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 University of Michigan   |   College of Pharmacy   |   Medicinal Chemistry

1F88      
ATOM      1  N   MET A   1      -3.244  18.282  15.898  1.00 54.29
ATOM      2  CA  MET A   1      -3.881  17.764  14.682  1.00 53.52
ATOM      3  C   MET A   1      -3.231  16.473  14.187  1.00 52.77
ATOM      4  O   MET A   1      -1.997  16.382  14.099  1.00 51.10
ATOM      5  CB  MET A   1      -3.829  18.816  13.569  1.00 53.58
ATOM      6  CG  MET A   1      -5.142  19.537  13.318  1.00 52.13
ATOM      7  SD  MET A   1      -5.946  19.998  14.838  1.00 51.12
ATOM      8  CE  MET A   1      -7.616  19.525  14.514  1.00 51.57
ATOM      9  OXT MET A   1      -3.995  16.650  17.265  1.00 54.79
ATOM     10  N   ASN A   2      -4.076  15.490  13.863  1.00 52.60
ATOM     11  CA  ASN A   2      -3.634  14.175  13.374  1.00 52.31
ATOM     12  C   ASN A   2      -3.460  14.190  11.861  1.00 50.52
ATOM     13  O   ASN A   2      -3.023  13.206  11.260  1.00 49.47
ATOM     14  CB  ASN A   2      -4.647  13.078  13.735  1.00 53.74
ATOM     15  CG  ASN A   2      -5.007  13.065  15.209  1.00 55.48
ATOM     16  OD1 ASN A   2      -4.278  12.510  16.040  1.00 54.59
ATOM     17  ND2 ASN A   2      -6.148  13.676  15.524  1.00 59.21
ATOM     18  N   GLY A   3      -3.834  15.310  11.258  1.00 49.38
ATOM     19  CA  GLY A   3      -3.718  15.449   9.827  1.00 48.15
ATOM     20  C   GLY A   3      -3.495  16.874   9.371  1.00 47.25
ATOM     21  O   GLY A   3      -4.028  17.831   9.939  1.00 48.00
ATOM     22  N   THR A   4      -2.691  17.001   8.328  1.00 45.08
ATOM     23  CA  THR A   4      -2.388  18.285   7.749  1.00 44.41
ATOM     24  C   THR A   4      -3.497  18.608   6.752  1.00 44.61
ATOM     25  O   THR A   4      -3.663  17.895   5.768  1.00 44.85
ATOM     26  CB  THR A   4      -1.032  18.231   7.026  1.00 43.60
ATOM     27  OG1 THR A   4      -0.033  17.764   7.934  1.00 44.84
ATOM     28  CG2 THR A   4      -0.628  19.590   6.536  1.00 43.69
ATOM     29  N   GLU A   5      -4.306  19.622   7.061  1.00 45.88
ATOM     30  CA  GLU A   5      -5.392  20.060   6.176  1.00 47.26
ATOM     31  C   GLU A   5      -4.922  21.238   5.332  1.00 48.31
ATOM     32  O   GLU A   5      -4.474  22.251   5.870  1.00 49.86
ATOM     33  CB  GLU A   5      -6.643  20.492   6.961  1.00 46.89
ATOM     34  CG  GLU A   5      -7.726  21.154   6.067  1.00 49.26
ATOM     35  CD  GLU A   5      -9.035  21.522   6.796  1.00 52.49
ATOM     36  OE1 GLU A   5      -9.181  21.186   7.994  1.00 55.51
ATOM     37  OE2 GLU A   5      -9.931  22.146   6.165  1.00 51.62
ATOM     38  N   GLY A   6      -5.001  21.093   4.012  1.00 48.23
ATOM     39  CA  GLY A   6      -4.606  22.168   3.122  1.00 47.09
ATOM     40  C   GLY A   6      -5.858  22.751   2.501  1.00 47.73
ATOM     41  O   GLY A   6      -6.961  22.261   2.755  1.00 48.01
ATOM     42  N   PRO A   7      -5.733  23.801   1.681  1.00 48.43
ATOM     43  CA  PRO A   7      -6.909  24.412   1.046  1.00 49.55
ATOM     44  C   PRO A   7      -7.473  23.544  -0.080  1.00 50.59
ATOM     45  O   PRO A   7      -8.572  23.790  -0.586  1.00 51.69
ATOM     46  CB  PRO A   7      -6.350  25.726   0.506  1.00 49.28
ATOM     47  CG  PRO A   7      -4.939  25.354   0.144  1.00 49.99
ATOM     48  CD  PRO A   7      -4.497  24.523   1.330  1.00 48.82
ATOM     49  N   ASN A   8      -6.720  22.496  -0.408  1.00 50.89
ATOM     50  CA  ASN A   8      -7.028  21.549  -1.479  1.00 49.69
ATOM     51  C   ASN A   8      -7.070  20.088  -1.038  1.00 49.33
ATOM     52  O   ASN A   8      -7.677  19.245  -1.710  1.00 50.17
ATOM     53  CB  ASN A   8      -5.916  21.627  -2.518  1.00 48.85
ATOM     54  CG  ASN A   8      -6.247  22.522  -3.658  1.00 50.39
ATOM     55  OD1 ASN A   8      -5.513  22.556  -4.642  1.00 49.94
ATOM     56  ND2 ASN A   8      -7.364  23.251  -3.559  1.00 51.61
ATOM     57  N   PHE A   9      -6.428  19.801   0.091  1.00 47.46
ATOM     58  CA  PHE A   9      -6.293  18.437   0.562  1.00 45.23
ATOM     59  C   PHE A   9      -6.407  18.180   2.056  1.00 45.07
ATOM     60  O   PHE A   9      -6.746  19.047   2.856  1.00 46.00
ATOM     61  CB  PHE A   9      -4.911  17.970   0.140  1.00 44.41
ATOM     62  CG  PHE A   9      -3.803  18.825   0.696  1.00 42.95
ATOM     63  CD1 PHE A   9      -3.149  18.465   1.871  1.00 43.85
ATOM     64  CD2 PHE A   9      -3.422  19.995   0.052  1.00 43.07
ATOM     65  CE1 PHE A   9      -2.130  19.260   2.394  1.00 44.01
ATOM     66  CE2 PHE A   9      -2.407  20.798   0.564  1.00 43.15
ATOM     67  CZ  PHE A   9      -1.758  20.431   1.737  1.00 43.06
ATOM     68  N   TYR A  10      -6.081  16.944   2.397  1.00 43.73
ATOM     69  CA  TYR A  10      -6.050  16.463   3.754  1.00 42.36
ATOM     70  C   TYR A  10      -5.149  15.240   3.693  1.00 42.93
ATOM     71  O   TYR A  10      -5.529  14.197   3.138  1.00 43.04
ATOM     72  CB  TYR A  10      -7.442  16.074   4.268  1.00 40.92
ATOM     73  CG  TYR A  10      -7.442  15.631   5.729  1.00 40.85
ATOM     74  CD1 TYR A  10      -7.360  14.276   6.078  1.00 41.14
ATOM     75  CD2 TYR A  10      -7.509  16.568   6.763  1.00 41.16
ATOM     76  CE1 TYR A  10      -7.348  13.869   7.429  1.00 42.34
ATOM     77  CE2 TYR A  10      -7.493  16.175   8.117  1.00 41.72
ATOM     78  CZ  TYR A  10      -7.415  14.830   8.441  1.00 41.97
ATOM     79  OH  TYR A  10      -7.411  14.458   9.764  1.00 39.70
ATOM     80  N   VAL A  11      -3.903  15.425   4.122  1.00 42.03
ATOM     81  CA  VAL A  11      -2.947  14.322   4.163  1.00 41.22
ATOM     82  C   VAL A  11      -3.221  13.692   5.526  1.00 39.65
ATOM     83  O   VAL A  11      -3.309  14.405   6.523  1.00 39.15
ATOM     84  CB  VAL A  11      -1.456  14.816   4.093  1.00 41.48
ATOM     85  CG1 VAL A  11      -0.496  13.638   4.204  1.00 40.16
ATOM     86  CG2 VAL A  11      -1.195  15.568   2.791  1.00 40.21
ATOM     87  N   PRO A  12      -3.455  12.368   5.571  1.00 38.66
ATOM     88  CA  PRO A  12      -3.731  11.628   6.809  1.00 39.74
ATOM     89  C   PRO A  12      -2.492  11.491   7.704  1.00 41.65
ATOM     90  O   PRO A  12      -2.394  10.550   8.489  1.00 41.57
ATOM     91  CB  PRO A  12      -4.167  10.261   6.289  1.00 38.00
ATOM     92  CG  PRO A  12      -4.654  10.544   4.915  1.00 36.57
ATOM     93  CD  PRO A  12      -3.627  11.488   4.409  1.00 36.38
ATOM     94  N   PHE A  13      -1.584  12.464   7.597  1.00 44.76
ATOM     95  CA  PHE A  13      -0.306  12.509   8.326  1.00 46.90
ATOM     96  C   PHE A  13      -0.188  13.761   9.196  1.00 48.02
ATOM     97  O   PHE A  13      -0.760  14.801   8.877  1.00 48.77
ATOM     98  CB  PHE A  13       0.828  12.550   7.303  1.00 46.86
ATOM     99  CG  PHE A  13       2.075  11.832   7.726  1.00 47.54
ATOM    100  CD1 PHE A  13       3.286  12.517   7.817  1.00 46.89
ATOM    101  CD2 PHE A  13       2.061  10.456   7.950  1.00 47.01
ATOM    102  CE1 PHE A  13       4.459  11.845   8.114  1.00 45.91
ATOM    103  CE2 PHE A  13       3.233   9.777   8.247  1.00 47.20
ATOM    104  CZ  PHE A  13       4.435  10.473   8.327  1.00 46.12
ATOM    105  N   SER A  14       0.610  13.676  10.257  1.00 49.27
ATOM    106  CA  SER A  14       0.806  14.817  11.142  1.00 50.97
ATOM    107  C   SER A  14       1.993  15.678  10.712  1.00 52.82
ATOM    108  O   SER A  14       3.087  15.167  10.438  1.00 52.56
ATOM    109  CB  SER A  14       0.995  14.355  12.583  1.00 49.47
ATOM    110  OG  SER A  14       0.970  15.474  13.454  1.00 51.42
ATOM    111  N   ASN A  15       1.781  16.989  10.673  1.00 54.68
ATOM    112  CA  ASN A  15       2.844  17.892  10.279  1.00 57.02
ATOM    113  C   ASN A  15       3.599  18.497  11.447  1.00 58.28
ATOM    114  O   ASN A  15       4.275  19.522  11.315  1.00 57.76
ATOM    115  CB  ASN A  15       2.306  19.004   9.408  1.00 59.15
ATOM    116  CG  ASN A  15       3.389  19.642   8.608  1.00 61.16
ATOM    117  OD1 ASN A  15       4.260  18.936   8.094  1.00 60.00
ATOM    118  ND2 ASN A  15       3.387  20.967   8.536  1.00 62.81
ATOM    119  N   LYS A  16       3.497  17.851  12.598  1.00 60.91
ATOM    120  CA  LYS A  16       4.182  18.323  13.793  1.00 63.78
ATOM    121  C   LYS A  16       5.665  18.037  13.586  1.00 63.36
ATOM    122  O   LYS A  16       6.461  18.072  14.522  1.00 63.28
ATOM    123  CB  LYS A  16       3.646  17.585  15.027  1.00 66.93
ATOM    124  CG  LYS A  16       3.767  18.356  16.348  1.00 70.42
ATOM    125  CD  LYS A  16       3.175  17.557  17.515  1.00 72.52
ATOM    126  CE  LYS A  16       3.305  18.303  18.846  1.00 73.66
ATOM    127  NZ  LYS A  16       2.816  17.487  20.003  1.00 73.63
ATOM    128  N   THR A  17       6.005  17.733  12.339  1.00 63.53
ATOM    129  CA  THR A  17       7.368  17.440  11.912  1.00 63.46
ATOM    130  C   THR A  17       7.697  18.295  10.678  1.00 63.30
ATOM    131  O   THR A  17       8.838  18.295  10.198  1.00 62.61
ATOM    132  CB  THR A  17       7.509  15.959  11.506  1.00 63.52
ATOM    133  OG1 THR A  17       6.905  15.130  12.508  1.00 62.34
ATOM    134  CG2 THR A  17       8.987  15.585  11.330  1.00 63.03
ATOM    135  N   GLY A  18       6.685  18.993  10.153  1.00 62.84
ATOM    136  CA  GLY A  18       6.870  19.825   8.973  1.00 61.48
ATOM    137  C   GLY A  18       7.168  19.001   7.730  1.00 60.27
ATOM    138  O   GLY A  18       7.307  19.539   6.628  1.00 60.65
ATOM    139  N   VAL A  19       7.217  17.682   7.912  1.00 59.01
ATOM    140  CA  VAL A  19       7.527  16.735   6.844  1.00 57.11
ATOM    141  C   VAL A  19       6.414  16.589   5.814  1.00 55.03
ATOM    142  O   VAL A  19       6.665  16.129   4.702  1.00 55.92
ATOM    143  CB  VAL A  19       7.914  15.342   7.431  1.00 57.75
ATOM    144  CG1 VAL A  19       6.684  14.626   7.978  1.00 58.84
ATOM    145  CG2 VAL A  19       8.636  14.495   6.389  1.00 58.30
ATOM    146  N   VAL A  20       5.193  16.978   6.175  1.00 52.44
ATOM    147  CA  VAL A  20       4.076  16.889   5.239  1.00 49.44
ATOM    148  C   VAL A  20       4.276  17.914   4.133  1.00 49.17
ATOM    149  O   VAL A  20       4.895  18.955   4.342  1.00 47.73
ATOM    150  CB  VAL A  20       2.707  17.122   5.929  1.00 47.32
ATOM    151  CG1 VAL A  20       1.579  17.066   4.908  1.00 45.00
ATOM    152  CG2 VAL A  20       2.482  16.080   7.009  1.00 45.35
ATOM    153  N   ARG A  21       3.814  17.576   2.936  1.00 50.62
ATOM    154  CA  ARG A  21       3.923  18.472   1.788  1.00 53.01
ATOM    155  C   ARG A  21       2.757  18.241   0.816  1.00 52.31
ATOM    156  O   ARG A  21       2.360  17.098   0.569  1.00 52.37
ATOM    157  CB  ARG A  21       5.278  18.289   1.089  1.00 55.05
ATOM    158  CG  ARG A  21       5.644  19.419   0.125  1.00 58.89
ATOM    159  CD  ARG A  21       5.433  20.815   0.743  1.00 62.98
ATOM    160  NE  ARG A  21       6.080  20.954   2.052  1.00 67.54
ATOM    161  CZ  ARG A  21       6.946  21.918   2.382  1.00 68.85
ATOM    162  NH1 ARG A  21       7.284  22.856   1.494  1.00 68.39
ATOM    163  NH2 ARG A  21       7.495  21.929   3.598  1.00 68.44
ATOM    164  N   SER A  22       2.210  19.333   0.280  1.00 51.22
ATOM    165  CA  SER A  22       1.071  19.289  -0.637  1.00 50.10
ATOM    166  C   SER A  22       1.191  18.186  -1.675  1.00 51.63
ATOM    167  O   SER A  22       2.228  18.047  -2.318  1.00 51.08
ATOM    168  CB  SER A  22       0.894  20.639  -1.336  1.00 48.55
ATOM    169  OG  SER A  22      -0.325  20.694  -2.059  1.00 46.28
ATOM    170  N   PRO A  23       0.144  17.348  -1.809  1.00 53.17
ATOM    171  CA  PRO A  23       0.102  16.237  -2.767  1.00 53.10
ATOM    172  C   PRO A  23       0.064  16.734  -4.206  1.00 53.62
ATOM    173  O   PRO A  23      -0.168  15.953  -5.127  1.00 54.67
ATOM    174  CB  PRO A  23      -1.200  15.525  -2.409  1.00 52.54
ATOM    175  CG  PRO A  23      -1.350  15.801  -0.964  1.00 53.80
ATOM    176  CD  PRO A  23      -1.008  17.269  -0.896  1.00 53.51
ATOM    177  N   PHE A  24       0.272  18.038  -4.384  1.00 53.54
ATOM    178  CA  PHE A  24       0.282  18.660  -5.702  1.00 53.55
ATOM    179  C   PHE A  24       1.612  19.365  -5.972  1.00 54.14
ATOM    180  O   PHE A  24       1.779  19.990  -7.026  1.00 55.09
ATOM    181  CB  PHE A  24      -0.862  19.671  -5.822  1.00 52.82
ATOM    182  CG  PHE A  24      -2.226  19.077  -5.607  1.00 51.58
ATOM    183  CD1 PHE A  24      -2.842  18.331  -6.606  1.00 50.71
ATOM    184  CD2 PHE A  24      -2.901  19.270  -4.405  1.00 51.14
ATOM    185  CE1 PHE A  24      -4.108  17.785  -6.413  1.00 50.01
ATOM    186  CE2 PHE A  24      -4.171  18.727  -4.203  1.00 50.49
ATOM    187  CZ  PHE A  24      -4.772  17.984  -5.209  1.00 49.77
ATOM    188  N   GLU A  25       2.550  19.251  -5.027  1.00 53.80
ATOM    189  CA  GLU A  25       3.868  19.886  -5.136  1.00 53.81
ATOM    190  C   GLU A  25       5.072  18.964  -4.857  1.00 52.76
ATOM    191  O   GLU A  25       6.197  19.289  -5.257  1.00 53.47
ATOM    192  CB  GLU A  25       3.962  21.096  -4.193  1.00 54.63
ATOM    193  CG  GLU A  25       2.952  22.211  -4.426  1.00 57.13
ATOM    194  CD  GLU A  25       2.766  23.099  -3.190  1.00 60.14
ATOM    195  OE1 GLU A  25       3.637  23.170  -2.312  1.00 61.50
ATOM    196  OE2 GLU A  25       1.614  23.759  -3.107  1.00 61.76
ATOM    197  N   ALA A  26       4.850  17.834  -4.177  1.00 51.16
ATOM    198  CA  ALA A  26       5.945  16.905  -3.840  1.00 49.92
ATOM    199  C   ALA A  26       5.516  15.457  -3.530  1.00 47.89
ATOM    200  O   ALA A  26       4.411  15.227  -3.044  1.00 49.53
ATOM    201  CB  ALA A  26       6.752  17.472  -2.657  1.00 51.01
ATOM    202  N   PRO A  27       6.400  14.466  -3.782  1.00 45.18
ATOM    203  CA  PRO A  27       6.081  13.061  -3.515  1.00 44.59
ATOM    204  C   PRO A  27       5.743  12.801  -2.041  1.00 44.98
ATOM    205  O   PRO A  27       6.330  13.410  -1.145  1.00 46.89
ATOM    206  CB  PRO A  27       7.364  12.344  -3.937  1.00 43.52
ATOM    207  CG  PRO A  27       8.417  13.356  -3.708  1.00 42.66
ATOM    208  CD  PRO A  27       7.779  14.580  -4.282  1.00 43.83
ATOM    209  N   GLN A  28       4.802  11.891  -1.803  1.00 43.29
ATOM    210  CA  GLN A  28       4.357  11.550  -0.455  1.00 41.96
ATOM    211  C   GLN A  28       5.109  10.387   0.170  1.00 42.34
ATOM    212  O   GLN A  28       4.564   9.655   0.988  1.00 40.96
ATOM    213  CB  GLN A  28       2.878  11.225  -0.494  1.00 40.20
ATOM    214  CG  GLN A  28       2.069  12.314  -1.118  1.00 38.81
ATOM    215  CD  GLN A  28       2.159  13.600  -0.341  1.00 38.69
ATOM    216  OE1 GLN A  28       2.752  14.569  -0.799  1.00 39.52
ATOM    217  NE2 GLN A  28       1.568  13.618   0.846  1.00 38.63
ATOM    218  N   TYR A  29       6.376  10.246  -0.194  1.00 44.31
ATOM    219  CA  TYR A  29       7.222   9.167   0.307  1.00 45.46
ATOM    220  C   TYR A  29       7.360   9.183   1.807  1.00 44.67
ATOM    221  O   TYR A  29       7.739   8.190   2.409  1.00 44.06
ATOM    222  CB  TYR A  29       8.613   9.230  -0.331  1.00 47.48
ATOM    223  CG  TYR A  29       8.593   9.082  -1.839  1.00 48.68
ATOM    224  CD1 TYR A  29       7.448   8.636  -2.506  1.00 48.18
ATOM    225  CD2 TYR A  29       9.713   9.398  -2.598  1.00 49.96
ATOM    226  CE1 TYR A  29       7.417   8.510  -3.885  1.00 49.11
ATOM    227  CE2 TYR A  29       9.697   9.276  -3.983  1.00 51.23
ATOM    228  CZ  TYR A  29       8.546   8.833  -4.620  1.00 50.96
ATOM    229  OH  TYR A  29       8.533   8.725  -5.995  1.00 52.82
ATOM    230  N   TYR A  30       7.081  10.324   2.411  1.00 45.45
ATOM    231  CA  TYR A  30       7.173  10.413   3.853  1.00 47.09
ATOM    232  C   TYR A  30       5.986   9.669   4.485  1.00 48.71
ATOM    233  O   TYR A  30       6.026   9.313   5.659  1.00 48.83
ATOM    234  CB  TYR A  30       7.236  11.886   4.291  1.00 44.86
ATOM    235  CG  TYR A  30       6.016  12.690   3.927  1.00 41.65
ATOM    236  CD1 TYR A  30       4.868  12.618   4.705  1.00 40.41
ATOM    237  CD2 TYR A  30       6.003  13.510   2.804  1.00 39.35
ATOM    238  CE1 TYR A  30       3.739  13.326   4.382  1.00 39.23
ATOM    239  CE2 TYR A  30       4.868  14.234   2.471  1.00 37.86
ATOM    240  CZ  TYR A  30       3.737  14.133   3.269  1.00 38.65
ATOM    241  OH  TYR A  30       2.587  14.833   2.982  1.00 39.22
ATOM    242  N   LEU A  31       4.951   9.411   3.683  1.00 51.35
ATOM    243  CA  LEU A  31       3.743   8.707   4.135  1.00 53.63
ATOM    244  C   LEU A  31       3.924   7.188   4.199  1.00 55.90
ATOM    245  O   LEU A  31       3.138   6.492   4.846  1.00 57.75
ATOM    246  CB  LEU A  31       2.555   9.019   3.215  1.00 51.97
ATOM    247  CG  LEU A  31       1.870  10.382   3.271  1.00 50.51
ATOM    248  CD1 LEU A  31       0.782  10.460   2.230  1.00 50.47
ATOM    249  CD2 LEU A  31       1.270  10.581   4.615  1.00 48.95
ATOM    250  N   ALA A  32       4.923   6.688   3.477  1.00 57.91
ATOM    251  CA  ALA A  32       5.259   5.259   3.407  1.00 59.37
ATOM    252  C   ALA A  32       6.358   5.070   2.344  1.00 60.78
ATOM    253  O   ALA A  32       6.523   5.913   1.458  1.00 62.07
ATOM    254  CB  ALA A  32       4.021   4.421   3.057  1.00 57.91
ATOM    255  N   GLU A  33       7.083   3.956   2.420  1.00 61.40
ATOM    256  CA  GLU A  33       8.183   3.647   1.497  1.00 62.60
ATOM    257  C   GLU A  33       7.953   3.841  -0.014  1.00 63.09
ATOM    258  O   GLU A  33       6.819   3.804  -0.493  1.00 63.11
ATOM    259  CB  GLU A  33       8.690   2.223   1.763  1.00 62.74
ATOM    260  CG  GLU A  33       9.640   2.101   2.959  1.00 64.60
ATOM    261  CD  GLU A  33       9.022   2.569   4.268  1.00 64.61
ATOM    262  OE1 GLU A  33       9.595   3.471   4.923  1.00 62.82
ATOM    263  OE2 GLU A  33       7.955   2.033   4.635  1.00 66.63
ATOM    264  N   PRO A  34       9.039   4.115  -0.771  1.00 63.75
ATOM    265  CA  PRO A  34       8.986   4.318  -2.226  1.00 63.46
ATOM    266  C   PRO A  34       8.499   3.087  -3.013  1.00 62.49
ATOM    267  O   PRO A  34       7.775   3.222  -4.003  1.00 63.09
ATOM    268  CB  PRO A  34      10.442   4.666  -2.574  1.00 63.81
ATOM    269  CG  PRO A  34      10.909   5.399  -1.351  1.00 62.98
ATOM    270  CD  PRO A  34      10.364   4.510  -0.247  1.00 64.27
ATOM    271  N   TRP A  35       8.887   1.894  -2.564  1.00 60.64
ATOM    272  CA  TRP A  35       8.489   0.661  -3.236  1.00 58.66
ATOM    273  C   TRP A  35       6.975   0.403  -3.206  1.00 56.05
ATOM    274  O   TRP A  35       6.437  -0.281  -4.074  1.00 56.26
ATOM    275  CB  TRP A  35       9.268  -0.534  -2.670  1.00 59.96
ATOM    276  CG  TRP A  35       8.862  -0.967  -1.283  1.00 61.20
ATOM    277  CD1 TRP A  35       9.482  -0.650  -0.105  1.00 61.73
ATOM    278  CD2 TRP A  35       7.767  -1.829  -0.938  1.00 61.31
ATOM    279  NE1 TRP A  35       8.843  -1.263   0.950  1.00 60.85
ATOM    280  CE2 TRP A  35       7.788  -1.991   0.466  1.00 60.95
ATOM    281  CE3 TRP A  35       6.769  -2.480  -1.683  1.00 62.27
ATOM    282  CZ2 TRP A  35       6.849  -2.776   1.144  1.00 61.30
ATOM    283  CZ3 TRP A  35       5.835  -3.262  -1.009  1.00 61.96
ATOM    284  CH2 TRP A  35       5.883  -3.402   0.393  1.00 61.56
ATOM    285  N   GLN A  36       6.294   0.933  -2.197  1.00 53.04
ATOM    286  CA  GLN A  36       4.850   0.771  -2.094  1.00 51.03
ATOM    287  C   GLN A  36       4.199   1.588  -3.210  1.00 48.90
ATOM    288  O   GLN A  36       3.227   1.151  -3.834  1.00 48.33
ATOM    289  CB  GLN A  36       4.368   1.231  -0.723  1.00 52.20
ATOM    290  CG  GLN A  36       5.191   0.640   0.411  1.00 55.50
ATOM    291  CD  GLN A  36       4.457   0.645   1.735  1.00 58.30
ATOM    292  OE1 GLN A  36       4.938   1.197   2.731  1.00 59.56
ATOM    293  NE2 GLN A  36       3.284   0.017   1.759  1.00 60.11
ATOM    294  N   PHE A  37       4.761   2.768  -3.469  1.00 45.86
ATOM    295  CA  PHE A  37       4.288   3.635  -4.538  1.00 43.14
ATOM    296  C   PHE A  37       4.593   2.925  -5.852  1.00 42.57
ATOM    297  O   PHE A  37       3.863   3.058  -6.832  1.00 42.19
ATOM    298  CB  PHE A  37       4.998   4.993  -4.490  1.00 41.82
ATOM    299  CG  PHE A  37       4.493   5.903  -3.407  1.00 41.51
ATOM    300  CD1 PHE A  37       3.397   6.728  -3.630  1.00 41.18
ATOM    301  CD2 PHE A  37       5.088   5.913  -2.149  1.00 42.69
ATOM    302  CE1 PHE A  37       2.895   7.552  -2.614  1.00 42.20
ATOM    303  CE2 PHE A  37       4.595   6.734  -1.122  1.00 41.94
ATOM    304  CZ  PHE A  37       3.495   7.553  -1.360  1.00 42.84
ATOM    305  N   SER A  38       5.673   2.148  -5.851  1.00 42.12
ATOM    306  CA  SER A  38       6.073   1.394  -7.030  1.00 42.48
ATOM    307  C   SER A  38       5.071   0.277  -7.320  1.00 41.88
ATOM    308  O   SER A  38       4.809  -0.028  -8.481  1.00 41.85
ATOM    309  CB  SER A  38       7.486   0.820  -6.859  1.00 43.61
ATOM    310  OG  SER A  38       8.470   1.842  -6.864  1.00 45.76
ATOM    311  N   MET A  39       4.519  -0.333  -6.272  1.00 41.48
ATOM    312  CA  MET A  39       3.537  -1.395  -6.455  1.00 41.80
ATOM    313  C   MET A  39       2.216  -0.856  -7.003  1.00 40.72
ATOM    314  O   MET A  39       1.544  -1.529  -7.801  1.00 40.26
ATOM    315  CB  MET A  39       3.332  -2.197  -5.171  1.00 45.03
ATOM    316  CG  MET A  39       4.423  -3.240  -4.961  1.00 51.01
ATOM    317  SD  MET A  39       4.851  -4.160  -6.516  1.00 60.78
ATOM    318  CE  MET A  39       6.605  -3.634  -6.792  1.00 57.60
ATOM    319  N   LEU A  40       1.863   0.366  -6.598  1.00 37.50
ATOM    320  CA  LEU A  40       0.653   1.006  -7.094  1.00 34.17
ATOM    321  C   LEU A  40       0.872   1.253  -8.577  1.00 34.32
ATOM    322  O   LEU A  40       0.027   0.898  -9.393  1.00 36.24
ATOM    323  CB  LEU A  40       0.401   2.334  -6.396  1.00 30.85
ATOM    324  CG  LEU A  40       0.200   2.298  -4.887  1.00 28.41
ATOM    325  CD1 LEU A  40      -0.278   3.661  -4.425  1.00 26.70
ATOM    326  CD2 LEU A  40      -0.810   1.235  -4.521  1.00 27.70
ATOM    327  N   ALA A  41       2.021   1.836  -8.921  1.00 33.20
ATOM    328  CA  ALA A  41       2.360   2.102 -10.313  1.00 33.72
ATOM    329  C   ALA A  41       2.325   0.796 -11.136  1.00 35.56
ATOM    330  O   ALA A  41       1.765   0.769 -12.236  1.00 37.43
ATOM    331  CB  ALA A  41       3.716   2.757 -10.404  1.00 33.06
ATOM    332  N   ALA A  42       2.892  -0.290 -10.597  1.00 34.23
ATOM    333  CA  ALA A  42       2.883  -1.583 -11.289  1.00 31.19
ATOM    334  C   ALA A  42       1.428  -1.997 -11.435  1.00 31.14
ATOM    335  O   ALA A  42       0.925  -2.149 -12.548  1.00 30.96
ATOM    336  CB  ALA A  42       3.631  -2.615 -10.494  1.00 29.34
ATOM    337  N   TYR A  43       0.745  -2.108 -10.298  1.00 29.41
ATOM    338  CA  TYR A  43      -0.666  -2.479 -10.250  1.00 28.48
ATOM    339  C   TYR A  43      -1.543  -1.746 -11.277  1.00 30.08
ATOM    340  O   TYR A  43      -2.338  -2.366 -11.997  1.00 29.68
ATOM    341  CB  TYR A  43      -1.193  -2.199  -8.858  1.00 24.59
ATOM    342  CG  TYR A  43      -2.687  -2.270  -8.736  1.00 21.29
ATOM    343  CD1 TYR A  43      -3.415  -1.161  -8.346  1.00 19.52
ATOM    344  CD2 TYR A  43      -3.366  -3.476  -8.914  1.00 21.36
ATOM    345  CE1 TYR A  43      -4.769  -1.244  -8.117  1.00 16.88
ATOM    346  CE2 TYR A  43      -4.725  -3.568  -8.689  1.00 17.91
ATOM    347  CZ  TYR A  43      -5.407  -2.445  -8.283  1.00 18.51
ATOM    348  OH  TYR A  43      -6.732  -2.532  -7.987  1.00 25.45
ATOM    349  N   MET A  44      -1.435  -0.422 -11.299  1.00 32.40
ATOM    350  CA  MET A  44      -2.208   0.392 -12.241  1.00 33.44
ATOM    351  C   MET A  44      -1.813   0.074 -13.675  1.00 33.50
ATOM    352  O   MET A  44      -2.649   0.056 -14.562  1.00 32.57
ATOM    353  CB  MET A  44      -2.029   1.890 -11.961  1.00 32.25
ATOM    354  CG  MET A  44      -2.783   2.376 -10.740  1.00 30.57
ATOM    355  SD  MET A  44      -4.483   1.745 -10.651  1.00 31.09
ATOM    356  CE  MET A  44      -5.169   2.263 -12.201  1.00 30.48
ATOM    357  N   PHE A  45      -0.532  -0.198 -13.883  1.00 34.98
ATOM    358  CA  PHE A  45      -0.024  -0.543 -15.197  1.00 36.61
ATOM    359  C   PHE A  45      -0.669  -1.846 -15.692  1.00 35.82
ATOM    360  O   PHE A  45      -1.069  -1.944 -16.856  1.00 35.70
ATOM    361  CB  PHE A  45       1.504  -0.665 -15.142  1.00 39.96
ATOM    362  CG  PHE A  45       2.116  -1.169 -16.410  1.00 43.15
ATOM    363  CD1 PHE A  45       2.721  -2.417 -16.454  1.00 45.76
ATOM    364  CD2 PHE A  45       2.063  -0.409 -17.572  1.00 46.04
ATOM    365  CE1 PHE A  45       3.266  -2.912 -17.644  1.00 47.87
ATOM    366  CE2 PHE A  45       2.604  -0.889 -18.770  1.00 48.09
ATOM    367  CZ  PHE A  45       3.206  -2.145 -18.805  1.00 48.18
ATOM    368  N   LEU A  46      -0.793  -2.827 -14.796  1.00 34.81
ATOM    369  CA  LEU A  46      -1.408  -4.119 -15.116  1.00 33.64
ATOM    370  C   LEU A  46      -2.903  -3.990 -15.342  1.00 33.52
ATOM    371  O   LEU A  46      -3.471  -4.775 -16.092  1.00 33.46
ATOM    372  CB  LEU A  46      -1.164  -5.128 -13.996  1.00 34.08
ATOM    373  CG  LEU A  46       0.118  -5.962 -14.016  1.00 34.61
ATOM    374  CD1 LEU A  46       1.265  -5.214 -14.665  1.00 35.60
ATOM    375  CD2 LEU A  46       0.474  -6.382 -12.596  1.00 34.14
ATOM    376  N   LEU A  47      -3.550  -3.044 -14.656  1.00 33.61
ATOM    377  CA  LEU A  47      -4.996  -2.823 -14.832  1.00 34.18
ATOM    378  C   LEU A  47      -5.263  -2.150 -16.172  1.00 34.67
ATOM    379  O   LEU A  47      -6.279  -2.389 -16.824  1.00 34.80
ATOM    380  CB  LEU A  47      -5.567  -1.928 -13.737  1.00 32.84
ATOM    381  CG  LEU A  47      -5.849  -2.504 -12.366  1.00 30.47
ATOM    382  CD1 LEU A  47      -6.514  -1.420 -11.528  1.00 29.43
ATOM    383  CD2 LEU A  47      -6.750  -3.705 -12.520  1.00 29.13
ATOM    384  N   ILE A  48      -4.364  -1.251 -16.546  1.00 34.81
ATOM    385  CA  ILE A  48      -4.486  -0.547 -17.798  1.00 34.71
ATOM    386  C   ILE A  48      -4.200  -1.514 -18.934  1.00 35.53
ATOM    387  O   ILE A  48      -4.747  -1.374 -20.030  1.00 36.38
ATOM    388  CB  ILE A  48      -3.529   0.642 -17.845  1.00 34.15
ATOM    389  CG1 ILE A  48      -3.974   1.699 -16.828  1.00 33.30
ATOM    390  CG2 ILE A  48      -3.478   1.221 -19.255  1.00 36.00
ATOM    391  CD1 ILE A  48      -3.083   2.933 -16.773  1.00 30.33
ATOM    392  N   MET A  49      -3.375  -2.521 -18.657  1.00 36.08
ATOM    393  CA  MET A  49      -3.035  -3.519 -19.671  1.00 36.63
ATOM    394  C   MET A  49      -4.177  -4.513 -19.877  1.00 36.74
ATOM    395  O   MET A  49      -4.348  -5.052 -20.976  1.00 37.70
ATOM    396  CB  MET A  49      -1.744  -4.253 -19.302  1.00 36.94
ATOM    397  CG  MET A  49      -1.190  -5.105 -20.423  1.00 37.03
ATOM    398  SD  MET A  49       0.507  -5.587 -20.146  1.00 38.32
ATOM    399  CE  MET A  49       1.358  -4.397 -21.200  1.00 36.49
ATOM    400  N   LEU A  50      -4.955  -4.744 -18.822  1.00 35.73
ATOM    401  CA  LEU A  50      -6.097  -5.652 -18.887  1.00 36.17
ATOM    402  C   LEU A  50      -7.394  -4.932 -19.292  1.00 36.79
ATOM    403  O   LEU A  50      -8.075  -5.334 -20.242  1.00 37.30
ATOM    404  CB  LEU A  50      -6.317  -6.327 -17.534  1.00 35.90
ATOM    405  CG  LEU A  50      -5.425  -7.465 -17.050  1.00 35.23
ATOM    406  CD1 LEU A  50      -5.790  -7.818 -15.609  1.00 34.07
ATOM    407  CD2 LEU A  50      -5.594  -8.665 -17.953  1.00 34.16
ATOM    408  N   GLY A  51      -7.728  -3.873 -18.552  1.00 36.20
ATOM    409  CA  GLY A  51      -8.938  -3.111 -18.800  1.00 33.55
ATOM    410  C   GLY A  51      -9.063  -2.597 -20.210  1.00 32.05
ATOM    411  O   GLY A  51     -10.164  -2.425 -20.707  1.00 29.47
ATOM    412  N   PHE A  52      -7.937  -2.343 -20.860  1.00 32.80
ATOM    413  CA  PHE A  52      -8.002  -1.847 -22.217  1.00 35.21
ATOM    414  C   PHE A  52      -8.523  -2.901 -23.213  1.00 36.35
ATOM    415  O   PHE A  52      -9.659  -2.779 -23.701  1.00 37.25
ATOM    416  CB  PHE A  52      -6.671  -1.246 -22.665  1.00 35.33
ATOM    417  CG  PHE A  52      -6.653  -0.886 -24.110  1.00 38.91
ATOM    418  CD1 PHE A  52      -7.775  -0.317 -24.708  1.00 40.56
ATOM    419  CD2 PHE A  52      -5.546  -1.161 -24.893  1.00 41.77
ATOM    420  CE1 PHE A  52      -7.801  -0.028 -26.072  1.00 42.08
ATOM    421  CE2 PHE A  52      -5.565  -0.874 -26.265  1.00 43.27
ATOM    422  CZ  PHE A  52      -6.699  -0.307 -26.850  1.00 41.65
ATOM    423  N   PRO A  53      -7.721  -3.955 -23.510  1.00 35.37
ATOM    424  CA  PRO A  53      -8.142  -5.003 -24.448  1.00 32.36
ATOM    425  C   PRO A  53      -9.479  -5.621 -24.066  1.00 30.13
ATOM    426  O   PRO A  53     -10.429  -5.548 -24.831  1.00 30.27
ATOM    427  CB  PRO A  53      -7.022  -6.027 -24.331  1.00 32.73
ATOM    428  CG  PRO A  53      -5.842  -5.195 -23.996  1.00 34.40
ATOM    429  CD  PRO A  53      -6.393  -4.279 -22.959  1.00 35.17
ATOM    430  N   ILE A  54      -9.552  -6.200 -22.873  1.00 27.22
ATOM    431  CA  ILE A  54     -10.779  -6.826 -22.401  1.00 26.76
ATOM    432  C   ILE A  54     -11.981  -5.953 -22.676  1.00 26.01
ATOM    433  O   ILE A  54     -12.971  -6.423 -23.193  1.00 23.76
ATOM    434  CB  ILE A  54     -10.727  -7.104 -20.897  1.00 27.82
ATOM    435  CG1 ILE A  54      -9.640  -8.134 -20.596  1.00 28.56
ATOM    436  CG2 ILE A  54     -12.062  -7.621 -20.414  1.00 25.13
ATOM    437  CD1 ILE A  54      -9.282  -8.238 -19.124  1.00 29.11
ATOM    438  N   ASN A  55     -11.870  -4.674 -22.350  1.00 28.19
ATOM    439  CA  ASN A  55     -12.964  -3.742 -22.575  1.00 30.88
ATOM    440  C   ASN A  55     -13.094  -3.350 -24.025  1.00 32.07
ATOM    441  O   ASN A  55     -14.203  -3.164 -24.514  1.00 32.20
ATOM    442  CB  ASN A  55     -12.819  -2.500 -21.706  1.00 31.24
ATOM    443  CG  ASN A  55     -13.250  -2.745 -20.287  1.00 31.44
ATOM    444  OD1 ASN A  55     -14.424  -2.978 -20.023  1.00 32.99
ATOM    445  ND2 ASN A  55     -12.303  -2.723 -19.367  1.00 31.26
ATOM    446  N   PHE A  56     -11.965  -3.229 -24.714  1.00 33.43
ATOM    447  CA  PHE A  56     -11.993  -2.872 -26.125  1.00 35.02
ATOM    448  C   PHE A  56     -12.440  -4.011 -27.061  1.00 34.34
ATOM    449  O   PHE A  56     -13.021  -3.758 -28.113  1.00 34.31
ATOM    450  CB  PHE A  56     -10.654  -2.322 -26.587  1.00 36.55
ATOM    451  CG  PHE A  56     -10.672  -1.880 -28.012  1.00 39.19
ATOM    452  CD1 PHE A  56     -11.478  -0.810 -28.403  1.00 39.45
ATOM    453  CD2 PHE A  56      -9.946  -2.570 -28.981  1.00 39.46
ATOM    454  CE1 PHE A  56     -11.566  -0.433 -29.736  1.00 38.81
ATOM    455  CE2 PHE A  56     -10.026  -2.201 -30.322  1.00 38.79
ATOM    456  CZ  PHE A  56     -10.839  -1.130 -30.699  1.00 39.55
ATOM    457  N   LEU A  57     -12.109  -5.251 -26.710  1.00 33.09
ATOM    458  CA  LEU A  57     -12.517  -6.415 -27.492  1.00 30.73
ATOM    459  C   LEU A  57     -14.012  -6.591 -27.273  1.00 31.67
ATOM    460  O   LEU A  57     -14.756  -6.882 -28.192  1.00 31.53
ATOM    461  CB  LEU A  57     -11.804  -7.658 -26.992  1.00 28.30
ATOM    462  CG  LEU A  57     -12.455  -8.977 -27.392  1.00 26.93
ATOM    463  CD1 LEU A  57     -12.234  -9.207 -28.849  1.00 26.14
ATOM    464  CD2 LEU A  57     -11.871 -10.124 -26.585  1.00 29.12
ATOM    465  N   THR A  58     -14.433  -6.441 -26.024  1.00 32.44
ATOM    466  CA  THR A  58     -15.831  -6.551 -25.659  1.00 32.66
ATOM    467  C   THR A  58     -16.606  -5.538 -26.481  1.00 34.41
ATOM    468  O   THR A  58     -17.690  -5.820 -26.983  1.00 33.84
ATOM    469  CB  THR A  58     -16.014  -6.207 -24.187  1.00 31.99
ATOM    470  OG1 THR A  58     -15.220  -7.094 -23.400  1.00 33.29
ATOM    471  CG2 THR A  58     -17.457  -6.354 -23.782  1.00 32.28
ATOM    472  N   LEU A  59     -16.033  -4.348 -26.597  1.00 36.66
ATOM    473  CA  LEU A  59     -16.635  -3.260 -27.354  1.00 39.07
ATOM    474  C   LEU A  59     -16.650  -3.562 -28.864  1.00 39.92
ATOM    475  O   LEU A  59     -17.707  -3.538 -29.503  1.00 38.34
ATOM    476  CB  LEU A  59     -15.883  -1.958 -27.039  1.00 39.48
ATOM    477  CG  LEU A  59     -15.811  -0.805 -28.047  1.00 41.64
ATOM    478  CD1 LEU A  59     -17.174  -0.367 -28.535  1.00 41.27
ATOM    479  CD2 LEU A  59     -15.114   0.345 -27.389  1.00 41.92
ATOM    480  N   TYR A  60     -15.480  -3.886 -29.411  1.00 41.04
ATOM    481  CA  TYR A  60     -15.342  -4.195 -30.826  1.00 41.93
ATOM    482  C   TYR A  60     -16.220  -5.376 -31.247  1.00 41.78
ATOM    483  O   TYR A  60     -16.700  -5.436 -32.374  1.00 41.83
ATOM    484  CB  TYR A  60     -13.872  -4.478 -31.175  1.00 45.06
ATOM    485  CG  TYR A  60     -13.624  -4.650 -32.668  1.00 49.03
ATOM    486  CD1 TYR A  60     -13.124  -5.852 -33.190  1.00 49.70
ATOM    487  CD2 TYR A  60     -13.963  -3.633 -33.565  1.00 50.73
ATOM    488  CE1 TYR A  60     -12.980  -6.034 -34.576  1.00 52.14
ATOM    489  CE2 TYR A  60     -13.830  -3.803 -34.941  1.00 53.36
ATOM    490  CZ  TYR A  60     -13.343  -5.002 -35.448  1.00 54.00
ATOM    491  OH  TYR A  60     -13.274  -5.160 -36.823  1.00 55.11
ATOM    492  N   VAL A  61     -16.446  -6.316 -30.346  1.00 41.81
ATOM    493  CA  VAL A  61     -17.265  -7.454 -30.703  1.00 42.49
ATOM    494  C   VAL A  61     -18.735  -7.038 -30.876  1.00 45.35
ATOM    495  O   VAL A  61     -19.300  -7.235 -31.953  1.00 46.29
ATOM    496  CB  VAL A  61     -17.090  -8.638 -29.685  1.00 41.73
ATOM    497  CG1 VAL A  61     -18.074  -9.758 -29.974  1.00 40.21
ATOM    498  CG2 VAL A  61     -15.676  -9.204 -29.760  1.00 38.23
ATOM    499  N   THR A  62     -19.310  -6.357 -29.878  1.00 47.37
ATOM    500  CA  THR A  62     -20.733  -5.949 -29.919  1.00 48.40
ATOM    501  C   THR A  62     -21.159  -5.150 -31.173  1.00 49.57
ATOM    502  O   THR A  62     -22.250  -5.358 -31.728  1.00 48.53
ATOM    503  CB  THR A  62     -21.169  -5.167 -28.619  1.00 47.42
ATOM    504  OG1 THR A  62     -20.734  -5.860 -27.438  1.00 45.60
ATOM    505  CG2 THR A  62     -22.690  -5.047 -28.563  1.00 47.10
ATOM    506  N   VAL A  63     -20.280  -4.254 -31.614  1.00 51.72
ATOM    507  CA  VAL A  63     -20.517  -3.397 -32.781  1.00 54.11
ATOM    508  C   VAL A  63     -20.548  -4.189 -34.092  1.00 55.14
ATOM    509  O   VAL A  63     -21.445  -4.006 -34.928  1.00 55.04
ATOM    510  CB  VAL A  63     -19.397  -2.325 -32.897  1.00 54.34
ATOM    511  CG1 VAL A  63     -19.679  -1.373 -34.052  1.00 54.68
ATOM    512  CG2 VAL A  63     -19.257  -1.570 -31.590  1.00 53.47
ATOM    513  N   GLN A  64     -19.539  -5.044 -34.254  1.00 55.88
ATOM    514  CA  GLN A  64     -19.361  -5.881 -35.433  1.00 56.47
ATOM    515  C   GLN A  64     -20.463  -6.899 -35.647  1.00 56.39
ATOM    516  O   GLN A  64     -20.812  -7.200 -36.792  1.00 56.66
ATOM    517  CB  GLN A  64     -18.017  -6.607 -35.364  1.00 57.09
ATOM    518  CG  GLN A  64     -17.784  -7.556 -36.525  1.00 57.11
ATOM    519  CD  GLN A  64     -16.482  -8.308 -36.411  1.00 56.30
ATOM    520  OE1 GLN A  64     -15.511  -8.008 -37.116  1.00 55.67
ATOM    521  NE2 GLN A  64     -16.455  -9.307 -35.534  1.00 54.87
ATOM    522  N   HIS A  65     -20.960  -7.467 -34.549  1.00 56.87
ATOM    523  CA  HIS A  65     -22.027  -8.460 -34.609  1.00 57.65
ATOM    524  C   HIS A  65     -23.386  -7.771 -34.528  1.00 57.86
ATOM    525  O   HIS A  65     -23.913  -7.512 -33.445  1.00 57.68
ATOM    526  CB  HIS A  65     -21.837  -9.525 -33.524  1.00 58.81
ATOM    527  CG  HIS A  65     -20.637 -10.400 -33.747  1.00 61.00
ATOM    528  ND1 HIS A  65     -20.389 -11.037 -34.945  1.00 62.25
ATOM    529  CD2 HIS A  65     -19.597 -10.712 -32.935  1.00 61.66
ATOM    530  CE1 HIS A  65     -19.245 -11.696 -34.864  1.00 62.28
ATOM    531  NE2 HIS A  65     -18.745 -11.515 -33.654  1.00 61.02
ATOM    532  N   LYS A  66     -23.933  -7.493 -35.711  1.00 58.51
ATOM    533  CA  LYS A  66     -25.196  -6.781 -35.907  1.00 58.66
ATOM    534  C   LYS A  66     -26.477  -7.218 -35.192  1.00 58.03
ATOM    535  O   LYS A  66     -27.393  -6.404 -35.047  1.00 57.81
ATOM    536  CB  LYS A  66     -25.447  -6.566 -37.407  1.00 59.61
ATOM    537  CG  LYS A  66     -24.543  -5.491 -38.040  1.00 60.80
ATOM    538  CD  LYS A  66     -24.819  -4.126 -37.414  1.00 62.72
ATOM    539  CE  LYS A  66     -23.911  -3.028 -37.943  1.00 63.89
ATOM    540  NZ  LYS A  66     -24.197  -1.730 -37.243  1.00 65.60
ATOM    541  N   LYS A  67     -26.546  -8.469 -34.731  1.00 57.65
ATOM    542  CA  LYS A  67     -27.741  -8.949 -34.017  1.00 56.75
ATOM    543  C   LYS A  67     -27.557  -9.061 -32.495  1.00 55.19
ATOM    544  O   LYS A  67     -28.424  -9.583 -31.795  1.00 55.42
ATOM    545  CB  LYS A  67     -28.264 -10.286 -34.589  1.00 58.01
ATOM    546  CG  LYS A  67     -28.881 -10.214 -36.011  1.00 58.98
ATOM    547  CD  LYS A  67     -30.019 -11.239 -36.215  1.00 59.60
ATOM    548  CE  LYS A  67     -29.557 -12.694 -36.038  1.00 60.48
ATOM    549  NZ  LYS A  67     -30.655 -13.720 -36.104  1.00 59.89
ATOM    550  N   LEU A  68     -26.419  -8.589 -31.992  1.00 53.67
ATOM    551  CA  LEU A  68     -26.131  -8.613 -30.555  1.00 52.45
ATOM    552  C   LEU A  68     -26.680  -7.298 -29.983  1.00 53.05
ATOM    553  O   LEU A  68     -25.920  -6.418 -29.554  1.00 52.70
ATOM    554  CB  LEU A  68     -24.614  -8.724 -30.326  1.00 49.27
ATOM    555  CG  LEU A  68     -24.003  -9.991 -29.705  1.00 45.55
ATOM    556  CD1 LEU A  68     -24.373 -11.232 -30.479  1.00 46.15
ATOM    557  CD2 LEU A  68     -22.512  -9.846 -29.664  1.00 43.96
ATOM    558  N   ARG A  69     -28.009  -7.191 -29.951  1.00 52.56
ATOM    559  CA  ARG A  69     -28.653  -5.966 -29.512  1.00 51.95
ATOM    560  C   ARG A  69     -29.758  -6.025 -28.455  1.00 52.65
ATOM    561  O   ARG A  69     -30.673  -5.210 -28.478  1.00 52.86
ATOM    562  CB  ARG A  69     -29.154  -5.223 -30.748  1.00 51.01
ATOM    563  CG  ARG A  69     -28.078  -4.987 -31.795  1.00 50.88
ATOM    564  CD  ARG A  69     -27.001  -4.077 -31.254  1.00 52.80
ATOM    565  NE  ARG A  69     -25.715  -4.285 -31.908  1.00 55.47
ATOM    566  CZ  ARG A  69     -25.373  -3.759 -33.081  1.00 58.00
ATOM    567  NH1 ARG A  69     -26.229  -2.984 -33.748  1.00 59.57
ATOM    568  NH2 ARG A  69     -24.161  -3.988 -33.575  1.00 58.64
ATOM    569  N   THR A  70     -29.666  -6.952 -27.508  1.00 54.39
ATOM    570  CA  THR A  70     -30.673  -7.031 -26.438  1.00 56.36
ATOM    571  C   THR A  70     -30.279  -6.038 -25.328  1.00 57.32
ATOM    572  O   THR A  70     -29.123  -5.597 -25.283  1.00 57.67
ATOM    573  CB  THR A  70     -30.755  -8.460 -25.831  1.00 56.22
ATOM    574  OG1 THR A  70     -29.648  -8.689 -24.951  1.00 55.24
ATOM    575  CG2 THR A  70     -30.722  -9.505 -26.936  1.00 58.31
ATOM    576  N   PRO A  71     -31.236  -5.628 -24.454  1.00 57.45
ATOM    577  CA  PRO A  71     -30.875  -4.687 -23.381  1.00 55.95
ATOM    578  C   PRO A  71     -29.568  -5.093 -22.691  1.00 53.90
ATOM    579  O   PRO A  71     -28.690  -4.258 -22.495  1.00 54.52
ATOM    580  CB  PRO A  71     -32.080  -4.764 -22.448  1.00 55.58
ATOM    581  CG  PRO A  71     -33.200  -4.829 -23.440  1.00 57.10
ATOM    582  CD  PRO A  71     -32.696  -5.856 -24.464  1.00 57.30
ATOM    583  N   LEU A  72     -29.413  -6.386 -22.409  1.00 50.61
ATOM    584  CA  LEU A  72     -28.199  -6.894 -21.787  1.00 47.03
ATOM    585  C   LEU A  72     -26.993  -6.622 -22.677  1.00 45.94
ATOM    586  O   LEU A  72     -25.985  -6.100 -22.224  1.00 45.99
ATOM    587  CB  LEU A  72     -28.302  -8.397 -21.563  1.00 46.96
ATOM    588  CG  LEU A  72     -27.018  -8.993 -20.982  1.00 46.03
ATOM    589  CD1 LEU A  72     -26.930  -8.598 -19.521  1.00 46.30
ATOM    590  CD2 LEU A  72     -26.981 -10.510 -21.124  1.00 45.63
ATOM    591  N   ASN A  73     -27.102  -6.994 -23.946  1.00 46.19
ATOM    592  CA  ASN A  73     -26.020  -6.797 -24.910  1.00 45.96
ATOM    593  C   ASN A  73     -25.679  -5.319 -25.010  1.00 45.95
ATOM    594  O   ASN A  73     -24.526  -4.967 -25.246  1.00 47.43
ATOM    595  CB  ASN A  73     -26.412  -7.336 -26.298  1.00 45.47
ATOM    596  CG  ASN A  73     -26.573  -8.860 -26.328  1.00 46.41
ATOM    597  OD1 ASN A  73     -27.226  -9.469 -25.466  1.00 46.64
ATOM    598  ND2 ASN A  73     -25.997  -9.480 -27.344  1.00 45.86
ATOM    599  N   TYR A  74     -26.689  -4.472 -24.801  1.00 45.11
ATOM    600  CA  TYR A  74     -26.565  -3.014 -24.857  1.00 45.59
ATOM    601  C   TYR A  74     -25.894  -2.421 -23.636  1.00 46.97
ATOM    602  O   TYR A  74     -24.926  -1.668 -23.737  1.00 47.40
ATOM    603  CB  TYR A  74     -27.949  -2.381 -24.960  1.00 44.61
ATOM    604  CG  TYR A  74     -28.205  -1.727 -26.277  1.00 43.22
ATOM    605  CD1 TYR A  74     -27.691  -0.463 -26.558  1.00 42.34
ATOM    606  CD2 TYR A  74     -28.930  -2.388 -27.262  1.00 43.86
ATOM    607  CE1 TYR A  74     -27.893   0.125 -27.795  1.00 43.73
ATOM    608  CE2 TYR A  74     -29.138  -1.819 -28.502  1.00 43.66
ATOM    609  CZ  TYR A  74     -28.621  -0.564 -28.767  1.00 44.74
ATOM    610  OH  TYR A  74     -28.834  -0.009 -30.006  1.00 45.19
ATOM    611  N   ILE A  75     -26.499  -2.693 -22.486  1.00 49.15
ATOM    612  CA  ILE A  75     -26.019  -2.215 -21.196  1.00 50.01
ATOM    613  C   ILE A  75     -24.585  -2.675 -20.937  1.00 50.01
ATOM    614  O   ILE A  75     -23.880  -2.091 -20.113  1.00 50.90
ATOM    615  CB  ILE A  75     -26.984  -2.669 -20.043  1.00 49.91
ATOM    616  CG1 ILE A  75     -28.065  -1.608 -19.787  1.00 51.15
ATOM    617  CG2 ILE A  75     -26.229  -2.916 -18.770  1.00 49.53
ATOM    618  CD1 ILE A  75     -29.059  -1.384 -20.935  1.00 52.28
ATOM    619  N   LEU A  76     -24.141  -3.702 -21.659  1.00 48.97
ATOM    620  CA  LEU A  76     -22.785  -4.195 -21.477  1.00 48.51
ATOM    621  C   LEU A  76     -21.756  -3.600 -22.431  1.00 48.34
ATOM    622  O   LEU A  76     -20.553  -3.792 -22.253  1.00 48.90
ATOM    623  CB  LEU A  76     -22.742  -5.722 -21.452  1.00 47.47
ATOM    624  CG  LEU A  76     -22.584  -6.237 -20.014  1.00 46.48
ATOM    625  CD1 LEU A  76     -23.520  -7.384 -19.752  1.00 46.15
ATOM    626  CD2 LEU A  76     -21.136  -6.618 -19.726  1.00 44.56
ATOM    627  N   LEU A  77     -22.231  -2.860 -23.429  1.00 47.23
ATOM    628  CA  LEU A  77     -21.346  -2.185 -24.374  1.00 45.34
ATOM    629  C   LEU A  77     -21.017  -0.882 -23.659  1.00 43.96
ATOM    630  O   LEU A  77     -19.904  -0.355 -23.752  1.00 43.85
ATOM    631  CB  LEU A  77     -22.097  -1.867 -25.663  1.00 46.52
ATOM    632  CG  LEU A  77     -21.304  -1.765 -26.962  1.00 47.29
ATOM    633  CD1 LEU A  77     -22.186  -1.092 -28.005  1.00 48.07
ATOM    634  CD2 LEU A  77     -20.017  -0.991 -26.767  1.00 46.80
ATOM    635  N   ASN A  78     -22.019  -0.397 -22.925  1.00 42.01
ATOM    636  CA  ASN A  78     -21.963   0.826 -22.127  1.00 39.72
ATOM    637  C   ASN A  78     -20.827   0.733 -21.120  1.00 37.80
ATOM    638  O   ASN A  78     -20.061   1.673 -20.938  1.00 37.59
ATOM    639  CB  ASN A  78     -23.298   0.995 -21.383  1.00 39.77
ATOM    640  CG  ASN A  78     -23.450   2.358 -20.718  1.00 38.22
ATOM    641  OD1 ASN A  78     -22.832   3.339 -21.124  1.00 33.85
ATOM    642  ND2 ASN A  78     -24.309   2.422 -19.703  1.00 39.99
ATOM    643  N   LEU A  79     -20.707  -0.427 -20.497  1.00 36.49
ATOM    644  CA  LEU A  79     -19.681  -0.646 -19.504  1.00 36.04
ATOM    645  C   LEU A  79     -18.279  -0.702 -20.111  1.00 37.22
ATOM    646  O   LEU A  79     -17.325  -0.192 -19.517  1.00 38.18
ATOM    647  CB  LEU A  79     -20.019  -1.895 -18.691  1.00 33.88
ATOM    648  CG  LEU A  79     -21.397  -1.753 -18.032  1.00 33.16
ATOM    649  CD1 LEU A  79     -21.754  -2.990 -17.260  1.00 33.14
ATOM    650  CD2 LEU A  79     -21.429  -0.535 -17.119  1.00 33.07
ATOM    651  N   ALA A  80     -18.158  -1.261 -21.315  1.00 37.08
ATOM    652  CA  ALA A  80     -16.859  -1.341 -21.981  1.00 36.94
ATOM    653  C   ALA A  80     -16.317   0.067 -22.267  1.00 37.25
ATOM    654  O   ALA A  80     -15.117   0.317 -22.146  1.00 38.39
ATOM    655  CB  ALA A  80     -16.967  -2.143 -23.268  1.00 36.28
ATOM    656  N   VAL A  81     -17.208   0.991 -22.617  1.00 36.22
ATOM    657  CA  VAL A  81     -16.801   2.366 -22.901  1.00 34.81
ATOM    658  C   VAL A  81     -16.424   3.092 -21.606  1.00 34.03
ATOM    659  O   VAL A  81     -15.355   3.704 -21.525  1.00 34.17
ATOM    660  CB  VAL A  81     -17.916   3.152 -23.633  1.00 32.83
ATOM    661  CG1 VAL A  81     -17.352   4.436 -24.231  1.00 31.22
ATOM    662  CG2 VAL A  81     -18.535   2.291 -24.698  1.00 29.65
ATOM    663  N   ALA A  82     -17.308   3.013 -20.608  1.00 32.91
ATOM    664  CA  ALA A  82     -17.088   3.631 -19.304  1.00 32.09
ATOM    665  C   ALA A  82     -15.772   3.112 -18.728  1.00 32.33
ATOM    666  O   ALA A  82     -15.008   3.888 -18.141  1.00 33.84
ATOM    667  CB  ALA A  82     -18.247   3.323 -18.359  1.00 30.14
ATOM    668  N   ASP A  83     -15.500   1.816 -18.929  1.00 30.52
ATOM    669  CA  ASP A  83     -14.262   1.205 -18.457  1.00 30.52
ATOM    670  C   ASP A  83     -13.075   1.742 -19.263  1.00 32.03
ATOM    671  O   ASP A  83     -12.036   2.067 -18.678  1.00 33.61
ATOM    672  CB  ASP A  83     -14.324  -0.320 -18.534  1.00 29.81
ATOM    673  CG  ASP A  83     -15.276  -0.930 -17.510  1.00 31.00
ATOM    674  OD1 ASP A  83     -16.157  -0.224 -16.991  1.00 31.66
ATOM    675  OD2 ASP A  83     -15.169  -2.139 -17.227  1.00 32.92
ATOM    676  N   LEU A  84     -13.234   1.869 -20.587  1.00 31.57
ATOM    677  CA  LEU A  84     -12.169   2.411 -21.443  1.00 29.71
ATOM    678  C   LEU A  84     -11.918   3.855 -21.030  1.00 29.73
ATOM    679  O   LEU A  84     -10.782   4.319 -21.022  1.00 29.41
ATOM    680  CB  LEU A  84     -12.543   2.357 -22.929  1.00 29.38
ATOM    681  CG  LEU A  84     -12.699   1.019 -23.669  1.00 28.51
ATOM    682  CD1 LEU A  84     -12.934   1.322 -25.105  1.00 26.39
ATOM    683  CD2 LEU A  84     -11.489   0.128 -23.542  1.00 28.46
ATOM    684  N   PHE A  85     -12.986   4.558 -20.666  1.00 30.42
ATOM    685  CA  PHE A  85     -12.868   5.941 -20.208  1.00 31.48
ATOM    686  C   PHE A  85     -12.088   5.983 -18.911  1.00 31.54
ATOM    687  O   PHE A  85     -11.336   6.923 -18.656  1.00 31.13
ATOM    688  CB  PHE A  85     -14.233   6.556 -19.982  1.00 31.89
ATOM    689  CG  PHE A  85     -14.759   7.277 -21.165  1.00 32.99
ATOM    690  CD1 PHE A  85     -13.942   8.145 -21.872  1.00 33.14
ATOM    691  CD2 PHE A  85     -16.085   7.123 -21.559  1.00 34.00
ATOM    692  CE1 PHE A  85     -14.440   8.854 -22.955  1.00 34.60
ATOM    693  CE2 PHE A  85     -16.594   7.826 -22.638  1.00 33.02
ATOM    694  CZ  PHE A  85     -15.774   8.694 -23.339  1.00 34.18
ATOM    695  N   MET A  86     -12.309   4.981 -18.069  1.00 30.53
ATOM    696  CA  MET A  86     -11.580   4.901 -16.818  1.00 30.89
ATOM    697  C   MET A  86     -10.111   4.674 -17.186  1.00 30.80
ATOM    698  O   MET A  86      -9.237   5.476 -16.840  1.00 30.54
ATOM    699  CB  MET A  86     -12.093   3.732 -15.966  1.00 31.23
ATOM    700  CG  MET A  86     -13.526   3.882 -15.483  1.00 30.27
ATOM    701  SD  MET A  86     -14.001   2.716 -14.181  1.00 28.89
ATOM    702  CE  MET A  86     -14.884   1.635 -15.056  1.00 30.52
ATOM    703  N   VAL A  87      -9.874   3.627 -17.975  1.00 29.28
ATOM    704  CA  VAL A  87      -8.539   3.247 -18.414  1.00 28.00
ATOM    705  C   VAL A  87      -7.724   4.412 -18.971  1.00 29.45
ATOM    706  O   VAL A  87      -6.526   4.515 -18.723  1.00 27.76
ATOM    707  CB  VAL A  87      -8.613   2.120 -19.463  1.00 26.34
ATOM    708  CG1 VAL A  87      -7.238   1.803 -19.995  1.00 26.81
ATOM    709  CG2 VAL A  87      -9.223   0.881 -18.857  1.00 24.52
ATOM    710  N   PHE A  88      -8.387   5.308 -19.695  1.00 32.58
ATOM    711  CA  PHE A  88      -7.705   6.452 -20.300  1.00 34.42
ATOM    712  C   PHE A  88      -7.908   7.736 -19.526  1.00 34.10
ATOM    713  O   PHE A  88      -6.956   8.459 -19.262  1.00 33.75
ATOM    714  CB  PHE A  88      -8.184   6.655 -21.739  1.00 37.34
ATOM    715  CG  PHE A  88      -8.103   5.420 -22.579  1.00 39.60
ATOM    716  CD1 PHE A  88      -6.940   4.648 -22.591  1.00 40.30
ATOM    717  CD2 PHE A  88      -9.205   4.997 -23.320  1.00 41.12
ATOM    718  CE1 PHE A  88      -6.872   3.467 -23.322  1.00 41.74
ATOM    719  CE2 PHE A  88      -9.154   3.818 -24.057  1.00 43.80
ATOM    720  CZ  PHE A  88      -7.980   3.048 -24.057  1.00 43.22
ATOM    721  N   GLY A  89      -9.157   8.024 -19.182  1.00 34.06
ATOM    722  CA  GLY A  89      -9.462   9.239 -18.453  1.00 33.70
ATOM    723  C   GLY A  89      -8.833   9.311 -17.079  1.00 33.35
ATOM    724  O   GLY A  89      -8.098  10.251 -16.772  1.00 33.72
ATOM    725  N   GLY A  90      -9.107   8.308 -16.255  1.00 32.59
ATOM    726  CA  GLY A  90      -8.570   8.306 -14.912  1.00 31.93
ATOM    727  C   GLY A  90      -7.261   7.575 -14.747  1.00 32.68
ATOM    728  O   GLY A  90      -6.255   8.175 -14.406  1.00 30.86
ATOM    729  N   PHE A  91      -7.280   6.281 -15.051  1.00 35.52
ATOM    730  CA  PHE A  91      -6.132   5.376 -14.908  1.00 36.38
ATOM    731  C   PHE A  91      -4.779   5.830 -15.469  1.00 36.82
ATOM    732  O   PHE A  91      -3.725   5.419 -14.973  1.00 36.26
ATOM    733  CB  PHE A  91      -6.480   3.979 -15.445  1.00 36.64
ATOM    734  CG  PHE A  91      -7.572   3.267 -14.674  1.00 37.15
ATOM    735  CD1 PHE A  91      -7.644   1.883 -14.678  1.00 39.19
ATOM    736  CD2 PHE A  91      -8.527   3.970 -13.957  1.00 38.52
ATOM    737  CE1 PHE A  91      -8.646   1.213 -13.978  1.00 38.89
ATOM    738  CE2 PHE A  91      -9.524   3.310 -13.260  1.00 38.55
ATOM    739  CZ  PHE A  91      -9.581   1.930 -13.272  1.00 38.81
ATOM    740  N   THR A  92      -4.799   6.645 -16.517  1.00 36.28
ATOM    741  CA  THR A  92      -3.558   7.133 -17.099  1.00 35.68
ATOM    742  C   THR A  92      -2.902   8.117 -16.122  1.00 36.63
ATOM    743  O   THR A  92      -1.684   8.129 -15.950  1.00 33.80
ATOM    744  CB  THR A  92      -3.821   7.830 -18.461  1.00 35.26
ATOM    745  OG1 THR A  92      -4.725   8.930 -18.287  1.00 35.38
ATOM    746  CG2 THR A  92      -4.418   6.852 -19.446  1.00 34.60
ATOM    747  N   THR A  93      -3.758   8.886 -15.442  1.00 38.50
ATOM    748  CA  THR A  93      -3.387   9.920 -14.471  1.00 38.29
ATOM    749  C   THR A  93      -3.069   9.348 -13.090  1.00 38.17
ATOM    750  O   THR A  93      -2.411   9.997 -12.279  1.00 37.81
ATOM    751  CB  THR A  93      -4.547  10.951 -14.309  1.00 39.57
ATOM    752  OG1 THR A  93      -5.136  11.227 -15.591  1.00 41.77
ATOM    753  CG2 THR A  93      -4.039  12.252 -13.701  1.00 37.82
ATOM    754  N   THR A  94      -3.582   8.153 -12.809  1.00 38.41
ATOM    755  CA  THR A  94      -3.347   7.498 -11.527  1.00 37.21
ATOM    756  C   THR A  94      -2.001   6.769 -11.537  1.00 38.25
ATOM    757  O   THR A  94      -1.339   6.670 -10.498  1.00 39.03
ATOM    758  CB  THR A  94      -4.503   6.544 -11.160  1.00 35.66
ATOM    759  OG1 THR A  94      -4.252   5.941  -9.891  1.00 35.29
ATOM    760  CG2 THR A  94      -4.654   5.481 -12.172  1.00 34.82
ATOM    761  N   LEU A  95      -1.599   6.275 -12.712  1.00 38.09
ATOM    762  CA  LEU A  95      -0.313   5.597 -12.874  1.00 37.35
ATOM    763  C   LEU A  95       0.829   6.622 -12.940  1.00 37.78
ATOM    764  O   LEU A  95       1.924   6.357 -12.435  1.00 37.75
ATOM    765  CB  LEU A  95      -0.309   4.712 -14.130  1.00 37.03
ATOM    766  CG  LEU A  95       1.031   4.205 -14.696  1.00 35.68
ATOM    767  CD1 LEU A  95       1.817   3.448 -13.637  1.00 36.38
ATOM    768  CD2 LEU A  95       0.800   3.326 -15.901  1.00 32.78
ATOM    769  N   TYR A  96       0.587   7.778 -13.569  1.00 37.85
ATOM    770  CA  TYR A  96       1.617   8.820 -13.663  1.00 38.72
ATOM    771  C   TYR A  96       1.838   9.354 -12.256  1.00 37.48
ATOM    772  O   TYR A  96       2.979   9.550 -11.828  1.00 37.14
ATOM    773  CB  TYR A  96       1.187   9.960 -14.612  1.00 41.71
ATOM    774  CG  TYR A  96       2.290  10.961 -14.989  1.00 46.06
ATOM    775  CD1 TYR A  96       3.054  10.793 -16.156  1.00 48.75
ATOM    776  CD2 TYR A  96       2.569  12.073 -14.183  1.00 47.95
ATOM    777  CE1 TYR A  96       4.085  11.713 -16.512  1.00 49.76
ATOM    778  CE2 TYR A  96       3.589  12.995 -14.526  1.00 50.25
ATOM    779  CZ  TYR A  96       4.349  12.809 -15.691  1.00 50.74
ATOM    780  OH  TYR A  96       5.380  13.691 -16.000  1.00 50.66
ATOM    781  N   THR A  97       0.731   9.532 -11.536  1.00 35.94
ATOM    782  CA  THR A  97       0.735  10.029 -10.163  1.00 35.44
ATOM    783  C   THR A  97       1.494   9.109  -9.208  1.00 35.15
ATOM    784  O   THR A  97       2.251   9.593  -8.379  1.00 35.19
ATOM    785  CB  THR A  97      -0.709  10.233  -9.649  1.00 36.02
ATOM    786  OG1 THR A  97      -1.293  11.365 -10.304  1.00 34.91
ATOM    787  CG2 THR A  97      -0.738  10.442  -8.151  1.00 33.32
ATOM    788  N   SER A  98       1.272   7.796  -9.312  1.00 35.75
ATOM    789  CA  SER A  98       1.950   6.807  -8.463  1.00 35.63
ATOM    790  C   SER A  98       3.440   6.781  -8.797  1.00 37.98
ATOM    791  O   SER A  98       4.292   6.781  -7.901  1.00 39.22
ATOM    792  CB  SER A  98       1.367   5.411  -8.676  1.00 33.28
ATOM    793  OG  SER A  98       0.047   5.324  -8.186  1.00 31.36
ATOM    794  N   LEU A  99       3.741   6.762 -10.097  1.00 38.46
ATOM    795  CA  LEU A  99       5.113   6.755 -10.587  1.00 37.54
ATOM    796  C   LEU A  99       5.913   7.921 -10.050  1.00 38.36
ATOM    797  O   LEU A  99       7.096   7.767  -9.763  1.00 39.22
ATOM    798  CB  LEU A  99       5.145   6.793 -12.112  1.00 35.11
ATOM    799  CG  LEU A  99       5.090   5.432 -12.789  1.00 32.22
ATOM    800  CD1 LEU A  99       5.022   5.632 -14.291  1.00 30.02
ATOM    801  CD2 LEU A  99       6.313   4.617 -12.383  1.00 28.17
ATOM    802  N   HIS A 100       5.260   9.074  -9.905  1.00 39.34
ATOM    803  CA  HIS A 100       5.912  10.285  -9.404  1.00 41.03
ATOM    804  C   HIS A 100       5.761  10.600  -7.910  1.00 40.79
ATOM    805  O   HIS A 100       6.439  11.493  -7.406  1.00 40.79
ATOM    806  CB  HIS A 100       5.500  11.493 -10.244  1.00 43.31
ATOM    807  CG  HIS A 100       5.999  11.439 -11.656  1.00 46.02
ATOM    808  ND1 HIS A 100       5.364  10.717 -12.644  1.00 46.45
ATOM    809  CD2 HIS A 100       7.086  12.000 -12.238  1.00 47.61
ATOM    810  CE1 HIS A 100       6.041  10.835 -13.772  1.00 48.44
ATOM    811  NE2 HIS A 100       7.089  11.610 -13.556  1.00 48.66
ATOM    812  N   GLY A 101       4.887   9.869  -7.215  1.00 41.35
ATOM    813  CA  GLY A 101       4.678  10.071  -5.784  1.00 41.43
ATOM    814  C   GLY A 101       3.668  11.121  -5.333  1.00 41.77
ATOM    815  O   GLY A 101       3.521  11.358  -4.134  1.00 41.86
ATOM    816  N   TYR A 102       2.978  11.746  -6.285  1.00 43.23
ATOM    817  CA  TYR A 102       1.973  12.783  -6.012  1.00 43.70
ATOM    818  C   TYR A 102       1.287  13.196  -7.322  1.00 42.70
ATOM    819  O   TYR A 102       1.655  12.717  -8.402  1.00 42.37
ATOM    820  CB  TYR A 102       2.627  14.019  -5.363  1.00 45.92
ATOM    821  CG  TYR A 102       3.472  14.882  -6.306  1.00 48.47
ATOM    822  CD1 TYR A 102       4.759  14.491  -6.700  1.00 47.45
ATOM    823  CD2 TYR A 102       2.972  16.086  -6.814  1.00 49.47
ATOM    824  CE1 TYR A 102       5.516  15.272  -7.577  1.00 47.53
ATOM    825  CE2 TYR A 102       3.722  16.870  -7.689  1.00 49.25
ATOM    826  CZ  TYR A 102       4.989  16.460  -8.066  1.00 48.42
ATOM    827  OH  TYR A 102       5.713  17.253  -8.934  1.00 49.80
ATOM    828  N   PHE A 103       0.292  14.076  -7.223  1.00 41.63
ATOM    829  CA  PHE A 103      -0.425  14.560  -8.403  1.00 41.89
ATOM    830  C   PHE A 103       0.345  15.675  -9.117  1.00 42.98
ATOM    831  O   PHE A 103       0.153  16.862  -8.851  1.00 42.90
ATOM    832  CB  PHE A 103      -1.846  15.013  -8.038  1.00 39.89
ATOM    833  CG  PHE A 103      -2.809  13.874  -7.827  1.00 38.96
ATOM    834  CD1 PHE A 103      -3.202  13.504  -6.545  1.00 38.65
ATOM    835  CD2 PHE A 103      -3.286  13.143  -8.909  1.00 37.91
ATOM    836  CE1 PHE A 103      -4.056  12.413  -6.345  1.00 39.46
ATOM    837  CE2 PHE A 103      -4.133  12.057  -8.723  1.00 38.63
ATOM    838  CZ  PHE A 103      -4.520  11.688  -7.439  1.00 38.45
ATOM    839  N   VAL A 104       1.224  15.271 -10.029  1.00 44.95
ATOM    840  CA  VAL A 104       2.049  16.204 -10.794  1.00 46.56
ATOM    841  C   VAL A 104       1.197  17.165 -11.625  1.00 48.40
ATOM    842  O   VAL A 104       1.468  18.365 -11.630  1.00 49.99
ATOM    843  CB  VAL A 104       3.096  15.446 -11.696  1.00 46.06
ATOM    844  CG1 VAL A 104       3.903  16.421 -12.561  1.00 44.03
ATOM    845  CG2 VAL A 104       4.042  14.628 -10.822  1.00 44.27
ATOM    846  N   PHE A 105       0.162  16.658 -12.301  1.00 50.03
ATOM    847  CA  PHE A 105      -0.717  17.519 -13.112  1.00 51.65
ATOM    848  C   PHE A 105      -1.683  18.302 -12.228  1.00 51.04
ATOM    849  O   PHE A 105      -2.684  18.839 -12.707  1.00 51.79
ATOM    850  CB  PHE A 105      -1.515  16.707 -14.142  1.00 54.49
ATOM    851  CG  PHE A 105      -0.660  15.943 -15.103  1.00 58.43
ATOM    852  CD1 PHE A 105       0.481  16.529 -15.658  1.00 59.49
ATOM    853  CD2 PHE A 105      -0.970  14.622 -15.428  1.00 60.65
ATOM    854  CE1 PHE A 105       1.307  15.813 -16.522  1.00 61.62
ATOM    855  CE2 PHE A 105      -0.148  13.886 -16.297  1.00 63.11
ATOM    856  CZ  PHE A 105       0.994  14.483 -16.844  1.00 62.80
ATOM    857  N   GLY A 106      -1.401  18.303 -10.929  1.00 49.86
ATOM    858  CA  GLY A 106      -2.215  19.021  -9.972  1.00 49.23
ATOM    859  C   GLY A 106      -3.676  18.637  -9.835  1.00 48.63
ATOM    860  O   GLY A 106      -4.068  17.506 -10.096  1.00 48.67
ATOM    861  N   PRO A 107      -4.515  19.607  -9.456  1.00 48.84
ATOM    862  CA  PRO A 107      -5.956  19.479  -9.248  1.00 48.75
ATOM    863  C   PRO A 107      -6.772  18.869 -10.381  1.00 48.23
ATOM    864  O   PRO A 107      -7.735  18.152 -10.101  1.00 50.81
ATOM    865  CB  PRO A 107      -6.378  20.912  -8.920  1.00 48.98
ATOM    866  CG  PRO A 107      -5.380  21.737  -9.662  1.00 50.28
ATOM    867  CD  PRO A 107      -4.106  21.016  -9.341  1.00 49.93
ATOM    868  N   THR A 108      -6.426  19.154 -11.641  1.00 46.41
ATOM    869  CA  THR A 108      -7.169  18.569 -12.766  1.00 44.44
ATOM    870  C   THR A 108      -6.762  17.092 -12.869  1.00 43.42
ATOM    871  O   THR A 108      -7.586  16.231 -13.188  1.00 42.83
ATOM    872  CB  THR A 108      -6.930  19.315 -14.109  1.00 43.24
ATOM    873  OG1 THR A 108      -5.629  19.003 -14.609  1.00 44.16
ATOM    874  CG2 THR A 108      -7.035  20.820 -13.917  1.00 42.03
ATOM    875  N   GLY A 109      -5.501  16.809 -12.525  1.00 42.19
ATOM    876  CA  GLY A 109      -4.997  15.444 -12.520  1.00 41.62
ATOM    877  C   GLY A 109      -5.700  14.653 -11.426  1.00 41.12
ATOM    878  O   GLY A 109      -5.778  13.421 -11.461  1.00 42.11
ATOM    879  N   CYS A 110      -6.193  15.387 -10.435  1.00 39.46
ATOM    880  CA  CYS A 110      -6.938  14.823  -9.326  1.00 38.31
ATOM    881  C   CYS A 110      -8.391  14.697  -9.764  1.00 38.39
ATOM    882  O   CYS A 110      -9.091  13.761  -9.383  1.00 38.67
ATOM    883  CB  CYS A 110      -6.858  15.750  -8.122  1.00 38.11
ATOM    884  SG  CYS A 110      -7.797  15.176  -6.679  1.00 37.03
ATOM    885  N   ASN A 111      -8.834  15.651 -10.574  1.00 37.94
ATOM    886  CA  ASN A 111     -10.197  15.661 -11.079  1.00 37.88
ATOM    887  C   ASN A 111     -10.427  14.553 -12.102  1.00 37.75
ATOM    888  O   ASN A 111     -11.440  13.868 -12.045  1.00 37.14
ATOM    889  CB  ASN A 111     -10.530  17.025 -11.695  1.00 38.97
ATOM    890  CG  ASN A 111     -10.784  18.113 -10.643  1.00 38.87
ATOM    891  OD1 ASN A 111     -11.473  17.898  -9.647  1.00 40.62
ATOM    892  ND2 ASN A 111     -10.264  19.300 -10.901  1.00 37.83
ATOM    893  N   LEU A 112      -9.482  14.363 -13.019  1.00 37.38
ATOM    894  CA  LEU A 112      -9.606  13.325 -14.045  1.00 38.02
ATOM    895  C   LEU A 112      -9.537  11.932 -13.449  1.00 38.85
ATOM    896  O   LEU A 112     -10.214  11.009 -13.912  1.00 38.91
ATOM    897  CB  LEU A 112      -8.507  13.467 -15.101  1.00 37.37
ATOM    898  CG  LEU A 112      -8.633  14.622 -16.099  1.00 36.97
ATOM    899  CD1 LEU A 112      -7.320  14.735 -16.849  1.00 36.15
ATOM    900  CD2 LEU A 112      -9.817  14.432 -17.059  1.00 33.76
ATOM    901  N   GLU A 113      -8.682  11.795 -12.435  1.00 40.64
ATOM    902  CA  GLU A 113      -8.454  10.541 -11.712  1.00 40.03
ATOM    903  C   GLU A 113      -9.679  10.176 -10.859  1.00 38.99
ATOM    904  O   GLU A 113     -10.104   9.020 -10.841  1.00 38.68
ATOM    905  CB  GLU A 113      -7.204  10.681 -10.828  1.00 39.32
ATOM    906  CG  GLU A 113      -6.464   9.384 -10.541  1.00 40.75
ATOM    907  CD  GLU A 113      -7.287   8.384  -9.754  1.00 42.34
ATOM    908  OE1 GLU A 113      -7.393   7.217 -10.203  1.00 42.78
ATOM    909  OE2 GLU A 113      -7.836   8.771  -8.696  1.00 42.07
ATOM    910  N   GLY A 114     -10.235  11.171 -10.168  1.00 38.65
ATOM    911  CA  GLY A 114     -11.403  10.958  -9.328  1.00 38.53
ATOM    912  C   GLY A 114     -12.712  10.917 -10.097  1.00 38.80
ATOM    913  O   GLY A 114     -13.600  10.116  -9.769  1.00 38.34
ATOM    914  N   PHE A 115     -12.821  11.765 -11.127  1.00 38.15
ATOM    915  CA  PHE A 115     -14.020  11.846 -11.961  1.00 36.59
ATOM    916  C   PHE A 115     -14.320  10.567 -12.710  1.00 35.62
ATOM    917  O   PHE A 115     -15.402  10.011 -12.577  1.00 36.51
ATOM    918  CB  PHE A 115     -13.932  12.994 -12.965  1.00 35.69
ATOM    919  CG  PHE A 115     -15.152  13.130 -13.819  1.00 35.20
ATOM    920  CD1 PHE A 115     -15.113  12.804 -15.166  1.00 34.22
ATOM    921  CD2 PHE A 115     -16.365  13.525 -13.261  1.00 35.50
ATOM    922  CE1 PHE A 115     -16.263  12.862 -15.943  1.00 33.09
ATOM    923  CE2 PHE A 115     -17.526  13.588 -14.034  1.00 33.32
ATOM    924  CZ  PHE A 115     -17.474  13.253 -15.373  1.00 33.27
ATOM    925  N   PHE A 116     -13.365  10.104 -13.500  1.00 35.51
ATOM    926  CA  PHE A 116     -13.555   8.886 -14.269  1.00 36.45
ATOM    927  C   PHE A 116     -13.612   7.590 -13.457  1.00 38.00
ATOM    928  O   PHE A 116     -13.867   6.532 -14.022  1.00 39.64
ATOM    929  CB  PHE A 116     -12.504   8.785 -15.372  1.00 34.93
ATOM    930  CG  PHE A 116     -12.682   9.793 -16.459  1.00 33.86
ATOM    931  CD1 PHE A 116     -13.762   9.706 -17.329  1.00 34.03
ATOM    932  CD2 PHE A 116     -11.780  10.840 -16.611  1.00 33.34
ATOM    933  CE1 PHE A 116     -13.939  10.652 -18.335  1.00 32.24
ATOM    934  CE2 PHE A 116     -11.949  11.783 -17.608  1.00 31.44
ATOM    935  CZ  PHE A 116     -13.029  11.689 -18.470  1.00 31.14
ATOM    936  N   ALA A 117     -13.345   7.652 -12.153  1.00 38.57
ATOM    937  CA  ALA A 117     -13.417   6.454 -11.314  1.00 39.73
ATOM    938  C   ALA A 117     -14.811   6.414 -10.695  1.00 41.52
ATOM    939  O   ALA A 117     -15.351   5.345 -10.387  1.00 41.37
ATOM    940  CB  ALA A 117     -12.359   6.487 -10.247  1.00 39.30
ATOM    941  N   THR A 118     -15.383   7.603 -10.523  1.00 43.65
ATOM    942  CA  THR A 118     -16.727   7.762  -9.984  1.00 45.08
ATOM    943  C   THR A 118     -17.705   7.517 -11.123  1.00 45.63
ATOM    944  O   THR A 118     -18.650   6.750 -10.980  1.00 45.85
ATOM    945  CB  THR A 118     -16.948   9.179  -9.451  1.00 45.37
ATOM    946  OG1 THR A 118     -15.952   9.472  -8.469  1.00 46.51
ATOM    947  CG2 THR A 118     -18.328   9.301  -8.817  1.00 45.56
ATOM    948  N   LEU A 119     -17.464   8.182 -12.252  1.00 46.55
ATOM    949  CA  LEU A 119     -18.297   8.036 -13.440  1.00 47.71
ATOM    950  C   LEU A 119     -18.425   6.556 -13.790  1.00 48.83
ATOM    951  O   LEU A 119     -19.531   6.059 -13.971  1.00 49.95
ATOM    952  CB  LEU A 119     -17.669   8.768 -14.627  1.00 48.19
ATOM    953  CG  LEU A 119     -18.400   8.658 -15.970  1.00 47.99
ATOM    954  CD1 LEU A 119     -19.638   9.531 -15.961  1.00 48.11
ATOM    955  CD2 LEU A 119     -17.481   9.083 -17.087  1.00 48.48
ATOM    956  N   GLY A 120     -17.295   5.854 -13.850  1.00 48.67
ATOM    957  CA  GLY A 120     -17.316   4.438 -14.182  1.00 47.88
ATOM    958  C   GLY A 120     -17.988   3.576 -13.130  1.00 47.25
ATOM    959  O   GLY A 120     -18.599   2.550 -13.448  1.00 46.57
ATOM    960  N   GLY A 121     -17.854   3.980 -11.870  1.00 46.57
ATOM    961  CA  GLY A 121     -18.467   3.227 -10.791  1.00 46.78
ATOM    962  C   GLY A 121     -19.974   3.391 -10.807  1.00 46.17
ATOM    963  O   GLY A 121     -20.713   2.447 -10.526  1.00 45.42
ATOM    964  N   GLU A 122     -20.413   4.606 -11.136  1.00 45.79
ATOM    965  CA  GLU A 122     -21.829   4.959 -11.220  1.00 45.48
ATOM    966  C   GLU A 122     -22.482   4.515 -12.542  1.00 44.32
ATOM    967  O   GLU A 122     -23.679   4.229 -12.569  1.00 44.69
ATOM    968  CB  GLU A 122     -22.012   6.464 -11.005  1.00 47.05
ATOM    969  CG  GLU A 122     -21.644   6.941  -9.607  1.00 47.88
ATOM    970  CD  GLU A 122     -22.632   6.481  -8.557  1.00 49.44
ATOM    971  OE1 GLU A 122     -23.853   6.619  -8.787  1.00 49.41
ATOM    972  OE2 GLU A 122     -22.187   5.989  -7.500  1.00 50.74
ATOM    973  N   ILE A 123     -21.720   4.491 -13.640  1.00 42.83
ATOM    974  CA  ILE A 123     -22.257   4.016 -14.923  1.00 40.80
ATOM    975  C   ILE A 123     -22.633   2.563 -14.630  1.00 40.50
ATOM    976  O   ILE A 123     -23.611   2.037 -15.149  1.00 40.10
ATOM    977  CB  ILE A 123     -21.180   3.974 -16.056  1.00 40.27
ATOM    978  CG1 ILE A 123     -20.734   5.377 -16.490  1.00 38.62
ATOM    979  CG2 ILE A 123     -21.688   3.159 -17.231  1.00 39.58
ATOM    980  CD1 ILE A 123     -21.819   6.260 -17.011  1.00 37.47
ATOM    981  N   ALA A 124     -21.824   1.938 -13.775  1.00 40.31
ATOM    982  CA  ALA A 124     -21.999   0.559 -13.352  1.00 40.10
ATOM    983  C   ALA A 124     -23.237   0.388 -12.466  1.00 39.93
ATOM    984  O   ALA A 124     -24.165  -0.332 -12.828  1.00 40.55
ATOM    985  CB  ALA A 124     -20.738   0.080 -12.619  1.00 40.58
ATOM    986  N   LEU A 125     -23.260   1.080 -11.328  1.00 39.63
ATOM    987  CA  LEU A 125     -24.380   1.007 -10.374  1.00 39.18
ATOM    988  C   LEU A 125     -25.761   1.177 -11.031  1.00 38.87
ATOM    989  O   LEU A 125     -26.649   0.333 -10.869  1.00 37.39
ATOM    990  CB  LEU A 125     -24.206   2.070  -9.278  1.00 37.78
ATOM    991  CG  LEU A 125     -24.847   1.923  -7.889  1.00 36.83
ATOM    992  CD1 LEU A 125     -25.570   3.212  -7.553  1.00 37.13
ATOM    993  CD2 LEU A 125     -25.778   0.720  -7.784  1.00 35.73
ATOM    994  N   TRP A 126     -25.926   2.271 -11.766  1.00 38.28
ATOM    995  CA  TRP A 126     -27.180   2.566 -12.427  1.00 38.09
ATOM    996  C   TRP A 126     -27.544   1.547 -13.495  1.00 39.20
ATOM    997  O   TRP A 126     -28.711   1.192 -13.643  1.00 38.70
ATOM    998  CB  TRP A 126     -27.151   3.987 -12.972  1.00 37.24
ATOM    999  CG  TRP A 126     -27.140   4.991 -11.865  1.00 37.29
ATOM   1000  CD1 TRP A 126     -26.071   5.714 -11.420  1.00 38.43
ATOM   1001  CD2 TRP A 126     -28.238   5.338 -11.014  1.00 38.77
ATOM   1002  NE1 TRP A 126     -26.429   6.486 -10.337  1.00 38.39
ATOM   1003  CE2 TRP A 126     -27.754   6.271 -10.066  1.00 39.09
ATOM   1004  CE3 TRP A 126     -29.585   4.946 -10.955  1.00 39.11
ATOM   1005  CZ2 TRP A 126     -28.570   6.817  -9.070  1.00 38.99
ATOM   1006  CZ3 TRP A 126     -30.394   5.489  -9.969  1.00 39.17
ATOM   1007  CH2 TRP A 126     -29.882   6.416  -9.037  1.00 40.42
ATOM   1008  N   SER A 127     -26.544   1.036 -14.204  1.00 40.70
ATOM   1009  CA  SER A 127     -26.801   0.030 -15.227  1.00 42.92
ATOM   1010  C   SER A 127     -27.385  -1.220 -14.562  1.00 44.93
ATOM   1011  O   SER A 127     -28.188  -1.942 -15.161  1.00 45.30
ATOM   1012  CB  SER A 127     -25.526  -0.308 -15.999  1.00 41.64
ATOM   1013  OG  SER A 127     -25.190   0.731 -16.902  1.00 41.92
ATOM   1014  N   LEU A 128     -27.002  -1.449 -13.310  1.00 47.25
ATOM   1015  CA  LEU A 128     -27.509  -2.585 -12.545  1.00 49.72
ATOM   1016  C   LEU A 128     -28.986  -2.404 -12.222  1.00 50.93
ATOM   1017  O   LEU A 128     -29.687  -3.382 -11.946  1.00 51.41
ATOM   1018  CB  LEU A 128     -26.734  -2.754 -11.241  1.00 49.65
ATOM   1019  CG  LEU A 128     -25.347  -3.359 -11.397  1.00 49.92
ATOM   1020  CD1 LEU A 128     -24.744  -3.630 -10.024  1.00 49.57
ATOM   1021  CD2 LEU A 128     -25.463  -4.646 -12.193  1.00 49.62
ATOM   1022  N   VAL A 129     -29.433  -1.146 -12.213  1.00 51.42
ATOM   1023  CA  VAL A 129     -30.827  -0.820 -11.936  1.00 51.78
ATOM   1024  C   VAL A 129     -31.641  -0.971 -13.231  1.00 52.29
ATOM   1025  O   VAL A 129     -32.743  -1.532 -13.216  1.00 53.79
ATOM   1026  CB  VAL A 129     -30.983   0.605 -11.329  1.00 50.96
ATOM   1027  CG1 VAL A 129     -32.430   0.869 -10.953  1.00 50.58
ATOM   1028  CG2 VAL A 129     -30.117   0.747 -10.092  1.00 51.19
ATOM   1029  N   VAL A 130     -31.088  -0.512 -14.356  1.00 50.44
ATOM   1030  CA  VAL A 130     -31.782  -0.649 -15.634  1.00 48.89
ATOM   1031  C   VAL A 130     -31.916  -2.143 -15.928  1.00 49.38
ATOM   1032  O   VAL A 130     -32.915  -2.588 -16.503  1.00 50.26
ATOM   1033  CB  VAL A 130     -31.018   0.044 -16.774  1.00 48.24
ATOM   1034  CG1 VAL A 130     -31.673  -0.254 -18.120  1.00 47.82
ATOM   1035  CG2 VAL A 130     -30.982   1.536 -16.532  1.00 46.84
ATOM   1036  N   LEU A 131     -30.914  -2.912 -15.498  1.00 48.43
ATOM   1037  CA  LEU A 131     -30.910  -4.357 -15.686  1.00 47.17
ATOM   1038  C   LEU A 131     -31.782  -5.048 -14.648  1.00 46.74
ATOM   1039  O   LEU A 131     -32.521  -5.968 -14.983  1.00 47.78
ATOM   1040  CB  LEU A 131     -29.487  -4.909 -15.650  1.00 46.43
ATOM   1041  CG  LEU A 131     -28.588  -4.667 -16.872  1.00 45.15
ATOM   1042  CD1 LEU A 131     -27.171  -5.025 -16.507  1.00 45.04
ATOM   1043  CD2 LEU A 131     -29.038  -5.488 -18.073  1.00 44.18
ATOM   1044  N   ALA A 132     -31.699  -4.610 -13.392  1.00 45.79
ATOM   1045  CA  ALA A 132     -32.532  -5.181 -12.334  1.00 45.63
ATOM   1046  C   ALA A 132     -33.999  -5.013 -12.755  1.00 46.02
ATOM   1047  O   ALA A 132     -34.838  -5.866 -12.465  1.00 45.93
ATOM   1048  CB  ALA A 132     -32.272  -4.482 -11.001  1.00 44.78
ATOM   1049  N   ILE A 133     -34.287  -3.918 -13.463  1.00 46.38
ATOM   1050  CA  ILE A 133     -35.630  -3.640 -13.984  1.00 46.64
ATOM   1051  C   ILE A 133     -35.875  -4.588 -15.150  1.00 47.16
ATOM   1052  O   ILE A 133     -36.839  -5.348 -15.156  1.00 45.39
ATOM   1053  CB  ILE A 133     -35.762  -2.186 -14.528  1.00 45.20
ATOM   1054  CG1 ILE A 133     -35.770  -1.180 -13.376  1.00 43.90
ATOM   1055  CG2 ILE A 133     -37.020  -2.050 -15.386  1.00 42.61
ATOM   1056  CD1 ILE A 133     -35.882   0.269 -13.831  1.00 44.56
ATOM   1057  N   GLU A 134     -34.975  -4.535 -16.127  1.00 49.52
ATOM   1058  CA  GLU A 134     -35.061  -5.374 -17.306  1.00 52.86
ATOM   1059  C   GLU A 134     -35.376  -6.793 -16.887  1.00 53.10
ATOM   1060  O   GLU A 134     -36.219  -7.446 -17.487  1.00 53.30
ATOM   1061  CB  GLU A 134     -33.746  -5.332 -18.088  1.00 55.64
ATOM   1062  CG  GLU A 134     -33.820  -5.938 -19.498  1.00 59.58
ATOM   1063  CD  GLU A 134     -33.277  -7.365 -19.590  1.00 61.80
ATOM   1064  OE1 GLU A 134     -33.421  -8.136 -18.616  1.00 61.49
ATOM   1065  OE2 GLU A 134     -32.699  -7.713 -20.649  1.00 63.81
ATOM   1066  N   ARG A 135     -34.719  -7.263 -15.836  1.00 54.84
ATOM   1067  CA  ARG A 135     -34.975  -8.612 -15.365  1.00 57.61
ATOM   1068  C   ARG A 135     -36.439  -8.764 -14.984  1.00 60.78
ATOM   1069  O   ARG A 135     -37.134  -9.613 -15.544  1.00 60.97
ATOM   1070  CB  ARG A 135     -34.087  -8.983 -14.173  1.00 55.24
ATOM   1071  CG  ARG A 135     -32.623  -9.156 -14.497  1.00 53.22
ATOM   1072  CD  ARG A 135     -32.402  -9.648 -15.918  1.00 52.86
ATOM   1073  NE  ARG A 135     -32.883 -11.003 -16.162  1.00 51.63
ATOM   1074  CZ  ARG A 135     -33.171 -11.489 -17.370  1.00 51.19
ATOM   1075  NH1 ARG A 135     -33.037 -10.728 -18.451  1.00 48.43
ATOM   1076  NH2 ARG A 135     -33.553 -12.755 -17.505  1.00 49.25
ATOM   1077  N   TYR A 136     -36.913  -7.907 -14.079  1.00 64.12
ATOM   1078  CA  TYR A 136     -38.299  -7.965 -13.624  1.00 67.16
ATOM   1079  C   TYR A 136     -39.278  -8.078 -14.798  1.00 69.05
ATOM   1080  O   TYR A 136     -39.917  -9.121 -14.953  1.00 69.41
ATOM   1081  CB  TYR A 136     -38.650  -6.761 -12.728  1.00 68.08
ATOM   1082  CG  TYR A 136     -39.960  -6.934 -11.970  1.00 69.84
ATOM   1083  CD1 TYR A 136     -40.070  -7.872 -10.941  1.00 71.40
ATOM   1084  CD2 TYR A 136     -41.108  -6.218 -12.329  1.00 70.00
ATOM   1085  CE1 TYR A 136     -41.292  -8.101 -10.294  1.00 72.14
ATOM   1086  CE2 TYR A 136     -42.336  -6.442 -11.688  1.00 70.45
ATOM   1087  CZ  TYR A 136     -42.418  -7.389 -10.674  1.00 71.54
ATOM   1088  OH  TYR A 136     -43.624  -7.658 -10.059  1.00 71.19
ATOM   1089  N   VAL A 137     -39.312  -7.059 -15.666  1.00 70.85
ATOM   1090  CA  VAL A 137     -40.209  -7.011 -16.838  1.00 72.54
ATOM   1091  C   VAL A 137     -40.218  -8.280 -17.697  1.00 74.50
ATOM   1092  O   VAL A 137     -41.143  -8.507 -18.486  1.00 75.85
ATOM   1093  CB  VAL A 137     -39.923  -5.754 -17.730  1.00 71.61
ATOM   1094  CG1 VAL A 137     -40.691  -5.812 -19.052  1.00 70.57
ATOM   1095  CG2 VAL A 137     -40.316  -4.496 -16.985  1.00 71.34
ATOM   1096  N   VAL A 138     -39.221  -9.137 -17.506  1.00 76.24
ATOM   1097  CA  VAL A 138     -39.151 -10.372 -18.267  1.00 77.43
ATOM   1098  C   VAL A 138     -39.442 -11.628 -17.431  1.00 79.40
ATOM   1099  O   VAL A 138     -40.237 -12.471 -17.838  1.00 78.16
ATOM   1100  CB  VAL A 138     -37.782 -10.516 -18.961  1.00 75.87
ATOM   1101  CG1 VAL A 138     -37.817 -11.675 -19.922  1.00 76.58
ATOM   1102  CG2 VAL A 138     -37.424  -9.241 -19.700  1.00 74.58
ATOM   1103  N   VAL A 139     -38.859 -11.707 -16.235  1.00 82.71
ATOM   1104  CA  VAL A 139     -39.010 -12.878 -15.366  1.00 86.50
ATOM   1105  C   VAL A 139     -40.230 -12.991 -14.438  1.00 89.65
ATOM   1106  O   VAL A 139     -40.991 -13.959 -14.539  1.00 90.26
ATOM   1107  CB  VAL A 139     -37.718 -13.123 -14.516  1.00 86.16
ATOM   1108  CG1 VAL A 139     -37.800 -14.450 -13.781  1.00 85.38
ATOM   1109  CG2 VAL A 139     -36.483 -13.106 -15.398  1.00 86.35
ATOM   1110  N   CYS A 140     -40.411 -12.041 -13.520  1.00 93.11
ATOM   1111  CA  CYS A 140     -41.524 -12.138 -12.574  1.00 96.51
ATOM   1112  C   CYS A 140     -42.911 -11.796 -13.112  1.00 99.41
ATOM   1113  O   CYS A 140     -43.696 -11.108 -12.446  1.00100.56
ATOM   1114  CB  CYS A 140     -41.233 -11.367 -11.284  1.00 95.45
ATOM   1115  SG  CYS A 140     -42.332 -11.834  -9.911  1.00 95.88
ATOM   1116  N   LYS A 141     -43.198 -12.286 -14.319  1.00101.79
ATOM   1117  CA  LYS A 141     -44.492 -12.110 -14.994  1.00103.77
ATOM   1118  C   LYS A 141     -45.080 -10.685 -14.974  1.00104.53
ATOM   1119  O   LYS A 141     -46.153 -10.459 -14.400  1.00104.59
ATOM   1120  CB  LYS A 141     -45.513 -13.104 -14.402  1.00104.54
ATOM   1121  CG  LYS A 141     -45.040 -14.563 -14.377  1.00105.49
ATOM   1122  CD  LYS A 141     -46.030 -15.508 -13.671  1.00106.49
ATOM   1123  CE  LYS A 141     -47.309 -15.759 -14.479  1.00106.18
ATOM   1124  NZ  LYS A 141     -48.192 -16.780 -13.836  1.00104.77
ATOM   1125  N   PRO A 142     -44.366  -9.702 -15.557  1.00105.24
ATOM   1126  CA  PRO A 142     -44.847  -8.310 -15.588  1.00105.81
ATOM   1127  C   PRO A 142     -45.515  -7.866 -16.893  1.00106.14
ATOM   1128  O   PRO A 142     -45.501  -8.595 -17.892  1.00106.22
ATOM   1129  CB  PRO A 142     -43.572  -7.497 -15.329  1.00105.63
ATOM   1130  CG  PRO A 142     -42.596  -8.521 -14.796  1.00106.05
ATOM   1131  CD  PRO A 142     -42.903  -9.708 -15.647  1.00105.21
ATOM   1132  N   MET A 143     -46.040  -6.638 -16.875  1.00106.33
ATOM   1133  CA  MET A 143     -46.743  -6.035 -18.010  1.00106.85
ATOM   1134  C   MET A 143     -47.971  -6.859 -18.401  1.00107.60
ATOM   1135  O   MET A 143     -48.795  -7.185 -17.538  1.00107.85
ATOM   1136  CB  MET A 143     -45.808  -5.835 -19.214  1.00106.51
ATOM   1137  CG  MET A 143     -44.951  -4.568 -19.156  1.00106.38
ATOM   1138  SD  MET A 143     -45.891  -3.009 -19.165  1.00106.56
ATOM   1139  CE  MET A 143     -46.254  -2.781 -20.936  1.00105.74
ATOM   1140  N   SER A 144     -48.096  -7.184 -19.691  1.00108.10
ATOM   1141  CA  SER A 144     -49.225  -7.973 -20.198  1.00108.13
ATOM   1142  C   SER A 144     -48.950  -8.652 -21.549  1.00107.55
ATOM   1143  O   SER A 144     -49.582  -9.658 -21.880  1.00107.47
ATOM   1144  CB  SER A 144     -50.514  -7.116 -20.272  1.00108.49
ATOM   1145  OG  SER A 144     -50.332  -5.888 -20.973  1.00108.27
ATOM   1146  N   ASN A 145     -47.978  -8.126 -22.295  1.00106.91
ATOM   1147  CA  ASN A 145     -47.614  -8.655 -23.617  1.00106.25
ATOM   1148  C   ASN A 145     -46.239  -8.147 -24.076  1.00105.46
ATOM   1149  O   ASN A 145     -45.611  -8.719 -24.975  1.00105.07
ATOM   1150  CB  ASN A 145     -48.673  -8.238 -24.655  1.00107.51
ATOM   1151  CG  ASN A 145     -48.761  -6.705 -24.854  1.00108.78
ATOM   1152  OD1 ASN A 145     -49.149  -6.232 -25.930  1.00108.64
ATOM   1153  ND2 ASN A 145     -48.413  -5.935 -23.817  1.00108.64
ATOM   1154  N   PHE A 146     -45.790  -7.079 -23.419  1.00104.45
ATOM   1155  CA  PHE A 146     -44.535  -6.373 -23.683  1.00102.91
ATOM   1156  C   PHE A 146     -43.206  -7.146 -23.801  1.00101.50
ATOM   1157  O   PHE A 146     -42.984  -8.174 -23.151  1.00101.91
ATOM   1158  CB  PHE A 146     -44.382  -5.261 -22.640  1.00103.12
ATOM   1159  CG  PHE A 146     -43.342  -4.242 -22.982  1.00103.26
ATOM   1160  CD1 PHE A 146     -43.422  -3.520 -24.171  1.00103.66
ATOM   1161  CD2 PHE A 146     -42.290  -3.993 -22.110  1.00103.11
ATOM   1162  CE1 PHE A 146     -42.467  -2.562 -24.487  1.00103.96
ATOM   1163  CE2 PHE A 146     -41.328  -3.036 -22.415  1.00103.74
ATOM   1164  CZ  PHE A 146     -41.416  -2.318 -23.604  1.00103.82
ATOM   1165  N   ARG A 147     -42.315  -6.581 -24.614  1.00 98.85
ATOM   1166  CA  ARG A 147     -40.980  -7.109 -24.873  1.00 95.60
ATOM   1167  C   ARG A 147     -40.114  -5.896 -25.204  1.00 93.22
ATOM   1168  O   ARG A 147     -40.564  -4.977 -25.898  1.00 92.94
ATOM   1169  CB  ARG A 147     -41.014  -8.075 -26.058  1.00 96.56
ATOM   1170  CG  ARG A 147     -39.658  -8.644 -26.461  1.00 97.64
ATOM   1171  CD  ARG A 147     -39.816  -9.910 -27.297  1.00 98.24
ATOM   1172  NE  ARG A 147     -40.465 -10.965 -26.523  1.00 98.91
ATOM   1173  CZ  ARG A 147     -41.760 -11.262 -26.594  1.00 99.35
ATOM   1174  NH1 ARG A 147     -42.556 -10.597 -27.423  1.00100.09
ATOM   1175  NH2 ARG A 147     -42.276 -12.165 -25.773  1.00 99.39
ATOM   1176  N   PHE A 148     -38.883  -5.886 -24.692  1.00 90.36
ATOM   1177  CA  PHE A 148     -37.951  -4.773 -24.915  1.00 87.50
ATOM   1178  C   PHE A 148     -37.373  -4.670 -26.331  1.00 85.83
ATOM   1179  O   PHE A 148     -37.067  -5.680 -26.976  1.00 85.52
ATOM   1180  CB  PHE A 148     -36.789  -4.823 -23.905  1.00 86.57
ATOM   1181  CG  PHE A 148     -37.178  -4.461 -22.495  1.00 84.84
ATOM   1182  CD1 PHE A 148     -37.218  -5.430 -21.500  1.00 84.51
ATOM   1183  CD2 PHE A 148     -37.496  -3.151 -22.158  1.00 83.95
ATOM   1184  CE1 PHE A 148     -37.570  -5.095 -20.196  1.00 83.84
ATOM   1185  CE2 PHE A 148     -37.850  -2.811 -20.852  1.00 82.58
ATOM   1186  CZ  PHE A 148     -37.887  -3.782 -19.874  1.00 82.50
ATOM   1187  N   GLY A 149     -37.230  -3.431 -26.797  1.00 83.47
ATOM   1188  CA  GLY A 149     -36.660  -3.161 -28.105  1.00 80.87
ATOM   1189  C   GLY A 149     -35.351  -2.422 -27.887  1.00 78.79
ATOM   1190  O   GLY A 149     -35.005  -2.116 -26.748  1.00 78.60
ATOM   1191  N   GLU A 150     -34.612  -2.149 -28.958  1.00 77.16
ATOM   1192  CA  GLU A 150     -33.340  -1.431 -28.840  1.00 75.94
ATOM   1193  C   GLU A 150     -33.556  -0.047 -28.234  1.00 74.43
ATOM   1194  O   GLU A 150     -32.721   0.466 -27.486  1.00 74.73
ATOM   1195  CB  GLU A 150     -32.663  -1.272 -30.211  1.00 77.16
ATOM   1196  CG  GLU A 150     -31.765  -2.430 -30.656  1.00 78.06
ATOM   1197  CD  GLU A 150     -30.883  -2.073 -31.856  1.00 78.34
ATOM   1198  OE1 GLU A 150     -29.651  -1.905 -31.685  1.00 78.14
ATOM   1199  OE2 GLU A 150     -31.421  -1.964 -32.977  1.00 78.69
ATOM   1200  N   ASN A 151     -34.690   0.550 -28.571  1.00 72.83
ATOM   1201  CA  ASN A 151     -35.052   1.871 -28.083  1.00 71.66
ATOM   1202  C   ASN A 151     -35.004   1.973 -26.554  1.00 70.41
ATOM   1203  O   ASN A 151     -34.355   2.867 -25.999  1.00 69.18
ATOM   1204  CB  ASN A 151     -36.435   2.282 -28.646  1.00 72.00
ATOM   1205  CG  ASN A 151     -37.522   1.204 -28.461  1.00 70.98
ATOM   1206  OD1 ASN A 151     -38.681   1.529 -28.202  1.00 70.04
ATOM   1207  ND2 ASN A 151     -37.157  -0.065 -28.625  1.00 69.85
ATOM   1208  N   HIS A 152     -35.642   1.009 -25.892  1.00 69.66
ATOM   1209  CA  HIS A 152     -35.709   0.939 -24.431  1.00 69.31
ATOM   1210  C   HIS A 152     -34.311   0.799 -23.837  1.00 67.89
ATOM   1211  O   HIS A 152     -34.013   1.352 -22.777  1.00 66.92
ATOM   1212  CB  HIS A 152     -36.570  -0.257 -24.007  1.00 71.21
ATOM   1213  CG  HIS A 152     -37.884  -0.347 -24.729  1.00 72.73
ATOM   1214  ND1 HIS A 152     -38.229  -1.426 -25.515  1.00 73.28
ATOM   1215  CD2 HIS A 152     -38.925   0.518 -24.801  1.00 72.09
ATOM   1216  CE1 HIS A 152     -39.423  -1.220 -26.043  1.00 74.07
ATOM   1217  NE2 HIS A 152     -39.867  -0.048 -25.625  1.00 72.62
ATOM   1218  N   ALA A 153     -33.461   0.064 -24.553  1.00 66.36
ATOM   1219  CA  ALA A 153     -32.085  -0.180 -24.155  1.00 63.90
ATOM   1220  C   ALA A 153     -31.267   1.110 -24.162  1.00 62.45
ATOM   1221  O   ALA A 153     -30.434   1.321 -23.275  1.00 62.76
ATOM   1222  CB  ALA A 153     -31.453  -1.227 -25.068  1.00 62.99
ATOM   1223  N   ILE A 154     -31.517   1.983 -25.138  1.00 60.15
ATOM   1224  CA  ILE A 154     -30.782   3.246 -25.208  1.00 59.30
ATOM   1225  C   ILE A 154     -31.244   4.239 -24.136  1.00 59.18
ATOM   1226  O   ILE A 154     -30.469   5.087 -23.685  1.00 59.28
ATOM   1227  CB  ILE A 154     -30.883   3.901 -26.592  1.00 57.98
ATOM   1228  CG1 ILE A 154     -30.557   2.878 -27.670  1.00 57.87
ATOM   1229  CG2 ILE A 154     -29.872   5.023 -26.701  1.00 56.42
ATOM   1230  CD1 ILE A 154     -30.650   3.415 -29.064  1.00 57.23
ATOM   1231  N   MET A 155     -32.503   4.137 -23.728  1.00 58.72
ATOM   1232  CA  MET A 155     -33.005   5.027 -22.690  1.00 59.08
ATOM   1233  C   MET A 155     -32.394   4.662 -21.352  1.00 56.72
ATOM   1234  O   MET A 155     -32.082   5.537 -20.555  1.00 57.70
ATOM   1235  CB  MET A 155     -34.537   5.024 -22.640  1.00 62.96
ATOM   1236  CG  MET A 155     -35.157   6.258 -23.331  1.00 67.63
ATOM   1237  SD  MET A 155     -34.405   6.672 -24.983  1.00 74.72
ATOM   1238  CE  MET A 155     -33.099   7.952 -24.567  1.00 71.22
ATOM   1239  N   GLY A 156     -32.191   3.367 -21.126  1.00 54.55
ATOM   1240  CA  GLY A 156     -31.573   2.909 -19.893  1.00 50.62
ATOM   1241  C   GLY A 156     -30.131   3.375 -19.885  1.00 47.98
ATOM   1242  O   GLY A 156     -29.654   3.873 -18.872  1.00 48.46
ATOM   1243  N   VAL A 157     -29.464   3.251 -21.034  1.00 44.84
ATOM   1244  CA  VAL A 157     -28.078   3.682 -21.206  1.00 42.08
ATOM   1245  C   VAL A 157     -27.958   5.187 -21.049  1.00 41.50
ATOM   1246  O   VAL A 157     -27.021   5.672 -20.427  1.00 41.60
ATOM   1247  CB  VAL A 157     -27.540   3.326 -22.600  1.00 41.38
ATOM   1248  CG1 VAL A 157     -26.193   3.992 -22.831  1.00 38.94
ATOM   1249  CG2 VAL A 157     -27.418   1.825 -22.752  1.00 40.89
ATOM   1250  N   ALA A 158     -28.883   5.923 -21.659  1.00 41.44
ATOM   1251  CA  ALA A 158     -28.881   7.382 -21.573  1.00 41.52
ATOM   1252  C   ALA A 158     -29.141   7.792 -20.123  1.00 41.19
ATOM   1253  O   ALA A 158     -28.522   8.718 -19.605  1.00 39.10
ATOM   1254  CB  ALA A 158     -29.943   7.963 -22.497  1.00 40.16
ATOM   1255  N   PHE A 159     -30.047   7.060 -19.482  1.00 43.19
ATOM   1256  CA  PHE A 159     -30.426   7.265 -18.085  1.00 45.18
ATOM   1257  C   PHE A 159     -29.209   7.034 -17.176  1.00 45.86
ATOM   1258  O   PHE A 159     -28.863   7.900 -16.363  1.00 47.45
ATOM   1259  CB  PHE A 159     -31.574   6.304 -17.723  1.00 45.41
ATOM   1260  CG  PHE A 159     -31.721   6.025 -16.246  1.00 46.51
ATOM   1261  CD1 PHE A 159     -32.569   6.795 -15.454  1.00 47.47
ATOM   1262  CD2 PHE A 159     -31.065   4.943 -15.659  1.00 46.84
ATOM   1263  CE1 PHE A 159     -32.771   6.490 -14.098  1.00 46.68
ATOM   1264  CE2 PHE A 159     -31.262   4.631 -14.308  1.00 46.45
ATOM   1265  CZ  PHE A 159     -32.119   5.406 -13.528  1.00 46.18
ATOM   1266  N   THR A 160     -28.553   5.882 -17.321  1.00 43.69
ATOM   1267  CA  THR A 160     -27.383   5.589 -16.502  1.00 41.47
ATOM   1268  C   THR A 160     -26.331   6.692 -16.597  1.00 41.85
ATOM   1269  O   THR A 160     -25.678   7.004 -15.602  1.00 42.50
ATOM   1270  CB  THR A 160     -26.727   4.268 -16.886  1.00 40.14
ATOM   1271  OG1 THR A 160     -26.181   4.364 -18.208  1.00 38.71
ATOM   1272  CG2 THR A 160     -27.732   3.140 -16.802  1.00 38.71
ATOM   1273  N   TRP A 161     -26.180   7.287 -17.781  1.00 41.03
ATOM   1274  CA  TRP A 161     -25.211   8.362 -17.980  1.00 40.97
ATOM   1275  C   TRP A 161     -25.594   9.650 -17.282  1.00 41.61
ATOM   1276  O   TRP A 161     -24.727  10.389 -16.811  1.00 41.78
ATOM   1277  CB  TRP A 161     -25.005   8.654 -19.459  1.00 41.01
ATOM   1278  CG  TRP A 161     -23.842   7.959 -19.997  1.00 40.12
ATOM   1279  CD1 TRP A 161     -23.795   6.674 -20.433  1.00 39.64
ATOM   1280  CD2 TRP A 161     -22.516   8.482 -20.120  1.00 40.80
ATOM   1281  NE1 TRP A 161     -22.518   6.355 -20.820  1.00 40.45
ATOM   1282  CE2 TRP A 161     -21.709   7.446 -20.638  1.00 40.92
ATOM   1283  CE3 TRP A 161     -21.928   9.725 -19.845  1.00 41.91
ATOM   1284  CZ2 TRP A 161     -20.335   7.613 -20.888  1.00 39.56
ATOM   1285  CZ3 TRP A 161     -20.554   9.892 -20.096  1.00 40.83
ATOM   1286  CH2 TRP A 161     -19.780   8.838 -20.612  1.00 39.46
ATOM   1287  N   VAL A 162     -26.889   9.938 -17.252  1.00 41.25
ATOM   1288  CA  VAL A 162     -27.375  11.149 -16.606  1.00 42.35
ATOM   1289  C   VAL A 162     -27.265  10.960 -15.086  1.00 43.12
ATOM   1290  O   VAL A 162     -26.843  11.867 -14.358  1.00 43.03
ATOM   1291  CB  VAL A 162     -28.835  11.453 -17.042  1.00 41.52
ATOM   1292  CG1 VAL A 162     -29.313  12.774 -16.475  1.00 41.47
ATOM   1293  CG2 VAL A 162     -28.917  11.492 -18.551  1.00 41.73
ATOM   1294  N   MET A 163     -27.568   9.745 -14.634  1.00 43.38
ATOM   1295  CA  MET A 163     -27.510   9.387 -13.219  1.00 43.99
ATOM   1296  C   MET A 163     -26.084   9.237 -12.689  1.00 44.30
ATOM   1297  O   MET A 163     -25.851   9.306 -11.483  1.00 44.26
ATOM   1298  CB  MET A 163     -28.290   8.094 -12.980  1.00 45.28
ATOM   1299  CG  MET A 163     -29.807   8.232 -13.087  1.00 46.07
ATOM   1300  SD  MET A 163     -30.467   9.382 -11.865  1.00 45.90
ATOM   1301  CE  MET A 163     -30.541  10.900 -12.854  1.00 47.00
ATOM   1302  N   ALA A 164     -25.139   8.979 -13.587  1.00 44.83
ATOM   1303  CA  ALA A 164     -23.737   8.838 -13.204  1.00 45.50
ATOM   1304  C   ALA A 164     -23.097  10.217 -13.228  1.00 45.80
ATOM   1305  O   ALA A 164     -22.239  10.538 -12.401  1.00 45.96
ATOM   1306  CB  ALA A 164     -23.025   7.910 -14.157  1.00 46.03
ATOM   1307  N   LEU A 165     -23.503  11.018 -14.208  1.00 46.61
ATOM   1308  CA  LEU A 165     -23.012  12.382 -14.343  1.00 47.23
ATOM   1309  C   LEU A 165     -23.629  13.223 -13.224  1.00 47.89
ATOM   1310  O   LEU A 165     -22.999  14.157 -12.730  1.00 48.60
ATOM   1311  CB  LEU A 165     -23.387  12.955 -15.710  1.00 47.15
ATOM   1312  CG  LEU A 165     -22.514  12.549 -16.896  1.00 46.58
ATOM   1313  CD1 LEU A 165     -23.260  12.782 -18.189  1.00 47.25
ATOM   1314  CD2 LEU A 165     -21.221  13.333 -16.873  1.00 45.85
ATOM   1315  N   ALA A 166     -24.857  12.880 -12.823  1.00 47.62
ATOM   1316  CA  ALA A 166     -25.548  13.584 -11.736  1.00 47.44
ATOM   1317  C   ALA A 166     -24.749  13.431 -10.424  1.00 47.94
ATOM   1318  O   ALA A 166     -24.785  14.298  -9.534  1.00 48.09
ATOM   1319  CB  ALA A 166     -26.955  13.029 -11.569  1.00 45.99
ATOM   1320  N   CYS A 167     -24.007  12.331 -10.328  1.00 46.94
ATOM   1321  CA  CYS A 167     -23.195  12.068  -9.157  1.00 45.02
ATOM   1322  C   CYS A 167     -21.779  12.576  -9.332  1.00 42.48
ATOM   1323  O   CYS A 167     -21.245  13.227  -8.449  1.00 43.07
ATOM   1324  CB  CYS A 167     -23.144  10.568  -8.858  1.00 46.98
ATOM   1325  SG  CYS A 167     -22.234  10.143  -7.336  1.00 49.01
ATOM   1326  N   ALA A 168     -21.181  12.308 -10.483  1.00 39.75
ATOM   1327  CA  ALA A 168     -19.799  12.701 -10.706  1.00 37.89
ATOM   1328  C   ALA A 168     -19.495  14.130 -11.135  1.00 36.56
ATOM   1329  O   ALA A 168     -18.421  14.638 -10.846  1.00 36.86
ATOM   1330  CB  ALA A 168     -19.138  11.717 -11.648  1.00 38.42
ATOM   1331  N   ALA A 169     -20.427  14.787 -11.810  1.00 36.15
ATOM   1332  CA  ALA A 169     -20.198  16.149 -12.287  1.00 35.37
ATOM   1333  C   ALA A 169     -20.160  17.282 -11.247  1.00 35.15
ATOM   1334  O   ALA A 169     -19.346  18.203 -11.362  1.00 35.61
ATOM   1335  CB  ALA A 169     -21.173  16.479 -13.403  1.00 35.17
ATOM   1336  N   PRO A 170     -21.055  17.253 -10.244  1.00 34.37
ATOM   1337  CA  PRO A 170     -21.074  18.297  -9.215  1.00 34.58
ATOM   1338  C   PRO A 170     -19.725  18.716  -8.589  1.00 36.23
ATOM   1339  O   PRO A 170     -19.450  19.899  -8.470  1.00 36.00
ATOM   1340  CB  PRO A 170     -22.035  17.724  -8.187  1.00 34.88
ATOM   1341  CG  PRO A 170     -23.049  17.021  -9.060  1.00 33.45
ATOM   1342  CD  PRO A 170     -22.194  16.326 -10.077  1.00 32.95
ATOM   1343  N   PRO A 171     -18.867  17.760  -8.193  1.00 38.22
ATOM   1344  CA  PRO A 171     -17.565  18.077  -7.590  1.00 41.34
ATOM   1345  C   PRO A 171     -16.632  18.892  -8.484  1.00 44.98
ATOM   1346  O   PRO A 171     -15.589  19.393  -8.026  1.00 46.59
ATOM   1347  CB  PRO A 171     -16.973  16.700  -7.322  1.00 40.27
ATOM   1348  CG  PRO A 171     -18.154  15.876  -7.074  1.00 40.67
ATOM   1349  CD  PRO A 171     -19.085  16.309  -8.166  1.00 40.00
ATOM   1350  N   LEU A 172     -16.984  18.981  -9.766  1.00 47.43
ATOM   1351  CA  LEU A 172     -16.207  19.737 -10.757  1.00 49.32
ATOM   1352  C   LEU A 172     -16.798  21.144 -10.905  1.00 50.05
ATOM   1353  O   LEU A 172     -16.177  22.055 -11.482  1.00 48.98
ATOM   1354  CB  LEU A 172     -16.288  19.048 -12.120  1.00 49.50
ATOM   1355  CG  LEU A 172     -15.799  17.615 -12.255  1.00 50.00
ATOM   1356  CD1 LEU A 172     -16.443  17.026 -13.485  1.00 51.02
ATOM   1357  CD2 LEU A 172     -14.285  17.554 -12.330  1.00 48.55
ATOM   1358  N   VAL A 173     -18.017  21.291 -10.392  1.00 49.36
ATOM   1359  CA  VAL A 173     -18.746  22.539 -10.471  1.00 48.31
ATOM   1360  C   VAL A 173     -18.811  23.361  -9.168  1.00 47.92
ATOM   1361  O   VAL A 173     -19.149  24.551  -9.199  1.00 48.79
ATOM   1362  CB  VAL A 173     -20.136  22.268 -11.104  1.00 47.90
ATOM   1363  CG1 VAL A 173     -21.147  23.366 -10.770  1.00 48.58
ATOM   1364  CG2 VAL A 173     -19.966  22.148 -12.611  1.00 45.31
ATOM   1365  N   GLY A 174     -18.436  22.757  -8.038  1.00 46.02
ATOM   1366  CA  GLY A 174     -18.459  23.498  -6.788  1.00 43.93
ATOM   1367  C   GLY A 174     -19.157  22.800  -5.640  1.00 43.45
ATOM   1368  O   GLY A 174     -19.107  23.269  -4.493  1.00 43.50
ATOM   1369  N   TRP A 175     -19.874  21.726  -5.958  1.00 41.44
ATOM   1370  CA  TRP A 175     -20.562  20.955  -4.941  1.00 40.37
ATOM   1371  C   TRP A 175     -19.572  19.848  -4.587  1.00 41.34
ATOM   1372  O   TRP A 175     -19.257  18.997  -5.435  1.00 41.69
ATOM   1373  CB  TRP A 175     -21.863  20.379  -5.491  1.00 36.83
ATOM   1374  CG  TRP A 175     -22.810  20.040  -4.409  1.00 35.08
ATOM   1375  CD1 TRP A 175     -22.718  20.417  -3.106  1.00 34.04
ATOM   1376  CD2 TRP A 175     -24.004  19.263  -4.522  1.00 35.16
ATOM   1377  NE1 TRP A 175     -23.779  19.931  -2.397  1.00 35.13
ATOM   1378  CE2 TRP A 175     -24.589  19.216  -3.242  1.00 35.98
ATOM   1379  CE3 TRP A 175     -24.637  18.598  -5.577  1.00 34.57
ATOM   1380  CZ2 TRP A 175     -25.786  18.530  -2.988  1.00 36.18
ATOM   1381  CZ3 TRP A 175     -25.823  17.918  -5.325  1.00 35.43
ATOM   1382  CH2 TRP A 175     -26.384  17.890  -4.040  1.00 35.24
ATOM   1383  N   SER A 176     -19.066  19.880  -3.349  1.00 39.84
ATOM   1384  CA  SER A 176     -18.050  18.929  -2.883  1.00 39.04
ATOM   1385  C   SER A 176     -16.837  19.063  -3.815  1.00 38.87
ATOM   1386  O   SER A 176     -16.747  20.028  -4.591  1.00 39.84
ATOM   1387  CB  SER A 176     -18.567  17.484  -2.875  1.00 37.55
ATOM   1388  OG  SER A 176     -17.608  16.600  -2.314  1.00 34.99
ATOM   1389  N   ARG A 177     -15.916  18.106  -3.768  1.00 37.00
ATOM   1390  CA  ARG A 177     -14.735  18.189  -4.622  1.00 35.74
ATOM   1391  C   ARG A 177     -13.911  16.922  -4.578  1.00 34.21
ATOM   1392  O   ARG A 177     -14.076  16.091  -3.684  1.00 34.56
ATOM   1393  CB  ARG A 177     -13.853  19.368  -4.202  1.00 35.74
ATOM   1394  CG  ARG A 177     -13.385  19.254  -2.774  1.00 36.53
ATOM   1395  CD  ARG A 177     -12.418  20.339  -2.380  1.00 38.34
ATOM   1396  NE  ARG A 177     -12.102  20.211  -0.961  1.00 40.20
ATOM   1397  CZ  ARG A 177     -11.260  20.994  -0.291  1.00 42.34
ATOM   1398  NH1 ARG A 177     -10.615  21.984  -0.911  1.00 42.27
ATOM   1399  NH2 ARG A 177     -11.111  20.818   1.019  1.00 42.45
ATOM   1400  N   TYR A 178     -13.033  16.777  -5.567  1.00 31.86
ATOM   1401  CA  TYR A 178     -12.161  15.623  -5.651  1.00 30.50
ATOM   1402  C   TYR A 178     -10.879  15.965  -4.911  1.00 31.63
ATOM   1403  O   TYR A 178     -10.179  16.931  -5.241  1.00 32.21
ATOM   1404  CB  TYR A 178     -11.916  15.232  -7.112  1.00 28.35
ATOM   1405  CG  TYR A 178     -13.113  14.565  -7.758  1.00 26.04
ATOM   1406  CD1 TYR A 178     -13.590  13.350  -7.281  1.00 25.82
ATOM   1407  CD2 TYR A 178     -13.808  15.177  -8.798  1.00 26.45
ATOM   1408  CE1 TYR A 178     -14.732  12.765  -7.808  1.00 25.90
ATOM   1409  CE2 TYR A 178     -14.959  14.596  -9.338  1.00 26.59
ATOM   1410  CZ  TYR A 178     -15.416  13.391  -8.831  1.00 27.07
ATOM   1411  OH  TYR A 178     -16.581  12.823  -9.310  1.00 27.88
ATOM   1412  N   ILE A 179     -10.596  15.167  -3.890  1.00 32.02
ATOM   1413  CA  ILE A 179      -9.440  15.365  -3.026  1.00 31.66
ATOM   1414  C   ILE A 179      -8.626  14.062  -2.996  1.00 31.69
ATOM   1415  O   ILE A 179      -9.199  12.983  -3.090  1.00 31.65
ATOM   1416  CB  ILE A 179      -9.966  15.760  -1.617  1.00 32.18
ATOM   1417  CG1 ILE A 179      -8.850  16.270  -0.716  1.00 33.49
ATOM   1418  CG2 ILE A 179     -10.742  14.602  -0.981  1.00 32.18
ATOM   1419  CD1 ILE A 179      -9.364  16.794   0.623  1.00 33.09
ATOM   1420  N   PRO A 180      -7.277  14.147  -2.936  1.00 32.77
ATOM   1421  CA  PRO A 180      -6.445  12.935  -2.907  1.00 32.33
ATOM   1422  C   PRO A 180      -6.655  12.112  -1.634  1.00 32.21
ATOM   1423  O   PRO A 180      -6.850  12.665  -0.545  1.00 30.36
ATOM   1424  CB  PRO A 180      -5.023  13.491  -2.995  1.00 32.10
ATOM   1425  CG  PRO A 180      -5.206  14.785  -3.706  1.00 32.42
ATOM   1426  CD  PRO A 180      -6.419  15.339  -3.016  1.00 33.45
ATOM   1427  N   GLU A 181      -6.570  10.790  -1.790  1.00 32.12
ATOM   1428  CA  GLU A 181      -6.794   9.864  -0.690  1.00 32.74
ATOM   1429  C   GLU A 181      -5.689   8.824  -0.437  1.00 32.90
ATOM   1430  O   GLU A 181      -4.982   8.387  -1.354  1.00 31.91
ATOM   1431  CB  GLU A 181      -8.116   9.123  -0.919  1.00 33.13
ATOM   1432  CG  GLU A 181      -9.290   9.980  -1.390  1.00 33.69
ATOM   1433  CD  GLU A 181     -10.549   9.156  -1.593  1.00 34.94
ATOM   1434  OE1 GLU A 181     -10.730   8.596  -2.706  1.00 37.57
ATOM   1435  OE2 GLU A 181     -11.339   9.044  -0.628  1.00 33.10
ATOM   1436  N   GLY A 182      -5.592   8.393   0.815  1.00 32.00
ATOM   1437  CA  GLY A 182      -4.616   7.391   1.161  1.00 33.02
ATOM   1438  C   GLY A 182      -3.198   7.868   0.987  1.00 34.21
ATOM   1439  O   GLY A 182      -2.797   8.821   1.647  1.00 34.46
ATOM   1440  N   MET A 183      -2.435   7.196   0.124  1.00 35.74
ATOM   1441  CA  MET A 183      -1.036   7.570  -0.132  1.00 37.26
ATOM   1442  C   MET A 183      -0.946   8.777  -1.049  1.00 37.05
ATOM   1443  O   MET A 183       0.144   9.141  -1.506  1.00 36.69
ATOM   1444  CB  MET A 183      -0.256   6.405  -0.738  1.00 37.82
ATOM   1445  CG  MET A 183      -0.178   5.201   0.166  1.00 39.59
ATOM   1446  SD  MET A 183       0.615   3.808  -0.619  1.00 39.94
ATOM   1447  CE  MET A 183       2.306   4.217  -0.352  1.00 42.90
ATOM   1448  N   GLN A 184      -2.117   9.368  -1.300  1.00 37.28
ATOM   1449  CA  GLN A 184      -2.325  10.554  -2.137  1.00 37.70
ATOM   1450  C   GLN A 184      -2.205  10.367  -3.663  1.00 37.46
ATOM   1451  O   GLN A 184      -1.932  11.330  -4.371  1.00 38.76
ATOM   1452  CB  GLN A 184      -1.442  11.735  -1.666  1.00 36.47
ATOM   1453  CG  GLN A 184      -1.495  12.067  -0.163  1.00 36.38
ATOM   1454  CD  GLN A 184      -2.896  12.324   0.373  1.00 36.94
ATOM   1455  OE1 GLN A 184      -3.515  13.348   0.081  1.00 38.28
ATOM   1456  NE2 GLN A 184      -3.390  11.402   1.188  1.00 36.28
ATOM   1457  N   CYS A 185      -2.471   9.163  -4.174  1.00 37.16
ATOM   1458  CA  CYS A 185      -2.376   8.896  -5.616  1.00 35.97
ATOM   1459  C   CYS A 185      -3.699   8.563  -6.309  1.00 36.18
ATOM   1460  O   CYS A 185      -3.753   8.352  -7.524  1.00 35.05
ATOM   1461  CB  CYS A 185      -1.320   7.837  -5.874  1.00 35.73
ATOM   1462  SG  CYS A 185       0.288   8.403  -5.290  1.00 37.15
ATOM   1463  N   SER A 186      -4.760   8.546  -5.506  1.00 36.67
ATOM   1464  CA  SER A 186      -6.132   8.319  -5.941  1.00 35.99
ATOM   1465  C   SER A 186      -6.864   9.593  -5.507  1.00 36.74
ATOM   1466  O   SER A 186      -6.389  10.315  -4.632  1.00 35.42
ATOM   1467  CB  SER A 186      -6.733   7.104  -5.231  1.00 34.72
ATOM   1468  OG  SER A 186      -8.149   7.198  -5.143  1.00 37.09
ATOM   1469  N   CYS A 187      -7.994   9.887  -6.140  1.00 38.33
ATOM   1470  CA  CYS A 187      -8.770  11.074  -5.797  1.00 39.64
ATOM   1471  C   CYS A 187     -10.250  10.759  -5.697  1.00 39.64
ATOM   1472  O   CYS A 187     -10.815  10.100  -6.564  1.00 42.09
ATOM   1473  CB  CYS A 187      -8.525  12.202  -6.811  1.00 40.50
ATOM   1474  SG  CYS A 187      -7.113  13.289  -6.397  1.00 43.71
ATOM   1475  N   GLY A 188     -10.876  11.233  -4.630  1.00 38.45
ATOM   1476  CA  GLY A 188     -12.281  10.971  -4.447  1.00 37.82
ATOM   1477  C   GLY A 188     -13.019  12.142  -3.859  1.00 38.91
ATOM   1478  O   GLY A 188     -12.505  13.262  -3.820  1.00 36.25
ATOM   1479  N   ILE A 189     -14.236  11.863  -3.392  1.00 41.01
ATOM   1480  CA  ILE A 189     -15.099  12.873  -2.804  1.00 44.30
ATOM   1481  C   ILE A 189     -14.597  13.281  -1.433  1.00 47.07
ATOM   1482  O   ILE A 189     -14.122  12.453  -0.663  1.00 49.48
ATOM   1483  CB  ILE A 189     -16.541  12.365  -2.702  1.00 43.22
ATOM   1484  CG1 ILE A 189     -17.074  12.035  -4.099  1.00 43.17
ATOM   1485  CG2 ILE A 189     -17.421  13.419  -2.060  1.00 43.58
ATOM   1486  CD1 ILE A 189     -17.136  13.228  -5.028  1.00 41.68
ATOM   1487  N   ASP A 190     -14.706  14.565  -1.125  1.00 49.25
ATOM   1488  CA  ASP A 190     -14.238  15.059   0.151  1.00 50.51
ATOM   1489  C   ASP A 190     -15.151  14.659   1.306  1.00 50.97
ATOM   1490  O   ASP A 190     -16.285  15.135   1.399  1.00 51.05
ATOM   1491  CB  ASP A 190     -14.089  16.571   0.089  1.00 52.49
ATOM   1492  CG  ASP A 190     -13.232  17.120   1.207  1.00 56.02
ATOM   1493  OD1 ASP A 190     -12.935  16.377   2.175  1.00 57.35
ATOM   1494  OD2 ASP A 190     -12.842  18.304   1.113  1.00 57.97
ATOM   1495  N   TYR A 191     -14.646  13.766   2.164  1.00 51.18
ATOM   1496  CA  TYR A 191     -15.358  13.277   3.360  1.00 50.33
ATOM   1497  C   TYR A 191     -14.537  13.698   4.576  1.00 49.62
ATOM   1498  O   TYR A 191     -15.000  13.642   5.710  1.00 48.43
ATOM   1499  CB  TYR A 191     -15.438  11.732   3.408  1.00 50.20
ATOM   1500  CG  TYR A 191     -15.414  10.980   2.082  1.00 51.00
ATOM   1501  CD1 TYR A 191     -16.542  10.923   1.261  1.00 50.62
ATOM   1502  CD2 TYR A 191     -14.267  10.295   1.667  1.00 50.88
ATOM   1503  CE1 TYR A 191     -16.530  10.205   0.062  1.00 50.72
ATOM   1504  CE2 TYR A 191     -14.247   9.573   0.472  1.00 50.91
ATOM   1505  CZ  TYR A 191     -15.381   9.534  -0.330  1.00 51.47
ATOM   1506  OH  TYR A 191     -15.366   8.844  -1.529  1.00 51.76
ATOM   1507  N   TYR A 192     -13.304  14.107   4.300  1.00 50.32
ATOM   1508  CA  TYR A 192     -12.321  14.496   5.302  1.00 52.63
ATOM   1509  C   TYR A 192     -12.493  15.847   6.023  1.00 54.38
ATOM   1510  O   TYR A 192     -12.290  15.938   7.244  1.00 55.16
ATOM   1511  CB  TYR A 192     -10.928  14.455   4.660  1.00 51.81
ATOM   1512  CG  TYR A 192     -10.579  13.163   3.946  1.00 51.17
ATOM   1513  CD1 TYR A 192      -9.858  12.162   4.597  1.00 51.01
ATOM   1514  CD2 TYR A 192     -10.944  12.953   2.616  1.00 50.66
ATOM   1515  CE1 TYR A 192      -9.507  10.992   3.947  1.00 50.18
ATOM   1516  CE2 TYR A 192     -10.601  11.783   1.957  1.00 49.81
ATOM   1517  CZ  TYR A 192      -9.880  10.807   2.629  1.00 50.79
ATOM   1518  OH  TYR A 192      -9.518   9.643   1.993  1.00 52.45
ATOM   1519  N   THR A 193     -12.843  16.886   5.265  1.00 54.58
ATOM   1520  CA  THR A 193     -12.984  18.238   5.795  1.00 54.88
ATOM   1521  C   THR A 193     -14.404  18.791   5.691  1.00 56.86
ATOM   1522  O   THR A 193     -15.126  18.481   4.743  1.00 57.34
ATOM   1523  CB  THR A 193     -12.045  19.185   5.021  1.00 55.05
ATOM   1524  OG1 THR A 193     -12.588  19.432   3.719  1.00 53.33
ATOM   1525  CG2 THR A 193     -10.657  18.548   4.848  1.00 53.18
ATOM   1526  N   PRO A 194     -14.816  19.644   6.651  1.00 59.01
ATOM   1527  CA  PRO A 194     -16.166  20.225   6.621  1.00 60.26
ATOM   1528  C   PRO A 194     -16.335  21.151   5.421  1.00 61.42
ATOM   1529  O   PRO A 194     -17.370  21.092   4.736  1.00 61.12
ATOM   1530  CB  PRO A 194     -16.235  21.025   7.930  1.00 59.86
ATOM   1531  CG  PRO A 194     -15.272  20.324   8.825  1.00 60.81
ATOM   1532  CD  PRO A 194     -14.114  20.041   7.884  1.00 60.51
ATOM   1533  N   HIS A 195     -15.294  21.967   5.169  1.00 62.05
ATOM   1534  CA  HIS A 195     -15.232  22.968   4.079  1.00 62.39
ATOM   1535  C   HIS A 195     -16.640  23.429   3.738  1.00 63.90
ATOM   1536  O   HIS A 195     -17.145  23.208   2.635  1.00 62.34
ATOM   1537  CB  HIS A 195     -14.519  22.414   2.831  1.00 60.44
ATOM   1538  CG  HIS A 195     -13.780  23.449   2.023  1.00 57.53
ATOM   1539  ND1 HIS A 195     -13.917  23.565   0.656  1.00 55.26
ATOM   1540  CD2 HIS A 195     -12.845  24.364   2.380  1.00 57.56
ATOM   1541  CE1 HIS A 195     -13.097  24.499   0.205  1.00 54.27
ATOM   1542  NE2 HIS A 195     -12.435  25.001   1.230  1.00 55.18
ATOM   1543  N   GLU A 196     -17.278  24.011   4.749  1.00 66.51
ATOM   1544  CA  GLU A 196     -18.644  24.500   4.671  1.00 68.81
ATOM   1545  C   GLU A 196     -18.966  25.329   3.436  1.00 69.68
ATOM   1546  O   GLU A 196     -20.142  25.482   3.091  1.00 70.11
ATOM   1547  CB  GLU A 196     -18.972  25.300   5.934  1.00 69.92
ATOM   1548  CG  GLU A 196     -17.933  26.370   6.278  1.00 72.05
ATOM   1549  CD  GLU A 196     -18.365  27.242   7.439  1.00 73.59
ATOM   1550  OE1 GLU A 196     -18.421  28.483   7.264  1.00 73.91
ATOM   1551  OE2 GLU A 196     -18.658  26.684   8.523  1.00 74.47
ATOM   1552  N   GLU A 197     -17.934  25.816   2.744  1.00 70.46
ATOM   1553  CA  GLU A 197     -18.146  26.656   1.564  1.00 71.64
ATOM   1554  C   GLU A 197     -17.787  26.101   0.167  1.00 70.30
ATOM   1555  O   GLU A 197     -17.084  26.734  -0.622  1.00 67.22
ATOM   1556  CB  GLU A 197     -17.593  28.073   1.824  1.00 75.28
ATOM   1557  CG  GLU A 197     -18.345  28.789   3.000  1.00 78.65
ATOM   1558  CD  GLU A 197     -17.857  30.204   3.326  1.00 79.63
ATOM   1559  OE1 GLU A 197     -18.154  31.138   2.543  1.00 79.60
ATOM   1560  OE2 GLU A 197     -17.214  30.386   4.389  1.00 80.17
ATOM   1561  N   THR A 198     -18.333  24.906  -0.084  1.00 70.75
ATOM   1562  CA  THR A 198     -18.282  24.084  -1.316  1.00 70.31
ATOM   1563  C   THR A 198     -19.352  23.007  -1.075  1.00 69.68
ATOM   1564  O   THR A 198     -19.512  22.078  -1.872  1.00 69.57
ATOM   1565  CB  THR A 198     -16.944  23.308  -1.576  1.00 70.93
ATOM   1566  OG1 THR A 198     -16.568  22.547  -0.421  1.00 72.10
ATOM   1567  CG2 THR A 198     -15.833  24.232  -2.006  1.00 71.96
ATOM   1568  N   ASN A 199     -20.019  23.125   0.078  1.00 68.95
ATOM   1569  CA  ASN A 199     -21.084  22.234   0.537  1.00 67.97
ATOM   1570  C   ASN A 199     -20.705  20.762   0.592  1.00 67.25
ATOM   1571  O   ASN A 199     -21.339  19.914  -0.040  1.00 66.79
ATOM   1572  CB  ASN A 199     -22.358  22.448  -0.286  1.00 69.11
ATOM   1573  CG  ASN A 199     -22.974  23.829  -0.067  1.00 68.96
ATOM   1574  OD1 ASN A 199     -23.664  24.069   0.936  1.00 68.67
ATOM   1575  ND2 ASN A 199     -22.732  24.739  -1.009  1.00 66.57
ATOM   1576  N   ASN A 200     -19.668  20.473   1.375  1.00 66.84
ATOM   1577  CA  ASN A 200     -19.177  19.113   1.538  1.00 65.68
ATOM   1578  C   ASN A 200     -20.070  18.264   2.431  1.00 66.81
ATOM   1579  O   ASN A 200     -20.517  17.192   2.007  1.00 66.62
ATOM   1580  CB  ASN A 200     -17.733  19.110   2.048  1.00 62.26
ATOM   1581  CG  ASN A 200     -16.738  19.191   0.927  1.00 57.86
ATOM   1582  OD1 ASN A 200     -16.049  20.178   0.771  1.00 54.31
ATOM   1583  ND2 ASN A 200     -16.691  18.153   0.109  1.00 58.50
ATOM   1584  N   GLU A 201     -20.344  18.738   3.650  1.00 67.44
ATOM   1585  CA  GLU A 201     -21.205  17.994   4.572  1.00 67.65
ATOM   1586  C   GLU A 201     -22.548  17.671   3.856  1.00 66.51
ATOM   1587  O   GLU A 201     -23.181  16.640   4.116  1.00 66.71
ATOM   1588  CB  GLU A 201     -21.398  18.793   5.886  1.00 69.10
ATOM   1589  CG  GLU A 201     -22.391  18.196   6.944  1.00 70.29
ATOM   1590  CD  GLU A 201     -21.819  17.090   7.857  1.00 70.17
ATOM   1591  OE1 GLU A 201     -20.629  16.709   7.712  1.00 69.78
ATOM   1592  OE2 GLU A 201     -22.583  16.610   8.736  1.00 68.45
ATOM   1593  N   SER A 202     -22.890  18.489   2.859  1.00 64.12
ATOM   1594  CA  SER A 202     -24.120  18.337   2.074  1.00 60.49
ATOM   1595  C   SER A 202     -24.111  17.214   1.010  1.00 57.82
ATOM   1596  O   SER A 202     -24.908  16.278   1.079  1.00 56.84
ATOM   1597  CB  SER A 202     -24.456  19.682   1.425  1.00 60.02
ATOM   1598  OG  SER A 202     -25.562  19.572   0.560  1.00 60.60
ATOM   1599  N   PHE A 203     -23.211  17.331   0.033  1.00 55.36
ATOM   1600  CA  PHE A 203     -23.057  16.371  -1.070  1.00 52.57
ATOM   1601  C   PHE A 203     -22.933  14.903  -0.674  1.00 50.83
ATOM   1602  O   PHE A 203     -23.556  14.045  -1.285  1.00 49.41
ATOM   1603  CB  PHE A 203     -21.839  16.758  -1.910  1.00 52.39
ATOM   1604  CG  PHE A 203     -21.588  15.859  -3.093  1.00 50.98
ATOM   1605  CD1 PHE A 203     -20.964  14.631  -2.935  1.00 50.44
ATOM   1606  CD2 PHE A 203     -21.943  16.263  -4.372  1.00 51.08
ATOM   1607  CE1 PHE A 203     -20.696  13.824  -4.032  1.00 49.89
ATOM   1608  CE2 PHE A 203     -21.676  15.459  -5.471  1.00 50.36
ATOM   1609  CZ  PHE A 203     -21.052  14.238  -5.299  1.00 49.54
ATOM   1610  N   VAL A 204     -22.062  14.615   0.286  1.00 50.05
ATOM   1611  CA  VAL A 204     -21.842  13.249   0.759  1.00 50.03
ATOM   1612  C   VAL A 204     -23.140  12.570   1.223  1.00 51.56
ATOM   1613  O   VAL A 204     -23.280  11.349   1.115  1.00 52.01
ATOM   1614  CB  VAL A 204     -20.825  13.212   1.926  1.00 48.64
ATOM   1615  CG1 VAL A 204     -20.455  11.785   2.258  1.00 48.29
ATOM   1616  CG2 VAL A 204     -19.593  14.000   1.586  1.00 48.38
ATOM   1617  N   ILE A 205     -24.062  13.344   1.796  1.00 52.38
ATOM   1618  CA  ILE A 205     -25.334  12.787   2.246  1.00 52.33
ATOM   1619  C   ILE A 205     -26.151  12.511   0.999  1.00 52.70
ATOM   1620  O   ILE A 205     -26.770  11.457   0.881  1.00 53.24
ATOM   1621  CB  ILE A 205     -26.108  13.760   3.154  1.00 52.55
ATOM   1622  CG1 ILE A 205     -25.353  13.950   4.470  1.00 52.76
ATOM   1623  CG2 ILE A 205     -27.515  13.231   3.414  1.00 51.53
ATOM   1624  CD1 ILE A 205     -25.982  14.957   5.405  1.00 52.47
ATOM   1625  N   TYR A 206     -26.134  13.469   0.073  1.00 52.48
ATOM   1626  CA  TYR A 206     -26.842  13.350  -1.197  1.00 52.57
ATOM   1627  C   TYR A 206     -26.361  12.102  -1.967  1.00 51.96
ATOM   1628  O   TYR A 206     -27.153  11.201  -2.262  1.00 51.87
ATOM   1629  CB  TYR A 206     -26.633  14.636  -2.019  1.00 54.36
ATOM   1630  CG  TYR A 206     -26.637  14.481  -3.540  1.00 56.04
ATOM   1631  CD1 TYR A 206     -25.467  14.680  -4.280  1.00 56.56
ATOM   1632  CD2 TYR A 206     -27.814  14.189  -4.239  1.00 56.22
ATOM   1633  CE1 TYR A 206     -25.470  14.601  -5.673  1.00 57.82
ATOM   1634  CE2 TYR A 206     -27.827  14.106  -5.633  1.00 56.67
ATOM   1635  CZ  TYR A 206     -26.652  14.316  -6.340  1.00 57.92
ATOM   1636  OH  TYR A 206     -26.656  14.258  -7.712  1.00 58.45
ATOM   1637  N   MET A 207     -25.057  12.025  -2.233  1.00 50.54
ATOM   1638  CA  MET A 207     -24.478  10.901  -2.964  1.00 48.45
ATOM   1639  C   MET A 207     -24.782   9.535  -2.353  1.00 46.81
ATOM   1640  O   MET A 207     -25.155   8.609  -3.064  1.00 47.96
ATOM   1641  CB  MET A 207     -22.969  11.076  -3.095  1.00 49.40
ATOM   1642  CG  MET A 207     -22.281   9.909  -3.781  1.00 51.02
ATOM   1643  SD  MET A 207     -20.513   9.847  -3.442  1.00 53.27
ATOM   1644  CE  MET A 207     -20.511   9.591  -1.682  1.00 50.87
ATOM   1645  N   PHE A 208     -24.600   9.397  -1.047  1.00 44.47
ATOM   1646  CA  PHE A 208     -24.879   8.130  -0.388  1.00 43.28
ATOM   1647  C   PHE A 208     -26.357   7.765  -0.392  1.00 43.06
ATOM   1648  O   PHE A 208     -26.704   6.588  -0.355  1.00 44.18
ATOM   1649  CB  PHE A 208     -24.373   8.141   1.049  1.00 42.63
ATOM   1650  CG  PHE A 208     -22.982   7.616   1.203  1.00 42.31
ATOM   1651  CD1 PHE A 208     -22.739   6.247   1.172  1.00 41.78
ATOM   1652  CD2 PHE A 208     -21.910   8.488   1.391  1.00 41.88
ATOM   1653  CE1 PHE A 208     -21.448   5.754   1.328  1.00 40.24
ATOM   1654  CE2 PHE A 208     -20.617   8.002   1.546  1.00 39.02
ATOM   1655  CZ  PHE A 208     -20.388   6.636   1.514  1.00 39.62
ATOM   1656  N   VAL A 209     -27.227   8.766  -0.398  1.00 42.55
ATOM   1657  CA  VAL A 209     -28.662   8.509  -0.402  1.00 43.42
ATOM   1658  C   VAL A 209     -29.140   8.194  -1.822  1.00 43.52
ATOM   1659  O   VAL A 209     -29.597   7.083  -2.106  1.00 43.23
ATOM   1660  CB  VAL A 209     -29.463   9.719   0.180  1.00 43.49
ATOM   1661  CG1 VAL A 209     -30.955   9.525  -0.039  1.00 44.01
ATOM   1662  CG2 VAL A 209     -29.189   9.874   1.670  1.00 42.52
ATOM   1663  N   VAL A 210     -28.973   9.170  -2.713  1.00 43.47
ATOM   1664  CA  VAL A 210     -29.393   9.067  -4.114  1.00 42.92
ATOM   1665  C   VAL A 210     -28.544   8.144  -4.987  1.00 43.36
ATOM   1666  O   VAL A 210     -29.064   7.508  -5.904  1.00 43.95
ATOM   1667  CB  VAL A 210     -29.418  10.478  -4.790  1.00 41.80
ATOM   1668  CG1 VAL A 210     -29.815  10.369  -6.271  1.00 37.86
ATOM   1669  CG2 VAL A 210     -30.349  11.425  -4.020  1.00 38.14
ATOM   1670  N   HIS A 211     -27.251   8.060  -4.692  1.00 43.15
ATOM   1671  CA  HIS A 211     -26.348   7.251  -5.499  1.00 44.49
ATOM   1672  C   HIS A 211     -25.712   6.020  -4.846  1.00 44.35
ATOM   1673  O   HIS A 211     -24.565   5.674  -5.154  1.00 44.26
ATOM   1674  CB  HIS A 211     -25.265   8.154  -6.113  1.00 46.07
ATOM   1675  CG  HIS A 211     -25.806   9.209  -7.030  1.00 45.84
ATOM   1676  ND1 HIS A 211     -25.792   9.084  -8.403  1.00 45.95
ATOM   1677  CD2 HIS A 211     -26.394  10.399  -6.766  1.00 46.81
ATOM   1678  CE1 HIS A 211     -26.352  10.151  -8.944  1.00 47.28
ATOM   1679  NE2 HIS A 211     -26.725  10.964  -7.972  1.00 48.06
ATOM   1680  N   PHE A 212     -26.480   5.314  -4.022  1.00 44.26
ATOM   1681  CA  PHE A 212     -25.974   4.121  -3.348  1.00 44.30
ATOM   1682  C   PHE A 212     -27.083   3.306  -2.663  1.00 43.64
ATOM   1683  O   PHE A 212     -27.406   2.191  -3.080  1.00 43.15
ATOM   1684  CB  PHE A 212     -24.895   4.519  -2.334  1.00 44.65
ATOM   1685  CG  PHE A 212     -24.286   3.359  -1.602  1.00 47.35
ATOM   1686  CD1 PHE A 212     -23.689   2.306  -2.303  1.00 48.10
ATOM   1687  CD2 PHE A 212     -24.293   3.321  -0.205  1.00 48.01
ATOM   1688  CE1 PHE A 212     -23.104   1.231  -1.623  1.00 49.07
ATOM   1689  CE2 PHE A 212     -23.714   2.255   0.486  1.00 48.13
ATOM   1690  CZ  PHE A 212     -23.117   1.207  -0.224  1.00 48.82
ATOM   1691  N   ILE A 213     -27.649   3.862  -1.601  1.00 42.79
ATOM   1692  CA  ILE A 213     -28.715   3.199  -0.870  1.00 42.26
ATOM   1693  C   ILE A 213     -29.912   2.928  -1.773  1.00 41.90
ATOM   1694  O   ILE A 213     -30.329   1.777  -1.929  1.00 40.81
ATOM   1695  CB  ILE A 213     -29.167   4.059   0.313  1.00 42.96
ATOM   1696  CG1 ILE A 213     -28.008   4.214   1.305  1.00 42.79
ATOM   1697  CG2 ILE A 213     -30.420   3.459   0.961  1.00 42.86
ATOM   1698  CD1 ILE A 213     -28.262   5.238   2.404  1.00 42.77
ATOM   1699  N   ILE A 214     -30.427   3.987  -2.398  1.00 41.57
ATOM   1700  CA  ILE A 214     -31.583   3.868  -3.276  1.00 41.64
ATOM   1701  C   ILE A 214     -31.425   2.824  -4.378  1.00 41.98
ATOM   1702  O   ILE A 214     -32.149   1.828  -4.378  1.00 43.24
ATOM   1703  CB  ILE A 214     -32.012   5.222  -3.868  1.00 40.69
ATOM   1704  CG1 ILE A 214     -32.514   6.138  -2.757  1.00 40.26
ATOM   1705  CG2 ILE A 214     -33.131   5.022  -4.872  1.00 40.74
ATOM   1706  CD1 ILE A 214     -33.017   7.474  -3.256  1.00 39.32
ATOM   1707  N   PRO A 215     -30.483   3.021  -5.324  1.00 41.41
ATOM   1708  CA  PRO A 215     -30.340   2.008  -6.374  1.00 41.28
ATOM   1709  C   PRO A 215     -30.209   0.609  -5.774  1.00 42.91
ATOM   1710  O   PRO A 215     -30.782  -0.345  -6.293  1.00 43.16
ATOM   1711  CB  PRO A 215     -29.070   2.441  -7.084  1.00 40.24
ATOM   1712  CG  PRO A 215     -29.119   3.924  -6.956  1.00 40.31
ATOM   1713  CD  PRO A 215     -29.512   4.112  -5.518  1.00 40.74
ATOM   1714  N   LEU A 216     -29.525   0.513  -4.633  1.00 44.12
ATOM   1715  CA  LEU A 216     -29.343  -0.763  -3.946  1.00 45.80
ATOM   1716  C   LEU A 216     -30.629  -1.274  -3.331  1.00 47.06
ATOM   1717  O   LEU A 216     -30.811  -2.477  -3.162  1.00 48.43
ATOM   1718  CB  LEU A 216     -28.281  -0.651  -2.873  1.00 45.65
ATOM   1719  CG  LEU A 216     -26.884  -0.743  -3.455  1.00 46.75
ATOM   1720  CD1 LEU A 216     -25.899  -0.540  -2.341  1.00 48.66
ATOM   1721  CD2 LEU A 216     -26.680  -2.093  -4.119  1.00 46.54
ATOM   1722  N   ILE A 217     -31.498  -0.352  -2.943  1.00 47.71
ATOM   1723  CA  ILE A 217     -32.789  -0.716  -2.380  1.00 48.58
ATOM   1724  C   ILE A 217     -33.604  -1.351  -3.525  1.00 48.50
ATOM   1725  O   ILE A 217     -34.067  -2.496  -3.424  1.00 48.00
ATOM   1726  CB  ILE A 217     -33.482   0.552  -1.770  1.00 49.24
ATOM   1727  CG1 ILE A 217     -33.503   0.457  -0.245  1.00 49.11
ATOM   1728  CG2 ILE A 217     -34.883   0.759  -2.329  1.00 49.87
ATOM   1729  CD1 ILE A 217     -32.137   0.229   0.368  1.00 51.08
ATOM   1730  N   VAL A 218     -33.667  -0.634  -4.645  1.00 47.40
ATOM   1731  CA  VAL A 218     -34.379  -1.071  -5.831  1.00 46.87
ATOM   1732  C   VAL A 218     -33.822  -2.396  -6.346  1.00 49.32
ATOM   1733  O   VAL A 218     -34.576  -3.347  -6.540  1.00 50.44
ATOM   1734  CB  VAL A 218     -34.306   0.013  -6.932  1.00 44.98
ATOM   1735  CG1 VAL A 218     -34.801  -0.515  -8.267  1.00 43.26
ATOM   1736  CG2 VAL A 218     -35.133   1.210  -6.522  1.00 42.90
ATOM   1737  N   ILE A 219     -32.506  -2.466  -6.539  1.00 51.21
ATOM   1738  CA  ILE A 219     -31.868  -3.687  -7.036  1.00 53.48
ATOM   1739  C   ILE A 219     -32.120  -4.865  -6.096  1.00 55.86
ATOM   1740  O   ILE A 219     -32.203  -6.023  -6.526  1.00 57.84
ATOM   1741  CB  ILE A 219     -30.336  -3.511  -7.214  1.00 52.59
ATOM   1742  CG1 ILE A 219     -30.034  -2.393  -8.209  1.00 52.47
ATOM   1743  CG2 ILE A 219     -29.722  -4.794  -7.752  1.00 53.28
ATOM   1744  CD1 ILE A 219     -28.557  -2.108  -8.373  1.00 50.56
ATOM   1745  N   PHE A 220     -32.243  -4.562  -4.810  1.00 57.04
ATOM   1746  CA  PHE A 220     -32.488  -5.589  -3.826  1.00 58.87
ATOM   1747  C   PHE A 220     -33.940  -5.968  -3.696  1.00 60.25
ATOM   1748  O   PHE A 220     -34.253  -7.097  -3.319  1.00 60.48
ATOM   1749  CB  PHE A 220     -31.916  -5.183  -2.486  1.00 60.05
ATOM   1750  CG  PHE A 220     -30.557  -5.731  -2.248  1.00 62.00
ATOM   1751  CD1 PHE A 220     -29.443  -4.905  -2.280  1.00 62.44
ATOM   1752  CD2 PHE A 220     -30.384  -7.094  -2.023  1.00 62.83
ATOM   1753  CE1 PHE A 220     -28.172  -5.425  -2.094  1.00 62.87
ATOM   1754  CE2 PHE A 220     -29.119  -7.627  -1.836  1.00 63.11
ATOM   1755  CZ  PHE A 220     -28.009  -6.791  -1.872  1.00 63.60
ATOM   1756  N   PHE A 221     -34.833  -5.021  -3.967  1.00 61.85
ATOM   1757  CA  PHE A 221     -36.250  -5.324  -3.897  1.00 63.09
ATOM   1758  C   PHE A 221     -36.690  -6.046  -5.168  1.00 62.89
ATOM   1759  O   PHE A 221     -37.614  -6.851  -5.133  1.00 63.65
ATOM   1760  CB  PHE A 221     -37.104  -4.081  -3.667  1.00 64.55
ATOM   1761  CG  PHE A 221     -38.550  -4.401  -3.462  1.00 67.05
ATOM   1762  CD1 PHE A 221     -38.923  -5.406  -2.565  1.00 67.28
ATOM   1763  CD2 PHE A 221     -39.536  -3.766  -4.212  1.00 67.98
ATOM   1764  CE1 PHE A 221     -40.255  -5.781  -2.421  1.00 67.52
ATOM   1765  CE2 PHE A 221     -40.877  -4.131  -4.078  1.00 68.63
ATOM   1766  CZ  PHE A 221     -41.237  -5.144  -3.179  1.00 68.67
ATOM   1767  N   CYS A 222     -36.047  -5.737  -6.292  1.00 63.25
ATOM   1768  CA  CYS A 222     -36.365  -6.414  -7.547  1.00 63.43
ATOM   1769  C   CYS A 222     -35.905  -7.854  -7.387  1.00 64.66
ATOM   1770  O   CYS A 222     -36.635  -8.784  -7.716  1.00 65.19
ATOM   1771  CB  CYS A 222     -35.636  -5.785  -8.738  1.00 62.27
ATOM   1772  SG  CYS A 222     -35.611  -6.858 -10.223  1.00 56.87
ATOM   1773  N   TYR A 223     -34.691  -8.032  -6.873  1.00 65.57
ATOM   1774  CA  TYR A 223     -34.153  -9.361  -6.655  1.00 67.20
ATOM   1775  C   TYR A 223     -35.050 -10.124  -5.681  1.00 69.83
ATOM   1776  O   TYR A 223     -35.116 -11.349  -5.725  1.00 70.16
ATOM   1777  CB  TYR A 223     -32.725  -9.287  -6.115  1.00 65.99
ATOM   1778  CG  TYR A 223     -32.200 -10.630  -5.669  1.00 65.04
ATOM   1779  CD1 TYR A 223     -31.890 -11.619  -6.595  1.00 65.27
ATOM   1780  CD2 TYR A 223     -32.054 -10.932  -4.317  1.00 65.77
ATOM   1781  CE1 TYR A 223     -31.448 -12.886  -6.187  1.00 64.78
ATOM   1782  CE2 TYR A 223     -31.611 -12.194  -3.895  1.00 64.96
ATOM   1783  CZ  TYR A 223     -31.311 -13.169  -4.837  1.00 64.61
ATOM   1784  OH  TYR A 223     -30.872 -14.417  -4.434  1.00 63.82
ATOM   1785  N   GLY A 224     -35.731  -9.392  -4.800  1.00 73.00
ATOM   1786  CA  GLY A 224     -36.632 -10.007  -3.838  1.00 75.87
ATOM   1787  C   GLY A 224     -37.900 -10.477  -4.526  1.00 78.22
ATOM   1788  O   GLY A 224     -38.583 -11.383  -4.048  1.00 77.88
ATOM   1789  N   GLN A 225     -38.220  -9.830  -5.645  1.00 80.96
ATOM   1790  CA  GLN A 225     -39.391 -10.166  -6.448  1.00 84.22
ATOM   1791  C   GLN A 225     -39.070 -11.359  -7.347  1.00 86.87
ATOM   1792  O   GLN A 225     -39.896 -12.258  -7.516  1.00 87.14
ATOM   1793  CB  GLN A 225     -39.828  -8.963  -7.295  1.00 83.45
ATOM   1794  CG  GLN A 225     -40.349  -7.800  -6.481  1.00 82.89
ATOM   1795  CD  GLN A 225     -41.351  -8.250  -5.433  1.00 83.54
ATOM   1796  OE1 GLN A 225     -40.985  -8.537  -4.290  1.00 83.14
ATOM   1797  NE2 GLN A 225     -42.620  -8.335  -5.823  1.00 83.86
ATOM   1798  N   LEU A 226     -37.859 -11.363  -7.909  1.00 90.04
ATOM   1799  CA  LEU A 226     -37.408 -12.451  -8.777  1.00 92.88
ATOM   1800  C   LEU A 226     -37.059 -13.701  -7.979  1.00 95.23
ATOM   1801  O   LEU A 226     -36.093 -14.393  -8.300  1.00 95.35
ATOM   1802  CB  LEU A 226     -36.191 -12.046  -9.620  1.00 92.74
ATOM   1803  CG  LEU A 226     -36.340 -11.006 -10.731  1.00 92.83
ATOM   1804  CD1 LEU A 226     -35.159 -11.142 -11.679  1.00 92.54
ATOM   1805  CD2 LEU A 226     -37.634 -11.211 -11.487  1.00 92.66
ATOM   1806  N   VAL A 227     -37.790 -13.920  -6.886  1.00 97.91
ATOM   1807  CA  VAL A 227     -37.621 -15.100  -6.041  1.00100.68
ATOM   1808  C   VAL A 227     -38.928 -15.886  -6.176  1.00102.93
ATOM   1809  O   VAL A 227     -39.024 -17.035  -5.748  1.00103.58
ATOM   1810  CB  VAL A 227     -37.332 -14.742  -4.551  1.00100.65
ATOM   1811  CG1 VAL A 227     -37.156 -16.011  -3.722  1.00100.79
ATOM   1812  CG2 VAL A 227     -36.062 -13.914  -4.444  1.00100.82
ATOM   1813  N   PHE A 228     -39.927 -15.245  -6.790  1.00105.66
ATOM   1814  CA  PHE A 228     -41.232 -15.854  -7.060  1.00108.32
ATOM   1815  C   PHE A 228     -40.967 -17.008  -8.038  1.00109.72
ATOM   1816  O   PHE A 228     -41.560 -18.090  -7.925  1.00109.92
ATOM   1817  CB  PHE A 228     -42.174 -14.797  -7.681  1.00108.82
ATOM   1818  CG  PHE A 228     -43.364 -15.370  -8.442  1.00109.74
ATOM   1819  CD1 PHE A 228     -44.117 -16.433  -7.926  1.00109.66
ATOM   1820  CD2 PHE A 228     -43.733 -14.826  -9.677  1.00109.41
ATOM   1821  CE1 PHE A 228     -45.218 -16.942  -8.630  1.00109.26
ATOM   1822  CE2 PHE A 228     -44.830 -15.327 -10.385  1.00109.19
ATOM   1823  CZ  PHE A 228     -45.575 -16.387  -9.861  1.00109.10
ATOM   1824  N   THR A 229     -40.032 -16.769  -8.960  1.00110.96
ATOM   1825  CA  THR A 229     -39.630 -17.748  -9.968  1.00112.33
ATOM   1826  C   THR A 229     -38.166 -18.198  -9.773  1.00112.71
ATOM   1827  O   THR A 229     -37.910 -19.205  -9.106  1.00112.37
ATOM   1828  CB  THR A 229     -39.845 -17.201 -11.417  1.00112.86
ATOM   1829  OG1 THR A 229     -39.276 -15.890 -11.530  1.00113.53
ATOM   1830  CG2 THR A 229     -41.337 -17.134 -11.769  1.00112.79
ATOM   1831  N   VAL A 230     -37.217 -17.441 -10.330  1.00113.28
ATOM   1832  CA  VAL A 230     -35.787 -17.760 -10.227  1.00114.03
ATOM   1833  C   VAL A 230     -35.243 -17.524  -8.806  1.00115.49
ATOM   1834  O   VAL A 230     -34.705 -16.448  -8.514  1.00115.82
ATOM   1835  CB  VAL A 230     -34.939 -16.917 -11.232  1.00113.01
ATOM   1836  CG1 VAL A 230     -33.501 -17.430 -11.283  1.00111.70
ATOM   1837  CG2 VAL A 230     -35.568 -16.940 -12.618  1.00112.59
ATOM   1838  N   LYS A 231     -35.361 -18.541  -7.944  1.00116.60
ATOM   1839  CA  LYS A 231     -34.894 -18.473  -6.548  1.00117.30
ATOM   1840  C   LYS A 231     -33.408 -18.100  -6.452  1.00118.54
ATOM   1841  O   LYS A 231     -33.074 -16.939  -6.188  1.00119.32
ATOM   1842  CB  LYS A 231     -35.114 -19.815  -5.829  1.00116.03
ATOM   1843  CG  LYS A 231     -36.502 -20.415  -5.965  1.00114.38
ATOM   1844  CD  LYS A 231     -36.463 -21.912  -5.664  1.00112.83
ATOM   1845  CE  LYS A 231     -37.748 -22.606  -6.095  1.00111.68
ATOM   1846  NZ  LYS A 231     -37.666 -24.084  -5.943  1.00110.17
ATOM   1847  N   GLU A 232     -32.533 -19.091  -6.665  1.00119.05
ATOM   1848  CA  GLU A 232     -31.071 -18.921  -6.606  1.00119.00
ATOM   1849  C   GLU A 232     -30.377 -19.818  -7.631  1.00119.13
ATOM   1850  O   GLU A 232     -29.183 -19.653  -7.907  1.00118.80
ATOM   1851  CB  GLU A 232     -30.537 -19.301  -5.215  1.00118.61
ATOM   1852  CG  GLU A 232     -31.006 -18.417  -4.063  1.00118.85
ATOM   1853  CD  GLU A 232     -30.765 -19.046  -2.698  1.00118.59
ATOM   1854  OE1 GLU A 232     -29.610 -19.431  -2.408  1.00118.29
ATOM   1855  OE2 GLU A 232     -31.735 -19.150  -1.915  1.00118.18
ATOM   1856  N   ALA A 233     -31.133 -20.779  -8.167  1.00119.62
ATOM   1857  CA  ALA A 233     -30.630 -21.755  -9.139  1.00119.87
ATOM   1858  C   ALA A 233     -30.580 -21.274 -10.589  1.00119.91
ATOM   1859  O   ALA A 233     -31.115 -20.209 -10.924  1.00120.45
ATOM   1860  CB  ALA A 233     -31.450 -23.047  -9.043  1.00118.96
ATOM   1861  N   ALA A 234     -29.917 -22.072 -11.430  1.00119.61
ATOM   1862  CA  ALA A 234     -29.764 -21.812 -12.866  1.00119.41
ATOM   1863  C   ALA A 234     -28.794 -22.809 -13.499  1.00119.59
ATOM   1864  O   ALA A 234     -28.010 -22.446 -14.384  1.00119.55
ATOM   1865  CB  ALA A 234     -29.282 -20.391 -13.113  1.00118.94
ATOM   1866  N   ALA A 235     -28.853 -24.061 -13.034  1.00119.69
ATOM   1867  CA  ALA A 235     -27.986 -25.134 -13.533  1.00119.56
ATOM   1868  C   ALA A 235     -28.509 -25.742 -14.837  1.00119.33
ATOM   1869  O   ALA A 235     -27.796 -25.798 -15.844  1.00119.03
ATOM   1870  CB  ALA A 235     -27.817 -26.223 -12.465  1.00118.67
ATOM   1871  N   SER A 240     -28.525 -19.607 -23.972  1.00110.02
ATOM   1872  CA  SER A 240     -28.129 -18.488 -24.826  1.00110.65
ATOM   1873  C   SER A 240     -29.067 -18.353 -26.024  1.00111.03
ATOM   1874  O   SER A 240     -28.765 -18.855 -27.111  1.00110.81
ATOM   1875  CB  SER A 240     -26.699 -18.693 -25.324  1.00110.64
ATOM   1876  OG  SER A 240     -26.597 -19.872 -26.106  1.00109.91
ATOM   1877  N   ALA A 241     -30.190 -17.659 -25.826  1.00111.81
ATOM   1878  CA  ALA A 241     -31.204 -17.463 -26.870  1.00112.79
ATOM   1879  C   ALA A 241     -31.609 -18.802 -27.515  1.00113.33
ATOM   1880  O   ALA A 241     -31.927 -18.867 -28.709  1.00113.27
ATOM   1881  CB  ALA A 241     -30.704 -16.473 -27.931  1.00112.88
ATOM   1882  N   THR A 242     -31.581 -19.862 -26.699  1.00113.80
ATOM   1883  CA  THR A 242     -31.920 -21.228 -27.116  1.00113.50
ATOM   1884  C   THR A 242     -33.346 -21.663 -26.701  1.00112.39
ATOM   1885  O   THR A 242     -34.160 -21.982 -27.575  1.00112.93
ATOM   1886  CB  THR A 242     -30.870 -22.271 -26.585  1.00114.30
ATOM   1887  OG1 THR A 242     -29.550 -21.898 -27.009  1.00114.63
ATOM   1888  CG2 THR A 242     -31.173 -23.675 -27.121  1.00114.35
ATOM   1889  N   THR A 243     -33.648 -21.674 -25.394  1.00110.18
ATOM   1890  CA  THR A 243     -34.985 -22.082 -24.920  1.00107.06
ATOM   1891  C   THR A 243     -35.537 -21.339 -23.681  1.00104.81
ATOM   1892  O   THR A 243     -35.523 -20.106 -23.623  1.00103.87
ATOM   1893  CB  THR A 243     -35.058 -23.615 -24.662  1.00107.09
ATOM   1894  OG1 THR A 243     -34.146 -24.301 -25.528  1.00107.15
ATOM   1895  CG2 THR A 243     -36.462 -24.130 -24.949  1.00107.05
ATOM   1896  N   GLN A 244     -36.055 -22.108 -22.719  1.00102.70
ATOM   1897  CA  GLN A 244     -36.654 -21.590 -21.476  1.00100.11
ATOM   1898  C   GLN A 244     -35.614 -21.054 -20.482  1.00 97.83
ATOM   1899  O   GLN A 244     -35.843 -20.047 -19.792  1.00 95.86
ATOM   1900  CB  GLN A 244     -37.468 -22.703 -20.783  1.00 99.84
ATOM   1901  CG  GLN A 244     -38.182 -23.693 -21.715  1.00 98.73
ATOM   190