ATOM    854  CB  VAL A 110       8.432   2.783  44.667  1.00 19.26
ATOM    855  CG1 VAL A 110       9.900   3.053  44.739  1.00 18.84
ATOM    856  CG2 VAL A 110       7.627   2.709  45.946  1.00 24.54
ATOM    857  N   GLU A 111       8.946   5.363  42.375  1.00 19.12
ATOM    858  CA  GLU A 111       9.575   5.813  41.060  1.00 18.05
ATOM    859  C   GLU A 111      11.055   5.901  41.097  1.00 17.63
ATOM    860  O   GLU A 111      11.665   6.478  42.044  1.00 17.48
ATOM    861  CB  GLU A 111       8.944   7.213  40.782  1.00 15.13
ATOM    862  CG  GLU A 111       7.445   7.353  40.682  1.00 15.53
ATOM    863  CD  GLU A 111       7.095   8.754  40.327  1.00 14.88
ATOM    864  OE1 GLU A 111       7.896   9.661  40.337  1.00 20.98
ATOM    865  OE2 GLU A 111       5.939   8.935  39.907  1.00 17.19
ATOM    866  N   ALA A 112      11.859   5.306  40.131  1.00 16.11
ATOM    867  CA  ALA A 112      13.287   5.450  40.066  1.00 16.29
ATOM    868  C   ALA A 112      13.596   5.540  38.535  1.00 16.18
ATOM    869  O   ALA A 112      12.853   4.921  37.758  1.00 17.75
ATOM    870  CB  ALA A 112      14.104   4.403  40.727  1.00 17.57
ATOM    871  N   LEU A 113      14.524   6.373  38.197  1.00 15.81
ATOM    872  CA  LEU A 113      14.992   6.475  36.795  1.00 16.31
ATOM    873  C   LEU A 113      15.779   5.207  36.435  1.00 17.37
ATOM    874  O   LEU A 113      16.563   4.592  37.259  1.00 16.95
ATOM    875  CB  LEU A 113      15.948   7.690  36.724  1.00 12.97
ATOM    876  CG  LEU A 113      15.269   9.058  36.830  1.00 16.08
ATOM    877  CD1 LEU A 113      16.309  10.173  36.962  1.00 15.89
ATOM    878  CD2 LEU A 113      14.344   9.371  35.594  1.00 14.66
ATOM    879  N   SER A 114      15.751   4.800  35.164  1.00 17.56
ATOM    880  CA  SER A 114      16.506   3.673  34.557  1.00 16.88
ATOM    881  C   SER A 114      17.190   4.079  33.203  1.00 16.45
ATOM    882  O   SER A 114      16.855   5.167  32.777  1.00 15.05
ATOM    883  CB  SER A 114      15.566   2.522  34.240  1.00 17.43
ATOM    884  OG  SER A 114      15.273   1.908  35.456  1.00 18.50
ATOM    885  N   LEU A 115      18.155   3.274  32.804  1.00 16.59
ATOM    886  CA  LEU A 115      18.773   3.520  31.496  1.00 18.16
ATOM    887  C   LEU A 115      17.830   2.804  30.543  1.00 15.78
ATOM    888  O   LEU A 115      17.542   1.609  30.725  1.00 17.76
ATOM    889  CB  LEU A 115      20.123   2.905  31.515  1.00 21.46
ATOM    890  CG  LEU A 115      21.367   3.289  30.653  1.00 25.25
ATOM    891  CD1 LEU A 115      22.063   2.092  30.030  1.00 26.37
ATOM    892  CD2 LEU A 115      21.141   4.471  29.735  1.00 23.62
ATOM    893  N   ILE A 116      17.356   3.439  29.514  1.00 18.00
ATOM    894  CA  ILE A 116      16.518   2.842  28.423  1.00 17.85
ATOM    895  C   ILE A 116      17.381   2.852  27.162  1.00 19.11
ATOM    896  O   ILE A 116      17.993   3.907  26.830  1.00 19.58
ATOM    897  CB  ILE A 116      15.229   3.671  28.236  1.00 18.14
ATOM    898  CG1 ILE A 116      14.512   3.780  29.674  1.00 15.11
ATOM    899  CG2 ILE A 116      14.332   3.194  27.070  1.00 17.15
ATOM    900  CD1 ILE A 116      13.363   4.821  29.656  1.00 15.93
ATOM    901  N   TYR A 117      17.464   1.703  26.513  1.00 21.13
ATOM    902  CA  TYR A 117      18.417   1.714  25.319  1.00 21.95
ATOM    903  C   TYR A 117      17.671   1.037  24.174  1.00 25.23
ATOM    904  O   TYR A 117      16.705   0.223  24.470  1.00 23.97
ATOM    905  CB  TYR A 117      19.736   1.067  25.685  1.00 18.27
ATOM    906  CG  TYR A 117      19.578  -0.360  26.080  1.00 18.45
ATOM    907  CD1 TYR A 117      19.042  -0.837  27.268  1.00 17.53
ATOM    908  CD2 TYR A 117      19.981  -1.387  25.125  1.00 21.09
ATOM    909  CE1 TYR A 117      18.933  -2.183  27.549  1.00 19.38
ATOM    910  CE2 TYR A 117      19.920  -2.741  25.387  1.00 21.48
ATOM    911  CZ  TYR A 117      19.408  -3.113  26.584  1.00 22.33
ATOM    912  OH  TYR A 117      19.323  -4.438  26.903  1.00 26.17
ATOM    913  N   ASN A 118      18.170   1.426  22.968  1.00 24.59
ATOM    914  CA  ASN A 118      17.557   0.905  21.693  1.00 25.44
ATOM    915  C   ASN A 118      18.289  -0.377  21.386  1.00 26.69
ATOM    916  O   ASN A 118      19.506  -0.222  21.069  1.00 27.32
ATOM    917  CB  ASN A 118      17.711   1.981  20.627  1.00 26.59
ATOM    918  CG  ASN A 118      17.049   1.629  19.274  1.00 27.12
ATOM    919  OD1 ASN A 118      17.115   0.418  19.004  1.00 29.87
ATOM    920  ND2 ASN A 118      16.462   2.559  18.601  1.00 21.35
ATOM    921  N   LYS A 119      17.635  -1.513  21.540  1.00 29.38
ATOM    922  CA  LYS A 119      18.309  -2.819  21.311  1.00 32.47
ATOM    923  C   LYS A 119      18.879  -3.061  19.880  1.00 33.14
ATOM    924  O   LYS A 119      19.770  -3.886  19.725  1.00 32.70
ATOM    925  CB  LYS A 119      17.404  -4.007  21.582  1.00 31.77
ATOM    926  CG  LYS A 119      17.518  -4.488  22.999  1.00 35.09
ATOM    927  CD  LYS A 119      16.296  -5.225  23.514  1.00 35.12
ATOM    928  CE  LYS A 119      16.359  -5.642  24.965  1.00 34.21
ATOM    929  NZ  LYS A 119      15.217  -6.488  25.378  1.00 35.24
ATOM    930  N   ASP A 120      18.318  -2.288  19.006  1.00 35.33
ATOM    931  CA  ASP A 120      18.693  -2.341  17.588  1.00 39.15
ATOM    932  C   ASP A 120      19.923  -1.476  17.348  1.00 39.04
ATOM    933  O   ASP A 120      20.636  -1.927  16.409  1.00 40.70
ATOM    934  CB  ASP A 120      17.515  -2.047  16.656  1.00 41.65
ATOM    935  CG  ASP A 120      16.435  -3.096  16.637  1.00 43.82
ATOM    936  OD1 ASP A 120      16.684  -4.294  16.979  1.00 45.34
ATOM    937  OD2 ASP A 120      15.294  -2.709  16.301  1.00 45.82
ATOM    938  N   LEU A 121      20.172  -0.364  17.982  1.00 38.50
ATOM    939  CA  LEU A 121      21.423   0.389  17.801  1.00 36.34
ATOM    940  C   LEU A 121      22.451  -0.169  18.791  1.00 37.77
ATOM    941  O   LEU A 121      23.648  -0.044  18.491  1.00 38.65
ATOM    942  CB  LEU A 121      21.275   1.875  18.047  1.00 36.56
ATOM    943  CG  LEU A 121      20.402   2.698  17.131  1.00 39.79
ATOM    944  CD1 LEU A 121      20.271   4.197  17.459  1.00 38.11
ATOM    945  CD2 LEU A 121      21.197   2.503  15.817  1.00 40.75
ATOM    946  N   LEU A 122      22.036  -0.712  19.908  1.00 39.02
ATOM    947  CA  LEU A 122      22.901  -1.158  21.038  1.00 40.84
ATOM    948  C   LEU A 122      22.415  -2.372  21.784  1.00 40.90
ATOM    949  O   LEU A 122      21.783  -2.245  22.858  1.00 40.10
ATOM    950  CB  LEU A 122      22.843   0.074  22.038  1.00 37.41
ATOM    951  CG  LEU A 122      24.045   0.545  22.773  1.00 36.20
ATOM    952  CD1 LEU A 122      25.172   1.133  21.918  1.00 31.92
ATOM    953  CD2 LEU A 122      23.560   1.681  23.729  1.00 35.75
ATOM    954  N   PRO A 123      22.602  -3.527  21.227  1.00 42.48
ATOM    955  CA  PRO A 123      22.122  -4.771  21.828  1.00 42.51
ATOM    956  C   PRO A 123      22.633  -4.856  23.250  1.00 42.49
ATOM    957  O   PRO A 123      21.889  -5.396  24.116  1.00 44.14
ATOM    958  CB  PRO A 123      22.697  -5.851  20.907  1.00 43.39
ATOM    959  CG  PRO A 123      23.921  -5.160  20.290  1.00 43.08
ATOM    960  CD  PRO A 123      23.281  -3.797  19.929  1.00 43.36
ATOM    961  N   ASN A 124      23.848  -4.411  23.500  1.00 40.11
ATOM    962  CA  ASN A 124      24.436  -4.430  24.893  1.00 39.28
ATOM    963  C   ASN A 124      24.699  -2.983  25.408  1.00 35.36
ATOM    964  O   ASN A 124      25.544  -2.200  24.866  1.00 35.83
ATOM    965  CB  ASN A 124      25.688  -5.242  24.919  1.00 43.22
ATOM    966  CG  ASN A 124      25.888  -6.630  24.398  1.00 45.68
ATOM    967  OD1 ASN A 124      25.135  -7.621  24.520  1.00 46.42
ATOM    968  ND2 ASN A 124      27.121  -6.708  23.831  1.00 48.20
ATOM    969  N   PRO A 125      24.023  -2.653  26.478  1.00 32.94
ATOM    970  CA  PRO A 125      24.146  -1.284  27.048  1.00 32.58
ATOM    971  C   PRO A 125      25.483  -1.158  27.717  1.00 32.47
ATOM    972  O   PRO A 125      26.119  -2.126  28.132  1.00 32.68
ATOM    973  CB  PRO A 125      22.934  -1.129  27.895  1.00 31.36
ATOM    974  CG  PRO A 125      22.571  -2.546  28.323  1.00 33.73
ATOM    975  CD  PRO A 125      23.048  -3.488  27.189  1.00 32.55
ATOM    976  N   PRO A 126      26.015   0.050  27.726  1.00 32.55
ATOM    977  CA  PRO A 126      27.316   0.333  28.373  1.00 33.12
ATOM    978  C   PRO A 126      27.197   0.107  29.898  1.00 32.17
ATOM    979  O   PRO A 126      26.114   0.402  30.493  1.00 32.16
ATOM    980  CB  PRO A 126      27.654   1.792  27.990  1.00 33.63
ATOM    981  CG  PRO A 126      26.534   2.218  27.065  1.00 34.70
ATOM    982  CD  PRO A 126      25.313   1.286  27.272  1.00 33.73
ATOM    983  N   LYS A 127      28.244  -0.322  30.560  1.00 29.30
ATOM    984  CA  LYS A 127      28.123  -0.543  32.003  1.00 30.59
ATOM    985  C   LYS A 127      28.671   0.640  32.807  1.00 29.38
ATOM    986  O   LYS A 127      28.465   0.821  34.026  1.00 27.74
ATOM    987  CB  LYS A 127      28.815  -1.906  32.256  1.00 35.30
ATOM    988  CG  LYS A 127      27.672  -2.976  32.501  1.00 41.24
ATOM    989  CD  LYS A 127      27.409  -3.916  31.380  1.00 47.13
ATOM    990  CE  LYS A 127      25.965  -4.441  31.151  1.00 48.12
ATOM    991  NZ  LYS A 127      25.942  -4.992  29.743  1.00 49.46
ATOM    992  N   THR A 128      29.275   1.560  32.043  1.00 26.29
ATOM    993  CA  THR A 128      30.002   2.696  32.648  1.00 26.05
ATOM    994  C   THR A 128      29.751   3.992  31.985  1.00 25.56
ATOM    995  O   THR A 128      29.543   4.077  30.763  1.00 24.55
ATOM    996  CB  THR A 128      31.509   2.123  32.488  1.00 25.96
ATOM    997  OG1 THR A 128      31.980   1.657  33.780  1.00 29.55
ATOM    998  CG2 THR A 128      32.328   2.998  31.601  1.00 25.62
ATOM    999  N   TRP A 129      29.686   5.095  32.775  1.00 22.57
ATOM   1000  CA  TRP A 129      29.465   6.386  32.176  1.00 21.86
ATOM   1001  C   TRP A 129      30.691   6.689  31.289  1.00 21.46
ATOM   1002  O   TRP A 129      30.647   7.383  30.271  1.00 21.15
ATOM   1003  CB  TRP A 129      29.350   7.436  33.317  1.00 23.76
ATOM   1004  CG  TRP A 129      27.973   7.644  33.848  1.00 24.64
ATOM   1005  CD1 TRP A 129      27.344   7.148  34.971  1.00 21.70
ATOM   1006  CD2 TRP A 129      26.994   8.467  33.156  1.00 23.36
ATOM   1007  NE1 TRP A 129      25.993   7.569  35.025  1.00 19.15
ATOM   1008  CE2 TRP A 129      25.784   8.394  33.975  1.00 22.69
ATOM   1009  CE3 TRP A 129      27.112   9.224  31.981  1.00 20.23
ATOM   1010  CZ2 TRP A 129      24.633   9.125  33.644  1.00 19.81
ATOM   1011  CZ3 TRP A 129      25.978   9.965  31.693  1.00 22.64
ATOM   1012  CH2 TRP A 129      24.821   9.925  32.549  1.00 22.50
ATOM   1013  N   GLU A 130      31.842   6.199  31.802  1.00 22.82
ATOM   1014  CA  GLU A 130      33.126   6.541  31.119  1.00 24.25
ATOM   1015  C   GLU A 130      33.219   6.034  29.700  1.00 25.21
ATOM   1016  O   GLU A 130      33.899   6.714  28.877  1.00 26.38
ATOM   1017  CB  GLU A 130      34.312   5.985  31.893  1.00 23.64
ATOM   1018  CG  GLU A 130      34.639   6.512  33.275  1.00 23.29
ATOM   1019  CD  GLU A 130      33.820   6.110  34.451  1.00 23.53
ATOM   1020  OE1 GLU A 130      32.810   5.417  34.290  1.00 25.25
ATOM   1021  OE2 GLU A 130      34.245   6.492  35.507  1.00 22.59
ATOM   1022  N   GLU A 131      32.555   4.966  29.351  1.00 26.58
ATOM   1023  CA  GLU A 131      32.687   4.538  27.900  1.00 28.26
ATOM   1024  C   GLU A 131      31.685   5.175  27.016  1.00 29.45
ATOM   1025  O   GLU A 131      31.565   4.850  25.804  1.00 31.04
ATOM   1026  CB  GLU A 131      32.585   3.038  27.821  1.00 29.03
ATOM   1027  CG  GLU A 131      31.257   2.417  28.043  1.00 32.54
ATOM   1028  CD  GLU A 131      31.238   1.034  28.644  1.00 37.41
ATOM   1029  OE1 GLU A 131      31.296   0.638  29.811  1.00 34.16
ATOM   1030  OE2 GLU A 131      31.135   0.166  27.697  1.00 40.94
ATOM   1031  N   ILE A 132      30.963   6.168  27.483  1.00 27.99
ATOM   1032  CA  ILE A 132      29.934   6.793  26.670  1.00 29.27
ATOM   1033  C   ILE A 132      30.536   7.669  25.596  1.00 28.86
ATOM   1034  O   ILE A 132      30.010   7.680  24.485  1.00 26.35
ATOM   1035  CB  ILE A 132      28.836   7.449  27.638  1.00 31.57
ATOM   1036  CG1 ILE A 132      28.032   6.218  28.228  1.00 31.14
ATOM   1037  CG2 ILE A 132      27.918   8.499  27.031  1.00 32.36
ATOM   1038  CD1 ILE A 132      26.841   6.685  29.152  1.00 31.26
ATOM   1039  N   PRO A 133      31.564   8.425  25.897  1.00 28.91
ATOM   1040  CA  PRO A 133      32.157   9.342  24.872  1.00 31.07
ATOM   1041  C   PRO A 133      32.598   8.567  23.602  1.00 31.73
ATOM   1042  O   PRO A 133      32.226   9.090  22.506  1.00 29.60
ATOM   1043  CB  PRO A 133      33.235  10.139  25.597  1.00 28.81
ATOM   1044  CG  PRO A 133      32.754  10.004  27.071  1.00 28.14
ATOM   1045  CD  PRO A 133      32.302   8.503  27.152  1.00 28.79
ATOM   1046  N   ALA A 134      33.318   7.463  23.823  1.00 31.30
ATOM   1047  CA  ALA A 134      33.800   6.605  22.741  1.00 33.72
ATOM   1048  C   ALA A 134      32.622   6.102  21.890  1.00 36.08
ATOM   1049  O   ALA A 134      32.423   6.103  20.647  1.00 35.96
ATOM   1050  CB  ALA A 134      34.529   5.397  23.285  1.00 31.65
ATOM   1051  N   LEU A 135      31.656   5.661  22.700  1.00 34.15
ATOM   1052  CA  LEU A 135      30.445   5.131  22.063  1.00 34.93
ATOM   1053  C   LEU A 135      29.796   6.160  21.167  1.00 33.16
ATOM   1054  O   LEU A 135      29.376   5.743  20.043  1.00 33.26
ATOM   1055  CB  LEU A 135      29.680   4.547  23.238  1.00 39.50
ATOM   1056  CG  LEU A 135      28.564   3.612  23.005  1.00 41.83
ATOM   1057  CD1 LEU A 135      28.801   2.802  21.706  1.00 47.69
ATOM   1058  CD2 LEU A 135      28.560   2.584  24.177  1.00 45.01
ATOM   1059  N   ASP A 136      29.671   7.398  21.520  1.00 30.98
ATOM   1060  CA  ASP A 136      29.034   8.489  20.776  1.00 32.77
ATOM   1061  C   ASP A 136      29.795   8.762  19.419  1.00 33.00
ATOM   1062  O   ASP A 136      29.090   9.043  18.463  1.00 32.16
ATOM   1063  CB  ASP A 136      28.971   9.772  21.588  1.00 28.33
ATOM   1064  CG  ASP A 136      28.260  10.882  20.962  1.00 25.93
ATOM   1065  OD1 ASP A 136      27.068  10.763  20.778  1.00 27.43
ATOM   1066  OD2 ASP A 136      28.822  11.936  20.566  1.00 26.00
ATOM   1067  N   LYS A 137      31.093   8.708  19.609  1.00 34.67
ATOM   1068  CA  LYS A 137      32.082   8.878  18.517  1.00 37.30
ATOM   1069  C   LYS A 137      31.658   7.898  17.382  1.00 37.40
ATOM   1070  O   LYS A 137      31.547   8.337  16.212  1.00 39.63
ATOM   1071  CB  LYS A 137      33.465   8.503  18.836  1.00 39.09
ATOM   1072  CG  LYS A 137      34.584   8.924  19.662  1.00 46.92
ATOM   1073  CD  LYS A 137      35.710   9.768  19.032  1.00 49.26
ATOM   1074  CE  LYS A 137      36.352   9.060  17.851  1.00 52.78
ATOM   1075  NZ  LYS A 137      36.712   9.901  16.659  1.00 51.95
ATOM   1076  N   GLU A 138      31.506   6.657  17.706  1.00 36.37
ATOM   1077  CA  GLU A 138      31.131   5.567  16.792  1.00 38.49
ATOM   1078  C   GLU A 138      29.771   5.708  16.157  1.00 38.52
ATOM   1079  O   GLU A 138      29.541   5.565  14.852  1.00 39.03
ATOM   1080  CB  GLU A 138      31.322   4.250  17.584  1.00 44.58
ATOM   1081  CG  GLU A 138      31.231   2.942  16.852  1.00 55.47
ATOM   1082  CD  GLU A 138      30.385   1.813  17.385  1.00 62.97
ATOM   1083  OE1 GLU A 138      30.769   1.052  18.312  1.00 67.50
ATOM   1084  OE2 GLU A 138      29.205   1.648  16.863  1.00 65.91
ATOM   1085  N   LEU A 139      28.747   6.087  16.923  1.00 34.54
ATOM   1086  CA  LEU A 139      27.379   6.218  16.456  1.00 31.46
ATOM   1087  C   LEU A 139      27.255   7.428  15.568  1.00 30.26
ATOM   1088  O   LEU A 139      26.443   7.412  14.653  1.00 28.42
ATOM   1089  CB  LEU A 139      26.496   6.315  17.760  1.00 29.40
ATOM   1090  CG  LEU A 139      26.319   4.913  18.331  1.00 31.35
ATOM   1091  CD1 LEU A 139      25.802   4.838  19.755  1.00 30.17
ATOM   1092  CD2 LEU A 139      25.261   4.245  17.425  1.00 31.91
ATOM   1093  N   LYS A 140      27.915   8.488  15.908  1.00 30.18
ATOM   1094  CA  LYS A 140      27.885   9.780  15.257  1.00 32.84
ATOM   1095  C   LYS A 140      28.353   9.786  13.782  1.00 34.06
ATOM   1096  O   LYS A 140      27.988  10.749  13.069  1.00 34.27
ATOM   1097  CB  LYS A 140      28.795  10.733  16.063  1.00 34.78
ATOM   1098  CG  LYS A 140      28.098  12.024  16.486  1.00 37.71
ATOM   1099  CD  LYS A 140      27.192  11.899  17.633  1.00 40.28
ATOM   1100  CE  LYS A 140      26.706  13.215  18.238  1.00 41.69
ATOM   1101  NZ  LYS A 140      27.399  13.479  19.505  1.00 41.23
ATOM   1102  N   ALA A 141      29.199   8.859  13.488  1.00 33.89
ATOM   1103  CA  ALA A 141      29.829   8.499  12.246  1.00 37.28
ATOM   1104  C   ALA A 141      28.768   7.876  11.334  1.00 39.10
ATOM   1105  O   ALA A 141      28.751   7.767  10.058  1.00 39.46
ATOM   1106  CB  ALA A 141      30.962   7.471  12.526  1.00 32.82
ATOM   1107  N   LYS A 142      27.733   7.409  12.009  1.00 40.23
ATOM   1108  CA  LYS A 142      26.545   6.718  11.422  1.00 39.72
ATOM   1109  C   LYS A 142      25.279   7.568  11.480  1.00 37.42
ATOM   1110  O   LYS A 142      24.146   7.027  11.255  1.00 38.80
ATOM   1111  CB  LYS A 142      26.519   5.416  12.193  1.00 45.85
ATOM   1112  CG  LYS A 142      25.419   4.444  12.319  1.00 52.15
ATOM   1113  CD  LYS A 142      25.357   3.596  13.589  1.00 55.05
ATOM   1114  CE  LYS A 142      26.666   3.127  14.222  1.00 56.87
ATOM   1115  NZ  LYS A 142      26.426   1.746  14.801  1.00 58.67
ATOM   1116  N   GLY A 143      25.377   8.849  11.717  1.00 33.77
ATOM   1117  CA  GLY A 143      24.403   9.876  11.883  1.00 33.48
ATOM   1118  C   GLY A 143      23.620   9.839  13.225  1.00 35.29
ATOM   1119  O   GLY A 143      22.631  10.619  13.312  1.00 35.98
ATOM   1120  N   LYS A 144      23.921   9.000  14.194  1.00 35.17
ATOM   1121  CA  LYS A 144      23.218   8.844  15.491  1.00 35.16
ATOM   1122  C   LYS A 144      24.012   9.459  16.644  1.00 35.75
ATOM   1123  O   LYS A 144      24.980  10.225  16.415  1.00 38.19
ATOM   1124  CB  LYS A 144      22.949   7.395  15.876  1.00 35.87
ATOM   1125  CG  LYS A 144      22.443   6.460  14.823  1.00 35.99
ATOM   1126  CD  LYS A 144      21.036   6.075  14.663  1.00 33.97
ATOM   1127  CE  LYS A 144      20.180   7.068  13.925  1.00 38.75
ATOM   1128  NZ  LYS A 144      19.044   6.314  13.281  1.00 38.43
ATOM   1129  N   SER A 145      23.500   9.239  17.888  1.00 34.06
ATOM   1130  CA  SER A 145      24.133   9.702  19.163  1.00 28.65
ATOM   1131  C   SER A 145      23.901   8.582  20.223  1.00 23.82
ATOM   1132  O   SER A 145      23.001   7.780  20.078  1.00 22.93
ATOM   1133  CB  SER A 145      23.728  11.013  19.723  1.00 31.63
ATOM   1134  OG  SER A 145      22.383  11.199  19.917  1.00 27.82
ATOM   1135  N   ALA A 146      24.792   8.593  21.155  1.00 20.93
ATOM   1136  CA  ALA A 146      24.775   7.628  22.196  1.00 19.86
ATOM   1137  C   ALA A 146      23.649   7.892  23.204  1.00 19.94
ATOM   1138  O   ALA A 146      23.000   6.951  23.609  1.00 21.08
ATOM   1139  CB  ALA A 146      26.157   7.671  22.899  1.00 21.37
ATOM   1140  N   LEU A 147      23.475   9.108  23.689  1.00 21.36
ATOM   1141  CA  LEU A 147      22.561   9.427  24.770  1.00 21.37
ATOM   1142  C   LEU A 147      21.951  10.756  24.782  1.00 22.34
ATOM   1143  O   LEU A 147      22.687  11.779  24.540  1.00 25.69
ATOM   1144  CB  LEU A 147      23.510   9.166  26.075  1.00 21.18
ATOM   1145  CG  LEU A 147      22.834   9.704  27.401  1.00 19.46
ATOM   1146  CD1 LEU A 147      21.742   8.728  27.775  1.00 18.99
ATOM   1147  CD2 LEU A 147      23.874   9.666  28.476  1.00 22.26
ATOM   1148  N   MET A 148      20.646  10.871  25.127  1.00 21.41
ATOM   1149  CA  MET A 148      20.095  12.204  25.251  1.00 20.17
ATOM   1150  C   MET A 148      19.099  12.118  26.386  1.00 19.47
ATOM   1151  O   MET A 148      18.278  11.150  26.345  1.00 20.53
ATOM   1152  CB  MET A 148      19.465  12.546  23.893  1.00 27.47
ATOM   1153  CG  MET A 148      20.633  13.059  22.976  1.00 35.08
ATOM   1154  SD  MET A 148      19.904  14.717  22.457  1.00 46.75
ATOM   1155  CE  MET A 148      18.929  13.863  21.182  1.00 42.98
ATOM   1156  N   PHE A 149      19.129  13.060  27.285  1.00 18.88
ATOM   1157  CA  PHE A 149      18.078  12.987  28.421  1.00 19.68
ATOM   1158  C   PHE A 149      17.851  14.415  28.854  1.00 18.60
ATOM   1159  O   PHE A 149      18.684  15.375  28.532  1.00 19.25
ATOM   1160  CB  PHE A 149      18.515  12.014  29.546  1.00 19.01
ATOM   1161  CG  PHE A 149      19.710  12.438  30.282  1.00 20.43
ATOM   1162  CD1 PHE A 149      21.015  12.177  29.802  1.00 21.31
ATOM   1163  CD2 PHE A 149      19.544  13.190  31.466  1.00 20.80
ATOM   1164  CE1 PHE A 149      22.206  12.535  30.425  1.00 21.32
ATOM   1165  CE2 PHE A 149      20.727  13.522  32.140  1.00 21.42
ATOM   1166  CZ  PHE A 149      22.064  13.274  31.626  1.00 23.43
ATOM   1167  N   ASN A 150      16.797  14.626  29.603  1.00 19.32
ATOM   1168  CA  ASN A 150      16.416  15.963  30.070  1.00 20.03
ATOM   1169  C   ASN A 150      17.490  16.600  30.962  1.00 22.66
ATOM   1170  O   ASN A 150      17.538  16.189  32.149  1.00 24.25
ATOM   1171  CB  ASN A 150      15.083  15.914  30.815  1.00 19.28
ATOM   1172  CG  ASN A 150      14.534  17.258  31.189  1.00 18.73
ATOM   1173  OD1 ASN A 150      15.109  18.351  30.884  1.00 20.25
ATOM   1174  ND2 ASN A 150      13.400  17.371  31.846  1.00 16.14
ATOM   1175  N   LEU A 151      18.162  17.657  30.553  1.00 20.81
ATOM   1176  CA  LEU A 151      19.160  18.367  31.294  1.00 21.48
ATOM   1177  C   LEU A 151      18.607  19.600  32.032  1.00 19.34
ATOM   1178  O   LEU A 151      19.390  20.171  32.835  1.00 22.89
ATOM   1179  CB  LEU A 151      20.364  18.788  30.381  1.00 25.44
ATOM   1180  CG  LEU A 151      21.236  17.826  29.682  1.00 23.21
ATOM   1181  CD1 LEU A 151      22.403  18.619  29.067  1.00 26.52
ATOM   1182  CD2 LEU A 151      21.863  16.771  30.613  1.00 26.43
ATOM   1183  N   GLN A 152      17.396  19.936  31.792  1.00 19.02
ATOM   1184  CA  GLN A 152      16.756  21.068  32.351  1.00 18.15
ATOM   1185  C   GLN A 152      16.245  20.741  33.763  1.00 19.90
ATOM   1186  O   GLN A 152      16.090  21.729  34.538  1.00 21.14
ATOM   1187  CB  GLN A 152      15.589  21.588  31.512  1.00 19.90
ATOM   1188  CG  GLN A 152      16.003  21.983  30.072  1.00 22.68
ATOM   1189  CD  GLN A 152      17.369  22.594  29.985  1.00 29.43
ATOM   1190  OE1 GLN A 152      17.703  23.649  30.614  1.00 32.52
ATOM   1191  NE2 GLN A 152      18.280  21.940  29.258  1.00 29.24
ATOM   1192  N   GLU A 153      15.950  19.566  34.152  1.00 19.66
ATOM   1193  CA  GLU A 153      15.435  19.056  35.492  1.00 18.94
ATOM   1194  C   GLU A 153      16.489  18.289  36.268  1.00 15.92
ATOM   1195  O   GLU A 153      16.988  17.255  35.745  1.00 14.78
ATOM   1196  CB  GLU A 153      14.168  18.215  35.200  1.00 17.08
ATOM   1197  CG  GLU A 153      12.916  19.120  35.085  1.00 19.50
ATOM   1198  CD  GLU A 153      12.481  19.954  36.237  1.00 23.65
ATOM   1199  OE1 GLU A 153      12.974  19.921  37.378  1.00 26.26
ATOM   1200  OE2 GLU A 153      11.689  20.876  36.066  1.00 28.40
ATOM   1201  N   PRO A 154      16.875  18.840  37.451  1.00 16.54
ATOM   1202  CA  PRO A 154      17.996  18.313  38.233  1.00 17.66
ATOM   1203  C   PRO A 154      17.848  16.878  38.632  1.00 17.05
ATOM   1204  O   PRO A 154      18.799  16.177  38.912  1.00 15.56
ATOM   1205  CB  PRO A 154      18.201  19.321  39.422  1.00 16.88
ATOM   1206  CG  PRO A 154      16.893  20.069  39.596  1.00 14.65
ATOM   1207  CD  PRO A 154      16.372  20.097  38.096  1.00 16.95
ATOM   1208  N   TYR A 155      16.560  16.473  38.633  1.00 17.84
ATOM   1209  CA  TYR A 155      16.161  15.098  38.967  1.00 17.52
ATOM   1210  C   TYR A 155      16.866  14.065  38.016  1.00 17.68
ATOM   1211  O   TYR A 155      17.290  13.006  38.534  1.00 15.47
ATOM   1212  CB  TYR A 155      14.683  14.891  38.778  1.00 15.96
ATOM   1213  CG  TYR A 155      14.044  13.567  39.058  1.00 17.22
ATOM   1214  CD1 TYR A 155      13.805  13.113  40.408  1.00 15.10
ATOM   1215  CD2 TYR A 155      13.636  12.713  38.019  1.00 15.47
ATOM   1216  CE1 TYR A 155      13.150  11.942  40.613  1.00 12.71
ATOM   1217  CE2 TYR A 155      12.912  11.556  38.245  1.00 18.63
ATOM   1218  CZ  TYR A 155      12.684  11.121  39.606  1.00 16.35
ATOM   1219  OH  TYR A 155      12.033   9.935  39.696  1.00 14.77
ATOM   1220  N   PHE A 156      17.083  14.498  36.771  1.00 17.87
ATOM   1221  CA  PHE A 156      17.662  13.542  35.740  1.00 18.74
ATOM   1222  C   PHE A 156      19.169  13.375  35.796  1.00 15.96
ATOM   1223  O   PHE A 156      19.715  12.297  35.517  1.00 16.44
ATOM   1224  CB  PHE A 156      17.109  14.011  34.371  1.00 16.91
ATOM   1225  CG  PHE A 156      15.678  13.760  34.189  1.00 14.20
ATOM   1226  CD1 PHE A 156      15.292  12.566  33.622  1.00 15.82
ATOM   1227  CD2 PHE A 156      14.751  14.773  34.473  1.00 14.97
ATOM   1228  CE1 PHE A 156      13.947  12.297  33.394  1.00 16.32
ATOM   1229  CE2 PHE A 156      13.385  14.475  34.326  1.00 17.43
ATOM   1230  CZ  PHE A 156      13.018  13.251  33.761  1.00 15.10
ATOM   1231  N   THR A 157      19.730  14.511  36.248  1.00 16.55
ATOM   1232  CA  THR A 157      21.187  14.607  36.451  1.00 19.13
ATOM   1233  C   THR A 157      21.685  14.160  37.857  1.00 18.04
ATOM   1234  O   THR A 157      22.863  13.801  37.917  1.00 16.39
ATOM   1235  CB  THR A 157      21.713  16.042  36.071  1.00 19.65
ATOM   1236  OG1 THR A 157      20.925  17.040  36.805  1.00 24.06
ATOM   1237  CG2 THR A 157      21.573  16.240  34.565  1.00 18.96
ATOM   1238  N   TRP A 158      20.879  14.247  38.927  1.00 15.63
ATOM   1239  CA  TRP A 158      21.282  13.853  40.256  1.00 13.96
ATOM   1240  C   TRP A 158      21.878  12.517  40.319  1.00 12.85
ATOM   1241  O   TRP A 158      22.886  12.381  41.060  1.00 14.31
ATOM   1242  CB  TRP A 158      19.973  13.879  41.152  1.00 16.97
ATOM   1243  CG  TRP A 158      20.410  13.643  42.566  1.00 17.27
ATOM   1244  CD1 TRP A 158      20.221  12.506  43.308  1.00 17.36
ATOM   1245  CD2 TRP A 158      21.188  14.562  43.352  1.00 17.58
ATOM   1246  NE1 TRP A 158      20.794  12.674  44.560  1.00 18.30
ATOM   1247  CE2 TRP A 158      21.418  13.919  44.600  1.00 17.36
ATOM   1248  CE3 TRP A 158      21.714  15.844  43.096  1.00 15.95
ATOM   1249  CZ2 TRP A 158      22.097  14.537  45.619  1.00 16.45
ATOM   1250  CZ3 TRP A 158      22.511  16.413  44.081  1.00 16.21
ATOM   1251  CH2 TRP A 158      22.637  15.773  45.353  1.00 18.62
ATOM   1252  N   PRO A 159      21.496  11.456  39.651  1.00 14.65
ATOM   1253  CA  PRO A 159      22.179  10.139  39.824  1.00 15.35
ATOM   1254  C   PRO A 159      23.664  10.138  39.596  1.00 17.00
ATOM   1255  O   PRO A 159      24.461   9.407  40.229  1.00 15.38
ATOM   1256  CB  PRO A 159      21.464   9.187  38.852  1.00 17.35
ATOM   1257  CG  PRO A 159      20.227   9.897  38.347  1.00 14.75
ATOM   1258  CD  PRO A 159      20.306  11.344  38.763  1.00 13.38
ATOM   1259  N   LEU A 160      24.125  10.963  38.636  1.00 16.15
ATOM   1260  CA  LEU A 160      25.553  11.047  38.332  1.00 17.64
ATOM   1261  C   LEU A 160      26.295  11.886  39.399  1.00 19.03
ATOM   1262  O   LEU A 160      27.464  11.657  39.732  1.00 17.80
ATOM   1263  CB  LEU A 160      25.708  11.732  36.951  1.00 19.59
ATOM   1264  CG  LEU A 160      26.820  11.568  35.979  1.00 24.01
ATOM   1265  CD1 LEU A 160      27.009  12.822  35.144  1.00 23.52
ATOM   1266  CD2 LEU A 160      28.131  11.016  36.464  1.00 21.49
ATOM   1267  N   ILE A 161      25.607  12.985  39.831  1.00 17.61
ATOM   1268  CA  ILE A 161      26.181  13.856  40.870  1.00 19.06
ATOM   1269  C   ILE A 161      26.339  13.119  42.200  1.00 15.48
ATOM   1270  O   ILE A 161      27.359  13.193  42.932  1.00 17.73
ATOM   1271  CB  ILE A 161      25.277  15.153  41.048  1.00 19.32
ATOM   1272  CG1 ILE A 161      25.427  15.948  39.723  1.00 17.80
ATOM   1273  CG2 ILE A 161      25.638  15.949  42.317  1.00 17.58
ATOM   1274  CD1 ILE A 161      24.445  17.147  39.579  1.00 26.58
ATOM   1275  N   ALA A 162      25.351  12.363  42.506  1.00 16.22
ATOM   1276  CA  ALA A 162      25.404  11.598  43.751  1.00 15.36
ATOM   1277  C   ALA A 162      26.294  10.402  43.617  1.00 18.02
ATOM   1278  O   ALA A 162      26.746   9.939  44.710  1.00 18.02
ATOM   1279  CB  ALA A 162      23.991  11.152  44.030  1.00 13.85
ATOM   1280  N   ALA A 163      26.625   9.758  42.465  1.00 15.72
ATOM   1281  CA  ALA A 163      27.381   8.530  42.375  1.00 14.97
ATOM   1282  C   ALA A 163      28.645   8.449  43.163  1.00 16.66
ATOM   1283  O   ALA A 163      28.884   7.475  43.916  1.00 16.94
ATOM   1284  CB  ALA A 163      27.709   8.320  40.824  1.00 16.08
ATOM   1285  N   ASP A 164      29.545   9.407  43.027  1.00 18.03
ATOM   1286  CA  ASP A 164      30.852   9.452  43.690  1.00 20.53
ATOM   1287  C   ASP A 164      30.766  10.218  45.023  1.00 22.27
ATOM   1288  O   ASP A 164      31.848  10.567  45.554  1.00 21.20
ATOM   1289  CB  ASP A 164      31.915  10.029  42.724  1.00 21.07
ATOM   1290  CG  ASP A 164      33.364   9.854  43.220  1.00 25.94
ATOM   1291  OD1 ASP A 164      33.696   8.790  43.729  1.00 26.99
ATOM   1292  OD2 ASP A 164      34.043  10.944  43.108  1.00 28.83
ATOM   1293  N   GLY A 165      29.579  10.475  45.565  1.00 23.05
ATOM   1294  CA  GLY A 165      29.453  11.145  46.880  1.00 20.68
ATOM   1295  C   GLY A 165      28.612  12.336  46.997  1.00 21.01
ATOM   1296  O   GLY A 165      28.681  12.788  48.176  1.00 21.59
ATOM   1297  N   GLY A 166      28.003  12.989  46.016  1.00 18.67
ATOM   1298  CA  GLY A 166      27.192  14.211  46.280  1.00 18.91
ATOM   1299  C   GLY A 166      26.043  13.782  47.120  1.00 18.36
ATOM   1300  O   GLY A 166      25.593  12.616  47.113  1.00 17.37
ATOM   1301  N   TYR A 167      25.458  14.694  47.900  1.00 19.38
ATOM   1302  CA  TYR A 167      24.266  14.299  48.741  1.00 18.48
ATOM   1303  C   TYR A 167      23.469  15.565  49.068  1.00 18.17
ATOM   1304  O   TYR A 167      24.098  16.657  48.969  1.00 19.60
ATOM   1305  CB  TYR A 167      24.541  13.501  50.036  1.00 17.22
ATOM   1306  CG  TYR A 167      25.450  14.158  51.046  1.00 18.37
ATOM   1307  CD1 TYR A 167      24.844  15.002  52.014  1.00 14.44
ATOM   1308  CD2 TYR A 167      26.834  13.891  51.017  1.00 16.39
ATOM   1309  CE1 TYR A 167      25.681  15.613  52.940  1.00 16.23
ATOM   1310  CE2 TYR A 167      27.662  14.520  51.975  1.00 18.28
ATOM   1311  CZ  TYR A 167      27.009  15.305  52.965  1.00 16.57
ATOM   1312  OH  TYR A 167      27.859  15.955  53.867  1.00 17.88
ATOM   1313  N   ALA A 168      22.184  15.399  49.329  1.00 16.38
ATOM   1314  CA  ALA A 168      21.333  16.559  49.663  1.00 17.55
ATOM   1315  C   ALA A 168      21.587  17.005  51.112  1.00 16.43
ATOM   1316  O   ALA A 168      22.267  17.998  51.343  1.00 16.71
ATOM   1317  CB  ALA A 168      19.851  16.252  49.280  1.00 15.16
ATOM   1318  N   PHE A 169      21.019  16.376  52.087  1.00 16.65
ATOM   1319  CA  PHE A 169      21.056  16.599  53.545  1.00 18.18
ATOM   1320  C   PHE A 169      21.531  15.291  54.210  1.00 18.73
ATOM   1321  O   PHE A 169      21.146  14.178  53.787  1.00 20.00
ATOM   1322  CB  PHE A 169      19.641  17.044  54.041  1.00 17.00
ATOM   1323  CG  PHE A 169      19.187  18.317  53.366  1.00 21.24
ATOM   1324  CD1 PHE A 169      19.772  19.566  53.711  1.00 19.53
ATOM   1325  CD2 PHE A 169      18.146  18.304  52.397  1.00 20.17
ATOM   1326  CE1 PHE A 169      19.346  20.727  53.120  1.00 20.94
ATOM   1327  CE2 PHE A 169      17.771  19.465  51.706  1.00 18.36
ATOM   1328  CZ  PHE A 169      18.322  20.665  52.128  1.00 21.41
ATOM   1329  N   LYS A 170      22.466  15.432  55.067  1.00 16.42
ATOM   1330  CA  LYS A 170      23.008  14.346  55.852  1.00 19.52
ATOM   1331  C   LYS A 170      21.893  13.922  56.854  1.00 25.16
ATOM   1332  O   LYS A 170      21.265  14.817  57.443  1.00 23.27
ATOM   1333  CB  LYS A 170      24.218  14.756  56.642  1.00 18.39
ATOM   1334  CG  LYS A 170      24.945  13.675  57.369  1.00 24.00
ATOM   1335  CD  LYS A 170      25.676  12.689  56.481  1.00 28.25
ATOM   1336  CE  LYS A 170      26.993  13.220  55.939  1.00 32.53
ATOM   1337  NZ  LYS A 170      27.822  14.096  56.841  1.00 30.72
ATOM   1338  N   TYR A 171      21.622  12.627  56.863  1.00 27.38
ATOM   1339  CA  TYR A 171      20.700  11.975  57.710  1.00 34.77
ATOM   1340  C   TYR A 171      21.521  11.621  58.989  1.00 39.14
ATOM   1341  O   TYR A 171      22.473  10.809  58.911  1.00 41.35
ATOM   1342  CB  TYR A 171      20.113  10.697  57.096  1.00 40.41
ATOM   1343  CG  TYR A 171      19.030  10.240  58.058  1.00 48.20
ATOM   1344  CD1 TYR A 171      17.815  10.947  58.096  1.00 50.76
ATOM   1345  CD2 TYR A 171      19.231   9.224  58.990  1.00 52.69
ATOM   1346  CE1 TYR A 171      16.764  10.560  58.916  1.00 54.59
ATOM   1347  CE2 TYR A 171      18.202   8.852  59.897  1.00 55.71
ATOM   1348  CZ  TYR A 171      16.972   9.509  59.842  1.00 57.07
ATOM   1349  OH  TYR A 171      15.972   9.199  60.751  1.00 59.64
ATOM   1350  N   GLU A 172      21.286  12.262  60.119  1.00 41.29
ATOM   1351  CA  GLU A 172      22.138  11.971  61.270  1.00 44.84
ATOM   1352  C   GLU A 172      21.301  11.846  62.516  1.00 49.78
ATOM   1353  O   GLU A 172      20.620  12.859  62.879  1.00 50.32
ATOM   1354  CB  GLU A 172      23.021  13.212  61.453  1.00 44.88
ATOM   1355  CG  GLU A 172      23.795  13.137  62.802  1.00 47.17
ATOM   1356  CD  GLU A 172      24.821  12.015  62.751  1.00 49.17
ATOM   1357  OE1 GLU A 172      25.156  11.364  61.748  1.00 49.86
ATOM   1358  OE2 GLU A 172      25.274  11.902  63.912  1.00 49.72
ATOM   1359  N   ASN A 173      21.279  10.674  63.123  1.00 54.43
ATOM   1360  CA  ASN A 173      20.508  10.338  64.364  1.00 56.20
ATOM   1361  C   ASN A 173      19.044  10.803  64.308  1.00 54.73
ATOM   1362  O   ASN A 173      18.562  11.819  64.886  1.00 53.96
ATOM   1363  CB  ASN A 173      21.273  10.719  65.605  1.00 61.89
ATOM   1364  CG  ASN A 173      20.796  11.858  66.455  1.00 66.68
ATOM   1365  OD1 ASN A 173      20.584  11.689  67.707  1.00 69.43
ATOM   1366  ND2 ASN A 173      20.627  13.056  65.859  1.00 68.20
ATOM   1367  N   GLY A 174      18.315   9.956  63.541  1.00 53.11
ATOM   1368  CA  GLY A 174      16.875  10.139  63.369  1.00 51.08
ATOM   1369  C   GLY A 174      16.386  11.368  62.602  1.00 48.26
ATOM   1370  O   GLY A 174      15.144  11.513  62.392  1.00 47.86
ATOM   1371  N   LYS A 175      17.379  12.205  62.204  1.00 43.97
ATOM   1372  CA  LYS A 175      16.866  13.341  61.398  1.00 39.57
ATOM   1373  C   LYS A 175      17.946  13.869  60.487  1.00 34.32
ATOM   1374  O   LYS A 175      19.106  13.543  60.446  1.00 32.03
ATOM   1375  CB  LYS A 175      16.086  14.224  62.334  1.00 45.04
ATOM   1376  CG  LYS A 175      16.595  15.514  62.855  1.00 48.29
ATOM   1377  CD  LYS A 175      17.353  15.337  64.160  1.00 53.19
ATOM   1378  CE  LYS A 175      18.181  16.637  64.329  1.00 57.90
ATOM   1379  NZ  LYS A 175      17.122  17.755  64.454  1.00 60.97
ATOM   1380  N   TYR A 176      17.443  14.712  59.567  1.00 32.03
ATOM   1381  CA  TYR A 176      18.196  15.411  58.561  1.00 27.31
ATOM   1382  C   TYR A 176      18.776  16.704  59.166  1.00 26.63
ATOM   1383  O   TYR A 176      17.971  17.515  59.661  1.00 24.94
ATOM   1384  CB  TYR A 176      17.288  15.832  57.367  1.00 26.98
ATOM   1385  CG  TYR A 176      17.036  14.617  56.476  1.00 25.30
ATOM   1386  CD1 TYR A 176      18.012  14.074  55.674  1.00 24.47
ATOM   1387  CD2 TYR A 176      15.766  14.021  56.564  1.00 26.58
ATOM   1388  CE1 TYR A 176      17.762  12.921  54.942  1.00 26.71
ATOM   1389  CE2 TYR A 176      15.481  12.848  55.834  1.00 24.27
ATOM   1390  CZ  TYR A 176      16.495  12.337  55.048  1.00 26.88
ATOM   1391  OH  TYR A 176      16.194  11.177  54.359  1.00 30.46
ATOM   1392  N   ASP A 177      20.082  16.824  58.975  1.00 22.24
ATOM   1393  CA  ASP A 177      20.814  18.013  59.325  1.00 21.72
ATOM   1394  C   ASP A 177      20.753  18.954  58.071  1.00 22.98
ATOM   1395  O   ASP A 177      21.354  18.758  56.974  1.00 22.36
ATOM   1396  CB  ASP A 177      22.220  17.695  59.810  1.00 20.48
ATOM   1397  CG  ASP A 177      23.032  18.858  60.287  1.00 20.00
ATOM   1398  OD1 ASP A 177      22.716  20.037  59.984  1.00 21.11
ATOM   1399  OD2 ASP A 177      24.135  18.666  60.930  1.00 23.61
ATOM   1400  N   ILE A 178      19.989  20.013  58.268  1.00 20.56
ATOM   1401  CA  ILE A 178      19.766  21.042  57.269  1.00 21.01
ATOM   1402  C   ILE A 178      20.967  21.920  56.971  1.00 22.14
ATOM   1403  O   ILE A 178      21.050  22.651  55.914  1.00 21.96
ATOM   1404  CB  ILE A 178      18.445  21.830  57.588  1.00 25.30
ATOM   1405  CG1 ILE A 178      18.564  22.717  58.859  1.00 26.02
ATOM   1406  CG2 ILE A 178      17.192  20.878  57.640  1.00 25.59
ATOM   1407  CD1 ILE A 178      17.646  24.020  58.690  1.00 28.97
ATOM   1408  N   LYS A 179      21.992  21.788  57.825  1.00 21.35
ATOM   1409  CA  LYS A 179      23.180  22.617  57.631  1.00 20.35
ATOM   1410  C   LYS A 179      24.258  21.738  57.060  1.00 20.36
ATOM   1411  O   LYS A 179      25.280  22.337  56.786  1.00 21.95
ATOM   1412  CB  LYS A 179      23.638  23.216  58.950  1.00 25.32
ATOM   1413  CG  LYS A 179      22.688  24.299  59.603  1.00 23.83
ATOM   1414  CD  LYS A 179      22.345  25.314  58.528  1.00 29.38
ATOM   1415  CE  LYS A 179      21.955  26.665  59.042  1.00 34.12
ATOM   1416  NZ  LYS A 179      20.908  27.283  58.140  1.00 39.01
ATOM   1417  N   ASP A 180      24.072  20.437  56.978  1.00 19.40
ATOM   1418  CA  ASP A 180      25.063  19.533  56.391  1.00 18.28
ATOM   1419  C   ASP A 180      24.538  19.080  54.989  1.00 18.53
ATOM   1420  O   ASP A 180      23.811  18.154  54.817  1.00 19.18
ATOM   1421  CB  ASP A 180      25.449  18.394  57.364  1.00 19.14
ATOM   1422  CG  ASP A 180      26.481  17.392  56.828  1.00 18.04
ATOM   1423  OD1 ASP A 180      26.880  17.564  55.617  1.00 20.66
ATOM   1424  OD2 ASP A 180      26.948  16.443  57.488  1.00 19.45
ATOM   1425  N   VAL A 181      25.057  19.779  53.930  1.00 18.25
ATOM   1426  CA  VAL A 181      24.697  19.586  52.544  1.00 19.42
ATOM   1427  C   VAL A 181      25.834  19.026  51.699  1.00 20.26
ATOM   1428  O   VAL A 181      27.009  19.418  51.956  1.00 22.09
ATOM   1429  CB  VAL A 181      24.099  20.952  52.017  1.00 19.84
ATOM   1430  CG1 VAL A 181      23.872  21.080  50.545  1.00 23.06
ATOM   1431  CG2 VAL A 181      22.789  21.337  52.784  1.00 22.24
ATOM   1432  N   GLY A 182      25.633  18.200  50.654  1.00 19.30
ATOM   1433  CA  GLY A 182      26.819  17.629  49.970  1.00 17.47
ATOM   1434  C   GLY A 182      26.757  17.866  48.524  1.00 18.58
ATOM   1435  O   GLY A 182      27.109  17.019  47.727  1.00 17.93
ATOM   1436  N   VAL A 183      26.403  19.155  48.304  1.00 18.41
ATOM   1437  CA  VAL A 183      26.238  19.575  46.845  1.00 19.05
ATOM   1438  C   VAL A 183      27.515  20.123  46.325  1.00 21.56
ATOM   1439  O   VAL A 183      27.725  20.097  45.088  1.00 23.71
ATOM   1440  CB  VAL A 183      25.042  20.465  46.499  1.00 18.11
ATOM   1441  CG1 VAL A 183      23.680  20.025  47.026  1.00 16.33
ATOM   1442  CG2 VAL A 183      25.180  21.883  46.833  1.00 21.20
ATOM   1443  N   ASP A 184      28.429  20.500  47.148  1.00 22.46
ATOM   1444  CA  ASP A 184      29.700  21.035  46.686  1.00 21.61
ATOM   1445  C   ASP A 184      30.872  20.210  47.112  1.00 21.88
ATOM   1446  O   ASP A 184      32.024  20.769  47.251  1.00 25.88
ATOM   1447  CB  ASP A 184      29.676  22.474  47.278  1.00 24.20
ATOM   1448  CG  ASP A 184      30.870  23.211  46.797  1.00 28.76
ATOM   1449  OD1 ASP A 184      31.254  22.939  45.588  1.00 34.87
ATOM   1450  OD2 ASP A 184      31.463  24.010  47.498  1.00 31.18
ATOM   1451  N   ASN A 185      30.674  18.972  47.483  1.00 20.12
ATOM   1452  CA  ASN A 185      31.863  18.174  47.932  1.00 18.13
ATOM   1453  C   ASN A 185      32.600  17.575  46.686  1.00 19.20
ATOM   1454  O   ASN A 185      32.236  17.820  45.491  1.00 18.29
ATOM   1455  CB  ASN A 185      31.324  17.188  48.976  1.00 20.37
ATOM   1456  CG  ASN A 185      30.421  16.095  48.566  1.00 22.20
ATOM   1457  OD1 ASN A 185      30.299  15.777  47.303  1.00 22.18
ATOM   1458  ND2 ASN A 185      29.713  15.385  49.419  1.00 21.74
ATOM   1459  N   ALA A 186      33.662  16.836  46.929  1.00 17.44
ATOM   1460  CA  ALA A 186      34.482  16.287  45.862  1.00 19.37
ATOM   1461  C   ALA A 186      33.638  15.350  45.002  1.00 19.66
ATOM   1462  O   ALA A 186      33.935  15.386  43.754  1.00 22.04
ATOM   1463  CB  ALA A 186      35.744  15.595  46.440  1.00 18.22
ATOM   1464  N   GLY A 187      32.725  14.550  45.439  1.00 17.85
ATOM   1465  CA  GLY A 187      31.970  13.637  44.538  1.00 18.40
ATOM   1466  C   GLY A 187      31.026  14.327  43.632  1.00 16.98
ATOM   1467  O   GLY A 187      30.782  13.974  42.446  1.00 16.61
ATOM   1468  N   ALA A 188      30.375  15.325  44.210  1.00 16.28
ATOM   1469  CA  ALA A 188      29.435  16.165  43.476  1.00 16.04
ATOM   1470  C   ALA A 188      30.194  16.946  42.364  1.00 18.67
ATOM   1471  O   ALA A 188      29.673  16.980  41.173  1.00 18.92
ATOM   1472  CB  ALA A 188      28.704  17.121  44.403  1.00 16.65
ATOM   1473  N   LYS A 189      31.341  17.500  42.716  1.00 18.63
ATOM   1474  CA  LYS A 189      32.166  18.215  41.705  1.00 20.48
ATOM   1475  C   LYS A 189      32.641  17.227  40.572  1.00 20.71
ATOM   1476  O   LYS A 189      32.599  17.614  39.310  1.00 18.91
ATOM   1477  CB  LYS A 189      33.410  18.941  42.250  1.00 17.18
ATOM   1478  CG  LYS A 189      32.930  20.175  43.085  1.00 17.51
ATOM   1479  CD  LYS A 189      34.120  20.844  43.813  1.00 18.61
ATOM   1480  CE  LYS A 189      35.007  19.843  44.441  1.00 20.99
ATOM   1481  NZ  LYS A 189      35.885  20.437  45.591  1.00 22.95
ATOM   1482  N   ALA A 190      33.056  16.039  40.884  1.00 18.62
ATOM   1483  CA  ALA A 190      33.535  15.067  39.872  1.00 19.71
ATOM   1484  C   ALA A 190      32.420  14.717  38.862  1.00 19.64
ATOM   1485  O   ALA A 190      32.689  14.678  37.660  1.00 18.88
ATOM   1486  CB  ALA A 190      33.954  13.820  40.570  1.00 16.94
ATOM   1487  N   GLY A 191      31.202  14.521  39.422  1.00 16.97
ATOM   1488  CA  GLY A 191      29.984  14.197  38.709  1.00 18.06
ATOM   1489  C   GLY A 191      29.537  15.241  37.725  1.00 18.40
ATOM   1490  O   GLY A 191      29.368  14.940  36.515  1.00 15.97
ATOM   1491  N   LEU A 192      29.409  16.502  38.241  1.00 19.22
ATOM   1492  CA  LEU A 192      29.016  17.585  37.313  1.00 20.21
ATOM   1493  C   LEU A 192      30.080  17.875  36.236  1.00 20.74
ATOM   1494  O   LEU A 192      29.798  18.302  35.086  1.00 20.92
ATOM   1495  CB  LEU A 192      28.551  18.781  38.210  1.00 22.81
ATOM   1496  CG  LEU A 192      27.905  19.929  37.362  1.00 22.73
ATOM   1497  CD1 LEU A 192      26.677  19.397  36.587  1.00 22.91
ATOM   1498  CD2 LEU A 192      27.515  21.049  38.291  1.00 24.30
ATOM   1499  N   THR A 193      31.343  17.751  36.611  1.00 21.29
ATOM   1500  CA  THR A 193      32.469  17.989  35.683  1.00 22.73
ATOM   1501  C   THR A 193      32.364  17.037  34.485  1.00 23.30
ATOM   1502  O   THR A 193      32.483  17.439  33.377  1.00 22.21
ATOM   1503  CB  THR A 193      33.882  17.713  36.317  1.00 24.68
ATOM   1504  OG1 THR A 193      34.002  18.881  37.214  1.00 23.91
ATOM   1505  CG2 THR A 193      35.033  17.631  35.297  1.00 23.78
ATOM   1506  N   PHE A 194      32.163  15.808  34.779  1.00 22.25
ATOM   1507  CA  PHE A 194      31.954  14.732  33.813  1.00 22.42
ATOM   1508  C   PHE A 194      30.786  15.145  32.925  1.00 22.56
ATOM   1509  O   PHE A 194      30.917  14.861  31.695  1.00 21.88
ATOM   1510  CB  PHE A 194      31.707  13.338  34.398  1.00 23.49
ATOM   1511  CG  PHE A 194      31.635  12.266  33.337  1.00 25.80
ATOM   1512  CD1 PHE A 194      32.827  11.713  32.864  1.00 26.27
ATOM   1513  CD2 PHE A 194      30.350  11.921  32.828  1.00 27.23
ATOM   1514  CE1 PHE A 194      32.760  10.780  31.789  1.00 27.24
ATOM   1515  CE2 PHE A 194      30.293  10.979  31.792  1.00 26.67
ATOM   1516  CZ  PHE A 194      31.510  10.442  31.297  1.00 25.95
ATOM   1517  N   LEU A 195      29.702  15.575  33.412  1.00 20.76
ATOM   1518  CA  LEU A 195      28.586  15.967  32.585  1.00 22.60
ATOM   1519  C   LEU A 195      28.960  17.140  31.633  1.00 20.42
ATOM   1520  O   LEU A 195      28.503  17.178  30.488  1.00 21.34
ATOM   1521  CB  LEU A 195      27.386  16.367  33.515  1.00 23.97
ATOM   1522  CG  LEU A 195      26.119  16.795  32.681  1.00 27.45
ATOM   1523  CD1 LEU A 195      25.491  15.631  31.968  1.00 26.97
ATOM   1524  CD2 LEU A 195      25.180  17.545  33.634  1.00 25.98
ATOM   1525  N   VAL A 196      29.548  18.157  32.147  1.00 21.83
ATOM   1526  CA  VAL A 196      29.912  19.390  31.456  1.00 24.71
ATOM   1527  C   VAL A 196      30.907  19.006  30.345  1.00 25.11
ATOM   1528  O   VAL A 196      30.929  19.557  29.242  1.00 23.53
ATOM   1529  CB  VAL A 196      30.409  20.458  32.492  1.00 24.75
ATOM   1530  CG1 VAL A 196      30.932  21.698  31.722  1.00 23.63
ATOM   1531  CG2 VAL A 196      29.360  20.860  33.452  1.00 24.70
ATOM   1532  N   ASP A 197      31.781  18.037  30.615  1.00 25.17
ATOM   1533  CA  ASP A 197      32.770  17.598  29.661  1.00 27.74
ATOM   1534  C   ASP A 197      32.070  16.931  28.453  1.00 29.03
ATOM   1535  O   ASP A 197      32.583  17.017  27.334  1.00 25.83
ATOM   1536  CB  ASP A 197      33.779  16.716  30.284  1.00 32.08
ATOM   1537  CG  ASP A 197      35.024  17.351  30.856  1.00 38.43
ATOM   1538  OD1 ASP A 197      35.246  18.586  30.967  1.00 40.92
ATOM   1539  OD2 ASP A 197      35.808  16.442  31.331  1.00 43.30
ATOM   1540  N   LEU A 198      30.954  16.270  28.677  1.00 28.16
ATOM   1541  CA  LEU A 198      30.153  15.593  27.671  1.00 28.86
ATOM   1542  C   LEU A 198      29.652  16.639  26.676  1.00 29.29
ATOM   1543  O   LEU A 198      29.659  16.376  25.486  1.00 32.61
ATOM   1544  CB  LEU A 198      28.990  14.847  28.282  1.00 26.82
ATOM   1545  CG  LEU A 198      29.213  13.467  28.867  1.00 27.84
ATOM   1546  CD1 LEU A 198      27.845  12.946  29.346  1.00 28.48
ATOM   1547  CD2 LEU A 198      29.798  12.467  27.855  1.00 27.80
ATOM   1548  N   ILE A 199      29.230  17.720  27.240  1.00 29.17
ATOM   1549  CA  ILE A 199      28.727  18.831  26.457  1.00 30.02
ATOM   1550  C   ILE A 199      29.897  19.530  25.768  1.00 33.01
ATOM   1551  O   ILE A 199      29.855  19.744  24.550  1.00 33.16
ATOM   1552  CB  ILE A 199      27.920  19.791  27.357  1.00 29.00
ATOM   1553  CG1 ILE A 199      26.656  19.061  27.891  1.00 26.86
ATOM   1554  CG2 ILE A 199      27.606  21.079  26.561  1.00 28.03
ATOM   1555  CD1 ILE A 199      26.021  19.861  29.111  1.00 29.10
ATOM   1556  N   LYS A 200      30.876  19.915  26.508  1.00 33.49
ATOM   1557  CA  LYS A 200      32.057  20.580  25.999  1.00 37.48
ATOM   1558  C   LYS A 200      32.506  19.948  24.684  1.00 37.91
ATOM   1559  O   LYS A 200      32.868  20.683  23.724  1.00 39.27
ATOM   1560  CB  LYS A 200      33.303  20.311  26.886  1.00 41.99
ATOM   1561  CG  LYS A 200      34.113  21.505  27.353  1.00 46.64
ATOM   1562  CD  LYS A 200      33.313  22.176  28.472  1.00 51.19
ATOM   1563  CE  LYS A 200      33.962  23.218  29.357  1.00 52.17
ATOM   1564  NZ  LYS A 200      32.947  24.291  29.752  1.00 52.63
ATOM   1565  N   ASN A 201      32.614  18.643  24.753  1.00 35.61
ATOM   1566  CA  ASN A 201      33.138  17.756  23.696  1.00 34.84
ATOM   1567  C   ASN A 201      32.106  17.295  22.691  1.00 33.01
ATOM   1568  O   ASN A 201      32.260  16.264  22.003  1.00 34.31
ATOM   1569  CB  ASN A 201      33.916  16.597  24.358  1.00 35.80
ATOM   1570  CG  ASN A 201      35.257  17.049  24.941  1.00 40.07
ATOM   1571  OD1 ASN A 201      35.648  16.599  26.047  1.00 41.68
ATOM   1572  ND2 ASN A 201      36.032  17.947  24.290  1.00 42.48
ATOM   1573  N   LYS A 202      31.010  17.968  22.682  1.00 34.25
ATOM   1574  CA  LYS A 202      29.899  17.747  21.740  1.00 36.87
ATOM   1575  C   LYS A 202      29.230  16.427  21.749  1.00 36.56
ATOM   1576  O   LYS A 202      28.578  16.007  20.776  1.00 38.53
ATOM   1577  CB  LYS A 202      30.478  18.088  20.341  1.00 41.88
ATOM   1578  CG  LYS A 202      31.034  19.548  20.328  1.00 45.39
ATOM   1579  CD  LYS A 202      30.017  20.620  20.015  1.00 51.30
ATOM   1580  CE  LYS A 202      28.743  20.720  20.851  1.00 55.52
ATOM   1581  NZ  LYS A 202      27.643  21.431  20.034  1.00 59.01
ATOM   1582  N   HIS A 203      29.198  15.739  22.903  1.00 34.71
ATOM   1583  CA  HIS A 203      28.488  14.446  22.954  1.00 32.46
ATOM   1584  C   HIS A 203      27.045  14.665  23.310  1.00 32.87
ATOM   1585  O   HIS A 203      26.219  13.791  23.077  1.00 35.43
ATOM   1586  CB  HIS A 203      29.159  13.479  23.956  1.00 30.54
ATOM   1587  CG  HIS A 203      30.482  13.091  23.327  1.00 31.41
ATOM   1588  ND1 HIS A 203      31.691  13.478  23.781  1.00 32.60
ATOM   1589  CD2 HIS A 203      30.728  12.345  22.228  1.00 27.60
ATOM   1590  CE1 HIS A 203      32.669  13.003  23.005  1.00 29.94
ATOM   1591  NE2 HIS A 203      32.067  12.298  22.072  1.00 30.92
ATOM   1592  N   MET A 204      26.792  15.826  23.884  1.00 33.05
ATOM   1593  CA  MET A 204      25.506  16.242  24.401  1.00 32.72
ATOM   1594  C   MET A 204      25.269  17.687  24.248  1.00 32.20
ATOM   1595  O   MET A 204      26.313  18.397  24.242  1.00 34.16
ATOM   1596  CB  MET A 204      25.692  15.936  25.928  1.00 37.49
ATOM   1597  CG  MET A 204      24.383  15.853  26.612  1.00 40.20
ATOM   1598  SD  MET A 204      24.634  14.331  27.663  1.00 42.49
ATOM   1599  CE  MET A 204      22.920  13.813  27.680  1.00 40.99
ATOM   1600  N   ASN A 205      24.033  18.147  24.199  1.00 32.12
ATOM   1601  CA  ASN A 205      23.814  19.596  24.129  1.00 33.25
ATOM   1602  C   ASN A 205      23.101  20.073  25.387  1.00 29.24
ATOM   1603  O   ASN A 205      22.200  19.424  25.808  1.00 31.21
ATOM   1604  CB  ASN A 205      23.126  20.035  22.840  1.00 43.50
ATOM   1605  CG  ASN A 205      24.048  19.676  21.626  1.00 49.48
ATOM   1606  OD1 ASN A 205      25.218  20.138  21.505  1.00 53.34
ATOM   1607  ND2 ASN A 205      23.422  18.779  20.837  1.00 50.34
ATOM   1608  N   ALA A 206      23.534  21.206  25.816  1.00 27.45
ATOM   1609  CA  ALA A 206      23.115  21.963  26.938  1.00 25.46
ATOM   1610  C   ALA A 206      21.642  22.279  26.906  1.00 28.06
ATOM   1611  O   ALA A 206      21.030  22.550  27.999  1.00 31.20
ATOM   1612  CB  ALA A 206      23.881  23.278  26.999  1.00 27.06
ATOM   1613  N   ASP A 207      21.068  22.268  25.705  1.00 26.97
ATOM   1614  CA  ASP A 207      19.626  22.646  25.680  1.00 28.54
ATOM   1615  C   ASP A 207      18.697  21.447  25.788  1.00 26.90
ATOM   1616  O   ASP A 207      17.447  21.673  25.884  1.00 29.09
ATOM   1617  CB  ASP A 207      19.369  23.599  24.473  1.00 33.37
ATOM   1618  CG  ASP A 207      19.203  22.834  23.139  1.00 37.58
ATOM   1619  OD1 ASP A 207      20.120  22.053  22.771  1.00 39.99
ATOM   1620  OD2 ASP A 207      18.089  23.029  22.455  1.00 41.97
ATOM   1621  N   THR A 208      19.162  20.188  25.663  1.00 25.79
ATOM   1622  CA  THR A 208      18.184  19.095  25.701  1.00 24.04
ATOM   1623  C   THR A 208      17.213  19.164  26.881  1.00 25.38
ATOM   1624  O   THR A 208      17.700  19.349  28.033  1.00 24.32
ATOM   1625  CB  THR A 208      18.960  17.760  25.629  1.00 24.81
ATOM   1626  OG1 THR A 208      19.907  18.035  24.545  1.00 28.11
ATOM   1627  CG2 THR A 208      17.991  16.609  25.458  1.00 22.67
ATOM   1628  N   ASP A 209      15.938  19.076  26.460  1.00 24.12
ATOM   1629  CA  ASP A 209      14.887  19.039  27.458  1.00 23.13
ATOM   1630  C   ASP A 209      14.147  17.679  27.353  1.00 22.24
ATOM   1631  O   ASP A 209      14.492  16.767  26.569  1.00 22.67
ATOM   1632  CB  ASP A 209      14.049  20.283  27.421  1.00 23.94
ATOM   1633  CG  ASP A 209      13.138  20.443  26.221  1.00 27.38
ATOM   1634  OD1 ASP A 209      13.159  19.507  25.436  1.00 28.04
ATOM   1635  OD2 ASP A 209      12.397  21.438  26.018  1.00 31.42
ATOM   1636  N   TYR A 210      13.043  17.572  28.052  1.00 22.22
ATOM   1637  CA  TYR A 210      12.192  16.374  28.101  1.00 23.62
ATOM   1638  C   TYR A 210      11.657  15.957  26.728  1.00 23.94
ATOM   1639  O   TYR A 210      11.837  14.814  26.290  1.00 25.04
ATOM   1640  CB  TYR A 210      11.009  16.413  29.107  1.00 20.91
ATOM   1641  CG  TYR A 210      10.425  15.015  29.346  1.00 23.15
ATOM   1642  CD1 TYR A 210       9.439  14.483  28.492  1.00 20.22
ATOM   1643  CD2 TYR A 210      10.792  14.261  30.519  1.00 20.57
ATOM   1644  CE1 TYR A 210       8.850  13.297  28.773  1.00 22.17
ATOM   1645  CE2 TYR A 210      10.169  13.047  30.804  1.00 21.11
ATOM   1646  CZ  TYR A 210       9.208  12.569  29.953  1.00 23.40
ATOM   1647  OH  TYR A 210       8.644  11.365  30.145  1.00 24.29
ATOM   1648  N   SER A 211      11.063  16.873  26.053  1.00 24.99
ATOM   1649  CA  SER A 211      10.557  16.662  24.680  1.00 26.76
ATOM   1650  C   SER A 211      11.642  16.354  23.699  1.00 26.16
ATOM   1651  O   SER A 211      11.502  15.370  22.928  1.00 30.42
ATOM   1652  CB  SER A 211       9.894  17.971  24.168  1.00 27.38
ATOM   1653  OG  SER A 211       8.592  17.811  24.686  1.00 36.62
ATOM   1654  N   ILE A 212      12.708  17.115  23.585  1.00 27.99
ATOM   1655  CA  ILE A 212      13.786  16.864  22.619  1.00 25.10
ATOM   1656  C   ILE A 212      14.321  15.462  22.827  1.00 26.40
ATOM   1657  O   ILE A 212      14.517  14.703  21.848  1.00 24.51
ATOM   1658  CB  ILE A 212      14.983  17.862  22.836  1.00 25.59
ATOM   1659  CG1 ILE A 212      14.684  19.376  22.618  1.00 29.88
ATOM   1660  CG2 ILE A 212      16.201  17.352  22.035  1.00 27.13
ATOM   1661  CD1 ILE A 212      13.403  19.407  21.786  1.00 33.25
ATOM   1662  N   ALA A 213      14.582  15.107  24.182  1.00 26.23
ATOM   1663  CA  ALA A 213      15.132  13.735  24.501  1.00 23.83
ATOM   1664  C   ALA A 213      14.174  12.643  24.142  1.00 23.00
ATOM   1665  O   ALA A 213      14.480  11.597  23.484  1.00 23.58
ATOM   1666  CB  ALA A 213      15.503  13.617  25.972  1.00 22.66
ATOM   1667  N   GLU A 214      12.929  12.899  24.527  1.00 22.85
ATOM   1668  CA  GLU A 214      11.895  11.901  24.171  1.00 23.45
ATOM   1669  C   GLU A 214      11.758  11.742  22.672  1.00 25.44
ATOM   1670  O   GLU A 214      11.858  10.553  22.263  1.00 25.00
ATOM   1671  CB  GLU A 214      10.545  12.232  24.790  1.00 26.21
ATOM   1672  CG  GLU A 214       9.475  11.084  24.721  1.00 26.88
ATOM   1673  CD  GLU A 214       8.185  11.453  25.324  1.00 25.98
ATOM   1674  OE1 GLU A 214       7.812  12.582  25.360  1.00 28.16
ATOM   1675  OE2 GLU A 214       7.653  10.534  25.945  1.00 27.05
ATOM   1676  N   ALA A 215      11.588  12.760  21.865  1.00 25.50
ATOM   1677  CA  ALA A 215      11.457  12.611  20.406  1.00 27.59
ATOM   1678  C   ALA A 215      12.666  11.950  19.791  1.00 27.85
ATOM   1679  O   ALA A 215      12.485  11.049  18.884  1.00 29.34
ATOM   1680  CB  ALA A 215      11.261  13.983  19.725  1.00 28.31
ATOM   1681  N   ALA A 216      13.830  12.337  20.316  1.00 28.03
ATOM   1682  CA  ALA A 216      15.065  11.739  19.797  1.00 27.69
ATOM   1683  C   ALA A 216      15.028  10.254  19.960  1.00 28.51
ATOM   1684  O   ALA A 216      15.271   9.517  18.991  1.00 29.54
ATOM   1685  CB  ALA A 216      16.364  12.290  20.430  1.00 26.91
ATOM   1686  N   PHE A 217      14.760   9.723  21.195  1.00 23.57
ATOM   1687  CA  PHE A 217      14.869   8.241  21.303  1.00 22.55
ATOM   1688  C   PHE A 217      13.774   7.519  20.563  1.00 23.16
ATOM   1689  O   PHE A 217      13.983   6.405  20.051  1.00 24.95
ATOM   1690  CB  PHE A 217      14.903   7.941  22.814  1.00 21.93
ATOM   1691  CG  PHE A 217      15.003   6.486  23.093  1.00 18.47
ATOM   1692  CD1 PHE A 217      13.877   5.687  23.137  1.00 21.23
ATOM   1693  CD2 PHE A 217      16.236   5.944  23.302  1.00 18.03
ATOM   1694  CE1 PHE A 217      13.970   4.322  23.416  1.00 22.62
ATOM   1695  CE2 PHE A 217      16.360   4.623  23.578  1.00 20.24
ATOM   1696  CZ  PHE A 217      15.237   3.779  23.668  1.00 18.05
ATOM   1697  N   ASN A 218      12.580   8.071  20.592  1.00 23.23
ATOM   1698  CA  ASN A 218      11.372   7.503  20.023  1.00 26.21
ATOM   1699  C   ASN A 218      11.478   7.458  18.452  1.00 29.15
ATOM   1700  O   ASN A 218      10.909   6.530  17.866  1.00 27.83
ATOM   1701  CB  ASN A 218      10.097   8.180  20.497  1.00 24.62
ATOM   1702  CG  ASN A 218       9.739   7.703  21.927  1.00 25.68
ATOM   1703  OD1 ASN A 218       8.679   8.008  22.461  1.00 27.23
ATOM   1704  ND2 ASN A 218      10.683   7.028  22.601  1.00 24.93
ATOM   1705  N   LYS A 219      12.268   8.374  17.884  1.00 30.33
ATOM   1706  CA  LYS A 219      12.450   8.360  16.400  1.00 32.01
ATOM   1707  C   LYS A 219      13.635   7.572  15.931  1.00 32.49
ATOM   1708  O   LYS A 219      13.913   7.548  14.675  1.00 35.24
ATOM   1709  CB  LYS A 219      12.640   9.795  15.851  1.00 35.74
ATOM   1710  CG  LYS A 219      11.371  10.605  16.311  1.00 42.88
ATOM   1711  CD  LYS A 219      11.638  12.099  16.269  1.00 50.01
ATOM   1712  CE  LYS A 219      12.563  12.511  15.118  1.00 53.18
ATOM   1713  NZ  LYS A 219      13.347  13.716  15.638  1.00 59.32
ATOM   1714  N   GLY A 220      14.359   7.000  16.843  1.00 28.38
ATOM   1715  CA  GLY A 220      15.536   6.196  16.576  1.00 27.11
ATOM   1716  C   GLY A 220      16.789   6.956  16.410  1.00 26.76
ATOM   1717  O   GLY A 220      17.845   6.338  15.945  1.00 29.32
ATOM   1718  N   GLU A 221      16.797   8.226  16.773  1.00 28.48
ATOM   1719  CA  GLU A 221      18.104   8.951  16.563  1.00 29.37
ATOM   1720  C   GLU A 221      19.132   8.827  17.636  1.00 29.96
ATOM   1721  O   GLU A 221      20.330   9.095  17.315  1.00 30.49
ATOM   1722  CB  GLU A 221      17.750  10.405  16.332  1.00 34.70
ATOM   1723  CG  GLU A 221      16.455  10.570  15.443  1.00 40.91
ATOM   1724  CD  GLU A 221      16.248  12.062  15.240  1.00 46.03
ATOM   1725  OE1 GLU A 221      16.766  12.919  15.964  1.00 48.55
ATOM   1726  OE2 GLU A 221      15.529  12.264  14.211  1.00 53.44
ATOM   1727  N   THR A 222      18.741   8.496  18.890  1.00 26.81
ATOM   1728  CA  THR A 222      19.747   8.375  19.941  1.00 24.33
ATOM   1729  C   THR A 222      19.671   6.948  20.419  1.00 23.39
ATOM   1730  O   THR A 222      18.573   6.410  20.422  1.00 21.99
ATOM   1731  CB  THR A 222      19.494   9.444  21.057  1.00 26.01
ATOM   1732  OG1 THR A 222      20.759   9.419  21.820  1.00 27.75
ATOM   1733  CG2 THR A 222      18.273   9.141  21.923  1.00 25.07
ATOM   1734  N   ALA A 223      20.807   6.331  20.836  1.00 22.81
ATOM   1735  CA  ALA A 223      20.704   4.946  21.276  1.00 21.91
ATOM   1736  C   ALA A 223      20.210   4.799  22.740  1.00 22.26
ATOM   1737  O   ALA A 223      19.747   3.668  22.992  1.00 21.98
ATOM   1738  CB  ALA A 223      22.061   4.236  21.141  1.00 23.51
ATOM   1739  N   MET A 224      20.262   5.798  23.597  1.00 22.50
ATOM   1740  CA  MET A 224      19.839   5.626  25.051  1.00 19.70
ATOM   1741  C   MET A 224      19.245   6.906  25.542  1.00 19.08
ATOM   1742  O   MET A 224      19.479   8.000  25.057  1.00 17.71
ATOM   1743  CB  MET A 224      21.160   5.405  25.845  1.00 19.25
ATOM   1744  CG  MET A 224      21.816   4.118  25.666  1.00 21.55
ATOM   1745  SD  MET A 224      23.356   4.003  26.581  1.00 27.08
ATOM   1746  CE  MET A 224      24.477   5.155  25.828  1.00 25.34
ATOM   1747  N   THR A 225      18.427   6.751  26.602  1.00 19.19
ATOM   1748  CA  THR A 225      17.826   7.969  27.267  1.00 17.61
ATOM   1749  C   THR A 225      17.701   7.557  28.747  1.00 19.51
ATOM   1750  O   THR A 225      17.925   6.345  29.095  1.00 18.99
ATOM   1751  CB  THR A 225      16.507   8.438  26.597  1.00 13.98
ATOM   1752  OG1 THR A 225      16.119   9.697  27.154  1.00 21.69
ATOM   1753  CG2 THR A 225      15.375   7.356  26.691  1.00 17.53
ATOM   1754  N   ILE A 226      17.453   8.460  29.635  1.00 18.10
ATOM   1755  CA  ILE A 226      17.275   8.098  31.065  1.00 15.93
ATOM   1756  C   ILE A 226      15.896   8.592  31.358  1.00 15.68
ATOM   1757  O   ILE A 226      15.651   9.779  31.030  1.00 17.30
ATOM   1758  CB  ILE A 226      18.355   8.783  31.904  1.00 16.97
ATOM   1759  CG1 ILE A 226      19.762   8.038  31.620  1.00 16.31
ATOM   1760  CG2 ILE A 226      17.951   8.769  33.387  1.00 18.79
ATOM   1761  CD1 ILE A 226      20.871   9.057  32.213  1.00 18.28
ATOM   1762  N   ASN A 227      14.976   7.811  31.841  1.00 15.21
ATOM   1763  CA  ASN A 227      13.636   8.274  32.174  1.00 15.29
ATOM   1764  C   ASN A 227      12.964   7.273  33.210  1.00 16.75
ATOM   1765  O   ASN A 227      13.586   6.241  33.548  1.00 17.04
ATOM   1766  CB  ASN A 227      12.813   8.442  30.891  1.00 19.15
ATOM   1767  CG  ASN A 227      11.891   9.636  30.922  1.00 20.59
ATOM   1768  OD1 ASN A 227      11.240  10.061  31.945  1.00 25.03
ATOM   1769  ND2 ASN A 227      11.622  10.280  29.798  1.00 21.39
ATOM   1770  N   GLY A 228      11.781   7.660  33.692  1.00 16.86
ATOM   1771  CA  GLY A 228      11.007   6.887  34.639  1.00 16.25
ATOM   1772  C   GLY A 228       9.944   6.086  33.921  1.00 19.00
ATOM   1773  O   GLY A 228       9.735   6.143  32.663  1.00 19.13
ATOM   1774  N   PRO A 229       9.217   5.241  34.698  1.00 19.24
ATOM   1775  CA  PRO A 229       8.236   4.320  34.188  1.00 17.81
ATOM   1776  C   PRO A 229       7.187   4.927  33.306  1.00 18.56
ATOM   1777  O   PRO A 229       6.679   4.230  32.384  1.00 17.71
ATOM   1778  CB  PRO A 229       7.664   3.576  35.420  1.00 17.05
ATOM   1779  CG  PRO A 229       8.576   3.886  36.515  1.00 19.44
ATOM   1780  CD  PRO A 229       9.450   5.068  36.164  1.00 18.37
ATOM   1781  N   TRP A 230       6.712   6.176  33.592  1.00 17.59
ATOM   1782  CA  TRP A 230       5.734   6.924  32.919  1.00 16.85
ATOM   1783  C   TRP A 230       6.125   7.127  31.419  1.00 17.44
ATOM   1784  O   TRP A 230       5.195   7.207  30.608  1.00 19.47
ATOM   1785  CB  TRP A 230       5.448   8.289  33.641  1.00 16.91
ATOM   1786  CG  TRP A 230       6.722   9.099  33.695  1.00 19.47
ATOM   1787  CD1 TRP A 230       7.315   9.800  32.695  1.00 19.47
ATOM   1788  CD2 TRP A 230       7.657   9.193  34.820  1.00 20.47
ATOM   1789  NE1 TRP A 230       8.517  10.366  33.132  1.00 19.66
ATOM   1790  CE2 TRP A 230       8.754   9.942  34.435  1.00 20.33
ATOM   1791  CE3 TRP A 230       7.606   8.669  36.114  1.00 21.16
ATOM   1792  CZ2 TRP A 230       9.767  10.285  35.265  1.00 19.60
ATOM   1793  CZ3 TRP A 230       8.710   8.936  36.918  1.00 18.79
ATOM   1794  CH2 TRP A 230       9.764   9.710  36.511  1.00 22.05
ATOM   1795  N   ALA A 231       7.345   7.152  30.995  1.00 19.60
ATOM   1796  CA  ALA A 231       7.736   7.302  29.569  1.00 18.83
ATOM   1797  C   ALA A 231       7.559   6.024  28.762  1.00 18.79
ATOM   1798  O   ALA A 231       7.526   6.031  27.481  1.00 19.11
ATOM   1799  CB  ALA A 231       9.236   7.533  29.685  1.00 17.18
ATOM   1800  N   TRP A 232       7.379   4.839  29.339  1.00 18.62
ATOM   1801  CA  TRP A 232       7.403   3.562  28.628  1.00 21.07
ATOM   1802  C   TRP A 232       6.290   3.520  27.578  1.00 23.97
ATOM   1803  O   TRP A 232       6.453   2.846  26.547  1.00 21.87
ATOM   1804  CB  TRP A 232       7.365   2.280  29.496  1.00 19.90
ATOM   1805  CG  TRP A 232       8.497   2.191  30.506  1.00 18.81
ATOM   1806  CD1 TRP A 232       9.737   2.784  30.520  1.00 18.39
ATOM   1807  CD2 TRP A 232       8.439   1.419  31.740  1.00 17.55
ATOM   1808  NE1 TRP A 232      10.436   2.444  31.640  1.00 16.62
ATOM   1809  CE2 TRP A 232       9.631   1.582  32.382  1.00 15.06
ATOM   1810  CE3 TRP A 232       7.393   0.611  32.250  1.00 18.32
ATOM   1811  CZ2 TRP A 232       9.928   0.955  33.637  1.00 20.58
ATOM   1812  CZ3 TRP A 232       7.649   0.008  33.482  1.00 18.91
ATOM   1813  CH2 TRP A 232       8.864   0.129  34.122  1.00 17.77
ATOM   1814  N   SER A 233       5.169   4.099  27.961  1.00 24.57
ATOM   1815  CA  SER A 233       3.982   4.097  27.045  1.00 28.37
ATOM   1816  C   SER A 233       4.225   4.642  25.657  1.00 27.00
ATOM   1817  O   SER A 233       3.783   3.982  24.697  1.00 28.52
ATOM   1818  CB  SER A 233       2.800   4.945  27.646  1.00 28.20
ATOM   1819  OG  SER A 233       2.281   3.856  28.405  1.00 35.62
ATOM   1820  N   ASN A 234       4.864   5.778  25.596  1.00 25.65
ATOM   1821  CA  ASN A 234       5.124   6.389  24.262  1.00 27.45
ATOM   1822  C   ASN A 234       6.170   5.578  23.435  1.00 25.88
ATOM   1823  O   ASN A 234       6.134   5.672  22.197  1.00 26.65
ATOM   1824  CB  ASN A 234       5.560   7.830  24.376  1.00 27.20
ATOM   1825  CG  ASN A 234       4.515   8.800  24.825  1.00 32.73
ATOM   1826  OD1 ASN A 234       3.313   8.548  24.569  1.00 34.93
ATOM   1827  ND2 ASN A 234       4.849   9.872  25.578  1.00 34.92
ATOM   1828  N   ILE A 235       7.114   5.014  24.183  1.00 25.01
ATOM   1829  CA  ILE A 235       8.115   4.183  23.586  1.00 23.56
ATOM   1830  C   ILE A 235       7.370   3.000  22.931  1.00 25.58
ATOM   1831  O   ILE A 235       7.666   2.590  21.770  1.00 26.71
ATOM   1832  CB  ILE A 235       9.203   3.650  24.561  1.00 19.34
ATOM   1833  CG1 ILE A 235       9.903   4.834  25.272  1.00 18.44
ATOM   1834  CG2 ILE A 235      10.227   2.842  23.723  1.00 22.65
ATOM   1835  CD1 ILE A 235      10.920   4.384  26.351  1.00 19.01
ATOM   1836  N   ASP A 236       6.432   2.424  23.663  1.00 25.62
ATOM   1837  CA  ASP A 236       5.804   1.190  23.133  1.00 28.44
ATOM   1838  C   ASP A 236       5.118   1.466  21.765  1.00 32.41
ATOM   1839  O   ASP A 236       5.125   0.567  20.923  1.00 31.56
ATOM   1840  CB  ASP A 236       4.757   0.546  23.983  1.00 26.70
ATOM   1841  CG  ASP A 236       5.359  -0.147  25.240  1.00 28.31
ATOM   1842  OD1 ASP A 236       6.526  -0.472  25.341  1.00 25.76
ATOM   1843  OD2 ASP A 236       4.469  -0.256  26.130  1.00 30.38
ATOM   1844  N   THR A 237       4.511   2.638  21.851  1.00 33.40
ATOM   1845  CA  THR A 237       3.729   3.212  20.797  1.00 34.18
ATOM   1846  C   THR A 237       4.572   3.527  19.540  1.00 34.60
ATOM   1847  O   THR A 237       3.966   3.522  18.437  1.00 34.43
ATOM   1848  CB  THR A 237       2.950   4.540  21.105  1.00 33.57
ATOM   1849  OG1 THR A 237       1.917   4.214  22.004  1.00 35.33
ATOM   1850  CG2 THR A 237       2.218   4.888  19.792  1.00 39.52
ATOM   1851  N   SER A 238       5.808   3.839  19.781  1.00 33.33
ATOM   1852  CA  SER A 238       6.705   4.126  18.641  1.00 34.83
ATOM   1853  C   SER A 238       7.301   2.795  18.137  1.00 35.05
ATOM   1854  O   SER A 238       8.054   2.728  17.178  1.00 31.67
ATOM   1855  CB  SER A 238       7.763   5.118  19.204  1.00 35.96
ATOM   1856  OG  SER A 238       8.945   4.225  19.502  1.00 36.71
ATOM   1857  N   LYS A 239       7.038   1.688  18.865  1.00 37.42
ATOM   1858  CA  LYS A 239       7.578   0.364  18.581  1.00 42.05
ATOM   1859  C   LYS A 239       9.099   0.345  18.606  1.00 41.41
ATOM   1860  O   LYS A 239       9.633  -0.615  17.967  1.00 40.74
ATOM   1861  CB  LYS A 239       7.140  -0.328  17.252  1.00 43.06
ATOM   1862  CG  LYS A 239       7.870  -1.647  16.984  1.00 49.69
ATOM   1863  CD  LYS A 239       9.199  -1.966  16.362  1.00 50.19
ATOM   1864  CE  LYS A 239      10.514  -2.223  17.004  1.00 49.43
ATOM   1865  NZ  LYS A 239      11.091  -3.522  17.406  1.00 46.73
ATOM   1866  N   VAL A 240       9.862   1.286  19.207  1.00 40.43
ATOM   1867  CA  VAL A 240      11.363   1.074  19.164  1.00 36.57
ATOM   1868  C   VAL A 240      11.579  -0.273  19.838  1.00 35.68
ATOM   1869  O   VAL A 240      10.662  -0.682  20.650  1.00 37.66
ATOM   1870  CB  VAL A 240      12.054   2.246  19.895  1.00 34.25
ATOM   1871  CG1 VAL A 240      13.309   1.759  20.671  1.00 28.26
ATOM   1872  CG2 VAL A 240      12.285   3.439  18.995  1.00 31.90
ATOM   1873  N   ASN A 241      12.656  -0.992  19.610  1.00 35.28
ATOM   1874  CA  ASN A 241      13.007  -2.255  20.317  1.00 32.94
ATOM   1875  C   ASN A 241      13.969  -1.847  21.492  1.00 29.39
ATOM   1876  O   ASN A 241      15.157  -1.821  21.450  1.00 28.65
ATOM   1877  CB  ASN A 241      13.602  -3.255  19.386  1.00 33.85
ATOM   1878  CG  ASN A 241      13.964  -4.582  20.044  1.00 39.23
ATOM   1879  OD1 ASN A 241      13.334  -5.159  20.978  1.00 36.88
ATOM   1880  ND2 ASN A 241      15.073  -5.173  19.489  1.00 41.90
ATOM   1881  N   TYR A 242      13.353  -1.585  22.649  1.00 29.99
ATOM   1882  CA  TYR A 242      14.068  -1.075  23.831  1.00 25.45
ATOM   1883  C   TYR A 242      14.222  -1.987  25.011  1.00 26.26
ATOM   1884  O   TYR A 242      13.368  -2.874  25.265  1.00 27.76
ATOM   1885  CB  TYR A 242      13.302   0.210  24.323  1.00 24.55
ATOM   1886  CG  TYR A 242      12.015   0.045  25.060  1.00 25.49
ATOM   1887  CD1 TYR A 242      10.808  -0.155  24.328  1.00 25.96
ATOM   1888  CD2 TYR A 242      11.889   0.115  26.483  1.00 22.24
ATOM   1889  CE1 TYR A 242       9.560  -0.279  24.992  1.00 27.59
ATOM   1890  CE2 TYR A 242      10.700  -0.001  27.134  1.00 22.93
ATOM   1891  CZ  TYR A 242       9.510  -0.178  26.404  1.00 24.82
ATOM   1892  OH  TYR A 242       8.249  -0.306  26.967  1.00 25.64
ATOM   1893  N   GLY A 243      15.306  -1.723  25.788  1.00 22.77
ATOM   1894  CA  GLY A 243      15.435  -2.522  27.027  1.00 20.02
ATOM   1895  C   GLY A 243      15.438  -1.406  28.118  1.00 20.94
ATOM   1896  O   GLY A 243      15.609  -0.212  27.820  1.00 19.26
ATOM   1897  N   VAL A 244      15.257  -1.872  29.344  1.00 21.00
ATOM   1898  CA  VAL A 244      15.265  -0.945  30.529  1.00 21.23
ATOM   1899  C   VAL A 244      16.321  -1.547  31.443  1.00 22.15
ATOM   1900  O   VAL A 244      16.118  -2.749  31.763  1.00 23.13
ATOM   1901  CB  VAL A 244      13.865  -0.754  31.172  1.00 17.16
ATOM   1902  CG1 VAL A 244      14.074   0.039  32.487  1.00 17.47
ATOM   1903  CG2 VAL A 244      12.818  -0.154  30.312  1.00 16.45
ATOM   1904  N   THR A 245      17.372  -0.834  31.864  1.00 19.82
ATOM   1905  CA  THR A 245      18.281  -1.551  32.783  1.00 21.22
ATOM   1906  C   THR A 245      18.868  -0.660  33.876  1.00 20.99
ATOM   1907  O   THR A 245      18.514   0.520  34.014  1.00 19.84
ATOM   1908  CB  THR A 245      19.372  -2.181  31.812  1.00 24.12
ATOM   1909  OG1 THR A 245      20.338  -3.041  32.488  1.00 26.10
ATOM   1910  CG2 THR A 245      20.087  -1.059  30.997  1.00 25.89
ATOM   1911  N   VAL A 246      19.840  -1.180  34.614  1.00 19.99
ATOM   1912  CA  VAL A 246      20.504  -0.379  35.632  1.00 23.38
ATOM   1913  C   VAL A 246      21.231   0.821  35.002  1.00 23.21
ATOM   1914  O   VAL A 246      21.884   0.624  33.975  1.00 23.62
ATOM   1915  CB  VAL A 246      21.613  -1.178  36.409  1.00 27.54
ATOM   1916  CG1 VAL A 246      22.003  -0.676  37.842  1.00 25.50
ATOM   1917  CG2 VAL A 246      21.055  -2.562  36.470  1.00 34.17
ATOM   1918  N   LEU A 247      21.298   1.941  35.653  1.00 21.06
ATOM   1919  CA  LEU A 247      22.122   3.062  35.218  1.00 20.17
ATOM   1920  C   LEU A 247      23.606   2.700  35.257  1.00 21.20
ATOM   1921  O   LEU A 247      24.156   1.851  36.033  1.00 22.52
ATOM   1922  CB  LEU A 247      21.778   4.220  36.197  1.00 18.74
ATOM   1923  CG  LEU A 247      20.331   4.741  36.069  1.00 18.60
ATOM   1924  CD1 LEU A 247      20.063   5.655  37.318  1.00 18.93
ATOM   1925  CD2 LEU A 247      20.173   5.533  34.790  1.00 18.94
ATOM   1926  N   PRO A 248      24.418   3.348  34.393  1.00 21.31
ATOM   1927  CA  PRO A 248      25.872   3.063  34.428  1.00 22.85
ATOM   1928  C   PRO A 248      26.540   3.588  35.725  1.00 23.34
ATOM   1929  O   PRO A 248      25.998   4.524  36.453  1.00 22.85
ATOM   1930  CB  PRO A 248      26.407   3.729  33.155  1.00 20.22
ATOM   1931  CG  PRO A 248      25.328   4.585  32.689  1.00 20.59
ATOM   1932  CD  PRO A 248      24.051   4.378  33.459  1.00 21.09
ATOM   1933  N   THR A 249      27.701   3.032  36.019  1.00 22.52
ATOM   1934  CA  THR A 249      28.516   3.403  37.153  1.00 19.87
ATOM   1935  C   THR A 249      29.391   4.560  36.746  1.00 21.30
ATOM   1936  O   THR A 249      29.750   4.854  35.596  1.00 21.30
ATOM   1937  CB  THR A 249      29.429   2.224  37.692  1.00 21.47
ATOM   1938  OG1 THR A 249      30.453   1.932  36.622  1.00 25.49
ATOM   1939  CG2 THR A 249      28.677   1.020  38.212  1.00 19.39
ATOM   1940  N   PHE A 250      29.857   5.256  37.780  1.00 19.36
ATOM   1941  CA  PHE A 250      30.726   6.367  37.541  1.00 21.37
ATOM   1942  C   PHE A 250      31.854   6.106  38.569  1.00 23.36
ATOM   1943  O   PHE A 250      31.484   6.076  39.767  1.00 22.78
ATOM   1944  CB  PHE A 250      30.011   7.717  37.768  1.00 20.48
ATOM   1945  CG  PHE A 250      30.888   8.925  37.652  1.00 18.81
ATOM   1946  CD1 PHE A 250      31.561   9.180  36.456  1.00 18.62
ATOM   1947  CD2 PHE A 250      31.072   9.815  38.701  1.00 18.64
ATOM   1948  CE1 PHE A 250      32.433  10.286  36.415  1.00 19.05
ATOM   1949  CE2 PHE A 250      31.892  10.929  38.665  1.00 18.50
ATOM   1950  CZ  PHE A 250      32.602  11.166  37.464  1.00 17.78
ATOM   1951  N   LYS A 251      33.080   6.005  38.174  1.00 23.69
ATOM   1952  CA  LYS A 251      34.241   5.881  39.108  1.00 25.44
ATOM   1953  C   LYS A 251      34.035   4.583  39.851  1.00 24.99
ATOM   1954  O   LYS A 251      34.381   4.474  41.046  1.00 27.25
ATOM   1955  CB  LYS A 251      34.442   7.078  40.078  1.00 29.26
ATOM   1956  CG  LYS A 251      34.977   8.357  39.374  1.00 31.89
ATOM   1957  CD  LYS A 251      35.517   9.482  40.150  1.00 34.06
ATOM   1958  CE  LYS A 251      36.510  10.481  39.758  1.00 37.64
ATOM   1959  NZ  LYS A 251      36.647  10.955  38.354  1.00 37.78
ATOM   1960  N   GLY A 252      33.350   3.689  39.179  1.00 22.07
ATOM   1961  CA  GLY A 252      33.122   2.355  39.770  1.00 22.28
ATOM   1962  C   GLY A 252      31.967   2.314  40.749  1.00 25.31
ATOM   1963  O   GLY A 252      31.670   1.166  41.309  1.00 27.62
ATOM   1964  N   GLN A 253      31.288   3.444  41.032  1.00 21.35
ATOM   1965  CA  GLN A 253      30.180   3.388  41.997  1.00 20.46
ATOM   1966  C   GLN A 253      28.895   3.450  41.189  1.00 21.04
ATOM   1967  O   GLN A 253      28.839   4.046  40.056  1.00 19.95
ATOM   1968  CB  GLN A 253      30.185   4.632  42.914  1.00 21.38
ATOM   1969  CG  GLN A 253      31.516   5.372  43.039  1.00 28.07
ATOM   1970  CD  GLN A 253      31.934   5.006  44.427  1.00 33.68
ATOM   1971  OE1 GLN A 253      31.690   3.811  44.691  1.00 37.58
ATOM   1972  NE2 GLN A 253      32.301   5.934  45.302  1.00 40.06
ATOM   1973  N   PRO A 254      27.820   2.894  41.741  1.00 20.25
ATOM   1974  CA  PRO A 254      26.553   2.943  41.095  1.00 19.81
ATOM   1975  C   PRO A 254      26.064   4.382  40.945  1.00 19.71
ATOM   1976  O   PRO A 254      26.356   5.208  41.900  1.00 20.39
ATOM   1977  CB  PRO A 254      25.567   2.132  42.003  1.00 19.11
ATOM   1978  CG  PRO A 254      26.426   1.528  43.039  1.00 21.38
ATOM   1979  CD  PRO A 254      27.847   2.138  43.026  1.00 19.37
ATOM   1980  N   SER A 255      25.363   4.719  39.887  1.00 18.71
ATOM   1981  CA  SER A 255      24.591   5.984  39.748  1.00 18.55
ATOM   1982  C   SER A 255      23.502   5.835  40.862  1.00 20.09
ATOM   1983  O   SER A 255      23.006   4.688  41.192  1.00 18.06
ATOM   1984  CB  SER A 255      23.859   6.161  38.391  1.00 17.14
ATOM   1985  OG  SER A 255      24.976   6.478  37.502  1.00 19.50
ATOM   1986  N   LYS A 256      23.154   6.899  41.532  1.00 19.40
ATOM   1987  CA  LYS A 256      22.191   6.790  42.697  1.00 20.71
ATOM   1988  C   LYS A 256      21.040   7.709  42.505  1.00 18.36
ATOM   1989  O   LYS A 256      21.163   8.904  42.911  1.00 17.16
ATOM   1990  CB  LYS A 256      22.896   7.379  43.920  1.00 23.96
ATOM   1991  CG  LYS A 256      23.676   6.616  44.926  1.00 32.07
ATOM   1992  CD  LYS A 256      24.965   6.107  44.226  1.00 36.18
ATOM   1993  CE  LYS A 256      25.924   5.277  45.080  1.00 36.75
ATOM   1994  NZ  LYS A 256      27.328   5.509  44.700  1.00 31.97
ATOM   1995  N   PRO A 257      19.961   7.231  41.903  1.00 19.72
ATOM   1996  CA  PRO A 257      18.802   8.109  41.671  1.00 20.42
ATOM   1997  C   PRO A 257      18.139   8.484  43.020  1.00 19.31
ATOM   1998  O   PRO A 257      18.198   7.711  43.932  1.00 15.36
ATOM   1999  CB  PRO A 257      17.854   7.276  40.802  1.00 20.91
ATOM   2000  CG  PRO A 257      18.276   5.795  40.928  1.00 18.43
ATOM   2001  CD  PRO A 257      19.712   5.880  41.401  1.00 18.52
ATOM   2002  N   PHE A 258      17.527   9.629  43.097  1.00 17.43
ATOM   2003  CA  PHE A 258      16.724  10.012  44.224  1.00 17.73
ATOM   2004  C   PHE A 258      15.451   9.202  43.982  1.00 20.84
ATOM   2005  O   PHE A 258      14.926   9.202  42.799  1.00 24.35
ATOM   2006  CB  PHE A 258      16.450  11.532  44.284  1.00 17.12
ATOM   2007  CG  PHE A 258      17.117  12.246  45.393  1.00 19.14
ATOM   2008  CD1 PHE A 258      17.260  11.589  46.659  1.00 22.37
ATOM   2009  CD2 PHE A 258      17.615  13.557  45.175  1.00 22.12
ATOM   2010  CE1 PHE A 258      17.794  12.241  47.761  1.00 24.66
ATOM   2011  CE2 PHE A 258      18.224  14.198  46.285  1.00 25.08
ATOM   2012  CZ  PHE A 258      18.255  13.567  47.582  1.00 26.99
ATOM   2013  N   VAL A 259      14.890   8.515  44.931  1.00 15.41
ATOM   2014  CA  VAL A 259      13.641   7.775  44.694  1.00 15.38
ATOM   2015  C   VAL A 259      12.464   8.530  45.220  1.00 17.28
ATOM   2016  O   VAL A 259      12.382   9.099  46.371  1.00 18.07
ATOM   2017  CB  VAL A 259      13.868   6.353  45.321  1.00 18.40
ATOM   2018  CG1 VAL A 259      12.631   5.501  45.282  1.00 16.65
ATOM   2019  CG2 VAL A 259      15.135   5.681  44.693  1.00 18.04
ATOM   2020  N   GLY A 260      11.379   8.588  44.417  1.00 17.42
ATOM   2021  CA  GLY A 260      10.154   9.295  44.722  1.00 15.41
ATOM   2022  C   GLY A 260       9.065   8.249  44.890  1.00 16.34
ATOM   2023  O   GLY A 260       8.972   7.222  44.230  1.00 16.77
ATOM   2024  N   VAL A 261       8.198   8.527  45.849  1.00 16.08
ATOM   2025  CA  VAL A 261       7.011   7.768  46.207  1.00 16.15
ATOM   2026  C   VAL A 261       5.894   8.647  45.709  1.00 16.66
ATOM   2027  O   VAL A 261       5.670   9.701  46.432  1.00 18.50
ATOM   2028  CB  VAL A 261       6.853   7.383  47.753  1.00 17.05
ATOM   2029  CG1 VAL A 261       5.522   6.727  47.972  1.00 17.45
ATOM   2030  CG2 VAL A 261       7.967   6.538  48.302  1.00 18.27
ATOM   2031  N   LEU A 262       5.222   8.357  44.563  1.00 16.02
ATOM   2032  CA  LEU A 262       4.088   9.038  44.032  1.00 17.63
ATOM   2033  C   LEU A 262       3.027   8.972  45.233  1.00 16.69
ATOM   2034  O   LEU A 262       2.792   7.826  45.656  1.00 18.15
ATOM   2035  CB  LEU A 262       3.482   8.532  42.743  1.00 16.65
ATOM   2036  CG  LEU A 262       2.251   9.132  42.152  1.00 17.06
ATOM   2037  CD1 LEU A 262       2.438  10.613  41.715  1.00 16.98
ATOM   2038  CD2 LEU A 262       1.729   8.339  40.925  1.00 20.38
ATOM   2039  N   SER A 263       2.513  10.139  45.544  1.00 18.04
ATOM   2040  CA  SER A 263       1.602  10.254  46.689  1.00 20.14
ATOM   2041  C   SER A 263       0.370  11.147  46.400  1.00 18.92
ATOM   2042  O   SER A 263       0.437  12.063  45.646  1.00 17.51
ATOM   2043  CB  SER A 263       2.376  10.786  47.904  1.00 20.36
ATOM   2044  OG  SER A 263       3.477   9.968  48.225  1.00 24.42
ATOM   2045  N   ALA A 264      -0.745  10.811  47.174  1.00 19.84
ATOM   2046  CA  ALA A 264      -2.046  11.537  47.004  1.00 18.06
ATOM   2047  C   ALA A 264      -2.398  12.176  48.360  1.00 19.68
ATOM   2048  O   ALA A 264      -2.533  11.410  49.348  1.00 21.06
ATOM   2049  CB  ALA A 264      -3.227  10.763  46.504  1.00 15.61
ATOM   2050  N   GLY A 265      -2.476  13.487  48.336  1.00 20.86
ATOM   2051  CA  GLY A 265      -2.779  14.207  49.625  1.00 21.38
ATOM   2052  C   GLY A 265      -4.113  14.860  49.549  1.00 23.25
ATOM   2053  O   GLY A 265      -4.620  15.117  48.466  1.00 23.67
ATOM   2054  N   ILE A 266      -4.710  15.070  50.781  1.00 26.12
ATOM   2055  CA  ILE A 266      -6.077  15.713  50.789  1.00 24.73
ATOM   2056  C   ILE A 266      -5.964  17.126  51.317  1.00 26.51
ATOM   2057  O   ILE A 266      -5.261  17.455  52.322  1.00 26.58
ATOM   2058  CB  ILE A 266      -7.046  14.784  51.588  1.00 26.71
ATOM   2059  CG1 ILE A 266      -7.108  13.338  50.966  1.00 26.96
ATOM   2060  CG2 ILE A 266      -8.434  15.402  51.761  1.00 23.77
ATOM   2061  CD1 ILE A 266      -7.802  12.407  52.011  1.00 28.14
ATOM   2062  N   ASN A 267      -6.517  18.009  50.513  1.00 27.81
ATOM   2063  CA  ASN A 267      -6.501  19.448  50.776  1.00 30.65
ATOM   2064  C   ASN A 267      -7.229  19.579  52.095  1.00 33.63
ATOM   2065  O   ASN A 267      -8.367  19.092  52.238  1.00 33.06
ATOM   2066  CB  ASN A 267      -7.103  20.177  49.595  1.00 28.39
ATOM   2067  CG  ASN A 267      -6.958  21.653  49.552  1.00 29.79
ATOM   2068  OD1 ASN A 267      -6.844  22.222  50.696  1.00 30.71
ATOM   2069  ND2 ASN A 267      -6.981  22.288  48.391  1.00 24.61
ATOM   2070  N   ALA A 268      -6.468  20.240  52.979  1.00 38.69
ATOM   2071  CA  ALA A 268      -6.978  20.528  54.386  1.00 40.84
ATOM   2072  C   ALA A 268      -8.323  21.325  54.275  1.00 41.69
ATOM   2073  O   ALA A 268      -9.245  21.114  55.111  1.00 41.47
ATOM   2074  CB  ALA A 268      -5.956  21.212  55.283  1.00 33.60
ATOM   2075  N   ALA A 269      -8.386  22.153  53.224  1.00 42.17
ATOM   2076  CA  ALA A 269      -9.457  23.017  52.782  1.00 43.82
ATOM   2077  C   ALA A 269     -10.642  22.286  52.101  1.00 43.91
ATOM   2078  O   ALA A 269     -11.540  23.089  51.782  1.00 45.62
ATOM   2079  CB  ALA A 269      -9.026  24.146  51.777  1.00 42.37
ATOM   2080  N   SER A 270     -10.674  20.984  51.889  1.00 43.22
ATOM   2081  CA  SER A 270     -11.768  20.302  51.298  1.00 42.91
ATOM   2082  C   SER A 270     -12.849  19.923  52.343  1.00 43.35
ATOM   2083  O   SER A 270     -12.496  19.429  53.423  1.00 43.05
ATOM   2084  CB  SER A 270     -11.465  18.915  50.632  1.00 40.62
ATOM   2085  N   PRO A 271     -14.078  20.065  51.859  1.00 43.58
ATOM   2086  CA  PRO A 271     -15.322  19.656  52.469  1.00 44.93
ATOM   2087  C   PRO A 271     -15.608  18.135  52.272  1.00 46.11
ATOM   2088  O   PRO A 271     -16.396  17.416  52.957  1.00 45.88
ATOM   2089  CB  PRO A 271     -16.409  20.403  51.701  1.00 44.76
ATOM   2090  CG  PRO A 271     -15.740  21.277  50.673  1.00 44.50
ATOM   2091  CD  PRO A 271     -14.364  20.644  50.508  1.00 45.24
ATOM   2092  N   ASN A 272     -14.931  17.669  51.192  1.00 45.16
ATOM   2093  CA  ASN A 272     -15.043  16.289  50.724  1.00 42.93
ATOM   2094  C   ASN A 272     -14.045  15.401  51.386  1.00 42.70
ATOM   2095  O   ASN A 272     -13.704  14.487  50.584  1.00 45.22
ATOM   2096  CB  ASN A 272     -14.848  16.392  49.181  1.00 42.30
ATOM   2097  CG  ASN A 272     -15.725  17.476  48.559  1.00 44.10
ATOM   2098  OD1 ASN A 272     -16.959  17.144  48.563  1.00 47.06
ATOM   2099  ND2 ASN A 272     -15.391  18.648  48.007  1.00 39.66
ATOM   2100  N   LYS A 273     -13.520  15.407  52.562  1.00 41.00
ATOM   2101  CA  LYS A 273     -12.469  14.490  52.986  1.00 42.06
ATOM   2102  C   LYS A 273     -12.782  13.002  52.998  1.00 43.32
ATOM   2103  O   LYS A 273     -11.857  12.142  52.841  1.00 42.20
ATOM   2104  CB  LYS A 273     -11.900  14.710  54.439  1.00 43.03
ATOM   2105  CG  LYS A 273     -11.513  16.145  54.722  1.00 45.48
ATOM   2106  CD  LYS A 273     -10.383  16.409  55.668  1.00 48.86
ATOM   2107  CE  LYS A 273      -9.622  17.733  55.521  1.00 50.21
ATOM   2108  NZ  LYS A 273     -10.427  18.974  55.546  1.00 49.62
ATOM   2109  N   GLU A 274     -14.037  12.756  53.387  1.00 43.25
ATOM   2110  CA  GLU A 274     -14.614  11.429  53.561  1.00 42.62
ATOM   2111  C   GLU A 274     -14.795  10.793  52.185  1.00 40.74
ATOM   2112  O   GLU A 274     -14.399   9.598  52.123  1.00 41.76
ATOM   2113  CB  GLU A 274     -15.877  11.346  54.394  1.00 48.11
ATOM   2114  CG  GLU A 274     -16.042  10.283  55.493  1.00 54.86
ATOM   2115  CD  GLU A 274     -14.965   9.645  56.302  1.00 58.92
ATOM   2116  OE1 GLU A 274     -14.268  10.182  57.198  1.00 60.51
ATOM   2117  OE2 GLU A 274     -14.739   8.388  56.039  1.00 60.94
ATOM   2118  N   LEU A 275     -15.257  11.520  51.219  1.00 39.62
ATOM   2119  CA  LEU A 275     -15.412  11.112  49.825  1.00 39.50
ATOM   2120  C   LEU A 275     -14.028  10.689  49.243  1.00 39.07
ATOM   2121  O   LEU A 275     -13.788   9.699  48.572  1.00 38.33
ATOM   2122  CB  LEU A 275     -15.907  12.298  48.955  1.00 38.16
ATOM   2123  CG  LEU A 275     -17.327  12.817  49.256  1.00 39.52
ATOM   2124  CD1 LEU A 275     -17.909  13.672  48.135  1.00 38.49
ATOM   2125  CD2 LEU A 275     -18.154  11.563  49.498  1.00 37.75
ATOM   2126  N   ALA A 276     -13.120  11.633  49.513  1.00 38.83
ATOM   2127  CA  ALA A 276     -11.702  11.588  49.132  1.00 36.98
ATOM   2128  C   ALA A 276     -11.144  10.306  49.704  1.00 36.67
ATOM   2129  O   ALA A 276     -10.607   9.457  48.947  1.00 33.27
ATOM   2130  CB  ALA A 276     -11.019  12.876  49.554  1.00 38.64
ATOM   2131  N   LYS A 277     -11.309  10.147  51.027  1.00 35.90
ATOM   2132  CA  LYS A 277     -10.777   8.868  51.586  1.00 37.91
ATOM   2133  C   LYS A 277     -11.454   7.676  50.949  1.00 38.29
ATOM   2134  O   LYS A 277     -10.809   6.623  50.629  1.00 37.92
ATOM   2135  CB  LYS A 277     -10.741   8.899  53.126  1.00 38.85
ATOM   2136  CG  LYS A 277     -11.789   8.234  53.903  1.00 45.72
ATOM   2137  CD  LYS A 277     -11.668   7.757  55.368  1.00 48.11
ATOM   2138  CE  LYS A 277     -10.603   6.716  55.618  1.00 51.36
ATOM   2139  NZ  LYS A 277     -10.590   5.849  56.824  1.00 52.97
ATOM   2140  N   GLU A 278     -12.758   7.680  50.686  1.00 40.78
ATOM   2141  CA  GLU A 278     -13.426   6.473  50.118  1.00 42.39
ATOM   2142  C   GLU A 278     -12.737   6.072  48.794  1.00 40.26
ATOM   2143  O   GLU A 278     -12.314   4.902  48.625  1.00 40.14
ATOM   2144  CB  GLU A 278     -14.910   6.551  49.925  1.00 49.14
ATOM   2145  CG  GLU A 278     -15.988   6.804  50.903  1.00 55.93
ATOM   2146  CD  GLU A 278     -16.030   6.404  52.323  1.00 62.04
ATOM   2147  OE1 GLU A 278     -15.439   5.323  52.676  1.00 63.86
ATOM   2148  OE2 GLU A 278     -16.639   7.166  53.133  1.00 64.36
ATOM   2149  N   PHE A 279     -12.649   7.017  47.919  1.00 38.70
ATOM   2150  CA  PHE A 279     -11.991   7.033  46.593  1.00 37.81
ATOM   2151  C   PHE A 279     -10.583   6.454  46.585  1.00 36.25
ATOM   2152  O   PHE A 279     -10.178   5.561  45.830  1.00 37.28
ATOM   2153  CB  PHE A 279     -11.948   8.508  46.041  1.00 37.03
ATOM   2154  CG  PHE A 279     -11.338   8.534  44.654  1.00 38.73
ATOM   2155  CD1 PHE A 279      -9.957   8.655  44.503  1.00 38.71
ATOM   2156  CD2 PHE A 279     -12.142   8.363  43.535  1.00 41.56
ATOM   2157  CE1 PHE A 279      -9.404   8.683  43.240  1.00 39.71
ATOM   2158  CE2 PHE A 279     -11.602   8.360  42.230  1.00 43.00
ATOM   2159  CZ  PHE A 279     -10.201   8.513  42.107  1.00 41.76
ATOM   2160  N   LEU A 280      -9.746   7.010  47.461  1.00 34.49
ATOM   2161  CA  LEU A 280      -8.387   6.578  47.511  1.00 33.06
ATOM   2162  C   LEU A 280      -8.330   5.157  48.001  1.00 36.38
ATOM   2163  O   LEU A 280      -7.788   4.329  47.233  1.00 37.77
ATOM   2164  CB  LEU A 280      -7.572   7.588  48.339  1.00 30.09
ATOM   2165  CG  LEU A 280      -7.410   8.935  47.632  1.00 29.88
ATOM   2166  CD1 LEU A 280      -6.724   9.939  48.558  1.00 27.36
ATOM   2167  CD2 LEU A 280      -6.569   8.781  46.324  1.00 29.42
ATOM   2168  N   GLU A 281      -8.780   4.935  49.242  1.00 37.69
ATOM   2169  CA  GLU A 281      -8.660   3.587  49.864  1.00 36.83
ATOM   2170  C   GLU A 281      -9.485   2.456  49.285  1.00 36.15
ATOM   2171  O   GLU A 281      -9.044   1.295  49.327  1.00 35.94
ATOM   2172  CB  GLU A 281      -9.027   3.693  51.337  1.00 39.75
ATOM   2173  CG  GLU A 281      -8.690   5.011  52.086  1.00 40.65
ATOM   2174  CD  GLU A 281      -8.877   4.652  53.550  1.00 44.73
ATOM   2175  OE1 GLU A 281      -9.538   3.637  53.834  1.00 47.00
ATOM   2176  OE2 GLU A 281      -8.357   5.377  54.389  1.00 46.11
ATOM   2177  N   ASN A 282     -10.677   2.777  48.764  1.00 36.66
ATOM   2178  CA  ASN A 282     -11.578   1.802  48.175  1.00 37.18
ATOM   2179  C   ASN A 282     -11.711   1.751  46.640  1.00 35.96
ATOM   2180  O   ASN A 282     -12.282   0.683  46.271  1.00 34.56
ATOM   2181  CB  ASN A 282     -13.022   1.930  48.739  1.00 38.18
ATOM   2182  CG  ASN A 282     -13.017   1.779  50.257  1.00 38.66
ATOM   2183  OD1 ASN A 282     -12.149   1.147  50.924  1.00 40.16
ATOM   2184  ND2 ASN A 282     -14.022   2.539  50.740  1.00 40.19
ATOM   2185  N   TYR A 283     -11.283   2.730  45.876  1.00 35.92
ATOM   2186  CA  TYR A 283     -11.367   2.738  44.404  1.00 35.40
ATOM   2187  C   TYR A 283      -9.988   2.624  43.743  1.00 34.40
ATOM   2188  O   TYR A 283      -9.666   1.634  43.014  1.00 33.01
ATOM   2189  CB  TYR A 283     -12.176   3.951  43.817  1.00 40.10
ATOM   2190  CG  TYR A 283     -13.662   3.660  44.006  1.00 44.33
ATOM   2191  CD1 TYR A 283     -14.239   3.840  45.281  1.00 46.92
ATOM   2192  CD2 TYR A 283     -14.428   3.062  43.009  1.00 46.04
ATOM   2193  CE1 TYR A 283     -15.582   3.495  45.510  1.00 49.80
ATOM   2194  CE2 TYR A 283     -15.772   2.706  43.214  1.00 47.35
ATOM   2195  CZ  TYR A 283     -16.335   2.941  44.458  1.00 48.23
ATOM   2196  OH  TYR A 283     -17.624   2.610  44.675  1.00 49.84
ATOM   2197  N   LEU A 284      -9.165   3.656  44.047  1.00 32.87
ATOM   2198  CA  LEU A 284      -7.787   3.707  43.461  1.00 29.50
ATOM   2199  C   LEU A 284      -6.847   2.731  44.094  1.00 26.56
ATOM   2200  O   LEU A 284      -6.220   1.955  43.393  1.00 28.11
ATOM   2201  CB  LEU A 284      -7.256   5.122  43.620  1.00 26.55
ATOM   2202  CG  LEU A 284      -5.918   5.225  42.843  1.00 26.19
ATOM   2203  CD1 LEU A 284      -6.078   5.279  41.343  1.00 27.65
ATOM   2204  CD2 LEU A 284      -5.355   6.544  43.320  1.00 24.64
ATOM   2205  N   LEU A 285      -6.735   2.718  45.364  1.00 26.19
ATOM   2206  CA  LEU A 285      -5.788   1.822  46.006  1.00 28.57
ATOM   2207  C   LEU A 285      -6.254   0.361  46.076  1.00 30.35
ATOM   2208  O   LEU A 285      -6.161  -0.462  47.034  1.00 31.83
ATOM   2209  CB  LEU A 285      -5.302   2.512  47.291  1.00 29.05
ATOM   2210  CG  LEU A 285      -4.241   3.615  47.262  1.00 29.33
ATOM   2211  CD1 LEU A 285      -3.926   4.306  48.595  1.00 23.75
ATOM   2212  CD2 LEU A 285      -2.987   2.897  46.646  1.00 30.26
ATOM   2213  N   THR A 286      -6.686  -0.172  44.956  1.00 31.16
ATOM   2214  CA  THR A 286      -7.062  -1.573  44.761  1.00 33.00
ATOM   2215  C   THR A 286      -6.247  -2.173  43.628  1.00 32.28
ATOM   2216  O   THR A 286      -5.546  -1.422  42.915  1.00 35.56
ATOM   2217  CB  THR A 286      -8.610  -1.626  44.457  1.00 35.25
ATOM   2218  OG1 THR A 286      -8.940  -0.770  43.247  1.00 36.89
ATOM   2219  CG2 THR A 286      -9.424  -1.310  45.717  1.00 34.72
ATOM   2220  N   ASP A 287      -6.335  -3.394  43.257  1.00 31.15
ATOM   2221  CA  ASP A 287      -5.615  -3.992  42.090  1.00 29.63
ATOM   2222  C   ASP A 287      -6.251  -3.449  40.830  1.00 30.14
ATOM   2223  O   ASP A 287      -5.604  -3.231  39.826  1.00 32.00
ATOM   2224  CB  ASP A 287      -5.783  -5.474  42.093  1.00 28.32
ATOM   2225  CG  ASP A 287      -4.857  -6.257  42.894  1.00 29.50
ATOM   2226  OD1 ASP A 287      -3.964  -5.869  43.651  1.00 34.03
ATOM   2227  OD2 ASP A 287      -4.943  -7.510  42.795  1.00 37.41
ATOM   2228  N   GLU A 288      -7.527  -3.207  40.859  1.00 29.72
ATOM   2229  CA  GLU A 288      -8.272  -2.773  39.704  1.00 29.98
ATOM   2230  C   GLU A 288      -8.070  -1.349  39.360  1.00 28.84
ATOM   2231  O   GLU A 288      -7.990  -0.979  38.214  1.00 28.48
ATOM   2232  CB  GLU A 288      -9.763  -3.091  40.042  1.00 37.35
ATOM   2233  CG  GLU A 288      -9.850  -4.526  40.748  1.00 44.73
ATOM   2234  CD  GLU A 288      -9.924  -4.639  42.230  1.00 46.60
ATOM   2235  OE1 GLU A 288     -10.822  -4.088  42.914  1.00 49.73
ATOM   2236  OE2 GLU A 288      -9.005  -5.284  42.811  1.00 49.22
ATOM   2237  N   GLY A 289      -8.018  -0.494  40.387  1.00 29.56
ATOM   2238  CA  GLY A 289      -7.837   0.952  40.193  1.00 25.68
ATOM   2239  C   GLY A 289      -6.412   1.242  39.721  1.00 23.46
ATOM   2240  O   GLY A 289      -6.266   2.082  38.842  1.00 21.86
ATOM   2241  N   LEU A 290      -5.467   0.581  40.333  1.00 24.53
ATOM   2242  CA  LEU A 290      -4.048   0.766  39.984  1.00 25.64
ATOM   2243  C   LEU A 290      -3.820   0.327  38.525  1.00 27.65
ATOM   2244  O   LEU A 290      -3.054   1.002  37.827  1.00 25.48
ATOM   2245  CB  LEU A 290      -3.097   0.061  40.939  1.00 25.31
ATOM   2246  CG  LEU A 290      -3.065   0.710  42.320  1.00 21.12
ATOM   2247  CD1 LEU A 290      -2.060   0.014  43.162  1.00 25.13
ATOM   2248  CD2 LEU A 290      -2.700   2.175  42.059  1.00 23.36
ATOM   2249  N   GLU A 291      -4.522  -0.760  38.197  1.00 28.25
ATOM   2250  CA  GLU A 291      -4.331  -1.223  36.809  1.00 30.34
ATOM   2251  C   GLU A 291      -4.958  -0.340  35.773  1.00 26.80
ATOM   2252  O   GLU A 291      -4.244  -0.277  34.741  1.00 27.44
ATOM   2253  CB  GLU A 291      -4.723  -2.660  36.673  1.00 37.38
ATOM   2254  CG  GLU A 291      -6.119  -3.025  36.307  1.00 48.46
ATOM   2255  CD  GLU A 291      -6.107  -4.144  35.238  1.00 51.59
ATOM   2256  OE1 GLU A 291      -5.251  -4.041  34.367  1.00 52.16
ATOM   2257  OE2 GLU A 291      -7.013  -4.937  35.596  1.00 55.82
ATOM   2258  N   ALA A 292      -6.011   0.381  35.919  1.00 26.00
ATOM   2259  CA  ALA A 292      -6.599   1.309  34.980  1.00 24.71
ATOM   2260  C   ALA A 292      -5.612   2.429  34.710  1.00 24.42
ATOM   2261  O   ALA A 292      -5.495   3.014  33.671  1.00 25.84
ATOM   2262  CB  ALA A 292      -7.849   2.025  35.525  1.00 22.58
ATOM   2263  N   VAL A 293      -4.947   2.863  35.804  1.00 24.74
ATOM   2264  CA  VAL A 293      -3.960   3.949  35.776  1.00 24.38
ATOM   2265  C   VAL A 293      -2.691   3.445  35.028  1.00 24.89
ATOM   2266  O   VAL A 293      -2.315   4.198  34.145  1.00 24.06
ATOM   2267  CB  VAL A 293      -3.603   4.576  37.173  1.00 25.65
ATOM   2268  CG1 VAL A 293      -2.513   5.659  37.025  1.00 23.87
ATOM   2269  CG2 VAL A 293      -4.805   5.145  37.936  1.00 23.92
ATOM   2270  N   ASN A 294      -2.102   2.329  35.426  1.00 25.24
ATOM   2271  CA  ASN A 294      -0.915   1.724  34.907  1.00 26.72
ATOM   2272  C   ASN A 294      -1.022   1.378  33.429  1.00 27.44
ATOM   2273  O   ASN A 294      -0.039   1.442  32.707  1.00 30.55
ATOM   2274  CB  ASN A 294      -0.467   0.549  35.769  1.00 28.51
ATOM   2275  CG  ASN A 294       0.957   0.042  35.487  1.00 29.07
ATOM   2276  OD1 ASN A 294       1.941   0.567  36.010  1.00 27.38
ATOM   2277  ND2 ASN A 294       1.076  -1.064  34.709  1.00 26.93
ATOM   2278  N   LYS A 295      -2.147   1.095  32.877  1.00 31.09
ATOM   2279  CA  LYS A 295      -2.392   0.796  31.438  1.00 32.69
ATOM   2280  C   LYS A 295      -2.311   2.118  30.687  1.00 32.30
ATOM   2281  O   LYS A 295      -1.805   2.078  29.521  1.00 35.27
ATOM   2282  CB  LYS A 295      -3.620  -0.007  31.173  1.00 38.08
ATOM   2283  CG  LYS A 295      -5.010   0.545  31.222  1.00 45.95
ATOM   2284  CD  LYS A 295      -5.207   1.810  30.430  1.00 53.62
ATOM   2285  CE  LYS A 295      -5.866   1.701  29.042  1.00 58.68
ATOM   2286  NZ  LYS A 295      -5.791   3.031  28.290  1.00 60.11
ATOM   2287  N   ASP A 296      -2.655   3.230  31.299  1.00 27.71
ATOM   2288  CA  ASP A 296      -2.508   4.559  30.693  1.00 26.59
ATOM   2289  C   ASP A 296      -1.019   4.914  30.677  1.00 26.02
ATOM   2290  O   ASP A 296      -0.379   4.858  29.537  1.00 26.93
ATOM   2291  CB  ASP A 296      -3.521   5.513  31.323  1.00 25.58
ATOM   2292  CG  ASP A 296      -3.400   6.903  30.810  1.00 25.34
ATOM   2293  OD1 ASP A 296      -2.797   7.103  29.709  1.00 28.67
ATOM   2294  OD2 ASP A 296      -3.876   7.876  31.403  1.00 28.14
ATOM   2295  N   LYS A 297      -0.406   5.212  31.797  1.00 22.68
ATOM   2296  CA  LYS A 297       1.080   5.467  31.890  1.00 21.42
ATOM   2297  C   LYS A 297       1.601   4.594  32.970  1.00 19.90
ATOM   2298  O   LYS A 297       1.072   4.664  34.082  1.00 22.20
ATOM   2299  CB  LYS A 297       1.387   6.934  32.106  1.00 20.77
ATOM   2300  CG  LYS A 297       1.156   7.719  30.830  1.00 27.53
ATOM   2301  CD  LYS A 297       0.924   9.146  31.231  1.00 37.26
ATOM   2302  CE  LYS A 297       1.243  10.145  30.095  1.00 40.57
ATOM   2303  NZ  LYS A 297       0.298  11.370  30.255  1.00 40.85
ATOM   2304  N   PRO A 298       2.541   3.703  32.818  1.00 20.53
ATOM   2305  CA  PRO A 298       3.008   2.820  33.878  1.00 19.54
ATOM   2306  C   PRO A 298       3.414   3.560  35.118  1.00 19.85
ATOM   2307  O   PRO A 298       4.078   4.613  35.073  1.00 17.94
ATOM   2308  CB  PRO A 298       4.232   2.071  33.279  1.00 20.51
ATOM   2309  CG  PRO A 298       3.950   2.193  31.754  1.00 21.20
ATOM   2310  CD  PRO A 298       3.236   3.493  31.541  1.00 19.27
ATOM   2311  N   LEU A 299       3.063   2.999  36.294  1.00 21.08
ATOM   2312  CA  LEU A 299       3.416   3.623  37.573  1.00 20.11
ATOM   2313  C   LEU A 299       4.800   3.335  38.103  1.00 18.73
ATOM   2314  O   LEU A 299       5.328   4.166  38.931  1.00 21.38
ATOM   2315  CB  LEU A 299       2.293   3.221  38.595  1.00 21.52
ATOM   2316  CG  LEU A 299       0.905   3.759  38.505  1.00 23.94
ATOM   2317  CD1 LEU A 299      -0.003   2.900  39.450  1.00 23.54
ATOM   2318  CD2 LEU A 299       0.775   5.218  38.927  1.00 23.25
ATOM   2319  N   GLY A 300       5.415   2.227  37.820  1.00 18.95
ATOM   2320  CA  GLY A 300       6.682   1.825  38.400  1.00 18.40
ATOM   2321  C   GLY A 300       6.217   0.644  39.370  1.00 21.72
ATOM   2322  O   GLY A 300       5.184  -0.025  39.094  1.00 21.48
ATOM   2323  N   ALA A 301       6.969   0.573  40.435  1.00 20.58
ATOM   2324  CA  ALA A 301       6.747  -0.450  41.501  1.00 22.75
ATOM   2325  C   ALA A 301       5.612   0.062  42.332  1.00 24.25
ATOM   2326  O   ALA A 301       5.787   1.241  42.731  1.00 27.75
ATOM   2327  CB  ALA A 301       8.096  -0.623  42.262  1.00 19.62
ATOM   2328  N   VAL A 302       4.447  -0.486  42.576  1.00 22.94
ATOM   2329  CA  VAL A 302       3.308   0.029  43.321  1.00 22.51
ATOM   2330  C   VAL A 302       3.453  -0.272  44.814  1.00 24.21
ATOM   2331  O   VAL A 302       4.165  -1.226  45.222  1.00 25.58
ATOM   2332  CB  VAL A 302       1.965  -0.486  42.789  1.00 22.57
ATOM   2333  CG1 VAL A 302       1.630   0.027  41.392  1.00 21.36
ATOM   2334  CG2 VAL A 302       1.834  -2.009  42.858  1.00 22.06
ATOM   2335  N   ALA A 303       2.851   0.594  45.621  1.00 24.53
ATOM   2336  CA  ALA A 303       2.990   0.304  47.105  1.00 25.60
ATOM   2337  C   ALA A 303       2.036  -0.790  47.559  1.00 25.64
ATOM   2338  O   ALA A 303       2.251  -1.349  48.674  1.00 28.64
ATOM   2339  CB  ALA A 303       2.774   1.599  47.836  1.00 23.88
ATOM   2340  N   LEU A 304       1.004  -1.086  46.781  1.00 27.46
ATOM   2341  CA  LEU A 304      -0.010  -2.147  47.065  1.00 27.72
ATOM   2342  C   LEU A 304       0.647  -3.500  46.766  1.00 27.24
ATOM   2343  O   LEU A 304       1.040  -3.874  45.640  1.00 23.14
ATOM   2344  CB  LEU A 304      -1.264  -1.817  46.297  1.00 29.54
ATOM   2345  CG  LEU A 304      -2.545  -2.572  46.617  1.00 30.50
ATOM   2346  CD1 LEU A 304      -2.974  -2.027  48.009  1.00 29.34
ATOM   2347  CD2 LEU A 304      -3.611  -2.399  45.497  1.00 27.41
ATOM   2348  N   LYS A 305       0.812  -4.212  47.913  1.00 26.72
ATOM   2349  CA  LYS A 305       1.515  -5.508  47.763  1.00 28.47
ATOM   2350  C   LYS A 305       0.967  -6.501  46.763  1.00 26.16
ATOM   2351  O   LYS A 305       1.744  -7.252  46.111  1.00 26.59
ATOM   2352  CB  LYS A 305       1.663  -6.173  49.180  1.00 28.60
ATOM   2353  CG  LYS A 305       2.661  -5.297  49.928  1.00 30.41
ATOM   2354  CD  LYS A 305       3.182  -5.810  51.200  1.00 33.73
ATOM   2355  CE  LYS A 305       2.175  -5.714  52.341  1.00 37.16
ATOM   2356  NZ  LYS A 305       2.999  -5.859  53.618  1.00 41.24
ATOM   2357  N   SER A 306      -0.312  -6.605  46.670  1.00 28.46
ATOM   2358  CA  SER A 306      -1.097  -7.541  45.872  1.00 29.48
ATOM   2359  C   SER A 306      -0.832  -7.318  44.395  1.00 31.28
ATOM   2360  O   SER A 306      -0.484  -8.285  43.702  1.00 33.56
ATOM   2361  CB  SER A 306      -2.552  -7.435  46.223  1.00 28.01
ATOM   2362  OG  SER A 306      -3.118  -6.173  45.893  1.00 32.04
ATOM   2363  N   TYR A 307      -1.015  -6.083  43.949  1.00 31.97
ATOM   2364  CA  TYR A 307      -0.698  -5.624  42.578  1.00 30.91
ATOM   2365  C   TYR A 307       0.791  -5.683  42.253  1.00 29.77
ATOM   2366  O   TYR A 307       1.277  -6.132  41.143  1.00 28.61
ATOM   2367  CB  TYR A 307      -1.365  -4.238  42.325  1.00 32.07
ATOM   2368  CG  TYR A 307      -1.352  -3.935  40.844  1.00 32.85
ATOM   2369  CD1 TYR A 307      -1.994  -4.847  39.981  1.00 36.61
ATOM   2370  CD2 TYR A 307      -0.686  -2.860  40.277  1.00 35.39
ATOM   2371  CE1 TYR A 307      -2.067  -4.621  38.568  1.00 35.89
ATOM   2372  CE2 TYR A 307      -0.669  -2.645  38.872  1.00 35.31
ATOM   2373  CZ  TYR A 307      -1.361  -3.507  38.040  1.00 37.14
ATOM   2374  OH  TYR A 307      -1.375  -3.355  36.667  1.00 37.46
ATOM   2375  N   GLU A 308       1.649  -5.278  43.239  1.00 29.32
ATOM   2376  CA  GLU A 308       3.065  -5.247  43.026  1.00 28.64
ATOM   2377  C   GLU A 308       3.610  -6.617  42.657  1.00 33.09
ATOM   2378  O   GLU A 308       4.621  -6.864  41.933  1.00 32.77
ATOM   2379  CB  GLU A 308       3.891  -4.787  44.221  1.00 26.96
ATOM   2380  CG  GLU A 308       5.383  -4.841  43.820  1.00 24.83
ATOM   2381  CD  GLU A 308       5.774  -4.031  42.630  1.00 25.19
ATOM   2382  OE1 GLU A 308       4.991  -3.310  42.009  1.00 23.32
ATOM   2383  OE2 GLU A 308       6.919  -4.141  42.238  1.00 27.76
ATOM   2384  N   GLU A 309       2.893  -7.543  43.308  1.00 35.06
ATOM   2385  CA  GLU A 309       3.155  -8.995  43.123  1.00 37.44
ATOM   2386  C   GLU A 309       2.998  -9.439  41.661  1.00 37.07
ATOM   2387  O   GLU A 309       3.728 -10.263  41.128  1.00 34.96
ATOM   2388  CB  GLU A 309       2.189  -9.793  44.025  1.00 37.46
ATOM   2389  CG  GLU A 309       2.880 -10.925  44.714  1.00 44.63
ATOM   2390  CD  GLU A 309       2.068 -12.118  45.138  1.00 48.24
ATOM   2391  OE1 GLU A 309       1.735 -12.801  44.112  1.00 53.82
ATOM   2392  OE2 GLU A 309       1.823 -12.321  46.298  1.00 49.26
ATOM   2393  N   GLU A 310       2.017  -8.864  40.962  1.00 39.26
ATOM   2394  CA  GLU A 310       1.764  -9.191  39.578  1.00 41.74
ATOM   2395  C   GLU A 310       2.656  -8.346  38.653  1.00 42.96
ATOM   2396  O   GLU A 310       2.921  -8.757  37.461  1.00 44.07
ATOM   2397  CB  GLU A 310       0.309  -8.931  39.241  1.00 45.99
ATOM   2398  CG  GLU A 310      -0.789  -9.197  40.255  1.00 53.78
ATOM   2399  CD  GLU A 310      -2.179  -8.698  39.844  1.00 59.50
ATOM   2400  OE1 GLU A 310      -2.717  -8.676  38.705  1.00 60.18
ATOM   2401  OE2 GLU A 310      -2.827  -8.282  40.881  1.00 62.13
ATOM   2402  N   LEU A 311       3.084  -7.207  39.223  1.00 40.62
ATOM   2403  CA  LEU A 311       3.889  -6.214  38.434  1.00 39.00
ATOM   2404  C   LEU A 311       5.326  -6.610  38.299  1.00 39.37
ATOM   2405  O   LEU A 311       6.065  -6.264  37.292  1.00 34.71
ATOM   2406  CB  LEU A 311       3.657  -4.868  39.117  1.00 33.62
ATOM   2407  CG  LEU A 311       3.140  -3.751  38.278  1.00 33.27
ATOM   2408  CD1 LEU A 311       2.114  -4.208  37.284  1.00 27.90
ATOM   2409  CD2 LEU A 311       2.629  -2.765  39.332  1.00 32.20
ATOM   2410  N   ALA A 312       5.986  -7.363  39.288  1.00 41.27
ATOM   2411  CA  ALA A 312       7.269  -7.450  38.545  1.00 44.77
ATOM   2412  C   ALA A 312       8.251  -8.500  38.936  1.00 44.68
ATOM   2413  O   ALA A 312       8.734  -8.336  39.979  1.00 46.80
ATOM   2414  CB  ALA A 312       7.777  -6.068  38.273  1.00 48.19
ATOM   2415  N   LYS A 313       8.156  -9.396  38.067  1.00 43.40
ATOM   2416  CA  LYS A 313       8.227 -10.300  37.018  1.00 42.92
ATOM   2417  C   LYS A 313       8.569  -9.603  35.665  1.00 39.72
ATOM   2418  O   LYS A 313       9.305 -10.134  34.786  1.00 41.92
ATOM   2419  CB  LYS A 313       6.891 -11.060  36.777  1.00 44.36
ATOM   2420  CG  LYS A 313       5.952 -10.884  37.952  1.00 49.80
ATOM   2421  CD  LYS A 313       5.825 -12.118  38.858  1.00 52.47
ATOM   2422  CE  LYS A 313       4.562 -12.114  39.716  1.00 55.24
ATOM   2423  NZ  LYS A 313       3.415 -12.979  39.329  1.00 56.79
ATOM   2424  N   ASP A 314       8.024  -8.387  35.642  1.00 35.61
ATOM   2425  CA  ASP A 314       8.286  -7.512  34.442  1.00 33.24
ATOM   2426  C   ASP A 314       9.745  -7.066  34.563  1.00 29.14
ATOM   2427  O   ASP A 314      10.013  -6.527  35.645  1.00 30.71
ATOM   2428  CB  ASP A 314       7.254  -6.424  34.302  1.00 32.83
ATOM   2429  CG  ASP A 314       7.333  -5.527  33.083  1.00 31.36
ATOM   2430  OD1 ASP A 314       8.328  -5.335  32.400  1.00 32.19
ATOM   2431  OD2 ASP A 314       6.273  -4.868  32.813  1.00 36.91
ATOM   2432  N   PRO A 315      10.593  -7.339  33.620  1.00 26.01
ATOM   2433  CA  PRO A 315      11.969  -6.984  33.705  1.00 26.03
ATOM   2434  C   PRO A 315      12.179  -5.436  33.819  1.00 23.11
ATOM   2435  O   PRO A 315      13.263  -5.094  34.330  1.00 22.58
ATOM   2436  CB  PRO A 315      12.623  -7.677  32.498  1.00 27.67
ATOM   2437  CG  PRO A 315      11.515  -7.875  31.498  1.00 27.58
ATOM   2438  CD  PRO A 315      10.271  -8.078  32.357  1.00 28.10
ATOM   2439  N   ARG A 316      11.332  -4.648  33.311  1.00 22.71
ATOM   2440  CA  ARG A 316      11.319  -3.160  33.354  1.00 22.46
ATOM   2441  C   ARG A 316      11.155  -2.735  34.803  1.00 22.51
ATOM   2442  O   ARG A 316      11.915  -1.871  35.253  1.00 21.69
ATOM   2443  CB  ARG A 316      10.260  -2.542  32.458  1.00 24.55
ATOM   2444  CG  ARG A 316      10.691  -2.863  30.985  1.00 21.61
ATOM   2445  CD  ARG A 316       9.735  -2.366  30.018  1.00 24.42
ATOM   2446  NE  ARG A 316       8.379  -2.720  30.358  1.00 25.62
ATOM   2447  CZ  ARG A 316       7.185  -2.364  30.006  1.00 25.75
ATOM   2448  NH1 ARG A 316       6.836  -1.422  29.045  1.00 30.76
ATOM   2449  NH2 ARG A 316       6.105  -2.832  30.689  1.00 28.63
ATOM   2450  N   ILE A 317      10.236  -3.380  35.444  1.00 22.14
ATOM   2451  CA  ILE A 317       9.955  -3.207  36.885  1.00 24.72
ATOM   2452  C   ILE A 317      11.108  -3.712  37.706  1.00 25.68
ATOM   2453  O   ILE A 317      11.542  -3.141  38.744  1.00 23.31
ATOM   2454  CB  ILE A 317       8.545  -3.721  37.276  1.00 24.64
ATOM   2455  CG1 ILE A 317       7.602  -2.632  36.661  1.00 27.94
ATOM   2456  CG2 ILE A 317       8.331  -3.748  38.821  1.00 26.99
ATOM   2457  CD1 ILE A 317       6.287  -2.506  37.381  1.00 32.96
ATOM   2458  N   ALA A 318      11.694  -4.866  37.333  1.00 25.13
ATOM   2459  CA  ALA A 318      12.849  -5.339  38.102  1.00 23.36
ATOM   2460  C   ALA A 318      14.007  -4.370  38.042  1.00 23.40
ATOM   2461  O   ALA A 318      14.815  -4.145  38.957  1.00 23.37
ATOM   2462  CB  ALA A 318      13.251  -6.661  37.512  1.00 23.30
ATOM   2463  N   ALA A 319      14.153  -3.736  36.877  1.00 22.32
ATOM   2464  CA  ALA A 319      15.273  -2.783  36.728  1.00 20.47
ATOM   2465  C   ALA A 319      15.031  -1.506  37.532  1.00 19.03
ATOM   2466  O   ALA A 319      15.988  -0.886  38.018  1.00 18.75
ATOM   2467  CB  ALA A 319      15.401  -2.551  35.186  1.00 20.41
ATOM   2468  N   THR A 320      13.767  -1.139  37.572  1.00 18.38
ATOM   2469  CA  THR A 320      13.277   0.029  38.327  1.00 21.40
ATOM   2470  C   THR A 320      13.670  -0.163  39.815  1.00 22.53
ATOM   2471  O   THR A 320      14.363   0.726  40.400  1.00 21.62
ATOM   2472  CB  THR A 320      11.768   0.283  38.248  1.00 19.28
ATOM   2473  OG1 THR A 320      11.460   0.518  36.868  1.00 20.77
ATOM   2474  CG2 THR A 320      11.245   1.451  39.179  1.00 18.05
ATOM   2475  N   MET A 321      13.266  -1.368  40.292  1.00 20.96
ATOM   2476  CA  MET A 321      13.683  -1.771  41.680  1.00 24.11
ATOM   2477  C   MET A 321      15.161  -1.849  41.922  1.00 21.99
ATOM   2478  O   MET A 321      15.682  -1.460  43.030  1.00 21.03
ATOM   2479  CB  MET A 321      12.995  -3.090  42.079  1.00 30.25
ATOM   2480  CG  MET A 321      11.764  -2.723  42.942  1.00 38.08
ATOM   2481  SD  MET A 321      10.835  -4.318  42.838  1.00 48.07
ATOM   2482  CE  MET A 321      12.266  -5.373  43.270  1.00 43.91
ATOM   2483  N   GLU A 322      15.956  -2.271  40.973  1.00 21.26
ATOM   2484  CA  GLU A 322      17.376  -2.312  41.190  1.00 23.29
ATOM   2485  C   GLU A 322      17.976  -0.899  41.271  1.00 22.41
ATOM   2486  O   GLU A 322      18.891  -0.688  42.088  1.00 19.92
ATOM   2487  CB  GLU A 322      18.023  -3.095  40.035  1.00 30.03
ATOM   2488  CG  GLU A 322      19.541  -3.060  39.921  1.00 37.69
ATOM   2489  CD  GLU A 322      20.162  -4.415  39.567  1.00 45.45
ATOM   2490  OE1 GLU A 322      19.203  -5.296  39.522  1.00 48.17
ATOM   2491  OE2 GLU A 322      21.410  -4.494  39.454  1.00 46.30
ATOM   2492  N   ASN A 323      17.514  -0.002  40.380  1.00 19.96
ATOM   2493  CA  ASN A 323      18.078   1.401  40.441  1.00 17.98
ATOM   2494  C   ASN A 323      17.568   2.020  41.753  1.00 15.90
ATOM   2495  O   ASN A 323      18.351   2.771  42.310  1.00 16.18
ATOM   2496  CB  ASN A 323      17.536   2.106  39.181  1.00 17.12
ATOM   2497  CG  ASN A 323      18.364   1.762  37.917  1.00 16.19
ATOM   2498  OD1 ASN A 323      19.605   1.915  37.947  1.00 18.44
ATOM   2499  ND2 ASN A 323      17.701   1.335  36.935  1.00 16.14
ATOM   2500  N   ALA A 324      16.332   1.739  42.068  1.00 14.92
ATOM   2501  CA  ALA A 324      15.781   2.283  43.340  1.00 17.28
ATOM   2502  C   ALA A 324      16.592   1.898  44.556  1.00 19.22
ATOM   2503  O   ALA A 324      16.921   2.638  45.484  1.00 19.87
ATOM   2504  CB  ALA A 324      14.293   1.871  43.505  1.00 14.71
ATOM   2505  N   GLN A 325      16.981   0.615  44.627  1.00 23.76
ATOM   2506  CA  GLN A 325      17.836  -0.011  45.657  1.00 25.61
ATOM   2507  C   GLN A 325      19.201   0.627  45.715  1.00 23.27
ATOM   2508  O   GLN A 325      19.775   0.765  46.812  1.00 25.60
ATOM   2509  CB  GLN A 325      17.900  -1.554  45.454  1.00 32.46
ATOM   2510  CG  GLN A 325      16.660  -2.226  46.040  1.00 43.75
ATOM   2511  CD  GLN A 325      16.714  -2.166  47.580  1.00 53.35
ATOM   2512  OE1 GLN A 325      15.653  -1.973  48.245  1.00 59.01
ATOM   2513  NE2 GLN A 325      17.880  -2.305  48.272  1.00 54.67
ATOM   2514  N   LYS A 326      19.828   1.126  44.689  1.00 20.42
ATOM   2515  CA  LYS A 326      21.067   1.790  44.632  1.00 19.27
ATOM   2516  C   LYS A 326      20.910   3.291  44.881  1.00 20.63
ATOM   2517  O   LYS A 326      21.901   3.981  45.005  1.00 23.89
ATOM   2518  CB  LYS A 326      21.653   1.575  43.241  1.00 23.16
ATOM   2519  CG  LYS A 326      21.650   0.073  43.090  1.00 26.63
ATOM   2520  CD  LYS A 326      22.762  -0.662  42.509  1.00 35.11
ATOM   2521  CE  LYS A 326      22.424  -1.084  41.014  1.00 36.66
ATOM   2522  NZ  LYS A 326      23.461  -2.223  40.908  1.00 42.18
ATOM   2523  N   GLY A 327      19.697   3.721  44.902  1.00 19.85
ATOM   2524  CA  GLY A 327      19.441   5.115  45.103  1.00 20.10
ATOM   2525  C   GLY A 327      19.154   5.384  46.581  1.00 21.75
ATOM   2526  O   GLY A 327      19.465   4.636  47.514  1.00 24.65
ATOM   2527  N   GLU A 328      18.465   6.465  46.792  1.00 21.74
ATOM   2528  CA  GLU A 328      18.044   6.930  48.109  1.00 23.60
ATOM   2529  C   GLU A 328      16.715   7.634  47.986  1.00 20.20
ATOM   2530  O   GLU A 328      16.476   8.416  47.022  1.00 21.38
ATOM   2531  CB  GLU A 328      19.183   7.684  48.695  1.00 26.99
ATOM   2532  CG  GLU A 328      19.396   9.115  48.815  1.00 39.78
ATOM   2533  CD  GLU A 328      20.252   9.452  50.039  1.00 46.04
ATOM   2534  OE1 GLU A 328      21.435   9.049  50.012  1.00 50.45
ATOM   2535  OE2 GLU A 328      19.593  10.113  50.924  1.00 51.26
ATOM   2536  N   ILE A 329      15.835   7.278  48.865  1.00 18.47
ATOM   2537  CA  ILE A 329      14.512   7.850  48.978  1.00 22.81
ATOM   2538  C   ILE A 329      14.716   9.319  49.323  1.00 21.18
ATOM   2539  O   ILE A 329      15.558   9.632  50.177  1.00 22.50
ATOM   2540  CB  ILE A 329      13.705   7.175  50.148  1.00 26.47
ATOM   2541  CG1 ILE A 329      12.323   7.830  50.256  1.00 29.54
ATOM   2542  CG2 ILE A 329      14.590   7.436  51.445  1.00 32.85
ATOM   2543  CD1 ILE A 329      11.238   6.811  49.727  1.00 36.55
ATOM   2544  N   MET A 330      14.004  10.230  48.720  1.00 20.31
ATOM   2545  CA  MET A 330      14.214  11.676  48.984  1.00 16.70
ATOM   2546  C   MET A 330      13.681  11.962  50.407  1.00 16.98
ATOM   2547  O   MET A 330      12.640  11.384  50.844  1.00 16.93
ATOM   2548  CB  MET A 330      13.283  12.426  47.958  1.00 17.18
ATOM   2549  CG  MET A 330      13.995  12.330  46.582  1.00 15.84
ATOM   2550  SD  MET A 330      13.001  13.363  45.444  1.00 20.01
ATOM   2551  CE  MET A 330      11.719  12.344  44.943  1.00 12.57
ATOM   2552  N   PRO A 331      14.291  12.952  50.977  1.00 18.16
ATOM   2553  CA  PRO A 331      13.770  13.618  52.206  1.00 18.32
ATOM   2554  C   PRO A 331      12.455  14.279  51.832  1.00 19.51
ATOM   2555  O   PRO A 331      12.209  14.639  50.660  1.00 20.22
ATOM   2556  CB  PRO A 331      14.789  14.752  52.417  1.00 19.06
ATOM   2557  CG  PRO A 331      16.075  14.125  51.792  1.00 18.27
ATOM   2558  CD  PRO A 331      15.469  13.674  50.428  1.00 16.86
ATOM   2559  N   ASN A 332      11.459  14.570  52.699  1.00 19.62
ATOM   2560  CA  ASN A 332      10.258  15.282  52.456  1.00 17.83
ATOM   2561  C   ASN A 332      10.290  16.608  53.302  1.00 18.03
ATOM   2562  O   ASN A 332       9.232  17.222  53.316  1.00 22.06
ATOM   2563  CB  ASN A 332       9.029  14.515  52.841  1.00 20.22
ATOM   2564  CG  ASN A 332       8.854  14.227  54.338  1.00 22.63
ATOM   2565  OD1 ASN A 332       9.548  14.684  55.223  1.00 23.08
ATOM   2566  ND2 ASN A 332       7.942  13.296  54.563  1.00 24.29
ATOM   2567  N   ILE A 333      11.379  16.927  53.894  1.00 18.29
ATOM   2568  CA  ILE A 333      11.546  18.150  54.734  1.00 19.45
ATOM   2569  C   ILE A 333      11.199  19.379  53.956  1.00 20.34
ATOM   2570  O   ILE A 333      11.411  19.316  52.688  1.00 22.12
ATOM   2571  CB  ILE A 333      12.992  18.159  55.330  1.00 19.92
ATOM   2572  CG1 ILE A 333      14.137  18.246  54.262  1.00 19.00
ATOM   2573  CG2 ILE A 333      13.258  16.958  56.270  1.00 20.24
ATOM   2574  CD1 ILE A 333      15.557  18.449  54.905  1.00 20.32
ATOM   2575  N   PRO A 334      10.742  20.494  54.504  1.00 21.00
ATOM   2576  CA  PRO A 334      10.381  21.727  53.790  1.00 19.32
ATOM   2577  C   PRO A 334      11.540  22.259  52.966  1.00 20.33
ATOM   2578  O   PRO A 334      11.331  22.939  51.910  1.00 21.17
ATOM   2579  CB  PRO A 334       9.952  22.723  54.843  1.00 19.72
ATOM   2580  CG  PRO A 334       9.422  21.727  55.895  1.00 20.09
ATOM   2581  CD  PRO A 334      10.437  20.620  55.966  1.00 21.23
ATOM   2582  N   GLN A 335      12.756  22.002  53.423  1.00 18.96
ATOM   2583  CA  GLN A 335      13.949  22.471  52.725  1.00 20.55
ATOM   2584  C   GLN A 335      14.166  21.791  51.347  1.00 22.35
ATOM   2585  O   GLN A 335      15.045  22.355  50.651  1.00 20.15
ATOM   2586  CB  GLN A 335      15.223  22.199  53.498  1.00 20.40
ATOM   2587  CG  GLN A 335      15.280  23.111  54.677  1.00 23.71
ATOM   2588  CD  GLN A 335      14.291  22.720  55.746  1.00 25.17
ATOM   2589  OE1 GLN A 335      13.994  23.690  56.476  1.00 32.46
ATOM   2590  NE2 GLN A 335      13.784  21.532  56.025  1.00 20.49
ATOM   2591  N   MET A 336      13.451  20.729  50.982  1.00 22.07
ATOM   2592  CA  MET A 336      13.616  20.128  49.599  1.00 20.90
ATOM   2593  C   MET A 336      13.366  21.087  48.465  1.00 21.36
ATOM   2594  O   MET A 336      14.124  21.061  47.422  1.00 20.28
ATOM   2595  CB  MET A 336      12.756  18.876  49.491  1.00 21.12
ATOM   2596  CG  MET A 336      13.469  17.755  50.231  1.00 20.43
ATOM   2597  SD  MET A 336      15.148  17.364  49.709  1.00 21.75
ATOM   2598  CE  MET A 336      14.873  16.592  48.118  1.00 19.22
ATOM   2599  N   SER A 337      12.454  22.007  48.642  1.00 23.07
ATOM   2600  CA  SER A 337      12.275  23.030  47.555  1.00 26.38
ATOM   2601  C   SER A 337      13.459  23.994  47.358  1.00 24.84
ATOM   2602  O   SER A 337      13.716  24.310  46.188  1.00 24.32
ATOM   2603  CB  SER A 337      10.966  23.745  47.760  1.00 31.40
ATOM   2604  OG  SER A 337      11.064  25.006  48.268  1.00 38.53
ATOM   2605  N   ALA A 338      14.205  24.386  48.368  1.00 24.19
ATOM   2606  CA  ALA A 338      15.379  25.239  48.263  1.00 23.24
ATOM   2607  C   ALA A 338      16.494  24.444  47.576  1.00 21.74
ATOM   2608  O   ALA A 338      17.150  25.014  46.682  1.00 23.09
ATOM   2609  CB  ALA A 338      15.906  25.792  49.564  1.00 20.70
ATOM   2610  N   PHE A 339      16.683  23.241  48.055  1.00 19.84
ATOM   2611  CA  PHE A 339      17.666  22.328  47.454  1.00 18.27
ATOM   2612  C   PHE A 339      17.401  22.246  45.941  1.00 16.85
ATOM   2613  O   PHE A 339      18.367  22.430  45.171  1.00 18.64
ATOM   2614  CB  PHE A 339      17.469  20.940  48.142  1.00 18.85
ATOM   2615  CG  PHE A 339      18.221  19.836  47.385  1.00 20.26
ATOM   2616  CD1 PHE A 339      19.582  19.619  47.576  1.00 19.47
ATOM   2617  CD2 PHE A 339      17.458  19.027  46.477  1.00 18.45
ATOM   2618  CE1 PHE A 339      20.257  18.697  46.782  1.00 17.20
ATOM   2619  CE2 PHE A 339      18.192  18.002  45.816  1.00 19.23
ATOM   2620  CZ  PHE A 339      19.569  17.878  45.945  1.00 17.43
ATOM   2621  N   TRP A 340      16.183  21.910  45.546  1.00 15.64
ATOM   2622  CA  TRP A 340      15.949  21.735  44.090  1.00 19.80
ATOM   2623  C   TRP A 340      16.186  22.962  43.216  1.00 20.80
ATOM   2624  O   TRP A 340      16.697  22.936  42.098  1.00 20.98
ATOM   2625  CB  TRP A 340      14.495  21.162  43.854  1.00 17.62
ATOM   2626  CG  TRP A 340      14.291  19.742  44.201  1.00 15.81
ATOM   2627  CD1 TRP A 340      13.279  19.189  44.932  1.00 14.78
ATOM   2628  CD2 TRP A 340      15.068  18.632  43.651  1.00 18.26
ATOM   2629  NE1 TRP A 340      13.440  17.803  44.912  1.00 17.80
ATOM   2630  CE2 TRP A 340      14.502  17.393  44.179  1.00 16.28
ATOM   2631  CE3 TRP A 340      16.170  18.505  42.762  1.00 17.79
ATOM   2632  CZ2 TRP A 340      14.979  16.167  43.781  1.00 15.58
ATOM   2633  CZ3 TRP A 340      16.668  17.262  42.442  1.00 17.99
ATOM   2634  CH2 TRP A 340      16.122  16.060  42.991  1.00 18.45
ATOM   2635  N   TYR A 341      15.740  24.089  43.762  1.00 22.30
ATOM   2636  CA  TYR A 341      15.927  25.330  42.894  1.00 25.19
ATOM   2637  C   TYR A 341      17.370  25.692  42.838  1.00 21.63
ATOM   2638  O   TYR A 341      17.865  26.038  41.768  1.00 19.50
ATOM   2639  CB  TYR A 341      14.896  26.281  43.356  1.00 35.36
ATOM   2640  CG  TYR A 341      14.871  27.314  44.362  1.00 45.18
ATOM   2641  CD1 TYR A 341      15.594  28.518  44.442  1.00 49.31
ATOM   2642  CD2 TYR A 341      13.886  27.066  45.347  1.00 51.69
ATOM   2643  CE1 TYR A 341      15.417  29.424  45.516  1.00 53.83
ATOM   2644  CE2 TYR A 341      13.678  27.934  46.430  1.00 55.99
ATOM   2645  CZ  TYR A 341      14.456  29.107  46.487  1.00 56.86
ATOM   2646  OH  TYR A 341      14.093  29.844  47.609  1.00 61.27
ATOM   2647  N   ALA A 342      18.100  25.512  43.965  1.00 20.33
ATOM   2648  CA  ALA A 342      19.563  25.805  43.940  1.00 16.66
ATOM   2649  C   ALA A 342      20.297  24.884  43.000  1.00 18.51
ATOM   2650  O   ALA A 342      21.172  25.300  42.165  1.00 16.46
ATOM   2651  CB  ALA A 342      20.120  25.753  45.349  1.00 15.25
ATOM   2652  N   VAL A 343      19.953  23.578  43.026  1.00 17.57
ATOM   2653  CA  VAL A 343      20.668  22.598  42.167  1.00 17.31
ATOM   2654  C   VAL A 343      20.255  22.793  40.710  1.00 16.83
ATOM   2655  O   VAL A 343      21.038  22.608  39.807  1.00 15.53
ATOM   2656  CB  VAL A 343      20.470  21.200  42.822  1.00 18.41
ATOM   2657  CG1 VAL A 343      20.916  20.136  41.843  1.00 20.17
ATOM   2658  CG2 VAL A 343      21.226  21.170  44.160  1.00 18.69
ATOM   2659  N   ARG A 344      19.046  23.217  40.455  1.00 18.04
ATOM   2660  CA  ARG A 344      18.563  23.495  39.101  1.00 21.04
ATOM   2661  C   ARG A 344      19.387  24.631  38.497  1.00 20.30
ATOM   2662  O   ARG A 344      19.953  24.397  37.377  1.00 22.22
ATOM   2663  CB  ARG A 344      17.055  23.780  38.999  1.00 21.05
ATOM   2664  CG  ARG A 344      16.604  23.919  37.501  1.00 26.33
ATOM   2665  CD  ARG A 344      15.266  24.682  37.384  1.00 33.39
ATOM   2666  NE  ARG A 344      14.475  24.564  38.574  1.00 41.20
ATOM   2667  CZ  ARG A 344      13.872  23.412  38.933  1.00 44.60
ATOM   2668  NH1 ARG A 344      13.723  22.447  38.030  1.00 47.84
ATOM   2669  NH2 ARG A 344      13.311  23.204  40.149  1.00 50.39
ATOM   2670  N   THR A 345      19.483  25.723  39.236  1.00 19.84
ATOM   2671  CA  THR A 345      20.359  26.797  38.636  1.00 20.59
ATOM   2672  C   THR A 345      21.767  26.382  38.316  1.00 23.30
ATOM   2673  O   THR A 345      22.303  26.499  37.137  1.00 22.88
ATOM   2674  CB  THR A 345      20.279  27.978  39.708  1.00 20.73
ATOM   2675  OG1 THR A 345      18.891  28.297  39.857  1.00 21.65
ATOM   2676  CG2 THR A 345      21.189  29.142  39.397  1.00 21.30
ATOM   2677  N   ALA A 346      22.398  25.718  39.366  1.00 21.33
ATOM   2678  CA  ALA A 346      23.787  25.284  39.285  1.00 20.71
ATOM   2679  C   ALA A 346      24.077  24.516  38.043  1.00 19.84
ATOM   2680  O   ALA A 346      25.096  24.591  37.351  1.00 23.05
ATOM   2681  CB  ALA A 346      24.257  24.472  40.516  1.00 18.83
ATOM   2682  N   VAL A 347      23.254  23.566  37.693  1.00 22.85
ATOM   2683  CA  VAL A 347      23.544  22.641  36.539  1.00 22.00
ATOM   2684  C   VAL A 347      23.417  23.380  35.178  1.00 23.30
ATOM   2685  O   VAL A 347      24.231  23.104  34.280  1.00 23.48
ATOM   2686  CB  VAL A 347      22.648  21.386  36.603  1.00 22.26
ATOM   2687  CG1 VAL A 347      22.591  20.635  35.267  1.00 23.03
ATOM   2688  CG2 VAL A 347      22.960  20.375  37.731  1.00 18.05
ATOM   2689  N   ILE A 348      22.339  24.167  35.192  1.00 22.71
ATOM   2690  CA  ILE A 348      22.082  24.896  33.927  1.00 25.23
ATOM   2691  C   ILE A 348      23.239  25.872  33.717  1.00 24.58
ATOM   2692  O   ILE A 348      23.804  25.850  32.649  1.00 24.59
ATOM   2693  CB  ILE A 348      20.675  25.483  34.050  1.00 25.22
ATOM   2694  CG1 ILE A 348      19.588  24.485  33.594  1.00 23.57
ATOM   2695  CG2 ILE A 348      20.586  26.820  33.292  1.00 27.98
ATOM   2696  CD1 ILE A 348      18.254  25.174  34.094  1.00 28.81
ATOM   2697  N   ASN A 349      23.564  26.626  34.727  1.00 26.89
ATOM   2698  CA  ASN A 349      24.688  27.604  34.621  1.00 25.49
ATOM   2699  C   ASN A 349      25.976  26.878  34.270  1.00 24.40
ATOM   2700  O   ASN A 349      26.799  27.445  33.541  1.00 24.15
ATOM   2701  CB  ASN A 349      24.773  28.497  35.867  1.00 25.19
ATOM   2702  CG  ASN A 349      23.702  29.503  36.138  1.00 25.07
ATOM   2703  OD1 ASN A 349      22.858  29.843  35.320  1.00 31.75
ATOM   2704  ND2 ASN A 349      23.717  30.062  37.377  1.00 27.28
ATOM   2705  N   ALA A 350      26.266  25.694  34.801  1.00 22.84
ATOM   2706  CA  ALA A 350      27.471  24.994  34.532  1.00 22.87
ATOM   2707  C   ALA A 350      27.422  24.356  33.142  1.00 25.48
ATOM   2708  O   ALA A 350      28.527  24.329  32.461  1.00 25.91
ATOM   2709  CB  ALA A 350      27.832  23.864  35.536  1.00 19.82
ATOM   2710  N   ALA A 351      26.272  23.835  32.764  1.00 25.14
ATOM   2711  CA  ALA A 351      26.210  23.144  31.417  1.00 26.99
ATOM   2712  C   ALA A 351      26.326  24.136  30.244  1.00 27.64
ATOM   2713  O   ALA A 351      26.984  23.909  29.202  1.00 29.35
ATOM   2714  CB  ALA A 351      24.920  22.328  31.361  1.00 27.22
ATOM   2715  N   SER A 352      25.730  25.296  30.445  1.00 29.27
ATOM   2716  CA  SER A 352      25.669  26.460  29.551  1.00 30.40
ATOM   2717  C   SER A 352      27.006  27.206  29.527  1.00 31.95
ATOM   2718  O   SER A 352      27.151  28.066  28.645  1.00 35.02
ATOM   2719  CB  SER A 352      24.485  27.329  29.958  1.00 26.61
ATOM   2720  OG  SER A 352      24.845  28.101  31.104  1.00 30.58
ATOM   2721  N   GLY A 353      27.961  26.932  30.405  1.00 30.84
ATOM   2722  CA  GLY A 353      29.266  27.459  30.548  1.00 29.04
ATOM   2723  C   GLY A 353      29.268  28.848  31.129  1.00 31.84
ATOM   2724  O   GLY A 353      30.413  29.380  31.015  1.00 33.36
ATOM   2725  N   ARG A 354      28.153  29.274  31.755  1.00 30.68
ATOM   2726  CA  ARG A 354      28.007  30.580  32.361  1.00 33.29
ATOM   2727  C   ARG A 354      28.873  30.642  33.652  1.00 35.02
ATOM   2728  O   ARG A 354      29.288  31.748  34.106  1.00 38.74
ATOM   2729  CB  ARG A 354      26.651  31.135  32.730  1.00 31.66
ATOM   2730  CG  ARG A 354      25.479  31.278  31.822  1.00 35.91
ATOM   2731  CD  ARG A 354      24.595  32.491  32.152  1.00 36.12
ATOM   2732  NE  ARG A 354      23.232  32.034  32.132  1.00 41.26
ATOM   2733  CZ  ARG A 354      22.622  31.293  31.186  1.00 42.90
ATOM   2734  NH1 ARG A 354      22.834  30.810  29.969  1.00 40.51
ATOM   2735  NH2 ARG A 354      21.485  30.649  31.647  1.00 45.01
ATOM   2736  N   GLN A 355      29.058  29.487  34.291  1.00 32.88
ATOM   2737  CA  GLN A 355      29.822  29.377  35.518  1.00 28.32
ATOM   2738  C   GLN A 355      30.580  28.048  35.350  1.00 26.91
ATOM   2739  O   GLN A 355      30.151  27.187  34.610  1.00 25.60
ATOM   2740  CB  GLN A 355      28.991  29.277  36.789  1.00 27.33
ATOM   2741  CG  GLN A 355      28.299  30.515  37.289  1.00 27.67
ATOM   2742  CD  GLN A 355      27.496  30.260  38.538  1.00 30.61
ATOM   2743  OE1 GLN A 355      26.484  29.544  38.554  1.00 31.20
ATOM   2744  NE2 GLN A 355      27.887  30.907  39.650  1.00 28.51
ATOM   2745  N   THR A 356      31.662  28.005  36.075  1.00 26.36
ATOM   2746  CA  THR A 356      32.500  26.809  36.200  1.00 26.12
ATOM   2747  C   THR A 356      31.708  25.926  37.222  1.00 24.97
ATOM   2748  O   THR A 356      30.895  26.455  37.991  1.00 24.65
ATOM   2749  CB  THR A 356      33.957  26.965  36.739  1.00 26.48
ATOM   2750  OG1 THR A 356      33.944  27.558  38.085  1.00 25.11
ATOM   2751  CG2 THR A 356      34.885  27.801  35.806  1.00 29.29
ATOM   2752  N   VAL A 357      32.062  24.653  37.202  1.00 25.60
ATOM   2753  CA  VAL A 357      31.501  23.707  38.180  1.00 24.62
ATOM   2754  C   VAL A 357      31.734  24.166  39.593  1.00 24.29
ATOM   2755  O   VAL A 357      30.714  24.229  40.344  1.00 26.92
ATOM   2756  CB  VAL A 357      32.093  22.304  37.884  1.00 24.42
ATOM   2757  CG1 VAL A 357      31.678  21.268  38.931  1.00 22.52
ATOM   2758  CG2 VAL A 357      31.644  22.012  36.448  1.00 24.91
ATOM   2759  N   ASP A 358      32.953  24.484  39.942  1.00 25.19
ATOM   2760  CA  ASP A 358      33.344  24.926  41.334  1.00 27.18
ATOM   2761  C   ASP A 358      32.514  26.130  41.776  1.00 26.89
ATOM   2762  O   ASP A 358      31.905  26.093  42.883  1.00 25.43
ATOM   2763  CB  ASP A 358      34.843  25.101  41.393  1.00 34.51
ATOM   2764  CG  ASP A 358      35.802  23.967  41.224  1.00 39.72
ATOM   2765  OD1 ASP A 358      36.057  23.123  42.114  1.00 47.15
ATOM   2766  OD2 ASP A 358      36.537  23.785  40.200  1.00 49.39
ATOM   2767  N   GLU A 359      32.434  27.152  40.953  1.00 25.66
ATOM   2768  CA  GLU A 359      31.614  28.319  41.176  1.00 25.86
ATOM   2769  C   GLU A 359      30.142  27.927  41.252  1.00 23.65
ATOM   2770  O   GLU A 359      29.452  28.446  42.150  1.00 24.02
ATOM   2771  CB  GLU A 359      31.637  29.360  40.044  1.00 32.11
ATOM   2772  CG  GLU A 359      32.839  30.305  40.004  1.00 38.99
ATOM   2773  CD  GLU A 359      33.205  30.920  38.658  1.00 42.40
ATOM   2774  OE1 GLU A 359      32.254  31.002  37.852  1.00 41.52
ATOM   2775  OE2 GLU A 359      34.387  31.244  38.381  1.00 45.30
ATOM   2776  N   ALA A 360      29.610  27.138  40.378  1.00 20.82
ATOM   2777  CA  ALA A 360      28.185  26.769  40.421  1.00 19.55
ATOM   2778  C   ALA A 360      27.774  26.025  41.702  1.00 17.14
ATOM   2779  O   ALA A 360      26.691  26.412  42.251  1.00 18.13
ATOM   2780  CB  ALA A 360      27.877  25.907  39.169  1.00 18.90
ATOM   2781  N   LEU A 361      28.602  25.101  42.105  1.00 18.86
ATOM   2782  CA  LEU A 361      28.243  24.220  43.260  1.00 18.39
ATOM   2783  C   LEU A 361      28.434  24.944  44.549  1.00 22.29
ATOM   2784  O   LEU A 361      27.709  24.653  45.479  1.00 23.42
ATOM   2785  CB  LEU A 361      28.953  22.871  43.227  1.00 18.88
ATOM   2786  CG  LEU A 361      28.475  22.040  41.972  1.00 19.71
ATOM   2787  CD1 LEU A 361      29.335  20.843  41.840  1.00 17.72
ATOM   2788  CD2 LEU A 361      26.950  21.759  42.071  1.00 14.79
ATOM   2789  N   LYS A 362      29.337  25.906  44.408  1.00 23.80
ATOM   2790  CA  LYS A 362      29.568  26.661  45.693  1.00 23.44
ATOM   2791  C   LYS A 362      28.428  27.564  45.901  1.00 22.81
ATOM   2792  O   LYS A 362      27.987  27.787  47.084  1.00 25.51
ATOM   2793  CB  LYS A 362      30.873  27.335  45.512  1.00 29.64
ATOM   2794  CG  LYS A 362      31.402  27.999  46.763  1.00 37.21
ATOM   2795  CD  LYS A 362      31.527  29.478  46.318  1.00 45.09
ATOM   2796  CE  LYS A 362      30.144  30.127  46.682  1.00 50.12
ATOM   2797  NZ  LYS A 362      30.261  31.646  46.496  1.00 55.02
ATOM   2798  N   ASP A 363      27.921  28.164  44.894  1.00 22.46
ATOM   2799  CA  ASP A 363      26.787  29.099  45.077  1.00 23.70
ATOM   2800  C   ASP A 363      25.553  28.384  45.590  1.00 21.93
ATOM   2801  O   ASP A 363      24.697  28.907  46.258  1.00 22.41
ATOM   2802  CB  ASP A 363      26.390  29.666  43.703  1.00 30.99
ATOM   2803  CG  ASP A 363      27.041  31.019  43.435  1.00 41.33
ATOM   2804  OD1 ASP A 363      28.007  31.449  44.182  1.00 44.85
ATOM   2805  OD2 ASP A 363      26.525  31.627  42.421  1.00 46.02
ATOM   2806  N   ALA A 364      25.470  27.167  45.036  1.00 20.83
ATOM   2807  CA  ALA A 364      24.307  26.334  45.367  1.00 20.13
ATOM   2808  C   ALA A 364      24.311  26.015  46.839  1.00 19.47
ATOM   2809  O   ALA A 364      23.307  26.000  47.581  1.00 19.07
ATOM   2810  CB  ALA A 364      24.253  25.102  44.416  1.00 17.22
ATOM   2811  N   GLN A 365      25.545  25.630  47.270  1.00 20.72
ATOM   2812  CA  GLN A 365      25.793  25.252  48.697  1.00 23.13
ATOM   2813  C   GLN A 365      25.404  26.367  49.621  1.00 23.99
ATOM   2814  O   GLN A 365      24.720  26.209  50.643  1.00 25.68
ATOM   2815  CB  GLN A 365      27.245  24.855  48.775  1.00 27.82
ATOM   2816  CG  GLN A 365      27.764  24.633  50.172  1.00 33.30
ATOM   2817  CD  GLN A 365      27.336  23.322  50.734  1.00 39.43
ATOM   2818  OE1 GLN A 365      26.887  22.383  50.047  1.00 42.04
ATOM   2819  NE2 GLN A 365      27.543  23.272  52.061  1.00 41.78
ATOM   2820  N   THR A 366      25.836  27.614  49.306  1.00 25.64
ATOM   2821  CA  THR A 366      25.506  28.835  50.016  1.00 24.71
ATOM   2822  C   THR A 366      24.047  29.111  50.003  1.00 24.90
ATOM   2823  O   THR A 366      23.480  29.386  51.063  1.00 28.95
ATOM   2824  CB  THR A 366      26.193  30.108  49.303  1.00 26.56
ATOM   2825  OG1 THR A 366      27.536  29.683  49.314  1.00 29.29
ATOM   2826  CG2 THR A 366      25.759  31.337  50.087  1.00 28.25
ATOM   2827  N   ARG A 367      23.435  29.037  48.826  1.00 24.37
ATOM   2828  CA  ARG A 367      22.036  29.255  48.726  1.00 24.44
ATOM   2829  C   ARG A 367      21.287  28.297  49.628  1.00 27.44
ATOM   2830  O   ARG A 367      20.266  28.742  50.263  1.00 29.58
ATOM   2831  CB  ARG A 367      21.594  29.026  47.278  1.00 28.34
ATOM   2832  CG  ARG A 367      22.056  30.239  46.447  1.00 36.19
ATOM   2833  CD  ARG A 367      21.230  30.366  45.229  1.00 43.32
ATOM   2834  NE  ARG A 367      19.791  30.044  45.283  1.00 49.69
ATOM   2835  CZ  ARG A 367      19.145  29.885  44.063  1.00 56.63
ATOM   2836  NH1 ARG A 367      19.863  29.735  42.909  1.00 54.14
ATOM   2837  NH2 ARG A 367      17.777  29.752  43.897  1.00 60.31
ATOM   2838  N   ILE A 368      21.608  27.014  49.638  1.00 24.54
ATOM   2839  CA  ILE A 368      20.863  26.051  50.451  1.00 26.05
ATOM   2840  C   ILE A 368      21.022  26.211  51.945  1.00 25.93
ATOM   2841  O   ILE A 368      20.040  26.039  52.673  1.00 24.75
ATOM   2842  CB  ILE A 368      21.163  24.512  50.072  1.00 25.20
ATOM   2843  CG1 ILE A 368      20.838  24.255  48.583  1.00 21.49
ATOM   2844  CG2 ILE A 368      20.339  23.585  51.067  1.00 23.97
ATOM   2845  CD1 ILE A 368      21.697  23.122  47.907  1.00 22.00
ATOM   2846  N   THR A 369      22.235  26.464  52.387  1.00 29.61
ATOM   2847  CA  THR A 369      22.448  26.552  53.846  1.00 32.75
ATOM   2848  C   THR A 369      22.232  27.917  54.471  1.00 36.83
ATOM   2849  O   THR A 369      22.330  27.894  55.744  1.00 37.14
ATOM   2850  CB  THR A 369      23.892  26.042  54.237  1.00 30.83
ATOM   2851  OG1 THR A 369      24.789  27.010  53.631  1.00 27.79
ATOM   2852  CG2 THR A 369      24.040  24.561  53.813  1.00 31.27
ATOM   2853  N   LYS A 370      21.926  28.945  53.779  1.00 39.60
ATOM   2854  CA  LYS A 370      21.731  30.315  54.234  1.00 44.78
ATOM   2855  C   LYS A 370      20.879  30.604  55.430  1.00 47.81
ATOM   2856  CB  LYS A 370      21.177  31.156  53.033  1.00 49.22
ATOM   2857  CG  LYS A 370      22.370  31.851  52.305  1.00 54.39
ATOM   2858  CD  LYS A 370      21.942  33.223  51.814  1.00 59.84
ATOM   2859  CE  LYS A 370      22.219  34.389  52.766  1.00 64.71
ATOM   2860  NZ  LYS A 370      21.328  35.617  52.564  1.00 67.45
END


A second structure was input as follows:


ATOM      1  N   LYS A   1     -20.828  26.293  49.639  1.00 56.81
ATOM      2  CA  LYS A   1     -19.852  25.381  49.023  1.00 57.02
ATOM      3  C   LYS A   1     -18.680  24.991  49.921  1.00 56.60
ATOM      4  O   LYS A   1     -17.690  25.740  50.118  1.00 57.52
ATOM      5  CB  LYS A   1     -19.373  26.032  47.713  1.00 57.07
ATOM      6  N   ILE A   2     -18.752  23.782  50.476  1.00 54.94
ATOM      7  CA  ILE A   2     -17.735  23.195  51.347  1.00 52.17
ATOM      8  C   ILE A   2     -18.054  21.729  51.663  1.00 50.14
ATOM      9  O   ILE A   2     -18.175  21.296  52.806  1.00 48.68
ATOM     10  CB  ILE A   2     -17.417  24.030  52.569  1.00 52.43
ATOM     11  N   GLU A   3     -18.211  20.994  50.579  1.00 48.65
ATOM     12  CA  GLU A   3     -18.423  19.552  50.497  1.00 47.01
ATOM     13  C   GLU A   3     -19.657  19.032  51.204  1.00 44.31
ATOM     14  O   GLU A   3     -20.749  19.529  50.926  1.00 44.45
ATOM     15  CB  GLU A   3     -17.133  18.920  51.117  1.00 48.31
ATOM     16  N   GLU A   4     -19.459  18.030  52.024  1.00 40.81
ATOM     17  CA  GLU A   4     -20.408  17.397  52.905  1.00 38.78
ATOM     18  C   GLU A   4     -21.314  16.326  52.351  1.00 37.13
ATOM     19  O   GLU A   4     -22.318  16.661  51.704  1.00 37.52
ATOM     20  CB  GLU A   4     -21.238  18.505  53.562  1.00 39.35
ATOM     21  N   GLY A   5     -21.002  15.071  52.625  1.00 35.06
ATOM     22  CA  GLY A   5     -21.777  13.915  52.156  1.00 33.11
ATOM     23  C   GLY A   5     -21.456  13.379  50.767  1.00 30.69
ATOM     24  O   GLY A   5     -22.195  12.549  50.200  1.00 30.13
ATOM     25  N   LYS A   6     -20.365  13.858  50.198  1.00 28.47
ATOM     26  CA  LYS A   6     -19.895  13.409  48.896  1.00 26.55
ATOM     27  C   LYS A   6     -18.387  13.551  48.861  1.00 25.71
ATOM     28  O   LYS A   6     -17.762  13.880  49.878  1.00 25.21
ATOM     29  CB  LYS A   6     -20.579  14.092  47.766  1.00 26.80
ATOM     30  CG  LYS A   6     -20.330  15.573  47.618  1.00 27.86
ATOM     31  CD  LYS A   6     -20.887  16.072  46.297  1.00 31.02
ATOM     32  CE  LYS A   6     -20.660  15.174  45.097  1.00 32.98
ATOM     33  NZ  LYS A   6     -19.284  14.609  45.022  1.00 32.95
ATOM     34  N   LEU A   7     -17.806  13.217  47.727  1.00 24.11
ATOM     35  CA  LEU A   7     -16.334  13.347  47.586  1.00 22.29
ATOM     36  C   LEU A   7     -16.053  14.090  46.291  1.00 21.35
ATOM     37  O   LEU A   7     -16.673  13.907  45.261  1.00 21.91
ATOM     38  CB  LEU A   7     -15.688  11.989  47.731  1.00 20.78
ATOM     39  CG  LEU A   7     -15.416  11.328  49.048  1.00 18.45
ATOM     40  CD1 LEU A   7     -14.939   9.890  48.865  1.00 18.81
ATOM     41  CD2 LEU A   7     -14.348  12.052  49.845  1.00 17.75
ATOM     42  N   VAL A   8     -15.150  15.043  46.373  1.00 21.25
ATOM     43  CA  VAL A   8     -14.683  15.767  45.191  1.00 20.48
ATOM     44  C   VAL A   8     -13.160  15.546  45.204  1.00 19.02
ATOM     45  O   VAL A   8     -12.477  15.601  46.215  1.00 18.19
ATOM     46  CB  VAL A   8     -15.272  17.065  44.796  1.00 22.06
ATOM     47  CG1 VAL A   8     -16.046  17.859  45.824  1.00 24.15
ATOM     48  CG2 VAL A   8     -14.262  17.968  44.082  1.00 21.85
ATOM     49  N   ILE A   9     -12.719  15.124  44.029  1.00 18.66
ATOM     50  CA  ILE A   9     -11.298  14.822  43.799  1.00 17.11
ATOM     51  C   ILE A   9     -10.766  15.646  42.630  1.00 16.86
ATOM     52  O   ILE A   9     -11.488  15.868  41.658  1.00 16.70
ATOM     53  CB  ILE A   9     -11.133  13.301  43.479  1.00 17.88
ATOM     54  CG1 ILE A   9     -11.821  12.466  44.582  1.00 18.31
ATOM     55  CG2 ILE A   9      -9.643  12.948  43.286  1.00 17.04
ATOM     56  CD1 ILE A   9     -11.799  10.947  44.253  1.00 19.61
ATOM     57  N   TRP A  10      -9.535  16.053  42.803  1.00 17.03
ATOM     58  CA  TRP A  10      -8.753  16.827  41.841  1.00 17.32
ATOM     59  C   TRP A  10      -7.511  16.030  41.451  1.00 16.61
ATOM     60  O   TRP A  10      -6.733  15.575  42.292  1.00 17.95
ATOM     61  CB  TRP A  10      -8.356  18.155  42.450  1.00 18.38
ATOM     62  CG  TRP A  10      -9.430  19.185  42.393  1.00 19.67
ATOM     63  CD1 TRP A  10     -10.752  19.031  42.131  1.00 19.53
ATOM     64  CD2 TRP A  10      -9.217  20.582  42.668  1.00 19.64
ATOM     65  NE1 TRP A  10     -11.389  20.233  42.183  1.00 21.28
ATOM     66  CE2 TRP A  10     -10.465  21.209  42.509  1.00 21.17
ATOM     67  CE3 TRP A  10      -8.095  21.332  43.015  1.00 19.18
ATOM     68  CZ2 TRP A  10     -10.620  22.575  42.710  1.00 20.58
ATOM     69  CZ3 TRP A  10      -8.248  22.681  43.225  1.00 20.22
ATOM     70  CH2 TRP A  10      -9.489  23.294  43.068  1.00 20.58
ATOM     71  N   ILE A  11      -7.359  15.873  40.157  1.00 16.81
ATOM     72  CA  ILE A  11      -6.234  15.138  39.568  1.00 15.52
ATOM     73  C   ILE A  11      -5.911  15.837  38.260  1.00 16.75
ATOM     74  O   ILE A  11      -6.815  16.415  37.656  1.00 17.99
ATOM     75  CB  ILE A  11      -6.648  13.622  39.392  1.00 14.80
ATOM     76  CG1 ILE A  11      -5.429  12.776  39.002  1.00 14.29
ATOM     77  CG2 ILE A  11      -7.837  13.411  38.428  1.00 12.82
ATOM     78  CD1 ILE A  11      -5.541  11.244  39.280  1.00 13.21
ATOM     79  N   ASN A  12      -4.686  15.809  37.839  1.00 18.72
ATOM     80  CA  ASN A  12      -4.270  16.436  36.565  1.00 19.92
ATOM     81  C   ASN A  12      -4.921  15.710  35.373  1.00 20.42
ATOM     82  O   ASN A  12      -5.111  14.497  35.384  1.00 18.72
ATOM     83  CB  ASN A  12      -2.744  16.450  36.481  1.00 20.56
ATOM     84  CG  ASN A  12      -2.214  17.610  35.663  1.00 22.28
ATOM     85  OD1 ASN A  12      -2.920  18.586  35.361  1.00 24.84
ATOM     86  ND2 ASN A  12      -0.951  17.533  35.304  1.00 24.20
ATOM     87  N   GLY A  13      -5.199  16.494  34.348  1.00 21.73
ATOM     88  CA  GLY A  13      -5.779  16.081  33.091  1.00 23.78
ATOM     89  C   GLY A  13      -5.010  15.031  32.302  1.00 24.20
ATOM     90  O   GLY A  13      -5.632  14.294  31.500  1.00 25.75
ATOM     91  N   ASP A  14      -3.755  14.875  32.539  1.00 24.92
ATOM     92  CA  ASP A  14      -2.818  13.944  31.909  1.00 26.74
ATOM     93  C   ASP A  14      -2.758  12.573  32.590  1.00 27.18
ATOM     94  O   ASP A  14      -1.863  11.738  32.310  1.00 27.74
ATOM     95  CB  ASP A  14      -1.446  14.613  31.796  1.00 28.05
ATOM     96  CG  ASP A  14      -0.634  14.719  33.056  1.00 30.88
ATOM     97  OD1 ASP A  14      -1.187  14.560  34.167  1.00 32.40
ATOM     98  OD2 ASP A  14       0.594  14.960  33.028  1.00 32.97
ATOM     99  N   LYS A  15      -3.670  12.341  33.507  1.00 26.37
ATOM    100  CA  LYS A  15      -3.807  11.131  34.306  1.00 25.09
ATOM    101  C   LYS A  15      -5.122  10.432  33.976  1.00 23.32
ATOM    102  O   LYS A  15      -5.998  11.006  33.356  1.00 22.97
ATOM    103  CB  LYS A  15      -3.856  11.438  35.816  1.00 26.22
ATOM    104  CG  LYS A  15      -2.789  12.405  36.300  1.00 25.46
ATOM    105  CD  LYS A  15      -1.530  11.715  36.700  1.00 25.02
ATOM    106  CE  LYS A  15      -0.368  12.130  35.831  1.00 27.99
ATOM    107  NZ  LYS A  15       0.795  11.287  36.211  1.00 31.92
ATOM    108  N   GLY A  16      -5.225   9.223  34.473  1.00 22.74
ATOM    109  CA  GLY A  16      -6.395   8.401  34.221  1.00 22.42
ATOM    110  C   GLY A  16      -7.558   8.774  35.115  1.00 22.81
ATOM    111  O   GLY A  16      -7.972   7.941  35.934  1.00 22.76
ATOM    112  N   TYR A  17      -8.062   9.973  34.909  1.00 22.81
ATOM    113  CA  TYR A  17      -9.218  10.437  35.699  1.00 23.16
ATOM    114  C   TYR A  17     -10.526   9.784  35.318  1.00 23.48
ATOM    115  O   TYR A  17     -11.551   9.925  36.020  1.00 23.84
ATOM    116  CB  TYR A  17      -9.249  11.955  35.617  1.00 23.34
ATOM    117  CG  TYR A  17      -9.383  12.493  34.219  1.00 23.32
ATOM    118  CD1 TYR A  17     -10.645  12.570  33.669  1.00 23.63
ATOM    119  CD2 TYR A  17      -8.302  12.937  33.469  1.00 23.65
ATOM    120  CE1 TYR A  17     -10.837  13.061  32.389  1.00 25.13
ATOM    121  CE2 TYR A  17      -8.469  13.467  32.198  1.00 24.05
ATOM    122  CZ  TYR A  17      -9.744  13.507  31.660  1.00 25.35
ATOM    123  OH  TYR A  17     -10.034  14.005  30.415  1.00 27.46
ATOM    124  N   ASN A  18     -10.572   9.076  34.198  1.00 23.47
ATOM    125  CA  ASN A  18     -11.778   8.368  33.736  1.00 22.16
ATOM    126  C   ASN A  18     -11.788   7.033  34.487  1.00 21.54
ATOM    127  O   ASN A  18     -12.854   6.519  34.835  1.00 22.57
ATOM    128  CB  ASN A  18     -11.861   8.214  32.235  1.00 23.69
ATOM    129  CG  ASN A  18     -12.191   9.495  31.520  1.00 25.61
ATOM    130  OD1 ASN A  18     -11.489   9.952  30.608  1.00 27.94
ATOM    131  ND2 ASN A  18     -13.278  10.110  31.987  1.00 28.44
ATOM    132  N   GLY A  19     -10.613   6.516  34.684  1.00 20.85
ATOM    133  CA  GLY A  19     -10.453   5.235  35.425  1.00 20.66
ATOM    134  C   GLY A  19     -10.734   5.518  36.900  1.00 21.38
ATOM    135  O   GLY A  19     -11.322   4.687  37.602  1.00 22.22
ATOM    136  N   LEU A  20     -10.251   6.671  37.359  1.00 21.27
ATOM    137  CA  LEU A  20     -10.496   7.060  38.758  1.00 21.30
ATOM    138  C   LEU A  20     -12.002   7.294  38.954  1.00 21.47
ATOM    139  O   LEU A  20     -12.505   6.891  40.025  1.00 22.74
ATOM    140  CB  LEU A  20      -9.577   8.200  39.172  1.00 19.91
ATOM    141  CG  LEU A  20      -9.672   8.570  40.664  1.00 18.70
ATOM    142  CD1 LEU A  20      -9.209   7.421  41.526  1.00 17.68
ATOM    143  CD2 LEU A  20      -8.887   9.845  40.872  1.00 18.90
ATOM    144  N   ALA A  21     -12.694   7.890  38.005  1.00 21.25
ATOM    145  CA  ALA A  21     -14.127   8.107  38.036  1.00 22.73
ATOM    146  C   ALA A  21     -14.871   6.765  38.073  1.00 24.89
ATOM    147  O   ALA A  21     -16.011   6.770  38.559  1.00 26.80
ATOM    148  CB  ALA A  21     -14.648   8.934  36.879  1.00 21.24
ATOM    149  N   GLU A  22     -14.309   5.687  37.587  1.00 25.46
ATOM    150  CA  GLU A  22     -14.841   4.344  37.573  1.00 26.32
ATOM    151  C   GLU A  22     -14.711   3.628  38.912  1.00 25.87
ATOM    152  O   GLU A  22     -15.506   2.722  39.257  1.00 25.29
ATOM    153  CB  GLU A  22     -14.129   3.438  36.544  1.00 29.83
ATOM    154  CG  GLU A  22     -14.557   3.657  35.083  1.00 34.89
ATOM    155  CD  GLU A  22     -16.006   3.335  34.822  1.00 37.82
ATOM    156  OE1 GLU A  22     -16.137   2.090  34.752  1.00 40.28
ATOM    157  OE2 GLU A  22     -16.909   4.151  34.726  1.00 39.64
ATOM    158  N   VAL A  23     -13.679   3.992  39.669  1.00 23.94
ATOM    159  CA  VAL A  23     -13.476   3.425  41.011  1.00 22.02
ATOM    160  C   VAL A  23     -14.555   4.076  41.902  1.00 22.46
ATOM    161  O   VAL A  23     -15.083   3.465  42.827  1.00 22.30
ATOM    162  CB  VAL A  23     -12.072   3.649  41.536  1.00 20.89
ATOM    163  CG1 VAL A  23     -11.904   3.169  42.960  1.00 19.19
ATOM    164  CG2 VAL A  23     -11.060   2.920  40.634  1.00 21.79
ATOM    165  N   GLY A  24     -14.837   5.298  41.546  1.00 22.72
ATOM    166  CA  GLY A  24     -15.812   6.147  42.192  1.00 24.83
ATOM    167  C   GLY A  24     -17.248   5.676  42.044  1.00 26.20
ATOM    168  O   GLY A  24     -18.054   5.881  42.954  1.00 25.15
ATOM    169  N   LYS A  25     -17.570   5.092  40.898  1.00 27.54
ATOM    170  CA  LYS A  25     -18.908   4.576  40.607  1.00 29.31
ATOM    171  C   LYS A  25     -19.128   3.336  41.454  1.00 28.97
ATOM    172  O   LYS A  25     -20.202   3.103  42.037  1.00 29.82
ATOM    173  CB  LYS A  25     -19.165   4.405  39.122  1.00 32.02
ATOM    174  CG  LYS A  25     -20.590   3.858  38.826  1.00 36.78
ATOM    175  CD  LYS A  25     -21.676   4.852  39.244  1.00 38.24
ATOM    176  CE  LYS A  25     -22.921   4.241  39.838  1.00 37.20
ATOM    177  NZ  LYS A  25     -22.589   3.291  40.927  1.00 36.59
ATOM    178  N   LYS A  26     -18.102   2.546  41.585  1.00 28.68
ATOM    179  CA  LYS A  26     -18.063   1.347  42.421  1.00 29.88
ATOM    180  C   LYS A  26     -18.250   1.749  43.885  1.00 31.25
ATOM    181  O   LYS A  26     -18.954   1.060  44.665  1.00 32.91
ATOM    182  CB  LYS A  26     -16.779   0.608  42.215  1.00 30.20
ATOM    183  CG  LYS A  26     -16.259  -0.361  43.235  1.00 33.13
ATOM    184  CD  LYS A  26     -17.180  -1.490  43.613  1.00 36.34
ATOM    185  CE  LYS A  26     -16.490  -2.797  43.926  1.00 37.97
ATOM    186  NZ  LYS A  26     -16.346  -3.061  45.386  1.00 39.59
ATOM    187  N   PHE A  27     -17.623   2.856  44.299  1.00 30.47
ATOM    188  CA  PHE A  27     -17.741   3.331  45.688  1.00 28.50
ATOM    189  C   PHE A  27     -19.190   3.777  45.917  1.00 28.75
ATOM    190  O   PHE A  27     -19.764   3.425  46.959  1.00 28.79
ATOM    191  CB  PHE A  27     -16.742   4.401  46.057  1.00 25.98
ATOM    192  CG  PHE A  27     -16.717   4.947  47.457  1.00 22.90
ATOM    193  CD1 PHE A  27     -16.102   4.239  48.482  1.00 20.15
ATOM    194  CD2 PHE A  27     -17.277   6.208  47.724  1.00 21.50
ATOM    195  CE1 PHE A  27     -16.041   4.727  49.782  1.00 18.40
ATOM    196  CE2 PHE A  27     -17.218   6.726  49.011  1.00 20.03
ATOM    197  CZ  PHE A  27     -16.615   5.982  50.022  1.00 18.01
ATOM    198  N   GLU A  28     -19.732   4.511  44.998  1.00 29.58
ATOM    199  CA  GLU A  28     -21.089   5.040  45.061  1.00 32.41
ATOM    200  C   GLU A  28     -22.133   3.929  45.098  1.00 34.42
ATOM    201  O   GLU A  28     -23.273   4.157  45.505  1.00 34.56
ATOM    202  CB  GLU A  28     -21.404   5.988  43.943  1.00 31.57
ATOM    203  CG  GLU A  28     -22.790   6.330  43.508  1.00 33.54
ATOM    204  CD  GLU A  28     -22.928   7.498  42.583  1.00 36.49
ATOM    205  OE1 GLU A  28     -21.942   7.683  41.841  1.00 37.19
ATOM    206  OE2 GLU A  28     -23.885   8.262  42.523  1.00 39.08
ATOM    207  N   LYS A  29     -21.724   2.749  44.684  1.00 36.98
ATOM    208  CA  LYS A  29     -22.565   1.551  44.629  1.00 38.62
ATOM    209  C   LYS A  29     -22.764   0.936  46.002  1.00 38.12
ATOM    210  O   LYS A  29     -23.921   0.624  46.371  1.00 38.99
ATOM    211  CB  LYS A  29     -21.967   0.480  43.704  1.00 41.39
ATOM    212  CG  LYS A  29     -22.892   0.070  42.556  1.00 44.19
ATOM    213  CD  LYS A  29     -22.088  -0.143  41.273  1.00 47.51
ATOM    214  CE  LYS A  29     -22.862   0.228  40.022  1.00 49.62
ATOM    215  NZ  LYS A  29     -23.657  -0.920  39.483  1.00 50.86
ATOM    216  N   ASP A  30     -21.680   0.753  46.736  1.00 36.99
ATOM    217  CA  ASP A  30     -21.797   0.147  48.068  1.00 37.15
ATOM    218  C   ASP A  30     -21.922   1.204  49.170  1.00 37.07
ATOM    219  O   ASP A  30     -21.824   0.802  50.350  1.00 38.75
ATOM    220  CB  ASP A  30     -20.633  -0.784  48.386  1.00 37.18
ATOM    221  CG  ASP A  30     -19.768  -1.187  47.229  1.00 36.17
ATOM    222  OD1 ASP A  30     -20.247  -1.234  46.098  1.00 37.27
ATOM    223  OD2 ASP A  30     -18.585  -1.470  47.518  1.00 35.82
ATOM    224  N   THR A  31     -22.123   2.453  48.808  1.00 36.02
ATOM    225  CA  THR A  31     -22.175   3.520  49.826  1.00 34.45
ATOM    226  C   THR A  31     -23.267   4.520  49.595  1.00 33.84
ATOM    227  O   THR A  31     -23.893   5.018  50.569  1.00 35.75
ATOM    228  CB  THR A  31     -20.716   4.195  49.885  1.00 33.09
ATOM    229  OG1 THR A  31     -19.869   3.205  50.554  1.00 31.71
ATOM    230  CG2 THR A  31     -20.652   5.532  50.550  1.00 31.90
ATOM    231  N   GLY A  32     -23.516   4.858  48.362  1.00 32.51
ATOM    232  CA  GLY A  32     -24.519   5.843  47.968  1.00 32.46
ATOM    233  C   GLY A  32     -23.910   7.231  47.868  1.00 32.55
ATOM    234  O   GLY A  32     -24.554   8.204  47.463  1.00 32.42
ATOM    235  N   ILE A  33     -22.636   7.278  48.278  1.00 33.39
ATOM    236  CA  ILE A  33     -21.873   8.532  48.246  1.00 32.26
ATOM    237  C   ILE A  33     -21.319   8.702  46.817  1.00 31.42
ATOM    238  O   ILE A  33     -20.616   7.805  46.344  1.00 30.22
ATOM    239  CB  ILE A  33     -20.744   8.546  49.324  1.00 32.63
ATOM    240  CG1 ILE A  33     -21.363   8.520  50.746  1.00 32.86
ATOM    241  CG2 ILE A  33     -19.780   9.747  49.147  1.00 32.23
ATOM    242  CD1 ILE A  33     -22.356   9.655  51.070  1.00 33.46
ATOM    243  N   LYS A  34     -21.684   9.823  46.251  1.00 30.65
ATOM    244  CA  LYS A  34     -21.245  10.208  44.920  1.00 32.14
ATOM    245  C   LYS A  34     -19.831  10.788  45.000  1.00 31.72
ATOM    246  O   LYS A  34     -19.556  11.621  45.893  1.00 32.45
ATOM    247  CB  LYS A  34     -22.143  11.293  44.329  1.00 34.72
ATOM    248  CG  LYS A  34     -22.706  12.233  45.400  1.00 39.86
ATOM    249  CD  LYS A  34     -23.720  13.190  44.780  1.00 44.39
ATOM    250  CE  LYS A  34     -24.892  13.491  45.712  1.00 47.08
ATOM    251  NZ  LYS A  34     -26.166  13.613  44.910  1.00 49.25
ATOM    252  N   VAL A  35     -18.985  10.362  44.091  1.00 30.33
ATOM    253  CA  VAL A  35     -17.586  10.841  43.977  1.00 28.49
ATOM    254  C   VAL A  35     -17.570  11.728  42.734  1.00 28.33
ATOM    255  O   VAL A  35     -18.322  11.419  41.807  1.00 30.32
ATOM    256  CB  VAL A  35     -16.587   9.686  43.975  1.00 27.11
ATOM    257  CG1 VAL A  35     -15.142  10.120  43.798  1.00 25.37
ATOM    258  CG2 VAL A  35     -16.711   8.818  45.219  1.00 25.98
ATOM    259  N   THR A  36     -16.866  12.814  42.726  1.00 28.12
ATOM    260  CA  THR A  36     -16.748  13.747  41.624  1.00 27.76
ATOM    261  C   THR A  36     -15.282  13.962  41.287  1.00 26.79
ATOM    262  O   THR A  36     -14.520  14.449  42.148  1.00 27.30
ATOM    263  CB  THR A  36     -17.393  15.156  41.948  1.00 28.80
ATOM    264  OG1 THR A  36     -18.703  14.843  42.526  1.00 31.82
ATOM    265  CG2 THR A  36     -17.494  16.079  40.742  1.00 29.32
ATOM    266  N   VAL A  37     -14.928  13.603  40.071  1.00 25.57
ATOM    267  CA  VAL A  37     -13.526  13.777  39.642  1.00 24.48
ATOM    268  C   VAL A  37     -13.495  14.962  38.683  1.00 24.44
ATOM    269  O   VAL A  37     -14.325  15.104  37.796  1.00 24.50
ATOM    270  CB  VAL A  37     -12.886  12.514  39.064  1.00 23.84
ATOM    271  CG1 VAL A  37     -11.431  12.802  38.672  1.00 23.67
ATOM    272  CG2 VAL A  37     -12.927  11.287  39.953  1.00 22.67
ATOM    273  N   GLU A  38     -12.523  15.806  38.917  1.00 25.96
ATOM    274  CA  GLU A  38     -12.285  16.997  38.090  1.00 26.85
ATOM    275  C   GLU A  38     -10.777  17.138  37.900  1.00 26.29
ATOM    276  O   GLU A  38     -10.014  16.576  38.683  1.00 25.12
ATOM    277  CB  GLU A  38     -12.870  18.251  38.673  1.00 29.22
ATOM    278  CG  GLU A  38     -13.577  18.133  40.010  1.00 34.00
ATOM    279  CD  GLU A  38     -14.622  19.142  40.347  1.00 37.52
ATOM    280  OE1 GLU A  38     -15.381  19.439  39.393  1.00 39.95
ATOM    281  OE2 GLU A  38     -14.728  19.613  41.470  1.00 39.62
ATOM    282  N   HIS A  39     -10.443  17.851  36.852  1.00 26.46
ATOM    283  CA  HIS A  39      -9.026  18.082  36.504  1.00 28.40
ATOM    284  C   HIS A  39      -8.842  19.524  36.051  1.00 29.85
ATOM    285  O   HIS A  39      -8.591  19.776  34.855  1.00 30.75
ATOM    286  CB  HIS A  39      -8.553  17.073  35.433  1.00 27.69
ATOM    287  CG  HIS A  39      -9.537  16.926  34.307  1.00 27.20
ATOM    288  ND1 HIS A  39      -9.383  17.492  33.078  1.00 27.08
ATOM    289  CD2 HIS A  39     -10.724  16.284  34.277  1.00 26.65
ATOM    290  CE1 HIS A  39     -10.423  17.202  32.321  1.00 26.84
ATOM    291  NE2 HIS A  39     -11.249  16.486  33.049  1.00 27.56
ATOM    292  N   PRO A  40      -8.968  20.454  36.991  1.00 30.72
ATOM    293  CA  PRO A  40      -8.844  21.886  36.703  1.00 31.77
ATOM    294  C   PRO A  40      -7.429  22.248  36.308  1.00 33.01
ATOM    295  O   PRO A  40      -6.458  21.583  36.651  1.00 32.47
ATOM    296  CB  PRO A  40      -9.352  22.568  37.971  1.00 31.40
ATOM    297  CG  PRO A  40      -9.040  21.588  39.064  1.00 30.44
ATOM    298  CD  PRO A  40      -9.235  20.233  38.419  1.00 30.66
ATOM    299  N   ASP A  41      -7.353  23.350  35.588  1.00 35.82
ATOM    300  CA  ASP A  41      -6.114  23.934  35.066  1.00 38.09
ATOM    301  C   ASP A  41      -5.270  24.444  36.232  1.00 37.66
ATOM    302  O   ASP A  41      -5.850  25.129  37.097  1.00 37.78
ATOM    303  CB  ASP A  41      -6.467  25.095  34.094  1.00 41.23
ATOM    304  CG  ASP A  41      -5.778  24.914  32.746  1.00 43.71
ATOM    305  OD1 ASP A  41      -4.556  25.175  32.631  1.00 44.20
ATOM    306  OD2 ASP A  41      -6.500  24.484  31.822  1.00 46.24
ATOM    307  N   LYS A  42      -3.991  24.155  36.186  1.00 36.80
ATOM    308  CA  LYS A  42      -3.033  24.579  37.226  1.00 35.88
ATOM    309  C   LYS A  42      -3.646  24.329  38.609  1.00 34.26
ATOM    310  O   LYS A  42      -3.611  25.244  39.436  1.00 34.24
ATOM    311  CB  LYS A  42      -2.666  26.051  37.133  1.00 36.01
ATOM    312  CG  LYS A  42      -2.163  26.617  35.828  1.00 37.86
ATOM    313  CD  LYS A  42      -1.216  25.724  35.062  1.00 39.47
ATOM    314  CE  LYS A  42       0.248  25.934  35.370  1.00 41.22
ATOM    315  NZ  LYS A  42       0.854  26.876  34.379  1.00 41.72
ATOM    316  N   LEU A  43      -4.187  23.140  38.804  1.00 31.86
ATOM    317  CA  LEU A  43      -4.870  22.814  40.070  1.00 29.59
ATOM    318  C   LEU A  43      -3.918  22.882  41.254  1.00 28.14
ATOM    319  O   LEU A  43      -4.386  23.090  42.401  1.00 28.24
ATOM    320  CB  LEU A  43      -5.641  21.485  39.903  1.00 27.54
ATOM    321  CG  LEU A  43      -4.776  20.226  39.818  1.00 25.53
ATOM    322  CD1 LEU A  43      -4.334  19.710  41.168  1.00 23.34
ATOM    323  CD2 LEU A  43      -5.550  19.155  39.076  1.00 24.55
ATOM    324  N   GLU A  44      -2.631  22.696  41.002  1.00 26.46
ATOM    325  CA  GLU A  44      -1.634  22.713  42.091  1.00 25.30
ATOM    326  C   GLU A  44      -1.369  24.153  42.543  1.00 24.95
ATOM    327  O   GLU A  44      -0.802  24.397  43.607  1.00 23.99
ATOM    328  CB  GLU A  44      -0.343  22.044  41.715  1.00 24.76
ATOM    329  CG  GLU A  44       0.602  22.814  40.809  1.00 25.54
ATOM    330  CD  GLU A  44       0.245  22.979  39.375  1.00 25.17
ATOM    331  OE1 GLU A  44      -0.945  22.801  39.057  1.00 26.33
ATOM    332  OE2 GLU A  44       1.091  23.227  38.541  1.00 26.29
ATOM    333  N   GLU A  45      -1.803  25.090  41.729  1.00 25.25
ATOM    334  CA  GLU A  45      -1.690  26.526  42.015  1.00 26.44
ATOM    335  C   GLU A  45      -2.988  26.976  42.686  1.00 25.54
ATOM    336  O   GLU A  45      -2.975  27.763  43.633  1.00 25.39
ATOM    337  CB  GLU A  45      -1.505  27.372  40.767  1.00 28.86
ATOM    338  CG  GLU A  45      -0.164  28.018  40.524  1.00 34.28
ATOM    339  CD  GLU A  45       1.052  27.163  40.635  1.00 38.38
ATOM    340  OE1 GLU A  45       1.438  26.933  41.800  1.00 38.83
ATOM    341  OE2 GLU A  45       1.660  26.732  39.653  1.00 43.01
ATOM    342  N   LYS A  46      -4.069  26.444  42.153  1.00 24.20
ATOM    343  CA  LYS A  46      -5.394  26.726  42.640  1.00 24.74
ATOM    344  C   LYS A  46      -5.643  26.120  44.010  1.00 24.31
ATOM    345  O   LYS A  46      -6.395  26.755  44.770  1.00 25.04
ATOM    346  CB  LYS A  46      -6.497  26.247  41.710  1.00 27.22
ATOM    347  CG  LYS A  46      -6.695  27.172  40.501  1.00 32.06
ATOM    348  CD  LYS A  46      -7.516  26.508  39.418  1.00 35.02
ATOM    349  CE  LYS A  46      -7.802  27.423  38.234  1.00 37.03
ATOM    350  NZ  LYS A  46      -6.609  28.215  37.852  1.00 38.04
ATOM    351  N   PHE A  47      -5.107  24.958  44.296  1.00 22.73
ATOM    352  CA  PHE A  47      -5.309  24.284  45.561  1.00 21.62
ATOM    353  C   PHE A  47      -5.014  25.216  46.753  1.00 22.32
ATOM    354  O   PHE A  47      -5.867  25.429  47.616  1.00 22.53
ATOM    355  CB  PHE A  47      -4.591  22.941  45.742  1.00 19.25
ATOM    356  CG  PHE A  47      -4.898  22.216  47.040  1.00 18.20
ATOM    357  CD1 PHE A  47      -6.149  21.628  47.267  1.00 16.60
ATOM    358  CD2 PHE A  47      -3.938  22.106  48.040  1.00 16.08
ATOM    359  CE1 PHE A  47      -6.409  20.956  48.461  1.00 16.25
ATOM    360  CE2 PHE A  47      -4.189  21.466  49.242  1.00 16.95
ATOM    361  CZ  PHE A  47      -5.438  20.886  49.460  1.00 15.37
ATOM    362  N   PRO A  48      -3.787  25.688  46.840  1.00 23.24
ATOM    363  CA  PRO A  48      -3.378  26.533  47.968  1.00 23.85
ATOM    364  C   PRO A  48      -4.295  27.702  48.201  1.00 24.74
ATOM    365  O   PRO A  48      -4.565  28.058  49.381  1.00 25.29
ATOM    366  CB  PRO A  48      -1.909  26.807  47.747  1.00 24.41
ATOM    367  CG  PRO A  48      -1.491  26.063  46.516  1.00 24.54
ATOM    368  CD  PRO A  48      -2.710  25.487  45.866  1.00 22.26
ATOM    369  N   GLN A  49      -4.860  28.287  47.184  1.00 25.21
ATOM    370  CA  GLN A  49      -5.764  29.408  47.225  1.00 26.43
ATOM    371  C   GLN A  49      -7.123  29.047  47.827  1.00 25.73
ATOM    372  O   GLN A  49      -7.567  29.766  48.741  1.00 26.93
ATOM    373  CB  GLN A  49      -6.036  30.058  45.871  1.00 30.09
ATOM    374  CG  GLN A  49      -5.069  31.136  45.495  1.00 37.69
ATOM    375  CD  GLN A  49      -3.943  30.752  44.568  1.00 41.73
ATOM    376  OE1 GLN A  49      -2.833  30.414  45.022  1.00 43.63
ATOM    377  NE2 GLN A  49      -4.264  30.836  43.258  1.00 42.64
ATOM    378  N   VAL A  50      -7.788  28.068  47.270  1.00 23.70
ATOM    379  CA  VAL A  50      -9.100  27.653  47.742  1.00 21.98
ATOM    380  C   VAL A  50      -9.033  26.952  49.074  1.00 21.22
ATOM    381  O   VAL A  50     -10.011  27.115  49.837  1.00 21.47
ATOM    382  CB  VAL A  50      -9.891  26.894  46.656  1.00 21.44
ATOM    383  CG1 VAL A  50     -10.072  27.710  45.384  1.00 22.19
ATOM    384  CG2 VAL A  50      -9.270  25.546  46.320  1.00 22.28
ATOM    385  N   ALA A  51      -8.021  26.174  49.369  1.00 20.96
ATOM    386  CA  ALA A  51      -7.899  25.442  50.618  1.00 21.83
ATOM    387  C   ALA A  51      -7.666  26.427  51.785  1.00 23.44
ATOM    388  O   ALA A  51      -8.181  26.148  52.879  1.00 24.21
ATOM    389  CB  ALA A  51      -6.854  24.345  50.634  1.00 18.68
ATOM    390  N   ALA A  52      -6.903  27.490  51.517  1.00 24.37
ATOM    391  CA  ALA A  52      -6.619  28.517  52.521  1.00 25.44
ATOM    392  C   ALA A  52      -7.919  29.162  53.027  1.00 26.20
ATOM    393  O   ALA A  52      -7.979  29.722  54.133  1.00 26.69
ATOM    394  CB  ALA A  52      -5.641  29.562  51.988  1.00 25.38
ATOM    395  N   THR A  53      -8.991  29.077  52.252  1.00 27.22
ATOM    396  CA  THR A  53     -10.284  29.619  52.610  1.00 27.91
ATOM    397  C   THR A  53     -11.315  28.542  52.975  1.00 27.95
ATOM    398  O   THR A  53     -12.517  28.843  52.993  1.00 28.42
ATOM    399  CB  THR A  53     -10.858  30.654  51.579  1.00 28.01
ATOM    400  OG1 THR A  53     -11.602  29.934  50.556  1.00 29.68
ATOM    401  CG2 THR A  53      -9.809  31.599  50.983  1.00 27.99
ATOM    402  N   GLY A  54     -10.852  27.345  53.253  1.00 27.95
ATOM    403  CA  GLY A  54     -11.629  26.176  53.601  1.00 27.32
ATOM    404  C   GLY A  54     -12.509  25.682  52.465  1.00 27.87
ATOM    405  O   GLY A  54     -13.630  25.170  52.646  1.00 28.48
ATOM    406  N   ASP A  55     -12.027  25.829  51.249  1.00 27.91
ATOM    407  CA  ASP A  55     -12.707  25.376  50.038  1.00 28.08
ATOM    408  C   ASP A  55     -11.785  24.333  49.363  1.00 26.74
ATOM    409  O   ASP A  55     -10.792  23.891  49.954  1.00 25.62
ATOM    410  CB  ASP A  55     -13.114  26.560  49.169  1.00 31.13
ATOM    411  CG  ASP A  55     -14.492  27.092  49.522  1.00 35.48
ATOM    412  OD1 ASP A  55     -15.192  26.352  50.254  1.00 37.40
ATOM    413  OD2 ASP A  55     -14.932  28.199  49.140  1.00 37.79
ATOM    414  N   GLY A  56     -12.165  23.984  48.152  1.00 25.46
ATOM    415  CA  GLY A  56     -11.427  23.019  47.323  1.00 24.66
ATOM    416  C   GLY A  56     -12.019  21.606  47.407  1.00 22.69
ATOM    417  O   GLY A  56     -13.153  21.426  47.896  1.00 23.58
ATOM    418  N   PRO A  57     -11.243  20.651  46.897  1.00 20.29
ATOM    419  CA  PRO A  57     -11.647  19.246  46.864  1.00 16.41
ATOM    420  C   PRO A  57     -11.305  18.587  48.173  1.00 14.29
ATOM    421  O   PRO A  57     -10.447  19.101  48.907  1.00 13.73
ATOM    422  CB  PRO A  57     -10.755  18.725  45.700  1.00 15.86
ATOM    423  CG  PRO A  57      -9.446  19.412  45.953  1.00 15.73
ATOM    424  CD  PRO A  57      -9.885  20.833  46.306  1.00 19.16
ATOM    425  N   ASP A  58     -11.908  17.462  48.444  1.00 12.04
ATOM    426  CA  ASP A  58     -11.675  16.634  49.604  1.00 13.38
ATOM    427  C   ASP A  58     -10.299  15.990  49.513  1.00 13.03
ATOM    428  O   ASP A  58      -9.544  15.801  50.476  1.00 13.17
ATOM    429  CB  ASP A  58     -12.762  15.526  49.698  1.00 15.11
ATOM    430  CG  ASP A  58     -14.122  16.115  49.993  1.00 16.59
ATOM    431  OD1 ASP A  58     -14.271  16.438  51.204  1.00 19.08
ATOM    432  OD2 ASP A  58     -14.917  16.266  49.065  1.00 17.09
ATOM    433  N   ILE A  59     -10.032  15.648  48.230  1.00 14.82
ATOM    434  CA  ILE A  59      -8.747  14.980  47.932  1.00 15.10
ATOM    435  C   ILE A  59      -8.097  15.513  46.683  1.00 14.13
ATOM    436  O   ILE A  59      -8.729  15.855  45.702  1.00 15.25
ATOM    437  CB  ILE A  59      -8.853  13.439  48.106  1.00 17.81
ATOM    438  CG1 ILE A  59      -8.298  12.705  46.848  1.00 18.86
ATOM    439  CG2 ILE A  59     -10.167  12.843  48.614  1.00 16.16
ATOM    440  CD1 ILE A  59      -6.955  12.028  47.217  1.00 20.85
ATOM    441  N   ILE A  60      -6.784  15.608  46.767  1.00 14.27
ATOM    442  CA  ILE A  60      -5.936  16.138  45.693  1.00 13.49
ATOM    443  C   ILE A  60      -4.836  15.148  45.352  1.00 12.23
ATOM    444  O   ILE A  60      -4.202  14.599  46.241  1.00 12.11
ATOM    445  CB  ILE A  60      -5.332  17.527  46.144  1.00 15.55
ATOM    446  CG1 ILE A  60      -4.368  18.101  45.050  1.00 14.36
ATOM    447  CG2 ILE A  60      -4.560  17.497  47.489  1.00 14.79
ATOM    448  CD1 ILE A  60      -5.182  19.082  44.165  1.00 18.68
ATOM    449  N   PHE A  61      -4.570  15.008  44.054  1.00 12.01
ATOM    450  CA  PHE A  61      -3.493  14.095  43.602  1.00 11.22
ATOM    451  C   PHE A  61      -2.379  14.977  42.998  1.00  8.85
ATOM    452  O   PHE A  61      -2.750  15.797  42.172  1.00 10.85
ATOM    453  CB  PHE A  61      -4.025  13.175  42.477  1.00 10.53
ATOM    454  CG  PHE A  61      -4.813  12.002  42.972  1.00 12.71
ATOM    455  CD1 PHE A  61      -6.168  12.138  43.262  1.00 13.92
ATOM    456  CD2 PHE A  61      -4.190  10.769  43.126  1.00 12.40
ATOM    457  CE1 PHE A  61      -6.896  11.027  43.719  1.00 14.76
ATOM    458  CE2 PHE A  61      -4.904   9.664  43.560  1.00 13.22
ATOM    459  CZ  PHE A  61      -6.253   9.795  43.855  1.00 12.91
ATOM    460  N   TRP A  62      -1.192  14.804  43.409  1.00  9.99
ATOM    461  CA  TRP A  62      -0.020  15.543  42.840  1.00 10.38
ATOM    462  C   TRP A  62       1.216  14.847  43.285  1.00  9.86
ATOM    463  O   TRP A  62       1.252  14.035  44.227  1.00 10.43
ATOM    464  CB  TRP A  62      -0.076  17.048  43.162  1.00 10.76
ATOM    465  CG  TRP A  62       0.709  17.851  42.171  1.00 14.47
ATOM    466  CD1 TRP A  62       2.010  18.294  42.282  1.00 15.37
ATOM    467  CD2 TRP A  62       0.246  18.305  40.886  1.00 14.45
ATOM    468  NE1 TRP A  62       2.391  18.985  41.141  1.00 15.36
ATOM    469  CE2 TRP A  62       1.324  19.019  40.288  1.00 15.60
ATOM    470  CE3 TRP A  62      -0.954  18.183  40.204  1.00 15.53
ATOM    471  CZ2 TRP A  62       1.205  19.582  39.021  1.00 14.99
ATOM    472  CZ3 TRP A  62      -1.096  18.772  38.953  1.00 15.58
ATOM    473  CH2 TRP A  62      -0.017  19.443  38.368  1.00 15.84
ATOM    474  N   ALA A  63       2.332  15.150  42.602  1.00 11.31
ATOM    475  CA  ALA A  63       3.638  14.634  42.989  1.00 11.16
ATOM    476  C   ALA A  63       3.855  15.090  44.456  1.00 11.79
ATOM    477  O   ALA A  63       3.505  16.234  44.792  1.00 11.50
ATOM    478  CB  ALA A  63       4.718  15.265  42.104  1.00 13.27
ATOM    479  N   HIS A  64       4.494  14.278  45.240  1.00 12.29
ATOM    480  CA  HIS A  64       4.761  14.479  46.644  1.00 12.96
ATOM    481  C   HIS A  64       5.513  15.757  47.014  1.00 15.58
ATOM    482  O   HIS A  64       5.320  16.288  48.130  1.00 15.35
ATOM    483  CB  HIS A  64       5.521  13.303  47.303  1.00 11.65
ATOM    484  CG  HIS A  64       6.951  13.241  46.894  1.00 13.29
ATOM    485  ND1 HIS A  64       8.028  13.569  47.686  1.00 15.69
ATOM    486  CD2 HIS A  64       7.491  12.896  45.693  1.00 13.42
ATOM    487  CE1 HIS A  64       9.166  13.445  46.978  1.00 13.78
ATOM    488  NE2 HIS A  64       8.837  13.029  45.758  1.00 14.23
ATOM    489  N   ASP A  65       6.416  16.184  46.145  1.00 16.58
ATOM    490  CA  ASP A  65       7.285  17.328  46.446  1.00 18.33
ATOM    491  C   ASP A  65       6.502  18.589  46.759  1.00 18.94
ATOM    492  O   ASP A  65       6.889  19.398  47.618  1.00 20.18
ATOM    493  CB  ASP A  65       8.438  17.409  45.465  1.00 19.31
ATOM    494  CG  ASP A  65       7.974  17.869  44.109  1.00 21.94
ATOM    495  OD1 ASP A  65       7.149  17.331  43.392  1.00 24.89
ATOM    496  OD2 ASP A  65       8.471  18.936  43.750  1.00 26.14
ATOM    497  N   ARG A  66       5.395  18.812  46.138  1.00 18.97
ATOM    498  CA  ARG A  66       4.529  19.939  46.300  1.00 20.66
ATOM    499  C   ARG A  66       3.773  19.905  47.633  1.00 20.38
ATOM    500  O   ARG A  66       3.367  20.996  48.033  1.00 21.15
ATOM    501  CB  ARG A  66       3.484  19.991  45.187  1.00 23.21
ATOM    502  CG  ARG A  66       2.990  21.336  44.764  1.00 29.13
ATOM    503  CD  ARG A  66       4.116  22.215  44.328  1.00 33.64
ATOM    504  NE  ARG A  66       3.743  23.228  43.394  1.00 38.88
ATOM    505  CZ  ARG A  66       2.986  24.307  43.509  1.00 40.55
ATOM    506  NH1 ARG A  66       2.381  24.671  44.648  1.00 40.54
ATOM    507  NH2 ARG A  66       2.830  25.073  42.409  1.00 42.28
ATOM    508  N   PHE A  67       3.607  18.746  48.216  1.00 19.97
ATOM    509  CA  PHE A  67       2.863  18.480  49.438  1.00 18.34
ATOM    510  C   PHE A  67       3.527  19.094  50.662  1.00 18.64
ATOM    511  O   PHE A  67       2.824  19.406  51.625  1.00 17.31
ATOM    512  CB  PHE A  67       2.479  17.016  49.664  1.00 16.59
ATOM    513  CG  PHE A  67       1.311  16.511  48.881  1.00 17.36
ATOM    514  CD1 PHE A  67       0.836  17.174  47.762  1.00 18.42
ATOM    515  CD2 PHE A  67       0.661  15.339  49.259  1.00 18.42
ATOM    516  CE1 PHE A  67      -0.253  16.726  47.004  1.00 19.10
ATOM    517  CE2 PHE A  67      -0.416  14.859  48.529  1.00 17.63
ATOM    518  CZ  PHE A  67      -0.874  15.539  47.418  1.00 17.63
ATOM    519  N   GLY A  68       4.821  19.265  50.583  1.00 19.12
ATOM    520  CA  GLY A  68       5.611  19.869  51.674  1.00 20.86
ATOM    521  C   GLY A  68       5.143  21.306  51.977  1.00 20.99
ATOM    522  O   GLY A  68       4.958  21.643  53.161  1.00 22.15
ATOM    523  N   GLY A  69       4.983  22.107  50.973  1.00 20.48
ATOM    524  CA  GLY A  69       4.534  23.484  51.018  1.00 20.74
ATOM    525  C   GLY A  69       3.088  23.574  51.463  1.00 20.84
ATOM    526  O   GLY A  69       2.696  24.462  52.204  1.00 21.01
ATOM    527  N   TYR A  70       2.256  22.644  50.997  1.00 20.79
ATOM    528  CA  TYR A  70       0.842  22.541  51.365  1.00 19.63
ATOM    529  C   TYR A  70       0.691  22.217  52.876  1.00 19.33
ATOM    530  O   TYR A  70      -0.145  22.827  53.568  1.00 19.61
ATOM    531  CB  TYR A  70       0.137  21.445  50.557  1.00 19.13
ATOM    532  CG  TYR A  70      -0.082  21.647  49.094  1.00 19.71
ATOM    533  CD1 TYR A  70       0.187  22.860  48.444  1.00 18.90
ATOM    534  CD2 TYR A  70      -0.568  20.575  48.322  1.00 18.93
ATOM    535  CE1 TYR A  70      -0.048  23.016  47.083  1.00 19.01
ATOM    536  CE2 TYR A  70      -0.799  20.727  46.954  1.00 18.43
ATOM    537  CZ  TYR A  70      -0.541  21.939  46.335  1.00 18.95
ATOM    538  OH  TYR A  70      -0.770  22.107  44.996  1.00 19.45
ATOM    539  N   ALA A  71       1.417  21.259  53.374  1.00 17.60
ATOM    540  CA  ALA A  71       1.487  20.775  54.717  1.00 19.31
ATOM    541  C   ALA A  71       1.971  21.896  55.678  1.00 21.08
ATOM    542  O   ALA A  71       1.506  22.006  56.817  1.00 20.66
ATOM    543  CB  ALA A  71       2.388  19.559  54.872  1.00 17.00
ATOM    544  N   GLN A  72       2.919  22.644  55.184  1.00 21.79
ATOM    545  CA  GLN A  72       3.533  23.754  55.922  1.00 23.26
ATOM    546  C   GLN A  72       2.397  24.714  56.296  1.00 22.22
ATOM    547  O   GLN A  72       2.408  25.074  57.468  1.00 24.64
ATOM    548  CB  GLN A  72       4.571  24.495  55.102  1.00 25.94
ATOM    549  CG  GLN A  72       5.723  25.080  55.919  1.00 30.41
ATOM    550  CD  GLN A  72       6.500  26.012  54.998  1.00 33.63
ATOM    551  OE1 GLN A  72       7.714  26.005  54.891  1.00 35.86
ATOM    552  NE2 GLN A  72       5.702  26.840  54.304  1.00 36.33
ATOM    553  N   SER A  73       1.547  25.067  55.372  1.00 19.13
ATOM    554  CA  SER A  73       0.426  25.944  55.583  1.00 17.59
ATOM    555  C   SER A  73      -0.811  25.309  56.200  1.00 17.54
ATOM    556  O   SER A  73      -1.862  25.981  56.170  1.00 17.41
ATOM    557  CB  SER A  73      -0.026  26.623  54.298  1.00 17.11
ATOM    558  OG  SER A  73       1.051  27.370  53.792  1.00 20.15
ATOM    559  N   GLY A  74      -0.702  24.081  56.625  1.00 16.86
ATOM    560  CA  GLY A  74      -1.689  23.259  57.269  1.00 16.76
ATOM    561  C   GLY A  74      -2.887  22.913  56.408  1.00 16.50
ATOM    562  O   GLY A  74      -4.000  22.774  56.921  1.00 16.03
ATOM    563  N   LEU A  75      -2.638  22.730  55.121  1.00 14.95
ATOM    564  CA  LEU A  75      -3.702  22.435  54.165  1.00 15.00
ATOM    565  C   LEU A  75      -4.070  20.956  54.070  1.00 13.66
ATOM    566  O   LEU A  75      -5.134  20.652  53.519  1.00 14.09
ATOM    567  CB  LEU A  75      -3.264  23.027  52.823  1.00 15.18
ATOM    568  CG  LEU A  75      -2.936  24.517  52.806  1.00 15.38
ATOM    569  CD1 LEU A  75      -2.530  24.889  51.376  1.00 16.20
ATOM    570  CD2 LEU A  75      -4.194  25.279  53.185  1.00 13.76
ATOM    571  N   LEU A  76      -3.278  20.080  54.584  1.00 13.94
ATOM    572  CA  LEU A  76      -3.476  18.654  54.550  1.00 15.37
ATOM    573  C   LEU A  76      -3.726  18.002  55.910  1.00 16.40
ATOM    574  O   LEU A  76      -2.992  18.260  56.886  1.00 17.73
ATOM    575  CB  LEU A  76      -2.239  18.016  53.863  1.00 14.72
ATOM    576  CG  LEU A  76      -1.937  18.418  52.437  1.00 14.46
ATOM    577  CD1 LEU A  76      -0.760  17.584  51.895  1.00 15.08
ATOM    578  CD2 LEU A  76      -3.128  18.194  51.529  1.00 14.61
ATOM    579  N   ALA A  77      -4.685  17.076  55.890  1.00 14.92
ATOM    580  CA  ALA A  77      -4.988  16.290  57.075  1.00 15.54
ATOM    581  C   ALA A  77      -3.904  15.232  57.232  1.00 17.53
ATOM    582  O   ALA A  77      -3.307  14.691  56.269  1.00 16.81
ATOM    583  CB  ALA A  77      -6.363  15.678  56.977  1.00 15.24
ATOM    584  N   GLU A  78      -3.639  14.978  58.502  1.00 18.63
ATOM    585  CA  GLU A  78      -2.685  13.957  58.908  1.00 20.54
ATOM    586  C   GLU A  78      -3.424  12.626  58.643  1.00 19.76
ATOM    587  O   GLU A  78      -4.649  12.568  58.842  1.00 19.46
ATOM    588  CB  GLU A  78      -2.296  13.952  60.367  1.00 22.78
ATOM    589  CG  GLU A  78      -1.302  12.895  60.841  1.00 25.81
ATOM    590  CD  GLU A  78      -0.913  12.906  62.282  1.00 26.33
ATOM    591  OE1 GLU A  78      -1.173  13.809  63.028  1.00 28.96
ATOM    592  OE2 GLU A  78      -0.320  11.896  62.689  1.00 28.58
ATOM    593  N   ILE A  79      -2.685  11.672  58.141  1.00 20.01
ATOM    594  CA  ILE A  79      -3.283  10.349  57.827  1.00 19.96
ATOM    595  C   ILE A  79      -2.756   9.330  58.794  1.00 20.56
ATOM    596  O   ILE A  79      -1.661   9.369  59.333  1.00 19.44
ATOM    597  CB  ILE A  79      -3.175   9.952  56.308  1.00 19.32
ATOM    598  CG1 ILE A  79      -1.695   9.781  55.892  1.00 18.76
ATOM    599  CG2 ILE A  79      -3.914  10.932  55.364  1.00 17.46
ATOM    600  CD1 ILE A  79      -1.404   8.575  54.980  1.00 18.13
ATOM    601  N   THR A  80      -3.615   8.320  59.002  1.00 24.30
ATOM    602  CA  THR A  80      -3.208   7.252  59.917  1.00 28.10
ATOM    603  C   THR A  80      -3.562   5.857  59.475  1.00 29.43
ATOM    604  O   THR A  80      -4.400   5.202  60.125  1.00 30.84
ATOM    605  CB  THR A  80      -3.819   7.576  61.359  1.00 29.96
ATOM    606  OG1 THR A  80      -5.193   8.006  61.034  1.00 32.20
ATOM    607  CG2 THR A  80      -2.924   8.560  62.110  1.00 28.97
ATOM    608  N   PRO A  81      -2.903   5.409  58.417  1.00 29.73
ATOM    609  CA  PRO A  81      -3.131   4.031  57.950  1.00 29.63
ATOM    610  C   PRO A  81      -2.543   3.178  59.059  1.00 30.69
ATOM    611  O   PRO A  81      -1.521   3.611  59.647  1.00 31.05
ATOM    612  CB  PRO A  81      -2.274   3.931  56.690  1.00 29.65
ATOM    613  CG  PRO A  81      -1.314   5.067  56.727  1.00 28.01
ATOM    614  CD  PRO A  81      -1.886   6.121  57.634  1.00 28.77
ATOM    615  N   ASP A  82      -3.085   2.018  59.314  1.00 32.66
ATOM    616  CA  ASP A  82      -2.476   1.155  60.374  1.00 34.02
ATOM    617  C   ASP A  82      -1.329   0.367  59.729  1.00 33.44
ATOM    618  O   ASP A  82      -1.173   0.352  58.492  1.00 32.42
ATOM    619  CB  ASP A  82      -3.542   0.373  61.101  1.00 37.77
ATOM    620  CG  ASP A  82      -3.845  -0.950  60.433  1.00 40.64
ATOM    621  OD1 ASP A  82      -4.412  -0.956  59.336  1.00 42.96
ATOM    622  OD2 ASP A  82      -3.437  -1.969  61.063  1.00 44.36
ATOM    623  N   LYS A  83      -0.549  -0.234  60.589  1.00 32.64
ATOM    624  CA  LYS A  83       0.644  -1.012  60.250  1.00 31.86
ATOM    625  C   LYS A  83       0.447  -1.921  59.052  1.00 30.36
ATOM    626  O   LYS A  83       1.276  -2.000  58.146  1.00 30.14
ATOM    627  CB  LYS A  83       1.127  -1.856  61.417  1.00 33.78
ATOM    628  CG  LYS A  83       2.503  -1.534  61.962  1.00 36.39
ATOM    629  CD  LYS A  83       3.566  -2.503  61.467  1.00 39.44
ATOM    630  CE  LYS A  83       4.969  -2.030  61.817  1.00 42.64
ATOM    631  NZ  LYS A  83       5.915  -3.166  62.035  1.00 43.96
ATOM    632  N   ALA A  84      -0.654  -2.602  59.097  1.00 29.04
ATOM    633  CA  ALA A  84      -1.117  -3.583  58.134  1.00 27.89
ATOM    634  C   ALA A  84      -1.328  -2.995  56.748  1.00 26.41
ATOM    635  O   ALA A  84      -1.010  -3.666  55.761  1.00 26.74
ATOM    636  CB  ALA A  84      -2.407  -4.224  58.650  1.00 28.50
ATOM    637  N   PHE A  85      -1.907  -1.799  56.724  1.00 24.31
ATOM    638  CA  PHE A  85      -2.139  -1.142  55.447  1.00 21.71
ATOM    639  C   PHE A  85      -0.753  -0.685  54.929  1.00 21.75
ATOM    640  O   PHE A  85      -0.476  -0.767  53.751  1.00 21.20
ATOM    641  CB  PHE A  85      -3.143  -0.026  55.447  1.00 20.41
ATOM    642  CG  PHE A  85      -3.252   0.686  54.121  1.00 19.75
ATOM    643  CD1 PHE A  85      -4.096   0.193  53.135  1.00 18.99
ATOM    644  CD2 PHE A  85      -2.484   1.817  53.866  1.00 18.44
ATOM    645  CE1 PHE A  85      -4.206   0.834  51.889  1.00 19.39
ATOM    646  CE2 PHE A  85      -2.596   2.474  52.640  1.00 18.24
ATOM    647  CZ  PHE A  85      -3.427   1.978  51.666  1.00 18.02
ATOM    648  N   GLN A  86       0.058  -0.234  55.837  1.00 21.73
ATOM    649  CA  GLN A  86       1.372   0.297  55.536  1.00 23.26
ATOM    650  C   GLN A  86       2.287  -0.712  54.876  1.00 24.08
ATOM    651  O   GLN A  86       3.149  -0.334  54.056  1.00 23.52
ATOM    652  CB  GLN A  86       2.020   0.919  56.783  1.00 24.05
ATOM    653  CG  GLN A  86       1.533   2.360  56.983  1.00 26.55
ATOM    654  CD  GLN A  86       2.039   2.904  58.288  1.00 28.41
ATOM    655  OE1 GLN A  86       1.295   3.031  59.258  1.00 31.73
ATOM    656  NE2 GLN A  86       3.316   3.227  58.320  1.00 28.84
ATOM    657  N   ASP A  87       2.133  -1.949  55.275  1.00 25.01
ATOM    658  CA  ASP A  87       2.956  -3.063  54.766  1.00 26.41
ATOM    659  C   ASP A  87       2.557  -3.479  53.365  1.00 24.18
ATOM    660  O   ASP A  87       3.302  -4.244  52.723  1.00 25.02
ATOM    661  CB  ASP A  87       3.061  -4.150  55.838  1.00 30.14
ATOM    662  CG  ASP A  87       4.039  -3.829  56.944  1.00 34.56
ATOM    663  OD1 ASP A  87       4.558  -2.702  57.140  1.00 37.91
ATOM    664  OD2 ASP A  87       4.346  -4.762  57.727  1.00 37.48
ATOM    665  N   LYS A  88       1.472  -2.992  52.842  1.00 22.96
ATOM    666  CA  LYS A  88       0.995  -3.273  51.495  1.00 23.05
ATOM    667  C   LYS A  88       1.757  -2.476  50.417  1.00 21.82
ATOM    668  O   LYS A  88       1.645  -2.814  49.245  1.00 21.29
ATOM    669  CB  LYS A  88      -0.479  -3.026  51.255  1.00 22.96
ATOM    670  CG  LYS A  88      -1.416  -3.633  52.285  1.00 26.15
ATOM    671  CD  LYS A  88      -2.133  -4.869  51.840  1.00 29.40
ATOM    672  CE  LYS A  88      -3.379  -5.133  52.679  1.00 30.84
ATOM    673  NZ  LYS A  88      -4.376  -4.089  52.275  1.00 33.19
ATOM    674  N   LEU A  89       2.459  -1.444  50.793  1.00 21.18
ATOM    675  CA  LEU A  89       3.230  -0.568  49.933  1.00 19.72
ATOM    676  C   LEU A  89       4.724  -0.656  50.250  1.00 20.17
ATOM    677  O   LEU A  89       5.152  -1.038  51.337  1.00 20.60
ATOM    678  CB  LEU A  89       2.708   0.849  49.983  1.00 18.10
ATOM    679  CG  LEU A  89       1.296   1.254  50.171  1.00 17.19
ATOM    680  CD1 LEU A  89       1.184   2.770  49.915  1.00 17.94
ATOM    681  CD2 LEU A  89       0.379   0.501  49.235  1.00 18.18
ATOM    682  N   TYR A  90       5.520  -0.310  49.226  1.00 20.59
ATOM    683  CA  TYR A  90       6.995  -0.296  49.369  1.00 20.03
ATOM    684  C   TYR A  90       7.327   0.719  50.456  1.00 19.86
ATOM    685  O   TYR A  90       6.814   1.858  50.386  1.00 20.24
ATOM    686  CB  TYR A  90       7.621   0.112  48.004  1.00 20.39
ATOM    687  CG  TYR A  90       7.426  -0.988  46.980  1.00 19.43
ATOM    688  CD1 TYR A  90       8.247  -2.109  47.033  1.00 20.30
ATOM    689  CD2 TYR A  90       6.437  -0.929  46.025  1.00 18.88
ATOM    690  CE1 TYR A  90       8.087  -3.166  46.120  1.00 21.37
ATOM    691  CE2 TYR A  90       6.265  -1.977  45.119  1.00 19.72
ATOM    692  CZ  TYR A  90       7.083  -3.078  45.166  1.00 20.24
ATOM    693  OH  TYR A  90       6.947  -4.135  44.309  1.00 23.22
ATOM    694  N   PRO A  91       8.130   0.296  51.409  1.00 19.81
ATOM    695  CA  PRO A  91       8.506   1.130  52.558  1.00 19.85
ATOM    696  C   PRO A  91       9.011   2.519  52.217  1.00 18.84
ATOM    697  O   PRO A  91       8.595   3.547  52.790  1.00 18.99
ATOM    698  CB  PRO A  91       9.492   0.255  53.339  1.00 20.27
ATOM    699  CG  PRO A  91       9.030  -1.158  53.027  1.00 20.27
ATOM    700  CD  PRO A  91       8.700  -1.066  51.527  1.00 20.59
ATOM    701  N   PHE A  92       9.883   2.571  51.211  1.00 17.93
ATOM    702  CA  PHE A  92      10.517   3.781  50.721  1.00 15.97
ATOM    703  C   PHE A  92       9.481   4.773  50.257  1.00 14.65
ATOM    704  O   PHE A  92       9.768   5.985  50.278  1.00 15.44
ATOM    705  CB  PHE A  92      11.617   3.449  49.673  1.00 15.70
ATOM    706  CG  PHE A  92      11.102   3.310  48.268  1.00 16.10
ATOM    707  CD1 PHE A  92      11.050   4.413  47.425  1.00 15.91
ATOM    708  CD2 PHE A  92      10.693   2.061  47.783  1.00 15.61
ATOM    709  CE1 PHE A  92      10.542   4.304  46.119  1.00 15.33
ATOM    710  CE2 PHE A  92      10.202   1.946  46.502  1.00 15.03
ATOM    711  CZ  PHE A  92      10.131   3.063  45.662  1.00 14.74
ATOM    712  N   THR A  93       8.313   4.344  49.847  1.00 13.77
ATOM    713  CA  THR A  93       7.288   5.249  49.367  1.00 13.93
ATOM    714  C   THR A  93       6.665   6.067  50.518  1.00 13.93
ATOM    715  O   THR A  93       6.250   7.205  50.233  1.00 13.19
ATOM    716  CB  THR A  93       6.211   4.629  48.419  1.00 13.63
ATOM    717  OG1 THR A  93       5.455   3.666  49.208  1.00 15.78
ATOM    718  CG2 THR A  93       6.826   3.949  47.173  1.00 15.12
ATOM    719  N   TRP A  94       6.672   5.513  51.697  1.00 14.10
ATOM    720  CA  TRP A  94       6.117   6.224  52.880  1.00 14.60
ATOM    721  C   TRP A  94       7.015   7.393  53.260  1.00 15.32
ATOM    722  O   TRP A  94       6.523   8.386  53.820  1.00 16.10
ATOM    723  CB  TRP A  94       5.862   5.242  54.021  1.00 13.64
ATOM    724  CG  TRP A  94       4.685   4.338  53.802  1.00 13.98
ATOM    725  CD1 TRP A  94       4.741   2.956  53.713  1.00 14.15
ATOM    726  CD2 TRP A  94       3.315   4.698  53.664  1.00 13.12
ATOM    727  NE1 TRP A  94       3.490   2.454  53.509  1.00 13.70
ATOM    728  CE2 TRP A  94       2.589   3.479  53.473  1.00 13.92
ATOM    729  CE3 TRP A  94       2.607   5.878  53.730  1.00 11.40
ATOM    730  CZ2 TRP A  94       1.201   3.455  53.328  1.00 13.44
ATOM    731  CZ3 TRP A  94       1.232   5.876  53.558  1.00 12.27
ATOM    732  CH2 TRP A  94       0.533   4.683  53.361  1.00 13.85
ATOM    733  N   ASP A  95       8.282   7.350  52.946  1.00 14.96
ATOM    734  CA  ASP A  95       9.241   8.405  53.202  1.00 15.85
ATOM    735  C   ASP A  95       8.972   9.667  52.408  1.00 16.08
ATOM    736  O   ASP A  95       9.390  10.774  52.844  1.00 17.71
ATOM    737  CB  ASP A  95      10.689   7.932  52.990  1.00 18.52
ATOM    738  CG  ASP A  95      11.104   6.961  54.036  1.00 21.33
ATOM    739  OD1 ASP A  95      10.691   7.070  55.203  1.00 26.28
ATOM    740  OD2 ASP A  95      11.843   6.009  53.754  1.00 25.72
ATOM    741  N   ALA A  96       8.309   9.573  51.282  1.00 13.99
ATOM    742  CA  ALA A  96       7.996  10.647  50.391  1.00 13.76
ATOM    743  C   ALA A  96       6.831  11.543  50.851  1.00 14.49
ATOM    744  O   ALA A  96       6.652  12.662  50.351  1.00 14.33
ATOM    745  CB  ALA A  96       7.621  10.137  48.988  1.00  9.79
ATOM    746  N   VAL A  97       5.980  10.945  51.669  1.00 15.40
ATOM    747  CA  VAL A  97       4.755  11.608  52.139  1.00 15.52
ATOM    748  C   VAL A  97       4.765  11.930  53.645  1.00 17.45
ATOM    749  O   VAL A  97       3.705  11.996  54.255  1.00 15.65
ATOM    750  CB  VAL A  97       3.553  10.692  51.787  1.00 13.85
ATOM    751  CG1 VAL A  97       3.255  10.722  50.303  1.00 13.01
ATOM    752  CG2 VAL A  97       3.694   9.322  52.362  1.00 12.36
ATOM    753  N   ARG A  98       5.922  12.062  54.196  1.00 19.71
ATOM    754  CA  ARG A  98       6.186  12.426  55.585  1.00 23.97
ATOM    755  C   ARG A  98       6.613  13.905  55.583  1.00 26.39
ATOM    756  O   ARG A  98       7.496  14.315  54.804  1.00 26.81
ATOM    757  CB  ARG A  98       7.262  11.559  56.189  1.00 24.88
ATOM    758  CG  ARG A  98       6.910  10.854  57.461  1.00 28.34
ATOM    759  CD  ARG A  98       7.864   9.781  57.803  1.00 31.29
ATOM    760  NE  ARG A  98       7.652   8.571  57.026  1.00 36.32
ATOM    761  CZ  ARG A  98       8.135   7.380  57.385  1.00 37.39
ATOM    762  NH1 ARG A  98       8.801   7.332  58.560  1.00 41.21
ATOM    763  NH2 ARG A  98       8.025   6.261  56.703  1.00 36.66
ATOM    764  N   TYR A  99       5.963  14.711  56.400  1.00 28.66
ATOM    765  CA  TYR A  99       6.285  16.134  56.536  1.00 31.21
ATOM    766  C   TYR A  99       6.511  16.366  58.045  1.00 34.00
ATOM    767  O   TYR A  99       5.547  16.426  58.810  1.00 34.53
ATOM    768  CB  TYR A  99       5.288  17.128  55.977  1.00 30.84
ATOM    769  CG  TYR A  99       5.811  18.550  55.973  1.00 31.78
ATOM    770  CD1 TYR A  99       6.861  18.876  55.110  1.00 32.60
ATOM    771  CD2 TYR A  99       5.309  19.535  56.820  1.00 32.48
ATOM    772  CE1 TYR A  99       7.385  20.158  55.077  1.00 34.93
ATOM    773  CE2 TYR A  99       5.812  20.835  56.793  1.00 33.79
ATOM    774  CZ  TYR A  99       6.851  21.139  55.923  1.00 35.22
ATOM    775  OH  TYR A  99       7.367  22.405  55.886  1.00 37.38
ATOM    776  N   ASN A 100       7.781  16.390  58.361  1.00 37.03
ATOM    777  CA  ASN A 100       8.310  16.567  59.708  1.00 39.43
ATOM    778  C   ASN A 100       7.727  15.531  60.651  1.00 39.36
ATOM    779  O   ASN A 100       7.149  15.861  61.677  1.00 39.65
ATOM    780  CB  ASN A 100       8.139  18.009  60.187  1.00 43.24
ATOM    781  CG  ASN A 100       9.270  18.889  59.654  1.00 45.78
ATOM    782  OD1 ASN A 100      10.287  18.399  59.148  1.00 47.06
ATOM    783  ND2 ASN A 100       9.063  20.204  59.754  1.00 48.97
ATOM    784  N   GLY A 101       7.870  14.290  60.213  1.00 39.48
ATOM    785  CA  GLY A 101       7.412  13.128  60.941  1.00 37.94
ATOM    786  C   GLY A 101       5.975  12.726  60.703  1.00 36.41
ATOM    787  O   GLY A 101       5.693  11.515  60.856  1.00 37.65
ATOM    788  N   LYS A 102       5.110  13.644  60.354  1.00 34.19
ATOM    789  CA  LYS A 102       3.688  13.384  60.115  1.00 31.24
ATOM    790  C   LYS A 102       3.433  12.880  58.681  1.00 27.73
ATOM    791  O   LYS A 102       3.981  13.478  57.754  1.00 26.10
ATOM    792  CB  LYS A 102       2.874  14.668  60.295  1.00 34.22
ATOM    793  CG  LYS A 102       1.996  14.755  61.531  1.00 37.28
ATOM    794  CD  LYS A 102       2.719  15.450  62.671  1.00 42.03
ATOM    795  CE  LYS A 102       2.032  15.307  64.021  1.00 44.71
ATOM    796  NZ  LYS A 102       2.415  14.053  64.729  1.00 46.03
ATOM    797  N   LEU A 103       2.639  11.842  58.572  1.00 23.77
ATOM    798  CA  LEU A 103       2.205  11.263  57.285  1.00 20.24
ATOM    799  C   LEU A 103       1.105  12.196  56.761  1.00 17.94
ATOM    800  O   LEU A 103       0.046  12.328  57.424  1.00 16.66
ATOM    801  CB  LEU A 103       1.681   9.856  57.519  1.00 21.15
ATOM    802  CG  LEU A 103       2.444   8.599  57.297  1.00 20.40
ATOM    803  CD1 LEU A 103       3.507   8.377  58.349  1.00 23.86
ATOM    804  CD2 LEU A 103       1.493   7.402  57.419  1.00 22.19
ATOM    805  N   ILE A 104       1.298  12.788  55.608  1.00 14.54
ATOM    806  CA  ILE A 104       0.349  13.720  55.018  1.00 12.61
ATOM    807  C   ILE A 104      -0.231  13.331  53.676  1.00 11.57
ATOM    808  O   ILE A 104      -0.931  14.152  53.045  1.00 11.38
ATOM    809  CB  ILE A 104       0.959  15.184  55.060  1.00 12.62
ATOM    810  CG1 ILE A 104       2.373  15.211  54.462  1.00 12.72
ATOM    811  CG2 ILE A 104       0.997  15.697  56.526  1.00 14.33
ATOM    812  CD1 ILE A 104       2.496  15.347  52.951  1.00 12.83
ATOM    813  N   ALA A 105      -0.021  12.086  53.254  1.00 11.27
ATOM    814  CA  ALA A 105      -0.602  11.635  51.960  1.00 11.68
ATOM    815  C   ALA A 105      -0.340  10.148  51.740  1.00 10.24
ATOM    816  O   ALA A 105       0.502   9.579  52.379  1.00 10.59
ATOM    817  CB  ALA A 105      -0.008  12.453  50.808  1.00 11.31
ATOM    818  N   TYR A 106      -1.111   9.596  50.813  1.00 11.34
ATOM    819  CA  TYR A 106      -0.894   8.151  50.452  1.00 11.25
ATOM    820  C   TYR A 106      -0.119   8.134  49.096  1.00 10.46
ATOM    821  O   TYR A 106      -0.560   8.835  48.207  1.00  8.70
ATOM    822  CB  TYR A 106      -2.253   7.479  50.163  1.00 11.77
ATOM    823  CG  TYR A 106      -3.158   7.305  51.374  1.00 13.95
ATOM    824  CD1 TYR A 106      -3.087   6.159  52.172  1.00 13.42
ATOM    825  CD2 TYR A 106      -4.114   8.288  51.681  1.00 15.69
ATOM    826  CE1 TYR A 106      -3.959   5.961  53.261  1.00 12.56
ATOM    827  CE2 TYR A 106      -4.980   8.094  52.794  1.00 15.81
ATOM    828  CZ  TYR A 106      -4.880   6.947  53.553  1.00 13.75
ATOM    829  OH  TYR A 106      -5.715   6.752  54.621  1.00 15.88
ATOM    830  N   PRO A 107       0.896   7.308  49.071  1.00 11.78
ATOM    831  CA  PRO A 107       1.752   7.135  47.856  1.00 11.74
ATOM    832  C   PRO A 107       0.944   6.372  46.817  1.00 11.24
ATOM    833  O   PRO A 107       0.202   5.465  47.222  1.00 12.61
ATOM    834  CB  PRO A 107       2.947   6.408  48.382  1.00 12.46
ATOM    835  CG  PRO A 107       2.853   6.192  49.848  1.00 11.42
ATOM    836  CD  PRO A 107       1.388   6.460  50.165  1.00 11.82
ATOM    837  N   ILE A 108       0.948   6.729  45.574  1.00 11.76
ATOM    838  CA  ILE A 108       0.188   6.059  44.510  1.00 12.69
ATOM    839  C   ILE A 108       1.105   5.387  43.456  1.00 13.42
ATOM    840  O   ILE A 108       1.137   4.157  43.325  1.00 12.05
ATOM    841  CB  ILE A 108      -0.824   7.010  43.820  1.00 11.64
ATOM    842  CG1 ILE A 108      -1.714   7.792  44.819  1.00 12.32
ATOM    843  CG2 ILE A 108      -1.698   6.292  42.746  1.00 13.13
ATOM    844  CD1 ILE A 108      -2.594   7.014  45.766  1.00 12.38
ATOM    845  N   ALA A 109       1.865   6.238  42.769  1.00 14.28
ATOM    846  CA  ALA A 109       2.805   5.777  41.690  1.00 13.47
ATOM    847  C   ALA A 109       4.197   6.286  41.939  1.00 14.11
ATOM    848  O   ALA A 109       4.373   7.215  42.743  1.00 12.94
ATOM    849  CB  ALA A 109       2.205   6.320  40.388  1.00 12.95
ATOM    850  N   VAL A 110       5.213   5.720  41.340  1.00 14.52
ATOM    851  CA  VAL A 110       6.634   6.073  41.482  1.00 14.87
ATOM    852  C   VAL A 110       7.260   6.333  40.095  1.00 16.14
ATOM    853  O   VAL A 110       6.959   5.649  39.094  1.00 16.24
ATOM    854  CB  VAL A 110       7.314   4.939  42.266  1.00 15.78
ATOM    855  CG1 VAL A 110       8.798   5.159  42.543  1.00 15.44
ATOM    856  CG2 VAL A 110       6.569   4.575  43.554  1.00 16.08
ATOM    857  N   GLU A 111       8.091   7.354  39.992  1.00 15.12
ATOM    858  CA  GLU A 111       8.752   7.728  38.725  1.00 14.98
ATOM    859  C   GLU A 111      10.204   8.031  38.977  1.00 14.19
ATOM    860  O   GLU A 111      10.542   8.625  40.031  1.00 14.54
ATOM    861  CB  GLU A 111       8.151   8.965  38.105  1.00 17.47
ATOM    862  CG  GLU A 111       7.344   8.796  36.844  1.00 22.67
ATOM    863  CD  GLU A 111       6.721  10.066  36.316  1.00 26.09
ATOM    864  OE1 GLU A 111       7.008  11.154  36.821  1.00 27.17
ATOM    865  OE2 GLU A 111       5.960   9.774  35.366  1.00 27.04
ATOM    866  N   ALA A 112      11.075   7.565  38.079  1.00 12.07
ATOM    867  CA  ALA A 112      12.511   7.787  38.188  1.00  9.91
ATOM    868  C   ALA A 112      13.073   7.618  36.764  1.00 10.79
ATOM    869  O   ALA A 112      12.398   6.936  35.948  1.00 12.57
ATOM    870  CB  ALA A 112      13.198   6.862  39.166  1.00  7.95
ATOM    871  N   LEU A 113      14.199   8.254  36.526  1.00  9.85
ATOM    872  CA  LEU A 113      14.878   8.132  35.201  1.00  8.62
ATOM    873  C   LEU A 113      15.414   6.722  35.082  1.00  6.99
ATOM    874  O   LEU A 113      15.746   6.051  36.034  1.00  5.87
ATOM    875  CB  LEU A 113      16.031   9.159  35.200  1.00  8.28
ATOM    876  CG  LEU A 113      15.660  10.604  34.974  1.00  7.20
ATOM    877  CD1 LEU A 113      16.906  11.497  35.124  1.00  8.03
ATOM    878  CD2 LEU A 113      14.950  10.837  33.669  1.00  5.88
ATOM    879  N   SER A 114      15.612   6.319  33.814  1.00  8.98
ATOM    880  CA  SER A 114      16.185   4.985  33.536  1.00  7.65
ATOM    881  C   SER A 114      17.146   5.161  32.305  1.00  6.31
ATOM    882  O   SER A 114      17.043   6.210  31.712  1.00  6.74
ATOM    883  CB  SER A 114      15.064   4.021  33.134  1.00  8.73
ATOM    884  OG  SER A 114      14.386   3.468  34.235  1.00  8.45
ATOM    885  N   LEU A 115      17.932   4.171  32.119  1.00  7.32
ATOM    886  CA  LEU A 115      18.852   4.126  30.922  1.00  8.45
ATOM    887  C   LEU A 115      18.026   3.529  29.765  1.00  7.94
ATOM    888  O   LEU A 115      17.506   2.433  29.999  1.00  8.70
ATOM    889  CB  LEU A 115      20.047   3.300  31.242  1.00  8.88
ATOM    890  CG  LEU A 115      21.374   3.571  30.551  1.00 13.50
ATOM    891  CD1 LEU A 115      22.037   2.305  30.052  1.00 13.68
ATOM    892  CD2 LEU A 115      21.384   4.680  29.550  1.00 13.97
ATOM    893  N   ILE A 116      17.870   4.226  28.695  1.00  8.36
ATOM    894  CA  ILE A 116      17.104   3.793  27.502  1.00  9.63
ATOM    895  C   ILE A 116      18.151   3.472  26.424  1.00 11.47
ATOM    896  O   ILE A 116      18.968   4.378  26.239  1.00 12.88
ATOM    897  CB  ILE A 116      16.077   4.826  27.037  1.00  8.42
ATOM    898  CG1 ILE A 116      15.073   5.164  28.208  1.00  7.94
ATOM    899  CG2 ILE A 116      15.257   4.405  25.776  1.00  8.26
ATOM    900  CD1 ILE A 116      14.096   6.282  27.844  1.00  7.74
ATOM    901  N   TYR A 117      18.108   2.344  25.749  1.00 11.46
ATOM    902  CA  TYR A 117      19.182   2.074  24.754  1.00 10.41
ATOM    903  C   TYR A 117      18.590   1.439  23.507  1.00 11.01
ATOM    904  O   TYR A 117      17.491   0.921  23.575  1.00 11.37
ATOM    905  CB  TYR A 117      20.268   1.236  25.397  1.00 12.64
ATOM    906  CG  TYR A 117      19.821  -0.173  25.727  1.00 15.52
ATOM    907  CD1 TYR A 117      19.050  -0.477  26.853  1.00 16.31
ATOM    908  CD2 TYR A 117      20.174  -1.198  24.856  1.00 17.27
ATOM    909  CE1 TYR A 117      18.654  -1.791  27.115  1.00 18.13
ATOM    910  CE2 TYR A 117      19.765  -2.503  25.089  1.00 18.79
ATOM    911  CZ  TYR A 117      19.017  -2.797  26.205  1.00 19.16
ATOM    912  OH  TYR A 117      18.671  -4.089  26.460  1.00 21.49
ATOM    913  N   ASN A 118      19.313   1.547  22.439  1.00 10.95
ATOM    914  CA  ASN A 118      18.931   1.080  21.084  1.00 12.04
ATOM    915  C   ASN A 118      19.488  -0.340  20.962  1.00 12.91
ATOM    916  O   ASN A 118      20.692  -0.447  20.914  1.00 12.41
ATOM    917  CB  ASN A 118      19.482   2.100  20.087  1.00 12.21
ATOM    918  CG  ASN A 118      19.040   1.784  18.659  1.00 12.82
ATOM    919  OD1 ASN A 118      18.946   0.573  18.362  1.00 16.81
ATOM    920  ND2 ASN A 118      18.710   2.771  17.890  1.00 11.52
ATOM    921  N   LYS A 119      18.589  -1.320  20.988  1.00 14.83
ATOM    922  CA  LYS A 119      18.954  -2.743  20.960  1.00 16.85
ATOM    923  C   LYS A 119      19.655  -3.148  19.668  1.00 17.35
ATOM    924  O   LYS A 119      20.415  -4.144  19.722  1.00 18.35
ATOM    925  CB  LYS A 119      17.788  -3.658  21.230  1.00 17.35
ATOM    926  CG  LYS A 119      17.517  -3.870  22.700  1.00 21.76
ATOM    927  CD  LYS A 119      16.084  -3.946  23.122  1.00 23.76
ATOM    928  CE  LYS A 119      15.259  -5.055  22.664  1.00 26.95
ATOM    929  NZ  LYS A 119      14.674  -5.918  23.716  1.00 30.33
ATOM    930  N   ASP A 120      19.423  -2.383  18.632  1.00 18.01
ATOM    931  CA  ASP A 120      20.078  -2.627  17.322  1.00 19.92
ATOM    932  C   ASP A 120      21.504  -2.097  17.283  1.00 20.62
ATOM    933  O   ASP A 120      22.324  -2.612  16.466  1.00 23.24
ATOM    934  CB  ASP A 120      19.227  -2.085  16.172  1.00 19.84
ATOM    935  CG  ASP A 120      17.912  -2.751  15.925  1.00 19.41
ATOM    936  OD1 ASP A 120      17.791  -3.925  16.298  1.00 20.54
ATOM    937  OD2 ASP A 120      17.000  -2.146  15.352  1.00 21.55
ATOM    938  N   LEU A 121      21.908  -1.117  18.060  1.00 19.62
ATOM    939  CA  LEU A 121      23.270  -0.574  18.047  1.00 18.15
ATOM    940  C   LEU A 121      24.117  -1.146  19.163  1.00 19.58
ATOM    941  O   LEU A 121      25.341  -1.222  19.045  1.00 19.17
ATOM    942  CB  LEU A 121      23.168   0.955  18.223  1.00 15.91
ATOM    943  CG  LEU A 121      22.536   1.702  17.078  1.00 17.00
ATOM    944  CD1 LEU A 121      22.378   3.200  17.349  1.00 15.81
ATOM    945  CD2 LEU A 121      23.404   1.465  15.819  1.00 15.96
ATOM    946  N   LEU A 122      23.397  -1.503  20.223  1.00 20.54
ATOM    947  CA  LEU A 122      24.024  -1.976  21.455  1.00 22.99
ATOM    948  C   LEU A 122      23.323  -3.239  21.937  1.00 26.02
ATOM    949  O   LEU A 122      22.178  -3.150  22.363  1.00 26.24
ATOM    950  CB  LEU A 122      23.921  -0.746  22.391  1.00 21.89
ATOM    951  CG  LEU A 122      24.971  -0.520  23.425  1.00 21.81
ATOM    952  CD1 LEU A 122      26.349  -0.377  22.809  1.00 21.80
ATOM    953  CD2 LEU A 122      24.657   0.733  24.254  1.00 21.68
ATOM    954  N   PRO A 123      24.062  -4.337  21.874  1.00 29.42
ATOM    955  CA  PRO A 123      23.614  -5.663  22.283  1.00 31.26
ATOM    956  C   PRO A 123      23.207  -5.699  23.747  1.00 31.53
ATOM    957  O   PRO A 123      22.105  -6.099  24.158  1.00 32.70
ATOM    958  CB  PRO A 123      24.825  -6.582  22.031  1.00 31.73
ATOM    959  CG  PRO A 123      26.020  -5.649  22.111  1.00 32.31
ATOM    960  CD  PRO A 123      25.483  -4.387  21.406  1.00 31.27
ATOM    961  N   ASN A 124      24.185  -5.290  24.538  1.00 31.60
ATOM    962  CA  ASN A 124      24.006  -5.225  26.002  1.00 31.41
ATOM    963  C   ASN A 124      24.447  -3.822  26.438  1.00 28.48
ATOM    964  O   ASN A 124      25.508  -3.371  26.013  1.00 28.20
ATOM    965  CB  ASN A 124      24.723  -6.368  26.692  1.00 34.71
ATOM    966  CG  ASN A 124      23.943  -7.674  26.585  1.00 38.69
ATOM    967  OD1 ASN A 124      23.677  -8.362  27.582  1.00 41.25
ATOM    968  ND2 ASN A 124      23.571  -8.027  25.350  1.00 40.58
ATOM    969  N   PRO A 125      23.590  -3.228  27.238  1.00 26.02
ATOM    970  CA  PRO A 125      23.887  -1.872  27.767  1.00 23.80
ATOM    971  C   PRO A 125      25.088  -1.981  28.683  1.00 20.47
ATOM    972  O   PRO A 125      25.289  -3.036  29.287  1.00 18.62
ATOM    973  CB  PRO A 125      22.610  -1.500  28.514  1.00 25.24
ATOM    974  CG  PRO A 125      21.939  -2.793  28.864  1.00 25.15
ATOM    975  CD  PRO A 125      22.317  -3.749  27.721  1.00 25.12
ATOM    976  N   PRO A 126      25.828  -0.886  28.821  1.00 18.83
ATOM    977  CA  PRO A 126      27.005  -0.854  29.700  1.00 16.79
ATOM    978  C   PRO A 126      26.524  -0.920  31.150  1.00 15.65
ATOM    979  O   PRO A 126      25.458  -0.360  31.394  1.00 15.04
ATOM    980  CB  PRO A 126      27.658   0.496  29.411  1.00 17.74
ATOM    981  CG  PRO A 126      26.538   1.357  28.905  1.00 18.12
ATOM    982  CD  PRO A 126      25.626   0.394  28.140  1.00 18.46
ATOM    983  N   LYS A 127      27.276  -1.572  31.988  1.00 13.46
ATOM    984  CA  LYS A 127      26.924  -1.696  33.366  1.00 15.42
ATOM    985  C   LYS A 127      27.477  -0.551  34.205  1.00 14.21
ATOM    986  O   LYS A 127      26.993  -0.243  35.279  1.00 12.96
ATOM    987  CB  LYS A 127      27.355  -3.042  33.942  1.00 18.50
ATOM    988  CG  LYS A 127      26.372  -4.141  33.421  1.00 23.79
ATOM    989  CD  LYS A 127      24.914  -3.770  33.718  1.00 28.78
ATOM    990  CE  LYS A 127      23.987  -3.716  32.513  1.00 29.77
ATOM    991  NZ  LYS A 127      22.568  -3.406  32.874  1.00 29.36
ATOM    992  N   THR A 128      28.447   0.078  33.632  1.00 13.90
ATOM    993  CA  THR A 128      29.266   1.149  34.216  1.00 14.12
ATOM    994  C   THR A 128      29.324   2.410  33.408  1.00 13.69
ATOM    995  O   THR A 128      29.245   2.387  32.165  1.00 13.97
ATOM    996  CB  THR A 128      30.708   0.444  34.230  1.00 16.06
ATOM    997  OG1 THR A 128      30.945  -0.151  35.527  1.00 20.05
ATOM    998  CG2 THR A 128      31.828   1.194  33.616  1.00 16.06
ATOM    999  N   TRP A 129      29.495   3.548  34.115  1.00 12.44
ATOM   1000  CA  TRP A 129      29.677   4.841  33.478  1.00 11.36
ATOM   1001  C   TRP A 129      31.144   4.897  32.924  1.00 10.70
ATOM   1002  O   TRP A 129      31.360   5.566  31.942  1.00 11.31
ATOM   1003  CB  TRP A 129      29.514   6.046  34.415  1.00 11.74
ATOM   1004  CG  TRP A 129      28.114   6.514  34.653  1.00 12.02
ATOM   1005  CD1 TRP A 129      27.253   6.204  35.672  1.00  9.63
ATOM   1006  CD2 TRP A 129      27.413   7.429  33.795  1.00 12.45
ATOM   1007  NE1 TRP A 129      26.039   6.873  35.481  1.00  9.70
ATOM   1008  CE2 TRP A 129      26.145   7.656  34.376  1.00 10.62
ATOM   1009  CE3 TRP A 129      27.794   8.121  32.639  1.00 11.23
ATOM   1010  CZ2 TRP A 129      25.223   8.500  33.781  1.00  9.89
ATOM   1011  CZ3 TRP A 129      26.888   8.997  32.119  1.00 10.80
ATOM   1012  CH2 TRP A 129      25.615   9.169  32.644  1.00 10.60
ATOM   1013  N   GLU A 130      32.056   4.265  33.612  1.00 12.18
ATOM   1014  CA  GLU A 130      33.476   4.269  33.315  1.00 14.00
ATOM   1015  C   GLU A 130      33.813   3.706  31.951  1.00 15.44
ATOM   1016  O   GLU A 130      34.824   4.099  31.346  1.00 16.46
ATOM   1017  CB  GLU A 130      34.355   3.617  34.370  1.00 13.21
ATOM   1018  CG  GLU A 130      34.424   4.370  35.720  1.00 14.39
ATOM   1019  CD  GLU A 130      33.429   4.036  36.764  1.00 14.62
ATOM   1020  OE1 GLU A 130      32.380   3.466  36.429  1.00 14.60
ATOM   1021  OE2 GLU A 130      33.602   4.291  37.948  1.00 18.25
ATOM   1022  N   GLU A 131      32.926   2.884  31.438  1.00 16.68
ATOM   1023  CA  GLU A 131      33.139   2.258  30.123  1.00 17.26
ATOM   1024  C   GLU A 131      32.481   3.003  29.015  1.00 17.84
ATOM   1025  O   GLU A 131      32.626   2.554  27.851  1.00 18.95
ATOM   1026  CB  GLU A 131      32.673   0.815  30.182  1.00 18.53
ATOM   1027  CG  GLU A 131      31.203   0.504  30.269  1.00 20.87
ATOM   1028  CD  GLU A 131      30.824  -0.931  30.509  1.00 23.18
ATOM   1029  OE1 GLU A 131      30.813  -1.454  31.610  1.00 23.74
ATOM   1030  OE2 GLU A 131      30.485  -1.520  29.456  1.00 24.27
ATOM   1031  N   ILE A 132      31.819   4.130  29.230  1.00 16.49
ATOM   1032  CA  ILE A 132      31.172   4.888  28.184  1.00 16.00
ATOM   1033  C   ILE A 132      32.118   5.556  27.198  1.00 17.03
ATOM   1034  O   ILE A 132      31.868   5.518  25.970  1.00 15.59
ATOM   1035  CB  ILE A 132      30.005   5.770  28.721  1.00 15.57
ATOM   1036  CG1 ILE A 132      28.919   4.796  29.253  1.00 16.27
ATOM   1037  CG2 ILE A 132      29.474   6.769  27.683  1.00 15.85
ATOM   1038  CD1 ILE A 132      27.638   5.509  29.760  1.00 16.98
ATOM   1039  N   PRO A 133      33.159   6.197  27.668  1.00 17.55
ATOM   1040  CA  PRO A 133      34.143   6.833  26.791  1.00 18.55
ATOM   1041  C   PRO A 133      34.665   5.902  25.687  1.00 17.75
ATOM   1042  O   PRO A 133      34.684   6.328  24.525  1.00 19.00
ATOM   1043  CB  PRO A 133      35.249   7.257  27.772  1.00 18.73
ATOM   1044  CG  PRO A 133      34.480   7.524  29.051  1.00 17.84
ATOM   1045  CD  PRO A 133      33.536   6.323  29.097  1.00 18.09
ATOM   1046  N   ALA A 134      35.085   4.718  25.992  1.00 16.95
ATOM   1047  CA  ALA A 134      35.598   3.663  25.134  1.00 17.06
ATOM   1048  C   ALA A 134      34.563   3.186  24.125  1.00 18.94
ATOM   1049  O   ALA A 134      34.813   2.908  22.918  1.00 19.68
ATOM   1050  CB  ALA A 134      36.161   2.553  25.990  1.00 15.81
ATOM   1051  N   LEU A 135      33.339   3.059  24.577  1.00 18.37
ATOM   1052  CA  LEU A 135      32.182   2.662  23.793  1.00 18.66
ATOM   1053  C   LEU A 135      31.862   3.748  22.765  1.00 17.37
ATOM   1054  O   LEU A 135      31.484   3.442  21.637  1.00 17.30
ATOM   1055  CB  LEU A 135      31.003   2.454  24.758  1.00 18.76
ATOM   1056  CG  LEU A 135      29.839   1.657  24.282  1.00 20.62
ATOM   1057  CD1 LEU A 135      30.300   0.183  24.283  1.00 22.01
ATOM   1058  CD2 LEU A 135      28.670   1.817  25.259  1.00 20.31
ATOM   1059  N   ASP A 136      31.995   4.991  23.210  1.00 16.21
ATOM   1060  CA  ASP A 136      31.732   6.133  22.344  1.00 16.74
ATOM   1061  C   ASP A 136      32.764   6.141  21.174  1.00 17.81
ATOM   1062  O   ASP A 136      32.324   6.479  20.082  1.00 17.70
ATOM   1063  CB  ASP A 136      31.759   7.454  23.083  1.00 15.14
ATOM   1064  CG  ASP A 136      31.242   8.560  22.214  1.00 14.79
ATOM   1065  OD1 ASP A 136      30.128   8.575  21.719  1.00 16.04
ATOM   1066  OD2 ASP A 136      32.059   9.476  22.002  1.00 16.11
ATOM   1067  N   LYS A 137      33.994   5.829  21.469  1.00 19.72
ATOM   1068  CA  LYS A 137      35.051   5.799  20.418  1.00 22.31
ATOM   1069  C   LYS A 137      34.754   4.665  19.430  1.00 21.35
ATOM   1070  O   LYS A 137      34.843   4.876  18.202  1.00 20.15
ATOM   1071  CB  LYS A 137      36.417   5.800  21.013  1.00 25.50
ATOM   1072  CG  LYS A 137      37.111   4.463  21.187  1.00 32.24
ATOM   1073  CD  LYS A 137      37.834   3.978  19.944  1.00 36.76
ATOM   1074  CE  LYS A 137      38.015   2.459  19.926  1.00 39.32
ATOM   1075  NZ  LYS A 137      38.283   2.012  18.520  1.00 41.28
ATOM   1076  N   GLU A 138      34.243   3.536  19.874  1.00 21.30
ATOM   1077  CA  GLU A 138      33.875   2.427  18.997  1.00 21.19
ATOM   1078  C   GLU A 138      32.680   2.739  18.128  1.00 20.77
ATOM   1079  O   GLU A 138      32.642   2.341  16.941  1.00 20.19
ATOM   1080  CB  GLU A 138      33.553   1.124  19.692  1.00 23.72
ATOM   1081  CG  GLU A 138      34.734   0.382  20.321  1.00 29.27
ATOM   1082  CD  GLU A 138      34.353  -0.888  21.051  1.00 33.60
ATOM   1083  OE1 GLU A 138      33.540  -1.547  20.348  1.00 33.80
ATOM   1084  OE2 GLU A 138      34.784  -1.156  22.179  1.00 35.57
ATOM   1085  N   LEU A 139      31.705   3.453  18.687  1.00 18.91
ATOM   1086  CA  LEU A 139      30.507   3.845  17.965  1.00 17.16
ATOM   1087  C   LEU A 139      30.743   4.964  16.974  1.00 16.16
ATOM   1088  O   LEU A 139      30.064   5.085  15.952  1.00 15.64
ATOM   1089  CB  LEU A 139      29.382   4.105  18.966  1.00 16.97
ATOM   1090  CG  LEU A 139      28.670   2.873  19.523  1.00 19.22
ATOM   1091  CD1 LEU A 139      27.882   3.233  20.783  1.00 16.35
ATOM   1092  CD2 LEU A 139      27.691   2.390  18.428  1.00 19.09
ATOM   1093  N   LYS A 140      31.679   5.820  17.283  1.00 16.25
ATOM   1094  CA  LYS A 140      32.093   6.971  16.496  1.00 17.13
ATOM   1095  C   LYS A 140      32.734   6.480  15.166  1.00 17.38
ATOM   1096  O   LYS A 140      32.635   7.152  14.149  1.00 17.86
ATOM   1097  CB  LYS A 140      33.054   7.858  17.259  1.00 17.56
ATOM   1098  CG  LYS A 140      32.473   8.726  18.387  1.00 19.44
ATOM   1099  CD  LYS A 140      31.435   9.693  17.903  1.00 21.41
ATOM   1100  CE  LYS A 140      30.676  10.421  18.973  1.00 24.09
ATOM   1101  NZ  LYS A 140      31.618  11.056  19.969  1.00 25.43
ATOM   1102  N   ALA A 141      33.354   5.345  15.252  1.00 18.18
ATOM   1103  CA  ALA A 141      33.963   4.633  14.111  1.00 19.99
ATOM   1104  C   ALA A 141      32.913   4.361  13.034  1.00 20.94
ATOM   1105  O   ALA A 141      33.303   4.207  11.872  1.00 22.05
ATOM   1106  CB  ALA A 141      34.603   3.342  14.585  1.00 18.72
ATOM   1107  N   LYS A 142      31.641   4.299  13.371  1.00 21.60
ATOM   1108  CA  LYS A 142      30.516   4.075  12.491  1.00 22.35
ATOM   1109  C   LYS A 142      29.588   5.277  12.328  1.00 21.22
ATOM   1110  O   LYS A 142      28.476   5.154  11.729  1.00 20.91
ATOM   1111  CB  LYS A 142      29.590   2.955  12.926  1.00 25.58
ATOM   1112  CG  LYS A 142      30.182   1.565  12.925  1.00 31.58
ATOM   1113  CD  LYS A 142      29.816   0.806  14.192  1.00 34.48
ATOM   1114  CE  LYS A 142      28.338   0.555  14.423  1.00 35.00
ATOM   1115  NZ  LYS A 142      28.234  -0.435  15.560  1.00 37.58
ATOM   1116  N   GLY A 143      30.004   6.407  12.857  1.00 20.45
ATOM   1117  CA  GLY A 143      29.243   7.643  12.752  1.00 20.28
ATOM   1118  C   GLY A 143      28.120   7.734  13.811  1.00 19.91
ATOM   1119  O   GLY A 143      27.248   8.567  13.626  1.00 20.59
ATOM   1120  N   LYS A 144      28.188   6.947  14.848  1.00 19.56
ATOM   1121  CA  LYS A 144      27.175   6.965  15.925  1.00 19.04
ATOM   1122  C   LYS A 144      27.861   7.377  17.228  1.00 18.45
ATOM   1123  O   LYS A 144      29.081   7.178  17.367  1.00 19.05
ATOM   1124  CB  LYS A 144      26.574   5.572  16.111  1.00 18.97
ATOM   1125  CG  LYS A 144      25.961   4.850  14.923  1.00 17.82
ATOM   1126  CD  LYS A 144      24.878   5.648  14.270  1.00 18.60
ATOM   1127  CE  LYS A 144      24.096   4.973  13.169  1.00 20.08
ATOM   1128  NZ  LYS A 144      22.939   5.827  12.775  1.00 20.45
ATOM   1129  N   SER A 145      27.089   7.894  18.193  1.00 17.85
ATOM   1130  CA  SER A 145      27.637   8.243  19.519  1.00 15.94
ATOM   1131  C   SER A 145      27.017   7.264  20.544  1.00 14.84
ATOM   1132  O   SER A 145      25.967   6.665  20.315  1.00 14.65
ATOM   1133  CB  SER A 145      27.345   9.673  19.903  1.00 15.93
ATOM   1134  OG  SER A 145      25.960   9.877  20.065  1.00 19.00
ATOM   1135  N   ALA A 146      27.668   7.117  21.679  1.00 13.30
ATOM   1136  CA  ALA A 146      27.242   6.238  22.747  1.00 11.58
ATOM   1137  C   ALA A 146      26.015   6.761  23.493  1.00 13.16
ATOM   1138  O   ALA A 146      24.993   6.054  23.582  1.00 13.34
ATOM   1139  CB  ALA A 146      28.420   6.008  23.669  1.00  8.58
ATOM   1140  N   LEU A 147      26.080   7.983  24.007  1.00 13.63
ATOM   1141  CA  LEU A 147      25.001   8.549  24.825  1.00 12.68
ATOM   1142  C   LEU A 147      24.771  10.018  24.639  1.00 13.47
ATOM   1143  O   LEU A 147      25.764  10.761  24.436  1.00 15.31
ATOM   1144  CB  LEU A 147      25.544   8.295  26.288  1.00 11.85
ATOM   1145  CG  LEU A 147      24.750   8.972  27.423  1.00 11.88
ATOM   1146  CD1 LEU A 147      23.399   8.345  27.666  1.00 11.84
ATOM   1147  CD2 LEU A 147      25.596   8.867  28.693  1.00 11.12
ATOM   1148  N   MET A 148      23.536  10.451  24.700  1.00 12.27
ATOM   1149  CA  MET A 148      23.141  11.837  24.643  1.00 13.66
ATOM   1150  C   MET A 148      21.954  12.039  25.617  1.00 14.59
ATOM   1151  O   MET A 148      20.948  11.328  25.456  1.00 15.43
ATOM   1152  CB  MET A 148      22.766  12.309  23.246  1.00 16.42
ATOM   1153  CG  MET A 148      24.014  12.893  22.550  1.00 19.53
ATOM   1154  SD  MET A 148      23.496  13.372  20.918  1.00 28.20
ATOM   1155  CE  MET A 148      22.577  14.859  21.144  1.00 21.45
ATOM   1156  N   PHE A 149      22.062  12.982  26.527  1.00 13.52
ATOM   1157  CA  PHE A 149      20.968  13.298  27.464  1.00 14.03
ATOM   1158  C   PHE A 149      21.030  14.811  27.774  1.00 14.70
ATOM   1159  O   PHE A 149      21.993  15.497  27.436  1.00 14.65
ATOM   1160  CB  PHE A 149      20.994  12.443  28.705  1.00 13.14
ATOM   1161  CG  PHE A 149      22.111  12.564  29.672  1.00 13.09
ATOM   1162  CD1 PHE A 149      23.359  12.064  29.437  1.00 13.64
ATOM   1163  CD2 PHE A 149      21.904  13.248  30.886  1.00 14.21
ATOM   1164  CE1 PHE A 149      24.379  12.161  30.392  1.00 16.15
ATOM   1165  CE2 PHE A 149      22.868  13.334  31.851  1.00 13.77
ATOM   1166  CZ  PHE A 149      24.135  12.831  31.613  1.00 14.41
ATOM   1167  N   ASN A 150      19.965  15.283  28.404  1.00 15.14
ATOM   1168  CA  ASN A 150      19.823  16.686  28.789  1.00 14.34
ATOM   1169  C   ASN A 150      20.874  17.054  29.841  1.00 15.12
ATOM   1170  O   ASN A 150      20.798  16.596  30.959  1.00 15.41
ATOM   1171  CB  ASN A 150      18.416  16.909  29.343  1.00 15.40
ATOM   1172  CG  ASN A 150      18.124  18.389  29.562  1.00 15.30
ATOM   1173  OD1 ASN A 150      18.956  19.242  29.307  1.00 14.10
ATOM   1174  ND2 ASN A 150      16.911  18.628  30.035  1.00 17.17
ATOM   1175  N   LEU A 151      21.827  17.876  29.471  1.00 15.04
ATOM   1176  CA  LEU A 151      22.873  18.333  30.357  1.00 15.73
ATOM   1177  C   LEU A 151      22.514  19.660  31.048  1.00 15.23
ATOM   1178  O   LEU A 151      23.235  19.989  31.988  1.00 15.77
ATOM   1179  CB  LEU A 151      24.181  18.442  29.546  1.00 14.38
ATOM   1180  CG  LEU A 151      24.741  17.134  28.985  1.00 14.13
ATOM   1181  CD1 LEU A 151      26.042  17.424  28.227  1.00 14.97
ATOM   1182  CD2 LEU A 151      25.117  16.164  30.067  1.00 13.19
ATOM   1183  N   GLN A 152      21.501  20.323  30.641  1.00 15.70
ATOM   1184  CA  GLN A 152      21.075  21.636  31.100  1.00 17.70
ATOM   1185  C   GLN A 152      20.405  21.695  32.460  1.00 18.95
ATOM   1186  O   GLN A 152      20.583  22.677  33.208  1.00 19.24
ATOM   1187  CB  GLN A 152      20.136  22.295  30.080  1.00 16.95
ATOM   1188  CG  GLN A 152      20.736  22.615  28.745  1.00 22.33
ATOM   1189  CD  GLN A 152      22.187  22.977  28.714  1.00 24.80
ATOM   1190  OE1 GLN A 152      22.556  24.079  29.094  1.00 26.78
ATOM   1191  NE2 GLN A 152      23.056  22.048  28.233  1.00 26.75
ATOM   1192  N   GLU A 153      19.609  20.682  32.753  1.00 18.48
ATOM   1193  CA  GLU A 153      18.878  20.616  34.016  1.00 18.52
ATOM   1194  C   GLU A 153      19.440  19.597  34.937  1.00 16.69
ATOM   1195  O   GLU A 153      19.720  18.433  34.570  1.00 15.14
ATOM   1196  CB  GLU A 153      17.399  20.474  33.718  1.00 23.25
ATOM   1197  CG  GLU A 153      16.509  19.941  34.847  1.00 30.02
ATOM   1198  CD  GLU A 153      16.189  20.941  35.932  1.00 33.02
ATOM   1199  OE1 GLU A 153      16.027  22.136  35.658  1.00 34.38
ATOM   1200  OE2 GLU A 153      16.142  20.378  37.053  1.00 32.94
ATOM   1201  N   PRO A 154      19.648  20.000  36.217  1.00 14.75
ATOM   1202  CA  PRO A 154      20.199  19.123  37.227  1.00 13.27
ATOM   1203  C   PRO A 154      19.383  17.846  37.498  1.00 10.29
ATOM   1204  O   PRO A 154      19.961  16.916  38.020  1.00  8.84
ATOM   1205  CB  PRO A 154      20.385  19.962  38.472  1.00 13.30
ATOM   1206  CG  PRO A 154      19.982  21.340  38.101  1.00 14.81
ATOM   1207  CD  PRO A 154      19.392  21.353  36.719  1.00 13.92
ATOM   1208  N   TYR A 155      18.114  17.869  37.231  1.00 11.01
ATOM   1209  CA  TYR A 155      17.248  16.682  37.404  1.00 11.58
ATOM   1210  C   TYR A 155      17.890  15.514  36.604  1.00 11.98
ATOM   1211  O   TYR A 155      17.998  14.381  37.072  1.00 12.84
ATOM   1212  CB  TYR A 155      15.828  16.994  36.901  1.00 11.85
ATOM   1213  CG  TYR A 155      14.891  15.800  37.045  1.00 13.39
ATOM   1214  CD1 TYR A 155      14.278  15.448  38.249  1.00 15.25
ATOM   1215  CD2 TYR A 155      14.666  14.963  35.943  1.00 15.05
ATOM   1216  CE1 TYR A 155      13.444  14.344  38.365  1.00 15.47
ATOM   1217  CE2 TYR A 155      13.887  13.829  36.039  1.00 15.58
ATOM   1218  CZ  TYR A 155      13.222  13.538  37.219  1.00 16.89
ATOM   1219  OH  TYR A 155      12.449  12.408  37.264  1.00 16.58
ATOM   1220  N   PHE A 156      18.358  15.822  35.402  1.00 11.48
ATOM   1221  CA  PHE A 156      19.025  14.850  34.531  1.00 10.40
ATOM   1222  C   PHE A 156      20.451  14.535  34.896  1.00 10.54
ATOM   1223  O   PHE A 156      20.873  13.357  34.786  1.00 11.46
ATOM   1224  CB  PHE A 156      18.871  15.323  33.083  1.00 10.84
ATOM   1225  CG  PHE A 156      17.477  15.280  32.580  1.00 11.62
ATOM   1226  CD1 PHE A 156      16.629  16.372  32.760  1.00 11.61
ATOM   1227  CD2 PHE A 156      17.009  14.123  31.935  1.00 12.00
ATOM   1228  CE1 PHE A 156      15.320  16.342  32.308  1.00 12.35
ATOM   1229  CE2 PHE A 156      15.691  14.089  31.467  1.00 12.25
ATOM   1230  CZ  PHE A 156      14.836  15.186  31.654  1.00 13.11
ATOM   1231  N   THR A 157      21.264  15.451  35.414  1.00  9.12
ATOM   1232  CA  THR A 157      22.645  15.131  35.740  1.00  9.94
ATOM   1233  C   THR A 157      22.852  14.609  37.127  1.00 10.41
ATOM   1234  O   THR A 157      23.850  13.951  37.406  1.00  9.74
ATOM   1235  CB  THR A 157      23.583  16.361  35.400  1.00 11.30
ATOM   1236  OG1 THR A 157      22.973  17.433  36.183  1.00 12.39
ATOM   1237  CG2 THR A 157      23.492  16.716  33.880  1.00 12.16
ATOM   1238  N   TRP A 158      21.905  14.842  38.023  1.00 11.61
ATOM   1239  CA  TRP A 158      22.009  14.365  39.408  1.00 11.36
ATOM   1240  C   TRP A 158      22.340  12.912  39.581  1.00 11.12
ATOM   1241  O   TRP A 158      23.160  12.605  40.479  1.00 11.34
ATOM   1242  CB  TRP A 158      20.747  14.759  40.209  1.00 13.32
ATOM   1243  CG  TRP A 158      20.935  14.567  41.690  1.00 13.13
ATOM   1244  CD1 TRP A 158      20.348  13.655  42.493  1.00 12.10
ATOM   1245  CD2 TRP A 158      21.806  15.347  42.533  1.00 14.71
ATOM   1246  NE1 TRP A 158      20.770  13.802  43.773  1.00 11.99
ATOM   1247  CE2 TRP A 158      21.645  14.848  43.840  1.00 13.38
ATOM   1248  CE3 TRP A 158      22.694  16.397  42.296  1.00 14.89
ATOM   1249  CZ2 TRP A 158      22.356  15.373  44.930  1.00 13.88
ATOM   1250  CZ3 TRP A 158      23.395  16.916  43.394  1.00 15.67
ATOM   1251  CH2 TRP A 158      23.232  16.418  44.690  1.00 12.99
ATOM   1252  N   PRO A 159      21.734  11.976  38.808  1.00  9.40
ATOM   1253  CA  PRO A 159      22.059  10.552  38.991  1.00  8.77
ATOM   1254  C   PRO A 159      23.529  10.242  39.061  1.00  8.60
ATOM   1255  O   PRO A 159      23.954   9.423  39.896  1.00  8.88
ATOM   1256  CB  PRO A 159      21.293   9.844  37.894  1.00  6.62
ATOM   1257  CG  PRO A 159      20.332  10.803  37.328  1.00  6.54
ATOM   1258  CD  PRO A 159      20.743  12.198  37.775  1.00  7.59
ATOM   1259  N   LEU A 160      24.321  10.862  38.186  1.00  8.72
ATOM   1260  CA  LEU A 160      25.774  10.682  38.116  1.00 10.81
ATOM   1261  C   LEU A 160      26.506  11.425  39.254  1.00 10.33
ATOM   1262  O   LEU A 160      27.379  10.850  39.879  1.00 11.51
ATOM   1263  CB  LEU A 160      26.268  11.162  36.739  1.00  9.76
ATOM   1264  CG  LEU A 160      27.529  10.668  36.108  1.00 12.95
ATOM   1265  CD1 LEU A 160      28.180  11.767  35.264  1.00 12.88
ATOM   1266  CD2 LEU A 160      28.532   9.939  36.951  1.00  9.49
ATOM   1267  N   ILE A 161      26.121  12.677  39.459  1.00 12.49
ATOM   1268  CA  ILE A 161      26.722  13.532  40.504  1.00 13.21
ATOM   1269  C   ILE A 161      26.560  12.922  41.881  1.00 12.93
ATOM   1270  O   ILE A 161      27.507  12.853  42.659  1.00 14.88
ATOM   1271  CB  ILE A 161      26.212  15.015  40.370  1.00 12.87
ATOM   1272  CG1 ILE A 161      26.782  15.617  39.056  1.00 12.94
ATOM   1273  CG2 ILE A 161      26.606  15.917  41.575  1.00 13.89
ATOM   1274  CD1 ILE A 161      25.928  16.825  38.572  1.00 13.89
ATOM   1275  N   ALA A 162      25.392  12.410  42.199  1.00 12.95
ATOM   1276  CA  ALA A 162      25.059  11.771  43.458  1.00 11.99
ATOM   1277  C   ALA A 162      25.578  10.381  43.671  1.00 12.88
ATOM   1278  O   ALA A 162      25.777   9.943  44.829  1.00 13.80
ATOM   1279  CB  ALA A 162      23.513  11.719  43.520  1.00 13.02
ATOM   1280  N   ALA A 163      25.764   9.576  42.641  1.00 13.69
ATOM   1281  CA  ALA A 163      26.220   8.196  42.665  1.00 13.24
ATOM   1282  C   ALA A 163      27.209   7.852  43.764  1.00 14.22
ATOM   1283  O   ALA A 163      26.941   6.944  44.566  1.00 14.26
ATOM   1284  CB  ALA A 163      26.824   7.791  41.282  1.00 12.70
ATOM   1285  N   ASP A 164      28.355   8.523  43.774  1.00 14.59
ATOM   1286  CA  ASP A 164      29.408   8.286  44.739  1.00 15.31
ATOM   1287  C   ASP A 164      29.343   9.067  46.040  1.00 15.74
ATOM   1288  O   ASP A 164      30.369   9.236  46.728  1.00 16.28
ATOM   1289  CB  ASP A 164      30.756   8.500  44.038  1.00 16.25
ATOM   1290  CG  ASP A 164      31.857   7.790  44.810  1.00 17.84
ATOM   1291  OD1 ASP A 164      31.686   6.670  45.288  1.00 18.33
ATOM   1292  OD2 ASP A 164      32.881   8.481  44.921  1.00 19.58
ATOM   1293  N   GLY A 165      28.192   9.499  46.483  1.00 17.37
ATOM   1294  CA  GLY A 165      28.092  10.216  47.770  1.00 16.75
ATOM   1295  C   GLY A 165      27.330  11.485  47.823  1.00 15.61
ATOM   1296  O   GLY A 165      27.112  11.934  48.959  1.00 17.11
ATOM   1297  N   GLY A 166      26.879  12.104  46.784  1.00 15.17
ATOM   1298  CA  GLY A 166      26.118  13.362  46.841  1.00 16.21
ATOM   1299  C   GLY A 166      24.698  13.126  47.284  1.00 16.59
ATOM   1300  O   GLY A 166      24.145  12.045  47.091  1.00 17.18
ATOM   1301  N   TYR A 167      24.088  14.148  47.853  1.00 17.49
ATOM   1302  CA  TYR A 167      22.679  14.144  48.311  1.00 17.71
ATOM   1303  C   TYR A 167      22.265  15.618  48.446  1.00 17.10
ATOM   1304  O   TYR A 167      23.190  16.423  48.586  1.00 17.29
ATOM   1305  CB  TYR A 167      22.453  13.414  49.618  1.00 18.10
ATOM   1306  CG  TYR A 167      23.342  13.851  50.773  1.00 19.82
ATOM   1307  CD1 TYR A 167      22.967  14.898  51.624  1.00 19.06
ATOM   1308  CD2 TYR A 167      24.558  13.205  50.994  1.00 20.68
ATOM   1309  CE1 TYR A 167      23.801  15.278  52.668  1.00 19.02
ATOM   1310  CE2 TYR A 167      25.400  13.566  52.041  1.00 21.32
ATOM   1311  CZ  TYR A 167      24.977  14.629  52.872  1.00 20.28
ATOM   1312  OH  TYR A 167      25.811  15.006  53.876  1.00 22.70
ATOM   1313  N   ALA A 168      21.001  15.924  48.373  1.00 16.91
ATOM   1314  CA  ALA A 168      20.500  17.293  48.465  1.00 17.80
ATOM   1315  C   ALA A 168      20.563  17.715  49.951  1.00 19.84
ATOM   1316  O   ALA A 168      21.390  18.563  50.290  1.00 20.16
ATOM   1317  CB  ALA A 168      19.149  17.499  47.843  1.00 15.78
ATOM   1318  N   PHE A 169      19.780  17.034  50.764  1.00 21.06
ATOM   1319  CA  PHE A 169      19.661  17.254  52.213  1.00 21.29
ATOM   1320  C   PHE A 169      19.641  15.945  52.974  1.00 22.35
ATOM   1321  O   PHE A 169      18.880  15.009  52.623  1.00 23.65
ATOM   1322  CB  PHE A 169      18.421  18.093  52.508  1.00 19.40
ATOM   1323  CG  PHE A 169      18.300  19.428  51.888  1.00 18.77
ATOM   1324  CD1 PHE A 169      18.895  20.550  52.510  1.00 18.71
ATOM   1325  CD2 PHE A 169      17.581  19.625  50.722  1.00 18.67
ATOM   1326  CE1 PHE A 169      18.770  21.799  51.949  1.00 18.12
ATOM   1327  CE2 PHE A 169      17.466  20.881  50.128  1.00 19.05
ATOM   1328  CZ  PHE A 169      18.058  21.993  50.767  1.00 18.92
ATOM   1329  N   LYS A 170      20.435  15.833  54.003  1.00 23.99
ATOM   1330  CA  LYS A 170      20.480  14.613  54.809  1.00 26.97
ATOM   1331  C   LYS A 170      19.116  14.325  55.427  1.00 29.79
ATOM   1332  O   LYS A 170      18.500  15.169  56.069  1.00 29.89
ATOM   1333  CB  LYS A 170      21.549  14.668  55.868  1.00 26.11
ATOM   1334  CG  LYS A 170      21.599  13.400  56.693  1.00 28.09
ATOM   1335  CD  LYS A 170      21.849  12.165  55.846  1.00 28.21
ATOM   1336  CE  LYS A 170      23.230  11.616  56.127  1.00 29.44
ATOM   1337  NZ  LYS A 170      24.215  12.559  55.567  1.00 29.99
ATOM   1338  N   TYR A 171      18.628  13.110  55.198  1.00 32.90
ATOM   1339  CA  TYR A 171      17.315  12.696  55.736  1.00 36.04
ATOM   1340  C   TYR A 171      17.578  11.536  56.693  1.00 39.48
ATOM   1341  O   TYR A 171      18.366  10.633  56.341  1.00 39.88
ATOM   1342  CB  TYR A 171      16.339  12.332  54.642  1.00 34.78
ATOM   1343  CG  TYR A 171      14.984  11.783  55.031  1.00 34.43
ATOM   1344  CD1 TYR A 171      14.834  10.489  55.495  1.00 34.21
ATOM   1345  CD2 TYR A 171      13.825  12.545  54.881  1.00 34.87
ATOM   1346  CE1 TYR A 171      13.599   9.972  55.840  1.00 35.22
ATOM   1347  CE2 TYR A 171      12.562  12.056  55.177  1.00 35.73
ATOM   1348  CZ  TYR A 171      12.462  10.756  55.670  1.00 36.09
ATOM   1349  OH  TYR A 171      11.254  10.211  56.006  1.00 36.60
ATOM   1350  N   GLU A 172      16.934  11.604  57.857  1.00 44.47
ATOM   1351  CA  GLU A 172      17.167  10.498  58.813  1.00 49.21
ATOM   1352  C   GLU A 172      16.096  10.267  59.829  1.00 49.97
ATOM   1353  O   GLU A 172      16.414   9.656  60.892  1.00 51.76
ATOM   1354  CB  GLU A 172      18.527  10.706  59.528  1.00 51.46
ATOM   1355  CG  GLU A 172      19.280   9.402  59.833  1.00 55.40
ATOM   1356  CD  GLU A 172      20.753   9.359  59.580  1.00 57.33
ATOM   1357  OE1 GLU A 172      21.312  10.460  59.810  1.00 58.65
ATOM   1358  OE2 GLU A 172      21.374   8.357  59.209  1.00 58.52
ATOM   1359  N   ASN A 173      14.847  10.636  59.550  1.00 50.35
ATOM   1360  CA  ASN A 173      13.779  10.455  60.550  1.00 50.40
ATOM   1361  C   ASN A 173      12.470  11.095  60.128  1.00 49.22
ATOM   1362  O   ASN A 173      11.776  11.661  61.019  1.00 50.26
ATOM   1363  CB  ASN A 173      14.276  11.172  61.856  1.00 52.78
ATOM   1364  CG  ASN A 173      14.520  12.658  61.536  1.00 54.80
ATOM   1365  OD1 ASN A 173      15.110  13.009  60.491  1.00 55.59
ATOM   1366  ND2 ASN A 173      14.037  13.533  62.424  1.00 55.58
ATOM   1367  N   GLY A 174      12.142  11.045  58.862  1.00 47.20
ATOM   1368  CA  GLY A 174      10.890  11.684  58.383  1.00 44.55
ATOM   1369  C   GLY A 174      11.131  13.200  58.325  1.00 42.58
ATOM   1370  O   GLY A 174      10.224  13.992  58.000  1.00 43.00
ATOM   1371  N   LYS A 175      12.380  13.510  58.624  1.00 39.94
ATOM   1372  CA  LYS A 175      12.883  14.878  58.694  1.00 37.51
ATOM   1373  C   LYS A 175      14.243  15.041  58.013  1.00 34.72
ATOM   1374  O   LYS A 175      15.184  14.249  58.101  1.00 32.35
ATOM   1375  CB  LYS A 175      12.930  15.308  60.165  1.00 38.27
ATOM   1376  CG  LYS A 175      13.652  16.584  60.497  1.00 40.52
ATOM   1377  CD  LYS A 175      12.840  17.831  60.261  1.00 42.96
ATOM   1378  CE  LYS A 175      13.484  19.101  60.792  1.00 44.35
ATOM   1379  NZ  LYS A 175      13.641  19.053  62.268  1.00 44.31
ATOM   1380  N   TYR A 176      14.292  16.169  57.325  1.00 33.09
ATOM   1381  CA  TYR A 176      15.429  16.655  56.568  1.00 32.62
ATOM   1382  C   TYR A 176      16.222  17.683  57.393  1.00 33.52
ATOM   1383  O   TYR A 176      15.596  18.648  57.868  1.00 34.94
ATOM   1384  CB  TYR A 176      14.958  17.346  55.258  1.00 29.73
ATOM   1385  CG  TYR A 176      14.541  16.361  54.188  1.00 28.21
ATOM   1386  CD1 TYR A 176      15.502  15.582  53.528  1.00 26.14
ATOM   1387  CD2 TYR A 176      13.193  16.193  53.849  1.00 26.42
ATOM   1388  CE1 TYR A 176      15.103  14.687  52.538  1.00 25.94
ATOM   1389  CE2 TYR A 176      12.779  15.280  52.896  1.00 25.03
ATOM   1390  CZ  TYR A 176      13.754  14.541  52.221  1.00 25.69
ATOM   1391  OH  TYR A 176      13.343  13.626  51.286  1.00 24.31
ATOM   1392  N   ASP A 177      17.511  17.461  57.500  1.00 33.51
ATOM   1393  CA  ASP A 177      18.452  18.371  58.188  1.00 32.65
ATOM   1394  C   ASP A 177      18.921  19.366  57.112  1.00 33.06
ATOM   1395  O   ASP A 177      19.780  18.993  56.293  1.00 33.42
ATOM   1396  CB  ASP A 177      19.584  17.601  58.835  1.00 31.30
ATOM   1397  CG  ASP A 177      20.617  18.566  59.440  1.00 31.75
ATOM   1398  OD1 ASP A 177      20.392  19.789  59.378  1.00 28.83
ATOM   1399  OD2 ASP A 177      21.626  18.005  59.938  1.00 31.17
ATOM   1400  N   ILE A 178      18.369  20.561  57.114  1.00 32.64
ATOM   1401  CA  ILE A 178      18.697  21.543  56.088  1.00 34.13
ATOM   1402  C   ILE A 178      20.066  22.174  56.129  1.00 33.35
ATOM   1403  O   ILE A 178      20.410  23.015  55.264  1.00 33.56
ATOM   1404  CB  ILE A 178      17.515  22.566  55.974  1.00 36.18
ATOM   1405  CG1 ILE A 178      17.614  23.630  57.100  1.00 37.48
ATOM   1406  CG2 ILE A 178      16.137  21.850  55.959  1.00 36.92
ATOM   1407  CD1 ILE A 178      16.997  25.002  56.664  1.00 37.41
ATOM   1408  N   LYS A 179      20.874  21.790  57.079  1.00 33.40
ATOM   1409  CA  LYS A 179      22.233  22.288  57.234  1.00 33.83
ATOM   1410  C   LYS A 179      23.204  21.156  56.912  1.00 33.07
ATOM   1411  O   LYS A 179      24.403  21.311  57.101  1.00 33.75
ATOM   1412  CB  LYS A 179      22.562  22.902  58.576  1.00 36.08
ATOM   1413  CG  LYS A 179      22.001  24.312  58.774  1.00 38.64
ATOM   1414  CD  LYS A 179      22.914  25.423  58.294  1.00 41.63
ATOM   1415  CE  LYS A 179      22.485  26.054  56.989  1.00 43.18
ATOM   1416  NZ  LYS A 179      21.351  26.997  57.156  1.00 43.84
ATOM   1417  N   ASP A 180      22.632  20.066  56.439  1.00 31.51
ATOM   1418  CA  ASP A 180      23.388  18.880  56.006  1.00 29.61
ATOM   1419  C   ASP A 180      23.036  18.746  54.505  1.00 28.20
ATOM   1420  O   ASP A 180      22.020  18.179  54.112  1.00 26.92
ATOM   1421  CB  ASP A 180      23.121  17.663  56.851  1.00 30.30
ATOM   1422  CG  ASP A 180      24.228  16.639  56.827  1.00 32.26
ATOM   1423  OD1 ASP A 180      25.213  16.776  56.077  1.00 33.77
ATOM   1424  OD2 ASP A 180      24.159  15.646  57.590  1.00 34.09
ATOM   1425  N   VAL A 181      23.874  19.401  53.748  1.00 27.89
ATOM   1426  CA  VAL A 181      23.793  19.476  52.260  1.00 26.79
ATOM   1427  C   VAL A 181      24.955  18.696  51.687  1.00 26.07
ATOM   1428  O   VAL A 181      26.070  18.786  52.261  1.00 25.59
ATOM   1429  CB  VAL A 181      23.713  20.947  51.824  1.00 26.44
ATOM   1430  CG1 VAL A 181      23.787  21.136  50.326  1.00 25.18
ATOM   1431  CG2 VAL A 181      22.421  21.547  52.385  1.00 26.79
ATOM   1432  N   GLY A 182      24.698  17.939  50.623  1.00 24.89
ATOM   1433  CA  GLY A 182      25.758  17.117  50.025  1.00 24.23
ATOM   1434  C   GLY A 182      26.172  17.399  48.599  1.00 24.46
ATOM   1435  O   GLY A 182      26.406  16.454  47.809  1.00 21.84
ATOM   1436  N   VAL A 183      26.292  18.667  48.219  1.00 25.37
ATOM   1437  CA  VAL A 183      26.681  19.000  46.850  1.00 27.16
ATOM   1438  C   VAL A 183      28.173  19.288  46.730  1.00 28.39
ATOM   1439  O   VAL A 183      28.689  19.317  45.601  1.00 28.59
ATOM   1440  CB  VAL A 183      25.770  20.080  46.236  1.00 26.62
ATOM   1441  CG1 VAL A 183      24.320  19.941  46.663  1.00 26.36
ATOM   1442  CG2 VAL A 183      26.293  21.465  46.358  1.00 26.86
ATOM   1443  N   ASP A 184      28.851  19.462  47.851  1.00 29.34
ATOM   1444  CA  ASP A 184      30.276  19.802  47.814  1.00 30.76
ATOM   1445  C   ASP A 184      31.147  18.688  48.305  1.00 29.86
ATOM   1446  O   ASP A 184      32.380  18.900  48.459  1.00 32.09
ATOM   1447  CB  ASP A 184      30.481  21.108  48.601  1.00 34.92
ATOM   1448  CG  ASP A 184      31.896  21.624  48.532  1.00 39.95
ATOM   1449  OD1 ASP A 184      32.569  21.276  47.521  1.00 43.41
ATOM   1450  OD2 ASP A 184      32.383  22.319  49.443  1.00 42.82
ATOM   1451  N   ASN A 185      30.589  17.533  48.595  1.00 28.38
ATOM   1452  CA  ASN A 185      31.494  16.449  49.088  1.00 26.79
ATOM   1453  C   ASN A 185      32.298  15.858  47.914  1.00 26.26
ATOM   1454  O   ASN A 185      32.169  16.210  46.736  1.00 25.59
ATOM   1455  CB  ASN A 185      30.770  15.515  50.007  1.00 26.35
ATOM   1456  CG  ASN A 185      29.614  14.740  49.407  1.00 25.21
ATOM   1457  OD1 ASN A 185      29.674  14.367  48.237  1.00 24.07
ATOM   1458  ND2 ASN A 185      28.634  14.499  50.260  1.00 24.38
ATOM   1459  N   ALA A 186      33.200  14.970  48.291  1.00 24.85
ATOM   1460  CA  ALA A 186      34.111  14.294  47.379  1.00 24.54
ATOM   1461  C   ALA A 186      33.280  13.489  46.374  1.00 24.70
ATOM   1462  O   ALA A 186      33.599  13.434  45.170  1.00 25.94
ATOM   1463  CB  ALA A 186      35.051  13.424  48.193  1.00 23.63
ATOM   1464  N   GLY A 187      32.198  12.939  46.890  1.00 23.83
ATOM   1465  CA  GLY A 187      31.234  12.136  46.139  1.00 21.47
ATOM   1466  C   GLY A 187      30.754  12.901  44.917  1.00 20.59
ATOM   1467  O   GLY A 187      30.965  12.443  43.787  1.00 19.50
ATOM   1468  N   ALA A 188      30.109  14.037  45.168  1.00 19.03
ATOM   1469  CA  ALA A 188      29.578  14.903  44.125  1.00 17.39
ATOM   1470  C   ALA A 188      30.715  15.401  43.226  1.00 18.21
ATOM   1471  O   ALA A 188      30.568  15.554  42.012  1.00 16.91
ATOM   1472  CB  ALA A 188      28.858  16.090  44.738  1.00 17.36
ATOM   1473  N   LYS A 189      31.842  15.680  43.873  1.00 18.95
ATOM   1474  CA  LYS A 189      33.031  16.151  43.173  1.00 20.84
ATOM   1475  C   LYS A 189      33.491  15.080  42.176  1.00 20.74
ATOM   1476  O   LYS A 189      33.781  15.429  41.012  1.00 21.86
ATOM   1477  CB  LYS A 189      34.179  16.437  44.125  1.00 24.23
ATOM   1478  CG  LYS A 189      34.897  17.750  43.858  1.00 29.09
ATOM   1479  CD  LYS A 189      34.344  18.892  44.710  1.00 31.68
ATOM   1480  CE  LYS A 189      34.794  18.814  46.156  1.00 33.18
ATOM   1481  NZ  LYS A 189      35.921  17.848  46.291  1.00 34.01
ATOM   1482  N   ALA A 190      33.558  13.835  42.625  1.00 19.77
ATOM   1483  CA  ALA A 190      33.971  12.738  41.717  1.00 19.19
ATOM   1484  C   ALA A 190      33.048  12.685  40.500  1.00 18.44
ATOM   1485  O   ALA A 190      33.534  12.631  39.362  1.00 18.71
ATOM   1486  CB  ALA A 190      34.070  11.399  42.406  1.00 17.71
ATOM   1487  N   GLY A 191      31.753  12.718  40.706  1.00 17.24
ATOM   1488  CA  GLY A 191      30.731  12.670  39.682  1.00 15.61
ATOM   1489  C   GLY A 191      30.708  13.735  38.624  1.00 15.65
ATOM   1490  O   GLY A 191      30.599  13.486  37.414  1.00 12.88
ATOM   1491  N   LEU A 192      30.772  15.003  39.065  1.00 15.56
ATOM   1492  CA  LEU A 192      30.775  16.173  38.204  1.00 15.55
ATOM   1493  C   LEU A 192      32.065  16.191  37.389  1.00 14.85
ATOM   1494  O   LEU A 192      32.057  16.600  36.247  1.00 14.73
ATOM   1495  CB  LEU A 192      30.604  17.468  39.048  1.00 15.57
ATOM   1496  CG  LEU A 192      30.428  18.735  38.253  1.00 17.18
ATOM   1497  CD1 LEU A 192      29.222  18.648  37.306  1.00 16.10
ATOM   1498  CD2 LEU A 192      30.191  19.968  39.124  1.00 17.95
ATOM   1499  N   THR A 193      33.132  15.779  38.020  1.00 16.89
ATOM   1500  CA  THR A 193      34.437  15.716  37.345  1.00 18.99
ATOM   1501  C   THR A 193      34.296  14.726  36.183  1.00 19.55
ATOM   1502  O   THR A 193      34.701  15.066  35.081  1.00 22.12
ATOM   1503  CB  THR A 193      35.642  15.319  38.241  1.00 19.96
ATOM   1504  OG1 THR A 193      35.860  16.381  39.198  1.00 20.48
ATOM   1505  CG2 THR A 193      36.939  15.039  37.428  1.00 22.45
ATOM   1506  N   PHE A 194      33.750  13.560  36.476  1.00 19.50
ATOM   1507  CA  PHE A 194      33.561  12.550  35.390  1.00 18.96
ATOM   1508  C   PHE A 194      32.741  13.145  34.255  1.00 18.83
ATOM   1509  O   PHE A 194      33.042  12.922  33.046  1.00 18.51
ATOM   1510  CB  PHE A 194      32.955  11.255  35.926  1.00 19.76
ATOM   1511  CG  PHE A 194      32.937  10.153  34.891  1.00 20.43
ATOM   1512  CD1 PHE A 194      34.054   9.342  34.735  1.00 21.47
ATOM   1513  CD2 PHE A 194      31.819   9.979  34.083  1.00 20.94
ATOM   1514  CE1 PHE A 194      34.042   8.327  33.756  1.00 22.96
ATOM   1515  CE2 PHE A 194      31.789   8.975  33.120  1.00 21.95
ATOM   1516  CZ  PHE A 194      32.906   8.159  32.956  1.00 22.09
ATOM   1517  N   LEU A 195      31.699  13.889  34.602  1.00 17.66
ATOM   1518  CA  LEU A 195      30.828  14.497  33.598  1.00 17.44
ATOM   1519  C   LEU A 195      31.576  15.507  32.733  1.00 17.92
ATOM   1520  O   LEU A 195      31.414  15.547  31.507  1.00 16.60
ATOM   1521  CB  LEU A 195      29.581  15.053  34.290  1.00 17.61
ATOM   1522  CG  LEU A 195      28.659  15.943  33.487  1.00 18.81
ATOM   1523  CD1 LEU A 195      27.996  15.108  32.390  1.00 21.32
ATOM   1524  CD2 LEU A 195      27.554  16.518  34.387  1.00 18.35
ATOM   1525  N   VAL A 196      32.349  16.344  33.402  1.00 18.31
ATOM   1526  CA  VAL A 196      33.113  17.413  32.762  1.00 18.00
ATOM   1527  C   VAL A 196      34.112  16.791  31.787  1.00 18.30
ATOM   1528  O   VAL A 196      34.187  17.331  30.677  1.00 18.71
ATOM   1529  CB  VAL A 196      33.711  18.372  33.786  1.00 19.94
ATOM   1530  CG1 VAL A 196      34.687  19.374  33.151  1.00 19.22
ATOM   1531  CG2 VAL A 196      32.604  19.138  34.530  1.00 18.06
ATOM   1532  N   ASP A 197      34.766  15.754  32.200  1.00 19.58
ATOM   1533  CA  ASP A 197      35.744  15.007  31.397  1.00 23.20
ATOM   1534  C   ASP A 197      35.075  14.448  30.116  1.00 23.84
ATOM   1535  O   ASP A 197      35.772  14.241  29.107  1.00 24.40
ATOM   1536  CB  ASP A 197      36.486  13.923  32.150  1.00 25.66
ATOM   1537  CG  ASP A 197      37.531  14.396  33.132  1.00 30.57
ATOM   1538  OD1 ASP A 197      37.860  15.591  33.213  1.00 33.33
ATOM   1539  OD2 ASP A 197      38.073  13.541  33.879  1.00 32.79
ATOM   1540  N   LEU A 198      33.793  14.169  30.180  1.00 23.64
ATOM   1541  CA  LEU A 198      33.050  13.637  29.065  1.00 23.94
ATOM   1542  C   LEU A 198      32.940  14.694  27.977  1.00 24.01
ATOM   1543  O   LEU A 198      33.112  14.337  26.820  1.00 24.28
ATOM   1544  CB  LEU A 198      31.659  13.144  29.452  1.00 24.54
ATOM   1545  CG  LEU A 198      31.557  11.789  30.120  1.00 25.14
ATOM   1546  CD1 LEU A 198      30.158  11.622  30.708  1.00 25.81
ATOM   1547  CD2 LEU A 198      31.811  10.721  29.056  1.00 25.27
ATOM   1548  N   ILE A 199      32.612  15.894  28.419  1.00 24.14
ATOM   1549  CA  ILE A 199      32.411  17.022  27.534  1.00 25.03
ATOM   1550  C   ILE A 199      33.716  17.521  26.900  1.00 26.00
ATOM   1551  O   ILE A 199      33.716  17.852  25.712  1.00 25.25
ATOM   1552  CB  ILE A 199      31.624  18.181  28.224  1.00 24.36
ATOM   1553  CG1 ILE A 199      30.273  17.685  28.769  1.00 24.42
ATOM   1554  CG2 ILE A 199      31.408  19.376  27.240  1.00 25.31
ATOM   1555  CD1 ILE A 199      29.541  18.723  29.686  1.00 23.39
ATOM   1556  N   LYS A 200      34.756  17.589  27.703  1.00 27.71
ATOM   1557  CA  LYS A 200      36.046  18.099  27.196  1.00 30.12
ATOM   1558  C   LYS A 200      36.733  17.089  26.288  1.00 30.61
ATOM   1559  O   LYS A 200      37.479  17.481  25.361  1.00 31.70
ATOM   1560  CB  LYS A 200      36.904  18.674  28.253  1.00 30.62
ATOM   1561  CG  LYS A 200      37.654  17.758  29.193  1.00 34.30
ATOM   1562  CD  LYS A 200      38.465  18.631  30.167  1.00 37.95
ATOM   1563  CE  LYS A 200      39.174  17.818  31.234  1.00 40.14
ATOM   1564  NZ  LYS A 200      38.577  18.129  32.583  1.00 42.09
ATOM   1565  N   ASN A 201      36.460  15.817  26.501  1.00 29.69
ATOM   1566  CA  ASN A 201      37.005  14.719  25.700  1.00 27.91
ATOM   1567  C   ASN A 201      36.082  14.428  24.499  1.00 26.86
ATOM   1568  O   ASN A 201      36.252  13.408  23.819  1.00 26.25
ATOM   1569  CB  ASN A 201      37.303  13.498  26.512  1.00 27.82
ATOM   1570  CG  ASN A 201      38.464  13.697  27.450  1.00 27.49
ATOM   1571  OD1 ASN A 201      38.336  13.294  28.608  1.00 30.62
ATOM   1572  ND2 ASN A 201      39.519  14.275  26.934  1.00 28.47
ATOM   1573  N   LYS A 202      35.166  15.318  24.313  1.00 25.76
ATOM   1574  CA  LYS A 202      34.225  15.366  23.237  1.00 26.75
ATOM   1575  C   LYS A 202      33.302  14.196  23.055  1.00 26.02
ATOM   1576  O   LYS A 202      32.704  14.062  21.972  1.00 26.47
ATOM   1577  CB  LYS A 202      34.978  15.712  21.925  1.00 29.12
ATOM   1578  CG  LYS A 202      35.529  17.171  21.991  1.00 29.69
ATOM   1579  CD  LYS A 202      34.377  18.153  21.853  1.00 34.06
ATOM   1580  CE  LYS A 202      33.823  18.835  23.065  1.00 35.49
ATOM   1581  NZ  LYS A 202      32.539  18.306  23.601  1.00 32.86
ATOM   1582  N   HIS A 203      33.097  13.432  24.102  1.00 25.13
ATOM   1583  CA  HIS A 203      32.189  12.285  24.116  1.00 24.08
ATOM   1584  C   HIS A 203      30.761  12.784  24.276  1.00 25.02
ATOM   1585  O   HIS A 203      29.835  12.005  24.053  1.00 26.32
ATOM   1586  CB  HIS A 203      32.440  11.281  25.247  1.00 21.66
ATOM   1587  CG  HIS A 203      33.762  10.624  25.066  1.00 19.73
ATOM   1588  ND1 HIS A 203      34.782  10.645  25.960  1.00 20.47
ATOM   1589  CD2 HIS A 203      34.210   9.932  23.992  1.00 19.78
ATOM   1590  CE1 HIS A 203      35.822   9.971  25.478  1.00 19.81
ATOM   1591  NE2 HIS A 203      35.481   9.523  24.281  1.00 21.23
ATOM   1592  N   MET A 204      30.676  14.035  24.616  1.00 26.30
ATOM   1593  CA  MET A 204      29.427  14.794  24.886  1.00 26.93
ATOM   1594  C   MET A 204      29.619  16.287  24.645  1.00 26.67
ATOM   1595  O   MET A 204      30.701  16.812  24.884  1.00 26.10
ATOM   1596  CB  MET A 204      29.161  14.466  26.374  1.00 26.96
ATOM   1597  CG  MET A 204      27.744  14.531  26.709  1.00 28.62
ATOM   1598  SD  MET A 204      27.273  13.176  27.890  1.00 29.02
ATOM   1599  CE  MET A 204      25.601  13.008  27.191  1.00 29.70
ATOM   1600  N   ASN A 205      28.629  16.974  24.146  1.00 27.75
ATOM   1601  CA  ASN A 205      28.534  18.390  23.852  1.00 28.54
ATOM   1602  C   ASN A 205      27.842  19.102  25.031  1.00 28.13
ATOM   1603  O   ASN A 205      26.777  18.651  25.460  1.00 26.56
ATOM   1604  CB  ASN A 205      27.721  18.730  22.600  1.00 31.75
ATOM   1605  CG  ASN A 205      28.517  18.519  21.327  1.00 35.31
ATOM   1606  OD1 ASN A 205      28.511  17.385  20.811  1.00 38.29
ATOM   1607  ND2 ASN A 205      29.186  19.570  20.869  1.00 37.63
ATOM   1608  N   ALA A 206      28.450  20.218  25.421  1.00 27.72
ATOM   1609  CA  ALA A 206      27.896  20.958  26.568  1.00 27.13
ATOM   1610  C   ALA A 206      26.552  21.573  26.301  1.00 26.67
ATOM   1611  O   ALA A 206      25.858  21.976  27.257  1.00 27.91
ATOM   1612  CB  ALA A 206      28.898  21.960  27.092  1.00 27.16
ATOM   1613  N   ASP A 207      26.123  21.657  25.055  1.00 26.81
ATOM   1614  CA  ASP A 207      24.828  22.286  24.762  1.00 26.50
ATOM   1615  C   ASP A 207      23.681  21.324  24.512  1.00 24.09
ATOM   1616  O   ASP A 207      22.626  21.782  24.075  1.00 22.02
ATOM   1617  CB  ASP A 207      25.015  23.334  23.667  1.00 30.17
ATOM   1618  CG  ASP A 207      25.252  22.760  22.293  1.00 33.03
ATOM   1619  OD1 ASP A 207      26.003  21.794  22.065  1.00 35.15
ATOM   1620  OD2 ASP A 207      24.617  23.347  21.382  1.00 35.71
ATOM   1621  N   THR A 208      23.874  20.065  24.834  1.00 22.68
ATOM   1622  CA  THR A 208      22.788  19.064  24.652  1.00 21.08
ATOM   1623  C   THR A 208      21.660  19.325  25.658  1.00 19.11
ATOM   1624  O   THR A 208      21.864  19.329  26.864  1.00 18.04
ATOM   1625  CB  THR A 208      23.370  17.593  24.746  1.00 20.07
ATOM   1626  OG1 THR A 208      24.476  17.523  23.799  1.00 18.62
ATOM   1627  CG2 THR A 208      22.325  16.510  24.444  1.00 19.58
ATOM   1628  N   ASP A 209      20.478  19.548  25.156  1.00 18.88
ATOM   1629  CA  ASP A 209      19.281  19.796  25.961  1.00 18.71
ATOM   1630  C   ASP A 209      18.307  18.638  25.779  1.00 17.98
ATOM   1631  O   ASP A 209      18.676  17.607  25.207  1.00 18.33
ATOM   1632  CB  ASP A 209      18.667  21.152  25.706  1.00 21.00
ATOM   1633  CG  ASP A 209      18.243  21.399  24.287  1.00 22.77
ATOM   1634  OD1 ASP A 209      18.153  20.424  23.522  1.00 25.04
ATOM   1635  OD2 ASP A 209      17.987  22.527  23.865  1.00 26.54
ATOM   1636  N   TYR A 210      17.092  18.820  26.248  1.00 16.94
ATOM   1637  CA  TYR A 210      16.043  17.801  26.188  1.00 15.78
ATOM   1638  C   TYR A 210      15.679  17.412  24.758  1.00 15.91
ATOM   1639  O   TYR A 210      15.613  16.225  24.448  1.00 14.92
ATOM   1640  CB  TYR A 210      14.794  18.181  26.976  1.00 13.93
ATOM   1641  CG  TYR A 210      13.799  17.055  27.169  1.00 13.30
ATOM   1642  CD1 TYR A 210      13.891  16.202  28.256  1.00 12.88
ATOM   1643  CD2 TYR A 210      12.761  16.839  26.253  1.00 13.39
ATOM   1644  CE1 TYR A 210      12.964  15.171  28.442  1.00 12.97
ATOM   1645  CE2 TYR A 210      11.856  15.791  26.417  1.00 13.10
ATOM   1646  CZ  TYR A 210      11.954  14.962  27.525  1.00 11.84
ATOM   1647  OH  TYR A 210      11.100  13.948  27.724  1.00 13.43
ATOM   1648  N   SER A 211      15.415  18.411  23.964  1.00 17.20
ATOM   1649  CA  SER A 211      15.032  18.279  22.584  1.00 19.75
ATOM   1650  C   SER A 211      16.090  17.618  21.707  1.00 20.33
ATOM   1651  O   SER A 211      15.731  16.778  20.881  1.00 21.55
ATOM   1652  CB  SER A 211      14.673  19.640  21.996  1.00 22.40
ATOM   1653  OG  SER A 211      13.444  20.051  22.588  1.00 29.57
ATOM   1654  N   ILE A 212      17.312  18.050  21.860  1.00 20.28
ATOM   1655  CA  ILE A 212      18.440  17.548  21.092  1.00 20.40
ATOM   1656  C   ILE A 212      18.681  16.075  21.393  1.00 20.05
ATOM   1657  O   ILE A 212      18.827  15.317  20.411  1.00 20.90
ATOM   1658  CB  ILE A 212      19.730  18.404  21.296  1.00 21.44
ATOM   1659  CG1 ILE A 212      19.540  19.787  20.608  1.00 22.27
ATOM   1660  CG2 ILE A 212      21.058  17.725  20.877  1.00 20.55
ATOM   1661  CD1 ILE A 212      20.734  20.763  20.876  1.00 22.87
ATOM   1662  N   ALA A 213      18.783  15.675  22.644  1.00 17.66
ATOM   1663  CA  ALA A 213      19.040  14.267  22.971  1.00 16.04
ATOM   1664  C   ALA A 213      17.917  13.341  22.518  1.00 16.20
ATOM   1665  O   ALA A 213      18.148  12.171  22.141  1.00 16.81
ATOM   1666  CB  ALA A 213      19.335  14.115  24.441  1.00 14.50
ATOM   1667  N   GLU A 214      16.708  13.822  22.628  1.00 15.92
ATOM   1668  CA  GLU A 214      15.512  13.113  22.293  1.00 17.90
ATOM   1669  C   GLU A 214      15.426  12.826  20.780  1.00 18.84
ATOM   1670  O   GLU A 214      15.063  11.718  20.418  1.00 19.35
ATOM   1671  CB  GLU A 214      14.208  13.860  22.600  1.00 18.19
ATOM   1672  CG  GLU A 214      12.975  12.960  22.647  1.00 20.89
ATOM   1673  CD  GLU A 214      11.678  13.721  22.761  1.00 22.89
ATOM   1674  OE1 GLU A 214      11.552  14.859  22.407  1.00 23.94
ATOM   1675  OE2 GLU A 214      10.784  13.050  23.309  1.00 26.56
ATOM   1676  N   ALA A 215      15.705  13.814  19.986  1.00 18.47
ATOM   1677  CA  ALA A 215      15.662  13.715  18.528  1.00 17.70
ATOM   1678  C   ALA A 215      16.776  12.765  18.080  1.00 17.27
ATOM   1679  O   ALA A 215      16.514  11.956  17.160  1.00 17.64
ATOM   1680  CB  ALA A 215      15.781  15.068  17.883  1.00 17.64
ATOM   1681  N   ALA A 216      17.896  12.867  18.721  1.00 15.71
ATOM   1682  CA  ALA A 216      19.080  12.067  18.429  1.00 15.25
ATOM   1683  C   ALA A 216      18.832  10.596  18.667  1.00 14.88
ATOM   1684  O   ALA A 216      19.206   9.745  17.821  1.00 14.32
ATOM   1685  CB  ALA A 216      20.312  12.616  19.123  1.00 14.26
ATOM   1686  N   PHE A 217      18.236  10.281  19.820  1.00 14.13
ATOM   1687  CA  PHE A 217      17.906   8.884  20.120  1.00 13.17
ATOM   1688  C   PHE A 217      16.837   8.362  19.144  1.00 13.17
ATOM   1689  O   PHE A 217      16.913   7.206  18.678  1.00 14.91
ATOM   1690  CB  PHE A 217      17.367   8.714  21.561  1.00 14.03
ATOM   1691  CG  PHE A 217      17.271   7.249  21.912  1.00 11.92
ATOM   1692  CD1 PHE A 217      18.396   6.498  22.200  1.00  8.72
ATOM   1693  CD2 PHE A 217      15.995   6.651  21.910  1.00 12.51
ATOM   1694  CE1 PHE A 217      18.304   5.166  22.477  1.00  8.35
ATOM   1695  CE2 PHE A 217      15.887   5.298  22.236  1.00 10.76
ATOM   1696  CZ  PHE A 217      17.039   4.572  22.514  1.00  8.61
ATOM   1697  N   ASN A 218      15.839   9.148  18.886  1.00 13.25
ATOM   1698  CA  ASN A 218      14.719   8.807  18.029  1.00 15.13
ATOM   1699  C   ASN A 218      15.074   8.684  16.556  1.00 16.55
ATOM   1700  O   ASN A 218      14.333   8.018  15.796  1.00 17.27
ATOM   1701  CB  ASN A 218      13.520   9.658  18.358  1.00 16.37
ATOM   1702  CG  ASN A 218      12.913   9.433  19.745  1.00 17.31
ATOM   1703  OD1 ASN A 218      11.943  10.149  20.064  1.00 20.49
ATOM   1704  ND2 ASN A 218      13.403   8.564  20.587  1.00 17.07
ATOM   1705  N   LYS A 219      16.168   9.254  16.143  1.00 17.40
ATOM   1706  CA  LYS A 219      16.693   9.199  14.788  1.00 17.52
ATOM   1707  C   LYS A 219      17.741   8.112  14.651  1.00 18.41
ATOM   1708  O   LYS A 219      18.372   7.912  13.598  1.00 19.19
ATOM   1709  CB  LYS A 219      17.278  10.550  14.337  1.00 17.67
ATOM   1710  CG  LYS A 219      16.130  11.496  13.996  1.00 19.09
ATOM   1711  CD  LYS A 219      16.530  12.840  13.478  1.00 22.26
ATOM   1712  CE  LYS A 219      17.505  13.587  14.331  1.00 23.69
ATOM   1713  NZ  LYS A 219      18.330  14.568  13.597  1.00 23.85
ATOM   1714  N   GLY A 220      17.941   7.372  15.722  1.00 18.43
ATOM   1715  CA  GLY A 220      18.925   6.286  15.770  1.00 18.89
ATOM   1716  C   GLY A 220      20.352   6.740  15.642  1.00 19.15
ATOM   1717  O   GLY A 220      21.241   5.926  15.340  1.00 18.82
ATOM   1718  N   GLU A 221      20.616   8.021  15.897  1.00 18.90
ATOM   1719  CA  GLU A 221      21.966   8.582  15.825  1.00 17.37
ATOM   1720  C   GLU A 221      22.804   8.282  17.043  1.00 16.08
ATOM   1721  O   GLU A 221      24.028   8.184  16.977  1.00 16.54
ATOM   1722  CB  GLU A 221      21.971  10.088  15.625  1.00 18.30
ATOM   1723  CG  GLU A 221      21.061  10.596  14.512  1.00 22.53
ATOM   1724  CD  GLU A 221      20.974  12.099  14.397  1.00 26.02
ATOM   1725  OE1 GLU A 221      21.214  12.892  15.294  1.00 26.16
ATOM   1726  OE2 GLU A 221      20.545  12.404  13.257  1.00 28.51
ATOM   1727  N   THR A 222      22.192   8.100  18.200  1.00 14.69
ATOM   1728  CA  THR A 222      22.928   7.818  19.430  1.00 12.32
ATOM   1729  C   THR A 222      22.439   6.511  20.030  1.00 12.04
ATOM   1730  O   THR A 222      21.240   6.231  19.928  1.00 14.34
ATOM   1731  CB  THR A 222      22.767   9.091  20.373  1.00 11.24
ATOM   1732  OG1 THR A 222      23.751   8.857  21.432  1.00 12.42
ATOM   1733  CG2 THR A 222      21.366   9.212  20.929  1.00  9.90
ATOM   1734  N   ALA A 223      23.288   5.740  20.687  1.00 10.91
ATOM   1735  CA  ALA A 223      22.906   4.459  21.225  1.00 11.93
ATOM   1736  C   ALA A 223      22.077   4.483  22.518  1.00 12.53
ATOM   1737  O   ALA A 223      21.310   3.538  22.732  1.00 12.71
ATOM   1738  CB  ALA A 223      24.088   3.532  21.462  1.00 11.93
ATOM   1739  N   MET A 224      22.275   5.490  23.325  1.00 11.85
ATOM   1740  CA  MET A 224      21.580   5.562  24.626  1.00 10.36
ATOM   1741  C   MET A 224      21.110   6.989  24.899  1.00 11.34
ATOM   1742  O   MET A 224      21.648   7.944  24.354  1.00 12.37
ATOM   1743  CB  MET A 224      22.558   5.137  25.708  1.00  9.53
ATOM   1744  CG  MET A 224      23.118   3.792  25.541  1.00 10.70
ATOM   1745  SD  MET A 224      24.200   3.254  26.862  1.00 12.87
ATOM   1746  CE  MET A 224      25.772   4.003  26.493  1.00 12.23
ATOM   1747  N   THR A 225      20.212   7.050  25.856  1.00 10.21
ATOM   1748  CA  THR A 225      19.621   8.248  26.416  1.00  9.87
ATOM   1749  C   THR A 225      19.186   7.944  27.853  1.00  9.35
ATOM   1750  O   THR A 225      19.232   6.827  28.320  1.00  8.84
ATOM   1751  CB  THR A 225      18.521   8.872  25.531  1.00  9.68
ATOM   1752  OG1 THR A 225      18.463  10.282  25.915  1.00 10.00
ATOM   1753  CG2 THR A 225      17.119   8.302  25.583  1.00  9.55
ATOM   1754  N   ILE A 226      18.952   9.035  28.586  1.00 11.69
ATOM   1755  CA  ILE A 226      18.486   8.977  30.000  1.00  9.40
ATOM   1756  C   ILE A 226      17.187   9.733  29.999  1.00  8.83
ATOM   1757  O   ILE A 226      17.190  10.918  29.609  1.00  8.98
ATOM   1758  CB  ILE A 226      19.533   9.474  31.028  1.00  9.39
ATOM   1759  CG1 ILE A 226      20.752   8.564  30.938  1.00  6.44
ATOM   1760  CG2 ILE A 226      18.979   9.415  32.497  1.00  8.90
ATOM   1761  CD1 ILE A 226      21.824   8.907  31.980  1.00  8.46
ATOM   1762  N   ASN A 227      16.094   9.018  30.297  1.00  8.04
ATOM   1763  CA  ASN A 227      14.789   9.673  30.266  1.00  7.73
ATOM   1764  C   ASN A 227      13.821   8.868  31.162  1.00  7.74
ATOM   1765  O   ASN A 227      14.220   7.853  31.739  1.00  7.33
ATOM   1766  CB  ASN A 227      14.303   9.944  28.839  1.00 10.16
ATOM   1767  CG  ASN A 227      13.678  11.311  28.670  1.00 10.87
ATOM   1768  OD1 ASN A 227      13.082  11.852  29.634  1.00 12.34
ATOM   1769  ND2 ASN A 227      13.820  11.904  27.509  1.00 13.11
ATOM   1770  N   GLY A 228      12.639   9.403  31.286  1.00  9.23
ATOM   1771  CA  GLY A 228      11.612   8.832  32.176  1.00 10.70
ATOM   1772  C   GLY A 228      10.467   8.267  31.386  1.00 10.95
ATOM   1773  O   GLY A 228      10.465   8.419  30.166  1.00 10.82
ATOM   1774  N   PRO A 229       9.487   7.715  32.120  1.00 12.61
ATOM   1775  CA  PRO A 229       8.328   7.050  31.518  1.00 12.76
ATOM   1776  C   PRO A 229       7.521   7.894  30.618  1.00 13.96
ATOM   1777  O   PRO A 229       6.856   7.419  29.660  1.00 16.10
ATOM   1778  CB  PRO A 229       7.577   6.417  32.671  1.00 12.55
ATOM   1779  CG  PRO A 229       8.596   6.318  33.775  1.00 12.50
ATOM   1780  CD  PRO A 229       9.508   7.515  33.571  1.00 11.91
ATOM   1781  N   TRP A 230       7.541   9.215  30.841  1.00 14.04
ATOM   1782  CA  TRP A 230       6.815  10.115  29.970  1.00 14.05
ATOM   1783  C   TRP A 230       7.332  10.136  28.538  1.00 15.33
ATOM   1784  O   TRP A 230       6.632  10.654  27.630  1.00 16.54
ATOM   1785  CB  TRP A 230       6.857  11.519  30.636  1.00 15.28
ATOM   1786  CG  TRP A 230       8.270  12.004  30.762  1.00 13.83
ATOM   1787  CD1 TRP A 230       9.034  12.596  29.787  1.00 12.60
ATOM   1788  CD2 TRP A 230       9.086  11.893  31.934  1.00 13.57
ATOM   1789  NE1 TRP A 230      10.275  12.826  30.281  1.00 15.21
ATOM   1790  CE2 TRP A 230      10.341  12.435  31.600  1.00 13.36
ATOM   1791  CE3 TRP A 230       8.866  11.391  33.219  1.00 11.85
ATOM   1792  CZ2 TRP A 230      11.396  12.498  32.508  1.00 12.12
ATOM   1793  CZ3 TRP A 230       9.927  11.436  34.102  1.00 12.17
ATOM   1794  CH2 TRP A 230      11.165  11.948  33.751  1.00 11.54
ATOM   1795  N   ALA A 231       8.539   9.680  28.288  1.00 15.92
ATOM   1796  CA  ALA A 231       9.192   9.692  26.990  1.00 16.41
ATOM   1797  C   ALA A 231       8.927   8.471  26.105  1.00 15.93
ATOM   1798  O   ALA A 231       9.163   8.590  24.878  1.00 17.29
ATOM   1799  CB  ALA A 231      10.720   9.784  27.209  1.00 15.63
ATOM   1800  N   TRP A 232       8.468   7.402  26.675  1.00 15.86
ATOM   1801  CA  TRP A 232       8.183   6.146  26.003  1.00 16.35
ATOM   1802  C   TRP A 232       7.286   6.316  24.796  1.00 19.92
ATOM   1803  O   TRP A 232       7.722   5.802  23.729  1.00 20.77
ATOM   1804  CB  TRP A 232       7.712   5.066  26.935  1.00 12.21
ATOM   1805  CG  TRP A 232       8.646   4.819  28.066  1.00 12.42
ATOM   1806  CD1 TRP A 232       9.936   5.215  28.210  1.00 11.43
ATOM   1807  CD2 TRP A 232       8.354   4.071  29.269  1.00 11.92
ATOM   1808  NE1 TRP A 232      10.479   4.740  29.355  1.00 11.22
ATOM   1809  CE2 TRP A 232       9.505   4.080  30.062  1.00 12.03
ATOM   1810  CE3 TRP A 232       7.196   3.419  29.709  1.00 11.83
ATOM   1811  CZ2 TRP A 232       9.585   3.405  31.276  1.00 11.49
ATOM   1812  CZ3 TRP A 232       7.269   2.820  30.934  1.00 11.59
ATOM   1813  CH2 TRP A 232       8.392   2.802  31.702  1.00 11.27
ATOM   1814  N   SER A 233       6.167   6.977  24.882  1.00 21.98
ATOM   1815  CA  SER A 233       5.257   7.123  23.736  1.00 25.35
ATOM   1816  C   SER A 233       5.898   7.696  22.475  1.00 25.94
ATOM   1817  O   SER A 233       5.471   7.383  21.331  1.00 25.67
ATOM   1818  CB  SER A 233       3.956   7.808  24.112  1.00 26.97
ATOM   1819  OG  SER A 233       4.113   8.998  24.865  1.00 30.61
ATOM   1820  N   ASN A 234       6.907   8.523  22.619  1.00 26.63
ATOM   1821  CA  ASN A 234       7.652   9.187  21.563  1.00 26.39
ATOM   1822  C   ASN A 234       8.615   8.217  20.870  1.00 24.58
ATOM   1823  O   ASN A 234       8.803   8.408  19.676  1.00 25.08
ATOM   1824  CB  ASN A 234       8.398  10.419  22.033  1.00 29.53
ATOM   1825  CG  ASN A 234       7.564  11.598  22.444  1.00 32.59
ATOM   1826  OD1 ASN A 234       7.645  12.616  21.754  1.00 33.42
ATOM   1827  ND2 ASN A 234       6.813  11.469  23.562  1.00 35.70
ATOM   1828  N   ILE A 235       9.195   7.312  21.605  1.00 23.21
ATOM   1829  CA  ILE A 235      10.137   6.322  21.102  1.00 22.44
ATOM   1830  C   ILE A 235       9.411   5.263  20.277  1.00 23.95
ATOM   1831  O   ILE A 235       9.868   4.879  19.206  1.00 25.14
ATOM   1832  CB  ILE A 235      11.022   5.690  22.234  1.00 19.78
ATOM   1833  CG1 ILE A 235      11.614   6.789  23.145  1.00 17.10
ATOM   1834  CG2 ILE A 235      12.134   4.807  21.592  1.00 19.49
ATOM   1835  CD1 ILE A 235      12.193   6.283  24.488  1.00 13.67
ATOM   1836  N   ASP A 236       8.266   4.840  20.779  1.00 25.72
ATOM   1837  CA  ASP A 236       7.377   3.869  20.149  1.00 26.92
ATOM   1838  C   ASP A 236       7.157   4.331  18.696  1.00 28.03
ATOM   1839  O   ASP A 236       7.392   3.592  17.744  1.00 29.42
ATOM   1840  CB  ASP A 236       6.063   3.752  20.892  1.00 27.04
ATOM   1841  CG  ASP A 236       6.170   3.360  22.331  1.00 28.89
ATOM   1842  OD1 ASP A 236       7.031   2.527  22.683  1.00 28.16
ATOM   1843  OD2 ASP A 236       5.362   3.912  23.122  1.00 31.28
ATOM   1844  N   THR A 237       6.687   5.541  18.559  1.00 28.38
ATOM   1845  CA  THR A 237       6.411   6.221  17.316  1.00 29.75
ATOM   1846  C   THR A 237       7.598   6.178  16.344  1.00 31.03
ATOM   1847  O   THR A 237       7.459   5.933  15.113  1.00 30.98
ATOM   1848  CB  THR A 237       6.007   7.717  17.646  1.00 29.82
ATOM   1849  OG1 THR A 237       4.791   7.604  18.434  1.00 30.27
ATOM   1850  CG2 THR A 237       5.785   8.604  16.435  1.00 31.88
ATOM   1851  N   SER A 238       8.752   6.429  16.923  1.00 30.85
ATOM   1852  CA  SER A 238      10.030   6.501  16.235  1.00 31.83
ATOM   1853  C   SER A 238      10.351   5.195  15.523  1.00 33.02
ATOM   1854  O   SER A 238      11.017   5.201  14.464  1.00 34.62
ATOM   1855  CB  SER A 238      11.138   6.942  17.184  1.00 31.02
ATOM   1856  OG  SER A 238      11.635   5.875  17.978  1.00 30.06
ATOM   1857  N   LYS A 239       9.920   4.092  16.082  1.00 33.62
ATOM   1858  CA  LYS A 239      10.160   2.755  15.538  1.00 34.33
ATOM   1859  C   LYS A 239      11.550   2.215  15.864  1.00 32.93
ATOM   1860  O   LYS A 239      12.055   1.279  15.210  1.00 34.29
ATOM   1861  CB  LYS A 239       9.881   2.656  14.041  1.00 36.40
ATOM   1862  CG  LYS A 239       8.517   2.061  13.710  1.00 39.39
ATOM   1863  CD  LYS A 239       7.357   2.952  14.131  1.00 42.31
ATOM   1864  CE  LYS A 239       6.052   2.156  14.267  1.00 43.20
ATOM   1865  NZ  LYS A 239       6.397   0.820  14.843  1.00 44.09
ATOM   1866  N   VAL A 240      12.165   2.776  16.886  1.00 29.31
ATOM   1867  CA  VAL A 240      13.474   2.354  17.377  1.00 25.46
ATOM   1868  C   VAL A 240      13.171   1.120  18.243  1.00 23.89
ATOM   1869  O   VAL A 240      12.137   1.106  18.919  1.00 23.32
ATOM   1870  CB  VAL A 240      14.162   3.507  18.150  1.00 24.48
ATOM   1871  CG1 VAL A 240      15.376   3.061  18.934  1.00 22.88
ATOM   1872  CG2 VAL A 240      14.539   4.663  17.253  1.00 23.31
ATOM   1873  N   ASN A 241      14.036   0.146  18.177  1.00 22.56
ATOM   1874  CA  ASN A 241      13.932  -1.095  18.952  1.00 21.94
ATOM   1875  C   ASN A 241      14.757  -0.832  20.235  1.00 19.28
ATOM   1876  O   ASN A 241      15.957  -1.084  20.287  1.00 17.76
ATOM   1877  CB  ASN A 241      14.336  -2.331  18.183  1.00 24.22
ATOM   1878  CG  ASN A 241      14.256  -3.604  18.996  1.00 27.64
ATOM   1879  OD1 ASN A 241      13.258  -3.853  19.713  1.00 29.45
ATOM   1880  ND2 ASN A 241      15.299  -4.437  18.876  1.00 29.26
ATOM   1881  N   TYR A 242      13.976  -0.313  21.181  1.00 17.15
ATOM   1882  CA  TYR A 242      14.577   0.112  22.474  1.00 14.72
ATOM   1883  C   TYR A 242      14.338  -0.767  23.653  1.00 13.92
ATOM   1884  O   TYR A 242      13.350  -1.518  23.676  1.00 15.89
ATOM   1885  CB  TYR A 242      14.043   1.532  22.726  1.00 13.22
ATOM   1886  CG  TYR A 242      12.670   1.708  23.299  1.00 15.26
ATOM   1887  CD1 TYR A 242      11.560   1.798  22.453  1.00 13.25
ATOM   1888  CD2 TYR A 242      12.442   1.809  24.693  1.00 15.09
ATOM   1889  CE1 TYR A 242      10.307   2.011  22.943  1.00 16.85
ATOM   1890  CE2 TYR A 242      11.152   2.010  25.189  1.00 17.03
ATOM   1891  CZ  TYR A 242      10.085   2.123  24.318  1.00 18.27
ATOM   1892  OH  TYR A 242       8.775   2.312  24.730  1.00 18.74
ATOM   1893  N   GLY A 243      15.140  -0.650  24.683  1.00 12.16
ATOM   1894  CA  GLY A 243      15.067  -1.352  25.954  1.00 11.08
ATOM   1895  C   GLY A 243      15.295  -0.241  27.058  1.00 12.41
ATOM   1896  O   GLY A 243      15.897   0.771  26.727  1.00 11.63
ATOM   1897  N   VAL A 244      14.766  -0.523  28.203  1.00 12.82
ATOM   1898  CA  VAL A 244      14.814   0.311  29.424  1.00 12.02
ATOM   1899  C   VAL A 244      15.494  -0.509  30.473  1.00 11.50
ATOM   1900  O   VAL A 244      15.071  -1.692  30.681  1.00 13.55
ATOM   1901  CB  VAL A 244      13.417   0.809  29.831  1.00 12.66
ATOM   1902  CG1 VAL A 244      13.454   1.768  31.033  1.00 11.92
ATOM   1903  CG2 VAL A 244      12.642   1.436  28.685  1.00 12.52
ATOM   1904  N   THR A 245      16.526   0.010  31.118  1.00 10.05
ATOM   1905  CA  THR A 245      17.229  -0.813  32.112  1.00 10.13
ATOM   1906  C   THR A 245      17.772   0.010  33.282  1.00 10.45
ATOM   1907  O   THR A 245      17.605   1.243  33.310  1.00 12.34
ATOM   1908  CB  THR A 245      18.348  -1.643  31.371  1.00  9.42
ATOM   1909  OG1 THR A 245      18.934  -2.578  32.301  1.00 12.33
ATOM   1910  CG2 THR A 245      19.501  -0.770  30.803  1.00  9.79
ATOM   1911  N   VAL A 246      18.434  -0.633  34.190  1.00 11.00
ATOM   1912  CA  VAL A 246      19.053   0.045  35.338  1.00 12.51
ATOM   1913  C   VAL A 246      20.150   0.998  34.846  1.00 12.90
ATOM   1914  O   VAL A 246      20.911   0.661  33.935  1.00 13.41
ATOM   1915  CB  VAL A 246      19.523  -0.963  36.368  1.00 13.64
ATOM   1916  CG1 VAL A 246      20.718  -1.821  35.897  1.00 15.34
ATOM   1917  CG2 VAL A 246      19.922  -0.296  37.691  1.00 13.68
ATOM   1918  N   LEU A 247      20.245   2.181  35.455  1.00 12.13
ATOM   1919  CA  LEU A 247      21.304   3.148  35.125  1.00 11.52
ATOM   1920  C   LEU A 247      22.647   2.519  35.480  1.00 10.55
ATOM   1921  O   LEU A 247      22.769   1.665  36.377  1.00 11.18
ATOM   1922  CB  LEU A 247      21.074   4.426  35.993  1.00 10.11
ATOM   1923  CG  LEU A 247      19.870   5.250  35.626  1.00 11.25
ATOM   1924  CD1 LEU A 247      19.586   6.250  36.756  1.00 10.31
ATOM   1925  CD2 LEU A 247      20.137   5.960  34.305  1.00  9.83
ATOM   1926  N   PRO A 248      23.710   3.016  34.851  1.00 11.07
ATOM   1927  CA  PRO A 248      25.039   2.501  35.093  1.00 11.70
ATOM   1928  C   PRO A 248      25.552   2.881  36.487  1.00 13.03
ATOM   1929  O   PRO A 248      25.078   3.879  37.042  1.00 14.00
ATOM   1930  CB  PRO A 248      25.893   3.105  33.956  1.00  9.62
ATOM   1931  CG  PRO A 248      24.976   3.804  33.032  1.00 10.74
ATOM   1932  CD  PRO A 248      23.657   4.049  33.790  1.00  9.70
ATOM   1933  N   THR A 249      26.494   2.128  37.010  1.00 13.82
ATOM   1934  CA  THR A 249      27.114   2.410  38.294  1.00 13.87
ATOM   1935  C   THR A 249      28.288   3.356  38.069  1.00 14.80
ATOM   1936  O   THR A 249      28.738   3.517  36.944  1.00 14.70
ATOM   1937  CB  THR A 249      27.594   1.132  39.069  1.00 12.52
ATOM   1938  OG1 THR A 249      28.629   0.511  38.237  1.00 13.82
ATOM   1939  CG2 THR A 249      26.476   0.167  39.426  1.00 13.20
ATOM   1940  N   PHE A 250      28.719   4.035  39.125  1.00 16.01
ATOM   1941  CA  PHE A 250      29.882   4.941  39.056  1.00 16.02
ATOM   1942  C   PHE A 250      30.685   4.678  40.350  1.00 17.32
ATOM   1943  O   PHE A 250      30.135   4.688  41.456  1.00 17.46
ATOM   1944  CB  PHE A 250      29.570   6.360  38.739  1.00 17.09
ATOM   1945  CG  PHE A 250      30.732   7.310  38.854  1.00 18.12
ATOM   1946  CD1 PHE A 250      31.731   7.301  37.882  1.00 17.44
ATOM   1947  CD2 PHE A 250      30.833   8.189  39.939  1.00 18.09
ATOM   1948  CE1 PHE A 250      32.802   8.188  37.921  1.00 17.68
ATOM   1949  CE2 PHE A 250      31.923   9.060  40.011  1.00 18.05
ATOM   1950  CZ  PHE A 250      32.890   9.073  39.010  1.00 18.43
ATOM   1951  N   LYS A 251      31.948   4.335  40.166  1.00 17.71
ATOM   1952  CA  LYS A 251      32.837   3.985  41.272  1.00 18.65
ATOM   1953  C   LYS A 251      32.244   2.849  42.078  1.00 19.15
ATOM   1954  O   LYS A 251      32.438   2.716  43.275  1.00 20.28
ATOM   1955  CB  LYS A 251      33.106   5.204  42.162  1.00 19.12
ATOM   1956  CG  LYS A 251      33.880   6.214  41.314  1.00 20.14
ATOM   1957  CD  LYS A 251      34.232   7.481  42.027  1.00 22.62
ATOM   1958  CE  LYS A 251      35.599   7.345  42.667  1.00 23.46
ATOM   1959  NZ  LYS A 251      35.521   6.132  43.523  1.00 27.44
ATOM   1960  N   GLY A 252      31.537   2.010  41.332  1.00 19.58
ATOM   1961  CA  GLY A 252      30.844   0.829  41.796  1.00 18.67
ATOM   1962  C   GLY A 252      29.547   1.156  42.530  1.00 18.35
ATOM   1963  O   GLY A 252      28.908   0.220  43.058  1.00 19.84
ATOM   1964  N   GLN A 253      29.145   2.399  42.552  1.00 16.14
ATOM   1965  CA  GLN A 253      27.921   2.814  43.239  1.00 14.94
ATOM   1966  C   GLN A 253      26.809   3.072  42.244  1.00 14.00
ATOM   1967  O   GLN A 253      27.034   3.663  41.193  1.00 14.58
ATOM   1968  CB  GLN A 253      28.219   4.110  44.035  1.00 17.07
ATOM   1969  CG  GLN A 253      29.385   3.997  45.001  1.00 16.94
ATOM   1970  CD  GLN A 253      29.293   2.860  45.969  1.00 18.13
ATOM   1971  OE1 GLN A 253      28.259   2.435  46.457  1.00 17.36
ATOM   1972  NE2 GLN A 253      30.479   2.309  46.306  1.00 20.54
ATOM   1973  N   PRO A 254      25.587   2.719  42.644  1.00 12.80
ATOM   1974  CA  PRO A 254      24.431   2.936  41.790  1.00 12.90
ATOM   1975  C   PRO A 254      24.205   4.405  41.525  1.00 13.34
ATOM   1976  O   PRO A 254      24.520   5.212  42.398  1.00 14.67
ATOM   1977  CB  PRO A 254      23.282   2.247  42.499  1.00 12.08
ATOM   1978  CG  PRO A 254      23.806   1.674  43.768  1.00 12.35
ATOM   1979  CD  PRO A 254      25.255   2.034  43.902  1.00 11.83
ATOM   1980  N   SER A 255      23.702   4.761  40.365  1.00 13.30
ATOM   1981  CA  SER A 255      23.315   6.135  39.987  1.00 13.32
ATOM   1982  C   SER A 255      22.112   6.433  40.919  1.00 14.57
ATOM   1983  O   SER A 255      21.415   5.453  41.243  1.00 13.75
ATOM   1984  CB  SER A 255      22.855   6.251  38.550  1.00 13.60
ATOM   1985  OG  SER A 255      23.937   6.049  37.656  1.00 14.05
ATOM   1986  N   LYS A 256      21.940   7.672  41.292  1.00 14.19
ATOM   1987  CA  LYS A 256      20.867   8.046  42.226  1.00 14.27
ATOM   1988  C   LYS A 256      19.951   9.094  41.654  1.00 12.63
ATOM   1989  O   LYS A 256      20.129  10.284  41.929  1.00 13.54
ATOM   1990  CB  LYS A 256      21.470   8.668  43.487  1.00 17.17
ATOM   1991  CG  LYS A 256      21.349   7.982  44.819  1.00 19.71
ATOM   1992  CD  LYS A 256      22.649   7.472  45.371  1.00 23.14
ATOM   1993  CE  LYS A 256      23.055   6.132  44.774  1.00 26.75
ATOM   1994  NZ  LYS A 256      24.400   5.649  45.230  1.00 25.87
ATOM   1995  N   PRO A 257      18.980   8.680  40.866  1.00 11.90
ATOM   1996  CA  PRO A 257      18.035   9.603  40.293  1.00 11.40
ATOM   1997  C   PRO A 257      17.045  10.018  41.415  1.00 12.47
ATOM   1998  O   PRO A 257      16.920   9.249  42.350  1.00 13.26
ATOM   1999  CB  PRO A 257      17.343   8.807  39.176  1.00 10.63
ATOM   2000  CG  PRO A 257      17.396   7.397  39.701  1.00 11.06
ATOM   2001  CD  PRO A 257      18.645   7.277  40.530  1.00 11.20
ATOM   2002  N   PHE A 258      16.507  11.182  41.262  1.00 12.82
ATOM   2003  CA  PHE A 258      15.487  11.703  42.207  1.00 13.06
ATOM   2004  C   PHE A 258      14.236  10.876  41.860  1.00 13.09
ATOM   2005  O   PHE A 258      13.988  10.571  40.672  1.00 13.27
ATOM   2006  CB  PHE A 258      15.203  13.187  41.984  1.00 12.31
ATOM   2007  CG  PHE A 258      16.177  14.165  42.565  1.00 13.41
ATOM   2008  CD1 PHE A 258      16.400  14.194  43.940  1.00 11.61
ATOM   2009  CD2 PHE A 258      16.871  15.040  41.703  1.00 13.41
ATOM   2010  CE1 PHE A 258      17.297  15.095  44.492  1.00 14.30
ATOM   2011  CE2 PHE A 258      17.800  15.946  42.237  1.00 13.74
ATOM   2012  CZ  PHE A 258      17.994  15.974  43.635  1.00 13.54
ATOM   2013  N   VAL A 259      13.468  10.575  42.874  1.00 14.04
ATOM   2014  CA  VAL A 259      12.202   9.790  42.783  1.00 12.16
ATOM   2015  C   VAL A 259      11.017  10.731  43.022  1.00 12.28
ATOM   2016  O   VAL A 259      11.112  11.497  44.026  1.00 13.39
ATOM   2017  CB  VAL A 259      12.268   8.674  43.826  1.00 10.95
ATOM   2018  CG1 VAL A 259      11.057   7.759  43.812  1.00 12.44
ATOM   2019  CG2 VAL A 259      13.537   7.891  43.822  1.00  9.13
ATOM   2020  N   GLY A 260      10.046  10.746  42.170  1.00  9.92
ATOM   2021  CA  GLY A 260       8.825  11.564  42.326  1.00 10.31
ATOM   2022  C   GLY A 260       7.726  10.533  42.663  1.00 10.92
ATOM   2023  O   GLY A 260       7.755   9.438  42.097  1.00 10.85
ATOM   2024  N   VAL A 261       6.824  10.816  43.573  1.00 10.28
ATOM   2025  CA  VAL A 261       5.767   9.873  43.970  1.00 10.83
ATOM   2026  C   VAL A 261       4.425  10.532  43.821  1.00 11.05
ATOM   2027  O   VAL A 261       4.256  11.583  44.491  1.00 13.20
ATOM   2028  CB  VAL A 261       6.022   9.397  45.403  1.00 10.64
ATOM   2029  CG1 VAL A 261       4.888   8.534  45.986  1.00 10.29
ATOM   2030  CG2 VAL A 261       7.325   8.681  45.626  1.00 10.52
ATOM   2031  N   LEU A 262       3.536  10.081  42.969  1.00 10.45
ATOM   2032  CA  LEU A 262       2.201  10.545  42.750  1.00  9.46
ATOM   2033  C   LEU A 262       1.467  10.217  44.098  1.00  8.81
ATOM   2034  O   LEU A 262       1.568   9.082  44.548  1.00  9.97
ATOM   2035  CB  LEU A 262       1.484   9.942  41.542  1.00  9.45
ATOM   2036  CG  LEU A 262       0.046  10.445  41.417  1.00 10.02
ATOM   2037  CD1 LEU A 262      -0.014  11.891  40.964  1.00 10.09
ATOM   2038  CD2 LEU A 262      -0.764   9.566  40.460  1.00 13.30
ATOM   2039  N   SER A 263       0.952  11.284  44.695  1.00  8.84
ATOM   2040  CA  SER A 263       0.379  11.165  46.041  1.00  8.57
ATOM   2041  C   SER A 263      -1.028  11.667  46.137  1.00  7.83
ATOM   2042  O   SER A 263      -1.482  12.460  45.338  1.00  8.28
ATOM   2043  CB  SER A 263       1.345  11.868  47.033  1.00  7.35
ATOM   2044  OG  SER A 263       2.518  11.102  47.170  1.00 10.27
ATOM   2045  N   ALA A 264      -1.734  11.110  47.154  1.00  8.47
ATOM   2046  CA  ALA A 264      -3.148  11.529  47.350  1.00  8.02
ATOM   2047  C   ALA A 264      -3.241  12.084  48.788  1.00  6.82
ATOM   2048  O   ALA A 264      -2.906  11.401  49.730  1.00  8.66
ATOM   2049  CB  ALA A 264      -4.078  10.357  47.138  1.00  7.51
ATOM   2050  N   GLY A 265      -3.656  13.343  48.839  1.00  9.27
ATOM   2051  CA  GLY A 265      -3.748  14.000  50.185  1.00  9.53
ATOM   2052  C   GLY A 265      -5.178  14.440  50.384  1.00  9.80
ATOM   2053  O   GLY A 265      -5.894  14.715  49.453  1.00 10.90
ATOM   2054  N   ILE A 266      -5.557  14.523  51.675  1.00 12.08
ATOM   2055  CA  ILE A 266      -6.930  14.926  52.086  1.00 10.40
ATOM   2056  C   ILE A 266      -6.932  16.377  52.590  1.00  8.46
ATOM   2057  O   ILE A 266      -6.086  16.691  53.436  1.00  9.80
ATOM   2058  CB  ILE A 266      -7.378  13.958  53.267  1.00 12.05
ATOM   2059  CG1 ILE A 266      -7.417  12.494  52.768  1.00 12.99
ATOM   2060  CG2 ILE A 266      -8.761  14.347  53.859  1.00 12.23
ATOM   2061  CD1 ILE A 266      -7.344  11.420  53.870  1.00 13.90
ATOM   2062  N   ASN A 267      -7.804  17.158  52.113  1.00  9.54
ATOM   2063  CA  ASN A 267      -7.970  18.584  52.500  1.00 11.59
ATOM   2064  C   ASN A 267      -8.280  18.626  54.016  1.00 12.46
ATOM   2065  O   ASN A 267      -9.176  17.941  54.493  1.00 11.46
ATOM   2066  CB  ASN A 267      -9.001  19.216  51.616  1.00 12.61
ATOM   2067  CG  ASN A 267      -9.068  20.718  51.687  1.00 15.49
ATOM   2068  OD1 ASN A 267      -8.686  21.275  52.731  1.00 18.04
ATOM   2069  ND2 ASN A 267      -9.538  21.385  50.659  1.00 16.32
ATOM   2070  N   ALA A 268      -7.457  19.372  54.742  1.00 13.70
ATOM   2071  CA  ALA A 268      -7.631  19.537  56.195  1.00 13.59
ATOM   2072  C   ALA A 268      -9.016  20.127  56.468  1.00 14.79
ATOM   2073  O   ALA A 268      -9.531  19.906  57.568  1.00 15.46
ATOM   2074  CB  ALA A 268      -6.562  20.506  56.733  1.00 15.28
ATOM   2075  N   ALA A 269      -9.567  20.883  55.542  1.00 15.98
ATOM   2076  CA  ALA A 269     -10.866  21.508  55.622  1.00 17.18
ATOM   2077  C   ALA A 269     -12.018  20.592  55.250  1.00 18.26
ATOM   2078  O   ALA A 269     -13.184  20.965  55.457  1.00 19.88
ATOM   2079  CB  ALA A 269     -10.989  22.811  54.831  1.00 16.25
ATOM   2080  N   SER A 270     -11.764  19.379  54.762  1.00 19.03
ATOM   2081  CA  SER A 270     -12.900  18.527  54.404  1.00 18.81
ATOM   2082  C   SER A 270     -13.644  17.944  55.605  1.00 17.41
ATOM   2083  O   SER A 270     -13.044  17.385  56.531  1.00 17.21
ATOM   2084  CB  SER A 270     -12.409  17.334  53.549  1.00 19.08
ATOM   2085  N   PRO A 271     -14.952  17.948  55.479  1.00 18.21
ATOM   2086  CA  PRO A 271     -15.847  17.323  56.472  1.00 19.41
ATOM   2087  C   PRO A 271     -15.990  15.821  56.272  1.00 19.52
ATOM   2088  O   PRO A 271     -16.593  15.067  57.038  1.00 20.25
ATOM   2089  CB  PRO A 271     -17.205  17.990  56.210  1.00 18.98
ATOM   2090  CG  PRO A 271     -17.123  18.715  54.940  1.00 18.49
ATOM   2091  CD  PRO A 271     -15.724  18.574  54.395  1.00 17.66
ATOM   2092  N   ASN A 272     -15.380  15.315  55.198  1.00 19.99
ATOM   2093  CA  ASN A 272     -15.452  13.916  54.772  1.00 17.53
ATOM   2094  C   ASN A 272     -14.183  13.134  54.879  1.00 17.15
ATOM   2095  O   ASN A 272     -14.004  12.283  53.978  1.00 17.40
ATOM   2096  CB  ASN A 272     -15.887  13.950  53.269  1.00 17.28
ATOM   2097  CG  ASN A 272     -17.055  14.853  53.057  1.00 17.75
ATOM   2098  OD1 ASN A 272     -18.124  14.603  53.684  1.00 21.09
ATOM   2099  ND2 ASN A 272     -16.989  15.872  52.238  1.00 16.61
ATOM   2100  N   LYS A 273     -13.349  13.292  55.861  1.00 15.89
ATOM   2101  CA  LYS A 273     -12.101  12.585  55.942  1.00 15.61
ATOM   2102  C   LYS A 273     -12.181  11.085  56.086  1.00 14.89
ATOM   2103  O   LYS A 273     -11.247  10.367  55.670  1.00 13.04
ATOM   2104  CB  LYS A 273     -11.178  13.152  57.017  1.00 16.44
ATOM   2105  CG  LYS A 273     -10.878  14.663  56.850  1.00 18.29
ATOM   2106  CD  LYS A 273     -10.006  15.042  58.077  1.00 19.08
ATOM   2107  CE  LYS A 273      -9.589  16.473  58.065  1.00 20.51
ATOM   2108  NZ  LYS A 273     -10.776  17.366  57.924  1.00 22.24
ATOM   2109  N   GLU A 274     -13.190  10.594  56.761  1.00 14.68
ATOM   2110  CA  GLU A 274     -13.396   9.166  56.989  1.00 15.40
ATOM   2111  C   GLU A 274     -13.817   8.554  55.662  1.00 14.46
ATOM   2112  O   GLU A 274     -13.277   7.489  55.304  1.00 16.55
ATOM   2113  CB  GLU A 274     -14.416   8.899  58.085  1.00 18.96
ATOM   2114  CG  GLU A 274     -13.862   8.993  59.519  1.00 25.13
ATOM   2115  CD  GLU A 274     -12.783   7.984  59.828  1.00 32.33
ATOM   2116  OE1 GLU A 274     -13.115   6.770  59.564  1.00 35.64
ATOM   2117  OE2 GLU A 274     -11.662   8.263  60.298  1.00 34.56
ATOM   2118  N   LEU A 275     -14.644   9.235  54.931  1.00 13.59
ATOM   2119  CA  LEU A 275     -15.060   8.765  53.605  1.00 14.16
ATOM   2120  C   LEU A 275     -13.831   8.682  52.667  1.00 15.21
ATOM   2121  O   LEU A 275     -13.685   7.691  51.932  1.00 14.68
ATOM   2122  CB  LEU A 275     -16.153   9.625  53.063  1.00 14.20
ATOM   2123  CG  LEU A 275     -17.592   9.421  53.463  1.00 12.87
ATOM   2124  CD1 LEU A 275     -18.442  10.528  52.870  1.00 14.03
ATOM   2125  CD2 LEU A 275     -18.046   8.042  52.989  1.00 13.72
ATOM   2126  N   ALA A 276     -13.005   9.704  52.708  1.00 14.79
ATOM   2127  CA  ALA A 276     -11.778   9.796  51.891  1.00 13.92
ATOM   2128  C   ALA A 276     -10.820   8.676  52.133  1.00 14.41
ATOM   2129  O   ALA A 276     -10.279   8.010  51.225  1.00 14.14
ATOM   2130  CB  ALA A 276     -11.105  11.171  52.081  1.00 13.30
ATOM   2131  N   LYS A 277     -10.549   8.388  53.393  1.00 14.69
ATOM   2132  CA  LYS A 277      -9.642   7.342  53.808  1.00 16.42
ATOM   2133  C   LYS A 277     -10.166   5.971  53.436  1.00 17.59
ATOM   2134  O   LYS A 277      -9.415   5.028  53.157  1.00 18.77
ATOM   2135  CB  LYS A 277      -9.307   7.499  55.256  1.00 17.87
ATOM   2136  CG  LYS A 277      -9.816   6.496  56.235  1.00 19.84
ATOM   2137  CD  LYS A 277      -8.763   5.568  56.694  1.00 20.70
ATOM   2138  CE  LYS A 277      -8.834   5.221  58.163  1.00 18.89
ATOM   2139  NZ  LYS A 277      -7.496   4.804  58.607  1.00 20.29
ATOM   2140  N   GLU A 278     -11.471   5.832  53.431  1.00 18.83
ATOM   2141  CA  GLU A 278     -12.086   4.553  53.077  1.00 19.98
ATOM   2142  C   GLU A 278     -12.012   4.362  51.566  1.00 19.03
ATOM   2143  O   GLU A 278     -11.665   3.251  51.157  1.00 18.64
ATOM   2144  CB  GLU A 278     -13.438   4.382  53.707  1.00 23.47
ATOM   2145  CG  GLU A 278     -13.380   3.639  55.074  1.00 29.80
ATOM   2146  CD  GLU A 278     -12.475   4.004  56.197  1.00 31.85
ATOM   2147  OE1 GLU A 278     -12.504   5.074  56.858  1.00 33.25
ATOM   2148  OE2 GLU A 278     -11.666   3.066  56.472  1.00 30.71
ATOM   2149  N   PHE A 279     -12.305   5.384  50.809  1.00 17.34
ATOM   2150  CA  PHE A 279     -12.206   5.373  49.355  1.00 17.26
ATOM   2151  C   PHE A 279     -10.754   5.031  48.976  1.00 17.36
ATOM   2152  O   PHE A 279     -10.454   4.061  48.276  1.00 17.91
ATOM   2153  CB  PHE A 279     -12.669   6.682  48.730  1.00 17.16
ATOM   2154  CG  PHE A 279     -12.413   6.784  47.257  1.00 19.28
ATOM   2155  CD1 PHE A 279     -13.307   6.247  46.340  1.00 18.39
ATOM   2156  CD2 PHE A 279     -11.231   7.378  46.773  1.00 19.29
ATOM   2157  CE1 PHE A 279     -13.080   6.327  44.979  1.00 17.31
ATOM   2158  CE2 PHE A 279     -10.968   7.442  45.412  1.00 18.78
ATOM   2159  CZ  PHE A 279     -11.908   6.932  44.519  1.00 18.26
ATOM   2160  N   LEU A 280      -9.814   5.816  49.499  1.00 16.13
ATOM   2161  CA  LEU A 280      -8.414   5.624  49.237  1.00 15.36
ATOM   2162  C   LEU A 280      -7.892   4.279  49.666  1.00 16.20
ATOM   2163  O   LEU A 280      -7.222   3.583  48.874  1.00 15.77
ATOM   2164  CB  LEU A 280      -7.616   6.815  49.839  1.00 14.09
ATOM   2165  CG  LEU A 280      -7.796   8.180  49.215  1.00 11.92
ATOM   2166  CD1 LEU A 280      -7.073   9.249  50.026  1.00 11.72
ATOM   2167  CD2 LEU A 280      -7.253   8.198  47.787  1.00 11.52
ATOM   2168  N   GLU A 281      -8.070   3.872  50.932  1.00 15.88
ATOM   2169  CA  GLU A 281      -7.474   2.628  51.354  1.00 16.94
ATOM   2170  C   GLU A 281      -8.133   1.351  50.848  1.00 17.58
ATOM   2171  O   GLU A 281      -7.416   0.335  50.615  1.00 16.71
ATOM   2172  CB  GLU A 281      -7.296   2.527  52.858  1.00 17.10
ATOM   2173  CG  GLU A 281      -6.789   3.734  53.621  1.00 18.57
ATOM   2174  CD  GLU A 281      -6.481   3.466  55.078  1.00 19.82
ATOM   2175  OE1 GLU A 281      -6.800   2.430  55.648  1.00 20.89
ATOM   2176  OE2 GLU A 281      -5.862   4.395  55.626  1.00 18.79
ATOM   2177  N   ASN A 282      -9.423   1.378  50.646  1.00 19.14
ATOM   2178  CA  ASN A 282     -10.149   0.143  50.278  1.00 19.67
ATOM   2179  C   ASN A 282     -10.717   0.093  48.912  1.00 20.17
ATOM   2180  O   ASN A 282     -11.276  -0.974  48.566  1.00 21.65
ATOM   2181  CB  ASN A 282     -11.199  -0.148  51.389  1.00 20.76
ATOM   2182  CG  ASN A 282     -10.519  -0.346  52.719  1.00 20.63
ATOM   2183  OD1 ASN A 282      -9.558  -1.088  52.887  1.00 21.70
ATOM   2184  ND2 ASN A 282     -11.006   0.377  53.734  1.00 24.21
ATOM   2185  N   TYR A 283     -10.639   1.148  48.127  1.00 20.76
ATOM   2186  CA  TYR A 283     -11.191   1.104  46.764  1.00 20.53
ATOM   2187  C   TYR A 283     -10.076   1.341  45.751  1.00 20.01
ATOM   2188  O   TYR A 283      -9.872   0.530  44.841  1.00 19.89
ATOM   2189  CB  TYR A 283     -12.325   2.133  46.589  1.00 22.76
ATOM   2190  CG  TYR A 283     -13.583   1.616  47.273  1.00 26.36
ATOM   2191  CD1 TYR A 283     -13.603   1.487  48.674  1.00 27.19
ATOM   2192  CD2 TYR A 283     -14.682   1.234  46.523  1.00 26.98
ATOM   2193  CE1 TYR A 283     -14.711   0.962  49.319  1.00 28.54
ATOM   2194  CE2 TYR A 283     -15.816   0.713  47.152  1.00 29.62
ATOM   2195  CZ  TYR A 283     -15.814   0.590  48.538  1.00 30.73
ATOM   2196  OH  TYR A 283     -16.941   0.078  49.128  1.00 33.63
ATOM   2197  N   LEU A 284      -9.398   2.466  45.988  1.00 18.07
ATOM   2198  CA  LEU A 284      -8.320   2.872  45.102  1.00 17.43
ATOM   2199  C   LEU A 284      -7.060   2.070  45.258  1.00 16.74
ATOM   2200  O   LEU A 284      -6.587   1.501  44.236  1.00 18.11
ATOM   2201  CB  LEU A 284      -8.181   4.407  45.085  1.00 16.91
ATOM   2202  CG  LEU A 284      -6.990   4.823  44.197  1.00 15.79
ATOM   2203  CD1 LEU A 284      -7.421   4.726  42.757  1.00 16.40
ATOM   2204  CD2 LEU A 284      -6.530   6.211  44.580  1.00 15.61
ATOM   2205  N   LEU A 285      -6.480   1.934  46.421  1.00 15.30
ATOM   2206  CA  LEU A 285      -5.266   1.228  46.662  1.00 13.87
ATOM   2207  C   LEU A 285      -5.457  -0.282  46.799  1.00 14.06
ATOM   2208  O   LEU A 285      -4.995  -0.869  47.755  1.00 13.53
ATOM   2209  CB  LEU A 285      -4.433   1.871  47.778  1.00 15.14
ATOM   2210  CG  LEU A 285      -3.798   3.224  47.362  1.00 15.18
ATOM   2211  CD1 LEU A 285      -3.617   4.096  48.570  1.00 15.89
ATOM   2212  CD2 LEU A 285      -2.511   2.882  46.637  1.00 13.93
ATOM   2213  N   THR A 286      -6.033  -0.780  45.727  1.00 15.17
ATOM   2214  CA  THR A 286      -6.295  -2.221  45.549  1.00 16.23
ATOM   2215  C   THR A 286      -5.901  -2.581  44.098  1.00 17.25
ATOM   2216  O   THR A 286      -5.905  -1.703  43.235  1.00 17.63
ATOM   2217  CB  THR A 286      -7.821  -2.531  45.753  1.00 12.87
ATOM   2218  OG1 THR A 286      -8.521  -1.885  44.654  1.00 15.23
ATOM   2219  CG2 THR A 286      -8.388  -2.003  47.084  1.00 16.42
ATOM   2220  N   ASP A 287      -5.694  -3.856  43.863  1.00 19.34
ATOM   2221  CA  ASP A 287      -5.349  -4.299  42.478  1.00 21.26
ATOM   2222  C   ASP A 287      -6.394  -3.822  41.487  1.00 21.51
ATOM   2223  O   ASP A 287      -6.080  -3.409  40.353  1.00 22.59
ATOM   2224  CB  ASP A 287      -5.128  -5.799  42.439  1.00 22.60
ATOM   2225  CG  ASP A 287      -3.908  -6.291  43.132  1.00 23.50
ATOM   2226  OD1 ASP A 287      -2.980  -5.537  43.409  1.00 25.65
ATOM   2227  OD2 ASP A 287      -3.850  -7.509  43.413  1.00 26.77
ATOM   2228  N   GLU A 288      -7.657  -3.879  41.866  1.00 21.60
ATOM   2229  CA  GLU A 288      -8.744  -3.485  40.969  1.00 22.44
ATOM   2230  C   GLU A 288      -8.855  -1.993  40.777  1.00 20.74
ATOM   2231  O   GLU A 288      -9.266  -1.514  39.718  1.00 19.77
ATOM   2232  CB  GLU A 288     -10.089  -4.063  41.430  1.00 26.83
ATOM   2233  CG  GLU A 288     -10.076  -5.467  42.027  1.00 33.37
ATOM   2234  CD  GLU A 288     -10.029  -5.638  43.516  1.00 37.04
ATOM   2235  OE1 GLU A 288     -11.043  -5.703  44.231  1.00 39.18
ATOM   2236  OE2 GLU A 288      -8.863  -5.749  43.974  1.00 37.24
ATOM   2237  N   GLY A 289      -8.511  -1.241  41.822  1.00 20.80
ATOM   2238  CA  GLY A 289      -8.590   0.238  41.737  1.00 19.14
ATOM   2239  C   GLY A 289      -7.456   0.755  40.815  1.00 17.83
ATOM   2240  O   GLY A 289      -7.738   1.572  39.953  1.00 17.06
ATOM   2241  N   LEU A 290      -6.247   0.310  41.056  1.00 17.52
ATOM   2242  CA  LEU A 290      -5.071   0.761  40.258  1.00 17.86
ATOM   2243  C   LEU A 290      -5.267   0.333  38.811  1.00 19.83
ATOM   2244  O   LEU A 290      -4.923   1.053  37.868  1.00 19.73
ATOM   2245  CB  LEU A 290      -3.792   0.293  40.932  1.00 16.15
ATOM   2246  CG  LEU A 290      -3.465   0.880  42.316  1.00 15.84
ATOM   2247  CD1 LEU A 290      -2.206   0.294  42.904  1.00 14.48
ATOM   2248  CD2 LEU A 290      -3.318   2.399  42.190  1.00 16.11
ATOM   2249  N   GLU A 291      -5.858  -0.847  38.651  1.00 21.59
ATOM   2250  CA  GLU A 291      -6.122  -1.400  37.322  1.00 24.23
ATOM   2251  C   GLU A 291      -7.093  -0.576  36.514  1.00 24.40
ATOM   2252  O   GLU A 291      -6.811  -0.333  35.317  1.00 26.19
ATOM   2253  CB  GLU A 291      -6.632  -2.824  37.407  1.00 27.33
ATOM   2254  CG  GLU A 291      -7.194  -3.411  36.123  1.00 33.79
ATOM   2255  CD  GLU A 291      -6.948  -4.878  35.929  1.00 37.57
ATOM   2256  OE1 GLU A 291      -7.055  -5.548  36.990  1.00 39.76
ATOM   2257  OE2 GLU A 291      -6.647  -5.304  34.819  1.00 40.97
ATOM   2258  N   ALA A 292      -8.209  -0.144  37.078  1.00 23.01
ATOM   2259  CA  ALA A 292      -9.185   0.694  36.378  1.00 21.51
ATOM   2260  C   ALA A 292      -8.543   2.012  35.962  1.00 21.20
ATOM   2261  O   ALA A 292      -8.827   2.523  34.861  1.00 22.23
ATOM   2262  CB  ALA A 292     -10.403   0.960  37.235  1.00 20.96
ATOM   2263  N   VAL A 293      -7.691   2.566  36.831  1.00 20.89
ATOM   2264  CA  VAL A 293      -7.021   3.834  36.522  1.00 20.46
ATOM   2265  C   VAL A 293      -5.969   3.636  35.392  1.00 20.47
ATOM   2266  O   VAL A 293      -5.995   4.403  34.433  1.00 19.67
ATOM   2267  CB  VAL A 293      -6.411   4.503  37.758  1.00 20.38
ATOM   2268  CG1 VAL A 293      -5.539   5.678  37.308  1.00 18.59
ATOM   2269  CG2 VAL A 293      -7.444   4.936  38.806  1.00 19.15
ATOM   2270  N   ASN A 294      -5.142   2.664  35.598  1.00 21.02
ATOM   2271  CA  ASN A 294      -4.060   2.257  34.679  1.00 23.28
ATOM   2272  C   ASN A 294      -4.598   1.998  33.277  1.00 24.79
ATOM   2273  O   ASN A 294      -3.968   2.422  32.286  1.00 25.95
ATOM   2274  CB  ASN A 294      -3.258   1.110  35.279  1.00 22.23
ATOM   2275  CG  ASN A 294      -1.922   0.876  34.604  1.00 23.27
ATOM   2276  OD1 ASN A 294      -0.913   1.561  34.815  1.00 22.58
ATOM   2277  ND2 ASN A 294      -1.884  -0.153  33.772  1.00 23.57
ATOM   2278  N   LYS A 295      -5.738   1.367  33.165  1.00 26.46
ATOM   2279  CA  LYS A 295      -6.422   1.076  31.904  1.00 27.92
ATOM   2280  C   LYS A 295      -6.736   2.340  31.127  1.00 28.43
ATOM   2281  O   LYS A 295      -6.681   2.384  29.873  1.00 29.46
ATOM   2282  CB  LYS A 295      -7.706   0.281  32.135  1.00 29.87
ATOM   2283  CG  LYS A 295      -7.554  -1.207  31.876  1.00 33.18
ATOM   2284  CD  LYS A 295      -8.545  -2.099  32.540  1.00 37.49
ATOM   2285  CE  LYS A 295      -9.821  -1.505  33.065  1.00 40.61
ATOM   2286  NZ  LYS A 295     -10.079  -1.995  34.476  1.00 43.43
ATOM   2287  N   ASP A 296      -7.039   3.406  31.845  1.00 28.17
ATOM   2288  CA  ASP A 296      -7.353   4.711  31.275  1.00 27.63
ATOM   2289  C   ASP A 296      -6.066   5.399  30.808  1.00 27.36
ATOM   2290  O   ASP A 296      -6.008   5.886  29.669  1.00 27.70
ATOM   2291  CB  ASP A 296      -8.199   5.553  32.224  1.00 28.58
ATOM   2292  CG  ASP A 296      -8.654   6.848  31.604  1.00 29.92
ATOM   2293  OD1 ASP A 296      -8.756   6.895  30.355  1.00 32.53
ATOM   2294  OD2 ASP A 296      -8.910   7.852  32.273  1.00 31.67
ATOM   2295  N   LYS A 297      -5.081   5.446  31.673  1.00 26.82
ATOM   2296  CA  LYS A 297      -3.757   6.058  31.431  1.00 25.88
ATOM   2297  C   LYS A 297      -2.776   5.353  32.346  1.00 24.82
ATOM   2298  O   LYS A 297      -3.013   5.283  33.566  1.00 25.04
ATOM   2299  CB  LYS A 297      -3.797   7.515  31.856  1.00 29.35
ATOM   2300  CG  LYS A 297      -3.508   8.579  30.837  1.00 33.36
ATOM   2301  CD  LYS A 297      -4.757   8.927  30.019  1.00 38.20
ATOM   2302  CE  LYS A 297      -5.724   9.821  30.737  1.00 40.38
ATOM   2303  NZ  LYS A 297      -7.104   9.832  30.178  1.00 42.45
ATOM   2304  N   PRO A 298      -1.692   4.832  31.819  1.00 23.64
ATOM   2305  CA  PRO A 298      -0.702   4.105  32.636  1.00 23.56
ATOM   2306  C   PRO A 298      -0.142   4.944  33.763  1.00 20.96
ATOM   2307  O   PRO A 298       0.143   6.138  33.551  1.00 22.34
ATOM   2308  CB  PRO A 298       0.356   3.601  31.640  1.00 22.05
ATOM   2309  CG  PRO A 298       0.246   4.648  30.538  1.00 23.79
ATOM   2310  CD  PRO A 298      -1.289   4.832  30.399  1.00 24.54
ATOM   2311  N   LEU A 299       0.047   4.317  34.897  1.00 19.38
ATOM   2312  CA  LEU A 299       0.607   4.967  36.090  1.00 18.86
ATOM   2313  C   LEU A 299       2.126   4.854  36.211  1.00 18.42
ATOM   2314  O   LEU A 299       2.765   5.577  36.989  1.00 17.48
ATOM   2315  CB  LEU A 299      -0.052   4.275  37.304  1.00 17.47
ATOM   2316  CG  LEU A 299      -1.498   4.629  37.563  1.00 18.29
ATOM   2317  CD1 LEU A 299      -2.079   3.678  38.621  1.00 16.21
ATOM   2318  CD2 LEU A 299      -1.542   6.069  38.079  1.00 18.30
ATOM   2319  N   GLY A 300       2.650   3.865  35.467  1.00 16.79
ATOM   2320  CA  GLY A 300       4.076   3.542  35.510  1.00 15.11
ATOM   2321  C   GLY A 300       4.194   2.543  36.650  1.00 14.69
ATOM   2322  O   GLY A 300       3.285   1.709  36.727  1.00 16.11
ATOM   2323  N   ALA A 301       5.224   2.610  37.445  1.00 12.77
ATOM   2324  CA  ALA A 301       5.433   1.718  38.560  1.00 13.31
ATOM   2325  C   ALA A 301       4.441   2.210  39.664  1.00 13.01
ATOM   2326  O   ALA A 301       4.184   3.408  39.694  1.00 13.82
ATOM   2327  CB  ALA A 301       6.867   1.726  39.037  1.00 12.96
ATOM   2328  N   VAL A 302       3.955   1.310  40.453  1.00 12.65
ATOM   2329  CA  VAL A 302       2.971   1.702  41.507  1.00 12.38
ATOM   2330  C   VAL A 302       3.532   1.365  42.870  1.00 12.45
ATOM   2331  O   VAL A 302       4.430   0.534  42.958  1.00 13.74
ATOM   2332  CB  VAL A 302       1.594   1.106  41.212  1.00 11.06
ATOM   2333  CG1 VAL A 302       0.919   1.702  40.023  1.00  8.40
ATOM   2334  CG2 VAL A 302       1.679  -0.420  41.248  1.00 11.78
ATOM   2335  N   ALA A 303       2.976   2.028  43.921  1.00 11.78
ATOM   2336  CA  ALA A 303       3.468   1.795  45.270  1.00 10.28
ATOM   2337  C   ALA A 303       2.943   0.514  45.910  1.00  8.94
ATOM   2338  O   ALA A 303       3.636  -0.039  46.773  1.00  8.91
ATOM   2339  CB  ALA A 303       3.183   3.068  46.081  1.00 11.49
ATOM   2340  N   LEU A 304       1.802   0.050  45.485  1.00  9.94
ATOM   2341  CA  LEU A 304       1.160  -1.188  46.000  1.00  9.82
ATOM   2342  C   LEU A 304       1.935  -2.416  45.506  1.00 11.25
ATOM   2343  O   LEU A 304       1.837  -2.623  44.291  1.00 13.27
ATOM   2344  CB  LEU A 304      -0.268  -1.193  45.487  1.00  8.98
ATOM   2345  CG  LEU A 304      -1.160  -2.304  46.057  1.00  8.95
ATOM   2346  CD1 LEU A 304      -1.380  -2.105  47.557  1.00 11.14
ATOM   2347  CD2 LEU A 304      -2.459  -2.336  45.282  1.00  8.20
ATOM   2348  N   LYS A 305       2.615  -3.113  46.332  1.00 12.00
ATOM   2349  CA  LYS A 305       3.426  -4.265  46.034  1.00 14.15
ATOM   2350  C   LYS A 305       2.770  -5.329  45.166  1.00 15.89
ATOM   2351  O   LYS A 305       3.399  -5.868  44.258  1.00 16.83
ATOM   2352  CB  LYS A 305       3.968  -5.000  47.232  1.00 14.13
ATOM   2353  CG  LYS A 305       5.004  -4.292  48.085  1.00 17.16
ATOM   2354  CD  LYS A 305       4.850  -4.775  49.523  1.00 18.41
ATOM   2355  CE  LYS A 305       6.156  -4.867  50.244  1.00 21.63
ATOM   2356  NZ  LYS A 305       5.845  -5.235  51.663  1.00 22.97
ATOM   2357  N   SER A 306       1.540  -5.650  45.452  1.00 16.87
ATOM   2358  CA  SER A 306       0.773  -6.692  44.767  1.00 17.39
ATOM   2359  C   SER A 306       0.544  -6.394  43.298  1.00 17.81
ATOM   2360  O   SER A 306       0.701  -7.269  42.408  1.00 17.25
ATOM   2361  CB  SER A 306      -0.493  -6.966  45.570  1.00 15.61
ATOM   2362  OG  SER A 306      -1.459  -5.960  45.393  1.00 17.47
ATOM   2363  N   TYR A 307       0.141  -5.162  43.002  1.00 16.77
ATOM   2364  CA  TYR A 307      -0.135  -4.769  41.638  1.00 16.79
ATOM   2365  C   TYR A 307       1.188  -4.483  40.898  1.00 16.58
ATOM   2366  O   TYR A 307       1.257  -4.706  39.692  1.00 17.27
ATOM   2367  CB  TYR A 307      -1.129  -3.621  41.516  1.00 15.73
ATOM   2368  CG  TYR A 307      -1.645  -3.375  40.120  1.00 16.86
ATOM   2369  CD1 TYR A 307      -2.163  -4.443  39.360  1.00 17.69
ATOM   2370  CD2 TYR A 307      -1.617  -2.116  39.542  1.00 17.22
ATOM   2371  CE1 TYR A 307      -2.660  -4.221  38.087  1.00 18.08
ATOM   2372  CE2 TYR A 307      -2.120  -1.873  38.274  1.00 19.05
ATOM   2373  CZ  TYR A 307      -2.624  -2.962  37.541  1.00 18.92
ATOM   2374  OH  TYR A 307      -3.114  -2.700  36.305  1.00 21.10
ATOM   2375  N   GLU A 308       2.167  -4.023  41.629  1.00 16.87
ATOM   2376  CA  GLU A 308       3.453  -3.707  40.993  1.00 18.28
ATOM   2377  C   GLU A 308       4.025  -5.014  40.411  1.00 20.86
ATOM   2378  O   GLU A 308       4.605  -5.033  39.317  1.00 21.33
ATOM   2379  CB  GLU A 308       4.453  -3.131  41.973  1.00 15.12
ATOM   2380  CG  GLU A 308       5.845  -2.872  41.473  1.00 13.23
ATOM   2381  CD  GLU A 308       6.094  -2.122  40.220  1.00 12.23
ATOM   2382  OE1 GLU A 308       5.144  -1.506  39.762  1.00 12.48
ATOM   2383  OE2 GLU A 308       7.210  -2.139  39.665  1.00 14.79
ATOM   2384  N   GLU A 309       3.846  -6.086  41.169  1.00 23.34
ATOM   2385  CA  GLU A 309       4.323  -7.412  40.752  1.00 25.28
ATOM   2386  C   GLU A 309       3.663  -7.838  39.458  1.00 23.96
ATOM   2387  O   GLU A 309       4.337  -8.525  38.666  1.00 24.41
ATOM   2388  CB  GLU A 309       4.268  -8.466  41.825  1.00 28.64
ATOM   2389  CG  GLU A 309       5.494  -8.546  42.756  1.00 34.63
ATOM   2390  CD  GLU A 309       5.297  -9.275  44.046  1.00 39.46
ATOM   2391  OE1 GLU A 309       4.491 -10.233  43.943  1.00 42.21
ATOM   2392  OE2 GLU A 309       5.851  -8.982  45.108  1.00 42.37
ATOM   2393  N   GLU A 310       2.464  -7.415  39.178  1.00 23.15
ATOM   2394  CA  GLU A 310       1.799  -7.753  37.923  1.00 23.31
ATOM   2395  C   GLU A 310       2.373  -6.896  36.800  1.00 21.42
ATOM   2396  O   GLU A 310       2.702  -7.315  35.681  1.00 20.02
ATOM   2397  CB  GLU A 310       0.291  -7.579  37.980  1.00 27.65
ATOM   2398  CG  GLU A 310      -0.507  -7.972  36.744  1.00 36.32
ATOM   2399  CD  GLU A 310      -1.973  -7.674  36.644  1.00 41.10
ATOM   2400  OE1 GLU A 310      -2.654  -8.322  37.488  1.00 42.60
ATOM   2401  OE2 GLU A 310      -2.487  -6.900  35.813  1.00 43.11
ATOM   2402  N   LEU A 311       2.518  -5.614  37.118  1.00 19.32
ATOM   2403  CA  LEU A 311       3.017  -4.609  36.184  1.00 17.23
ATOM   2404  C   LEU A 311       4.461  -4.822  35.749  1.00 15.25
ATOM   2405  O   LEU A 311       4.834  -4.436  34.626  1.00 14.94
ATOM   2406  CB  LEU A 311       2.784  -3.228  36.852  1.00 18.37
ATOM   2407  CG  LEU A 311       1.433  -2.584  36.900  1.00 18.05
ATOM   2408  CD1 LEU A 311       1.554  -1.142  37.459  1.00 16.89
ATOM   2409  CD2 LEU A 311       0.811  -2.512  35.525  1.00 17.02
ATOM   2410  N   ALA A 312       5.262  -5.319  36.636  1.00 14.32
ATOM   2411  CA  ALA A 312       6.667  -5.577  36.465  1.00 14.24
ATOM   2412  C   ALA A 312       6.978  -6.632  35.385  1.00 15.09
ATOM   2413  O   ALA A 312       8.174  -6.860  35.122  1.00 15.93
ATOM   2414  CB  ALA A 312       7.298  -5.886  37.795  1.00 13.86
ATOM   2415  N   LYS A 313       6.013  -7.224  34.753  1.00 15.62
ATOM   2416  CA  LYS A 313       6.161  -8.173  33.623  1.00 15.61
ATOM   2417  C   LYS A 313       6.559  -7.394  32.368  1.00 15.60
ATOM   2418  O   LYS A 313       6.910  -7.905  31.296  1.00 16.09
ATOM   2419  CB  LYS A 313       4.875  -8.941  33.331  1.00 15.73
ATOM   2420  CG  LYS A 313       4.576  -9.921  34.484  1.00 18.36
ATOM   2421  CD  LYS A 313       3.321 -10.757  34.123  1.00 20.05
ATOM   2422  CE  LYS A 313       3.219 -11.865  35.172  1.00 22.83
ATOM   2423  NZ  LYS A 313       1.996 -12.685  35.001  1.00 26.20
ATOM   2424  N   ASP A 314       6.414  -6.078  32.453  1.00 14.85
ATOM   2425  CA  ASP A 314       6.845  -5.119  31.442  1.00 13.62
ATOM   2426  C   ASP A 314       8.235  -4.744  31.981  1.00 14.54
ATOM   2427  O   ASP A 314       8.280  -4.206  33.112  1.00 14.79
ATOM   2428  CB  ASP A 314       5.900  -3.949  31.343  1.00 14.31
ATOM   2429  CG  ASP A 314       6.319  -2.929  30.325  1.00 14.22
ATOM   2430  OD1 ASP A 314       7.505  -2.865  29.968  1.00 15.63
ATOM   2431  OD2 ASP A 314       5.460  -2.196  29.824  1.00 17.39
ATOM   2432  N   PRO A 315       9.296  -5.089  31.285  1.00 13.58
ATOM   2433  CA  PRO A 315      10.629  -4.811  31.771  1.00 13.06
ATOM   2434  C   PRO A 315      10.896  -3.318  31.888  1.00 10.05
ATOM   2435  O   PRO A 315      11.790  -2.997  32.704  1.00 12.24
ATOM   2436  CB  PRO A 315      11.553  -5.614  30.841  1.00 14.11
ATOM   2437  CG  PRO A 315      10.793  -5.594  29.540  1.00 13.96
ATOM   2438  CD  PRO A 315       9.331  -5.740  29.965  1.00 14.82
ATOM   2439  N   ARG A 316      10.199  -2.480  31.231  1.00  9.18
ATOM   2440  CA  ARG A 316      10.373  -0.996  31.334  1.00  9.27
ATOM   2441  C   ARG A 316       9.900  -0.516  32.720  1.00 11.04
ATOM   2442  O   ARG A 316      10.507   0.376  33.368  1.00 10.27
ATOM   2443  CB  ARG A 316       9.560  -0.299  30.272  1.00  8.36
ATOM   2444  CG  ARG A 316       9.966  -0.644  28.841  1.00  9.10
ATOM   2445  CD  ARG A 316       9.082   0.033  27.882  1.00 10.22
ATOM   2446  NE  ARG A 316       7.702  -0.373  27.918  1.00 11.51
ATOM   2447  CZ  ARG A 316       6.654   0.126  27.364  1.00 11.88
ATOM   2448  NH1 ARG A 316       6.641   1.198  26.580  1.00 14.42
ATOM   2449  NH2 ARG A 316       5.443  -0.451  27.536  1.00 16.24
ATOM   2450  N   ILE A 317       8.812  -1.159  33.146  1.00 11.07
ATOM   2451  CA  ILE A 317       8.251  -0.836  34.486  1.00 10.52
ATOM   2452  C   ILE A 317       9.127  -1.393  35.576  1.00 10.62
ATOM   2453  O   ILE A 317       9.384  -0.685  36.604  1.00 11.02
ATOM   2454  CB  ILE A 317       6.739  -1.162  34.585  1.00 10.52
ATOM   2455  CG1 ILE A 317       5.942  -0.170  33.761  1.00 12.18
ATOM   2456  CG2 ILE A 317       6.320  -1.207  36.095  1.00  8.98
ATOM   2457  CD1 ILE A 317       4.492  -0.558  33.381  1.00 16.80
ATOM   2458  N   ALA A 318       9.678  -2.588  35.415  1.00  9.51
ATOM   2459  CA  ALA A 318      10.551  -3.204  36.371  1.00  9.00
ATOM   2460  C   ALA A 318      11.819  -2.350  36.566  1.00 10.36
ATOM   2461  O   ALA A 318      12.382  -2.329  37.682  1.00 10.91
ATOM   2462  CB  ALA A 318      10.999  -4.612  36.001  1.00  8.79
ATOM   2463  N   ALA A 319      12.307  -1.842  35.441  1.00 10.51
ATOM   2464  CA  ALA A 319      13.530  -1.039  35.461  1.00 11.00
ATOM   2465  C   ALA A 319      13.287   0.297  36.218  1.00 11.27
ATOM   2466  O   ALA A 319      14.177   0.665  36.987  1.00 11.44
ATOM   2467  CB  ALA A 319      13.947  -0.759  34.021  1.00 10.89
ATOM   2468  N   THR A 320      12.180   0.905  35.966  1.00 12.52
ATOM   2469  CA  THR A 320      11.718   2.163  36.572  1.00 13.21
ATOM   2470  C   THR A 320      11.759   1.972  38.094  1.00 13.30
ATOM   2471  O   THR A 320      12.385   2.760  38.813  1.00 12.64
ATOM   2472  CB  THR A 320      10.324   2.658  36.080  1.00 13.16
ATOM   2473  OG1 THR A 320      10.385   2.890  34.658  1.00 12.06
ATOM   2474  CG2 THR A 320       9.787   3.944  36.801  1.00 12.92
ATOM   2475  N   MET A 321      11.071   0.949  38.563  1.00 12.91
ATOM   2476  CA  MET A 321      11.060   0.622  40.007  1.00 11.31
ATOM   2477  C   MET A 321      12.415   0.370  40.553  1.00 11.45
ATOM   2478  O   MET A 321      12.786   0.830  41.656  1.00 10.75
ATOM   2479  CB  MET A 321      10.006  -0.434  40.321  1.00 12.72
ATOM   2480  CG  MET A 321      10.078  -0.909  41.746  1.00 13.26
ATOM   2481  SD  MET A 321       9.532   0.455  42.833  1.00 17.65
ATOM   2482  CE  MET A 321       7.784   0.436  42.590  1.00 12.84
ATOM   2483  N   GLU A 322      13.296  -0.374  39.867  1.00 11.40
ATOM   2484  CA  GLU A 322      14.635  -0.666  40.312  1.00 12.26
ATOM   2485  C   GLU A 322      15.523   0.577  40.532  1.00 10.44
ATOM   2486  O   GLU A 322      16.267   0.646  41.506  1.00 10.09
ATOM   2487  CB  GLU A 322      15.421  -1.530  39.265  1.00 15.44
ATOM   2488  CG  GLU A 322      16.608  -2.214  39.897  1.00 22.41
ATOM   2489  CD  GLU A 322      17.376  -3.187  39.076  1.00 27.16
ATOM   2490  OE1 GLU A 322      16.819  -3.426  37.975  1.00 31.40
ATOM   2491  OE2 GLU A 322      18.451  -3.645  39.433  1.00 29.95
ATOM   2492  N   ASN A 323      15.416   1.477  39.593  1.00  9.72
ATOM   2493  CA  ASN A 323      16.144   2.743  39.578  1.00  9.90
ATOM   2494  C   ASN A 323      15.618   3.625  40.770  1.00  9.84
ATOM   2495  O   ASN A 323      16.446   4.241  41.399  1.00  9.18
ATOM   2496  CB  ASN A 323      16.050   3.450  38.247  1.00  8.18
ATOM   2497  CG  ASN A 323      17.101   2.872  37.247  1.00  6.70
ATOM   2498  OD1 ASN A 323      18.232   2.591  37.581  1.00 10.74
ATOM   2499  ND2 ASN A 323      16.607   2.692  36.054  1.00  9.12
ATOM   2500  N   ALA A 324      14.326   3.615  40.899  1.00  9.59
ATOM   2501  CA  ALA A 324      13.622   4.353  41.954  1.00 11.72
ATOM   2502  C   ALA A 324      14.037   3.823  43.314  1.00 12.19
ATOM   2503  O   ALA A 324      14.273   4.622  44.229  1.00 13.37
ATOM   2504  CB  ALA A 324      12.153   4.431  41.701  1.00 11.56
ATOM   2505  N   GLN A 325      14.213   2.544  43.502  1.00 12.59
ATOM   2506  CA  GLN A 325      14.627   1.964  44.762  1.00 14.50
ATOM   2507  C   GLN A 325      16.045   2.323  45.104  1.00 15.10
ATOM   2508  O   GLN A 325      16.442   2.253  46.275  1.00 16.84
ATOM   2509  CB  GLN A 325      14.419   0.452  44.892  1.00 16.38
ATOM   2510  CG  GLN A 325      12.952   0.074  44.965  1.00 20.18
ATOM   2511  CD  GLN A 325      12.713  -1.402  44.867  1.00 24.80
ATOM   2512  OE1 GLN A 325      11.649  -1.836  44.412  1.00 29.73
ATOM   2513  NE2 GLN A 325      13.657  -2.232  45.283  1.00 25.88
ATOM   2514  N   LYS A 326      16.856   2.630  44.134  1.00 16.51
ATOM   2515  CA  LYS A 326      18.248   3.025  44.297  1.00 16.13
ATOM   2516  C   LYS A 326      18.435   4.550  44.316  1.00 14.56
ATOM   2517  O   LYS A 326      19.539   4.990  44.661  1.00 15.48
ATOM   2518  CB  LYS A 326      19.095   2.429  43.157  1.00 18.50
ATOM   2519  CG  LYS A 326      19.399   0.949  43.300  1.00 19.09
ATOM   2520  CD  LYS A 326      19.620   0.308  41.920  1.00 22.93
ATOM   2521  CE  LYS A 326      19.708  -1.204  42.094  1.00 25.58
ATOM   2522  NZ  LYS A 326      20.215  -1.846  40.858  1.00 30.23
ATOM   2523  N   GLY A 327      17.474   5.332  43.960  1.00 13.56
ATOM   2524  CA  GLY A 327      17.490   6.778  43.865  1.00 12.09
ATOM   2525  C   GLY A 327      17.313   7.498  45.200  1.00 12.11
ATOM   2526  O   GLY A 327      17.349   6.917  46.271  1.00 13.08
ATOM   2527  N   GLU A 328      17.178   8.780  45.119  1.00 12.62
ATOM   2528  CA  GLU A 328      17.008   9.744  46.208  1.00 12.63
ATOM   2529  C   GLU A 328      15.647  10.350  46.192  1.00 11.11
ATOM   2530  O   GLU A 328      15.249  11.051  45.207  1.00 11.61
ATOM   2531  CB  GLU A 328      18.078  10.868  46.043  1.00 13.55
ATOM   2532  CG  GLU A 328      17.988  11.953  47.151  1.00 15.48
ATOM   2533  CD  GLU A 328      19.084  12.949  47.333  1.00 18.39
ATOM   2534  OE1 GLU A 328      19.960  12.955  46.435  1.00 16.83
ATOM   2535  OE2 GLU A 328      19.133  13.728  48.281  1.00 17.93
ATOM   2536  N   ILE A 329      14.829  10.100  47.233  1.00 11.59
ATOM   2537  CA  ILE A 329      13.483  10.739  47.222  1.00 12.02
ATOM   2538  C   ILE A 329      13.698  12.265  47.146  1.00 12.33
ATOM   2539  O   ILE A 329      14.534  12.759  47.904  1.00 13.98
ATOM   2540  CB  ILE A 329      12.602  10.381  48.437  1.00 13.31
ATOM   2541  CG1 ILE A 329      12.109   8.917  48.377  1.00 14.53
ATOM   2542  CG2 ILE A 329      11.375  11.326  48.590  1.00 12.62
ATOM   2543  CD1 ILE A 329      12.091   8.253  49.794  1.00 17.67
ATOM   2544  N   MET A 330      13.018  12.959  46.301  1.00 12.42
ATOM   2545  CA  MET A 330      13.182  14.410  46.191  1.00 14.72
ATOM   2546  C   MET A 330      12.626  15.083  47.482  1.00 15.57
ATOM   2547  O   MET A 330      11.437  14.894  47.753  1.00 14.78
ATOM   2548  CB  MET A 330      12.358  14.888  44.997  1.00 15.11
ATOM   2549  CG  MET A 330      12.866  16.192  44.452  1.00 17.96
ATOM   2550  SD  MET A 330      11.737  16.625  43.101  1.00 27.27
ATOM   2551  CE  MET A 330      11.931  15.238  42.005  1.00 20.93
ATOM   2552  N   PRO A 331      13.452  15.836  48.175  1.00 16.28
ATOM   2553  CA  PRO A 331      13.037  16.584  49.392  1.00 16.35
ATOM   2554  C   PRO A 331      11.841  17.458  49.129  1.00 16.07
ATOM   2555  O   PRO A 331      11.667  18.125  48.121  1.00 15.60
ATOM   2556  CB  PRO A 331      14.300  17.362  49.781  1.00 15.51
ATOM   2557  CG  PRO A 331      15.418  16.448  49.273  1.00 16.41
ATOM   2558  CD  PRO A 331      14.887  16.075  47.883  1.00 15.66
ATOM   2559  N   ASN A 332      10.860  17.425  50.061  1.00 17.52
ATOM   2560  CA  ASN A 332       9.617  18.188  49.916  1.00 19.60
ATOM   2561  C   ASN A 332       9.600  19.572  50.596  1.00 21.69
ATOM   2562  O   ASN A 332       8.551  20.250  50.582  1.00 21.90
ATOM   2563  CB  ASN A 332       8.421  17.332  50.337  1.00 19.05
ATOM   2564  CG  ASN A 332       8.460  16.936  51.801  1.00 19.14
ATOM   2565  OD1 ASN A 332       9.452  17.186  52.492  1.00 19.49
ATOM   2566  ND2 ASN A 332       7.426  16.249  52.275  1.00 18.42
ATOM   2567  N   ILE A 333      10.724  19.968  51.143  1.00 23.54
ATOM   2568  CA  ILE A 333      10.950  21.225  51.863  1.00 23.73
ATOM   2569  C   ILE A 333      11.223  22.366  50.893  1.00 26.41
ATOM   2570  O   ILE A 333      11.666  22.169  49.756  1.00 26.88
ATOM   2571  CB  ILE A 333      12.096  21.072  52.891  1.00 22.71
ATOM   2572  CG1 ILE A 333      13.423  20.826  52.124  1.00 20.87
ATOM   2573  CG2 ILE A 333      11.792  19.973  53.960  1.00 22.55
ATOM   2574  CD1 ILE A 333      14.655  20.520  52.983  1.00 22.28
ATOM   2575  N   PRO A 334      10.921  23.564  51.411  1.00 28.09
ATOM   2576  CA  PRO A 334      11.079  24.813  50.685  1.00 27.09
ATOM   2577  C   PRO A 334      12.487  25.152  50.276  1.00 26.07
ATOM   2578  O   PRO A 334      12.670  25.767  49.220  1.00 25.78
ATOM   2579  CB  PRO A 334      10.439  25.850  51.622  1.00 28.87
ATOM   2580  CG  PRO A 334      10.505  25.246  52.989  1.00 29.02
ATOM   2581  CD  PRO A 334      10.401  23.751  52.790  1.00 28.33
ATOM   2582  N   GLN A 335      13.504  24.798  51.001  1.00 26.10
ATOM   2583  CA  GLN A 335      14.902  25.036  50.680  1.00 27.64
ATOM   2584  C   GLN A 335      15.357  24.348  49.387  1.00 27.88
ATOM   2585  O   GLN A 335      16.495  24.544  48.922  1.00 28.37
ATOM   2586  CB  GLN A 335      15.796  24.539  51.827  1.00 30.20
ATOM   2587  CG  GLN A 335      15.580  25.211  53.138  1.00 35.26
ATOM   2588  CD  GLN A 335      14.533  24.674  54.064  1.00 36.99
ATOM   2589  OE1 GLN A 335      14.416  23.482  54.330  1.00 39.83
ATOM   2590  NE2 GLN A 335      13.774  25.585  54.673  1.00 39.04
ATOM   2591  N   MET A 336      14.522  23.482  48.849  1.00 27.07
ATOM   2592  CA  MET A 336      14.777  22.722  47.612  1.00 25.43
ATOM   2593  C   MET A 336      14.834  23.708  46.457  1.00 25.18
ATOM   2594  O   MET A 336      15.507  23.433  45.453  1.00 25.17
ATOM   2595  CB  MET A 336      13.741  21.635  47.453  1.00 25.09
ATOM   2596  CG  MET A 336      14.017  20.503  46.565  1.00 22.74
ATOM   2597  SD  MET A 336      15.603  19.686  46.839  1.00 21.02
ATOM   2598  CE  MET A 336      15.740  18.937  45.203  1.00 20.76
ATOM   2599  N   SER A 337      14.160  24.842  46.593  1.00 24.45
ATOM   2600  CA  SER A 337      14.202  25.835  45.507  1.00 25.72
ATOM   2601  C   SER A 337      15.627  26.385  45.362  1.00 24.95
ATOM   2602  O   SER A 337      16.102  26.713  44.259  1.00 26.91
ATOM   2603  CB  SER A 337      13.237  26.971  45.770  1.00 27.38
ATOM   2604  OG  SER A 337      12.071  26.442  46.376  1.00 33.01
ATOM   2605  N   ALA A 338      16.308  26.519  46.465  1.00 24.10
ATOM   2606  CA  ALA A 338      17.684  27.013  46.480  1.00 22.50
ATOM   2607  C   ALA A 338      18.587  26.013  45.757  1.00 21.10
ATOM   2608  O   ALA A 338      19.499  26.398  45.022  1.00 19.75
ATOM   2609  CB  ALA A 338      18.148  27.204  47.914  1.00 23.74
ATOM   2610  N   PHE A 339      18.340  24.748  46.050  1.00 19.37
ATOM   2611  CA  PHE A 339      19.104  23.639  45.450  1.00 17.84
ATOM   2612  C   PHE A 339      18.950  23.668  43.932  1.00 17.13
ATOM   2613  O   PHE A 339      19.970  23.613  43.223  1.00 16.70
ATOM   2614  CB  PHE A 339      18.773  22.289  46.085  1.00 17.26
ATOM   2615  CG  PHE A 339      19.355  21.052  45.438  1.00 16.13
ATOM   2616  CD1 PHE A 339      18.783  20.531  44.274  1.00 16.92
ATOM   2617  CD2 PHE A 339      20.445  20.412  45.998  1.00 15.34
ATOM   2618  CE1 PHE A 339      19.308  19.402  43.657  1.00 14.62
ATOM   2619  CE2 PHE A 339      20.980  19.278  45.417  1.00 15.91
ATOM   2620  CZ  PHE A 339      20.391  18.788  44.258  1.00 14.44
ATOM   2621  N   TRP A 340      17.761  23.791  43.407  1.00 17.90
ATOM   2622  CA  TRP A 340      17.582  23.779  41.960  1.00 20.03
ATOM   2623  C   TRP A 340      18.450  24.815  41.272  1.00 21.91
ATOM   2624  O   TRP A 340      19.239  24.493  40.373  1.00 20.60
ATOM   2625  CB  TRP A 340      16.143  23.754  41.488  1.00 21.10
ATOM   2626  CG  TRP A 340      15.367  22.538  41.862  1.00 22.51
ATOM   2627  CD1 TRP A 340      14.250  22.498  42.647  1.00 23.59
ATOM   2628  CD2 TRP A 340      15.652  21.171  41.518  1.00 23.76
ATOM   2629  NE1 TRP A 340      13.824  21.206  42.807  1.00 24.52
ATOM   2630  CE2 TRP A 340      14.670  20.374  42.128  1.00 23.86
ATOM   2631  CE3 TRP A 340      16.624  20.556  40.738  1.00 24.45
ATOM   2632  CZ2 TRP A 340      14.646  18.989  41.989  1.00 24.36
ATOM   2633  CZ3 TRP A 340      16.598  19.191  40.590  1.00 23.78
ATOM   2634  CH2 TRP A 340      15.629  18.409  41.219  1.00 23.96
ATOM   2635  N   TYR A 341      18.256  26.072  41.694  1.00 23.83
ATOM   2636  CA  TYR A 341      19.008  27.187  41.075  1.00 24.81
ATOM   2637  C   TYR A 341      20.492  27.047  41.285  1.00 21.76
ATOM   2638  O   TYR A 341      21.225  27.222  40.295  1.00 21.78
ATOM   2639  CB  TYR A 341      18.450  28.588  41.443  1.00 30.63
ATOM   2640  CG  TYR A 341      19.407  29.334  42.345  1.00 38.04
ATOM   2641  CD1 TYR A 341      19.385  29.099  43.725  1.00 41.29
ATOM   2642  CD2 TYR A 341      20.402  30.182  41.834  1.00 41.27
ATOM   2643  CE1 TYR A 341      20.293  29.698  44.602  1.00 43.58
ATOM   2644  CE2 TYR A 341      21.309  30.812  42.696  1.00 44.43
ATOM   2645  CZ  TYR A 341      21.251  30.565  44.078  1.00 45.41
ATOM   2646  OH  TYR A 341      22.122  31.163  44.966  1.00 47.19
ATOM   2647  N   ALA A 342      20.965  26.770  42.471  1.00 19.43
ATOM   2648  CA  ALA A 342      22.374  26.643  42.755  1.00 19.79
ATOM   2649  C   ALA A 342      23.101  25.567  41.949  1.00 20.42
ATOM   2650  O   ALA A 342      24.182  25.798  41.365  1.00 20.16
ATOM   2651  CB  ALA A 342      22.647  26.443  44.223  1.00 18.12
ATOM   2652  N   VAL A 343      22.588  24.364  42.057  1.00 20.75
ATOM   2653  CA  VAL A 343      23.160  23.194  41.342  1.00 20.41
ATOM   2654  C   VAL A 343      23.007  23.404  39.834  1.00 19.97
ATOM   2655  O   VAL A 343      23.914  23.049  39.040  1.00 19.84
ATOM   2656  CB  VAL A 343      22.561  21.902  41.946  1.00 20.57
ATOM   2657  CG1 VAL A 343      22.929  20.692  41.067  1.00 20.75
ATOM   2658  CG2 VAL A 343      23.032  21.662  43.376  1.00 18.69
ATOM   2659  N   ARG A 344      21.956  24.046  39.388  1.00 20.27
ATOM   2660  CA  ARG A 344      21.791  24.300  37.943  1.00 22.58
ATOM   2661  C   ARG A 344      22.985  25.102  37.428  1.00 22.64
ATOM   2662  O   ARG A 344      23.685  24.786  36.453  1.00 22.17
ATOM   2663  CB  ARG A 344      20.455  24.910  37.606  1.00 23.90
ATOM   2664  CG  ARG A 344      20.373  25.411  36.166  1.00 28.13
ATOM   2665  CD  ARG A 344      19.232  24.897  35.445  1.00 32.95
ATOM   2666  NE  ARG A 344      18.003  25.610  35.419  1.00 37.83
ATOM   2667  CZ  ARG A 344      16.891  25.375  36.109  1.00 41.52
ATOM   2668  NH1 ARG A 344      16.807  24.412  37.030  1.00 42.62
ATOM   2669  NH2 ARG A 344      15.784  26.120  35.914  1.00 44.05
ATOM   2670  N   THR A 345      23.264  26.156  38.189  1.00 23.16
ATOM   2671  CA  THR A 345      24.385  27.065  37.912  1.00 22.26
ATOM   2672  C   THR A 345      25.700  26.361  38.047  1.00 20.53
ATOM   2673  O   THR A 345      26.521  26.476  37.116  1.00 22.20
ATOM   2674  CB  THR A 345      24.307  28.380  38.791  1.00 22.83
ATOM   2675  OG1 THR A 345      23.066  29.030  38.371  1.00 23.69
ATOM   2676  CG2 THR A 345      25.498  29.317  38.591  1.00 22.50
ATOM   2677  N   ALA A 346      25.968  25.634  39.085  1.00 19.87
ATOM   2678  CA  ALA A 346      27.226  24.929  39.264  1.00 19.65
ATOM   2679  C   ALA A 346      27.578  24.040  38.076  1.00 21.10
ATOM   2680  O   ALA A 346      28.752  23.969  37.670  1.00 21.76
ATOM   2681  CB  ALA A 346      27.250  24.100  40.555  1.00 18.82
ATOM   2682  N   VAL A 347      26.585  23.339  37.545  1.00 21.80
ATOM   2683  CA  VAL A 347      26.855  22.396  36.448  1.00 22.46
ATOM   2684  C   VAL A 347      27.133  23.104  35.136  1.00 22.77
ATOM   2685  O   VAL A 347      28.075  22.689  34.422  1.00 22.41
ATOM   2686  CB  VAL A 347      25.806  21.265  36.379  1.00 22.19
ATOM   2687  CG1 VAL A 347      26.015  20.373  35.149  1.00 21.50
ATOM   2688  CG2 VAL A 347      25.828  20.370  37.611  1.00 21.25
ATOM   2689  N   ILE A 348      26.348  24.103  34.809  1.00 23.64
ATOM   2690  CA  ILE A 348      26.550  24.832  33.534  1.00 24.52
ATOM   2691  C   ILE A 348      27.912  25.527  33.568  1.00 24.40
ATOM   2692  O   ILE A 348      28.555  25.620  32.535  1.00 25.73
ATOM   2693  CB  ILE A 348      25.388  25.813  33.216  1.00 25.06
ATOM   2694  CG1 ILE A 348      24.091  25.143  32.727  1.00 25.20
ATOM   2695  CG2 ILE A 348      25.832  26.880  32.177  1.00 26.57
ATOM   2696  CD1 ILE A 348      23.896  23.651  33.085  1.00 27.84
ATOM   2697  N   ASN A 349      28.340  25.976  34.718  1.00 24.62
ATOM   2698  CA  ASN A 349      29.576  26.689  34.942  1.00 23.42
ATOM   2699  C   ASN A 349      30.758  25.767  34.823  1.00 23.43
ATOM   2700  O   ASN A 349      31.693  26.193  34.139  1.00 23.96
ATOM   2701  CB  ASN A 349      29.614  27.498  36.238  1.00 24.50
ATOM   2702  CG  ASN A 349      28.824  28.799  36.135  1.00 24.78
ATOM   2703  OD1 ASN A 349      28.183  29.136  35.130  1.00 23.45
ATOM   2704  ND2 ASN A 349      28.831  29.508  37.270  1.00 25.68
ATOM   2705  N   ALA A 350      30.707  24.643  35.491  1.00 23.54
ATOM   2706  CA  ALA A 350      31.783  23.665  35.434  1.00 24.91
ATOM   2707  C   ALA A 350      31.925  23.086  34.023  1.00 26.39
ATOM   2708  O   ALA A 350      33.042  22.743  33.617  1.00 27.53
ATOM   2709  CB  ALA A 350      31.623  22.536  36.447  1.00 23.50
ATOM   2710  N   ALA A 351      30.839  22.938  33.333  1.00 28.87
ATOM   2711  CA  ALA A 351      30.709  22.362  32.007  1.00 31.67
ATOM   2712  C   ALA A 351      31.255  23.252  30.893  1.00 33.28
ATOM   2713  O   ALA A 351      31.778  22.721  29.895  1.00 34.67
ATOM   2714  CB  ALA A 351      29.240  22.040  31.660  1.00 31.04
ATOM   2715  N   SER A 352      31.050  24.526  31.063  1.00 34.40
ATOM   2716  CA  SER A 352      31.481  25.553  30.131  1.00 36.03
ATOM   2717  C   SER A 352      32.855  26.094  30.471  1.00 37.23
ATOM   2718  O   SER A 352      33.262  27.075  29.818  1.00 39.13
ATOM   2719  CB  SER A 352      30.449  26.692  30.095  1.00 37.12
ATOM   2720  OG  SER A 352      30.419  27.401  31.322  1.00 37.75
ATOM   2721  N   GLY A 353      33.573  25.574  31.438  1.00 37.48
ATOM   2722  CA  GLY A 353      34.890  26.009  31.841  1.00 37.54
ATOM   2723  C   GLY A 353      34.917  27.302  32.648  1.00 38.10
ATOM   2724  O   GLY A 353      35.974  27.678  33.209  1.00 38.07
ATOM   2725  N   ARG A 354      33.795  27.972  32.713  1.00 38.98
ATOM   2726  CA  ARG A 354      33.611  29.239  33.450  1.00 39.67
ATOM   2727  C   ARG A 354      34.072  29.114  34.897  1.00 38.66
ATOM   2728  O   ARG A 354      34.449  30.148  35.508  1.00 39.18
ATOM   2729  CB  ARG A 354      32.195  29.764  33.314  1.00 42.62
ATOM   2730  CG  ARG A 354      31.885  31.234  33.444  1.00 47.62
ATOM   2731  CD  ARG A 354      30.705  31.694  32.640  1.00 51.53
ATOM   2732  NE  ARG A 354      30.911  31.703  31.197  1.00 56.21
ATOM   2733  CZ  ARG A 354      30.154  32.107  30.175  1.00 56.98
ATOM   2734  NH1 ARG A 354      28.920  32.613  30.325  1.00 56.73
ATOM   2735  NH2 ARG A 354      30.602  32.017  28.908  1.00 56.65
ATOM   2736  N   GLN A 355      34.101  27.907  35.451  1.00 35.98
ATOM   2737  CA  GLN A 355      34.562  27.709  36.851  1.00 33.67
ATOM   2738  C   GLN A 355      35.064  26.277  36.960  1.00 32.55
ATOM   2739  O   GLN A 355      34.690  25.477  36.088  1.00 33.69
ATOM   2740  CB  GLN A 355      33.431  27.964  37.822  1.00 33.47
ATOM   2741  CG  GLN A 355      33.728  28.783  39.045  1.00 34.10
ATOM   2742  CD  GLN A 355      32.471  29.047  39.842  1.00 35.38
ATOM   2743  OE1 GLN A 355      31.372  29.003  39.271  1.00 37.00
ATOM   2744  NE2 GLN A 355      32.612  29.281  41.146  1.00 35.44
ATOM   2745  N   THR A 356      35.886  25.958  37.924  1.00 31.00
ATOM   2746  CA  THR A 356      36.388  24.599  38.127  1.00 30.03
ATOM   2747  C   THR A 356      35.322  23.831  38.933  1.00 29.61
ATOM   2748  O   THR A 356      34.370  24.457  39.436  1.00 29.53
ATOM   2749  CB  THR A 356      37.780  24.521  38.838  1.00 30.02
ATOM   2750  OG1 THR A 356      37.577  24.886  40.234  1.00 28.90
ATOM   2751  CG2 THR A 356      38.859  25.380  38.170  1.00 30.64
ATOM   2752  N   VAL A 357      35.504  22.532  39.033  1.00 28.81
ATOM   2753  CA  VAL A 357      34.573  21.648  39.739  1.00 27.35
ATOM   2754  C   VAL A 357      34.544  21.997  41.227  1.00 28.04
ATOM   2755  O   VAL A 357      33.483  22.172  41.834  1.00 26.74
ATOM   2756  CB  VAL A 357      34.813  20.178  39.377  1.00 24.47
ATOM   2757  CG1 VAL A 357      34.065  19.219  40.288  1.00 21.91
ATOM   2758  CG2 VAL A 357      34.379  19.962  37.921  1.00 23.58
ATOM   2759  N   ASP A 358      35.728  22.094  41.765  1.00 30.09
ATOM   2760  CA  ASP A 358      35.932  22.455  43.170  1.00 32.42
ATOM   2761  C   ASP A 358      35.256  23.797  43.499  1.00 31.97
ATOM   2762  O   ASP A 358      34.682  23.914  44.590  1.00 31.98
ATOM   2763  CB  ASP A 358      37.435  22.467  43.462  1.00 35.92
ATOM   2764  CG  ASP A 358      38.072  21.155  43.061  1.00 40.70
ATOM   2765  OD1 ASP A 358      37.867  20.213  43.859  1.00 43.43
ATOM   2766  OD2 ASP A 358      38.711  21.018  41.994  1.00 44.57
ATOM   2767  N   GLU A 359      35.353  24.750  42.618  1.00 31.20
ATOM   2768  CA  GLU A 359      34.826  26.097  42.725  1.00 31.07
ATOM   2769  C   GLU A 359      33.318  26.144  42.572  1.00 28.90
ATOM   2770  O   GLU A 359      32.589  26.728  43.387  1.00 27.68
ATOM   2771  CB  GLU A 359      35.366  27.030  41.629  1.00 34.64
ATOM   2772  CG  GLU A 359      36.789  27.514  41.598  1.00 40.11
ATOM   2773  CD  GLU A 359      37.382  28.173  40.374  1.00 42.50
ATOM   2774  OE1 GLU A 359      36.550  28.622  39.541  1.00 42.59
ATOM   2775  OE2 GLU A 359      38.607  28.288  40.188  1.00 42.58
ATOM   2776  N   ALA A 360      32.877  25.567  41.466  1.00 26.69
ATOM   2777  CA  ALA A 360      31.455  25.488  41.111  1.00 25.03
ATOM   2778  C   ALA A 360      30.618  24.869  42.234  1.00 23.30
ATOM   2779  O   ALA A 360      29.540  25.396  42.528  1.00 23.17
ATOM   2780  CB  ALA A 360      31.250  24.688  39.819  1.00 23.72
ATOM   2781  N   LEU A 361      31.113  23.788  42.822  1.00 22.80
ATOM   2782  CA  LEU A 361      30.366  23.109  43.876  1.00 22.41
ATOM   2783  C   LEU A 361      30.506  23.817  45.205  1.00 23.41
ATOM   2784  O   LEU A 361      29.509  23.822  45.944  1.00 23.56
ATOM   2785  CB  LEU A 361      30.636  21.616  43.964  1.00 20.85
ATOM   2786  CG  LEU A 361      30.227  20.754  42.758  1.00 19.58
ATOM   2787  CD1 LEU A 361      30.864  19.396  42.913  1.00 18.89
ATOM   2788  CD2 LEU A 361      28.719  20.679  42.635  1.00 16.98
ATOM   2789  N   LYS A 362      31.678  24.341  45.473  1.00 24.79
ATOM   2790  CA  LYS A 362      31.886  25.077  46.752  1.00 26.64
ATOM   2791  C   LYS A 362      30.858  26.205  46.808  1.00 26.64
ATOM   2792  O   LYS A 362      30.185  26.340  47.848  1.00 27.30
ATOM   2793  CB  LYS A 362      33.297  25.593  46.852  1.00 29.03
ATOM   2794  CG  LYS A 362      33.733  26.341  48.099  1.00 32.39
ATOM   2795  CD  LYS A 362      34.223  27.747  47.721  1.00 35.21
ATOM   2796  CE  LYS A 362      33.060  28.737  47.710  1.00 36.66
ATOM   2797  NZ  LYS A 362      33.407  29.912  46.869  1.00 37.14
ATOM   2798  N   ASP A 363      30.670  26.953  45.746  1.00 25.98
ATOM   2799  CA  ASP A 363      29.737  28.041  45.623  1.00 26.50
ATOM   2800  C   ASP A 363      28.280  27.614  45.849  1.00 26.21
ATOM   2801  O   ASP A 363      27.530  28.290  46.550  1.00 26.75
ATOM   2802  CB  ASP A 363      29.814  28.739  44.267  1.00 29.33
ATOM   2803  CG  ASP A 363      30.967  29.698  44.123  1.00 33.10
ATOM   2804  OD1 ASP A 363      31.874  29.677  44.978  1.00 35.62
ATOM   2805  OD2 ASP A 363      30.953  30.454  43.128  1.00 34.54
ATOM   2806  N   ALA A 364      27.891  26.570  45.156  1.00 25.29
ATOM   2807  CA  ALA A 364      26.522  26.040  45.240  1.00 24.17
ATOM   2808  C   ALA A 364      26.222  25.625  46.675  1.00 23.18
ATOM   2809  O   ALA A 364      25.158  25.967  47.173  1.00 21.49
ATOM   2810  CB  ALA A 364      26.346  24.908  44.240  1.00 24.44
ATOM   2811  N   GLN A 365      27.135  24.918  47.290  1.00 24.21
ATOM   2812  CA  GLN A 365      27.014  24.475  48.683  1.00 26.18
ATOM   2813  C   GLN A 365      26.720  25.712  49.559  1.00 27.66
ATOM   2814  O   GLN A 365      25.850  25.711  50.430  1.00 28.07
ATOM   2815  CB  GLN A 365      28.240  23.761  49.224  1.00 27.09
ATOM   2816  CG  GLN A 365      28.193  23.317  50.663  1.00 27.84
ATOM   2817  CD  GLN A 365      27.507  22.007  50.951  1.00 28.82
ATOM   2818  OE1 GLN A 365      27.416  21.106  50.120  1.00 27.93
ATOM   2819  NE2 GLN A 365      27.004  21.867  52.190  1.00 28.93
ATOM   2820  N   THR A 366      27.484  26.751  49.305  1.00 28.28
ATOM   2821  CA  THR A 366      27.378  28.034  49.990  1.00 29.21
ATOM   2822  C   THR A 366      26.004  28.644  49.842  1.00 29.72
ATOM   2823  O   THR A 366      25.438  29.001  50.890  1.00 30.59
ATOM   2824  CB  THR A 366      28.551  28.982  49.530  1.00 29.08
ATOM   2825  OG1 THR A 366      29.709  28.452  50.245  1.00 31.00
ATOM   2826  CG2 THR A 366      28.323  30.451  49.757  1.00 30.59
ATOM   2827  N   ARG A 367      25.452  28.763  48.665  1.00 30.18
ATOM   2828  CA  ARG A 367      24.144  29.342  48.445  1.00 32.31
ATOM   2829  C   ARG A 367      22.970  28.560  49.004  1.00 33.57
ATOM   2830  O   ARG A 367      21.875  29.168  49.124  1.00 34.04
ATOM   2831  CB  ARG A 367      23.904  29.520  46.929  1.00 34.56
ATOM   2832  CG  ARG A 367      24.939  30.433  46.300  1.00 39.11
ATOM   2833  CD  ARG A 367      24.882  30.434  44.819  1.00 43.21
ATOM   2834  NE  ARG A 367      26.213  30.447  44.224  1.00 48.22
ATOM   2835  CZ  ARG A 367      26.782  31.468  43.583  1.00 49.51
ATOM   2836  NH1 ARG A 367      26.121  32.612  43.412  1.00 49.79
ATOM   2837  NH2 ARG A 367      28.026  31.345  43.092  1.00 50.57
ATOM   2838  N   ILE A 368      23.146  27.260  49.259  1.00 33.93
ATOM   2839  CA  ILE A 368      22.087  26.383  49.756  1.00 33.32
ATOM   2840  C   ILE A 368      21.963  26.480  51.292  1.00 34.06
ATOM   2841  O   ILE A 368      20.846  26.516  51.810  1.00 33.94
ATOM   2842  CB  ILE A 368      22.232  24.863  49.375  1.00 31.69
ATOM   2843  CG1 ILE A 368      22.510  24.607  47.879  1.00 29.79
ATOM   2844  CG2 ILE A 368      20.981  24.041  49.821  1.00 29.88
ATOM   2845  CD1 ILE A 368      21.507  25.316  46.962  1.00 29.73
ATOM   2846  N   THR A 369      23.100  26.434  51.939  1.00 34.81
ATOM   2847  CA  THR A 369      23.238  26.478  53.389  1.00 36.71
ATOM   2848  C   THR A 369      23.331  27.926  53.900  1.00 39.41
ATOM   2849  O   THR A 369      23.637  28.118  55.084  1.00 40.66
ATOM   2850  CB  THR A 369      24.496  25.654  53.869  1.00 34.83
ATOM   2851  OG1 THR A 369      25.637  26.332  53.254  1.00 32.76
ATOM   2852  CG2 THR A 369      24.475  24.170  53.525  1.00 34.14
ATOM   2853  N   LYS A 370      23.128  28.870  53.013  1.00 42.01
ATOM   2854  CA  LYS A 370      23.141  30.325  53.240  1.00 44.26
ATOM   2855  C   LYS A 370      21.843  30.688  53.979  1.00 46.19
ATOM   2857  CB  LYS A 370      23.182  31.093  51.932  1.00 43.89
ATOM   2858  CG  LYS A 370      23.436  32.581  51.905  1.00 44.72
ATOM   2859  CD  LYS A 370      24.906  32.927  52.118  1.00 47.02
ATOM   2860  CE  LYS A 370      25.210  34.328  52.582  1.00 46.79
ATOM   2861  NZ  LYS A 370      24.794  34.569  53.990  1.00 46.84
TER   



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.