CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 210531105755105496

Job options:

ID        	=	 210531105755105496
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


ATOM      1  N   SER A   7     -20.074   2.536  -5.840  1.00 64.93
ATOM      2  CA  SER A   7     -19.973   3.781  -5.020  1.00 66.60
ATOM      3  C   SER A   7     -19.770   5.048  -5.860  1.00 65.89
ATOM      4  O   SER A   7     -19.717   6.154  -5.318  1.00 65.25
ATOM      5  CB  SER A   7     -18.833   3.643  -4.004  1.00 67.41
ATOM      6  OG  SER A   7     -17.666   3.103  -4.606  1.00 70.09
ATOM      7  N   LEU A   8     -19.666   4.875  -7.180  1.00 65.56
ATOM      8  CA  LEU A   8     -19.475   5.987  -8.119  1.00 63.97
ATOM      9  C   LEU A   8     -20.799   6.385  -8.793  1.00 63.51
ATOM     10  O   LEU A   8     -21.751   5.606  -8.808  1.00 63.84
ATOM     11  CB  LEU A   8     -18.436   5.598  -9.174  1.00 62.99
ATOM     12  CG  LEU A   8     -17.016   5.387  -8.636  1.00 62.00
ATOM     13  CD1 LEU A   8     -16.153   4.709  -9.675  1.00 60.30
ATOM     14  CD2 LEU A   8     -16.431   6.728  -8.234  1.00 61.96
ATOM     15  N   SER A   9     -20.840   7.585  -9.371  1.00 62.23
ATOM     16  CA  SER A   9     -22.051   8.122 -10.001  1.00 60.83
ATOM     17  C   SER A   9     -22.505   7.539 -11.329  1.00 60.43
ATOM     18  O   SER A   9     -23.319   8.158 -12.013  1.00 62.58
ATOM     19  CB  SER A   9     -21.914   9.633 -10.198  1.00 60.77
ATOM     20  OG  SER A   9     -21.156   9.920 -11.362  1.00 58.32
ATOM     21  N   ALA A  10     -22.005   6.370 -11.707  1.00 59.33
ATOM     22  CA  ALA A  10     -22.397   5.769 -12.986  1.00 58.17
ATOM     23  C   ALA A  10     -21.731   6.547 -14.112  1.00 55.53
ATOM     24  O   ALA A  10     -21.139   5.958 -15.013  1.00 54.42
ATOM     25  CB  ALA A  10     -23.921   5.795 -13.163  1.00 57.64
ATOM     26  N   ALA A  11     -21.845   7.871 -14.064  1.00 52.48
ATOM     27  CA  ALA A  11     -21.210   8.704 -15.071  1.00 51.69
ATOM     28  C   ALA A  11     -19.717   8.497 -14.835  1.00 51.08
ATOM     29  O   ALA A  11     -18.926   8.456 -15.775  1.00 49.60
ATOM     30  CB  ALA A  11     -21.589  10.163 -14.876  1.00 51.34
ATOM     31  N   ALA A  12     -19.347   8.347 -13.565  1.00 50.32
ATOM     32  CA  ALA A  12     -17.957   8.106 -13.201  1.00 49.63
ATOM     33  C   ALA A  12     -17.678   6.647 -13.497  1.00 49.99
ATOM     34  O   ALA A  12     -16.537   6.258 -13.746  1.00 50.61
ATOM     35  CB  ALA A  12     -17.730   8.389 -11.721  1.00 48.73
ATOM     36  N   GLN A  13     -18.729   5.836 -13.469  1.00 50.13
ATOM     37  CA  GLN A  13     -18.573   4.417 -13.749  1.00 51.15
ATOM     38  C   GLN A  13     -18.305   4.193 -15.232  1.00 48.67
ATOM     39  O   GLN A  13     -17.515   3.323 -15.605  1.00 49.55
ATOM     40  CB  GLN A  13     -19.814   3.635 -13.287  1.00 54.28
ATOM     41  CG  GLN A  13     -19.842   3.385 -11.771  1.00 59.50
ATOM     42  CD  GLN A  13     -21.097   2.656 -11.291  1.00 62.50
ATOM     43  OE1 GLN A  13     -21.464   1.610 -11.830  1.00 64.90
ATOM     44  NE2 GLN A  13     -21.751   3.203 -10.262  1.00 60.70
ATOM     45  N   ALA A  14     -18.949   4.990 -16.075  1.00 45.93
ATOM     46  CA  ALA A  14     -18.758   4.872 -17.513  1.00 44.78
ATOM     47  C   ALA A  14     -17.310   5.233 -17.845  1.00 44.52
ATOM     48  O   ALA A  14     -16.680   4.599 -18.689  1.00 44.13
ATOM     49  CB  ALA A  14     -19.712   5.794 -18.243  1.00 43.83
ATOM     50  N   CYS A  15     -16.784   6.249 -17.167  1.00 43.28
ATOM     51  CA  CYS A  15     -15.410   6.665 -17.394  1.00 42.02
ATOM     52  C   CYS A  15     -14.476   5.524 -17.028  1.00 42.42
ATOM     53  O   CYS A  15     -13.602   5.144 -17.818  1.00 41.49
ATOM     54  CB  CYS A  15     -15.074   7.897 -16.555  1.00 41.62
ATOM     55  SG  CYS A  15     -15.833   9.434 -17.121  1.00 43.96
ATOM     56  N   VAL A  16     -14.668   4.978 -15.828  1.00 42.94
ATOM     57  CA  VAL A  16     -13.844   3.875 -15.346  1.00 42.65
ATOM     58  C   VAL A  16     -13.893   2.727 -16.339  1.00 43.92
ATOM     59  O   VAL A  16     -12.853   2.216 -16.765  1.00 44.05
ATOM     60  CB  VAL A  16     -14.335   3.376 -13.980  1.00 43.12
ATOM     61  CG1 VAL A  16     -13.510   2.180 -13.530  1.00 43.96
ATOM     62  CG2 VAL A  16     -14.232   4.494 -12.968  1.00 44.81
ATOM     63  N   LYS A  17     -15.106   2.333 -16.714  1.00 44.69
ATOM     64  CA  LYS A  17     -15.279   1.251 -17.670  1.00 45.99
ATOM     65  C   LYS A  17     -14.522   1.563 -18.951  1.00 44.94
ATOM     66  O   LYS A  17     -13.715   0.753 -19.431  1.00 44.29
ATOM     67  CB  LYS A  17     -16.758   1.043 -18.004  1.00 47.51
ATOM     68  CG  LYS A  17     -16.956   0.009 -19.115  1.00 52.33
ATOM     69  CD  LYS A  17     -18.418  -0.369 -19.358  1.00 54.02
ATOM     70  CE  LYS A  17     -18.527  -1.315 -20.559  1.00 54.47
ATOM     71  NZ  LYS A  17     -17.566  -2.453 -20.447  1.00 54.44
ATOM     72  N   LYS A  18     -14.782   2.750 -19.491  1.00 42.85
ATOM     73  CA  LYS A  18     -14.140   3.169 -20.725  1.00 42.11
ATOM     74  C   LYS A  18     -12.625   3.142 -20.646  1.00 42.10
ATOM     75  O   LYS A  18     -11.962   2.714 -21.587  1.00 42.38
ATOM     76  CB  LYS A  18     -14.593   4.572 -21.131  1.00 40.05
ATOM     77  CG  LYS A  18     -14.078   4.951 -22.505  1.00 40.14
ATOM     78  CD  LYS A  18     -14.669   6.238 -23.040  1.00 38.85
ATOM     79  CE  LYS A  18     -14.224   6.454 -24.483  1.00 37.15
ATOM     80  NZ  LYS A  18     -14.905   7.612 -25.090  1.00 36.92
ATOM     81  N   MET A  19     -12.078   3.593 -19.524  1.00 42.69
ATOM     82  CA  MET A  19     -10.633   3.626 -19.362  1.00 43.66
ATOM     83  C   MET A  19     -10.029   2.242 -19.143  1.00 45.31
ATOM     84  O   MET A  19      -8.891   1.985 -19.547  1.00 45.21
ATOM     85  CB  MET A  19     -10.272   4.563 -18.216  1.00 44.09
ATOM     86  CG  MET A  19     -10.663   6.003 -18.486  1.00 44.93
ATOM     87  SD  MET A  19     -10.587   7.116 -16.917  1.00 48.39
ATOM     88  CE  MET A  19      -8.677   7.324 -16.780  1.00 45.63
ATOM     89  N   ARG A  20     -10.785   1.348 -18.509  1.00 46.67
ATOM     90  CA  ARG A  20     -10.300  -0.012 -18.274  1.00 46.86
ATOM     91  C   ARG A  20     -10.348  -0.821 -19.560  1.00 47.86
ATOM     92  O   ARG A  20      -9.490  -1.669 -19.796  1.00 46.52
ATOM     93  CB  ARG A  20     -11.129  -0.701 -17.192  1.00 47.54
ATOM     94  CG  ARG A  20     -10.412  -0.779 -15.872  1.00 48.39
ATOM     95  CD  ARG A  20     -11.356  -0.792 -14.701  1.00 47.95
ATOM     96  NE  ARG A  20     -10.603  -0.594 -13.467  1.00 52.09
ATOM     97  CZ  ARG A  20     -11.150  -0.434 -12.266  1.00 52.46
ATOM     98  NH1 ARG A  20     -12.469  -0.449 -12.123  1.00 50.25
ATOM     99  NH2 ARG A  20     -10.375  -0.248 -11.208  1.00 52.15
ATOM    100  N   ASP A  21     -11.353  -0.559 -20.392  1.00 48.26
ATOM    101  CA  ASP A  21     -11.465  -1.270 -21.653  1.00 49.73
ATOM    102  C   ASP A  21     -10.277  -0.929 -22.547  1.00 49.85
ATOM    103  O   ASP A  21      -9.722  -1.807 -23.207  1.00 50.33
ATOM    104  CB  ASP A  21     -12.784  -0.920 -22.350  1.00 52.53
ATOM    105  CG  ASP A  21     -13.987  -1.598 -21.699  1.00 55.21
ATOM    106  OD1 ASP A  21     -15.140  -1.314 -22.105  1.00 55.56
ATOM    107  OD2 ASP A  21     -13.776  -2.422 -20.782  1.00 56.05
ATOM    108  N   ALA A  22      -9.877   0.342 -22.557  1.00 49.67
ATOM    109  CA  ALA A  22      -8.747   0.782 -23.374  1.00 48.13
ATOM    110  C   ALA A  22      -7.424   0.515 -22.670  1.00 48.49
ATOM    111  O   ALA A  22      -6.362   0.922 -23.140  1.00 46.40
ATOM    112  CB  ALA A  22      -8.875   2.253 -23.697  1.00 47.37
ATOM    113  N   LYS A  23      -7.504  -0.163 -21.529  1.00 49.49
ATOM    114  CA  LYS A  23      -6.329  -0.531 -20.746  1.00 50.43
ATOM    115  C   LYS A  23      -5.529   0.632 -20.158  1.00 49.95
ATOM    116  O   LYS A  23      -4.297   0.628 -20.168  1.00 48.12
ATOM    117  CB  LYS A  23      -5.431  -1.436 -21.596  1.00 52.80
ATOM    118  CG  LYS A  23      -6.160  -2.709 -22.032  1.00 56.79
ATOM    119  CD  LYS A  23      -5.349  -3.580 -22.979  1.00 58.97
ATOM    120  CE  LYS A  23      -6.121  -4.858 -23.298  1.00 61.05
ATOM    121  NZ  LYS A  23      -5.470  -5.683 -24.357  1.00 62.64
ATOM    122  N   VAL A  24      -6.244   1.621 -19.633  1.00 49.83
ATOM    123  CA  VAL A  24      -5.620   2.781 -19.002  1.00 50.79
ATOM    124  C   VAL A  24      -5.157   2.350 -17.610  1.00 50.72
ATOM    125  O   VAL A  24      -5.963   1.844 -16.829  1.00 51.82
ATOM    126  CB  VAL A  24      -6.631   3.931 -18.832  1.00 50.24
ATOM    127  CG1 VAL A  24      -6.025   5.021 -17.967  1.00 50.60
ATOM    128  CG2 VAL A  24      -7.037   4.485 -20.199  1.00 50.65
ATOM    129  N   ASN A  25      -3.884   2.555 -17.283  1.00 49.84
ATOM    130  CA  ASN A  25      -3.398   2.137 -15.970  1.00 50.74
ATOM    131  C   ASN A  25      -4.260   2.686 -14.830  1.00 48.86
ATOM    132  O   ASN A  25      -4.849   3.764 -14.932  1.00 48.04
ATOM    133  CB  ASN A  25      -1.932   2.538 -15.774  1.00 53.30
ATOM    134  CG  ASN A  25      -1.773   3.979 -15.379  1.00 56.78
ATOM    135  OD1 ASN A  25      -2.090   4.371 -14.252  1.00 59.09
ATOM    136  ND2 ASN A  25      -1.280   4.789 -16.308  1.00 59.91
ATOM    137  N   GLU A  26      -4.321   1.922 -13.746  1.00 47.93
ATOM    138  CA  GLU A  26      -5.121   2.263 -12.576  1.00 44.92
ATOM    139  C   GLU A  26      -4.746   3.557 -11.856  1.00 43.05
ATOM    140  O   GLU A  26      -5.628   4.249 -11.350  1.00 42.66
ATOM    141  CB  GLU A  26      -5.101   1.093 -11.578  1.00 45.58
ATOM    142  CG  GLU A  26      -5.807  -0.180 -12.056  1.00 45.08
ATOM    143  CD  GLU A  26      -7.278   0.046 -12.377  1.00 48.19
ATOM    144  OE1 GLU A  26      -7.978   0.663 -11.544  1.00 50.71
ATOM    145  OE2 GLU A  26      -7.740  -0.398 -13.455  1.00 49.02
ATOM    146  N   ALA A  27      -3.457   3.887 -11.793  1.00 41.38
ATOM    147  CA  ALA A  27      -3.040   5.116 -11.109  1.00 40.99
ATOM    148  C   ALA A  27      -3.692   6.318 -11.778  1.00 40.54
ATOM    149  O   ALA A  27      -4.144   7.243 -11.112  1.00 41.16
ATOM    150  CB  ALA A  27      -1.530   5.260 -11.140  1.00 40.04
ATOM    151  N   CYS A  28      -3.739   6.284 -13.104  1.00 40.64
ATOM    152  CA  CYS A  28      -4.348   7.343 -13.901  1.00 40.96
ATOM    153  C   CYS A  28      -5.851   7.374 -13.632  1.00 40.62
ATOM    154  O   CYS A  28      -6.433   8.429 -13.355  1.00 41.80
ATOM    155  CB  CYS A  28      -4.076   7.078 -15.385  1.00 42.18
ATOM    156  SG  CYS A  28      -4.926   8.163 -16.527  1.00 41.62
ATOM    157  N   ILE A  29      -6.479   6.209 -13.708  1.00 39.95
ATOM    158  CA  ILE A  29      -7.910   6.104 -13.442  1.00 40.38
ATOM    159  C   ILE A  29      -8.247   6.715 -12.070  1.00 40.59
ATOM    160  O   ILE A  29      -9.146   7.546 -11.967  1.00 40.70
ATOM    161  CB  ILE A  29      -8.367   4.623 -13.486  1.00 38.77
ATOM    162  CG1 ILE A  29      -8.147   4.065 -14.893  1.00 36.91
ATOM    163  CG2 ILE A  29      -9.824   4.508 -13.070  1.00 40.53
ATOM    164  CD1 ILE A  29      -8.468   2.603 -15.055  1.00 36.12
ATOM    165  N   ARG A  30      -7.514   6.319 -11.028  1.00 40.36
ATOM    166  CA  ARG A  30      -7.763   6.846  -9.681  1.00 42.18
ATOM    167  C   ARG A  30      -7.710   8.367  -9.653  1.00 40.70
ATOM    168  O   ARG A  30      -8.642   9.027  -9.191  1.00 40.33
ATOM    169  CB  ARG A  30      -6.746   6.291  -8.664  1.00 44.41
ATOM    170  CG  ARG A  30      -6.836   4.780  -8.393  1.00 47.38
ATOM    171  CD  ARG A  30      -6.139   4.383  -7.083  1.00 46.24
ATOM    172  NE  ARG A  30      -4.696   4.604  -7.123  1.00 50.32
ATOM    173  CZ  ARG A  30      -3.825   3.793  -7.719  1.00 50.80
ATOM    174  NH1 ARG A  30      -4.241   2.692  -8.330  1.00 52.36
ATOM    175  NH2 ARG A  30      -2.533   4.085  -7.712  1.00 51.63
ATOM    176  N   THR A  31      -6.612   8.915 -10.163  1.00 41.85
ATOM    177  CA  THR A  31      -6.403  10.361 -10.198  1.00 40.02
ATOM    178  C   THR A  31      -7.534  11.056 -10.949  1.00 40.09
ATOM    179  O   THR A  31      -8.077  12.056 -10.481  1.00 39.86
ATOM    180  CB  THR A  31      -5.058  10.693 -10.871  1.00 38.93
ATOM    181  OG1 THR A  31      -4.014   9.967 -10.214  1.00 37.97
ATOM    182  CG2 THR A  31      -4.762  12.181 -10.783  1.00 35.68
ATOM    183  N   PHE A  32      -7.888  10.519 -12.112  1.00 39.82
ATOM    184  CA  PHE A  32      -8.957  11.095 -12.909  1.00 39.21
ATOM    185  C   PHE A  32     -10.314  11.013 -12.202  1.00 40.87
ATOM    186  O   PHE A  32     -11.126  11.939 -12.279  1.00 41.08
ATOM    187  CB  PHE A  32      -9.055  10.379 -14.257  1.00 38.39
ATOM    188  CG  PHE A  32     -10.158  10.904 -15.139  1.00 38.80
ATOM    189  CD1 PHE A  32      -9.946  12.011 -15.957  1.00 36.39
ATOM    190  CD2 PHE A  32     -11.419  10.311 -15.127  1.00 37.71
ATOM    191  CE1 PHE A  32     -10.972  12.519 -16.745  1.00 36.92
ATOM    192  CE2 PHE A  32     -12.446  10.811 -15.909  1.00 36.29
ATOM    193  CZ  PHE A  32     -12.224  11.919 -16.722  1.00 35.88
ATOM    194  N   ILE A  33     -10.574   9.910 -11.510  1.00 41.85
ATOM    195  CA  ILE A  33     -11.865   9.773 -10.843  1.00 42.01
ATOM    196  C   ILE A  33     -12.054  10.765  -9.705  1.00 41.14
ATOM    197  O   ILE A  33     -13.142  11.308  -9.529  1.00 40.54
ATOM    198  CB  ILE A  33     -12.081   8.340 -10.333  1.00 41.81
ATOM    199  CG1 ILE A  33     -12.115   7.382 -11.525  1.00 43.03
ATOM    200  CG2 ILE A  33     -13.392   8.249  -9.563  1.00 41.30
ATOM    201  CD1 ILE A  33     -13.136   7.763 -12.587  1.00 44.71
ATOM    202  N   ALA A  34     -10.997  11.002  -8.935  1.00 40.34
ATOM    203  CA  ALA A  34     -11.068  11.956  -7.837  1.00 39.17
ATOM    204  C   ALA A  34     -11.418  13.304  -8.450  1.00 39.58
ATOM    205  O   ALA A  34     -12.219  14.065  -7.909  1.00 40.59
ATOM    206  CB  ALA A  34      -9.728  12.035  -7.126  1.00 37.95
ATOM    207  N   GLN A  35     -10.817  13.585  -9.601  1.00 39.30
ATOM    208  CA  GLN A  35     -11.070  14.832 -10.301  1.00 39.49
ATOM    209  C   GLN A  35     -12.535  14.880 -10.707  1.00 39.42
ATOM    210  O   GLN A  35     -13.207  15.886 -10.497  1.00 40.74
ATOM    211  CB  GLN A  35     -10.174  14.939 -11.543  1.00 38.94
ATOM    212  CG  GLN A  35      -8.680  14.813 -11.249  1.00 38.27
ATOM    213  CD  GLN A  35      -7.823  15.032 -12.481  1.00 37.95
ATOM    214  OE1 GLN A  35      -8.217  14.692 -13.591  1.00 35.80
ATOM    215  NE2 GLN A  35      -6.636  15.585 -12.284  1.00 36.45
ATOM    216  N   HIS A  36     -13.017  13.788 -11.296  1.00 40.27
ATOM    217  CA  HIS A  36     -14.407  13.684 -11.737  1.00 41.07
ATOM    218  C   HIS A  36     -15.329  13.991 -10.551  1.00 40.74
ATOM    219  O   HIS A  36     -16.305  14.724 -10.687  1.00 36.04
ATOM    220  CB  HIS A  36     -14.673  12.269 -12.279  1.00 43.01
ATOM    221  CG  HIS A  36     -15.933  12.143 -13.084  1.00 46.86
ATOM    222  ND1 HIS A  36     -17.183  12.039 -12.509  1.00 49.30
ATOM    223  CD2 HIS A  36     -16.133  12.108 -14.424  1.00 47.94
ATOM    224  CE1 HIS A  36     -18.098  11.946 -13.459  1.00 49.30
ATOM    225  NE2 HIS A  36     -17.487  11.986 -14.631  1.00 48.99
ATOM    226  N   VAL A  37     -14.993  13.458  -9.380  1.00 41.79
ATOM    227  CA  VAL A  37     -15.812  13.692  -8.195  1.00 43.05
ATOM    228  C   VAL A  37     -15.863  15.167  -7.840  1.00 44.66
ATOM    229  O   VAL A  37     -16.935  15.715  -7.570  1.00 44.73
ATOM    230  CB  VAL A  37     -15.293  12.896  -6.983  1.00 42.79
ATOM    231  CG1 VAL A  37     -16.015  13.336  -5.723  1.00 43.43
ATOM    232  CG2 VAL A  37     -15.518  11.412  -7.209  1.00 38.89
ATOM    233  N   MET A  38     -14.701  15.811  -7.848  1.00 47.12
ATOM    234  CA  MET A  38     -14.620  17.231  -7.531  1.00 48.20
ATOM    235  C   MET A  38     -15.456  18.050  -8.500  1.00 47.71
ATOM    236  O   MET A  38     -16.179  18.945  -8.082  1.00 50.00
ATOM    237  CB  MET A  38     -13.160  17.705  -7.549  1.00 50.75
ATOM    238  CG  MET A  38     -12.319  17.154  -6.400  1.00 56.40
ATOM    239  SD  MET A  38     -13.082  17.560  -4.645  1.00 70.09
ATOM    240  CE  MET A  38     -12.962  19.489  -4.735  1.00 61.96
ATOM    241  N   VAL A  39     -15.363  17.744  -9.791  1.00 47.07
ATOM    242  CA  VAL A  39     -16.142  18.466 -10.794  1.00 47.32
ATOM    243  C   VAL A  39     -17.628  18.184 -10.570  1.00 48.14
ATOM    244  O   VAL A  39     -18.475  19.060 -10.764  1.00 47.53
ATOM    245  CB  VAL A  39     -15.744  18.035 -12.227  1.00 47.82
ATOM    246  CG1 VAL A  39     -16.600  18.760 -13.254  1.00 42.74
ATOM    247  CG2 VAL A  39     -14.266  18.333 -12.462  1.00 48.01
ATOM    248  N   SER A  40     -17.929  16.954 -10.156  1.00 49.80
ATOM    249  CA  SER A  40     -19.297  16.525  -9.862  1.00 52.05
ATOM    250  C   SER A  40     -19.904  17.340  -8.718  1.00 52.35
ATOM    251  O   SER A  40     -21.120  17.476  -8.637  1.00 50.31
ATOM    252  CB  SER A  40     -19.330  15.037  -9.482  1.00 52.74
ATOM    253  OG  SER A  40     -19.261  14.198 -10.626  1.00 57.68
ATOM    254  N   LYS A  41     -19.057  17.864  -7.831  1.00 54.08
ATOM    255  CA  LYS A  41     -19.528  18.678  -6.708  1.00 56.34
ATOM    256  C   LYS A  41     -19.563  20.155  -7.097  1.00 57.51
ATOM    257  O   LYS A  41     -19.779  21.024  -6.252  1.00 57.76
ATOM    258  CB  LYS A  41     -18.624  18.507  -5.482  1.00 57.05
ATOM    259  CG  LYS A  41     -18.693  17.143  -4.822  1.00 60.37
ATOM    260  CD  LYS A  41     -17.791  17.069  -3.592  1.00 63.32
ATOM    261  CE  LYS A  41     -17.830  15.675  -2.961  1.00 66.70
ATOM    262  NZ  LYS A  41     -16.943  15.540  -1.760  1.00 67.62
ATOM    263  N   GLY A  42     -19.340  20.435  -8.376  1.00 58.50
ATOM    264  CA  GLY A  42     -19.360  21.807  -8.844  1.00 60.57
ATOM    265  C   GLY A  42     -18.114  22.614  -8.523  1.00 62.65
ATOM    266  O   GLY A  42     -18.187  23.839  -8.417  1.00 62.71
ATOM    267  N   GLU A  43     -16.973  21.944  -8.368  1.00 64.04
ATOM    268  CA  GLU A  43     -15.724  22.639  -8.068  1.00 66.18
ATOM    269  C   GLU A  43     -15.506  23.762  -9.081  1.00 67.27
ATOM    270  O   GLU A  43     -15.654  23.563 -10.287  1.00 68.51
ATOM    271  CB  GLU A  43     -14.546  21.655  -8.097  1.00 67.17
ATOM    272  CG  GLU A  43     -13.160  22.300  -7.975  1.00 68.65
ATOM    273  CD  GLU A  43     -12.985  23.134  -6.712  1.00 68.68
ATOM    274  OE1 GLU A  43     -12.974  22.564  -5.600  1.00 69.64
ATOM    275  OE2 GLU A  43     -12.854  24.369  -6.834  1.00 68.95
ATOM    276  N   THR A  44     -15.164  24.944  -8.576  1.00 68.22
ATOM    277  CA  THR A  44     -14.934  26.118  -9.412  1.00 67.92
ATOM    278  C   THR A  44     -13.463  26.239  -9.787  1.00 66.90
ATOM    279  O   THR A  44     -13.130  26.573 -10.922  1.00 67.55
ATOM    280  CB  THR A  44     -15.332  27.421  -8.672  1.00 69.99
ATOM    281  OG1 THR A  44     -16.580  27.233  -7.991  1.00 72.01
ATOM    282  CG2 THR A  44     -15.467  28.580  -9.661  1.00 69.97
ATOM    283  N   GLY A  45     -12.594  25.965  -8.815  1.00 64.87
ATOM    284  CA  GLY A  45     -11.160  26.071  -9.024  1.00 61.20
ATOM    285  C   GLY A  45     -10.755  27.454  -8.562  1.00 59.04
ATOM    286  O   GLY A  45      -9.574  27.775  -8.421  1.00 58.74
ATOM    287  N   SER A  46     -11.777  28.264  -8.307  1.00 57.07
ATOM    288  CA  SER A  46     -11.637  29.649  -7.869  1.00 55.99
ATOM    289  C   SER A  46     -10.706  29.870  -6.675  1.00 55.47
ATOM    290  O   SER A  46     -10.701  29.095  -5.713  1.00 56.30
ATOM    291  CB  SER A  46     -13.028  30.219  -7.552  1.00 54.81
ATOM    292  OG  SER A  46     -12.969  31.575  -7.143  1.00 53.16
ATOM    293  N   ILE A  47      -9.926  30.944  -6.753  1.00 52.59
ATOM    294  CA  ILE A  47      -9.001  31.316  -5.693  1.00 49.24
ATOM    295  C   ILE A  47      -9.029  32.827  -5.507  1.00 48.52
ATOM    296  O   ILE A  47      -8.155  33.537  -6.007  1.00 50.01
ATOM    297  CB  ILE A  47      -7.559  30.918  -6.025  1.00 47.64
ATOM    298  CG1 ILE A  47      -7.474  29.420  -6.289  1.00 44.82
ATOM    299  CG2 ILE A  47      -6.642  31.309  -4.878  1.00 45.88
ATOM    300  CD1 ILE A  47      -6.102  28.995  -6.751  1.00 48.25
ATOM    301  N   PRO A  48     -10.038  33.341  -4.785  1.00 47.22
ATOM    302  CA  PRO A  48     -10.173  34.782  -4.534  1.00 46.50
ATOM    303  C   PRO A  48      -8.994  35.375  -3.756  1.00 44.94
ATOM    304  O   PRO A  48      -8.368  34.690  -2.956  1.00 44.28
ATOM    305  CB  PRO A  48     -11.491  34.875  -3.763  1.00 47.52
ATOM    306  CG  PRO A  48     -11.584  33.541  -3.073  1.00 47.00
ATOM    307  CD  PRO A  48     -11.121  32.584  -4.132  1.00 47.05
ATOM    308  N   ASP A  49      -8.695  36.647  -3.994  1.00 44.47
ATOM    309  CA  ASP A  49      -7.583  37.301  -3.306  1.00 46.58
ATOM    310  C   ASP A  49      -7.652  37.108  -1.791  1.00 47.58
ATOM    311  O   ASP A  49      -6.622  37.019  -1.118  1.00 48.16
ATOM    312  CB  ASP A  49      -7.565  38.805  -3.610  1.00 47.27
ATOM    313  CG  ASP A  49      -6.288  39.247  -4.308  1.00 48.59
ATOM    314  OD1 ASP A  49      -5.652  40.217  -3.840  1.00 46.63
ATOM    315  OD2 ASP A  49      -5.928  38.623  -5.331  1.00 50.33
ATOM    316  N   SER A  50      -8.873  37.046  -1.265  1.00 47.04
ATOM    317  CA  SER A  50      -9.091  36.894   0.168  1.00 46.58
ATOM    318  C   SER A  50      -8.617  35.551   0.721  1.00 45.00
ATOM    319  O   SER A  50      -8.518  35.380   1.935  1.00 44.28
ATOM    320  CB  SER A  50     -10.580  37.108   0.493  1.00 47.41
ATOM    321  OG  SER A  50     -11.419  36.330  -0.348  1.00 47.22
ATOM    322  N   ALA A  51      -8.304  34.618  -0.173  1.00 42.91
ATOM    323  CA  ALA A  51      -7.847  33.281   0.216  1.00 41.89
ATOM    324  C   ALA A  51      -6.330  33.099   0.122  1.00 41.31
ATOM    325  O   ALA A  51      -5.808  32.045   0.502  1.00 39.07
ATOM    326  CB  ALA A  51      -8.533  32.234  -0.653  1.00 41.76
ATOM    327  N   ILE A  52      -5.636  34.114  -0.395  1.00 39.20
ATOM    328  CA  ILE A  52      -4.188  34.062  -0.550  1.00 39.29
ATOM    329  C   ILE A  52      -3.502  35.349  -0.092  1.00 41.23
ATOM    330  O   ILE A  52      -4.137  36.388   0.080  1.00 42.87
ATOM    331  CB  ILE A  52      -3.771  33.822  -2.039  1.00 36.32
ATOM    332  CG1 ILE A  52      -4.290  34.967  -2.914  1.00 38.91
ATOM    333  CG2 ILE A  52      -4.280  32.481  -2.533  1.00 34.20
ATOM    334  CD1 ILE A  52      -4.085  34.773  -4.422  1.00 37.01
ATOM    335  N   MET A  53      -2.193  35.261   0.099  1.00 42.66
ATOM    336  CA  MET A  53      -1.382  36.405   0.490  1.00 46.87
ATOM    337  C   MET A  53      -0.155  36.424  -0.418  1.00 46.79
ATOM    338  O   MET A  53       0.267  35.379  -0.926  1.00 46.09
ATOM    339  CB  MET A  53      -0.949  36.288   1.957  1.00 50.32
ATOM    340  CG  MET A  53      -2.059  36.599   2.961  1.00 56.55
ATOM    341  SD  MET A  53      -2.711  38.424   2.786  1.00 65.88
ATOM    342  CE  MET A  53      -1.284  39.326   3.735  1.00 62.66
ATOM    343  N   PRO A  54       0.415  37.608  -0.665  1.00 45.48
ATOM    344  CA  PRO A  54       1.592  37.627  -1.527  1.00 46.66
ATOM    345  C   PRO A  54       2.819  37.076  -0.812  1.00 47.82
ATOM    346  O   PRO A  54       2.815  36.902   0.409  1.00 47.56
ATOM    347  CB  PRO A  54       1.731  39.104  -1.887  1.00 46.36
ATOM    348  CG  PRO A  54       1.182  39.792  -0.693  1.00 46.15
ATOM    349  CD  PRO A  54      -0.055  38.975  -0.404  1.00 47.70
ATOM    350  N   VAL A  55       3.847  36.776  -1.601  1.00 48.52
ATOM    351  CA  VAL A  55       5.126  36.260  -1.119  1.00 50.57
ATOM    352  C   VAL A  55       6.095  37.416  -1.348  1.00 52.64
ATOM    353  O   VAL A  55       6.496  37.671  -2.484  1.00 53.48
ATOM    354  CB  VAL A  55       5.589  35.048  -1.965  1.00 50.29
ATOM    355  CG1 VAL A  55       6.929  34.546  -1.468  1.00 48.43
ATOM    356  CG2 VAL A  55       4.542  33.941  -1.915  1.00 49.53
ATOM    357  N   ASP A  56       6.466  38.116  -0.280  1.00 54.47
ATOM    358  CA  ASP A  56       7.349  39.272  -0.408  1.00 55.83
ATOM    359  C   ASP A  56       8.805  38.993  -0.752  1.00 55.77
ATOM    360  O   ASP A  56       9.405  39.735  -1.533  1.00 54.55
ATOM    361  CB  ASP A  56       7.288  40.133   0.859  1.00 58.86
ATOM    362  CG  ASP A  56       5.932  40.802   1.044  1.00 62.33
ATOM    363  OD1 ASP A  56       5.323  41.205   0.026  1.00 63.19
ATOM    364  OD2 ASP A  56       5.481  40.941   2.203  1.00 63.58
ATOM    365  N   SER A  57       9.380  37.933  -0.190  1.00 54.26
ATOM    366  CA  SER A  57      10.778  37.641  -0.478  1.00 53.66
ATOM    367  C   SER A  57      11.156  36.164  -0.543  1.00 51.64
ATOM    368  O   SER A  57      10.619  35.322   0.182  1.00 51.31
ATOM    369  CB  SER A  57      11.676  38.365   0.531  1.00 55.23
ATOM    370  OG  SER A  57      11.282  38.076   1.860  1.00 59.28
ATOM    371  N   LEU A  58      12.100  35.875  -1.431  1.00 48.19
ATOM    372  CA  LEU A  58      12.601  34.530  -1.664  1.00 44.72
ATOM    373  C   LEU A  58      14.096  34.656  -1.890  1.00 42.31
ATOM    374  O   LEU A  58      14.589  35.736  -2.184  1.00 41.71
ATOM    375  CB  LEU A  58      11.964  33.954  -2.924  1.00 43.62
ATOM    376  CG  LEU A  58      10.439  33.882  -2.969  1.00 41.95
ATOM    377  CD1 LEU A  58       9.966  33.853  -4.413  1.00 43.37
ATOM    378  CD2 LEU A  58       9.969  32.654  -2.217  1.00 42.07
ATOM    379  N   ASP A  59      14.825  33.561  -1.755  1.00 40.03
ATOM    380  CA  ASP A  59      16.253  33.621  -1.993  1.00 38.45
ATOM    381  C   ASP A  59      16.469  33.718  -3.498  1.00 37.69
ATOM    382  O   ASP A  59      15.539  33.515  -4.281  1.00 35.21
ATOM    383  CB  ASP A  59      16.942  32.389  -1.415  1.00 40.26
ATOM    384  CG  ASP A  59      16.967  32.398   0.107  1.00 41.07
ATOM    385  OD1 ASP A  59      17.222  33.479   0.672  1.00 40.68
ATOM    386  OD2 ASP A  59      16.744  31.334   0.733  1.00 40.19
ATOM    387  N   ALA A  60      17.690  34.040  -3.904  1.00 37.00
ATOM    388  CA  ALA A  60      17.994  34.182  -5.321  1.00 36.23
ATOM    389  C   ALA A  60      19.131  33.273  -5.784  1.00 36.23
ATOM    390  O   ALA A  60      20.121  33.092  -5.069  1.00 38.25
ATOM    391  CB  ALA A  60      18.331  35.639  -5.620  1.00 31.80
ATOM    392  N   LEU A  61      18.995  32.713  -6.982  1.00 35.04
ATOM    393  CA  LEU A  61      20.026  31.844  -7.531  1.00 36.08
ATOM    394  C   LEU A  61      21.319  32.658  -7.727  1.00 38.12
ATOM    395  O   LEU A  61      22.410  32.110  -7.661  1.00 40.82
ATOM    396  CB  LEU A  61      19.572  31.254  -8.874  1.00 34.76
ATOM    397  CG  LEU A  61      20.076  29.861  -9.303  1.00 35.70
ATOM    398  CD1 LEU A  61      20.149  29.786 -10.824  1.00 31.19
ATOM    399  CD2 LEU A  61      21.439  29.564  -8.698  1.00 32.67
ATOM    400  N   ASP A  62      21.202  33.963  -7.966  1.00 39.42
ATOM    401  CA  ASP A  62      22.386  34.808  -8.150  1.00 42.93
ATOM    402  C   ASP A  62      23.168  35.030  -6.866  1.00 44.88
ATOM    403  O   ASP A  62      24.360  35.326  -6.913  1.00 47.06
ATOM    404  CB  ASP A  62      22.009  36.175  -8.722  1.00 46.41
ATOM    405  CG  ASP A  62      21.705  36.118 -10.200  1.00 50.77
ATOM    406  OD1 ASP A  62      21.257  37.146 -10.760  1.00 52.54
ATOM    407  OD2 ASP A  62      21.917  35.039 -10.802  1.00 53.82
ATOM    408  N   SER A  63      22.500  34.905  -5.724  1.00 44.48
ATOM    409  CA  SER A  63      23.167  35.085  -4.444  1.00 44.39
ATOM    410  C   SER A  63      23.881  33.798  -4.044  1.00 45.26
ATOM    411  O   SER A  63      24.809  33.822  -3.235  1.00 47.95
ATOM    412  CB  SER A  63      22.156  35.464  -3.356  1.00 45.07
ATOM    413  OG  SER A  63      21.517  36.697  -3.653  1.00 47.63
ATOM    414  N   LEU A  64      23.460  32.675  -4.617  1.00 43.39
ATOM    415  CA  LEU A  64      24.076  31.392  -4.291  1.00 42.26
ATOM    416  C   LEU A  64      25.437  31.213  -4.959  1.00 41.40
ATOM    417  O   LEU A  64      25.681  31.764  -6.033  1.00 42.00
ATOM    418  CB  LEU A  64      23.158  30.245  -4.719  1.00 39.93
ATOM    419  CG  LEU A  64      21.760  30.173  -4.102  1.00 37.17
ATOM    420  CD1 LEU A  64      21.167  28.814  -4.447  1.00 31.79
ATOM    421  CD2 LEU A  64      21.826  30.363  -2.585  1.00 35.39
ATOM    422  N   THR A  65      26.318  30.437  -4.332  1.00 40.06
ATOM    423  CA  THR A  65      27.636  30.203  -4.915  1.00 42.65
ATOM    424  C   THR A  65      28.160  28.777  -4.737  1.00 41.92
ATOM    425  O   THR A  65      28.988  28.320  -5.527  1.00 42.89
ATOM    426  CB  THR A  65      28.708  31.192  -4.354  1.00 43.27
ATOM    427  OG1 THR A  65      28.976  30.893  -2.978  1.00 45.98
ATOM    428  CG2 THR A  65      28.216  32.627  -4.457  1.00 43.67
ATOM    429  N   ILE A  66      27.685  28.070  -3.718  1.00 40.14
ATOM    430  CA  ILE A  66      28.150  26.706  -3.478  1.00 40.19
ATOM    431  C   ILE A  66      27.559  25.650  -4.412  1.00 40.54
ATOM    432  O   ILE A  66      26.342  25.527  -4.542  1.00 40.67
ATOM    433  CB  ILE A  66      27.840  26.255  -2.045  1.00 40.98
ATOM    434  CG1 ILE A  66      28.518  27.188  -1.039  1.00 42.47
ATOM    435  CG2 ILE A  66      28.296  24.816  -1.849  1.00 38.39
ATOM    436  CD1 ILE A  66      27.976  27.041   0.377  1.00 39.32
ATOM    437  N   GLU A  67      28.426  24.869  -5.043  1.00 41.53
ATOM    438  CA  GLU A  67      27.976  23.803  -5.930  1.00 43.76
ATOM    439  C   GLU A  67      27.973  22.508  -5.132  1.00 44.76
ATOM    440  O   GLU A  67      28.763  22.351  -4.210  1.00 47.00
ATOM    441  CB  GLU A  67      28.920  23.644  -7.125  1.00 43.04
ATOM    442  CG  GLU A  67      29.029  24.863  -8.022  1.00 45.88
ATOM    443  CD  GLU A  67      29.976  24.644  -9.187  1.00 48.40
ATOM    444  OE1 GLU A  67      30.165  25.579  -9.987  1.00 52.75
ATOM    445  OE2 GLU A  67      30.537  23.537  -9.312  1.00 53.22
ATOM    446  N   CYS A  68      27.082  21.588  -5.475  1.00 45.40
ATOM    447  CA  CYS A  68      27.016  20.302  -4.791  1.00 45.94
ATOM    448  C   CYS A  68      28.148  19.452  -5.363  1.00 47.20
ATOM    449  O   CYS A  68      28.609  19.708  -6.472  1.00 47.23
ATOM    450  CB  CYS A  68      25.679  19.614  -5.090  1.00 46.17
ATOM    451  SG  CYS A  68      25.481  19.091  -6.834  1.00 43.50
ATOM    452  N   ASP A  69      28.607  18.445  -4.630  1.00 48.76
ATOM    453  CA  ASP A  69      29.660  17.619  -5.191  1.00 51.03
ATOM    454  C   ASP A  69      29.054  16.658  -6.202  1.00 51.27
ATOM    455  O   ASP A  69      27.849  16.410  -6.202  1.00 51.93
ATOM    456  CB  ASP A  69      30.467  16.872  -4.109  1.00 54.10
ATOM    457  CG  ASP A  69      29.602  16.126  -3.115  1.00 57.48
ATOM    458  OD1 ASP A  69      28.730  15.342  -3.549  1.00 59.54
ATOM    459  OD2 ASP A  69      29.817  16.313  -1.893  1.00 57.40
ATOM    460  N   ASN A  70      29.899  16.137  -7.078  1.00 51.98
ATOM    461  CA  ASN A  70      29.469  15.242  -8.132  1.00 53.57
ATOM    462  C   ASN A  70      28.649  14.042  -7.698  1.00 53.04
ATOM    463  O   ASN A  70      27.997  13.411  -8.526  1.00 54.69
ATOM    464  CB  ASN A  70      30.686  14.795  -8.929  1.00 56.55
ATOM    465  CG  ASN A  70      31.478  15.972  -9.463  1.00 60.53
ATOM    466  OD1 ASN A  70      30.927  16.848 -10.134  1.00 62.76
ATOM    467  ND2 ASN A  70      32.774  16.006  -9.161  1.00 61.58
ATOM    468  N   ALA A  71      28.663  13.732  -6.409  1.00 50.96
ATOM    469  CA  ALA A  71      27.899  12.599  -5.896  1.00 50.25
ATOM    470  C   ALA A  71      26.399  12.853  -5.974  1.00 50.03
ATOM    471  O   ALA A  71      25.619  11.938  -6.252  1.00 50.15
ATOM    472  CB  ALA A  71      28.296  12.303  -4.448  1.00 50.79
ATOM    473  N   VAL A  72      25.986  14.090  -5.717  1.00 49.03
ATOM    474  CA  VAL A  72      24.568  14.411  -5.770  1.00 47.05
ATOM    475  C   VAL A  72      24.009  14.185  -7.178  1.00 46.84
ATOM    476  O   VAL A  72      22.880  13.713  -7.336  1.00 47.03
ATOM    477  CB  VAL A  72      24.305  15.867  -5.337  1.00 46.67
ATOM    478  CG1 VAL A  72      22.811  16.155  -5.376  1.00 42.89
ATOM    479  CG2 VAL A  72      24.856  16.094  -3.930  1.00 45.35
ATOM    480  N   LEU A  73      24.806  14.506  -8.195  1.00 45.20
ATOM    481  CA  LEU A  73      24.376  14.328  -9.575  1.00 46.05
ATOM    482  C   LEU A  73      24.211  12.863  -9.940  1.00 46.88
ATOM    483  O   LEU A  73      23.418  12.526 -10.817  1.00 46.79
ATOM    484  CB  LEU A  73      25.366  14.980 -10.543  1.00 46.95
ATOM    485  CG  LEU A  73      25.318  16.504 -10.652  1.00 48.93
ATOM    486  CD1 LEU A  73      26.366  16.965 -11.645  1.00 50.38
ATOM    487  CD2 LEU A  73      23.929  16.955 -11.101  1.00 49.53
ATOM    488  N   GLN A  74      24.956  11.993  -9.269  1.00 46.06
ATOM    489  CA  GLN A  74      24.875  10.566  -9.543  1.00 47.39
ATOM    490  C   GLN A  74      23.490  10.053  -9.182  1.00 47.63
ATOM    491  O   GLN A  74      23.061   9.008  -9.677  1.00 48.45
ATOM    492  CB  GLN A  74      25.933   9.800  -8.738  1.00 48.64
ATOM    493  CG  GLN A  74      27.368  10.058  -9.183  1.00 50.49
ATOM    494  CD  GLN A  74      27.759   9.277 -10.436  1.00 52.44
ATOM    495  OE1 GLN A  74      27.070   9.327 -11.458  1.00 53.72
ATOM    496  NE2 GLN A  74      28.878   8.559 -10.360  1.00 49.79
ATOM    497  N   SER A  75      22.790  10.789  -8.322  1.00 45.63
ATOM    498  CA  SER A  75      21.449  10.390  -7.895  1.00 44.50
ATOM    499  C   SER A  75      20.404  11.361  -8.430  1.00 43.30
ATOM    500  O   SER A  75      19.326  11.528  -7.851  1.00 42.77
ATOM    501  CB  SER A  75      21.377  10.346  -6.365  1.00 44.20
ATOM    502  OG  SER A  75      21.621  11.630  -5.824  1.00 45.64
ATOM    503  N   THR A  76      20.734  12.001  -9.546  1.00 40.94
ATOM    504  CA  THR A  76      19.837  12.964 -10.153  1.00 37.56
ATOM    505  C   THR A  76      19.284  12.487 -11.489  1.00 37.05
ATOM    506  O   THR A  76      19.964  11.803 -12.253  1.00 37.76
ATOM    507  CB  THR A  76      20.553  14.311 -10.335  1.00 35.75
ATOM    508  OG1 THR A  76      20.949  14.804  -9.051  1.00 35.77
ATOM    509  CG2 THR A  76      19.643  15.323 -11.003  1.00 34.08
ATOM    510  N   VAL A  77      18.028  12.842 -11.736  1.00 36.23
ATOM    511  CA  VAL A  77      17.329  12.508 -12.963  1.00 34.85
ATOM    512  C   VAL A  77      16.925  13.828 -13.617  1.00 36.17
ATOM    513  O   VAL A  77      16.323  14.686 -12.971  1.00 33.95
ATOM    514  CB  VAL A  77      16.023  11.699 -12.691  1.00 36.75
ATOM    515  CG1 VAL A  77      15.281  11.470 -13.991  1.00 34.82
ATOM    516  CG2 VAL A  77      16.337  10.358 -12.034  1.00 34.73
ATOM    517  N   VAL A  78      17.276  13.983 -14.892  1.00 37.36
ATOM    518  CA  VAL A  78      16.928  15.162 -15.666  1.00 36.92
ATOM    519  C   VAL A  78      15.768  14.727 -16.550  1.00 36.78
ATOM    520  O   VAL A  78      15.864  13.720 -17.237  1.00 38.57
ATOM    521  CB  VAL A  78      18.101  15.621 -16.569  1.00 38.94
ATOM    522  CG1 VAL A  78      17.708  16.867 -17.360  1.00 34.66
ATOM    523  CG2 VAL A  78      19.323  15.929 -15.712  1.00 42.32
ATOM    524  N   LEU A  79      14.669  15.472 -16.513  1.00 35.74
ATOM    525  CA  LEU A  79      13.490  15.160 -17.321  1.00 33.65
ATOM    526  C   LEU A  79      12.993  16.396 -18.083  1.00 32.77
ATOM    527  O   LEU A  79      12.840  17.475 -17.505  1.00 32.22
ATOM    528  CB  LEU A  79      12.359  14.624 -16.431  1.00 31.76
ATOM    529  CG  LEU A  79      11.068  14.187 -17.138  1.00 36.74
ATOM    530  CD1 LEU A  79      10.276  13.244 -16.251  1.00 39.01
ATOM    531  CD2 LEU A  79      10.227  15.397 -17.479  1.00 38.20
ATOM    532  N   LYS A  80      12.740  16.229 -19.377  1.00 31.45
ATOM    533  CA  LYS A  80      12.239  17.317 -20.214  1.00 32.50
ATOM    534  C   LYS A  80      10.847  17.008 -20.734  1.00 32.06
ATOM    535  O   LYS A  80      10.586  15.908 -21.221  1.00 32.75
ATOM    536  CB  LYS A  80      13.155  17.548 -21.412  1.00 30.80
ATOM    537  CG  LYS A  80      14.475  18.217 -21.085  1.00 36.55
ATOM    538  CD  LYS A  80      14.266  19.680 -20.752  1.00 39.06
ATOM    539  CE  LYS A  80      15.592  20.422 -20.619  1.00 42.31
ATOM    540  NZ  LYS A  80      15.401  21.910 -20.520  1.00 42.19
ATOM    541  N   LEU A  81       9.944  17.972 -20.618  1.00 30.94
ATOM    542  CA  LEU A  81       8.601  17.785 -21.144  1.00 29.49
ATOM    543  C   LEU A  81       8.785  17.770 -22.664  1.00 28.46
ATOM    544  O   LEU A  81       9.426  18.657 -23.225  1.00 26.88
ATOM    545  CB  LEU A  81       7.704  18.944 -20.709  1.00 31.16
ATOM    546  CG  LEU A  81       7.597  19.169 -19.190  1.00 33.51
ATOM    547  CD1 LEU A  81       6.719  20.384 -18.906  1.00 32.35
ATOM    548  CD2 LEU A  81       7.031  17.930 -18.516  1.00 29.15
ATOM    549  N   ASN A  82       8.243  16.757 -23.328  1.00 28.19
ATOM    550  CA  ASN A  82       8.407  16.633 -24.776  1.00 28.66
ATOM    551  C   ASN A  82       7.118  16.174 -25.442  1.00 29.34
ATOM    552  O   ASN A  82       7.159  15.482 -26.450  1.00 30.74
ATOM    553  CB  ASN A  82       9.524  15.618 -25.062  1.00 29.94
ATOM    554  CG  ASN A  82       9.832  15.458 -26.546  1.00 32.31
ATOM    555  OD1 ASN A  82      10.159  14.354 -27.006  1.00 34.68
ATOM    556  ND2 ASN A  82       9.757  16.546 -27.292  1.00 30.02
ATOM    557  N   GLY A  83       5.974  16.562 -24.889  1.00 29.69
ATOM    558  CA  GLY A  83       4.710  16.145 -25.469  1.00 32.38
ATOM    559  C   GLY A  83       4.193  17.078 -26.542  1.00 35.84
ATOM    560  O   GLY A  83       3.272  16.730 -27.297  1.00 36.22
ATOM    561  N   GLY A  84       4.803  18.260 -26.623  1.00 36.79
ATOM    562  CA  GLY A  84       4.370  19.266 -27.577  1.00 39.10
ATOM    563  C   GLY A  84       4.806  19.177 -29.029  1.00 42.11
ATOM    564  O   GLY A  84       5.912  18.737 -29.359  1.00 41.00
ATOM    565  N   LEU A  85       3.910  19.608 -29.907  1.00 43.80
ATOM    566  CA  LEU A  85       4.181  19.620 -31.330  1.00 45.99
ATOM    567  C   LEU A  85       4.436  21.069 -31.720  1.00 48.50
ATOM    568  O   LEU A  85       4.183  21.983 -30.939  1.00 48.80
ATOM    569  CB  LEU A  85       2.986  19.052 -32.084  1.00 44.92
ATOM    570  CG  LEU A  85       2.784  17.549 -31.872  1.00 43.21
ATOM    571  CD1 LEU A  85       1.373  17.147 -32.251  1.00 43.23
ATOM    572  CD2 LEU A  85       3.801  16.789 -32.697  1.00 41.89
ATOM    573  N   GLY A  86       4.965  21.289 -32.912  1.00 51.44
ATOM    574  CA  GLY A  86       5.221  22.656 -33.318  1.00 55.62
ATOM    575  C   GLY A  86       4.017  23.227 -34.034  1.00 58.48
ATOM    576  O   GLY A  86       4.171  24.002 -34.976  1.00 59.34
ATOM    577  N   THR A  87       2.821  22.843 -33.589  1.00 60.24
ATOM    578  CA  THR A  87       1.582  23.298 -34.217  1.00 62.19
ATOM    579  C   THR A  87       1.500  24.809 -34.318  1.00 62.25
ATOM    580  O   THR A  87       1.419  25.358 -35.415  1.00 60.89
ATOM    581  CB  THR A  87       0.335  22.801 -33.453  1.00 63.73
ATOM    582  OG1 THR A  87       0.286  21.371 -33.494  1.00 65.90
ATOM    583  CG2 THR A  87      -0.935  23.353 -34.093  1.00 65.20
ATOM    584  N   GLY A  88       1.511  25.474 -33.167  1.00 63.09
ATOM    585  CA  GLY A  88       1.441  26.923 -33.150  1.00 64.22
ATOM    586  C   GLY A  88       2.463  27.564 -34.070  1.00 64.97
ATOM    587  O   GLY A  88       2.394  28.761 -34.346  1.00 64.52
ATOM    588  N   MET A  89       3.408  26.765 -34.554  1.00 65.91
ATOM    589  CA  MET A  89       4.451  27.261 -35.444  1.00 67.20
ATOM    590  C   MET A  89       4.405  26.580 -36.801  1.00 68.45
ATOM    591  O   MET A  89       5.384  26.593 -37.553  1.00 68.85
ATOM    592  CB  MET A  89       5.820  27.053 -34.800  1.00 67.94
ATOM    593  CG  MET A  89       5.962  27.809 -33.501  1.00 68.90
ATOM    594  SD  MET A  89       7.616  27.482 -32.621  1.00 72.84
ATOM    595  CE  MET A  89       8.817  28.268 -33.920  1.00 65.95
ATOM    596  N   GLY A  90       3.259  25.987 -37.112  1.00 69.02
ATOM    597  CA  GLY A  90       3.105  25.315 -38.385  1.00 71.39
ATOM    598  C   GLY A  90       4.008  24.109 -38.528  1.00 72.53
ATOM    599  O   GLY A  90       4.744  23.979 -39.506  1.00 72.50
ATOM    600  N   LEU A  91       3.952  23.221 -37.546  1.00 73.29
ATOM    601  CA  LEU A  91       4.760  22.015 -37.579  1.00 73.99
ATOM    602  C   LEU A  91       3.969  20.910 -36.904  1.00 72.61
ATOM    603  O   LEU A  91       3.161  21.179 -36.014  1.00 72.23
ATOM    604  CB  LEU A  91       6.082  22.246 -36.850  1.00 76.37
ATOM    605  CG  LEU A  91       7.094  21.106 -36.959  1.00 79.41
ATOM    606  CD1 LEU A  91       7.381  20.811 -38.431  1.00 80.79
ATOM    607  CD2 LEU A  91       8.374  21.483 -36.214  1.00 80.92
ATOM    608  N   CYS A  92       4.178  19.673 -37.337  1.00 71.42
ATOM    609  CA  CYS A  92       3.457  18.551 -36.745  1.00 70.74
ATOM    610  C   CYS A  92       4.419  17.543 -36.156  1.00 68.43
ATOM    611  O   CYS A  92       4.017  16.458 -35.744  1.00 69.85
ATOM    612  CB  CYS A  92       2.556  17.869 -37.783  1.00 72.06
ATOM    613  SG  CYS A  92       1.103  18.847 -38.284  1.00 75.90
ATOM    614  N   ASP A  93       5.694  17.911 -36.117  1.00 64.60
ATOM    615  CA  ASP A  93       6.724  17.044 -35.562  1.00 61.16
ATOM    616  C   ASP A  93       6.934  17.501 -34.125  1.00 57.05
ATOM    617  O   ASP A  93       6.381  18.518 -33.713  1.00 58.31
ATOM    618  CB  ASP A  93       8.028  17.198 -36.360  1.00 63.34
ATOM    619  CG  ASP A  93       8.944  15.982 -36.241  1.00 65.65
ATOM    620  OD1 ASP A  93      10.065  16.027 -36.799  1.00 65.47
ATOM    621  OD2 ASP A  93       8.544  14.983 -35.600  1.00 65.83
ATOM    622  N   ALA A  94       7.727  16.755 -33.367  1.00 52.24
ATOM    623  CA  ALA A  94       8.009  17.106 -31.982  1.00 48.26
ATOM    624  C   ALA A  94       8.712  18.454 -31.902  1.00 47.14
ATOM    625  O   ALA A  94       9.631  18.746 -32.670  1.00 44.83
ATOM    626  CB  ALA A  94       8.867  16.041 -31.341  1.00 47.62
ATOM    627  N   LYS A  95       8.267  19.270 -30.960  1.00 46.63
ATOM    628  CA  LYS A  95       8.815  20.601 -30.743  1.00 46.25
ATOM    629  C   LYS A  95      10.322  20.594 -30.468  1.00 45.80
ATOM    630  O   LYS A  95      11.051  21.461 -30.953  1.00 46.58
ATOM    631  CB  LYS A  95       8.083  21.255 -29.573  1.00 46.28
ATOM    632  CG  LYS A  95       8.565  22.633 -29.219  1.00 45.75
ATOM    633  CD  LYS A  95       8.206  23.630 -30.290  1.00 46.10
ATOM    634  CE  LYS A  95       8.388  25.028 -29.756  1.00 47.34
ATOM    635  NZ  LYS A  95       7.569  25.229 -28.524  1.00 46.21
ATOM    636  N   THR A  96      10.788  19.617 -29.696  1.00 42.85
ATOM    637  CA  THR A  96      12.203  19.535 -29.361  1.00 41.38
ATOM    638  C   THR A  96      13.098  19.157 -30.529  1.00 40.58
ATOM    639  O   THR A  96      14.322  19.268 -30.437  1.00 40.66
ATOM    640  CB  THR A  96      12.449  18.522 -28.252  1.00 40.39
ATOM    641  OG1 THR A  96      11.814  17.284 -28.597  1.00 41.99
ATOM    642  CG2 THR A  96      11.904  19.037 -26.935  1.00 39.27
ATOM    643  N   LEU A  97      12.492  18.707 -31.620  1.00 39.47
ATOM    644  CA  LEU A  97      13.252  18.301 -32.790  1.00 39.29
ATOM    645  C   LEU A  97      13.431  19.474 -33.751  1.00 38.33
ATOM    646  O   LEU A  97      13.920  19.329 -34.867  1.00 36.25
ATOM    647  CB  LEU A  97      12.556  17.118 -33.474  1.00 38.31
ATOM    648  CG  LEU A  97      12.455  15.860 -32.598  1.00 38.80
ATOM    649  CD1 LEU A  97      11.811  14.736 -33.401  1.00 36.60
ATOM    650  CD2 LEU A  97      13.848  15.437 -32.110  1.00 35.58
ATOM    651  N   LEU A  98      13.042  20.652 -33.292  1.00 38.33
ATOM    652  CA  LEU A  98      13.178  21.846 -34.102  1.00 39.76
ATOM    653  C   LEU A  98      14.632  22.315 -34.030  1.00 39.25
ATOM    654  O   LEU A  98      15.225  22.321 -32.948  1.00 36.23
ATOM    655  CB  LEU A  98      12.264  22.927 -33.556  1.00 39.80
ATOM    656  CG  LEU A  98      12.172  24.131 -34.468  1.00 43.75
ATOM    657  CD1 LEU A  98      11.642  23.664 -35.818  1.00 48.21
ATOM    658  CD2 LEU A  98      11.251  25.185 -33.849  1.00 45.27
ATOM    659  N   GLU A  99      15.214  22.696 -35.164  1.00 38.15
ATOM    660  CA  GLU A  99      16.596  23.165 -35.143  1.00 39.34
ATOM    661  C   GLU A  99      16.704  24.527 -34.456  1.00 39.67
ATOM    662  O   GLU A  99      15.984  25.465 -34.799  1.00 39.87
ATOM    663  CB  GLU A  99      17.168  23.295 -36.549  1.00 38.61
ATOM    664  CG  GLU A  99      18.644  23.663 -36.518  1.00 40.70
ATOM    665  CD  GLU A  99      19.054  24.599 -37.638  1.00 40.73
ATOM    666  OE1 GLU A  99      20.266  24.860 -37.767  1.00 40.32
ATOM    667  OE2 GLU A  99      18.173  25.077 -38.385  1.00 44.37
ATOM    668  N   VAL A 100      17.624  24.633 -33.503  1.00 39.26
ATOM    669  CA  VAL A 100      17.828  25.872 -32.757  1.00 40.09
ATOM    670  C   VAL A 100      19.133  26.603 -33.108  1.00 41.17
ATOM    671  O   VAL A 100      19.166  27.833 -33.171  1.00 42.23
ATOM    672  CB  VAL A 100      17.781  25.589 -31.243  1.00 37.84
ATOM    673  CG1 VAL A 100      18.505  26.660 -30.486  1.00 39.27
ATOM    674  CG2 VAL A 100      16.336  25.511 -30.791  1.00 36.72
ATOM    675  N   LYS A 101      20.205  25.853 -33.326  1.00 41.59
ATOM    676  CA  LYS A 101      21.476  26.465 -33.671  1.00 41.28
ATOM    677  C   LYS A 101      22.464  25.501 -34.316  1.00 41.53
ATOM    678  O   LYS A 101      22.662  24.373 -33.856  1.00 39.36
ATOM    679  CB  LYS A 101      22.116  27.101 -32.435  1.00 41.58
ATOM    680  CG  LYS A 101      23.482  27.714 -32.723  1.00 41.99
ATOM    681  CD  LYS A 101      23.990  28.552 -31.567  1.00 43.94
ATOM    682  CE  LYS A 101      23.148  29.805 -31.365  1.00 45.04
ATOM    683  NZ  LYS A 101      23.183  30.733 -32.535  1.00 44.11
ATOM    684  N   ASP A 102      23.075  25.975 -35.396  1.00 42.22
ATOM    685  CA  ASP A 102      24.067  25.223 -36.157  1.00 41.96
ATOM    686  C   ASP A 102      23.711  23.750 -36.359  1.00 41.73
ATOM    687  O   ASP A 102      24.532  22.859 -36.120  1.00 41.11
ATOM    688  CB  ASP A 102      25.443  25.358 -35.489  1.00 43.06
ATOM    689  CG  ASP A 102      25.884  26.819 -35.339  1.00 44.90
ATOM    690  OD1 ASP A 102      25.859  27.570 -36.341  1.00 46.67
ATOM    691  OD2 ASP A 102      26.261  27.218 -34.217  1.00 45.91
ATOM    692  N   GLY A 103      22.481  23.504 -36.801  1.00 40.77
ATOM    693  CA  GLY A 103      22.040  22.144 -37.051  1.00 40.61
ATOM    694  C   GLY A 103      21.616  21.362 -35.826  1.00 40.18
ATOM    695  O   GLY A 103      21.158  20.231 -35.938  1.00 39.28
ATOM    696  N   LYS A 104      21.767  21.953 -34.649  1.00 40.64
ATOM    697  CA  LYS A 104      21.367  21.270 -33.433  1.00 40.16
ATOM    698  C   LYS A 104      19.943  21.669 -33.016  1.00 40.26
ATOM    699  O   LYS A 104      19.531  22.824 -33.178  1.00 38.34
ATOM    700  CB  LYS A 104      22.365  21.575 -32.315  1.00 42.87
ATOM    701  CG  LYS A 104      23.743  20.945 -32.518  1.00 46.11
ATOM    702  CD  LYS A 104      24.731  21.428 -31.455  1.00 49.95
ATOM    703  CE  LYS A 104      26.066  20.686 -31.525  1.00 52.54
ATOM    704  NZ  LYS A 104      26.779  20.839 -32.831  1.00 54.52
ATOM    705  N   THR A 105      19.201  20.694 -32.493  1.00 38.72
ATOM    706  CA  THR A 105      17.827  20.890 -32.039  1.00 35.42
ATOM    707  C   THR A 105      17.856  21.075 -30.531  1.00 35.26
ATOM    708  O   THR A 105      18.925  21.016 -29.927  1.00 33.04
ATOM    709  CB  THR A 105      16.963  19.650 -32.334  1.00 36.66
ATOM    710  OG1 THR A 105      17.475  18.533 -31.588  1.00 37.70
ATOM    711  CG2 THR A 105      16.992  19.312 -33.822  1.00 33.49
ATOM    712  N   PHE A 106      16.690  21.291 -29.922  1.00 35.11
ATOM    713  CA  PHE A 106      16.635  21.445 -28.472  1.00 35.18
ATOM    714  C   PHE A 106      17.157  20.152 -27.871  1.00 36.39
ATOM    715  O   PHE A 106      18.021  20.157 -26.984  1.00 36.84
ATOM    716  CB  PHE A 106      15.201  21.652 -27.967  1.00 35.02
ATOM    717  CG  PHE A 106      14.563  22.942 -28.410  1.00 35.23
ATOM    718  CD1 PHE A 106      13.731  22.979 -29.522  1.00 34.40
ATOM    719  CD2 PHE A 106      14.775  24.117 -27.700  1.00 34.73
ATOM    720  CE1 PHE A 106      13.117  24.174 -29.918  1.00 33.78
ATOM    721  CE2 PHE A 106      14.169  25.309 -28.090  1.00 33.81
ATOM    722  CZ  PHE A 106      13.337  25.334 -29.199  1.00 33.26
ATOM    723  N   LEU A 107      16.629  19.040 -28.372  1.00 35.28
ATOM    724  CA  LEU A 107      17.013  17.725 -27.882  1.00 35.69
ATOM    725  C   LEU A 107      18.529  17.498 -27.925  1.00 35.19
ATOM    726  O   LEU A 107      19.101  17.003 -26.960  1.00 35.00
ATOM    727  CB  LEU A 107      16.277  16.639 -28.677  1.00 34.39
ATOM    728  CG  LEU A 107      16.435  15.206 -28.172  1.00 35.43
ATOM    729  CD1 LEU A 107      16.130  15.139 -26.679  1.00 36.82
ATOM    730  CD2 LEU A 107      15.509  14.285 -28.966  1.00 38.35
ATOM    731  N   ASP A 108      19.178  17.857 -29.033  1.00 35.80
ATOM    732  CA  ASP A 108      20.633  17.692 -29.145  1.00 35.70
ATOM    733  C   ASP A 108      21.353  18.331 -27.955  1.00 36.15
ATOM    734  O   ASP A 108      22.221  17.717 -27.328  1.00 35.99
ATOM    735  CB  ASP A 108      21.165  18.342 -30.425  1.00 35.08
ATOM    736  CG  ASP A 108      20.937  17.497 -31.655  1.00 35.09
ATOM    737  OD1 ASP A 108      21.496  16.383 -31.720  1.00 36.53
ATOM    738  OD2 ASP A 108      20.204  17.950 -32.562  1.00 35.98
ATOM    739  N   PHE A 109      20.985  19.571 -27.651  1.00 35.69
ATOM    740  CA  PHE A 109      21.614  20.290 -26.561  1.00 36.17
ATOM    741  C   PHE A 109      21.427  19.649 -25.204  1.00 35.80
ATOM    742  O   PHE A 109      22.390  19.548 -24.441  1.00 37.93
ATOM    743  CB  PHE A 109      21.153  21.750 -26.544  1.00 37.77
ATOM    744  CG  PHE A 109      21.800  22.588 -27.610  1.00 40.85
ATOM    745  CD1 PHE A 109      21.042  23.158 -28.628  1.00 40.11
ATOM    746  CD2 PHE A 109      23.185  22.775 -27.617  1.00 41.77
ATOM    747  CE1 PHE A 109      21.649  23.896 -29.639  1.00 41.98
ATOM    748  CE2 PHE A 109      23.803  23.511 -28.623  1.00 42.23
ATOM    749  CZ  PHE A 109      23.032  24.073 -29.639  1.00 44.15
ATOM    750  N   THR A 110      20.214  19.213 -24.882  1.00 33.46
ATOM    751  CA  THR A 110      20.018  18.561 -23.591  1.00 33.06
ATOM    752  C   THR A 110      20.778  17.240 -23.576  1.00 32.73
ATOM    753  O   THR A 110      21.453  16.929 -22.597  1.00 32.81
ATOM    754  CB  THR A 110      18.558  18.246 -23.294  1.00 32.06
ATOM    755  OG1 THR A 110      17.802  19.461 -23.289  1.00 35.89
ATOM    756  CG2 THR A 110      18.447  17.566 -21.923  1.00 31.11
ATOM    757  N   ALA A 111      20.662  16.460 -24.652  1.00 30.87
ATOM    758  CA  ALA A 111      21.383  15.190 -24.726  1.00 31.41
ATOM    759  C   ALA A 111      22.889  15.424 -24.584  1.00 31.78
ATOM    760  O   ALA A 111      23.573  14.662 -23.906  1.00 34.11
ATOM    761  CB  ALA A 111      21.098  14.479 -26.035  1.00 27.43
ATOM    762  N   LEU A 112      23.401  16.481 -25.209  1.00 31.38
ATOM    763  CA  LEU A 112      24.833  16.769 -25.132  1.00 33.12
ATOM    764  C   LEU A 112      25.223  17.300 -23.758  1.00 34.64
ATOM    765  O   LEU A 112      26.329  17.040 -23.274  1.00 35.84
ATOM    766  CB  LEU A 112      25.238  17.763 -26.222  1.00 29.15
ATOM    767  CG  LEU A 112      25.098  17.175 -27.626  1.00 31.35
ATOM    768  CD1 LEU A 112      25.092  18.275 -28.679  1.00 28.47
ATOM    769  CD2 LEU A 112      26.227  16.187 -27.863  1.00 26.02
ATOM    770  N   GLN A 113      24.319  18.045 -23.126  1.00 32.79
ATOM    771  CA  GLN A 113      24.609  18.563 -21.804  1.00 33.23
ATOM    772  C   GLN A 113      24.744  17.365 -20.873  1.00 35.50
ATOM    773  O   GLN A 113      25.680  17.280 -20.072  1.00 36.83
ATOM    774  CB  GLN A 113      23.486  19.488 -21.334  1.00 32.70
ATOM    775  CG  GLN A 113      23.566  20.895 -21.904  1.00 30.95
ATOM    776  CD  GLN A 113      22.236  21.615 -21.821  1.00 32.42
ATOM    777  OE1 GLN A 113      21.408  21.296 -20.973  1.00 31.30
ATOM    778  NE2 GLN A 113      22.028  22.596 -22.696  1.00 31.00
ATOM    779  N   VAL A 114      23.812  16.431 -21.013  1.00 36.93
ATOM    780  CA  VAL A 114      23.785  15.216 -20.219  1.00 40.39
ATOM    781  C   VAL A 114      25.055  14.400 -20.416  1.00 41.71
ATOM    782  O   VAL A 114      25.710  14.013 -19.447  1.00 42.15
ATOM    783  CB  VAL A 114      22.567  14.360 -20.604  1.00 41.82
ATOM    784  CG1 VAL A 114      22.672  12.975 -19.991  1.00 42.54
ATOM    785  CG2 VAL A 114      21.299  15.053 -20.140  1.00 41.82
ATOM    786  N   GLN A 115      25.394  14.143 -21.676  1.00 44.22
ATOM    787  CA  GLN A 115      26.585  13.369 -22.024  1.00 44.85
ATOM    788  C   GLN A 115      27.821  13.991 -21.390  1.00 45.13
ATOM    789  O   GLN A 115      28.695  13.290 -20.884  1.00 45.66
ATOM    790  CB  GLN A 115      26.759  13.321 -23.543  1.00 43.03
ATOM    791  CG  GLN A 115      27.973  12.540 -24.005  1.00 45.62
ATOM    792  CD  GLN A 115      28.222  12.658 -25.514  1.00 49.98
ATOM    793  OE1 GLN A 115      27.416  12.206 -26.337  1.00 49.17
ATOM    794  NE2 GLN A 115      29.347  13.276 -25.878  1.00 52.09
ATOM    795  N   TYR A 116      27.880  15.316 -21.419  1.00 45.20
ATOM    796  CA  TYR A 116      29.003  16.041 -20.850  1.00 45.14
ATOM    797  C   TYR A 116      29.105  15.829 -19.337  1.00 45.13
ATOM    798  O   TYR A 116      30.196  15.651 -18.804  1.00 45.27
ATOM    799  CB  TYR A 116      28.873  17.534 -21.181  1.00 44.55
ATOM    800  CG  TYR A 116      30.044  18.356 -20.711  1.00 46.96
ATOM    801  CD1 TYR A 116      30.140  18.773 -19.383  1.00 47.32
ATOM    802  CD2 TYR A 116      31.098  18.657 -21.577  1.00 48.55
ATOM    803  CE1 TYR A 116      31.259  19.463 -18.929  1.00 49.27
ATOM    804  CE2 TYR A 116      32.225  19.346 -21.133  1.00 48.77
ATOM    805  CZ  TYR A 116      32.301  19.741 -19.809  1.00 49.99
ATOM    806  OH  TYR A 116      33.432  20.377 -19.353  1.00 52.23
ATOM    807  N   LEU A 117      27.970  15.850 -18.646  1.00 45.93
ATOM    808  CA  LEU A 117      27.957  15.649 -17.198  1.00 47.01
ATOM    809  C   LEU A 117      28.300  14.200 -16.848  1.00 46.70
ATOM    810  O   LEU A 117      28.908  13.922 -15.807  1.00 45.37
ATOM    811  CB  LEU A 117      26.583  16.025 -16.618  1.00 45.82
ATOM    812  CG  LEU A 117      26.269  17.523 -16.678  1.00 46.23
ATOM    813  CD1 LEU A 117      24.836  17.796 -16.239  1.00 44.99
ATOM    814  CD2 LEU A 117      27.254  18.267 -15.793  1.00 45.57
ATOM    815  N   ARG A 118      27.913  13.283 -17.728  1.00 45.94
ATOM    816  CA  ARG A 118      28.186  11.870 -17.524  1.00 48.93
ATOM    817  C   ARG A 118      29.664  11.522 -17.656  1.00 51.11
ATOM    818  O   ARG A 118      30.123  10.550 -17.062  1.00 51.75
ATOM    819  CB  ARG A 118      27.395  11.027 -18.521  1.00 48.61
ATOM    820  CG  ARG A 118      25.920  10.910 -18.207  1.00 50.88
ATOM    821  CD  ARG A 118      25.273   9.831 -19.049  1.00 48.08
ATOM    822  NE  ARG A 118      23.895   9.602 -18.648  1.00 47.97
ATOM    823  CZ  ARG A 118      23.117   8.661 -19.170  1.00 50.01
ATOM    824  NH1 ARG A 118      23.587   7.859 -20.116  1.00 49.14
ATOM    825  NH2 ARG A 118      21.867   8.524 -18.749  1.00 50.05
ATOM    826  N   GLN A 119      30.405  12.308 -18.433  1.00 53.00
ATOM    827  CA  GLN A 119      31.825  12.047 -18.638  1.00 56.29
ATOM    828  C   GLN A 119      32.730  12.849 -17.710  1.00 57.21
ATOM    829  O   GLN A 119      33.872  12.467 -17.471  1.00 58.64
ATOM    830  CB  GLN A 119      32.205  12.335 -20.092  1.00 56.45
ATOM    831  CG  GLN A 119      31.217  11.759 -21.090  1.00 60.47
ATOM    832  CD  GLN A 119      31.603  12.029 -22.534  1.00 63.37
ATOM    833  OE1 GLN A 119      31.979  13.146 -22.891  1.00 63.24
ATOM    834  NE2 GLN A 119      31.497  11.003 -23.378  1.00 63.92
ATOM    835  N   HIS A 120      32.223  13.954 -17.181  1.00 57.55
ATOM    836  CA  HIS A 120      33.024  14.788 -16.298  1.00 58.45
ATOM    837  C   HIS A 120      32.585  14.786 -14.845  1.00 58.92
ATOM    838  O   HIS A 120      33.381  15.111 -13.970  1.00 59.38
ATOM    839  CB  HIS A 120      33.030  16.244 -16.781  1.00 59.86
ATOM    840  CG  HIS A 120      33.838  16.475 -18.017  1.00 60.71
ATOM    841  ND1 HIS A 120      33.527  15.900 -19.230  1.00 62.36
ATOM    842  CD2 HIS A 120      34.938  17.234 -18.231  1.00 63.11
ATOM    843  CE1 HIS A 120      34.399  16.297 -20.140  1.00 63.55
ATOM    844  NE2 HIS A 120      35.266  17.107 -19.559  1.00 64.15
ATOM    845  N   CYS A 121      31.336  14.425 -14.572  1.00 59.57
ATOM    846  CA  CYS A 121      30.861  14.467 -13.194  1.00 60.29
ATOM    847  C   CYS A 121      30.160  13.233 -12.661  1.00 60.53
ATOM    848  O   CYS A 121      30.465  12.770 -11.565  1.00 59.92
ATOM    849  CB  CYS A 121      29.919  15.660 -13.007  1.00 60.81
ATOM    850  SG  CYS A 121      30.602  17.250 -13.498  1.00 63.98
ATOM    851  N   SER A 122      29.213  12.705 -13.424  1.00 61.51
ATOM    852  CA  SER A 122      28.452  11.556 -12.965  1.00 61.94
ATOM    853  C   SER A 122      27.931  10.712 -14.109  1.00 62.16
ATOM    854  O   SER A 122      27.002  11.112 -14.811  1.00 62.02
ATOM    855  CB  SER A 122      27.282  12.051 -12.126  1.00 64.41
ATOM    856  OG  SER A 122      26.556  13.044 -12.837  1.00 66.04
ATOM    857  N   GLU A 123      28.519   9.535 -14.284  1.00 62.65
ATOM    858  CA  GLU A 123      28.113   8.642 -15.357  1.00 62.34
ATOM    859  C   GLU A 123      26.738   8.028 -15.103  1.00 59.70
ATOM    860  O   GLU A 123      26.183   7.358 -15.972  1.00 58.88
ATOM    861  CB  GLU A 123      29.159   7.532 -15.562  1.00 65.44
ATOM    862  CG  GLU A 123      29.400   6.597 -14.370  1.00 71.11
ATOM    863  CD  GLU A 123      30.392   7.151 -13.343  1.00 75.94
ATOM    864  OE1 GLU A 123      30.803   6.384 -12.437  1.00 77.51
ATOM    865  OE2 GLU A 123      30.761   8.345 -13.436  1.00 76.71
ATOM    866  N   HIS A 124      26.185   8.271 -13.918  1.00 56.72
ATOM    867  CA  HIS A 124      24.880   7.724 -13.568  1.00 54.55
ATOM    868  C   HIS A 124      23.735   8.725 -13.672  1.00 52.90
ATOM    869  O   HIS A 124      22.591   8.393 -13.364  1.00 51.24
ATOM    870  CB  HIS A 124      24.924   7.139 -12.159  1.00 57.18
ATOM    871  CG  HIS A 124      25.809   5.941 -12.037  1.00 59.98
ATOM    872  ND1 HIS A 124      25.531   4.746 -12.665  1.00 61.96
ATOM    873  CD2 HIS A 124      26.987   5.763 -11.396  1.00 62.04
ATOM    874  CE1 HIS A 124      26.500   3.885 -12.418  1.00 61.50
ATOM    875  NE2 HIS A 124      27.396   4.476 -11.650  1.00 62.94
ATOM    876  N   LEU A 125      24.039   9.946 -14.102  1.00 50.42
ATOM    877  CA  LEU A 125      23.004  10.963 -14.255  1.00 48.75
ATOM    878  C   LEU A 125      21.953  10.439 -15.226  1.00 46.36
ATOM    879  O   LEU A 125      22.263  10.111 -16.366  1.00 46.00
ATOM    880  CB  LEU A 125      23.604  12.259 -14.801  1.00 48.76
ATOM    881  CG  LEU A 125      22.608  13.398 -15.020  1.00 48.18
ATOM    882  CD1 LEU A 125      21.933  13.740 -13.706  1.00 49.40
ATOM    883  CD2 LEU A 125      23.321  14.607 -15.573  1.00 49.02
ATOM    884  N   ARG A 126      20.709  10.361 -14.778  1.00 45.37
ATOM    885  CA  ARG A 126      19.643   9.853 -15.631  1.00 45.59
ATOM    886  C   ARG A 126      18.965  10.954 -16.469  1.00 43.10
ATOM    887  O   ARG A 126      18.766  12.069 -16.002  1.00 44.19
ATOM    888  CB  ARG A 126      18.611   9.121 -14.764  1.00 46.33
ATOM    889  CG  ARG A 126      17.559   8.363 -15.560  1.00 52.06
ATOM    890  CD  ARG A 126      18.175   7.215 -16.340  1.00 54.52
ATOM    891  NE  ARG A 126      18.566   6.124 -15.455  1.00 58.91
ATOM    892  CZ  ARG A 126      17.711   5.278 -14.889  1.00 60.40
ATOM    893  NH1 ARG A 126      16.408   5.390 -15.117  1.00 62.00
ATOM    894  NH2 ARG A 126      18.157   4.323 -14.087  1.00 61.01
ATOM    895  N   PHE A 127      18.618  10.632 -17.710  1.00 41.06
ATOM    896  CA  PHE A 127      17.953  11.585 -18.601  1.00 38.88
ATOM    897  C   PHE A 127      16.630  11.018 -19.122  1.00 37.48
ATOM    898  O   PHE A 127      16.608  10.011 -19.818  1.00 38.52
ATOM    899  CB  PHE A 127      18.882  11.938 -19.775  1.00 37.29
ATOM    900  CG  PHE A 127      18.230  12.761 -20.865  1.00 37.82
ATOM    901  CD1 PHE A 127      17.275  13.733 -20.569  1.00 34.57
ATOM    902  CD2 PHE A 127      18.627  12.606 -22.195  1.00 36.60
ATOM    903  CE1 PHE A 127      16.734  14.532 -21.577  1.00 33.78
ATOM    904  CE2 PHE A 127      18.088  13.405 -23.203  1.00 33.21
ATOM    905  CZ  PHE A 127      17.143  14.368 -22.893  1.00 31.85
ATOM    906  N   MET A 128      15.525  11.671 -18.784  1.00 36.46
ATOM    907  CA  MET A 128      14.216  11.212 -19.226  1.00 34.35
ATOM    908  C   MET A 128      13.458  12.219 -20.104  1.00 33.40
ATOM    909  O   MET A 128      13.718  13.424 -20.064  1.00 31.12
ATOM    910  CB  MET A 128      13.374  10.846 -18.007  1.00 34.60
ATOM    911  CG  MET A 128      13.909   9.663 -17.224  1.00 37.93
ATOM    912  SD  MET A 128      12.705   9.116 -15.810  1.00 46.57
ATOM    913  CE  MET A 128      11.315   8.414 -16.944  1.00 42.65
ATOM    914  N   LEU A 129      12.523  11.705 -20.899  1.00 32.16
ATOM    915  CA  LEU A 129      11.702  12.519 -21.795  1.00 32.32
ATOM    916  C   LEU A 129      10.242  12.143 -21.619  1.00 33.88
ATOM    917  O   LEU A 129       9.886  10.966 -21.692  1.00 35.66
ATOM    918  CB  LEU A 129      12.082  12.279 -23.263  1.00 29.00
ATOM    919  CG  LEU A 129      13.435  12.814 -23.746  1.00 30.45
ATOM    920  CD1 LEU A 129      13.860  12.126 -25.063  1.00 26.52
ATOM    921  CD2 LEU A 129      13.332  14.323 -23.922  1.00 28.83
ATOM    922  N   MET A 130       9.387  13.126 -21.373  1.00 35.37
ATOM    923  CA  MET A 130       7.979  12.809 -21.246  1.00 38.34
ATOM    924  C   MET A 130       7.358  13.017 -22.612  1.00 37.58
ATOM    925  O   MET A 130       7.262  14.141 -23.102  1.00 36.57
ATOM    926  CB  MET A 130       7.273  13.691 -20.230  1.00 39.40
ATOM    927  CG  MET A 130       5.876  13.179 -19.951  1.00 48.64
ATOM    928  SD  MET A 130       4.791  14.368 -18.912  1.00 66.14
ATOM    929  CE  MET A 130       4.117  15.445 -20.373  1.00 50.34
ATOM    930  N   ASP A 131       6.947  11.916 -23.225  1.00 37.01
ATOM    931  CA  ASP A 131       6.351  11.964 -24.544  1.00 38.40
ATOM    932  C   ASP A 131       4.860  11.713 -24.514  1.00 38.20
ATOM    933  O   ASP A 131       4.289  11.367 -23.480  1.00 38.36
ATOM    934  CB  ASP A 131       6.991  10.918 -25.457  1.00 38.37
ATOM    935  CG  ASP A 131       8.482  11.099 -25.595  1.00 41.36
ATOM    936  OD1 ASP A 131       8.943  12.260 -25.499  1.00 43.10
ATOM    937  OD2 ASP A 131       9.187  10.087 -25.819  1.00 40.00
ATOM    938  N   SER A 132       4.247  11.900 -25.677  1.00 38.23
ATOM    939  CA  SER A 132       2.829  11.666 -25.878  1.00 37.68
ATOM    940  C   SER A 132       2.788  10.743 -27.082  1.00 40.01
ATOM    941  O   SER A 132       3.828  10.430 -27.672  1.00 39.05
ATOM    942  CB  SER A 132       2.098  12.968 -26.198  1.00 35.15
ATOM    943  OG  SER A 132       2.633  13.570 -27.356  1.00 36.46
ATOM    944  N   PHE A 133       1.595  10.294 -27.443  1.00 42.07
ATOM    945  CA  PHE A 133       1.451   9.414 -28.587  1.00 42.34
ATOM    946  C   PHE A 133       1.951  10.142 -29.831  1.00 40.66
ATOM    947  O   PHE A 133       2.417   9.530 -30.780  1.00 40.98
ATOM    948  CB  PHE A 133      -0.017   9.032 -28.772  1.00 47.95
ATOM    949  CG  PHE A 133      -0.271   8.214 -30.001  1.00 53.87
ATOM    950  CD1 PHE A 133       0.046   6.855 -30.028  1.00 55.36
ATOM    951  CD2 PHE A 133      -0.762   8.816 -31.159  1.00 56.02
ATOM    952  CE1 PHE A 133      -0.119   6.108 -31.194  1.00 57.47
ATOM    953  CE2 PHE A 133      -0.929   8.076 -32.332  1.00 58.42
ATOM    954  CZ  PHE A 133      -0.604   6.717 -32.348  1.00 57.71
ATOM    955  N   ASN A 134       1.862  11.461 -29.813  1.00 40.07
ATOM    956  CA  ASN A 134       2.281  12.271 -30.948  1.00 39.68
ATOM    957  C   ASN A 134       3.785  12.524 -31.129  1.00 39.06
ATOM    958  O   ASN A 134       4.224  12.836 -32.233  1.00 40.21
ATOM    959  CB  ASN A 134       1.565  13.619 -30.887  1.00 40.30
ATOM    960  CG  ASN A 134       0.077  13.499 -31.138  1.00 42.61
ATOM    961  OD1 ASN A 134      -0.694  14.391 -30.789  1.00 43.63
ATOM    962  ND2 ASN A 134      -0.334  12.402 -31.761  1.00 42.83
ATOM    963  N   THR A 135       4.576  12.389 -30.071  1.00 36.32
ATOM    964  CA  THR A 135       6.003  12.668 -30.175  1.00 34.55
ATOM    965  C   THR A 135       6.910  11.467 -29.969  1.00 35.68
ATOM    966  O   THR A 135       8.109  11.518 -30.263  1.00 34.34
ATOM    967  CB  THR A 135       6.394  13.707 -29.151  1.00 35.45
ATOM    968  OG1 THR A 135       6.219  13.158 -27.838  1.00 35.20
ATOM    969  CG2 THR A 135       5.510  14.937 -29.294  1.00 34.99
ATOM    970  N   SER A 136       6.336  10.386 -29.465  1.00 35.09
ATOM    971  CA  SER A 136       7.102   9.182 -29.192  1.00 36.64
ATOM    972  C   SER A 136       7.935   8.657 -30.368  1.00 37.15
ATOM    973  O   SER A 136       9.166   8.645 -30.302  1.00 37.47
ATOM    974  CB  SER A 136       6.164   8.088 -28.694  1.00 36.34
ATOM    975  OG  SER A 136       6.882   7.114 -27.981  1.00 37.65
ATOM    976  N   ALA A 137       7.261   8.232 -31.437  1.00 36.72
ATOM    977  CA  ALA A 137       7.926   7.671 -32.612  1.00 36.38
ATOM    978  C   ALA A 137       9.033   8.552 -33.178  1.00 37.16
ATOM    979  O   ALA A 137      10.148   8.084 -33.419  1.00 37.24
ATOM    980  CB  ALA A 137       6.897   7.364 -33.692  1.00 32.81
ATOM    981  N   SER A 138       8.721   9.824 -33.397  1.00 37.43
ATOM    982  CA  SER A 138       9.700  10.768 -33.921  1.00 38.81
ATOM    983  C   SER A 138      10.896  10.962 -32.984  1.00 37.76
ATOM    984  O   SER A 138      12.023  11.158 -33.437  1.00 38.69
ATOM    985  CB  SER A 138       9.046  12.127 -34.172  1.00 39.18
ATOM    986  OG  SER A 138       8.795  12.320 -35.549  1.00 45.74
ATOM    987  N   THR A 139      10.642  10.921 -31.682  1.00 35.16
ATOM    988  CA  THR A 139      11.697  11.116 -30.704  1.00 35.51
ATOM    989  C   THR A 139      12.625   9.919 -30.727  1.00 37.04
ATOM    990  O   THR A 139      13.844  10.067 -30.751  1.00 34.84
ATOM    991  CB  THR A 139      11.108  11.298 -29.284  1.00 35.44
ATOM    992  OG1 THR A 139      10.329  12.498 -29.246  1.00 36.37
ATOM    993  CG2 THR A 139      12.205  11.379 -28.247  1.00 29.64
ATOM    994  N   LYS A 140      12.025   8.731 -30.735  1.00 38.48
ATOM    995  CA  LYS A 140      12.767   7.481 -30.766  1.00 37.74
ATOM    996  C   LYS A 140      13.656   7.364 -32.000  1.00 36.00
ATOM    997  O   LYS A 140      14.832   7.054 -31.887  1.00 36.28
ATOM    998  CB  LYS A 140      11.798   6.294 -30.717  1.00 40.28
ATOM    999  CG  LYS A 140      12.484   4.941 -30.600  1.00 40.00
ATOM   1000  CD  LYS A 140      11.486   3.840 -30.325  1.00 41.51
ATOM   1001  CE  LYS A 140      12.193   2.507 -30.156  1.00 42.83
ATOM   1002  NZ  LYS A 140      11.226   1.384 -29.979  1.00 49.23
ATOM   1003  N   SER A 141      13.103   7.611 -33.179  1.00 35.99
ATOM   1004  CA  SER A 141      13.912   7.492 -34.383  1.00 37.62
ATOM   1005  C   SER A 141      14.989   8.573 -34.464  1.00 38.28
ATOM   1006  O   SER A 141      16.007   8.392 -35.139  1.00 40.09
ATOM   1007  CB  SER A 141      13.030   7.505 -35.641  1.00 36.33
ATOM   1008  OG  SER A 141      12.357   8.733 -35.817  1.00 40.48
ATOM   1009  N   PHE A 142      14.778   9.691 -33.774  1.00 37.29
ATOM   1010  CA  PHE A 142      15.772  10.759 -33.777  1.00 36.95
ATOM   1011  C   PHE A 142      16.982  10.289 -32.973  1.00 36.21
ATOM   1012  O   PHE A 142      18.117  10.330 -33.446  1.00 37.60
ATOM   1013  CB  PHE A 142      15.219  12.038 -33.133  1.00 35.37
ATOM   1014  CG  PHE A 142      16.246  13.135 -32.999  1.00 33.50
ATOM   1015  CD1 PHE A 142      16.510  13.994 -34.057  1.00 32.64
ATOM   1016  CD2 PHE A 142      16.986  13.270 -31.828  1.00 33.39
ATOM   1017  CE1 PHE A 142      17.502  14.972 -33.955  1.00 33.85
ATOM   1018  CE2 PHE A 142      17.983  14.243 -31.712  1.00 34.71
ATOM   1019  CZ  PHE A 142      18.242  15.095 -32.780  1.00 34.30
ATOM   1020  N   LEU A 143      16.727   9.854 -31.747  1.00 35.10
ATOM   1021  CA  LEU A 143      17.787   9.384 -30.869  1.00 38.80
ATOM   1022  C   LEU A 143      18.494   8.172 -31.490  1.00 40.69
ATOM   1023  O   LEU A 143      19.721   8.064 -31.433  1.00 39.68
ATOM   1024  CB  LEU A 143      17.208   9.032 -29.493  1.00 35.06
ATOM   1025  CG  LEU A 143      16.624  10.240 -28.750  1.00 34.83
ATOM   1026  CD1 LEU A 143      15.748   9.767 -27.612  1.00 34.04
ATOM   1027  CD2 LEU A 143      17.753  11.142 -28.244  1.00 32.61
ATOM   1028  N   LYS A 144      17.718   7.280 -32.101  1.00 40.37
ATOM   1029  CA  LYS A 144      18.289   6.100 -32.727  1.00 42.33
ATOM   1030  C   LYS A 144      19.384   6.511 -33.705  1.00 43.89
ATOM   1031  O   LYS A 144      20.438   5.882 -33.782  1.00 45.32
ATOM   1032  CB  LYS A 144      17.205   5.323 -33.470  1.00 42.74
ATOM   1033  CG  LYS A 144      17.671   4.003 -34.041  1.00 41.41
ATOM   1034  CD  LYS A 144      16.549   3.337 -34.807  1.00 44.05
ATOM   1035  CE  LYS A 144      17.027   2.098 -35.550  1.00 42.90
ATOM   1036  NZ  LYS A 144      15.900   1.477 -36.306  1.00 45.61
ATOM   1037  N   ALA A 145      19.133   7.587 -34.439  1.00 43.34
ATOM   1038  CA  ALA A 145      20.090   8.071 -35.411  1.00 42.41
ATOM   1039  C   ALA A 145      21.221   8.929 -34.841  1.00 44.54
ATOM   1040  O   ALA A 145      22.344   8.875 -35.352  1.00 45.32
ATOM   1041  CB  ALA A 145      19.360   8.846 -36.493  1.00 40.44
ATOM   1042  N   ARG A 146      20.947   9.700 -33.787  1.00 43.15
ATOM   1043  CA  ARG A 146      21.962  10.606 -33.232  1.00 43.53
ATOM   1044  C   ARG A 146      22.544  10.295 -31.866  1.00 42.45
ATOM   1045  O   ARG A 146      23.623  10.781 -31.530  1.00 43.91
ATOM   1046  CB  ARG A 146      21.412  12.030 -33.157  1.00 44.51
ATOM   1047  CG  ARG A 146      20.760  12.529 -34.414  1.00 48.23
ATOM   1048  CD  ARG A 146      21.753  12.625 -35.533  1.00 51.06
ATOM   1049  NE  ARG A 146      21.377  13.678 -36.469  1.00 56.46
ATOM   1050  CZ  ARG A 146      21.245  14.954 -36.129  1.00 56.46
ATOM   1051  NH1 ARG A 146      21.459  15.329 -34.873  1.00 57.61
ATOM   1052  NH2 ARG A 146      20.908  15.856 -37.044  1.00 57.11
ATOM   1053  N   TYR A 147      21.821   9.531 -31.061  1.00 41.68
ATOM   1054  CA  TYR A 147      22.287   9.201 -29.725  1.00 40.03
ATOM   1055  C   TYR A 147      21.923   7.761 -29.402  1.00 41.51
ATOM   1056  O   TYR A 147      20.994   7.494 -28.640  1.00 41.60
ATOM   1057  CB  TYR A 147      21.670  10.164 -28.694  1.00 38.20
ATOM   1058  CG  TYR A 147      22.042  11.623 -28.931  1.00 35.78
ATOM   1059  CD1 TYR A 147      21.227  12.454 -29.695  1.00 32.19
ATOM   1060  CD2 TYR A 147      23.272  12.133 -28.490  1.00 35.06
ATOM   1061  CE1 TYR A 147      21.625  13.750 -30.031  1.00 33.33
ATOM   1062  CE2 TYR A 147      23.684  13.427 -28.821  1.00 33.69
ATOM   1063  CZ  TYR A 147      22.854  14.231 -29.597  1.00 36.60
ATOM   1064  OH  TYR A 147      23.258  15.497 -29.966  1.00 35.73
ATOM   1065  N   PRO A 148      22.665   6.805 -29.981  1.00 41.94
ATOM   1066  CA  PRO A 148      22.435   5.371 -29.772  1.00 42.25
ATOM   1067  C   PRO A 148      22.452   4.962 -28.306  1.00 42.29
ATOM   1068  O   PRO A 148      21.750   4.037 -27.908  1.00 43.83
ATOM   1069  CB  PRO A 148      23.570   4.715 -30.563  1.00 42.48
ATOM   1070  CG  PRO A 148      23.869   5.714 -31.640  1.00 41.54
ATOM   1071  CD  PRO A 148      23.802   7.027 -30.892  1.00 41.85
ATOM   1072  N   TRP A 149      23.256   5.645 -27.499  1.00 42.61
ATOM   1073  CA  TRP A 149      23.327   5.307 -26.085  1.00 43.47
ATOM   1074  C   TRP A 149      22.028   5.592 -25.350  1.00 43.46
ATOM   1075  O   TRP A 149      21.782   5.046 -24.280  1.00 45.38
ATOM   1076  CB  TRP A 149      24.481   6.045 -25.397  1.00 44.15
ATOM   1077  CG  TRP A 149      24.597   7.500 -25.740  1.00 45.62
ATOM   1078  CD1 TRP A 149      25.098   8.034 -26.894  1.00 45.07
ATOM   1079  CD2 TRP A 149      24.238   8.609 -24.904  1.00 45.81
ATOM   1080  NE1 TRP A 149      25.080   9.409 -26.826  1.00 46.62
ATOM   1081  CE2 TRP A 149      24.556   9.789 -25.617  1.00 45.53
ATOM   1082  CE3 TRP A 149      23.678   8.721 -23.623  1.00 45.02
ATOM   1083  CZ2 TRP A 149      24.335  11.066 -25.092  1.00 44.99
ATOM   1084  CZ3 TRP A 149      23.457   9.992 -23.098  1.00 45.67
ATOM   1085  CH2 TRP A 149      23.787  11.150 -23.835  1.00 45.04
ATOM   1086  N   LEU A 150      21.195   6.456 -25.911  1.00 42.46
ATOM   1087  CA  LEU A 150      19.927   6.764 -25.274  1.00 41.97
ATOM   1088  C   LEU A 150      18.882   5.879 -25.931  1.00 43.31
ATOM   1089  O   LEU A 150      17.929   5.443 -25.287  1.00 43.82
ATOM   1090  CB  LEU A 150      19.585   8.250 -25.444  1.00 40.17
ATOM   1091  CG  LEU A 150      20.525   9.221 -24.712  1.00 38.05
ATOM   1092  CD1 LEU A 150      20.375  10.630 -25.263  1.00 38.55
ATOM   1093  CD2 LEU A 150      20.227   9.191 -23.226  1.00 37.71
ATOM   1094  N   TYR A 151      19.081   5.596 -27.214  1.00 43.54
ATOM   1095  CA  TYR A 151      18.159   4.746 -27.947  1.00 45.89
ATOM   1096  C   TYR A 151      18.136   3.329 -27.385  1.00 47.45
ATOM   1097  O   TYR A 151      17.066   2.729 -27.235  1.00 48.47
ATOM   1098  CB  TYR A 151      18.541   4.673 -29.421  1.00 46.48
ATOM   1099  CG  TYR A 151      17.689   3.683 -30.172  1.00 45.95
ATOM   1100  CD1 TYR A 151      16.347   3.949 -30.430  1.00 45.74
ATOM   1101  CD2 TYR A 151      18.207   2.456 -30.576  1.00 45.53
ATOM   1102  CE1 TYR A 151      15.540   3.017 -31.070  1.00 44.78
ATOM   1103  CE2 TYR A 151      17.410   1.519 -31.217  1.00 44.88
ATOM   1104  CZ  TYR A 151      16.079   1.806 -31.463  1.00 45.59
ATOM   1105  OH  TYR A 151      15.295   0.890 -32.125  1.00 45.88
ATOM   1106  N   GLN A 152      19.317   2.790 -27.098  1.00 48.57
ATOM   1107  CA  GLN A 152      19.434   1.436 -26.558  1.00 50.17
ATOM   1108  C   GLN A 152      18.562   1.239 -25.327  1.00 48.67
ATOM   1109  O   GLN A 152      18.016   0.164 -25.118  1.00 50.59
ATOM   1110  CB  GLN A 152      20.887   1.131 -26.191  1.00 54.08
ATOM   1111  CG  GLN A 152      21.811   0.925 -27.379  1.00 59.72
ATOM   1112  CD  GLN A 152      21.662  -0.449 -28.008  1.00 64.18
ATOM   1113  OE1 GLN A 152      22.253  -0.730 -29.053  1.00 65.67
ATOM   1114  NE2 GLN A 152      20.874  -1.317 -27.372  1.00 65.58
ATOM   1115  N   VAL A 153      18.429   2.281 -24.515  1.00 46.53
ATOM   1116  CA  VAL A 153      17.628   2.200 -23.303  1.00 43.23
ATOM   1117  C   VAL A 153      16.437   3.152 -23.343  1.00 43.93
ATOM   1118  O   VAL A 153      16.026   3.697 -22.313  1.00 43.15
ATOM   1119  CB  VAL A 153      18.486   2.518 -22.063  1.00 43.31
ATOM   1120  CG1 VAL A 153      19.595   1.491 -21.929  1.00 41.11
ATOM   1121  CG2 VAL A 153      19.069   3.915 -22.173  1.00 40.85
ATOM   1122  N   PHE A 154      15.869   3.334 -24.532  1.00 43.03
ATOM   1123  CA  PHE A 154      14.738   4.229 -24.699  1.00 43.86
ATOM   1124  C   PHE A 154      13.523   3.867 -23.862  1.00 45.69
ATOM   1125  O   PHE A 154      12.993   4.710 -23.141  1.00 46.00
ATOM   1126  CB  PHE A 154      14.318   4.308 -26.164  1.00 43.72
ATOM   1127  CG  PHE A 154      13.248   5.332 -26.423  1.00 43.74
ATOM   1128  CD1 PHE A 154      13.563   6.684 -26.473  1.00 43.00
ATOM   1129  CD2 PHE A 154      11.918   4.947 -26.580  1.00 44.17
ATOM   1130  CE1 PHE A 154      12.570   7.639 -26.675  1.00 44.01
ATOM   1131  CE2 PHE A 154      10.916   5.895 -26.783  1.00 44.52
ATOM   1132  CZ  PHE A 154      11.243   7.244 -26.830  1.00 45.13
ATOM   1133  N   ASP A 155      13.072   2.623 -23.960  1.00 47.94
ATOM   1134  CA  ASP A 155      11.902   2.190 -23.203  1.00 51.45
ATOM   1135  C   ASP A 155      12.195   1.920 -21.728  1.00 52.95
ATOM   1136  O   ASP A 155      11.422   2.298 -20.846  1.00 55.27
ATOM   1137  CB  ASP A 155      11.304   0.925 -23.824  1.00 52.93
ATOM   1138  CG  ASP A 155      10.900   1.118 -25.268  1.00 56.14
ATOM   1139  OD1 ASP A 155      11.801   1.307 -26.111  1.00 59.30
ATOM   1140  OD2 ASP A 155       9.683   1.086 -25.563  1.00 56.38
ATOM   1141  N   SER A 156      13.317   1.271 -21.459  1.00 53.46
ATOM   1142  CA  SER A 156      13.666   0.925 -20.093  1.00 52.75
ATOM   1143  C   SER A 156      13.922   2.095 -19.157  1.00 52.56
ATOM   1144  O   SER A 156      13.595   2.012 -17.974  1.00 53.67
ATOM   1145  CB  SER A 156      14.888   0.001 -20.085  1.00 53.06
ATOM   1146  OG  SER A 156      16.014   0.631 -20.670  1.00 52.80
ATOM   1147  N   GLU A 157      14.495   3.185 -19.660  1.00 51.49
ATOM   1148  CA  GLU A 157      14.796   4.299 -18.765  1.00 50.51
ATOM   1149  C   GLU A 157      14.709   5.741 -19.251  1.00 47.81
ATOM   1150  O   GLU A 157      14.879   6.658 -18.453  1.00 50.14
ATOM   1151  CB  GLU A 157      16.177   4.075 -18.134  1.00 52.18
ATOM   1152  CG  GLU A 157      17.227   3.558 -19.091  1.00 53.23
ATOM   1153  CD  GLU A 157      18.556   3.309 -18.404  1.00 55.70
ATOM   1154  OE1 GLU A 157      19.315   4.281 -18.199  1.00 56.71
ATOM   1155  OE2 GLU A 157      18.836   2.141 -18.061  1.00 55.41
ATOM   1156  N   VAL A 158      14.449   5.957 -20.532  1.00 44.67
ATOM   1157  CA  VAL A 158      14.357   7.317 -21.045  1.00 41.00
ATOM   1158  C   VAL A 158      12.924   7.838 -21.147  1.00 41.08
ATOM   1159  O   VAL A 158      12.584   8.861 -20.560  1.00 42.60
ATOM   1160  CB  VAL A 158      15.004   7.440 -22.451  1.00 40.28
ATOM   1161  CG1 VAL A 158      14.753   8.827 -23.019  1.00 33.40
ATOM   1162  CG2 VAL A 158      16.487   7.171 -22.371  1.00 39.44
ATOM   1163  N   GLU A 159      12.080   7.130 -21.883  1.00 39.57
ATOM   1164  CA  GLU A 159      10.715   7.582 -22.086  1.00 39.64
ATOM   1165  C   GLU A 159       9.716   7.385 -20.956  1.00 38.83
ATOM   1166  O   GLU A 159       9.674   6.348 -20.298  1.00 40.81
ATOM   1167  CB  GLU A 159      10.147   6.958 -23.369  1.00 39.85
ATOM   1168  CG  GLU A 159       8.764   7.484 -23.764  1.00 41.32
ATOM   1169  CD  GLU A 159       8.242   6.867 -25.052  1.00 42.76
ATOM   1170  OE1 GLU A 159       8.132   5.629 -25.120  1.00 44.21
ATOM   1171  OE2 GLU A 159       7.933   7.615 -26.001  1.00 43.56
ATOM   1172  N   LEU A 160       8.927   8.426 -20.733  1.00 37.31
ATOM   1173  CA  LEU A 160       7.852   8.416 -19.755  1.00 37.20
ATOM   1174  C   LEU A 160       6.674   8.786 -20.657  1.00 38.09
ATOM   1175  O   LEU A 160       6.650   9.873 -21.241  1.00 36.81
ATOM   1176  CB  LEU A 160       8.052   9.494 -18.683  1.00 34.92
ATOM   1177  CG  LEU A 160       6.907   9.647 -17.674  1.00 34.35
ATOM   1178  CD1 LEU A 160       6.817   8.396 -16.789  1.00 33.02
ATOM   1179  CD2 LEU A 160       7.137  10.878 -16.819  1.00 30.34
ATOM   1180  N   MET A 161       5.723   7.875 -20.803  1.00 37.86
ATOM   1181  CA  MET A 161       4.579   8.125 -21.668  1.00 40.28
ATOM   1182  C   MET A 161       3.475   8.825 -20.888  1.00 40.23
ATOM   1183  O   MET A 161       3.033   8.328 -19.849  1.00 38.90
ATOM   1184  CB  MET A 161       4.062   6.800 -22.242  1.00 41.68
ATOM   1185  CG  MET A 161       3.179   6.946 -23.457  1.00 47.64
ATOM   1186  SD  MET A 161       4.139   7.695 -24.961  1.00 55.44
ATOM   1187  CE  MET A 161       5.224   6.182 -25.411  1.00 51.96
ATOM   1188  N   GLN A 162       3.047   9.988 -21.378  1.00 39.06
ATOM   1189  CA  GLN A 162       1.986  10.751 -20.722  1.00 38.46
ATOM   1190  C   GLN A 162       0.647  10.059 -20.971  1.00 38.71
ATOM   1191  O   GLN A 162       0.380   9.586 -22.075  1.00 39.57
ATOM   1192  CB  GLN A 162       1.947  12.196 -21.261  1.00 37.29
ATOM   1193  CG  GLN A 162       0.710  13.012 -20.855  1.00 37.76
ATOM   1194  CD  GLN A 162       0.711  14.445 -21.419  1.00 40.01
ATOM   1195  OE1 GLN A 162       0.896  14.658 -22.625  1.00 38.27
ATOM   1196  NE2 GLN A 162       0.490  15.428 -20.543  1.00 36.63
ATOM   1197  N   ASN A 163      -0.180   9.987 -19.935  1.00 38.70
ATOM   1198  CA  ASN A 163      -1.499   9.367 -20.031  1.00 38.78
ATOM   1199  C   ASN A 163      -2.439  10.174 -20.902  1.00 37.70
ATOM   1200  O   ASN A 163      -2.127  11.282 -21.305  1.00 38.96
ATOM   1201  CB  ASN A 163      -2.147   9.270 -18.655  1.00 37.28
ATOM   1202  CG  ASN A 163      -1.460   8.297 -17.765  1.00 38.21
ATOM   1203  OD1 ASN A 163      -1.453   7.100 -18.036  1.00 40.83
ATOM   1204  ND2 ASN A 163      -0.868   8.795 -16.687  1.00 40.00
ATOM   1205  N   GLN A 164      -3.598   9.594 -21.178  1.00 37.74
ATOM   1206  CA  GLN A 164      -4.639  10.257 -21.940  1.00 38.75
ATOM   1207  C   GLN A 164      -5.945   9.887 -21.247  1.00 38.30
ATOM   1208  O   GLN A 164      -6.214   8.712 -21.002  1.00 38.57
ATOM   1209  CB  GLN A 164      -4.628   9.792 -23.398  1.00 41.95
ATOM   1210  CG  GLN A 164      -3.423  10.320 -24.177  1.00 45.73
ATOM   1211  CD  GLN A 164      -3.808  10.995 -25.479  1.00 47.17
ATOM   1212  OE1 GLN A 164      -4.834  11.677 -25.564  1.00 47.98
ATOM   1213  NE2 GLN A 164      -2.973  10.826 -26.500  1.00 48.30
ATOM   1214  N   VAL A 165      -6.737  10.894 -20.899  1.00 36.32
ATOM   1215  CA  VAL A 165      -8.004  10.663 -20.217  1.00 35.54
ATOM   1216  C   VAL A 165      -9.210  10.995 -21.102  1.00 34.37
ATOM   1217  O   VAL A 165      -9.078  11.654 -22.127  1.00 34.78
ATOM   1218  CB  VAL A 165      -8.078  11.483 -18.896  1.00 35.04
ATOM   1219  CG1 VAL A 165      -6.953  11.064 -17.969  1.00 34.84
ATOM   1220  CG2 VAL A 165      -7.972  12.969 -19.181  1.00 33.65
ATOM   1221  N   PRO A 166     -10.406  10.535 -20.712  1.00 35.69
ATOM   1222  CA  PRO A 166     -11.634  10.784 -21.480  1.00 35.02
ATOM   1223  C   PRO A 166     -12.183  12.197 -21.334  1.00 35.02
ATOM   1224  O   PRO A 166     -12.288  12.706 -20.228  1.00 35.28
ATOM   1225  CB  PRO A 166     -12.624   9.764 -20.907  1.00 33.19
ATOM   1226  CG  PRO A 166     -11.767   8.753 -20.219  1.00 34.63
ATOM   1227  CD  PRO A 166     -10.659   9.565 -19.634  1.00 36.01
ATOM   1228  N   LYS A 167     -12.518  12.844 -22.440  1.00 35.23
ATOM   1229  CA  LYS A 167     -13.122  14.166 -22.330  1.00 36.37
ATOM   1230  C   LYS A 167     -14.558  13.812 -21.913  1.00 37.77
ATOM   1231  O   LYS A 167     -15.135  12.848 -22.431  1.00 36.46
ATOM   1232  CB  LYS A 167     -13.166  14.893 -23.684  1.00 35.92
ATOM   1233  CG  LYS A 167     -11.836  15.077 -24.394  1.00 36.49
ATOM   1234  CD  LYS A 167     -12.025  15.885 -25.666  1.00 36.34
ATOM   1235  CE  LYS A 167     -10.713  16.092 -26.398  1.00 35.70
ATOM   1236  NZ  LYS A 167     -10.941  16.861 -27.646  1.00 38.19
ATOM   1237  N   ILE A 168     -15.133  14.577 -20.992  1.00 38.68
ATOM   1238  CA  ILE A 168     -16.492  14.311 -20.536  1.00 39.54
ATOM   1239  C   ILE A 168     -17.497  15.399 -20.932  1.00 40.80
ATOM   1240  O   ILE A 168     -17.171  16.582 -20.964  1.00 41.45
ATOM   1241  CB  ILE A 168     -16.523  14.108 -19.001  1.00 38.91
ATOM   1242  CG1 ILE A 168     -15.983  15.347 -18.288  1.00 35.70
ATOM   1243  CG2 ILE A 168     -15.680  12.890 -18.627  1.00 36.04
ATOM   1244  CD1 ILE A 168     -15.902  15.184 -16.770  1.00 36.63
ATOM   1245  N   LEU A 169     -18.723  14.984 -21.239  1.00 41.79
ATOM   1246  CA  LEU A 169     -19.781  15.915 -21.635  1.00 42.15
ATOM   1247  C   LEU A 169     -20.121  16.851 -20.476  1.00 42.90
ATOM   1248  O   LEU A 169     -20.222  16.422 -19.332  1.00 43.67
ATOM   1249  CB  LEU A 169     -21.018  15.126 -22.073  1.00 40.70
ATOM   1250  CG  LEU A 169     -20.782  14.178 -23.252  1.00 41.25
ATOM   1251  CD1 LEU A 169     -21.976  13.249 -23.429  1.00 37.05
ATOM   1252  CD2 LEU A 169     -20.533  14.991 -24.513  1.00 40.24
ATOM   1253  N   GLN A 170     -20.316  18.129 -20.772  1.00 45.51
ATOM   1254  CA  GLN A 170     -20.597  19.101 -19.725  1.00 49.05
ATOM   1255  C   GLN A 170     -21.926  18.912 -19.004  1.00 51.40
ATOM   1256  O   GLN A 170     -22.025  19.167 -17.803  1.00 52.17
ATOM   1257  CB  GLN A 170     -20.530  20.521 -20.293  1.00 50.47
ATOM   1258  CG  GLN A 170     -19.248  20.828 -21.043  1.00 51.14
ATOM   1259  CD  GLN A 170     -19.046  22.312 -21.262  1.00 51.59
ATOM   1260  OE1 GLN A 170     -20.006  23.067 -21.407  1.00 52.46
ATOM   1261  NE2 GLN A 170     -17.790  22.736 -21.300  1.00 52.17
ATOM   1262  N   ASP A 171     -22.944  18.462 -19.729  1.00 52.74
ATOM   1263  CA  ASP A 171     -24.261  18.274 -19.139  1.00 53.57
ATOM   1264  C   ASP A 171     -24.400  17.033 -18.252  1.00 53.15
ATOM   1265  O   ASP A 171     -25.009  17.104 -17.181  1.00 53.57
ATOM   1266  CB  ASP A 171     -25.314  18.245 -20.245  1.00 56.16
ATOM   1267  CG  ASP A 171     -25.078  17.130 -21.232  1.00 61.52
ATOM   1268  OD1 ASP A 171     -23.898  16.857 -21.533  1.00 63.32
ATOM   1269  OD2 ASP A 171     -26.065  16.531 -21.716  1.00 65.04
ATOM   1270  N   THR A 172     -23.827  15.907 -18.675  1.00 50.33
ATOM   1271  CA  THR A 172     -23.945  14.674 -17.898  1.00 48.14
ATOM   1272  C   THR A 172     -22.662  14.181 -17.232  1.00 47.46
ATOM   1273  O   THR A 172     -22.715  13.313 -16.368  1.00 47.28
ATOM   1274  CB  THR A 172     -24.504  13.524 -18.773  1.00 47.93
ATOM   1275  OG1 THR A 172     -23.481  13.032 -19.648  1.00 45.52
ATOM   1276  CG2 THR A 172     -25.666  14.028 -19.620  1.00 48.52
ATOM   1277  N   LEU A 173     -21.523  14.735 -17.645  1.00 46.47
ATOM   1278  CA  LEU A 173     -20.201  14.371 -17.126  1.00 42.93
ATOM   1279  C   LEU A 173     -19.784  12.958 -17.517  1.00 43.65
ATOM   1280  O   LEU A 173     -18.909  12.355 -16.888  1.00 44.85
ATOM   1281  CB  LEU A 173     -20.145  14.545 -15.609  1.00 38.05
ATOM   1282  CG  LEU A 173     -20.503  15.959 -15.139  1.00 39.21
ATOM   1283  CD1 LEU A 173     -20.298  16.074 -13.634  1.00 40.03
ATOM   1284  CD2 LEU A 173     -19.652  16.993 -15.871  1.00 37.65
ATOM   1285  N   GLU A 174     -20.408  12.442 -18.570  1.00 43.84
ATOM   1286  CA  GLU A 174     -20.096  11.110 -19.075  1.00 45.78
ATOM   1287  C   GLU A 174     -19.140  11.180 -20.270  1.00 43.85
ATOM   1288  O   GLU A 174     -19.013  12.221 -20.917  1.00 44.17
ATOM   1289  CB  GLU A 174     -21.386  10.364 -19.461  1.00 48.19
ATOM   1290  CG  GLU A 174     -22.194   9.908 -18.236  1.00 55.21
ATOM   1291  CD  GLU A 174     -23.143   8.741 -18.506  1.00 59.07
ATOM   1292  OE1 GLU A 174     -22.811   7.879 -19.358  1.00 60.07
ATOM   1293  OE2 GLU A 174     -24.208   8.673 -17.841  1.00 59.93
ATOM   1294  N   PRO A 175     -18.443  10.073 -20.567  1.00 42.77
ATOM   1295  CA  PRO A 175     -17.495  10.019 -21.688  1.00 40.57
ATOM   1296  C   PRO A 175     -18.091  10.517 -22.993  1.00 41.06
ATOM   1297  O   PRO A 175     -19.057   9.939 -23.499  1.00 43.20
ATOM   1298  CB  PRO A 175     -17.142   8.537 -21.775  1.00 38.66
ATOM   1299  CG  PRO A 175     -17.259   8.080 -20.363  1.00 40.54
ATOM   1300  CD  PRO A 175     -18.503   8.774 -19.868  1.00 41.65
ATOM   1301  N   ALA A 176     -17.529  11.588 -23.544  1.00 39.94
ATOM   1302  CA  ALA A 176     -18.023  12.099 -24.816  1.00 38.73
ATOM   1303  C   ALA A 176     -17.743  11.058 -25.911  1.00 38.65
ATOM   1304  O   ALA A 176     -16.877  10.189 -25.764  1.00 38.10
ATOM   1305  CB  ALA A 176     -17.343  13.411 -25.156  1.00 35.34
ATOM   1306  N   ALA A 177     -18.489  11.143 -27.004  1.00 38.60
ATOM   1307  CA  ALA A 177     -18.306  10.219 -28.110  1.00 38.18
ATOM   1308  C   ALA A 177     -18.283  11.010 -29.412  1.00 37.85
ATOM   1309  O   ALA A 177     -19.020  11.976 -29.573  1.00 39.01
ATOM   1310  CB  ALA A 177     -19.434   9.195 -28.130  1.00 36.99
ATOM   1311  N   TRP A 178     -17.426  10.600 -30.334  1.00 37.13
ATOM   1312  CA  TRP A 178     -17.305  11.265 -31.621  1.00 38.60
ATOM   1313  C   TRP A 178     -16.965  10.158 -32.616  1.00 39.17
ATOM   1314  O   TRP A 178     -15.797   9.881 -32.875  1.00 39.73
ATOM   1315  CB  TRP A 178     -16.178  12.300 -31.555  1.00 39.25
ATOM   1316  CG  TRP A 178     -16.166  13.284 -32.690  1.00 40.34
ATOM   1317  CD1 TRP A 178     -15.118  13.562 -33.521  1.00 39.92
ATOM   1318  CD2 TRP A 178     -17.235  14.155 -33.088  1.00 39.02
ATOM   1319  NE1 TRP A 178     -15.466  14.553 -34.410  1.00 42.80
ATOM   1320  CE2 TRP A 178     -16.760  14.935 -34.166  1.00 40.63
ATOM   1321  CE3 TRP A 178     -18.546  14.350 -32.638  1.00 39.47
ATOM   1322  CZ2 TRP A 178     -17.549  15.898 -34.802  1.00 40.96
ATOM   1323  CZ3 TRP A 178     -19.332  15.307 -33.270  1.00 41.03
ATOM   1324  CH2 TRP A 178     -18.829  16.071 -34.343  1.00 39.84
ATOM   1325  N   ALA A 179     -17.997   9.510 -33.147  1.00 41.22
ATOM   1326  CA  ALA A 179     -17.826   8.407 -34.089  1.00 42.53
ATOM   1327  C   ALA A 179     -16.957   8.786 -35.280  1.00 43.34
ATOM   1328  O   ALA A 179     -16.251   7.949 -35.843  1.00 43.38
ATOM   1329  CB  ALA A 179     -19.190   7.917 -34.569  1.00 42.39
ATOM   1330  N   GLU A 180     -17.019  10.052 -35.664  1.00 43.86
ATOM   1331  CA  GLU A 180     -16.234  10.540 -36.782  1.00 44.37
ATOM   1332  C   GLU A 180     -14.755  10.280 -36.534  1.00 44.17
ATOM   1333  O   GLU A 180     -14.051   9.765 -37.399  1.00 45.04
ATOM   1334  CB  GLU A 180     -16.475  12.028 -36.949  1.00 46.66
ATOM   1335  CG  GLU A 180     -17.927  12.361 -37.190  1.00 48.75
ATOM   1336  CD  GLU A 180     -18.158  13.845 -37.283  1.00 48.95
ATOM   1337  OE1 GLU A 180     -17.174  14.580 -37.524  1.00 47.94
ATOM   1338  OE2 GLU A 180     -19.323  14.268 -37.121  1.00 49.50
ATOM   1339  N   ASN A 181     -14.286  10.638 -35.345  1.00 43.85
ATOM   1340  CA  ASN A 181     -12.887  10.437 -34.996  1.00 44.31
ATOM   1341  C   ASN A 181     -12.743  10.136 -33.500  1.00 44.24
ATOM   1342  O   ASN A 181     -12.503  11.031 -32.684  1.00 43.75
ATOM   1343  CB  ASN A 181     -12.072  11.675 -35.371  1.00 44.31
ATOM   1344  CG  ASN A 181     -10.615  11.351 -35.620  1.00 48.31
ATOM   1345  OD1 ASN A 181      -9.931  10.790 -34.759  1.00 49.59
ATOM   1346  ND2 ASN A 181     -10.130  11.697 -36.808  1.00 49.62
ATOM   1347  N   PRO A 182     -12.876   8.856 -33.129  1.00 43.97
ATOM   1348  CA  PRO A 182     -12.771   8.417 -31.733  1.00 44.22
ATOM   1349  C   PRO A 182     -11.561   8.944 -30.949  1.00 42.71
ATOM   1350  O   PRO A 182     -11.646   9.116 -29.732  1.00 43.72
ATOM   1351  CB  PRO A 182     -12.785   6.892 -31.849  1.00 43.78
ATOM   1352  CG  PRO A 182     -13.652   6.668 -33.057  1.00 45.51
ATOM   1353  CD  PRO A 182     -13.118   7.709 -34.023  1.00 43.03
ATOM   1354  N   ALA A 183     -10.445   9.208 -31.621  1.00 39.72
ATOM   1355  CA  ALA A 183      -9.272   9.725 -30.903  1.00 39.71
ATOM   1356  C   ALA A 183      -9.594  11.080 -30.279  1.00 38.28
ATOM   1357  O   ALA A 183      -8.926  11.511 -29.344  1.00 39.79
ATOM   1358  CB  ALA A 183      -8.063   9.862 -31.844  1.00 35.85
ATOM   1359  N   TYR A 184     -10.614  11.753 -30.794  1.00 38.33
ATOM   1360  CA  TYR A 184     -10.980  13.058 -30.258  1.00 40.39
ATOM   1361  C   TYR A 184     -11.644  12.944 -28.894  1.00 40.24
ATOM   1362  O   TYR A 184     -11.799  13.937 -28.184  1.00 39.46
ATOM   1363  CB  TYR A 184     -11.907  13.796 -31.229  1.00 40.61
ATOM   1364  CG  TYR A 184     -11.207  14.302 -32.468  1.00 44.66
ATOM   1365  CD1 TYR A 184     -11.877  15.107 -33.387  1.00 46.37
ATOM   1366  CD2 TYR A 184      -9.866  13.999 -32.716  1.00 46.43
ATOM   1367  CE1 TYR A 184     -11.231  15.605 -34.517  1.00 47.45
ATOM   1368  CE2 TYR A 184      -9.214  14.489 -33.844  1.00 48.18
ATOM   1369  CZ  TYR A 184      -9.903  15.292 -34.738  1.00 47.64
ATOM   1370  OH  TYR A 184      -9.268  15.785 -35.854  1.00 49.45
ATOM   1371  N   GLU A 185     -12.031  11.724 -28.536  1.00 38.23
ATOM   1372  CA  GLU A 185     -12.675  11.482 -27.260  1.00 38.36
ATOM   1373  C   GLU A 185     -11.671  11.537 -26.103  1.00 38.64
ATOM   1374  O   GLU A 185     -12.059  11.703 -24.942  1.00 37.14
ATOM   1375  CB  GLU A 185     -13.398  10.130 -27.300  1.00 38.69
ATOM   1376  CG  GLU A 185     -14.568  10.098 -28.314  1.00 39.12
ATOM   1377  CD  GLU A 185     -15.114   8.696 -28.596  1.00 38.57
ATOM   1378  OE1 GLU A 185     -16.057   8.575 -29.411  1.00 41.15
ATOM   1379  OE2 GLU A 185     -14.607   7.718 -28.013  1.00 37.13
ATOM   1380  N   TRP A 186     -10.382  11.423 -26.420  1.00 37.37
ATOM   1381  CA  TRP A 186      -9.349  11.464 -25.384  1.00 36.61
ATOM   1382  C   TRP A 186      -8.450  12.687 -25.502  1.00 35.64
ATOM   1383  O   TRP A 186      -8.321  13.268 -26.572  1.00 36.62
ATOM   1384  CB  TRP A 186      -8.470  10.221 -25.455  1.00 35.39
ATOM   1385  CG  TRP A 186      -9.229   8.939 -25.467  1.00 37.79
ATOM   1386  CD1 TRP A 186      -9.903   8.389 -26.523  1.00 36.88
ATOM   1387  CD2 TRP A 186      -9.387   8.032 -24.372  1.00 36.92
ATOM   1388  NE1 TRP A 186     -10.466   7.194 -26.149  1.00 38.40
ATOM   1389  CE2 TRP A 186     -10.166   6.953 -24.834  1.00 37.56
ATOM   1390  CE3 TRP A 186      -8.944   8.028 -23.042  1.00 37.64
ATOM   1391  CZ2 TRP A 186     -10.514   5.878 -24.014  1.00 38.11
ATOM   1392  CZ3 TRP A 186      -9.290   6.956 -22.225  1.00 37.36
ATOM   1393  CH2 TRP A 186     -10.068   5.896 -22.715  1.00 36.95
ATOM   1394  N   ALA A 187      -7.814  13.062 -24.401  1.00 33.62
ATOM   1395  CA  ALA A 187      -6.906  14.201 -24.399  1.00 33.95
ATOM   1396  C   ALA A 187      -5.888  14.069 -23.273  1.00 33.35
ATOM   1397  O   ALA A 187      -6.127  13.365 -22.298  1.00 33.81
ATOM   1398  CB  ALA A 187      -7.688  15.503 -24.236  1.00 29.72
ATOM   1399  N   PRO A 188      -4.723  14.724 -23.415  1.00 33.20
ATOM   1400  CA  PRO A 188      -3.684  14.669 -22.378  1.00 31.94
ATOM   1401  C   PRO A 188      -4.209  15.356 -21.121  1.00 31.90
ATOM   1402  O   PRO A 188      -5.048  16.255 -21.204  1.00 32.33
ATOM   1403  CB  PRO A 188      -2.501  15.404 -23.025  1.00 30.31
ATOM   1404  CG  PRO A 188      -3.138  16.249 -24.097  1.00 32.07
ATOM   1405  CD  PRO A 188      -4.219  15.372 -24.639  1.00 30.86
ATOM   1406  N   PRO A 189      -3.732  14.949 -19.935  1.00 31.94
ATOM   1407  CA  PRO A 189      -4.269  15.623 -18.747  1.00 32.53
ATOM   1408  C   PRO A 189      -3.395  16.706 -18.130  1.00 33.00
ATOM   1409  O   PRO A 189      -3.429  16.899 -16.919  1.00 34.77
ATOM   1410  CB  PRO A 189      -4.511  14.461 -17.791  1.00 29.74
ATOM   1411  CG  PRO A 189      -3.315  13.613 -18.045  1.00 31.69
ATOM   1412  CD  PRO A 189      -3.100  13.671 -19.566  1.00 31.42
ATOM   1413  N   GLY A 190      -2.640  17.425 -18.964  1.00 33.39
ATOM   1414  CA  GLY A 190      -1.771  18.482 -18.471  1.00 31.60
ATOM   1415  C   GLY A 190      -0.430  17.942 -17.996  1.00 33.26
ATOM   1416  O   GLY A 190      -0.287  16.734 -17.779  1.00 31.41
ATOM   1417  N   HIS A 191       0.567  18.811 -17.847  1.00 33.17
ATOM   1418  CA  HIS A 191       1.861  18.331 -17.374  1.00 35.78
ATOM   1419  C   HIS A 191       1.784  17.816 -15.933  1.00 35.75
ATOM   1420  O   HIS A 191       2.677  17.104 -15.481  1.00 36.24
ATOM   1421  CB  HIS A 191       2.955  19.410 -17.507  1.00 37.87
ATOM   1422  CG  HIS A 191       2.466  20.828 -17.358  1.00 42.29
ATOM   1423  ND1 HIS A 191       1.853  21.294 -16.212  1.00 41.81
ATOM   1424  CD2 HIS A 191       2.540  21.892 -18.201  1.00 40.73
ATOM   1425  CE1 HIS A 191       1.572  22.580 -16.354  1.00 41.04
ATOM   1426  NE2 HIS A 191       1.977  22.968 -17.549  1.00 41.82
ATOM   1427  N   GLY A 192       0.710  18.159 -15.224  1.00 35.38
ATOM   1428  CA  GLY A 192       0.551  17.680 -13.864  1.00 34.97
ATOM   1429  C   GLY A 192       0.542  16.160 -13.842  1.00 36.90
ATOM   1430  O   GLY A 192       0.846  15.548 -12.822  1.00 36.76
ATOM   1431  N   ASP A 193       0.199  15.555 -14.979  1.00 36.63
ATOM   1432  CA  ASP A 193       0.149  14.102 -15.128  1.00 35.95
ATOM   1433  C   ASP A 193       1.526  13.438 -14.982  1.00 38.31
ATOM   1434  O   ASP A 193       1.636  12.209 -14.874  1.00 38.88
ATOM   1435  CB  ASP A 193      -0.455  13.750 -16.489  1.00 36.26
ATOM   1436  CG  ASP A 193      -0.597  12.251 -16.705  1.00 36.99
ATOM   1437  OD1 ASP A 193       0.155  11.695 -17.538  1.00 33.86
ATOM   1438  OD2 ASP A 193      -1.463  11.633 -16.042  1.00 38.28
ATOM   1439  N   ILE A 194       2.580  14.246 -14.985  1.00 37.55
ATOM   1440  CA  ILE A 194       3.922  13.716 -14.821  1.00 36.74
ATOM   1441  C   ILE A 194       4.013  12.843 -13.562  1.00 37.62
ATOM   1442  O   ILE A 194       4.571  11.748 -13.607  1.00 39.98
ATOM   1443  CB  ILE A 194       4.953  14.860 -14.745  1.00 38.00
ATOM   1444  CG1 ILE A 194       6.356  14.289 -14.568  1.00 38.77
ATOM   1445  CG2 ILE A 194       4.616  15.806 -13.602  1.00 37.19
ATOM   1446  CD1 ILE A 194       7.430  15.364 -14.530  1.00 44.12
ATOM   1447  N   TYR A 195       3.453  13.314 -12.449  1.00 37.19
ATOM   1448  CA  TYR A 195       3.485  12.556 -11.192  1.00 38.01
ATOM   1449  C   TYR A 195       2.691  11.255 -11.300  1.00 40.06
ATOM   1450  O   TYR A 195       3.093  10.223 -10.747  1.00 40.63
ATOM   1451  CB  TYR A 195       2.933  13.402 -10.035  1.00 36.03
ATOM   1452  CG  TYR A 195       3.537  14.783  -9.981  1.00 30.56
ATOM   1453  CD1 TYR A 195       2.775  15.907 -10.297  1.00 29.54
ATOM   1454  CD2 TYR A 195       4.895  14.962  -9.687  1.00 27.85
ATOM   1455  CE1 TYR A 195       3.353  17.179 -10.330  1.00 28.99
ATOM   1456  CE2 TYR A 195       5.480  16.226  -9.718  1.00 26.20
ATOM   1457  CZ  TYR A 195       4.706  17.324 -10.041  1.00 26.57
ATOM   1458  OH  TYR A 195       5.278  18.563 -10.094  1.00 31.72
ATOM   1459  N   THR A 196       1.566  11.308 -12.011  1.00 38.29
ATOM   1460  CA  THR A 196       0.742  10.126 -12.199  1.00 36.66
ATOM   1461  C   THR A 196       1.524   9.093 -13.006  1.00 36.23
ATOM   1462  O   THR A 196       1.664   7.941 -12.601  1.00 36.41
ATOM   1463  CB  THR A 196      -0.550  10.441 -12.976  1.00 36.21
ATOM   1464  OG1 THR A 196      -1.341  11.392 -12.256  1.00 37.82
ATOM   1465  CG2 THR A 196      -1.356   9.174 -13.170  1.00 38.41
ATOM   1466  N   ALA A 197       2.032   9.516 -14.154  1.00 36.16
ATOM   1467  CA  ALA A 197       2.780   8.626 -15.031  1.00 35.40
ATOM   1468  C   ALA A 197       3.975   8.003 -14.331  1.00 36.05
ATOM   1469  O   ALA A 197       4.230   6.802 -14.482  1.00 35.18
ATOM   1470  CB  ALA A 197       3.238   9.381 -16.268  1.00 35.71
ATOM   1471  N   LEU A 198       4.713   8.811 -13.571  1.00 35.34
ATOM   1472  CA  LEU A 198       5.882   8.293 -12.864  1.00 36.29
ATOM   1473  C   LEU A 198       5.510   7.177 -11.882  1.00 38.15
ATOM   1474  O   LEU A 198       6.152   6.122 -11.838  1.00 36.67
ATOM   1475  CB  LEU A 198       6.607   9.424 -12.126  1.00 34.97
ATOM   1476  CG  LEU A 198       7.554  10.315 -12.949  1.00 36.70
ATOM   1477  CD1 LEU A 198       8.164  11.403 -12.060  1.00 35.30
ATOM   1478  CD2 LEU A 198       8.659   9.453 -13.571  1.00 36.58
ATOM   1479  N   TYR A 199       4.461   7.412 -11.102  1.00 39.02
ATOM   1480  CA  TYR A 199       4.012   6.435 -10.129  1.00 40.88
ATOM   1481  C   TYR A 199       3.388   5.223 -10.801  1.00 40.73
ATOM   1482  O   TYR A 199       3.806   4.094 -10.568  1.00 40.25
ATOM   1483  CB  TYR A 199       2.970   7.052  -9.201  1.00 42.70
ATOM   1484  CG  TYR A 199       2.501   6.109  -8.122  1.00 43.83
ATOM   1485  CD1 TYR A 199       3.184   6.025  -6.911  1.00 45.57
ATOM   1486  CD2 TYR A 199       1.366   5.311  -8.298  1.00 45.13
ATOM   1487  CE1 TYR A 199       2.751   5.184  -5.898  1.00 46.20
ATOM   1488  CE2 TYR A 199       0.921   4.455  -7.281  1.00 43.64
ATOM   1489  CZ  TYR A 199       1.622   4.405  -6.085  1.00 44.90
ATOM   1490  OH  TYR A 199       1.204   3.600  -5.054  1.00 47.16
ATOM   1491  N   GLY A 200       2.373   5.485 -11.621  1.00 41.98
ATOM   1492  CA  GLY A 200       1.650   4.437 -12.320  1.00 41.21
ATOM   1493  C   GLY A 200       2.461   3.479 -13.171  1.00 41.11
ATOM   1494  O   GLY A 200       2.198   2.280 -13.153  1.00 40.92
ATOM   1495  N   SER A 201       3.435   4.000 -13.912  1.00 40.58
ATOM   1496  CA  SER A 201       4.275   3.189 -14.795  1.00 42.27
ATOM   1497  C   SER A 201       5.246   2.333 -14.008  1.00 43.63
ATOM   1498  O   SER A 201       5.875   1.432 -14.560  1.00 43.78
ATOM   1499  CB  SER A 201       5.094   4.085 -15.718  1.00 42.48
ATOM   1500  OG  SER A 201       6.160   4.681 -14.995  1.00 42.21
ATOM   1501  N   GLY A 202       5.383   2.636 -12.721  1.00 45.14
ATOM   1502  CA  GLY A 202       6.297   1.891 -11.875  1.00 45.66
ATOM   1503  C   GLY A 202       7.681   2.516 -11.853  1.00 45.33
ATOM   1504  O   GLY A 202       8.573   2.066 -11.119  1.00 45.70
ATOM   1505  N   LYS A 203       7.853   3.569 -12.647  1.00 45.10
ATOM   1506  CA  LYS A 203       9.135   4.258 -12.745  1.00 44.28
ATOM   1507  C   LYS A 203       9.549   5.061 -11.514  1.00 42.73
ATOM   1508  O   LYS A 203      10.739   5.195 -11.232  1.00 41.69
ATOM   1509  CB  LYS A 203       9.141   5.132 -13.992  1.00 44.84
ATOM   1510  CG  LYS A 203       9.106   4.292 -15.242  1.00 47.73
ATOM   1511  CD  LYS A 203       9.060   5.110 -16.503  1.00 51.16
ATOM   1512  CE  LYS A 203       9.037   4.187 -17.718  1.00 54.34
ATOM   1513  NZ  LYS A 203      10.237   3.283 -17.748  1.00 54.74
ATOM   1514  N   LEU A 204       8.586   5.590 -10.772  1.00 41.59
ATOM   1515  CA  LEU A 204       8.939   6.338  -9.576  1.00 42.14
ATOM   1516  C   LEU A 204       9.581   5.364  -8.591  1.00 42.75
ATOM   1517  O   LEU A 204      10.713   5.555  -8.151  1.00 41.46
ATOM   1518  CB  LEU A 204       7.701   6.981  -8.946  1.00 39.39
ATOM   1519  CG  LEU A 204       8.013   7.823  -7.704  1.00 40.65
ATOM   1520  CD1 LEU A 204       9.077   8.856  -8.054  1.00 37.57
ATOM   1521  CD2 LEU A 204       6.744   8.497  -7.174  1.00 38.00
ATOM   1522  N   GLN A 205       8.844   4.308  -8.271  1.00 44.97
ATOM   1523  CA  GLN A 205       9.297   3.272  -7.349  1.00 47.13
ATOM   1524  C   GLN A 205      10.676   2.769  -7.766  1.00 47.35
ATOM   1525  O   GLN A 205      11.579   2.617  -6.939  1.00 47.95
ATOM   1526  CB  GLN A 205       8.309   2.102  -7.358  1.00 46.89
ATOM   1527  CG  GLN A 205       6.823   2.469  -7.118  1.00 51.70
ATOM   1528  CD  GLN A 205       6.222   3.437  -8.163  1.00 53.45
ATOM   1529  OE1 GLN A 205       6.648   3.484  -9.319  1.00 52.92
ATOM   1530  NE2 GLN A 205       5.211   4.193  -7.748  1.00 54.12
ATOM   1531  N   GLU A 206      10.831   2.521  -9.061  1.00 47.83
ATOM   1532  CA  GLU A 206      12.092   2.026  -9.609  1.00 49.63
ATOM   1533  C   GLU A 206      13.293   2.981  -9.424  1.00 48.62
ATOM   1534  O   GLU A 206      14.387   2.541  -9.046  1.00 48.66
ATOM   1535  CB  GLU A 206      11.905   1.693 -11.091  1.00 50.88
ATOM   1536  CG  GLU A 206      13.186   1.311 -11.800  1.00 56.66
ATOM   1537  CD  GLU A 206      13.010   1.197 -13.303  1.00 61.02
ATOM   1538  OE1 GLU A 206      14.038   1.129 -14.019  1.00 63.96
ATOM   1539  OE2 GLU A 206      11.845   1.175 -13.765  1.00 63.10
ATOM   1540  N   LEU A 207      13.096   4.273  -9.688  1.00 45.64
ATOM   1541  CA  LEU A 207      14.173   5.255  -9.537  1.00 43.96
ATOM   1542  C   LEU A 207      14.571   5.408  -8.075  1.00 43.69
ATOM   1543  O   LEU A 207      15.751   5.494  -7.750  1.00 42.70
ATOM   1544  CB  LEU A 207      13.751   6.615 -10.112  1.00 41.79
ATOM   1545  CG  LEU A 207      13.740   6.735 -11.646  1.00 42.32
ATOM   1546  CD1 LEU A 207      12.834   7.874 -12.089  1.00 42.26
ATOM   1547  CD2 LEU A 207      15.153   6.946 -12.153  1.00 40.48
ATOM   1548  N   VAL A 208      13.583   5.437  -7.192  1.00 45.43
ATOM   1549  CA  VAL A 208      13.853   5.573  -5.768  1.00 45.49
ATOM   1550  C   VAL A 208      14.627   4.365  -5.237  1.00 46.57
ATOM   1551  O   VAL A 208      15.605   4.519  -4.513  1.00 44.73
ATOM   1552  CB  VAL A 208      12.545   5.711  -4.962  1.00 45.47
ATOM   1553  CG1 VAL A 208      12.854   5.783  -3.473  1.00 42.75
ATOM   1554  CG2 VAL A 208      11.788   6.947  -5.409  1.00 43.90
ATOM   1555  N   GLU A 209      14.198   3.162  -5.607  1.00 48.99
ATOM   1556  CA  GLU A 209      14.874   1.966  -5.120  1.00 51.42
ATOM   1557  C   GLU A 209      16.273   1.838  -5.711  1.00 49.74
ATOM   1558  O   GLU A 209      17.114   1.108  -5.182  1.00 47.92
ATOM   1559  CB  GLU A 209      14.045   0.711  -5.419  1.00 54.12
ATOM   1560  CG  GLU A 209      14.194   0.167  -6.821  1.00 60.17
ATOM   1561  CD  GLU A 209      13.205  -0.945  -7.104  1.00 63.67
ATOM   1562  OE1 GLU A 209      13.286  -1.557  -8.193  1.00 64.36
ATOM   1563  OE2 GLU A 209      12.339  -1.202  -6.235  1.00 66.59
ATOM   1564  N   GLN A 210      16.521   2.554  -6.804  1.00 48.99
ATOM   1565  CA  GLN A 210      17.838   2.532  -7.427  1.00 47.56
ATOM   1566  C   GLN A 210      18.722   3.594  -6.791  1.00 45.53
ATOM   1567  O   GLN A 210      19.888   3.729  -7.140  1.00 46.02
ATOM   1568  CB  GLN A 210      17.742   2.788  -8.922  1.00 46.23
ATOM   1569  CG  GLN A 210      17.123   1.661  -9.692  1.00 50.57
ATOM   1570  CD  GLN A 210      17.389   1.786 -11.171  1.00 52.60
ATOM   1571  OE1 GLN A 210      18.544   1.867 -11.595  1.00 53.93
ATOM   1572  NE2 GLN A 210      16.327   1.810 -11.969  1.00 53.25
ATOM   1573  N   GLY A 211      18.160   4.356  -5.864  1.00 43.96
ATOM   1574  CA  GLY A 211      18.946   5.377  -5.200  1.00 44.53
ATOM   1575  C   GLY A 211      18.841   6.801  -5.715  1.00 44.36
ATOM   1576  O   GLY A 211      19.554   7.679  -5.226  1.00 43.89
ATOM   1577  N   TYR A 212      17.976   7.051  -6.695  1.00 42.98
ATOM   1578  CA  TYR A 212      17.825   8.404  -7.205  1.00 41.72
ATOM   1579  C   TYR A 212      17.065   9.270  -6.211  1.00 41.60
ATOM   1580  O   TYR A 212      16.027   8.867  -5.686  1.00 42.48
ATOM   1581  CB  TYR A 212      17.148   8.392  -8.571  1.00 40.72
ATOM   1582  CG  TYR A 212      18.091   7.912  -9.647  1.00 40.62
ATOM   1583  CD1 TYR A 212      18.212   6.559  -9.937  1.00 39.69
ATOM   1584  CD2 TYR A 212      18.933   8.806 -10.310  1.00 38.42
ATOM   1585  CE1 TYR A 212      19.148   6.106 -10.852  1.00 38.07
ATOM   1586  CE2 TYR A 212      19.871   8.361 -11.224  1.00 37.10
ATOM   1587  CZ  TYR A 212      19.974   7.006 -11.487  1.00 37.82
ATOM   1588  OH  TYR A 212      20.918   6.536 -12.367  1.00 37.28
ATOM   1589  N   ARG A 213      17.598  10.463  -5.964  1.00 40.71
ATOM   1590  CA  ARG A 213      17.037  11.390  -4.989  1.00 43.18
ATOM   1591  C   ARG A 213      16.362  12.630  -5.567  1.00 41.51
ATOM   1592  O   ARG A 213      15.303  13.053  -5.099  1.00 41.39
ATOM   1593  CB  ARG A 213      18.161  11.821  -4.034  1.00 47.27
ATOM   1594  CG  ARG A 213      17.731  12.630  -2.812  1.00 53.69
ATOM   1595  CD  ARG A 213      18.894  12.762  -1.817  1.00 58.00
ATOM   1596  NE  ARG A 213      18.463  13.173  -0.480  1.00 61.74
ATOM   1597  CZ  ARG A 213      17.698  12.439   0.330  1.00 64.47
ATOM   1598  NH1 ARG A 213      17.265  11.240  -0.050  1.00 64.42
ATOM   1599  NH2 ARG A 213      17.366  12.901   1.531  1.00 64.97
ATOM   1600  N   TYR A 214      16.986  13.221  -6.578  1.00 41.02
ATOM   1601  CA  TYR A 214      16.454  14.428  -7.182  1.00 37.94
ATOM   1602  C   TYR A 214      16.074  14.330  -8.649  1.00 37.21
ATOM   1603  O   TYR A 214      16.718  13.644  -9.443  1.00 35.68
ATOM   1604  CB  TYR A 214      17.450  15.573  -7.049  1.00 37.56
ATOM   1605  CG  TYR A 214      17.783  15.983  -5.641  1.00 38.79
ATOM   1606  CD1 TYR A 214      18.939  15.521  -5.015  1.00 37.23
ATOM   1607  CD2 TYR A 214      16.963  16.866  -4.945  1.00 36.90
ATOM   1608  CE1 TYR A 214      19.274  15.935  -3.728  1.00 36.55
ATOM   1609  CE2 TYR A 214      17.290  17.285  -3.662  1.00 38.33
ATOM   1610  CZ  TYR A 214      18.449  16.818  -3.061  1.00 35.95
ATOM   1611  OH  TYR A 214      18.783  17.257  -1.805  1.00 36.81
ATOM   1612  N   MET A 215      15.013  15.044  -8.995  1.00 35.19
ATOM   1613  CA  MET A 215      14.558  15.117 -10.363  1.00 32.98
ATOM   1614  C   MET A 215      14.373  16.592 -10.720  1.00 31.89
ATOM   1615  O   MET A 215      13.743  17.355  -9.974  1.00 29.95
ATOM   1616  CB  MET A 215      13.244  14.378 -10.557  1.00 32.15
ATOM   1617  CG  MET A 215      12.707  14.559 -11.968  1.00 36.23
ATOM   1618  SD  MET A 215      11.103  13.590 -12.371  1.00 43.13
ATOM   1619  CE  MET A 215      11.912  11.905 -12.906  1.00 34.39
ATOM   1620  N   PHE A 216      14.953  16.989 -11.848  1.00 29.47
ATOM   1621  CA  PHE A 216      14.843  18.351 -12.342  1.00 28.37
ATOM   1622  C   PHE A 216      13.988  18.273 -13.595  1.00 29.01
ATOM   1623  O   PHE A 216      14.355  17.607 -14.577  1.00 31.18
ATOM   1624  CB  PHE A 216      16.236  18.910 -12.659  1.00 30.36
ATOM   1625  CG  PHE A 216      16.221  20.220 -13.411  1.00 30.17
ATOM   1626  CD1 PHE A 216      15.451  21.292 -12.964  1.00 29.57
ATOM   1627  CD2 PHE A 216      16.990  20.380 -14.565  1.00 29.44
ATOM   1628  CE1 PHE A 216      15.446  22.509 -13.655  1.00 31.08
ATOM   1629  CE2 PHE A 216      16.997  21.587 -15.267  1.00 28.87
ATOM   1630  CZ  PHE A 216      16.225  22.658 -14.815  1.00 31.89
ATOM   1631  N   VAL A 217      12.833  18.923 -13.554  1.00 26.67
ATOM   1632  CA  VAL A 217      11.927  18.914 -14.690  1.00 26.08
ATOM   1633  C   VAL A 217      11.798  20.301 -15.309  1.00 27.87
ATOM   1634  O   VAL A 217      11.768  21.308 -14.602  1.00 28.54
ATOM   1635  CB  VAL A 217      10.515  18.428 -14.271  1.00 28.66
ATOM   1636  CG1 VAL A 217       9.664  18.140 -15.512  1.00 23.83
ATOM   1637  CG2 VAL A 217      10.633  17.190 -13.398  1.00 26.03
ATOM   1638  N   SER A 218      11.722  20.343 -16.636  1.00 29.19
ATOM   1639  CA  SER A 218      11.582  21.592 -17.366  1.00 31.07
ATOM   1640  C   SER A 218      11.045  21.320 -18.763  1.00 34.97
ATOM   1641  O   SER A 218      11.063  20.174 -19.234  1.00 34.90
ATOM   1642  CB  SER A 218      12.928  22.319 -17.461  1.00 30.29
ATOM   1643  OG  SER A 218      13.905  21.539 -18.125  1.00 31.00
ATOM   1644  N   ASN A 219      10.554  22.375 -19.413  1.00 37.58
ATOM   1645  CA  ASN A 219      10.019  22.269 -20.765  1.00 40.53
ATOM   1646  C   ASN A 219      11.142  21.918 -21.726  1.00 40.52
ATOM   1647  O   ASN A 219      12.262  22.432 -21.610  1.00 40.44
ATOM   1648  CB  ASN A 219       9.397  23.593 -21.227  1.00 42.31
ATOM   1649  CG  ASN A 219       8.128  23.943 -20.477  1.00 46.88
ATOM   1650  OD1 ASN A 219       8.081  24.917 -19.716  1.00 50.46
ATOM   1651  ND2 ASN A 219       7.085  23.151 -20.692  1.00 46.47
ATOM   1652  N   GLY A 220      10.838  21.045 -22.678  1.00 39.15
ATOM   1653  CA  GLY A 220      11.834  20.672 -23.656  1.00 37.68
ATOM   1654  C   GLY A 220      12.224  21.873 -24.498  1.00 36.77
ATOM   1655  O   GLY A 220      13.349  21.954 -24.975  1.00 37.24
ATOM   1656  N   ASP A 221      11.308  22.821 -24.675  1.00 37.01
ATOM   1657  CA  ASP A 221      11.618  23.995 -25.485  1.00 38.08
ATOM   1658  C   ASP A 221      12.227  25.172 -24.720  1.00 38.03
ATOM   1659  O   ASP A 221      12.353  26.269 -25.276  1.00 36.22
ATOM   1660  CB  ASP A 221      10.385  24.476 -26.263  1.00 38.88
ATOM   1661  CG  ASP A 221       9.219  24.861 -25.363  1.00 41.24
ATOM   1662  OD1 ASP A 221       9.417  25.104 -24.151  1.00 42.80
ATOM   1663  OD2 ASP A 221       8.091  24.936 -25.889  1.00 43.41
ATOM   1664  N   ASN A 222      12.604  24.949 -23.458  1.00 36.39
ATOM   1665  CA  ASN A 222      13.220  26.004 -22.647  1.00 35.79
ATOM   1666  C   ASN A 222      14.693  25.684 -22.474  1.00 35.70
ATOM   1667  O   ASN A 222      15.080  25.009 -21.525  1.00 35.22
ATOM   1668  CB  ASN A 222      12.553  26.107 -21.267  1.00 34.99
ATOM   1669  CG  ASN A 222      13.262  27.097 -20.336  1.00 35.28
ATOM   1670  OD1 ASN A 222      12.955  27.174 -19.144  1.00 30.93
ATOM   1671  ND2 ASN A 222      14.211  27.854 -20.880  1.00 35.07
ATOM   1672  N   LEU A 223      15.508  26.183 -23.397  1.00 38.60
ATOM   1673  CA  LEU A 223      16.947  25.947 -23.372  1.00 40.05
ATOM   1674  C   LEU A 223      17.701  26.553 -22.204  1.00 38.26
ATOM   1675  O   LEU A 223      18.823  26.150 -21.916  1.00 39.42
ATOM   1676  CB  LEU A 223      17.572  26.413 -24.686  1.00 43.47
ATOM   1677  CG  LEU A 223      17.357  25.345 -25.760  1.00 45.83
ATOM   1678  CD1 LEU A 223      17.885  25.824 -27.086  1.00 45.64
ATOM   1679  CD2 LEU A 223      18.044  24.045 -25.323  1.00 46.43
ATOM   1680  N   GLY A 224      17.094  27.515 -21.525  1.00 37.34
ATOM   1681  CA  GLY A 224      17.762  28.114 -20.387  1.00 34.68
ATOM   1682  C   GLY A 224      17.627  27.241 -19.150  1.00 34.13
ATOM   1683  O   GLY A 224      18.215  27.536 -18.120  1.00 33.75
ATOM   1684  N   ALA A 225      16.856  26.162 -19.247  1.00 32.94
ATOM   1685  CA  ALA A 225      16.658  25.270 -18.113  1.00 33.28
ATOM   1686  C   ALA A 225      17.689  24.148 -18.062  1.00 33.38
ATOM   1687  O   ALA A 225      17.437  23.042 -18.527  1.00 35.75
ATOM   1688  CB  ALA A 225      15.262  24.686 -18.154  1.00 31.54
ATOM   1689  N   THR A 226      18.847  24.432 -17.481  1.00 32.72
ATOM   1690  CA  THR A 226      19.906  23.437 -17.381  1.00 33.73
ATOM   1691  C   THR A 226      20.225  23.088 -15.924  1.00 34.83
ATOM   1692  O   THR A 226      19.782  23.770 -14.999  1.00 34.09
ATOM   1693  CB  THR A 226      21.202  23.938 -18.058  1.00 33.43
ATOM   1694  OG1 THR A 226      21.611  25.167 -17.452  1.00 33.26
ATOM   1695  CG2 THR A 226      20.976  24.169 -19.540  1.00 34.26
ATOM   1696  N   ILE A 227      20.998  22.022 -15.737  1.00 36.41
ATOM   1697  CA  ILE A 227      21.403  21.562 -14.409  1.00 37.22
ATOM   1698  C   ILE A 227      22.320  22.586 -13.747  1.00 37.78
ATOM   1699  O   ILE A 227      23.387  22.893 -14.266  1.00 37.02
ATOM   1700  CB  ILE A 227      22.175  20.210 -14.489  1.00 36.55
ATOM   1701  CG1 ILE A 227      21.221  19.075 -14.859  1.00 37.27
ATOM   1702  CG2 ILE A 227      22.846  19.903 -13.158  1.00 35.12
ATOM   1703  CD1 ILE A 227      20.219  18.754 -13.777  1.00 38.20
ATOM   1704  N   ASP A 228      21.900  23.126 -12.610  1.00 38.55
ATOM   1705  CA  ASP A 228      22.740  24.082 -11.900  1.00 40.20
ATOM   1706  C   ASP A 228      23.088  23.469 -10.550  1.00 39.07
ATOM   1707  O   ASP A 228      22.215  23.292  -9.695  1.00 39.77
ATOM   1708  CB  ASP A 228      22.018  25.433 -11.722  1.00 40.75
ATOM   1709  CG  ASP A 228      22.920  26.504 -11.102  1.00 41.23
ATOM   1710  OD1 ASP A 228      22.822  27.685 -11.501  1.00 42.75
ATOM   1711  OD2 ASP A 228      23.723  26.171 -10.207  1.00 43.04
ATOM   1712  N   LYS A 229      24.365  23.135 -10.372  1.00 38.91
ATOM   1713  CA  LYS A 229      24.839  22.518  -9.134  1.00 37.59
ATOM   1714  C   LYS A 229      24.562  23.332  -7.875  1.00 36.61
ATOM   1715  O   LYS A 229      24.550  22.783  -6.775  1.00 36.84
ATOM   1716  CB  LYS A 229      26.332  22.239  -9.217  1.00 40.02
ATOM   1717  CG  LYS A 229      26.733  21.189 -10.229  1.00 43.75
ATOM   1718  CD  LYS A 229      28.230  20.955 -10.127  1.00 50.53
ATOM   1719  CE  LYS A 229      28.754  20.001 -11.182  1.00 53.20
ATOM   1720  NZ  LYS A 229      30.239  19.897 -11.058  1.00 57.90
ATOM   1721  N   ARG A 230      24.352  24.634  -8.020  1.00 34.36
ATOM   1722  CA  ARG A 230      24.059  25.460  -6.859  1.00 34.06
ATOM   1723  C   ARG A 230      22.683  25.136  -6.292  1.00 33.36
ATOM   1724  O   ARG A 230      22.501  25.125  -5.085  1.00 34.82
ATOM   1725  CB  ARG A 230      24.142  26.938  -7.220  1.00 32.85
ATOM   1726  CG  ARG A 230      25.571  27.450  -7.289  1.00 35.09
ATOM   1727  CD  ARG A 230      25.623  28.847  -7.869  1.00 34.88
ATOM   1728  NE  ARG A 230      24.983  28.905  -9.179  1.00 30.14
ATOM   1729  CZ  ARG A 230      24.548  30.035  -9.719  1.00 33.95
ATOM   1730  NH1 ARG A 230      24.696  31.174  -9.051  1.00 32.06
ATOM   1731  NH2 ARG A 230      23.955  30.032 -10.907  1.00 31.03
ATOM   1732  N   VAL A 231      21.723  24.857  -7.166  1.00 33.66
ATOM   1733  CA  VAL A 231      20.366  24.527  -6.741  1.00 32.95
ATOM   1734  C   VAL A 231      20.314  23.238  -5.905  1.00 34.97
ATOM   1735  O   VAL A 231      19.620  23.174  -4.880  1.00 33.99
ATOM   1736  CB  VAL A 231      19.427  24.375  -7.965  1.00 30.39
ATOM   1737  CG1 VAL A 231      18.084  23.862  -7.529  1.00 28.68
ATOM   1738  CG2 VAL A 231      19.263  25.715  -8.657  1.00 28.90
ATOM   1739  N   LEU A 232      21.047  22.217  -6.343  1.00 33.16
ATOM   1740  CA  LEU A 232      21.069  20.950  -5.621  1.00 34.58
ATOM   1741  C   LEU A 232      21.719  21.120  -4.246  1.00 36.74
ATOM   1742  O   LEU A 232      21.290  20.507  -3.263  1.00 35.71
ATOM   1743  CB  LEU A 232      21.817  19.886  -6.439  1.00 32.24
ATOM   1744  CG  LEU A 232      21.127  19.466  -7.746  1.00 32.12
ATOM   1745  CD1 LEU A 232      22.073  18.650  -8.613  1.00 29.44
ATOM   1746  CD2 LEU A 232      19.865  18.672  -7.419  1.00 32.30
ATOM   1747  N   ALA A 233      22.747  21.959  -4.174  1.00 37.30
ATOM   1748  CA  ALA A 233      23.428  22.194  -2.906  1.00 39.17
ATOM   1749  C   ALA A 233      22.496  22.935  -1.963  1.00 40.68
ATOM   1750  O   ALA A 233      22.408  22.607  -0.780  1.00 42.38
ATOM   1751  CB  ALA A 233      24.697  23.007  -3.124  1.00 38.19
ATOM   1752  N   TYR A 234      21.801  23.939  -2.496  1.00 40.81
ATOM   1753  CA  TYR A 234      20.869  24.735  -1.701  1.00 40.69
ATOM   1754  C   TYR A 234      19.779  23.843  -1.096  1.00 40.90
ATOM   1755  O   TYR A 234      19.414  23.998   0.063  1.00 41.43
ATOM   1756  CB  TYR A 234      20.252  25.824  -2.583  1.00 37.99
ATOM   1757  CG  TYR A 234      19.172  26.681  -1.938  1.00 37.28
ATOM   1758  CD1 TYR A 234      19.482  27.627  -0.956  1.00 37.76
ATOM   1759  CD2 TYR A 234      17.845  26.584  -2.359  1.00 36.16
ATOM   1760  CE1 TYR A 234      18.488  28.464  -0.414  1.00 36.71
ATOM   1761  CE2 TYR A 234      16.851  27.404  -1.829  1.00 34.86
ATOM   1762  CZ  TYR A 234      17.175  28.341  -0.860  1.00 37.09
ATOM   1763  OH  TYR A 234      16.185  29.146  -0.355  1.00 34.72
ATOM   1764  N   MET A 235      19.279  22.896  -1.879  1.00 42.82
ATOM   1765  CA  MET A 235      18.233  22.000  -1.410  1.00 44.29
ATOM   1766  C   MET A 235      18.759  21.015  -0.374  1.00 45.83
ATOM   1767  O   MET A 235      18.043  20.647   0.561  1.00 47.17
ATOM   1768  CB  MET A 235      17.630  21.224  -2.578  1.00 44.15
ATOM   1769  CG  MET A 235      16.867  22.077  -3.570  1.00 46.89
ATOM   1770  SD  MET A 235      15.998  20.964  -4.875  1.00 48.31
ATOM   1771  CE  MET A 235      17.409  20.842  -6.159  1.00 47.68
ATOM   1772  N   GLU A 236      19.996  20.568  -0.555  1.00 44.48
ATOM   1773  CA  GLU A 236      20.600  19.642   0.389  1.00 44.33
ATOM   1774  C   GLU A 236      20.767  20.375   1.720  1.00 43.13
ATOM   1775  O   GLU A 236      20.493  19.822   2.787  1.00 41.77
ATOM   1776  CB  GLU A 236      21.960  19.169  -0.136  1.00 45.14
ATOM   1777  CG  GLU A 236      21.887  18.074  -1.187  1.00 45.46
ATOM   1778  CD  GLU A 236      21.730  16.702  -0.568  1.00 48.11
ATOM   1779  OE1 GLU A 236      22.558  16.364   0.302  1.00 50.38
ATOM   1780  OE2 GLU A 236      20.793  15.959  -0.941  1.00 48.36
ATOM   1781  N   LYS A 237      21.190  21.635   1.638  1.00 42.83
ATOM   1782  CA  LYS A 237      21.407  22.467   2.820  1.00 43.28
ATOM   1783  C   LYS A 237      20.126  22.874   3.552  1.00 44.51
ATOM   1784  O   LYS A 237      20.070  22.820   4.782  1.00 44.94
ATOM   1785  CB  LYS A 237      22.179  23.735   2.446  1.00 41.44
ATOM   1786  CG  LYS A 237      22.388  24.648   3.635  1.00 41.68
ATOM   1787  CD  LYS A 237      22.995  25.992   3.294  1.00 38.23
ATOM   1788  CE  LYS A 237      23.037  26.843   4.552  1.00 37.52
ATOM   1789  NZ  LYS A 237      23.485  28.237   4.316  1.00 40.16
ATOM   1790  N   GLU A 238      19.112  23.307   2.804  1.00 45.22
ATOM   1791  CA  GLU A 238      17.846  23.718   3.405  1.00 45.19
ATOM   1792  C   GLU A 238      16.899  22.535   3.582  1.00 45.95
ATOM   1793  O   GLU A 238      15.837  22.667   4.182  1.00 45.65
ATOM   1794  CB  GLU A 238      17.158  24.781   2.548  1.00 47.30
ATOM   1795  CG  GLU A 238      17.918  26.084   2.407  1.00 50.94
ATOM   1796  CD  GLU A 238      18.335  26.667   3.738  1.00 53.03
ATOM   1797  OE1 GLU A 238      17.537  26.583   4.694  1.00 55.12
ATOM   1798  OE2 GLU A 238      19.457  27.218   3.824  1.00 55.35
ATOM   1799  N   LYS A 239      17.281  21.379   3.056  1.00 46.57
ATOM   1800  CA  LYS A 239      16.450  20.189   3.173  1.00 46.74
ATOM   1801  C   LYS A 239      15.093  20.457   2.526  1.00 46.31
ATOM   1802  O   LYS A 239      14.036  20.310   3.153  1.00 46.87
ATOM   1803  CB  LYS A 239      16.266  19.817   4.649  1.00 48.94
ATOM   1804  CG  LYS A 239      17.552  19.817   5.463  1.00 51.41
ATOM   1805  CD  LYS A 239      17.380  19.084   6.795  1.00 56.69
ATOM   1806  CE  LYS A 239      17.180  17.581   6.567  1.00 60.31
ATOM   1807  NZ  LYS A 239      17.157  16.770   7.828  1.00 61.98
ATOM   1808  N   ILE A 240      15.136  20.861   1.263  1.00 43.34
ATOM   1809  CA  ILE A 240      13.934  21.164   0.503  1.00 40.73
ATOM   1810  C   ILE A 240      13.534  19.943  -0.321  1.00 39.12
ATOM   1811  O   ILE A 240      14.382  19.299  -0.923  1.00 38.00
ATOM   1812  CB  ILE A 240      14.189  22.380  -0.405  1.00 40.53
ATOM   1813  CG1 ILE A 240      14.579  23.578   0.470  1.00 40.98
ATOM   1814  CG2 ILE A 240      12.963  22.696  -1.228  1.00 38.77
ATOM   1815  CD1 ILE A 240      14.966  24.815  -0.303  1.00 41.16
ATOM   1816  N   ASP A 241      12.243  19.624  -0.337  1.00 37.76
ATOM   1817  CA  ASP A 241      11.753  18.458  -1.071  1.00 37.79
ATOM   1818  C   ASP A 241      11.122  18.796  -2.412  1.00 36.33
ATOM   1819  O   ASP A 241      10.899  17.920  -3.243  1.00 34.09
ATOM   1820  CB  ASP A 241      10.742  17.691  -0.215  1.00 40.09
ATOM   1821  CG  ASP A 241      11.331  17.239   1.102  1.00 42.73
ATOM   1822  OD1 ASP A 241      12.532  16.877   1.109  1.00 42.19
ATOM   1823  OD2 ASP A 241      10.599  17.237   2.117  1.00 41.41
ATOM   1824  N   PHE A 242      10.812  20.071  -2.605  1.00 34.96
ATOM   1825  CA  PHE A 242      10.226  20.535  -3.848  1.00 33.56
ATOM   1826  C   PHE A 242      10.610  21.995  -3.979  1.00 34.06
ATOM   1827  O   PHE A 242      10.359  22.786  -3.076  1.00 32.92
ATOM   1828  CB  PHE A 242       8.710  20.406  -3.821  1.00 32.52
ATOM   1829  CG  PHE A 242       8.047  20.786  -5.117  1.00 31.86
ATOM   1830  CD1 PHE A 242       7.644  19.809  -6.018  1.00 33.49
ATOM   1831  CD2 PHE A 242       7.853  22.122  -5.447  1.00 32.54
ATOM   1832  CE1 PHE A 242       7.057  20.151  -7.235  1.00 33.40
ATOM   1833  CE2 PHE A 242       7.272  22.477  -6.655  1.00 34.61
ATOM   1834  CZ  PHE A 242       6.873  21.487  -7.554  1.00 35.46
ATOM   1835  N   LEU A 243      11.217  22.345  -5.106  1.00 32.69
ATOM   1836  CA  LEU A 243      11.644  23.708  -5.325  1.00 33.16
ATOM   1837  C   LEU A 243      11.226  24.202  -6.704  1.00 33.60
ATOM   1838  O   LEU A 243      11.532  23.582  -7.724  1.00 34.09
ATOM   1839  CB  LEU A 243      13.166  23.807  -5.161  1.00 33.25
ATOM   1840  CG  LEU A 243      13.811  25.178  -5.358  1.00 35.39
ATOM   1841  CD1 LEU A 243      13.166  26.178  -4.412  1.00 39.59
ATOM   1842  CD2 LEU A 243      15.311  25.096  -5.102  1.00 37.31
ATOM   1843  N   MET A 244      10.517  25.323  -6.717  1.00 31.04
ATOM   1844  CA  MET A 244      10.059  25.933  -7.947  1.00 31.14
ATOM   1845  C   MET A 244      10.956  27.118  -8.269  1.00 30.97
ATOM   1846  O   MET A 244      11.230  27.944  -7.396  1.00 29.99
ATOM   1847  CB  MET A 244       8.620  26.432  -7.783  1.00 33.71
ATOM   1848  CG  MET A 244       8.107  27.298  -8.923  1.00 33.01
ATOM   1849  SD  MET A 244       6.320  27.977  -8.582  1.00 38.72
ATOM   1850  CE  MET A 244       5.408  26.291  -8.527  1.00 32.69
ATOM   1851  N   GLU A 245      11.429  27.198  -9.509  1.00 28.72
ATOM   1852  CA  GLU A 245      12.244  28.338  -9.900  1.00 28.59
ATOM   1853  C   GLU A 245      11.228  29.350 -10.417  1.00 28.31
ATOM   1854  O   GLU A 245      10.347  28.994 -11.203  1.00 24.53
ATOM   1855  CB  GLU A 245      13.218  27.992 -11.038  1.00 28.37
ATOM   1856  CG  GLU A 245      14.182  26.862 -10.779  1.00 27.26
ATOM   1857  CD  GLU A 245      15.234  26.783 -11.878  1.00 31.64
ATOM   1858  OE1 GLU A 245      15.980  25.783 -11.940  1.00 29.31
ATOM   1859  OE2 GLU A 245      15.315  27.735 -12.687  1.00 31.89
ATOM   1860  N   VAL A 246      11.353  30.600  -9.978  1.00 28.67
ATOM   1861  CA  VAL A 246      10.447  31.666 -10.401  1.00 29.58
ATOM   1862  C   VAL A 246      11.224  32.890 -10.899  1.00 32.55
ATOM   1863  O   VAL A 246      12.395  33.078 -10.555  1.00 33.71
ATOM   1864  CB  VAL A 246       9.548  32.152  -9.222  1.00 29.36
ATOM   1865  CG1 VAL A 246       8.635  31.037  -8.730  1.00 26.46
ATOM   1866  CG2 VAL A 246      10.420  32.661  -8.094  1.00 26.50
ATOM   1867  N   CYS A 247      10.560  33.722 -11.697  1.00 31.73
ATOM   1868  CA  CYS A 247      11.158  34.955 -12.197  1.00 36.31
ATOM   1869  C   CYS A 247      10.317  36.138 -11.726  1.00 37.03
ATOM   1870  O   CYS A 247       9.164  35.976 -11.347  1.00 37.34
ATOM   1871  CB  CYS A 247      11.213  34.958 -13.727  1.00 37.67
ATOM   1872  SG  CYS A 247      12.377  33.793 -14.393  1.00 40.60
ATOM   1873  N   ARG A 248      10.892  37.329 -11.737  1.00 41.05
ATOM   1874  CA  ARG A 248      10.134  38.501 -11.327  1.00 44.03
ATOM   1875  C   ARG A 248       9.193  38.816 -12.481  1.00 44.82
ATOM   1876  O   ARG A 248       9.607  38.808 -13.645  1.00 44.17
ATOM   1877  CB  ARG A 248      11.073  39.682 -11.056  1.00 46.67
ATOM   1878  CG  ARG A 248      10.671  40.507  -9.830  1.00 53.81
ATOM   1879  CD  ARG A 248      11.694  41.586  -9.505  1.00 58.94
ATOM   1880  NE  ARG A 248      13.027  41.026  -9.269  1.00 65.18
ATOM   1881  CZ  ARG A 248      13.390  40.352  -8.179  1.00 67.81
ATOM   1882  NH1 ARG A 248      12.522  40.142  -7.194  1.00 69.08
ATOM   1883  NH2 ARG A 248      14.628  39.882  -8.075  1.00 69.06
ATOM   1884  N   ARG A 249       7.922  39.059 -12.169  1.00 45.38
ATOM   1885  CA  ARG A 249       6.947  39.371 -13.205  1.00 47.23
ATOM   1886  C   ARG A 249       7.152  40.780 -13.735  1.00 49.42
ATOM   1887  O   ARG A 249       7.338  41.726 -12.966  1.00 50.35
ATOM   1888  CB  ARG A 249       5.515  39.255 -12.673  1.00 47.56
ATOM   1889  CG  ARG A 249       5.072  37.851 -12.290  1.00 48.75
ATOM   1890  CD  ARG A 249       3.694  37.891 -11.641  1.00 46.36
ATOM   1891  NE  ARG A 249       2.606  37.841 -12.610  1.00 44.14
ATOM   1892  CZ  ARG A 249       1.357  38.215 -12.346  1.00 42.84
ATOM   1893  NH1 ARG A 249       1.042  38.680 -11.151  1.00 39.74
ATOM   1894  NH2 ARG A 249       0.415  38.099 -13.272  1.00 43.11
ATOM   1895  N   THR A 250       7.116  40.908 -15.055  1.00 51.82
ATOM   1896  CA  THR A 250       7.267  42.199 -15.708  1.00 53.22
ATOM   1897  C   THR A 250       5.903  42.534 -16.289  1.00 55.58
ATOM   1898  O   THR A 250       5.005  41.692 -16.277  1.00 54.26
ATOM   1899  CB  THR A 250       8.294  42.127 -16.853  1.00 52.67
ATOM   1900  OG1 THR A 250       7.763  41.346 -17.931  1.00 49.33
ATOM   1901  CG2 THR A 250       9.580  41.486 -16.360  1.00 52.03
ATOM   1902  N   GLU A 251       5.753  43.755 -16.799  1.00 59.06
ATOM   1903  CA  GLU A 251       4.494  44.208 -17.391  1.00 62.22
ATOM   1904  C   GLU A 251       3.916  43.236 -18.417  1.00 62.19
ATOM   1905  O   GLU A 251       2.703  43.133 -18.571  1.00 61.60
ATOM   1906  CB  GLU A 251       4.685  45.575 -18.057  1.00 65.59
ATOM   1907  CG  GLU A 251       4.713  46.756 -17.094  1.00 70.55
ATOM   1908  CD  GLU A 251       3.460  46.833 -16.233  1.00 73.22
ATOM   1909  OE1 GLU A 251       2.354  46.595 -16.772  1.00 74.60
ATOM   1910  OE2 GLU A 251       3.585  47.141 -15.024  1.00 72.80
ATOM   1911  N   SER A 252       4.794  42.532 -19.121  1.00 63.60
ATOM   1912  CA  SER A 252       4.380  41.572 -20.139  1.00 64.75
ATOM   1913  C   SER A 252       3.828  40.278 -19.556  1.00 64.98
ATOM   1914  O   SER A 252       3.161  39.506 -20.250  1.00 65.08
ATOM   1915  CB  SER A 252       5.563  41.241 -21.047  1.00 65.81
ATOM   1916  OG  SER A 252       5.277  40.107 -21.847  1.00 68.63
ATOM   1917  N   ASP A 253       4.112  40.040 -18.281  1.00 64.98
ATOM   1918  CA  ASP A 253       3.656  38.829 -17.614  1.00 64.66
ATOM   1919  C   ASP A 253       2.370  39.020 -16.801  1.00 64.73
ATOM   1920  O   ASP A 253       1.791  38.043 -16.325  1.00 63.90
ATOM   1921  CB  ASP A 253       4.764  38.301 -16.691  1.00 64.46
ATOM   1922  CG  ASP A 253       6.094  38.123 -17.407  1.00 64.25
ATOM   1923  OD1 ASP A 253       6.133  37.368 -18.400  1.00 62.67
ATOM   1924  OD2 ASP A 253       7.099  38.732 -16.971  1.00 62.38
ATOM   1925  N   LYS A 254       1.913  40.262 -16.647  1.00 64.89
ATOM   1926  CA  LYS A 254       0.715  40.517 -15.850  1.00 66.85
ATOM   1927  C   LYS A 254      -0.534  39.746 -16.284  1.00 67.81
ATOM   1928  O   LYS A 254      -1.614  39.928 -15.717  1.00 68.69
ATOM   1929  CB  LYS A 254       0.405  42.020 -15.794  1.00 66.52
ATOM   1930  CG  LYS A 254      -0.060  42.639 -17.089  1.00 67.82
ATOM   1931  CD  LYS A 254      -0.607  44.040 -16.836  1.00 69.24
ATOM   1932  CE  LYS A 254      -1.097  44.686 -18.123  1.00 70.82
ATOM   1933  NZ  LYS A 254      -1.844  45.950 -17.872  1.00 70.78
ATOM   1934  N   LYS A 255      -0.383  38.880 -17.281  1.00 68.19
ATOM   1935  CA  LYS A 255      -1.490  38.069 -17.777  1.00 67.51
ATOM   1936  C   LYS A 255      -1.302  36.644 -17.281  1.00 65.56
ATOM   1937  O   LYS A 255      -2.271  35.923 -17.053  1.00 64.98
ATOM   1938  CB  LYS A 255      -1.503  38.062 -19.307  1.00 71.26
ATOM   1939  CG  LYS A 255      -0.287  37.379 -19.931  1.00 74.60
ATOM   1940  CD  LYS A 255      -0.365  37.387 -21.452  1.00 78.53
ATOM   1941  CE  LYS A 255       0.874  36.759 -22.086  1.00 80.42
ATOM   1942  NZ  LYS A 255       0.846  36.842 -23.578  1.00 79.66
ATOM   1943  N   GLY A 256      -0.040  36.251 -17.123  1.00 63.64
ATOM   1944  CA  GLY A 256       0.283  34.910 -16.669  1.00 60.32
ATOM   1945  C   GLY A 256       0.065  34.712 -15.183  1.00 58.92
ATOM   1946  O   GLY A 256      -0.160  35.673 -14.441  1.00 58.08
ATOM   1947  N   GLY A 257       0.135  33.457 -14.750  1.00 57.03
ATOM   1948  CA  GLY A 257      -0.065  33.142 -13.348  1.00 53.85
ATOM   1949  C   GLY A 257       1.023  33.691 -12.445  1.00 50.60
ATOM   1950  O   GLY A 257       1.963  34.328 -12.907  1.00 51.49
ATOM   1951  N   HIS A 258       0.897  33.433 -11.150  1.00 47.11
ATOM   1952  CA  HIS A 258       1.878  33.906 -10.188  1.00 42.68
ATOM   1953  C   HIS A 258       1.897  33.045  -8.930  1.00 39.97
ATOM   1954  O   HIS A 258       0.995  32.246  -8.681  1.00 38.61
ATOM   1955  CB  HIS A 258       1.581  35.358  -9.812  1.00 42.42
ATOM   1956  CG  HIS A 258       0.274  35.544  -9.108  1.00 43.13
ATOM   1957  ND1 HIS A 258       0.060  35.126  -7.813  1.00 42.55
ATOM   1958  CD2 HIS A 258      -0.890  36.097  -9.522  1.00 44.06
ATOM   1959  CE1 HIS A 258      -1.180  35.413  -7.459  1.00 43.85
ATOM   1960  NE2 HIS A 258      -1.778  36.003  -8.477  1.00 43.49
ATOM   1961  N   LEU A 259       2.948  33.223  -8.143  1.00 36.96
ATOM   1962  CA  LEU A 259       3.132  32.497  -6.904  1.00 33.61
ATOM   1963  C   LEU A 259       2.341  33.189  -5.805  1.00 34.00
ATOM   1964  O   LEU A 259       2.175  34.409  -5.819  1.00 33.78
ATOM   1965  CB  LEU A 259       4.611  32.506  -6.546  1.00 33.74
ATOM   1966  CG  LEU A 259       5.000  31.840  -5.239  1.00 31.98
ATOM   1967  CD1 LEU A 259       4.629  30.378  -5.296  1.00 29.92
ATOM   1968  CD2 LEU A 259       6.491  32.012  -5.012  1.00 34.36
ATOM   1969  N   ALA A 260       1.853  32.427  -4.841  1.00 33.79
ATOM   1970  CA  ALA A 260       1.103  33.049  -3.754  1.00 34.99
ATOM   1971  C   ALA A 260       1.206  32.233  -2.479  1.00 34.21
ATOM   1972  O   ALA A 260       1.600  31.078  -2.504  1.00 34.04
ATOM   1973  CB  ALA A 260      -0.374  33.243  -4.156  1.00 32.22
ATOM   1974  N   ARG A 261       0.845  32.848  -1.365  1.00 37.64
ATOM   1975  CA  ARG A 261       0.912  32.193  -0.066  1.00 41.65
ATOM   1976  C   ARG A 261      -0.515  31.896   0.381  1.00 41.70
ATOM   1977  O   ARG A 261      -1.445  32.608   0.025  1.00 42.12
ATOM   1978  CB  ARG A 261       1.597  33.136   0.928  1.00 45.40
ATOM   1979  CG  ARG A 261       2.331  32.487   2.081  1.00 51.98
ATOM   1980  CD  ARG A 261       2.614  33.548   3.140  1.00 58.37
ATOM   1981  NE  ARG A 261       1.358  34.086   3.673  1.00 63.81
ATOM   1982  CZ  ARG A 261       1.260  35.085   4.547  1.00 65.02
ATOM   1983  NH1 ARG A 261       2.348  35.685   5.013  1.00 66.35
ATOM   1984  NH2 ARG A 261       0.064  35.480   4.961  1.00 66.79
ATOM   1985  N   GLN A 262      -0.688  30.848   1.170  1.00 44.05
ATOM   1986  CA  GLN A 262      -2.013  30.478   1.642  1.00 44.83
ATOM   1987  C   GLN A 262      -1.876  29.825   3.012  1.00 45.35
ATOM   1988  O   GLN A 262      -0.904  29.117   3.266  1.00 45.55
ATOM   1989  CB  GLN A 262      -2.642  29.505   0.644  1.00 46.09
ATOM   1990  CG  GLN A 262      -4.081  29.145   0.904  1.00 46.81
ATOM   1991  CD  GLN A 262      -4.658  28.277  -0.200  1.00 48.49
ATOM   1992  OE1 GLN A 262      -4.236  27.139  -0.400  1.00 46.72
ATOM   1993  NE2 GLN A 262      -5.627  28.817  -0.927  1.00 51.09
ATOM   1994  N   THR A 263      -2.835  30.067   3.898  1.00 45.52
ATOM   1995  CA  THR A 263      -2.789  29.477   5.233  1.00 46.45
ATOM   1996  C   THR A 263      -3.894  28.449   5.398  1.00 48.22
ATOM   1997  O   THR A 263      -5.065  28.756   5.180  1.00 49.07
ATOM   1998  CB  THR A 263      -2.961  30.540   6.332  1.00 47.29
ATOM   1999  OG1 THR A 263      -1.837  31.432   6.328  1.00 46.10
ATOM   2000  CG2 THR A 263      -3.070  29.871   7.694  1.00 46.46
ATOM   2001  N   VAL A 264      -3.526  27.233   5.787  1.00 49.44
ATOM   2002  CA  VAL A 264      -4.509  26.175   5.973  1.00 51.92
ATOM   2003  C   VAL A 264      -4.575  25.623   7.392  1.00 55.59
ATOM   2004  O   VAL A 264      -3.659  25.800   8.198  1.00 54.71
ATOM   2005  CB  VAL A 264      -4.252  24.984   5.024  1.00 51.08
ATOM   2006  CG1 VAL A 264      -4.260  25.459   3.581  1.00 50.41
ATOM   2007  CG2 VAL A 264      -2.934  24.310   5.369  1.00 48.63
ATOM   2008  N   TYR A 265      -5.683  24.949   7.676  1.00 58.40
ATOM   2009  CA  TYR A 265      -5.934  24.321   8.962  1.00 62.30
ATOM   2010  C   TYR A 265      -6.458  22.933   8.608  1.00 67.08
ATOM   2011  O   TYR A 265      -7.540  22.811   8.030  1.00 68.61
ATOM   2012  CB  TYR A 265      -7.007  25.097   9.724  1.00 60.54
ATOM   2013  CG  TYR A 265      -7.488  24.411  10.981  1.00 60.44
ATOM   2014  CD1 TYR A 265      -6.955  24.737  12.225  1.00 60.49
ATOM   2015  CD2 TYR A 265      -8.470  23.422  10.925  1.00 60.16
ATOM   2016  CE1 TYR A 265      -7.386  24.099  13.381  1.00 61.14
ATOM   2017  CE2 TYR A 265      -8.907  22.776  12.074  1.00 61.57
ATOM   2018  CZ  TYR A 265      -8.361  23.119  13.299  1.00 61.94
ATOM   2019  OH  TYR A 265      -8.787  22.478  14.440  1.00 63.44
ATOM   2020  N   VAL A 266      -5.702  21.892   8.942  1.00 71.89
ATOM   2021  CA  VAL A 266      -6.117  20.526   8.622  1.00 77.10
ATOM   2022  C   VAL A 266      -6.592  19.738   9.849  1.00 80.31
ATOM   2023  O   VAL A 266      -5.951  19.753  10.903  1.00 81.81
ATOM   2024  CB  VAL A 266      -4.966  19.749   7.942  1.00 77.80
ATOM   2025  CG1 VAL A 266      -5.495  18.449   7.347  1.00 77.88
ATOM   2026  CG2 VAL A 266      -4.314  20.613   6.867  1.00 77.45
ATOM   2027  N   LYS A 267      -7.718  19.045   9.705  1.00 83.41
ATOM   2028  CA  LYS A 267      -8.272  18.263  10.804  1.00 86.39
ATOM   2029  C   LYS A 267      -7.354  17.114  11.209  1.00 88.21
ATOM   2030  O   LYS A 267      -6.678  17.182  12.235  1.00 88.41
ATOM   2031  CB  LYS A 267      -9.646  17.704  10.424  1.00 86.87
ATOM   2032  CG  LYS A 267     -10.333  16.950  11.555  1.00 87.72
ATOM   2033  CD  LYS A 267     -11.672  16.371  11.124  1.00 88.31
ATOM   2034  CE  LYS A 267     -11.501  15.293  10.066  1.00 88.73
ATOM   2035  NZ  LYS A 267     -12.807  14.692   9.677  1.00 89.01
ATOM   2036  N   GLY A 268      -7.335  16.061  10.397  1.00 90.26
ATOM   2037  CA  GLY A 268      -6.505  14.910  10.704  1.00 92.79
ATOM   2038  C   GLY A 268      -7.085  14.147  11.878  1.00 94.53
ATOM   2039  O   GLY A 268      -6.953  14.570  13.026  1.00 94.70
ATOM   2040  N   LYS A 269      -7.730  13.020  11.593  1.00 96.23
ATOM   2041  CA  LYS A 269      -8.343  12.210  12.638  1.00 97.95
ATOM   2042  C   LYS A 269      -7.647  10.864  12.813  1.00 98.81
ATOM   2043  O   LYS A 269      -7.423  10.138  11.844  1.00 99.00
ATOM   2044  CB  LYS A 269      -9.824  11.984  12.321  1.00 98.38
ATOM   2045  CG  LYS A 269     -10.612  11.334  13.446  1.00 99.02
ATOM   2046  CD  LYS A 269     -10.672  12.238  14.669  1.00 99.46
ATOM   2047  CE  LYS A 269     -11.457  11.593  15.799  1.00 99.77
ATOM   2048  NZ  LYS A 269     -10.834  10.320  16.251  1.00 99.95
ATOM   2049  N   ASP A 270      -7.312  10.540  14.058  1.00 99.75
ATOM   2050  CA  ASP A 270      -6.645   9.285  14.384  1.00100.54
ATOM   2051  C   ASP A 270      -5.365   9.093  13.578  1.00100.70
ATOM   2052  O   ASP A 270      -5.290   8.244  12.688  1.00100.83
ATOM   2053  CB  ASP A 270      -7.600   8.112  14.154  1.00101.13
ATOM   2054  CG  ASP A 270      -8.839   8.196  15.023  1.00101.63
ATOM   2055  OD1 ASP A 270      -8.694   8.220  16.264  1.00101.90
ATOM   2056  OD2 ASP A 270      -9.957   8.240  14.468  1.00101.86
ATOM   2057  N   GLY A 271      -4.361   9.896  13.911  1.00100.73
ATOM   2058  CA  GLY A 271      -3.076   9.842  13.241  1.00100.62
ATOM   2059  C   GLY A 271      -2.246  10.988  13.778  1.00100.45
ATOM   2060  O   GLY A 271      -1.235  10.785  14.451  1.00100.56
ATOM   2061  N   GLN A 272      -2.690  12.203  13.479  1.00100.12
ATOM   2062  CA  GLN A 272      -2.031  13.415  13.943  1.00 99.64
ATOM   2063  C   GLN A 272      -3.123  14.433  14.253  1.00 98.89
ATOM   2064  O   GLN A 272      -4.082  14.576  13.494  1.00 99.00
ATOM   2065  CB  GLN A 272      -1.083  13.965  12.872  1.00100.10
ATOM   2066  CG  GLN A 272      -1.752  14.340  11.560  1.00100.67
ATOM   2067  CD  GLN A 272      -0.778  14.940  10.564  1.00100.98
ATOM   2068  OE1 GLN A 272       0.214  14.312  10.193  1.00101.19
ATOM   2069  NE2 GLN A 272      -1.057  16.161  10.125  1.00101.16
ATOM   2070  N   PRO A 273      -2.998  15.150  15.380  1.00 98.00
ATOM   2071  CA  PRO A 273      -4.003  16.147  15.758  1.00 97.00
ATOM   2072  C   PRO A 273      -4.165  17.260  14.728  1.00 95.85
ATOM   2073  O   PRO A 273      -3.521  17.249  13.678  1.00 95.88
ATOM   2074  CB  PRO A 273      -3.484  16.661  17.099  1.00 97.36
ATOM   2075  CG  PRO A 273      -2.001  16.544  16.945  1.00 97.70
ATOM   2076  CD  PRO A 273      -1.855  15.181  16.309  1.00 97.92
ATOM   2077  N   ASP A 274      -5.034  18.217  15.035  1.00 94.33
ATOM   2078  CA  ASP A 274      -5.289  19.341  14.144  1.00 92.58
ATOM   2079  C   ASP A 274      -4.010  20.131  13.895  1.00 91.07
ATOM   2080  O   ASP A 274      -3.033  19.992  14.631  1.00 91.01
ATOM   2081  CB  ASP A 274      -6.360  20.251  14.747  1.00 93.03
ATOM   2082  CG  ASP A 274      -7.673  19.526  14.982  1.00 93.24
ATOM   2083  OD1 ASP A 274      -8.605  20.145  15.536  1.00 93.42
ATOM   2084  OD2 ASP A 274      -7.772  18.337  14.613  1.00 93.40
ATOM   2085  N   ALA A 275      -4.021  20.962  12.857  1.00 88.96
ATOM   2086  CA  ALA A 275      -2.848  21.761  12.516  1.00 87.09
ATOM   2087  C   ALA A 275      -3.145  22.968  11.624  1.00 85.09
ATOM   2088  O   ALA A 275      -4.099  22.964  10.846  1.00 84.70
ATOM   2089  CB  ALA A 275      -1.810  20.877  11.841  1.00 87.59
ATOM   2090  N   GLU A 276      -2.308  23.996  11.744  1.00 81.97
ATOM   2091  CA  GLU A 276      -2.441  25.212  10.949  1.00 78.96
ATOM   2092  C   GLU A 276      -1.131  25.460  10.196  1.00 76.57
ATOM   2093  O   GLU A 276      -0.139  25.879  10.792  1.00 77.13
ATOM   2094  CB  GLU A 276      -2.767  26.404  11.857  1.00 79.36
ATOM   2095  CG  GLU A 276      -2.742  27.752  11.146  1.00 81.09
ATOM   2096  CD  GLU A 276      -3.248  28.902  12.008  1.00 82.74
ATOM   2097  OE1 GLU A 276      -4.454  28.914  12.339  1.00 82.42
ATOM   2098  OE2 GLU A 276      -2.440  29.798  12.350  1.00 83.03
ATOM   2099  N   LYS A 277      -1.133  25.200   8.887  1.00 73.36
ATOM   2100  CA  LYS A 277       0.060  25.376   8.051  1.00 69.53
ATOM   2101  C   LYS A 277      -0.017  26.493   7.014  1.00 65.91
ATOM   2102  O   LYS A 277      -1.085  26.864   6.538  1.00 64.24
ATOM   2103  CB  LYS A 277       0.392  24.078   7.302  1.00 70.15
ATOM   2104  CG  LYS A 277       0.863  22.929   8.174  1.00 73.40
ATOM   2105  CD  LYS A 277       1.163  21.684   7.342  1.00 75.11
ATOM   2106  CE  LYS A 277      -0.078  21.175   6.616  1.00 75.78
ATOM   2107  NZ  LYS A 277       0.199  19.942   5.824  1.00 77.45
ATOM   2108  N   ARG A 278       1.147  27.013   6.657  1.00 62.64
ATOM   2109  CA  ARG A 278       1.231  28.047   5.647  1.00 60.21
ATOM   2110  C   ARG A 278       1.844  27.379   4.410  1.00 56.99
ATOM   2111  O   ARG A 278       2.991  26.936   4.437  1.00 56.51
ATOM   2112  CB  ARG A 278       2.107  29.196   6.145  1.00 62.63
ATOM   2113  CG  ARG A 278       2.386  30.261   5.098  1.00 66.88
ATOM   2114  CD  ARG A 278       3.089  31.477   5.692  1.00 69.24
ATOM   2115  NE  ARG A 278       2.179  32.300   6.487  1.00 70.77
ATOM   2116  CZ  ARG A 278       2.485  33.504   6.960  1.00 70.80
ATOM   2117  NH1 ARG A 278       3.683  34.026   6.716  1.00 68.88
ATOM   2118  NH2 ARG A 278       1.591  34.189   7.665  1.00 69.18
ATOM   2119  N   VAL A 279       1.065  27.273   3.337  1.00 52.39
ATOM   2120  CA  VAL A 279       1.555  26.645   2.118  1.00 46.95
ATOM   2121  C   VAL A 279       1.814  27.656   1.026  1.00 42.61
ATOM   2122  O   VAL A 279       1.518  28.840   1.167  1.00 41.87
ATOM   2123  CB  VAL A 279       0.569  25.609   1.550  1.00 47.01
ATOM   2124  CG1 VAL A 279       0.265  24.549   2.592  1.00 48.73
ATOM   2125  CG2 VAL A 279      -0.685  26.302   1.080  1.00 47.52
ATOM   2126  N   LEU A 280       2.367  27.153  -0.068  1.00 38.32
ATOM   2127  CA  LEU A 280       2.707  27.944  -1.241  1.00 34.71
ATOM   2128  C   LEU A 280       1.878  27.369  -2.384  1.00 33.70
ATOM   2129  O   LEU A 280       1.696  26.152  -2.473  1.00 29.89
ATOM   2130  CB  LEU A 280       4.195  27.770  -1.546  1.00 33.53
ATOM   2131  CG  LEU A 280       5.134  28.956  -1.755  1.00 36.96
ATOM   2132  CD1 LEU A 280       4.828  30.070  -0.791  1.00 38.18
ATOM   2133  CD2 LEU A 280       6.565  28.481  -1.572  1.00 36.69
ATOM   2134  N   LEU A 281       1.359  28.230  -3.247  1.00 32.66
ATOM   2135  CA  LEU A 281       0.580  27.733  -4.364  1.00 35.09
ATOM   2136  C   LEU A 281       0.708  28.654  -5.558  1.00 37.04
ATOM   2137  O   LEU A 281       1.323  29.723  -5.476  1.00 35.52
ATOM   2138  CB  LEU A 281      -0.896  27.584  -3.982  1.00 34.72
ATOM   2139  CG  LEU A 281      -1.806  28.802  -4.136  1.00 34.46
ATOM   2140  CD1 LEU A 281      -3.204  28.429  -3.676  1.00 35.50
ATOM   2141  CD2 LEU A 281      -1.268  29.966  -3.334  1.00 36.38
ATOM   2142  N   LEU A 282       0.099  28.222  -6.655  1.00 39.06
ATOM   2143  CA  LEU A 282       0.110  28.947  -7.916  1.00 42.65
ATOM   2144  C   LEU A 282      -1.322  29.357  -8.260  1.00 43.63
ATOM   2145  O   LEU A 282      -2.261  28.630  -7.963  1.00 45.31
ATOM   2146  CB  LEU A 282       0.639  28.017  -9.004  1.00 43.39
ATOM   2147  CG  LEU A 282       1.541  28.549 -10.104  1.00 45.29
ATOM   2148  CD1 LEU A 282       2.839  29.072  -9.499  1.00 47.30
ATOM   2149  CD2 LEU A 282       1.826  27.414 -11.079  1.00 47.03
ATOM   2150  N   ARG A 283      -1.500  30.520  -8.870  1.00 44.78
ATOM   2151  CA  ARG A 283      -2.838  30.931  -9.266  1.00 46.76
ATOM   2152  C   ARG A 283      -2.812  31.385 -10.716  1.00 50.08
ATOM   2153  O   ARG A 283      -2.106  32.328 -11.062  1.00 51.00
ATOM   2154  CB  ARG A 283      -3.375  32.063  -8.389  1.00 43.07
ATOM   2155  CG  ARG A 283      -4.839  32.358  -8.672  1.00 41.31
ATOM   2156  CD  ARG A 283      -5.442  33.396  -7.751  1.00 42.58
ATOM   2157  NE  ARG A 283      -4.843  34.712  -7.939  1.00 43.02
ATOM   2158  CZ  ARG A 283      -5.257  35.816  -7.328  1.00 42.76
ATOM   2159  NH1 ARG A 283      -6.280  35.775  -6.484  1.00 46.36
ATOM   2160  NH2 ARG A 283      -4.651  36.964  -7.564  1.00 41.84
ATOM   2161  N   GLU A 284      -3.577  30.709 -11.564  1.00 53.86
ATOM   2162  CA  GLU A 284      -3.623  31.073 -12.974  1.00 58.12
ATOM   2163  C   GLU A 284      -4.732  32.105 -13.139  1.00 59.12
ATOM   2164  O   GLU A 284      -5.459  32.390 -12.191  1.00 58.93
ATOM   2165  CB  GLU A 284      -3.905  29.836 -13.833  1.00 59.38
ATOM   2166  CG  GLU A 284      -3.081  28.603 -13.436  1.00 63.30
ATOM   2167  CD  GLU A 284      -1.600  28.697 -13.806  1.00 65.64
ATOM   2168  OE1 GLU A 284      -1.010  29.796 -13.695  1.00 65.85
ATOM   2169  OE2 GLU A 284      -1.023  27.653 -14.193  1.00 66.05
ATOM   2170  N   SER A 285      -4.845  32.681 -14.328  1.00 60.75
ATOM   2171  CA  SER A 285      -5.878  33.679 -14.596  1.00 62.93
ATOM   2172  C   SER A 285      -7.248  33.013 -14.498  1.00 63.66
ATOM   2173  O   SER A 285      -8.202  33.578 -13.956  1.00 63.10
ATOM   2174  CB  SER A 285      -5.695  34.251 -16.000  1.00 63.72
ATOM   2175  OG  SER A 285      -5.699  33.204 -16.961  1.00 63.42
ATOM   2176  N   ALA A 286      -7.328  31.802 -15.039  1.00 64.44
ATOM   2177  CA  ALA A 286      -8.558  31.031 -15.027  1.00 65.18
ATOM   2178  C   ALA A 286      -9.194  31.047 -13.642  1.00 65.35
ATOM   2179  O   ALA A 286     -10.355  31.431 -13.489  1.00 64.82
ATOM   2180  CB  ALA A 286      -8.266  29.599 -15.447  1.00 65.50
ATOM   2181  N   GLN A 287      -8.412  30.640 -12.643  1.00 64.99
ATOM   2182  CA  GLN A 287      -8.857  30.565 -11.251  1.00 64.41
ATOM   2183  C   GLN A 287      -9.072  31.922 -10.566  1.00 64.18
ATOM   2184  O   GLN A 287      -9.391  31.969  -9.378  1.00 63.99
ATOM   2185  CB  GLN A 287      -7.846  29.752 -10.432  1.00 64.89
ATOM   2186  CG  GLN A 287      -7.297  28.522 -11.144  1.00 66.80
ATOM   2187  CD  GLN A 287      -6.084  27.920 -10.437  1.00 68.71
ATOM   2188  OE1 GLN A 287      -6.213  27.245  -9.413  1.00 68.14
ATOM   2189  NE2 GLN A 287      -4.897  28.173 -10.981  1.00 67.86
ATOM   2190  N   CYS A 288      -8.907  33.022 -11.293  1.00 63.50
ATOM   2191  CA  CYS A 288      -9.095  34.333 -10.679  1.00 64.47
ATOM   2192  C   CYS A 288     -10.387  35.033 -11.090  1.00 67.03
ATOM   2193  O   CYS A 288     -10.643  35.253 -12.276  1.00 67.99
ATOM   2194  CB  CYS A 288      -7.908  35.255 -10.985  1.00 61.55
ATOM   2195  SG  CYS A 288      -7.974  36.869 -10.127  1.00 56.57
ATOM   2196  N   PRO A 289     -11.221  35.392 -10.100  1.00 68.53
ATOM   2197  CA  PRO A 289     -12.500  36.076 -10.301  1.00 70.37
ATOM   2198  C   PRO A 289     -12.278  37.512 -10.763  1.00 71.73
ATOM   2199  O   PRO A 289     -11.442  38.225 -10.209  1.00 71.43
ATOM   2200  CB  PRO A 289     -13.141  36.005  -8.920  1.00 70.02
ATOM   2201  CG  PRO A 289     -11.956  36.065  -8.011  1.00 69.48
ATOM   2202  CD  PRO A 289     -11.017  35.092  -8.672  1.00 68.39
ATOM   2203  N   LYS A 290     -13.036  37.928 -11.774  1.00 73.68
ATOM   2204  CA  LYS A 290     -12.916  39.270 -12.337  1.00 75.25
ATOM   2205  C   LYS A 290     -12.890  40.386 -11.300  1.00 75.60
ATOM   2206  O   LYS A 290     -12.451  41.500 -11.591  1.00 75.48
ATOM   2207  CB  LYS A 290     -14.040  39.522 -13.354  1.00 76.79
ATOM   2208  CG  LYS A 290     -15.442  39.162 -12.871  1.00 79.47
ATOM   2209  CD  LYS A 290     -16.471  39.299 -13.993  1.00 80.90
ATOM   2210  CE  LYS A 290     -17.850  38.812 -13.551  1.00 83.09
ATOM   2211  NZ  LYS A 290     -18.885  38.939 -14.625  1.00 84.20
ATOM   2212  N   ALA A 291     -13.353  40.093 -10.092  1.00 75.67
ATOM   2213  CA  ALA A 291     -13.360  41.095  -9.035  1.00 76.34
ATOM   2214  C   ALA A 291     -11.931  41.371  -8.572  1.00 76.49
ATOM   2215  O   ALA A 291     -11.604  42.484  -8.160  1.00 76.38
ATOM   2216  CB  ALA A 291     -14.212  40.611  -7.863  1.00 77.01
ATOM   2217  N   ASP A 292     -11.083  40.349  -8.654  1.00 76.72
ATOM   2218  CA  ASP A 292      -9.686  40.458  -8.239  1.00 76.91
ATOM   2219  C   ASP A 292      -8.745  40.386  -9.430  1.00 77.19
ATOM   2220  O   ASP A 292      -7.529  40.282  -9.263  1.00 76.68
ATOM   2221  CB  ASP A 292      -9.329  39.325  -7.279  1.00 76.09
ATOM   2222  CG  ASP A 292     -10.264  39.242  -6.104  1.00 73.90
ATOM   2223  OD1 ASP A 292     -10.406  40.259  -5.389  1.00 73.07
ATOM   2224  OD2 ASP A 292     -10.849  38.157  -5.898  1.00 73.01
ATOM   2225  N   MET A 293      -9.309  40.427 -10.630  1.00 77.85
ATOM   2226  CA  MET A 293      -8.501  40.349 -11.833  1.00 77.85
ATOM   2227  C   MET A 293      -7.514  41.498 -11.907  1.00 75.47
ATOM   2228  O   MET A 293      -6.404  41.334 -12.406  1.00 74.91
ATOM   2229  CB  MET A 293      -9.384  40.348 -13.078  1.00 82.57
ATOM   2230  CG  MET A 293      -8.618  40.003 -14.331  1.00 87.91
ATOM   2231  SD  MET A 293      -7.521  38.438 -14.016  1.00 96.95
ATOM   2232  CE  MET A 293      -8.809  37.056 -14.444  1.00 94.07
ATOM   2233  N   GLU A 294      -7.914  42.663 -11.414  1.00 73.02
ATOM   2234  CA  GLU A 294      -7.016  43.803 -11.438  1.00 71.45
ATOM   2235  C   GLU A 294      -5.844  43.484 -10.523  1.00 69.80
ATOM   2236  O   GLU A 294      -4.685  43.719 -10.867  1.00 69.13
ATOM   2237  CB  GLU A 294      -7.721  45.074 -10.960  1.00 72.18
ATOM   2238  CG  GLU A 294      -6.821  46.302 -11.010  1.00 74.08
ATOM   2239  CD  GLU A 294      -7.548  47.591 -10.688  1.00 76.34
ATOM   2240  OE1 GLU A 294      -8.464  47.970 -11.451  1.00 76.92
ATOM   2241  OE2 GLU A 294      -7.200  48.229  -9.670  1.00 77.18
ATOM   2242  N   SER A 295      -6.162  42.933  -9.356  1.00 67.41
ATOM   2243  CA  SER A 295      -5.151  42.566  -8.373  1.00 64.44
ATOM   2244  C   SER A 295      -4.209  41.502  -8.960  1.00 61.63
ATOM   2245  O   SER A 295      -2.998  41.533  -8.733  1.00 60.35
ATOM   2246  CB  SER A 295      -5.838  42.037  -7.107  1.00 64.20
ATOM   2247  OG  SER A 295      -4.932  41.923  -6.025  1.00 63.39
ATOM   2248  N   PHE A 296      -4.773  40.575  -9.727  1.00 58.07
ATOM   2249  CA  PHE A 296      -3.994  39.506 -10.349  1.00 56.11
ATOM   2250  C   PHE A 296      -2.886  40.054 -11.248  1.00 55.55
ATOM   2251  O   PHE A 296      -1.845  39.422 -11.410  1.00 53.13
ATOM   2252  CB  PHE A 296      -4.918  38.610 -11.178  1.00 53.49
ATOM   2253  CG  PHE A 296      -4.225  37.443 -11.828  1.00 50.36
ATOM   2254  CD1 PHE A 296      -4.208  36.199 -11.213  1.00 49.70
ATOM   2255  CD2 PHE A 296      -3.614  37.582 -13.074  1.00 49.69
ATOM   2256  CE1 PHE A 296      -3.593  35.101 -11.833  1.00 50.83
ATOM   2257  CE2 PHE A 296      -2.999  36.495 -13.700  1.00 48.09
ATOM   2258  CZ  PHE A 296      -2.989  35.254 -13.080  1.00 49.07
ATOM   2259  N   GLN A 297      -3.116  41.232 -11.826  1.00 56.63
ATOM   2260  CA  GLN A 297      -2.146  41.850 -12.727  1.00 57.64
ATOM   2261  C   GLN A 297      -1.187  42.821 -12.054  1.00 57.44
ATOM   2262  O   GLN A 297      -0.253  43.307 -12.685  1.00 58.99
ATOM   2263  CB  GLN A 297      -2.864  42.571 -13.867  1.00 57.92
ATOM   2264  CG  GLN A 297      -3.807  41.686 -14.662  1.00 59.74
ATOM   2265  CD  GLN A 297      -4.450  42.421 -15.822  1.00 62.30
ATOM   2266  OE1 GLN A 297      -4.707  43.625 -15.744  1.00 62.55
ATOM   2267  NE2 GLN A 297      -4.729  41.696 -16.902  1.00 63.52
ATOM   2268  N   ASP A 298      -1.411  43.107 -10.780  1.00 56.59
ATOM   2269  CA  ASP A 298      -0.535  44.020 -10.059  1.00 56.40
ATOM   2270  C   ASP A 298       0.818  43.349  -9.816  1.00 56.61
ATOM   2271  O   ASP A 298       1.096  42.869  -8.711  1.00 56.18
ATOM   2272  CB  ASP A 298      -1.180  44.414  -8.731  1.00 56.14
ATOM   2273  CG  ASP A 298      -0.314  45.345  -7.922  1.00 56.77
ATOM   2274  OD1 ASP A 298      -0.784  45.843  -6.872  1.00 57.84
ATOM   2275  OD2 ASP A 298       0.840  45.578  -8.335  1.00 57.26
ATOM   2276  N   ILE A 299       1.658  43.329 -10.850  1.00 55.66
ATOM   2277  CA  ILE A 299       2.972  42.699 -10.770  1.00 55.22
ATOM   2278  C   ILE A 299       3.842  43.161  -9.604  1.00 55.30
ATOM   2279  O   ILE A 299       4.930  42.620  -9.384  1.00 55.89
ATOM   2280  CB  ILE A 299       3.772  42.887 -12.073  1.00 54.77
ATOM   2281  CG1 ILE A 299       4.094  44.365 -12.284  1.00 56.31
ATOM   2282  CG2 ILE A 299       2.984  42.339 -13.248  1.00 53.92
ATOM   2283  CD1 ILE A 299       5.062  44.617 -13.425  1.00 56.41
ATOM   2284  N   ASN A 300       3.380  44.157  -8.858  1.00 55.08
ATOM   2285  CA  ASN A 300       4.143  44.629  -7.708  1.00 56.38
ATOM   2286  C   ASN A 300       3.665  43.940  -6.425  1.00 56.24
ATOM   2287  O   ASN A 300       4.372  43.933  -5.418  1.00 56.42
ATOM   2288  CB  ASN A 300       4.037  46.151  -7.577  1.00 58.56
ATOM   2289  CG  ASN A 300       4.955  46.887  -8.550  1.00 61.17
ATOM   2290  OD1 ASN A 300       6.184  46.823  -8.432  1.00 59.48
ATOM   2291  ND2 ASN A 300       4.362  47.587  -9.518  1.00 61.69
ATOM   2292  N   LYS A 301       2.463  43.365  -6.468  1.00 55.75
ATOM   2293  CA  LYS A 301       1.918  42.647  -5.320  1.00 54.62
ATOM   2294  C   LYS A 301       2.371  41.197  -5.492  1.00 52.85
ATOM   2295  O   LYS A 301       3.051  40.639  -4.632  1.00 53.06
ATOM   2296  CB  LYS A 301       0.385  42.720  -5.294  1.00 56.00
ATOM   2297  CG  LYS A 301      -0.207  42.256  -3.963  1.00 57.98
ATOM   2298  CD  LYS A 301      -1.711  41.986  -4.019  1.00 61.54
ATOM   2299  CE  LYS A 301      -2.556  43.249  -4.020  1.00 62.52
ATOM   2300  NZ  LYS A 301      -2.504  43.985  -5.311  1.00 67.42
ATOM   2301  N   TYR A 302       1.986  40.600  -6.617  1.00 50.59
ATOM   2302  CA  TYR A 302       2.377  39.235  -6.959  1.00 48.74
ATOM   2303  C   TYR A 302       3.443  39.395  -8.048  1.00 48.68
ATOM   2304  O   TYR A 302       3.142  39.442  -9.245  1.00 47.01
ATOM   2305  CB  TYR A 302       1.177  38.455  -7.490  1.00 48.88
ATOM   2306  CG  TYR A 302       0.040  38.411  -6.508  1.00 51.55
ATOM   2307  CD1 TYR A 302      -1.151  39.093  -6.761  1.00 51.39
ATOM   2308  CD2 TYR A 302       0.173  37.733  -5.289  1.00 51.26
ATOM   2309  CE1 TYR A 302      -2.185  39.110  -5.828  1.00 52.85
ATOM   2310  CE2 TYR A 302      -0.853  37.745  -4.345  1.00 53.16
ATOM   2311  CZ  TYR A 302      -2.032  38.437  -4.619  1.00 54.31
ATOM   2312  OH  TYR A 302      -3.044  38.477  -3.683  1.00 53.50
ATOM   2313  N   SER A 303       4.693  39.481  -7.609  1.00 47.18
ATOM   2314  CA  SER A 303       5.818  39.698  -8.503  1.00 45.52
ATOM   2315  C   SER A 303       6.583  38.467  -8.973  1.00 44.15
ATOM   2316  O   SER A 303       7.679  38.599  -9.511  1.00 44.38
ATOM   2317  CB  SER A 303       6.784  40.665  -7.830  1.00 47.40
ATOM   2318  OG  SER A 303       6.998  40.266  -6.486  1.00 51.05
ATOM   2319  N   PHE A 304       6.023  37.276  -8.791  1.00 40.30
ATOM   2320  CA  PHE A 304       6.720  36.075  -9.225  1.00 37.60
ATOM   2321  C   PHE A 304       5.849  35.117 -10.026  1.00 37.35
ATOM   2322  O   PHE A 304       4.675  34.912  -9.719  1.00 38.06
ATOM   2323  CB  PHE A 304       7.310  35.340  -8.015  1.00 35.47
ATOM   2324  CG  PHE A 304       8.293  36.160  -7.224  1.00 34.84
ATOM   2325  CD1 PHE A 304       8.061  36.442  -5.880  1.00 33.65
ATOM   2326  CD2 PHE A 304       9.466  36.636  -7.816  1.00 34.20
ATOM   2327  CE1 PHE A 304       8.978  37.180  -5.135  1.00 34.61
ATOM   2328  CE2 PHE A 304      10.392  37.375  -7.080  1.00 33.13
ATOM   2329  CZ  PHE A 304      10.150  37.647  -5.736  1.00 32.67
ATOM   2330  N   PHE A 305       6.427  34.526 -11.063  1.00 36.26
ATOM   2331  CA  PHE A 305       5.676  33.577 -11.863  1.00 35.93
ATOM   2332  C   PHE A 305       6.481  32.302 -12.038  1.00 33.93
ATOM   2333  O   PHE A 305       7.711  32.313 -11.985  1.00 33.17
ATOM   2334  CB  PHE A 305       5.285  34.184 -13.221  1.00 36.77
ATOM   2335  CG  PHE A 305       6.416  34.302 -14.197  1.00 39.49
ATOM   2336  CD1 PHE A 305       6.769  33.224 -15.007  1.00 39.53
ATOM   2337  CD2 PHE A 305       7.121  35.502 -14.323  1.00 39.95
ATOM   2338  CE1 PHE A 305       7.813  33.338 -15.937  1.00 41.15
ATOM   2339  CE2 PHE A 305       8.159  35.630 -15.243  1.00 39.92
ATOM   2340  CZ  PHE A 305       8.510  34.546 -16.054  1.00 41.05
ATOM   2341  N   ASN A 306       5.765  31.201 -12.222  1.00 33.91
ATOM   2342  CA  ASN A 306       6.375  29.888 -12.387  1.00 33.09
ATOM   2343  C   ASN A 306       7.050  29.698 -13.744  1.00 32.89
ATOM   2344  O   ASN A 306       6.458  29.941 -14.798  1.00 31.63
ATOM   2345  CB  ASN A 306       5.314  28.819 -12.167  1.00 31.27
ATOM   2346  CG  ASN A 306       5.845  27.427 -12.350  1.00 30.51
ATOM   2347  OD1 ASN A 306       6.962  27.110 -11.925  1.00 28.38
ATOM   2348  ND2 ASN A 306       5.039  26.570 -12.970  1.00 28.33
ATOM   2349  N   THR A 307       8.301  29.264 -13.698  1.00 30.91
ATOM   2350  CA  THR A 307       9.089  29.033 -14.899  1.00 31.46
ATOM   2351  C   THR A 307       8.894  27.617 -15.412  1.00 32.42
ATOM   2352  O   THR A 307       9.255  27.310 -16.546  1.00 32.31
ATOM   2353  CB  THR A 307      10.598  29.201 -14.619  1.00 32.31
ATOM   2354  OG1 THR A 307      11.000  28.256 -13.618  1.00 30.06
ATOM   2355  CG2 THR A 307      10.903  30.615 -14.136  1.00 29.76
ATOM   2356  N   ASN A 308       8.310  26.776 -14.565  1.00 32.69
ATOM   2357  CA  ASN A 308       8.096  25.363 -14.844  1.00 33.92
ATOM   2358  C   ASN A 308       9.413  24.606 -14.751  1.00 34.50
ATOM   2359  O   ASN A 308       9.564  23.518 -15.296  1.00 33.61
ATOM   2360  CB  ASN A 308       7.434  25.126 -16.202  1.00 35.21
ATOM   2361  CG  ASN A 308       6.038  24.551 -16.055  1.00 37.17
ATOM   2362  OD1 ASN A 308       5.620  24.209 -14.946  1.00 38.43
ATOM   2363  ND2 ASN A 308       5.311  24.437 -17.159  1.00 39.05
ATOM   2364  N   ASN A 309      10.375  25.215 -14.065  1.00 34.37
ATOM   2365  CA  ASN A 309      11.663  24.579 -13.814  1.00 33.90
ATOM   2366  C   ASN A 309      11.477  24.075 -12.379  1.00 34.82
ATOM   2367  O   ASN A 309      11.539  24.865 -11.438  1.00 32.47
ATOM   2368  CB  ASN A 309      12.799  25.604 -13.839  1.00 34.03
ATOM   2369  CG  ASN A 309      13.137  26.094 -15.244  1.00 33.57
ATOM   2370  OD1 ASN A 309      12.543  25.663 -16.238  1.00 29.56
ATOM   2371  ND2 ASN A 309      14.109  26.999 -15.325  1.00 27.34
ATOM   2372  N   LEU A 310      11.216  22.781 -12.213  1.00 35.30
ATOM   2373  CA  LEU A 310      10.996  22.225 -10.882  1.00 37.26
ATOM   2374  C   LEU A 310      12.060  21.219 -10.441  1.00 37.94
ATOM   2375  O   LEU A 310      12.644  20.519 -11.268  1.00 39.56
ATOM   2376  CB  LEU A 310       9.624  21.547 -10.802  1.00 38.00
ATOM   2377  CG  LEU A 310       8.322  22.336 -10.953  1.00 40.20
ATOM   2378  CD1 LEU A 310       8.484  23.718 -10.320  1.00 42.43
ATOM   2379  CD2 LEU A 310       7.952  22.455 -12.410  1.00 42.60
ATOM   2380  N   TRP A 311      12.298  21.161  -9.133  1.00 35.02
ATOM   2381  CA  TRP A 311      13.264  20.243  -8.539  1.00 34.87
ATOM   2382  C   TRP A 311      12.510  19.504  -7.447  1.00 36.57
ATOM   2383  O   TRP A 311      12.001  20.123  -6.510  1.00 37.78
ATOM   2384  CB  TRP A 311      14.445  21.004  -7.926  1.00 32.19
ATOM   2385  CG  TRP A 311      15.218  21.858  -8.922  1.00 30.89
ATOM   2386  CD1 TRP A 311      14.840  23.071  -9.434  1.00 28.31
ATOM   2387  CD2 TRP A 311      16.488  21.553  -9.517  1.00 26.29
ATOM   2388  NE1 TRP A 311      15.795  23.537 -10.301  1.00 27.13
ATOM   2389  CE2 TRP A 311      16.815  22.627 -10.374  1.00 26.59
ATOM   2390  CE3 TRP A 311      17.377  20.477  -9.409  1.00 26.23
ATOM   2391  CZ2 TRP A 311      17.998  22.659 -11.123  1.00 26.73
ATOM   2392  CZ3 TRP A 311      18.554  20.502 -10.153  1.00 26.22
ATOM   2393  CH2 TRP A 311      18.854  21.588 -11.001  1.00 27.05
ATOM   2394  N   ILE A 312      12.430  18.183  -7.566  1.00 36.83
ATOM   2395  CA  ILE A 312      11.691  17.386  -6.598  1.00 37.14
ATOM   2396  C   ILE A 312      12.511  16.261  -6.014  1.00 36.56
ATOM   2397  O   ILE A 312      13.283  15.618  -6.725  1.00 39.23
ATOM   2398  CB  ILE A 312      10.468  16.739  -7.248  1.00 38.81
ATOM   2399  CG1 ILE A 312       9.740  17.772  -8.104  1.00 39.34
ATOM   2400  CG2 ILE A 312       9.553  16.159  -6.168  1.00 38.22
ATOM   2401  CD1 ILE A 312       8.867  17.165  -9.167  1.00 43.24
ATOM   2402  N   ARG A 313      12.329  16.018  -4.722  1.00 35.05
ATOM   2403  CA  ARG A 313      13.016  14.934  -4.035  1.00 35.56
ATOM   2404  C   ARG A 313      12.152  13.682  -4.250  1.00 34.17
ATOM   2405  O   ARG A 313      11.123  13.503  -3.599  1.00 33.14
ATOM   2406  CB  ARG A 313      13.136  15.264  -2.543  1.00 38.68
ATOM   2407  CG  ARG A 313      14.070  14.342  -1.763  1.00 42.26
ATOM   2408  CD  ARG A 313      14.149  14.753  -0.297  1.00 44.98
ATOM   2409  NE  ARG A 313      14.778  16.061  -0.099  1.00 45.56
ATOM   2410  CZ  ARG A 313      16.091  16.268  -0.092  1.00 47.18
ATOM   2411  NH1 ARG A 313      16.924  15.253  -0.276  1.00 48.93
ATOM   2412  NH2 ARG A 313      16.575  17.487   0.120  1.00 47.61
ATOM   2413  N   LEU A 314      12.566  12.825  -5.173  1.00 33.60
ATOM   2414  CA  LEU A 314      11.810  11.614  -5.500  1.00 34.79
ATOM   2415  C   LEU A 314      11.297  10.743  -4.340  1.00 36.52
ATOM   2416  O   LEU A 314      10.131  10.343  -4.334  1.00 38.00
ATOM   2417  CB  LEU A 314      12.621  10.759  -6.472  1.00 32.39
ATOM   2418  CG  LEU A 314      12.897  11.455  -7.814  1.00 31.56
ATOM   2419  CD1 LEU A 314      13.954  10.693  -8.606  1.00 26.15
ATOM   2420  CD2 LEU A 314      11.594  11.572  -8.610  1.00 25.72
ATOM   2421  N   PRO A 315      12.152  10.430  -3.352  1.00 36.57
ATOM   2422  CA  PRO A 315      11.696   9.599  -2.232  1.00 36.88
ATOM   2423  C   PRO A 315      10.462  10.164  -1.551  1.00 37.03
ATOM   2424  O   PRO A 315       9.508   9.436  -1.263  1.00 35.90
ATOM   2425  CB  PRO A 315      12.907   9.581  -1.301  1.00 36.52
ATOM   2426  CG  PRO A 315      14.050   9.639  -2.258  1.00 36.40
ATOM   2427  CD  PRO A 315      13.598  10.700  -3.243  1.00 37.76
ATOM   2428  N   VAL A 316      10.493  11.468  -1.291  1.00 37.50
ATOM   2429  CA  VAL A 316       9.378  12.141  -0.636  1.00 38.51
ATOM   2430  C   VAL A 316       8.142  12.112  -1.531  1.00 38.88
ATOM   2431  O   VAL A 316       7.030  11.892  -1.061  1.00 39.12
ATOM   2432  CB  VAL A 316       9.744  13.601  -0.291  1.00 38.22
ATOM   2433  CG1 VAL A 316       8.559  14.309   0.337  1.00 38.39
ATOM   2434  CG2 VAL A 316      10.934  13.618   0.662  1.00 40.20
ATOM   2435  N   LEU A 317       8.345  12.339  -2.826  1.00 39.67
ATOM   2436  CA  LEU A 317       7.237  12.313  -3.769  1.00 38.29
ATOM   2437  C   LEU A 317       6.567  10.945  -3.697  1.00 37.83
ATOM   2438  O   LEU A 317       5.353  10.853  -3.588  1.00 38.37
ATOM   2439  CB  LEU A 317       7.728  12.571  -5.200  1.00 33.61
ATOM   2440  CG  LEU A 317       6.655  12.419  -6.285  1.00 32.40
ATOM   2441  CD1 LEU A 317       5.530  13.405  -6.017  1.00 31.15
ATOM   2442  CD2 LEU A 317       7.257  12.635  -7.667  1.00 28.06
ATOM   2443  N   LEU A 318       7.358   9.881  -3.751  1.00 39.87
ATOM   2444  CA  LEU A 318       6.782   8.543  -3.695  1.00 42.60
ATOM   2445  C   LEU A 318       5.972   8.373  -2.411  1.00 44.03
ATOM   2446  O   LEU A 318       4.813   7.960  -2.449  1.00 43.76
ATOM   2447  CB  LEU A 318       7.872   7.470  -3.742  1.00 41.92
ATOM   2448  CG  LEU A 318       7.507   6.125  -4.393  1.00 43.37
ATOM   2449  CD1 LEU A 318       8.490   5.069  -3.901  1.00 39.97
ATOM   2450  CD2 LEU A 318       6.077   5.711  -4.064  1.00 40.54
ATOM   2451  N   GLU A 319       6.579   8.706  -1.275  1.00 45.37
ATOM   2452  CA  GLU A 319       5.896   8.550  -0.001  1.00 46.23
ATOM   2453  C   GLU A 319       4.572   9.287   0.045  1.00 44.64
ATOM   2454  O   GLU A 319       3.544   8.695   0.377  1.00 44.12
ATOM   2455  CB  GLU A 319       6.783   9.005   1.166  1.00 48.58
ATOM   2456  CG  GLU A 319       6.171   8.674   2.521  1.00 54.69
ATOM   2457  CD  GLU A 319       7.163   8.716   3.671  1.00 58.36
ATOM   2458  OE1 GLU A 319       8.287   8.188   3.506  1.00 60.82
ATOM   2459  OE2 GLU A 319       6.808   9.260   4.746  1.00 59.97
ATOM   2460  N   THR A 320       4.585  10.572  -0.286  1.00 43.66
ATOM   2461  CA  THR A 320       3.351  11.344  -0.255  1.00 46.75
ATOM   2462  C   THR A 320       2.282  10.755  -1.176  1.00 45.48
ATOM   2463  O   THR A 320       1.106  10.707  -0.820  1.00 44.55
ATOM   2464  CB  THR A 320       3.584  12.784  -0.677  1.00 47.05
ATOM   2465  OG1 THR A 320       3.909  12.809  -2.067  1.00 52.26
ATOM   2466  CG2 THR A 320       4.722  13.389   0.117  1.00 48.92
ATOM   2467  N   MET A 321       2.683  10.325  -2.367  1.00 43.73
ATOM   2468  CA  MET A 321       1.713   9.752  -3.283  1.00 45.06
ATOM   2469  C   MET A 321       1.151   8.473  -2.680  1.00 45.89
ATOM   2470  O   MET A 321      -0.025   8.149  -2.863  1.00 47.35
ATOM   2471  CB  MET A 321       2.347   9.476  -4.645  1.00 42.01
ATOM   2472  CG  MET A 321       2.636  10.742  -5.425  1.00 43.03
ATOM   2473  SD  MET A 321       3.177  10.410  -7.238  1.00 43.90
ATOM   2474  CE  MET A 321       1.419  10.127  -8.013  1.00 41.44
ATOM   2475  N   GLN A 322       1.990   7.754  -1.944  1.00 45.94
ATOM   2476  CA  GLN A 322       1.555   6.521  -1.297  1.00 46.67
ATOM   2477  C   GLN A 322       0.582   6.808  -0.161  1.00 47.37
ATOM   2478  O   GLN A 322      -0.380   6.074   0.032  1.00 47.67
ATOM   2479  CB  GLN A 322       2.756   5.748  -0.774  1.00 44.52
ATOM   2480  CG  GLN A 322       3.441   4.947  -1.849  1.00 44.60
ATOM   2481  CD  GLN A 322       4.716   4.316  -1.369  1.00 44.06
ATOM   2482  OE1 GLN A 322       5.292   3.467  -2.047  1.00 44.71
ATOM   2483  NE2 GLN A 322       5.177   4.734  -0.196  1.00 43.12
ATOM   2484  N   GLU A 323       0.826   7.879   0.583  1.00 48.01
ATOM   2485  CA  GLU A 323      -0.064   8.237   1.674  1.00 50.76
ATOM   2486  C   GLU A 323      -1.417   8.667   1.116  1.00 50.29
ATOM   2487  O   GLU A 323      -2.405   8.691   1.838  1.00 50.60
ATOM   2488  CB  GLU A 323       0.519   9.388   2.503  1.00 54.25
ATOM   2489  CG  GLU A 323       1.879   9.112   3.139  1.00 61.95
ATOM   2490  CD  GLU A 323       1.848   7.983   4.160  1.00 65.24
ATOM   2491  OE1 GLU A 323       1.032   8.051   5.109  1.00 66.30
ATOM   2492  OE2 GLU A 323       2.649   7.032   4.015  1.00 67.92
ATOM   2493  N   HIS A 324      -1.461   9.011  -0.169  1.00 50.79
ATOM   2494  CA  HIS A 324      -2.708   9.454  -0.796  1.00 51.17
ATOM   2495  C   HIS A 324      -3.389   8.393  -1.643  1.00 50.90
ATOM   2496  O   HIS A 324      -4.202   8.717  -2.508  1.00 52.80
ATOM   2497  CB  HIS A 324      -2.457  10.685  -1.664  1.00 51.37
ATOM   2498  CG  HIS A 324      -2.279  11.948  -0.887  1.00 52.05
ATOM   2499  ND1 HIS A 324      -3.327  12.586  -0.258  1.00 52.75
ATOM   2500  CD2 HIS A 324      -1.178  12.695  -0.636  1.00 52.59
ATOM   2501  CE1 HIS A 324      -2.879  13.672   0.345  1.00 53.68
ATOM   2502  NE2 HIS A 324      -1.578  13.761   0.132  1.00 54.20
ATOM   2503  N   GLY A 325      -3.068   7.129  -1.393  1.00 49.95
ATOM   2504  CA  GLY A 325      -3.669   6.050  -2.155  1.00 49.16
ATOM   2505  C   GLY A 325      -3.078   5.920  -3.547  1.00 49.32
ATOM   2506  O   GLY A 325      -3.806   5.732  -4.521  1.00 50.18
ATOM   2507  N   GLY A 326      -1.754   6.023  -3.639  1.00 48.46
ATOM   2508  CA  GLY A 326      -1.086   5.918  -4.923  1.00 46.74
ATOM   2509  C   GLY A 326      -1.561   6.964  -5.913  1.00 45.86
ATOM   2510  O   GLY A 326      -1.899   6.645  -7.051  1.00 46.19
ATOM   2511  N   THR A 327      -1.582   8.220  -5.484  1.00 44.11
ATOM   2512  CA  THR A 327      -2.024   9.305  -6.342  1.00 44.15
ATOM   2513  C   THR A 327      -1.574  10.617  -5.708  1.00 43.87
ATOM   2514  O   THR A 327      -1.124  10.627  -4.562  1.00 43.90
ATOM   2515  CB  THR A 327      -3.581   9.281  -6.500  1.00 45.05
ATOM   2516  OG1 THR A 327      -3.979  10.172  -7.545  1.00 49.44
ATOM   2517  CG2 THR A 327      -4.261   9.701  -5.221  1.00 43.03
ATOM   2518  N   LEU A 328      -1.679  11.713  -6.456  1.00 42.99
ATOM   2519  CA  LEU A 328      -1.289  13.034  -5.959  1.00 43.07
ATOM   2520  C   LEU A 328      -2.463  13.971  -6.239  1.00 43.88
ATOM   2521  O   LEU A 328      -2.665  14.399  -7.367  1.00 44.37
ATOM   2522  CB  LEU A 328      -0.039  13.526  -6.691  1.00 42.23
ATOM   2523  CG  LEU A 328       0.644  14.751  -6.087  1.00 40.80
ATOM   2524  CD1 LEU A 328       1.218  14.359  -4.737  1.00 37.85
ATOM   2525  CD2 LEU A 328       1.742  15.256  -7.007  1.00 39.26
ATOM   2526  N   PRO A 329      -3.240  14.315  -5.204  1.00 44.68
ATOM   2527  CA  PRO A 329      -4.408  15.189  -5.325  1.00 44.78
ATOM   2528  C   PRO A 329      -4.145  16.648  -5.665  1.00 44.87
ATOM   2529  O   PRO A 329      -4.203  17.525  -4.801  1.00 47.33
ATOM   2530  CB  PRO A 329      -5.096  15.016  -3.975  1.00 44.45
ATOM   2531  CG  PRO A 329      -3.939  14.893  -3.052  1.00 44.21
ATOM   2532  CD  PRO A 329      -3.014  13.946  -3.795  1.00 44.90
ATOM   2533  N   LEU A 330      -3.881  16.906  -6.936  1.00 43.50
ATOM   2534  CA  LEU A 330      -3.627  18.256  -7.388  1.00 42.31
ATOM   2535  C   LEU A 330      -4.954  18.875  -7.766  1.00 42.15
ATOM   2536  O   LEU A 330      -5.860  18.183  -8.226  1.00 42.90
ATOM   2537  CB  LEU A 330      -2.694  18.244  -8.597  1.00 40.70
ATOM   2538  CG  LEU A 330      -1.312  17.637  -8.348  1.00 42.25
ATOM   2539  CD1 LEU A 330      -0.514  17.670  -9.645  1.00 44.04
ATOM   2540  CD2 LEU A 330      -0.587  18.400  -7.262  1.00 39.97
ATOM   2541  N   PRO A 331      -5.095  20.189  -7.565  1.00 40.94
ATOM   2542  CA  PRO A 331      -6.364  20.825  -7.922  1.00 40.45
ATOM   2543  C   PRO A 331      -6.645  20.650  -9.409  1.00 41.29
ATOM   2544  O   PRO A 331      -5.784  20.910 -10.251  1.00 40.11
ATOM   2545  CB  PRO A 331      -6.154  22.288  -7.510  1.00 40.33
ATOM   2546  CG  PRO A 331      -4.656  22.464  -7.538  1.00 39.93
ATOM   2547  CD  PRO A 331      -4.153  21.155  -6.975  1.00 40.08
ATOM   2548  N   VAL A 332      -7.852  20.189  -9.723  1.00 40.49
ATOM   2549  CA  VAL A 332      -8.248  19.960 -11.101  1.00 41.29
ATOM   2550  C   VAL A 332      -8.509  21.260 -11.834  1.00 42.46
ATOM   2551  O   VAL A 332      -8.970  22.241 -11.247  1.00 42.53
ATOM   2552  CB  VAL A 332      -9.537  19.102 -11.184  1.00 42.09
ATOM   2553  CG1 VAL A 332     -10.710  19.876 -10.599  1.00 43.71
ATOM   2554  CG2 VAL A 332      -9.824  18.706 -12.628  1.00 40.41
ATOM   2555  N   ILE A 333      -8.196  21.255 -13.123  1.00 42.58
ATOM   2556  CA  ILE A 333      -8.428  22.398 -13.979  1.00 43.80
ATOM   2557  C   ILE A 333      -9.492  21.892 -14.932  1.00 45.73
ATOM   2558  O   ILE A 333      -9.323  20.850 -15.568  1.00 44.10
ATOM   2559  CB  ILE A 333      -7.163  22.788 -14.762  1.00 45.18
ATOM   2560  CG1 ILE A 333      -6.089  23.275 -13.781  1.00 44.40
ATOM   2561  CG2 ILE A 333      -7.508  23.862 -15.804  1.00 40.40
ATOM   2562  CD1 ILE A 333      -4.686  23.332 -14.356  1.00 45.97
ATOM   2563  N   ARG A 334     -10.596  22.619 -15.025  1.00 47.68
ATOM   2564  CA  ARG A 334     -11.685  22.188 -15.879  1.00 49.42
ATOM   2565  C   ARG A 334     -11.711  22.937 -17.191  1.00 50.37
ATOM   2566  O   ARG A 334     -12.294  24.012 -17.295  1.00 50.16
ATOM   2567  CB  ARG A 334     -13.012  22.363 -15.152  1.00 50.27
ATOM   2568  CG  ARG A 334     -14.132  21.558 -15.747  1.00 53.51
ATOM   2569  CD  ARG A 334     -15.426  22.007 -15.144  1.00 57.58
ATOM   2570  NE  ARG A 334     -15.676  23.406 -15.461  1.00 59.59
ATOM   2571  CZ  ARG A 334     -16.467  24.196 -14.750  1.00 61.50
ATOM   2572  NH1 ARG A 334     -17.084  23.722 -13.675  1.00 62.45
ATOM   2573  NH2 ARG A 334     -16.639  25.460 -15.116  1.00 62.65
ATOM   2574  N   ASN A 335     -11.075  22.345 -18.193  1.00 52.35
ATOM   2575  CA  ASN A 335     -10.992  22.928 -19.521  1.00 54.16
ATOM   2576  C   ASN A 335     -12.280  22.759 -20.301  1.00 54.77
ATOM   2577  O   ASN A 335     -12.779  21.644 -20.449  1.00 55.34
ATOM   2578  CB  ASN A 335      -9.855  22.274 -20.295  1.00 57.00
ATOM   2579  CG  ASN A 335      -8.725  23.223 -20.558  1.00 59.88
ATOM   2580  OD1 ASN A 335      -8.253  23.909 -19.647  1.00 61.15
ATOM   2581  ND2 ASN A 335      -8.271  23.272 -21.809  1.00 60.23
ATOM   2582  N   GLU A 336     -12.809  23.868 -20.809  1.00 54.00
ATOM   2583  CA  GLU A 336     -14.037  23.832 -21.586  1.00 53.74
ATOM   2584  C   GLU A 336     -13.686  23.843 -23.067  1.00 53.19
ATOM   2585  O   GLU A 336     -12.943  24.702 -23.524  1.00 53.33
ATOM   2586  CB  GLU A 336     -14.912  25.035 -21.241  1.00 54.83
ATOM   2587  CG  GLU A 336     -15.373  25.062 -19.788  1.00 56.83
ATOM   2588  CD  GLU A 336     -16.139  26.320 -19.438  1.00 57.63
ATOM   2589  OE1 GLU A 336     -16.648  26.409 -18.304  1.00 59.38
ATOM   2590  OE2 GLU A 336     -16.228  27.226 -20.293  1.00 58.68
ATOM   2591  N   LYS A 337     -14.215  22.877 -23.811  1.00 51.48
ATOM   2592  CA  LYS A 337     -13.951  22.773 -25.240  1.00 49.40
ATOM   2593  C   LYS A 337     -15.118  22.024 -25.876  1.00 48.48
ATOM   2594  O   LYS A 337     -16.136  21.781 -25.227  1.00 48.03
ATOM   2595  CB  LYS A 337     -12.659  21.976 -25.472  1.00 50.26
ATOM   2596  CG  LYS A 337     -11.431  22.493 -24.718  1.00 53.71
ATOM   2597  CD  LYS A 337     -10.554  23.422 -25.570  1.00 58.47
ATOM   2598  CE  LYS A 337      -9.813  22.645 -26.671  1.00 60.15
ATOM   2599  NZ  LYS A 337      -8.863  23.484 -27.469  1.00 59.84
ATOM   2600  N   THR A 338     -14.975  21.681 -27.152  1.00 47.00
ATOM   2601  CA  THR A 338     -15.981  20.892 -27.854  1.00 46.52
ATOM   2602  C   THR A 338     -15.187  19.641 -28.221  1.00 45.70
ATOM   2603  O   THR A 338     -13.973  19.729 -28.391  1.00 47.08
ATOM   2604  CB  THR A 338     -16.499  21.597 -29.137  1.00 47.95
ATOM   2605  OG1 THR A 338     -15.447  21.707 -30.102  1.00 47.95
ATOM   2606  CG2 THR A 338     -17.023  22.988 -28.802  1.00 49.76
ATOM   2607  N   VAL A 339     -15.839  18.487 -28.330  1.00 43.89
ATOM   2608  CA  VAL A 339     -15.113  17.257 -28.651  1.00 42.95
ATOM   2609  C   VAL A 339     -14.145  17.439 -29.812  1.00 43.53
ATOM   2610  O   VAL A 339     -12.981  17.039 -29.736  1.00 40.93
ATOM   2611  CB  VAL A 339     -16.047  16.109 -29.030  1.00 42.21
ATOM   2612  CG1 VAL A 339     -15.616  14.839 -28.294  1.00 38.26
ATOM   2613  CG2 VAL A 339     -17.475  16.487 -28.744  1.00 43.93
ATOM   2614  N   ASP A 340     -14.650  18.017 -30.896  1.00 45.03
ATOM   2615  CA  ASP A 340     -13.843  18.273 -32.072  1.00 47.02
ATOM   2616  C   ASP A 340     -13.567  19.773 -32.094  1.00 49.46
ATOM   2617  O   ASP A 340     -14.464  20.592 -32.328  1.00 46.91
ATOM   2618  CB  ASP A 340     -14.585  17.856 -33.347  1.00 48.78
ATOM   2619  CG  ASP A 340     -13.701  17.916 -34.595  1.00 49.46
ATOM   2620  OD1 ASP A 340     -12.817  18.800 -34.663  1.00 49.40
ATOM   2621  OD2 ASP A 340     -13.905  17.087 -35.513  1.00 50.97
ATOM   2622  N   SER A 341     -12.314  20.117 -31.824  1.00 51.16
ATOM   2623  CA  SER A 341     -11.868  21.499 -31.816  1.00 52.92
ATOM   2624  C   SER A 341     -12.298  22.178 -33.114  1.00 52.35
ATOM   2625  O   SER A 341     -12.706  23.344 -33.117  1.00 52.34
ATOM   2626  CB  SER A 341     -10.342  21.530 -31.683  1.00 54.48
ATOM   2627  OG  SER A 341      -9.737  20.609 -32.590  1.00 55.77
ATOM   2628  N   SER A 342     -12.228  21.423 -34.208  1.00 51.38
ATOM   2629  CA  SER A 342     -12.578  21.928 -35.531  1.00 51.11
ATOM   2630  C   SER A 342     -14.074  21.981 -35.844  1.00 50.06
ATOM   2631  O   SER A 342     -14.454  22.018 -37.016  1.00 50.64
ATOM   2632  CB  SER A 342     -11.887  21.083 -36.603  1.00 51.66
ATOM   2633  OG  SER A 342     -10.484  21.056 -36.403  1.00 57.23
ATOM   2634  N   ASN A 343     -14.925  21.979 -34.820  1.00 48.10
ATOM   2635  CA  ASN A 343     -16.367  22.024 -35.059  1.00 44.48
ATOM   2636  C   ASN A 343     -17.097  22.597 -33.867  1.00 43.69
ATOM   2637  O   ASN A 343     -17.359  21.895 -32.895  1.00 43.49
ATOM   2638  CB  ASN A 343     -16.894  20.624 -35.369  1.00 44.92
ATOM   2639  CG  ASN A 343     -18.317  20.634 -35.914  1.00 48.00
ATOM   2640  OD1 ASN A 343     -18.745  19.681 -36.571  1.00 49.87
ATOM   2641  ND2 ASN A 343     -19.058  21.698 -35.637  1.00 46.00
ATOM   2642  N   SER A 344     -17.437  23.877 -33.955  1.00 43.64
ATOM   2643  CA  SER A 344     -18.138  24.564 -32.876  1.00 43.22
ATOM   2644  C   SER A 344     -19.496  23.956 -32.541  1.00 41.37
ATOM   2645  O   SER A 344     -20.080  24.279 -31.507  1.00 41.58
ATOM   2646  CB  SER A 344     -18.307  26.044 -33.225  1.00 45.83
ATOM   2647  OG  SER A 344     -18.888  26.203 -34.511  1.00 47.75
ATOM   2648  N   ALA A 345     -19.990  23.074 -33.407  1.00 39.60
ATOM   2649  CA  ALA A 345     -21.284  22.420 -33.194  1.00 38.67
ATOM   2650  C   ALA A 345     -21.142  21.060 -32.512  1.00 39.28
ATOM   2651  O   ALA A 345     -22.142  20.435 -32.158  1.00 38.51
ATOM   2652  CB  ALA A 345     -22.016  22.256 -34.521  1.00 35.35
ATOM   2653  N   SER A 346     -19.905  20.596 -32.344  1.00 39.83
ATOM   2654  CA  SER A 346     -19.667  19.313 -31.689  1.00 41.24
ATOM   2655  C   SER A 346     -19.981  19.456 -30.197  1.00 42.09
ATOM   2656  O   SER A 346     -19.832  20.533 -29.625  1.00 40.58
ATOM   2657  CB  SER A 346     -18.210  18.860 -31.880  1.00 43.06
ATOM   2658  OG  SER A 346     -17.293  19.645 -31.130  1.00 42.59
ATOM   2659  N   PRO A 347     -20.412  18.362 -29.551  1.00 43.20
ATOM   2660  CA  PRO A 347     -20.763  18.328 -28.126  1.00 43.81
ATOM   2661  C   PRO A 347     -19.772  19.027 -27.199  1.00 44.68
ATOM   2662  O   PRO A 347     -18.570  18.755 -27.241  1.00 43.01
ATOM   2663  CB  PRO A 347     -20.866  16.832 -27.836  1.00 44.89
ATOM   2664  CG  PRO A 347     -21.361  16.281 -29.146  1.00 44.28
ATOM   2665  CD  PRO A 347     -20.503  17.015 -30.145  1.00 43.75
ATOM   2666  N   LYS A 348     -20.284  19.930 -26.363  1.00 45.44
ATOM   2667  CA  LYS A 348     -19.437  20.654 -25.416  1.00 47.09
ATOM   2668  C   LYS A 348     -18.898  19.688 -24.369  1.00 46.04
ATOM   2669  O   LYS A 348     -19.616  18.805 -23.915  1.00 46.38
ATOM   2670  CB  LYS A 348     -20.227  21.773 -24.732  1.00 48.93
ATOM   2671  CG  LYS A 348     -20.618  22.885 -25.672  1.00 51.04
ATOM   2672  CD  LYS A 348     -21.172  24.081 -24.929  1.00 54.36
ATOM   2673  CE  LYS A 348     -21.541  25.171 -25.918  1.00 57.31
ATOM   2674  NZ  LYS A 348     -20.435  25.378 -26.905  1.00 58.28
ATOM   2675  N   VAL A 349     -17.642  19.859 -23.975  1.00 43.98
ATOM   2676  CA  VAL A 349     -17.058  18.948 -23.000  1.00 43.34
ATOM   2677  C   VAL A 349     -16.126  19.619 -22.019  1.00 43.61
ATOM   2678  O   VAL A 349     -15.792  20.796 -22.147  1.00 47.10
ATOM   2679  CB  VAL A 349     -16.234  17.838 -23.694  1.00 42.61
ATOM   2680  CG1 VAL A 349     -17.117  17.016 -24.630  1.00 41.39
ATOM   2681  CG2 VAL A 349     -15.086  18.471 -24.470  1.00 42.01
ATOM   2682  N   TYR A 350     -15.706  18.844 -21.032  1.00 42.67
ATOM   2683  CA  TYR A 350     -14.760  19.304 -20.039  1.00 41.60
ATOM   2684  C   TYR A 350     -13.545  18.407 -20.232  1.00 41.61
ATOM   2685  O   TYR A 350     -13.692  17.204 -20.450  1.00 41.09
ATOM   2686  CB  TYR A 350     -15.291  19.096 -18.618  1.00 42.55
ATOM   2687  CG  TYR A 350     -16.412  20.015 -18.188  1.00 44.89
ATOM   2688  CD1 TYR A 350     -17.495  19.515 -17.463  1.00 46.01
ATOM   2689  CD2 TYR A 350     -16.383  21.380 -18.471  1.00 45.92
ATOM   2690  CE1 TYR A 350     -18.527  20.344 -17.030  1.00 46.33
ATOM   2691  CE2 TYR A 350     -17.414  22.229 -18.036  1.00 47.15
ATOM   2692  CZ  TYR A 350     -18.487  21.699 -17.314  1.00 47.95
ATOM   2693  OH  TYR A 350     -19.518  22.506 -16.869  1.00 45.14
ATOM   2694  N   GLN A 351     -12.352  18.991 -20.194  1.00 41.25
ATOM   2695  CA  GLN A 351     -11.123  18.210 -20.299  1.00 39.60
ATOM   2696  C   GLN A 351     -10.427  18.474 -18.983  1.00 37.85
ATOM   2697  O   GLN A 351     -10.065  19.605 -18.691  1.00 36.24
ATOM   2698  CB  GLN A 351     -10.248  18.675 -21.465  1.00 40.14
ATOM   2699  CG  GLN A 351     -10.965  18.593 -22.791  1.00 44.08
ATOM   2700  CD  GLN A 351     -10.064  18.805 -23.997  1.00 44.81
ATOM   2701  OE1 GLN A 351     -10.549  18.899 -25.131  1.00 44.93
ATOM   2702  NE2 GLN A 351      -8.754  18.870 -23.765  1.00 44.12
ATOM   2703  N   LEU A 352     -10.275  17.428 -18.180  1.00 37.31
ATOM   2704  CA  LEU A 352      -9.646  17.550 -16.874  1.00 36.16
ATOM   2705  C   LEU A 352      -8.121  17.469 -16.941  1.00 36.97
ATOM   2706  O   LEU A 352      -7.563  16.516 -17.494  1.00 35.37
ATOM   2707  CB  LEU A 352     -10.186  16.457 -15.948  1.00 32.91
ATOM   2708  CG  LEU A 352     -11.714  16.369 -15.891  1.00 33.17
ATOM   2709  CD1 LEU A 352     -12.120  15.430 -14.786  1.00 32.92
ATOM   2710  CD2 LEU A 352     -12.309  17.743 -15.651  1.00 33.95
ATOM   2711  N   GLU A 353      -7.458  18.471 -16.366  1.00 36.82
ATOM   2712  CA  GLU A 353      -5.998  18.528 -16.346  1.00 39.05
ATOM   2713  C   GLU A 353      -5.481  19.175 -15.075  1.00 38.11
ATOM   2714  O   GLU A 353      -6.242  19.776 -14.321  1.00 36.49
ATOM   2715  CB  GLU A 353      -5.474  19.307 -17.561  1.00 42.19
ATOM   2716  CG  GLU A 353      -6.552  20.058 -18.326  1.00 48.54
ATOM   2717  CD  GLU A 353      -6.053  20.654 -19.625  1.00 52.31
ATOM   2718  OE1 GLU A 353      -5.139  21.505 -19.566  1.00 54.77
ATOM   2719  OE2 GLU A 353      -6.579  20.270 -20.700  1.00 55.29
ATOM   2720  N   THR A 354      -4.177  19.036 -14.846  1.00 37.62
ATOM   2721  CA  THR A 354      -3.517  19.613 -13.682  1.00 36.97
ATOM   2722  C   THR A 354      -2.179  20.166 -14.141  1.00 38.09
ATOM   2723  O   THR A 354      -1.653  19.746 -15.175  1.00 38.19
ATOM   2724  CB  THR A 354      -3.243  18.554 -12.579  1.00 36.98
ATOM   2725  OG1 THR A 354      -2.431  17.502 -13.111  1.00 35.78
ATOM   2726  CG2 THR A 354      -4.545  17.965 -12.057  1.00 36.82
ATOM   2727  N   ALA A 355      -1.632  21.106 -13.376  1.00 36.82
ATOM   2728  CA  ALA A 355      -0.343  21.705 -13.704  1.00 36.50
ATOM   2729  C   ALA A 355       0.692  21.129 -12.753  1.00 35.42
ATOM   2730  O   ALA A 355       0.439  21.029 -11.556  1.00 36.95
ATOM   2731  CB  ALA A 355      -0.415  23.223 -13.548  1.00 36.28
ATOM   2732  N   MET A 356       1.854  20.745 -13.269  1.00 34.12
ATOM   2733  CA  MET A 356       2.879  20.177 -12.401  1.00 34.08
ATOM   2734  C   MET A 356       3.391  21.145 -11.344  1.00 33.21
ATOM   2735  O   MET A 356       3.936  20.726 -10.324  1.00 32.37
ATOM   2736  CB  MET A 356       4.055  19.624 -13.217  1.00 34.75
ATOM   2737  CG  MET A 356       4.717  20.567 -14.182  1.00 35.30
ATOM   2738  SD  MET A 356       6.328  19.702 -14.878  1.00 42.22
ATOM   2739  CE  MET A 356       7.156  21.259 -15.645  1.00 36.94
ATOM   2740  N   GLY A 357       3.212  22.437 -11.590  1.00 33.32
ATOM   2741  CA  GLY A 357       3.640  23.436 -10.632  1.00 33.23
ATOM   2742  C   GLY A 357       2.705  23.471  -9.434  1.00 34.23
ATOM   2743  O   GLY A 357       3.088  23.917  -8.358  1.00 34.73
ATOM   2744  N   ALA A 358       1.472  23.003  -9.608  1.00 32.53
ATOM   2745  CA  ALA A 358       0.531  22.992  -8.494  1.00 31.66
ATOM   2746  C   ALA A 358       1.045  22.118  -7.346  1.00 30.70
ATOM   2747  O   ALA A 358       0.664  22.321  -6.198  1.00 32.09
ATOM   2748  CB  ALA A 358      -0.835  22.504  -8.953  1.00 27.58
ATOM   2749  N   ALA A 359       1.924  21.170  -7.655  1.00 29.09
ATOM   2750  CA  ALA A 359       2.472  20.269  -6.641  1.00 30.36
ATOM   2751  C   ALA A 359       3.204  20.974  -5.506  1.00 31.56
ATOM   2752  O   ALA A 359       3.404  20.396  -4.442  1.00 32.20
ATOM   2753  CB  ALA A 359       3.403  19.246  -7.290  1.00 28.00
ATOM   2754  N   ILE A 360       3.615  22.218  -5.726  1.00 33.31
ATOM   2755  CA  ILE A 360       4.327  22.946  -4.691  1.00 32.65
ATOM   2756  C   ILE A 360       3.523  22.975  -3.390  1.00 33.88
ATOM   2757  O   ILE A 360       4.094  23.087  -2.313  1.00 35.82
ATOM   2758  CB  ILE A 360       4.653  24.387  -5.146  1.00 33.51
ATOM   2759  CG1 ILE A 360       5.618  25.036  -4.153  1.00 32.91
ATOM   2760  CG2 ILE A 360       3.367  25.213  -5.278  1.00 29.69
ATOM   2761  CD1 ILE A 360       6.205  26.365  -4.632  1.00 33.22
ATOM   2762  N   ALA A 361       2.199  22.851  -3.490  1.00 34.16
ATOM   2763  CA  ALA A 361       1.333  22.867  -2.310  1.00 34.27
ATOM   2764  C   ALA A 361       1.240  21.510  -1.616  1.00 35.35
ATOM   2765  O   ALA A 361       0.704  21.404  -0.513  1.00 34.08
ATOM   2766  CB  ALA A 361      -0.060  23.328  -2.698  1.00 31.44
ATOM   2767  N   MET A 362       1.773  20.481  -2.263  1.00 36.66
ATOM   2768  CA  MET A 362       1.724  19.125  -1.742  1.00 38.73
ATOM   2769  C   MET A 362       2.853  18.737  -0.798  1.00 40.42
ATOM   2770  O   MET A 362       2.893  17.597  -0.328  1.00 38.37
ATOM   2771  CB  MET A 362       1.706  18.143  -2.909  1.00 41.78
ATOM   2772  CG  MET A 362       0.608  18.418  -3.916  1.00 48.98
ATOM   2773  SD  MET A 362      -1.143  18.141  -3.152  1.00 56.47
ATOM   2774  CE  MET A 362      -1.010  16.243  -3.018  1.00 51.80
ATOM   2775  N   PHE A 363       3.775  19.657  -0.520  1.00 42.53
ATOM   2776  CA  PHE A 363       4.899  19.328   0.367  1.00 43.08
ATOM   2777  C   PHE A 363       5.160  20.342   1.471  1.00 44.23
ATOM   2778  O   PHE A 363       5.107  21.548   1.242  1.00 45.69
ATOM   2779  CB  PHE A 363       6.184  19.133  -0.449  1.00 41.05
ATOM   2780  CG  PHE A 363       6.045  18.140  -1.564  1.00 39.81
ATOM   2781  CD1 PHE A 363       5.491  18.516  -2.782  1.00 39.94
ATOM   2782  CD2 PHE A 363       6.414  16.812  -1.379  1.00 41.72
ATOM   2783  CE1 PHE A 363       5.303  17.582  -3.798  1.00 39.82
ATOM   2784  CE2 PHE A 363       6.228  15.867  -2.393  1.00 40.89
ATOM   2785  CZ  PHE A 363       5.673  16.255  -3.600  1.00 39.52
ATOM   2786  N   GLU A 364       5.447  19.848   2.673  1.00 46.34
ATOM   2787  CA  GLU A 364       5.732  20.732   3.797  1.00 48.10
ATOM   2788  C   GLU A 364       7.046  21.466   3.595  1.00 45.72
ATOM   2789  O   GLU A 364       7.169  22.627   3.959  1.00 44.95
ATOM   2790  CB  GLU A 364       5.801  19.953   5.110  1.00 52.11
ATOM   2791  CG  GLU A 364       4.455  19.646   5.724  1.00 58.68
ATOM   2792  CD  GLU A 364       4.562  19.318   7.201  1.00 62.87
ATOM   2793  OE1 GLU A 364       3.501  19.179   7.856  1.00 64.75
ATOM   2794  OE2 GLU A 364       5.707  19.205   7.703  1.00 63.23
ATOM   2795  N   SER A 365       8.032  20.781   3.030  1.00 45.01
ATOM   2796  CA  SER A 365       9.336  21.397   2.782  1.00 46.16
ATOM   2797  C   SER A 365       9.396  21.897   1.346  1.00 45.33
ATOM   2798  O   SER A 365      10.330  21.592   0.606  1.00 47.75
ATOM   2799  CB  SER A 365      10.471  20.391   3.024  1.00 45.34
ATOM   2800  OG  SER A 365      10.436  19.891   4.353  1.00 52.03
ATOM   2801  N   ALA A 366       8.391  22.659   0.945  1.00 42.68
ATOM   2802  CA  ALA A 366       8.375  23.178  -0.411  1.00 40.46
ATOM   2803  C   ALA A 366       8.917  24.582  -0.397  1.00 37.89
ATOM   2804  O   ALA A 366       8.770  25.303   0.584  1.00 34.97
ATOM   2805  CB  ALA A 366       6.953  23.177  -0.975  1.00 39.56
ATOM   2806  N   SER A 367       9.553  24.970  -1.491  1.00 37.51
ATOM   2807  CA  SER A 367      10.078  26.309  -1.583  1.00 37.18
ATOM   2808  C   SER A 367      10.112  26.806  -3.020  1.00 36.49
ATOM   2809  O   SER A 367       9.857  26.051  -3.964  1.00 35.08
ATOM   2810  CB  SER A 367      11.476  26.369  -0.972  1.00 38.60
ATOM   2811  OG  SER A 367      11.740  27.688  -0.513  1.00 43.65
ATOM   2812  N   ALA A 368      10.403  28.094  -3.163  1.00 33.17
ATOM   2813  CA  ALA A 368      10.510  28.733  -4.459  1.00 34.35
ATOM   2814  C   ALA A 368      11.788  29.564  -4.427  1.00 35.99
ATOM   2815  O   ALA A 368      12.153  30.114  -3.384  1.00 35.47
ATOM   2816  CB  ALA A 368       9.312  29.629  -4.706  1.00 32.00
ATOM   2817  N   ILE A 369      12.475  29.655  -5.558  1.00 35.70
ATOM   2818  CA  ILE A 369      13.695  30.445  -5.600  1.00 36.53
ATOM   2819  C   ILE A 369      13.674  31.348  -6.835  1.00 35.72
ATOM   2820  O   ILE A 369      13.304  30.915  -7.927  1.00 37.24
ATOM   2821  CB  ILE A 369      14.950  29.510  -5.576  1.00 38.66
ATOM   2822  CG1 ILE A 369      16.229  30.340  -5.486  1.00 41.82
ATOM   2823  CG2 ILE A 369      14.979  28.616  -6.800  1.00 38.33
ATOM   2824  CD1 ILE A 369      17.500  29.496  -5.344  1.00 42.74
ATOM   2825  N   VAL A 370      14.031  32.615  -6.652  1.00 34.34
ATOM   2826  CA  VAL A 370      14.050  33.566  -7.757  1.00 33.37
ATOM   2827  C   VAL A 370      15.293  33.354  -8.617  1.00 33.48
ATOM   2828  O   VAL A 370      16.415  33.357  -8.117  1.00 32.56
ATOM   2829  CB  VAL A 370      14.038  35.035  -7.258  1.00 33.80
ATOM   2830  CG1 VAL A 370      13.884  35.981  -8.444  1.00 33.31
ATOM   2831  CG2 VAL A 370      12.903  35.249  -6.269  1.00 34.40
ATOM   2832  N   VAL A 371      15.079  33.172  -9.914  1.00 32.11
ATOM   2833  CA  VAL A 371      16.168  32.942 -10.849  1.00 31.66
ATOM   2834  C   VAL A 371      16.114  33.976 -11.960  1.00 31.74
ATOM   2835  O   VAL A 371      15.066  34.544 -12.232  1.00 32.52
ATOM   2836  CB  VAL A 371      16.057  31.553 -11.477  1.00 32.18
ATOM   2837  CG1 VAL A 371      16.127  30.493 -10.401  1.00 33.56
ATOM   2838  CG2 VAL A 371      14.748  31.439 -12.248  1.00 31.40
ATOM   2839  N   PRO A 372      17.248  34.236 -12.622  1.00 32.73
ATOM   2840  CA  PRO A 372      17.256  35.225 -13.702  1.00 34.14
ATOM   2841  C   PRO A 372      16.441  34.785 -14.922  1.00 35.15
ATOM   2842  O   PRO A 372      16.291  33.590 -15.186  1.00 34.49
ATOM   2843  CB  PRO A 372      18.740  35.375 -14.018  1.00 32.51
ATOM   2844  CG  PRO A 372      19.270  34.003 -13.768  1.00 33.35
ATOM   2845  CD  PRO A 372      18.576  33.614 -12.467  1.00 34.51
ATOM   2846  N   ARG A 373      15.924  35.769 -15.652  1.00 33.95
ATOM   2847  CA  ARG A 373      15.125  35.538 -16.849  1.00 34.93
ATOM   2848  C   ARG A 373      15.781  34.568 -17.829  1.00 34.30
ATOM   2849  O   ARG A 373      15.090  33.909 -18.600  1.00 35.31
ATOM   2850  CB  ARG A 373      14.887  36.856 -17.579  1.00 35.76
ATOM   2851  CG  ARG A 373      13.789  36.794 -18.631  1.00 37.24
ATOM   2852  CD  ARG A 373      12.472  37.107 -17.984  1.00 38.29
ATOM   2853  NE  ARG A 373      11.327  36.830 -18.837  1.00 35.88
ATOM   2854  CZ  ARG A 373      10.087  37.181 -18.520  1.00 35.51
ATOM   2855  NH1 ARG A 373       9.855  37.828 -17.383  1.00 32.01
ATOM   2856  NH2 ARG A 373       9.082  36.865 -19.322  1.00 34.33
ATOM   2857  N   SER A 374      17.109  34.492 -17.815  1.00 32.52
ATOM   2858  CA  SER A 374      17.801  33.606 -18.735  1.00 32.58
ATOM   2859  C   SER A 374      17.414  32.139 -18.546  1.00 32.19
ATOM   2860  O   SER A 374      17.548  31.343 -19.467  1.00 33.35
ATOM   2861  CB  SER A 374      19.323  33.776 -18.615  1.00 32.83
ATOM   2862  OG  SER A 374      19.787  33.515 -17.299  1.00 35.86
ATOM   2863  N   ARG A 375      16.941  31.767 -17.363  1.00 31.69
ATOM   2864  CA  ARG A 375      16.551  30.380 -17.157  1.00 28.79
ATOM   2865  C   ARG A 375      15.126  30.109 -17.635  1.00 30.75
ATOM   2866  O   ARG A 375      14.646  28.983 -17.565  1.00 27.58
ATOM   2867  CB  ARG A 375      16.716  29.981 -15.700  1.00 25.52
ATOM   2868  CG  ARG A 375      18.185  29.734 -15.319  1.00 25.53
ATOM   2869  CD  ARG A 375      18.319  29.273 -13.878  1.00 24.18
ATOM   2870  NE  ARG A 375      17.738  27.950 -13.672  1.00 25.87
ATOM   2871  CZ  ARG A 375      18.304  26.803 -14.035  1.00 27.66
ATOM   2872  NH1 ARG A 375      19.491  26.793 -14.629  1.00 29.19
ATOM   2873  NH2 ARG A 375      17.679  25.655 -13.805  1.00 29.58
ATOM   2874  N   PHE A 376      14.459  31.148 -18.130  1.00 30.86
ATOM   2875  CA  PHE A 376      13.105  31.004 -18.651  1.00 34.38
ATOM   2876  C   PHE A 376      13.138  31.563 -20.055  1.00 36.16
ATOM   2877  O   PHE A 376      12.717  32.691 -20.291  1.00 37.97
ATOM   2878  CB  PHE A 376      12.084  31.785 -17.817  1.00 33.35
ATOM   2879  CG  PHE A 376      10.676  31.656 -18.322  1.00 33.02
ATOM   2880  CD1 PHE A 376      10.025  30.431 -18.297  1.00 36.18
ATOM   2881  CD2 PHE A 376       9.999  32.761 -18.840  1.00 35.31
ATOM   2882  CE1 PHE A 376       8.702  30.300 -18.786  1.00 36.87
ATOM   2883  CE2 PHE A 376       8.683  32.646 -19.330  1.00 33.90
ATOM   2884  CZ  PHE A 376       8.037  31.416 -19.302  1.00 35.02
ATOM   2885  N   ALA A 377      13.647  30.766 -20.987  1.00 38.45
ATOM   2886  CA  ALA A 377      13.764  31.195 -22.370  1.00 39.65
ATOM   2887  C   ALA A 377      12.995  30.295 -23.324  1.00 41.17
ATOM   2888  O   ALA A 377      13.562  29.764 -24.275  1.00 42.36
ATOM   2889  CB  ALA A 377      15.223  31.225 -22.760  1.00 38.93
ATOM   2890  N   PRO A 378      11.691  30.110 -23.088  1.00 43.01
ATOM   2891  CA  PRO A 378      10.908  29.252 -23.980  1.00 43.45
ATOM   2892  C   PRO A 378      10.861  29.780 -25.408  1.00 44.79
ATOM   2893  O   PRO A 378      10.865  30.993 -25.634  1.00 44.85
ATOM   2894  CB  PRO A 378       9.527  29.262 -23.335  1.00 44.11
ATOM   2895  CG  PRO A 378       9.448  30.635 -22.762  1.00 43.83
ATOM   2896  CD  PRO A 378      10.814  30.785 -22.114  1.00 43.70
ATOM   2897  N   VAL A 379      10.849  28.866 -26.372  1.00 45.26
ATOM   2898  CA  VAL A 379      10.746  29.259 -27.768  1.00 45.06
ATOM   2899  C   VAL A 379       9.312  28.942 -28.124  1.00 45.89
ATOM   2900  O   VAL A 379       8.973  27.789 -28.341  1.00 47.09
ATOM   2901  CB  VAL A 379      11.658  28.440 -28.686  1.00 44.28
ATOM   2902  CG1 VAL A 379      11.312  28.741 -30.154  1.00 41.60
ATOM   2903  CG2 VAL A 379      13.110  28.770 -28.404  1.00 42.08
ATOM   2904  N   LYS A 380       8.470  29.963 -28.155  1.00 48.27
ATOM   2905  CA  LYS A 380       7.059  29.781 -28.461  1.00 50.55
ATOM   2906  C   LYS A 380       6.728  30.241 -29.873  1.00 51.20
ATOM   2907  O   LYS A 380       5.761  29.773 -30.471  1.00 52.89
ATOM   2908  CB  LYS A 380       6.201  30.545 -27.443  1.00 52.91
ATOM   2909  CG  LYS A 380       6.126  29.891 -26.058  1.00 55.83
ATOM   2910  CD  LYS A 380       5.222  28.644 -26.074  1.00 58.24
ATOM   2911  CE  LYS A 380       5.184  27.925 -24.721  1.00 58.07
ATOM   2912  NZ  LYS A 380       6.477  27.264 -24.383  1.00 56.46
ATOM   2913  N   THR A 381       7.534  31.151 -30.410  1.00 50.07
ATOM   2914  CA  THR A 381       7.300  31.659 -31.754  1.00 49.62
ATOM   2915  C   THR A 381       8.568  31.627 -32.586  1.00 48.90
ATOM   2916  O   THR A 381       9.670  31.489 -32.052  1.00 47.76
ATOM   2917  CB  THR A 381       6.814  33.106 -31.721  1.00 52.37
ATOM   2918  OG1 THR A 381       7.876  33.951 -31.246  1.00 52.76
ATOM   2919  CG2 THR A 381       5.601  33.234 -30.803  1.00 51.54
ATOM   2920  N   CYS A 382       8.407  31.769 -33.898  1.00 47.38
ATOM   2921  CA  CYS A 382       9.550  31.767 -34.790  1.00 46.51
ATOM   2922  C   CYS A 382      10.417  32.980 -34.491  1.00 44.71
ATOM   2923  O   CYS A 382      11.625  32.971 -34.734  1.00 45.08
ATOM   2924  CB  CYS A 382       9.083  31.769 -36.242  1.00 48.55
ATOM   2925  SG  CYS A 382       8.145  30.279 -36.680  1.00 52.50
ATOM   2926  N   ALA A 383       9.799  34.020 -33.945  1.00 41.74
ATOM   2927  CA  ALA A 383      10.534  35.221 -33.589  1.00 39.26
ATOM   2928  C   ALA A 383      11.578  34.836 -32.535  1.00 39.05
ATOM   2929  O   ALA A 383      12.734  35.247 -32.610  1.00 37.36
ATOM   2930  CB  ALA A 383       9.581  36.264 -33.028  1.00 38.10
ATOM   2931  N   ASP A 384      11.165  34.037 -31.555  1.00 38.72
ATOM   2932  CA  ASP A 384      12.074  33.604 -30.503  1.00 39.20
ATOM   2933  C   ASP A 384      13.148  32.704 -31.088  1.00 39.13
ATOM   2934  O   ASP A 384      14.249  32.597 -30.551  1.00 38.43
ATOM   2935  CB  ASP A 384      11.322  32.838 -29.417  1.00 40.86
ATOM   2936  CG  ASP A 384      10.285  33.684 -28.723  1.00 43.41
ATOM   2937  OD1 ASP A 384      10.607  34.831 -28.363  1.00 46.44
ATOM   2938  OD2 ASP A 384       9.153  33.198 -28.523  1.00 46.81
ATOM   2939  N   LEU A 385      12.824  32.056 -32.195  1.00 38.87
ATOM   2940  CA  LEU A 385      13.774  31.161 -32.840  1.00 40.89
ATOM   2941  C   LEU A 385      14.867  31.970 -33.547  1.00 40.58
ATOM   2942  O   LEU A 385      16.042  31.596 -33.521  1.00 40.32
ATOM   2943  CB  LEU A 385      13.039  30.267 -33.841  1.00 39.64
ATOM   2944  CG  LEU A 385      13.755  29.002 -34.293  1.00 39.57
ATOM   2945  CD1 LEU A 385      14.150  28.194 -33.069  1.00 37.82
ATOM   2946  CD2 LEU A 385      12.839  28.194 -35.214  1.00 37.35
ATOM   2947  N   LEU A 386      14.475  33.081 -34.170  1.00 40.10
ATOM   2948  CA  LEU A 386      15.433  33.932 -34.871  1.00 41.26
ATOM   2949  C   LEU A 386      16.540  34.389 -33.928  1.00 41.67
ATOM   2950  O   LEU A 386      17.726  34.304 -34.250  1.00 42.15
ATOM   2951  CB  LEU A 386      14.723  35.150 -35.474  1.00 40.06
ATOM   2952  CG  LEU A 386      15.581  36.259 -36.101  1.00 38.88
ATOM   2953  CD1 LEU A 386      16.615  35.676 -37.063  1.00 38.52
ATOM   2954  CD2 LEU A 386      14.662  37.235 -36.832  1.00 40.83
ATOM   2955  N   ALA A 387      16.143  34.874 -32.759  1.00 42.78
ATOM   2956  CA  ALA A 387      17.098  35.336 -31.757  1.00 44.40
ATOM   2957  C   ALA A 387      18.118  34.237 -31.476  1.00 44.41
ATOM   2958  O   ALA A 387      19.328  34.455 -31.533  1.00 43.56
ATOM   2959  CB  ALA A 387      16.354  35.704 -30.468  1.00 45.36
ATOM   2960  N   LEU A 388      17.611  33.048 -31.178  1.00 43.62
ATOM   2961  CA  LEU A 388      18.457  31.905 -30.881  1.00 43.53
ATOM   2962  C   LEU A 388      19.411  31.491 -31.987  1.00 43.89
ATOM   2963  O   LEU A 388      20.573  31.190 -31.714  1.00 42.79
ATOM   2964  CB  LEU A 388      17.595  30.714 -30.507  1.00 43.46
ATOM   2965  CG  LEU A 388      17.553  30.509 -29.008  1.00 44.27
ATOM   2966  CD1 LEU A 388      16.509  29.470 -28.692  1.00 45.49
ATOM   2967  CD2 LEU A 388      18.944  30.096 -28.514  1.00 43.99
ATOM   2968  N   ARG A 389      18.911  31.447 -33.224  1.00 44.08
ATOM   2969  CA  ARG A 389      19.733  31.061 -34.371  1.00 44.37
ATOM   2970  C   ARG A 389      20.894  32.025 -34.529  1.00 44.33
ATOM   2971  O   ARG A 389      22.006  31.618 -34.843  1.00 45.76
ATOM   2972  CB  ARG A 389      18.917  31.077 -35.668  1.00 43.95
ATOM   2973  CG  ARG A 389      17.760  30.083 -35.749  1.00 44.23
ATOM   2974  CD  ARG A 389      18.190  28.713 -36.260  1.00 44.25
ATOM   2975  NE  ARG A 389      17.033  27.835 -36.453  1.00 45.59
ATOM   2976  CZ  ARG A 389      16.385  27.684 -37.605  1.00 46.22
ATOM   2977  NH1 ARG A 389      16.781  28.347 -38.688  1.00 47.23
ATOM   2978  NH2 ARG A 389      15.329  26.882 -37.670  1.00 43.72
ATOM   2979  N   SER A 390      20.632  33.307 -34.301  1.00 44.54
ATOM   2980  CA  SER A 390      21.657  34.333 -34.452  1.00 44.94
ATOM   2981  C   SER A 390      22.886  34.202 -33.554  1.00 45.96
ATOM   2982  O   SER A 390      22.906  33.431 -32.586  1.00 45.89
ATOM   2983  CB  SER A 390      21.042  35.717 -34.244  1.00 44.50
ATOM   2984  OG  SER A 390      20.712  35.929 -32.888  1.00 42.33
ATOM   2985  N   ASP A 391      23.902  34.992 -33.894  1.00 46.76
ATOM   2986  CA  ASP A 391      25.174  35.043 -33.179  1.00 46.17
ATOM   2987  C   ASP A 391      25.032  35.716 -31.816  1.00 46.19
ATOM   2988  O   ASP A 391      26.024  35.966 -31.121  1.00 48.03
ATOM   2989  CB  ASP A 391      26.197  35.800 -34.025  1.00 49.00
ATOM   2990  CG  ASP A 391      25.710  37.193 -34.436  1.00 51.64
ATOM   2991  OD1 ASP A 391      26.362  37.812 -35.305  1.00 52.14
ATOM   2992  OD2 ASP A 391      24.688  37.673 -33.890  1.00 51.93
ATOM   2993  N   ALA A 392      23.794  36.028 -31.450  1.00 43.01
ATOM   2994  CA  ALA A 392      23.508  36.650 -30.170  1.00 41.13
ATOM   2995  C   ALA A 392      23.716  35.601 -29.073  1.00 40.10
ATOM   2996  O   ALA A 392      23.980  35.937 -27.913  1.00 38.29
ATOM   2997  CB  ALA A 392      22.072  37.159 -30.152  1.00 40.90
ATOM   2998  N   TYR A 393      23.595  34.333 -29.464  1.00 39.40
ATOM   2999  CA  TYR A 393      23.771  33.191 -28.564  1.00 38.24
ATOM   3000  C   TYR A 393      24.933  32.315 -28.994  1.00 38.88
ATOM   3001  O   TYR A 393      25.062  31.967 -30.171  1.00 39.53
ATOM   3002  CB  TYR A 393      22.510  32.326 -28.534  1.00 35.53
ATOM   3003  CG  TYR A 393      21.393  32.905 -27.713  1.00 34.50
ATOM   3004  CD1 TYR A 393      21.327  32.689 -26.342  1.00 32.25
ATOM   3005  CD2 TYR A 393      20.402  33.680 -28.308  1.00 36.53
ATOM   3006  CE1 TYR A 393      20.297  33.229 -25.577  1.00 35.72
ATOM   3007  CE2 TYR A 393      19.371  34.229 -27.559  1.00 36.34
ATOM   3008  CZ  TYR A 393      19.323  34.001 -26.195  1.00 36.02
ATOM   3009  OH  TYR A 393      18.307  34.559 -25.460  1.00 36.49
ATOM   3010  N   VAL A 394      25.772  31.952 -28.028  1.00 39.27
ATOM   3011  CA  VAL A 394      26.917  31.093 -28.290  1.00 38.74
ATOM   3012  C   VAL A 394      26.763  29.795 -27.515  1.00 39.58
ATOM   3013  O   VAL A 394      25.949  29.707 -26.595  1.00 40.36
ATOM   3014  CB  VAL A 394      28.235  31.770 -27.864  1.00 39.09
ATOM   3015  CG1 VAL A 394      28.371  33.095 -28.586  1.00 37.44
ATOM   3016  CG2 VAL A 394      28.278  31.954 -26.344  1.00 33.92
ATOM   3017  N   VAL A 395      27.547  28.789 -27.888  1.00 39.45
ATOM   3018  CA  VAL A 395      27.502  27.497 -27.221  1.00 39.72
ATOM   3019  C   VAL A 395      28.709  27.345 -26.307  1.00 41.11
ATOM   3020  O   VAL A 395      29.848  27.514 -26.741  1.00 42.32
ATOM   3021  CB  VAL A 395      27.528  26.343 -28.238  1.00 39.59
ATOM   3022  CG1 VAL A 395      27.313  25.018 -27.521  1.00 35.37
ATOM   3023  CG2 VAL A 395      26.477  26.567 -29.307  1.00 36.20
ATOM   3024  N   THR A 396      28.459  27.024 -25.044  1.00 42.23
ATOM   3025  CA  THR A 396      29.533  26.845 -24.079  1.00 41.33
ATOM   3026  C   THR A 396      30.201  25.496 -24.307  1.00 43.92
ATOM   3027  O   THR A 396      29.786  24.725 -25.172  1.00 44.46
ATOM   3028  CB  THR A 396      29.014  26.872 -22.637  1.00 38.51
ATOM   3029  OG1 THR A 396      28.132  25.766 -22.428  1.00 38.23
ATOM   3030  CG2 THR A 396      28.282  28.158 -22.362  1.00 36.07
ATOM   3031  N   ASP A 397      31.241  25.219 -23.527  1.00 46.49
ATOM   3032  CA  ASP A 397      31.965  23.960 -23.636  1.00 47.07
ATOM   3033  C   ASP A 397      31.121  22.809 -23.102  1.00 45.47
ATOM   3034  O   ASP A 397      31.221  21.690 -23.597  1.00 45.88
ATOM   3035  CB  ASP A 397      33.284  24.045 -22.867  1.00 52.84
ATOM   3036  CG  ASP A 397      34.193  25.149 -23.387  1.00 57.18
ATOM   3037  OD1 ASP A 397      34.614  25.083 -24.567  1.00 56.69
ATOM   3038  OD2 ASP A 397      34.481  26.089 -22.612  1.00 61.36
ATOM   3039  N   ASP A 398      30.302  23.075 -22.085  1.00 43.70
ATOM   3040  CA  ASP A 398      29.435  22.034 -21.537  1.00 43.27
ATOM   3041  C   ASP A 398      28.083  22.010 -22.266  1.00 43.46
ATOM   3042  O   ASP A 398      27.065  21.563 -21.726  1.00 42.25
ATOM   3043  CB  ASP A 398      29.237  22.202 -20.022  1.00 41.89
ATOM   3044  CG  ASP A 398      28.790  23.594 -19.630  1.00 43.44
ATOM   3045  OD1 ASP A 398      28.409  23.777 -18.456  1.00 44.10
ATOM   3046  OD2 ASP A 398      28.822  24.508 -20.477  1.00 45.60
ATOM   3047  N   PHE A 399      28.107  22.509 -23.502  1.00 43.83
ATOM   3048  CA  PHE A 399      26.959  22.549 -24.404  1.00 43.09
ATOM   3049  C   PHE A 399      25.694  23.266 -23.961  1.00 43.23
ATOM   3050  O   PHE A 399      24.590  22.732 -24.077  1.00 43.66
ATOM   3051  CB  PHE A 399      26.614  21.131 -24.839  1.00 41.20
ATOM   3052  CG  PHE A 399      27.740  20.435 -25.521  1.00 41.76
ATOM   3053  CD1 PHE A 399      28.680  19.728 -24.789  1.00 42.80
ATOM   3054  CD2 PHE A 399      27.893  20.523 -26.900  1.00 42.61
ATOM   3055  CE1 PHE A 399      29.763  19.112 -25.421  1.00 42.70
ATOM   3056  CE2 PHE A 399      28.968  19.915 -27.538  1.00 42.36
ATOM   3057  CZ  PHE A 399      29.907  19.208 -26.794  1.00 41.44
ATOM   3058  N   ARG A 400      25.860  24.484 -23.464  1.00 43.03
ATOM   3059  CA  ARG A 400      24.732  25.288 -23.038  1.00 42.72
ATOM   3060  C   ARG A 400      24.633  26.470 -23.986  1.00 43.67
ATOM   3061  O   ARG A 400      25.630  26.893 -24.578  1.00 45.21
ATOM   3062  CB  ARG A 400      24.930  25.804 -21.615  1.00 42.50
ATOM   3063  CG  ARG A 400      24.879  24.735 -20.559  1.00 44.85
ATOM   3064  CD  ARG A 400      25.072  25.314 -19.158  1.00 46.66
ATOM   3065  NE  ARG A 400      26.376  25.950 -18.977  1.00 46.51
ATOM   3066  CZ  ARG A 400      26.559  27.260 -18.819  1.00 47.88
ATOM   3067  NH1 ARG A 400      25.518  28.087 -18.820  1.00 45.47
ATOM   3068  NH2 ARG A 400      27.785  27.743 -18.647  1.00 45.97
ATOM   3069  N   LEU A 401      23.426  26.993 -24.136  1.00 42.08
ATOM   3070  CA  LEU A 401      23.197  28.132 -24.997  1.00 40.46
ATOM   3071  C   LEU A 401      23.048  29.370 -24.131  1.00 40.29
ATOM   3072  O   LEU A 401      22.097  29.486 -23.359  1.00 40.41
ATOM   3073  CB  LEU A 401      21.931  27.925 -25.817  1.00 41.67
ATOM   3074  CG  LEU A 401      22.065  27.268 -27.178  1.00 41.66
ATOM   3075  CD1 LEU A 401      20.672  27.046 -27.720  1.00 43.89
ATOM   3076  CD2 LEU A 401      22.871  28.158 -28.129  1.00 42.24
ATOM   3077  N   VAL A 402      23.992  30.293 -24.260  1.00 39.27
ATOM   3078  CA  VAL A 402      23.961  31.514 -23.477  1.00 38.12
ATOM   3079  C   VAL A 402      24.216  32.709 -24.379  1.00 40.21
ATOM   3080  O   VAL A 402      24.801  32.571 -25.448  1.00 41.03
ATOM   3081  CB  VAL A 402      25.044  31.486 -22.370  1.00 38.09
ATOM   3082  CG1 VAL A 402      24.821  30.293 -21.454  1.00 34.45
ATOM   3083  CG2 VAL A 402      26.439  31.435 -22.997  1.00 34.97
ATOM   3084  N   LEU A 403      23.766  33.882 -23.956  1.00 42.17
ATOM   3085  CA  LEU A 403      23.989  35.088 -24.736  1.00 45.82
ATOM   3086  C   LEU A 403      25.484  35.347 -24.899  1.00 49.32
ATOM   3087  O   LEU A 403      26.289  34.947 -24.050  1.00 50.14
ATOM   3088  CB  LEU A 403      23.356  36.292 -24.043  1.00 43.66
ATOM   3089  CG  LEU A 403      21.837  36.409 -24.085  1.00 43.31
ATOM   3090  CD1 LEU A 403      21.421  37.614 -23.242  1.00 43.86
ATOM   3091  CD2 LEU A 403      21.351  36.556 -25.526  1.00 38.04
ATOM   3092  N   ASP A 404      25.844  36.002 -26.003  1.00 52.66
ATOM   3093  CA  ASP A 404      27.227  36.363 -26.287  1.00 54.56
ATOM   3094  C   ASP A 404      27.539  37.455 -25.272  1.00 57.27
ATOM   3095  O   ASP A 404      26.621  38.113 -24.782  1.00 57.88
ATOM   3096  CB  ASP A 404      27.342  36.921 -27.707  1.00 56.28
ATOM   3097  CG  ASP A 404      28.773  37.251 -28.096  1.00 57.08
ATOM   3098  OD1 ASP A 404      29.323  36.558 -28.984  1.00 57.25
ATOM   3099  OD2 ASP A 404      29.342  38.201 -27.514  1.00 57.69
ATOM   3100  N   ASP A 405      28.814  37.659 -24.956  1.00 59.95
ATOM   3101  CA  ASP A 405      29.184  38.674 -23.968  1.00 61.91
ATOM   3102  C   ASP A 405      28.776  40.111 -24.308  1.00 61.90
ATOM   3103  O   ASP A 405      28.449  40.890 -23.410  1.00 61.88
ATOM   3104  CB  ASP A 405      30.692  38.627 -23.681  1.00 64.90
ATOM   3105  CG  ASP A 405      31.093  37.421 -22.839  1.00 67.73
ATOM   3106  OD1 ASP A 405      30.320  37.048 -21.927  1.00 67.97
ATOM   3107  OD2 ASP A 405      32.187  36.857 -23.077  1.00 68.87
ATOM   3108  N   ARG A 406      28.787  40.463 -25.591  1.00 61.46
ATOM   3109  CA  ARG A 406      28.422  41.818 -26.007  1.00 60.96
ATOM   3110  C   ARG A 406      26.929  42.129 -25.872  1.00 60.81
ATOM   3111  O   ARG A 406      26.460  43.157 -26.360  1.00 61.90
ATOM   3112  CB  ARG A 406      28.865  42.061 -27.454  1.00 61.54
ATOM   3113  CG  ARG A 406      30.366  41.933 -27.666  1.00 62.98
ATOM   3114  CD  ARG A 406      30.697  40.882 -28.716  1.00 63.31
ATOM   3115  NE  ARG A 406      30.575  41.387 -30.082  1.00 64.25
ATOM   3116  CZ  ARG A 406      30.663  40.621 -31.166  1.00 65.23
ATOM   3117  NH1 ARG A 406      30.866  39.315 -31.035  1.00 64.24
ATOM   3118  NH2 ARG A 406      30.561  41.157 -32.377  1.00 64.31
ATOM   3119  N   CYS A 407      26.184  41.245 -25.215  1.00 59.35
ATOM   3120  CA  CYS A 407      24.750  41.447 -25.020  1.00 58.01
ATOM   3121  C   CYS A 407      24.468  41.986 -23.620  1.00 57.80
ATOM   3122  O   CYS A 407      23.416  42.571 -23.366  1.00 54.63
ATOM   3123  CB  CYS A 407      23.996  40.131 -25.223  1.00 56.78
ATOM   3124  SG  CYS A 407      23.974  39.543 -26.918  1.00 56.36
ATOM   3125  N   HIS A 408      25.417  41.768 -22.716  1.00 58.04
ATOM   3126  CA  HIS A 408      25.298  42.232 -21.341  1.00 59.46
ATOM   3127  C   HIS A 408      24.065  41.685 -20.631  1.00 58.68
ATOM   3128  O   HIS A 408      23.460  42.373 -19.809  1.00 59.40
ATOM   3129  CB  HIS A 408      25.279  43.767 -21.305  1.00 62.93
ATOM   3130  CG  HIS A 408      26.512  44.398 -21.877  1.00 66.12
ATOM   3131  ND1 HIS A 408      27.767  44.204 -21.336  1.00 67.78
ATOM   3132  CD2 HIS A 408      26.687  45.199 -22.955  1.00 67.87
ATOM   3133  CE1 HIS A 408      28.661  44.858 -22.057  1.00 69.21
ATOM   3134  NE2 HIS A 408      28.032  45.470 -23.046  1.00 69.27
ATOM   3135  N   GLY A 409      23.698  40.447 -20.951  1.00 57.28
ATOM   3136  CA  GLY A 409      22.546  39.830 -20.316  1.00 54.87
ATOM   3137  C   GLY A 409      21.213  40.210 -20.925  1.00 54.89
ATOM   3138  O   GLY A 409      20.162  39.777 -20.452  1.00 55.33
ATOM   3139  N   HIS A 410      21.247  41.018 -21.979  1.00 54.46
ATOM   3140  CA  HIS A 410      20.025  41.450 -22.644  1.00 53.28
ATOM   3141  C   HIS A 410      19.889  40.824 -24.020  1.00 51.18
ATOM   3142  O   HIS A 410      20.666  41.110 -24.926  1.00 50.89
ATOM   3143  CB  HIS A 410      20.016  42.964 -22.787  1.00 56.49
ATOM   3144  CG  HIS A 410      20.056  43.693 -21.484  1.00 60.80
ATOM   3145  ND1 HIS A 410      18.998  43.695 -20.601  1.00 60.85
ATOM   3146  CD2 HIS A 410      21.028  44.443 -20.912  1.00 61.81
ATOM   3147  CE1 HIS A 410      19.315  44.417 -19.541  1.00 62.39
ATOM   3148  NE2 HIS A 410      20.542  44.882 -19.705  1.00 63.64
ATOM   3149  N   PRO A 411      18.894  39.951 -24.196  1.00 49.80
ATOM   3150  CA  PRO A 411      18.736  39.332 -25.514  1.00 48.66
ATOM   3151  C   PRO A 411      18.114  40.304 -26.510  1.00 47.35
ATOM   3152  O   PRO A 411      17.447  41.267 -26.124  1.00 47.70
ATOM   3153  CB  PRO A 411      17.818  38.139 -25.234  1.00 47.45
ATOM   3154  CG  PRO A 411      18.023  37.872 -23.751  1.00 49.15
ATOM   3155  CD  PRO A 411      18.071  39.262 -23.190  1.00 48.91
ATOM   3156  N   PRO A 412      18.355  40.086 -27.808  1.00 46.31
ATOM   3157  CA  PRO A 412      17.764  40.990 -28.794  1.00 44.49
ATOM   3158  C   PRO A 412      16.262  40.809 -28.712  1.00 43.12
ATOM   3159  O   PRO A 412      15.780  39.685 -28.578  1.00 43.16
ATOM   3160  CB  PRO A 412      18.308  40.466 -30.117  1.00 44.05
ATOM   3161  CG  PRO A 412      19.623  39.899 -29.735  1.00 47.19
ATOM   3162  CD  PRO A 412      19.327  39.181 -28.441  1.00 45.88
ATOM   3163  N   VAL A 413      15.519  41.904 -28.758  1.00 41.85
ATOM   3164  CA  VAL A 413      14.076  41.794 -28.736  1.00 39.33
ATOM   3165  C   VAL A 413      13.695  41.644 -30.198  1.00 40.02
ATOM   3166  O   VAL A 413      13.992  42.514 -31.011  1.00 42.67
ATOM   3167  CB  VAL A 413      13.394  43.053 -28.161  1.00 38.88
ATOM   3168  CG1 VAL A 413      11.882  42.946 -28.355  1.00 37.06
ATOM   3169  CG2 VAL A 413      13.717  43.198 -26.676  1.00 34.08
ATOM   3170  N   VAL A 414      13.052  40.535 -30.532  1.00 40.16
ATOM   3171  CA  VAL A 414      12.650  40.266 -31.900  1.00 39.90
ATOM   3172  C   VAL A 414      11.130  40.290 -32.033  1.00 41.08
ATOM   3173  O   VAL A 414      10.409  39.666 -31.258  1.00 40.37
ATOM   3174  CB  VAL A 414      13.206  38.901 -32.348  1.00 38.90
ATOM   3175  CG1 VAL A 414      12.861  38.626 -33.805  1.00 36.72
ATOM   3176  CG2 VAL A 414      14.704  38.881 -32.138  1.00 39.29
ATOM   3177  N   ASP A 415      10.645  41.037 -33.015  1.00 43.38
ATOM   3178  CA  ASP A 415       9.213  41.139 -33.256  1.00 45.52
ATOM   3179  C   ASP A 415       8.976  40.918 -34.735  1.00 45.73
ATOM   3180  O   ASP A 415       9.236  41.798 -35.556  1.00 45.81
ATOM   3181  CB  ASP A 415       8.691  42.517 -32.843  1.00 49.20
ATOM   3182  CG  ASP A 415       7.218  42.712 -33.176  1.00 53.15
ATOM   3183  OD1 ASP A 415       6.663  43.768 -32.801  1.00 55.32
ATOM   3184  OD2 ASP A 415       6.614  41.819 -33.815  1.00 55.55
ATOM   3185  N   LEU A 416       8.486  39.731 -35.070  1.00 45.07
ATOM   3186  CA  LEU A 416       8.225  39.383 -36.453  1.00 45.72
ATOM   3187  C   LEU A 416       6.739  39.468 -36.763  1.00 46.65
ATOM   3188  O   LEU A 416       5.901  39.064 -35.961  1.00 45.01
ATOM   3189  CB  LEU A 416       8.758  37.977 -36.742  1.00 44.41
ATOM   3190  CG  LEU A 416      10.279  37.817 -36.685  1.00 41.77
ATOM   3191  CD1 LEU A 416      10.648  36.375 -36.924  1.00 41.87
ATOM   3192  CD2 LEU A 416      10.932  38.696 -37.725  1.00 40.48
ATOM   3193  N   ASP A 417       6.420  40.015 -37.931  1.00 50.21
ATOM   3194  CA  ASP A 417       5.035  40.162 -38.359  1.00 52.36
ATOM   3195  C   ASP A 417       4.415  38.800 -38.640  1.00 55.06
ATOM   3196  O   ASP A 417       4.930  38.026 -39.447  1.00 54.32
ATOM   3197  CB  ASP A 417       4.973  41.046 -39.611  1.00 52.91
ATOM   3198  CG  ASP A 417       3.592  41.070 -40.259  1.00 52.77
ATOM   3199  OD1 ASP A 417       2.579  40.919 -39.541  1.00 53.36
ATOM   3200  OD2 ASP A 417       3.522  41.262 -41.493  1.00 52.15
ATOM   3201  N   SER A 418       3.318  38.498 -37.955  1.00 57.58
ATOM   3202  CA  SER A 418       2.643  37.233 -38.180  1.00 61.87
ATOM   3203  C   SER A 418       2.090  37.279 -39.605  1.00 63.81
ATOM   3204  O   SER A 418       2.459  38.155 -40.387  1.00 64.47
ATOM   3205  CB  SER A 418       1.518  37.047 -37.159  1.00 63.99
ATOM   3206  OG  SER A 418       2.046  37.008 -35.840  1.00 62.57
ATOM   3207  N   ALA A 419       1.217  36.345 -39.958  1.00 65.32
ATOM   3208  CA  ALA A 419       0.665  36.332 -41.311  1.00 65.52
ATOM   3209  C   ALA A 419       1.814  36.224 -42.304  1.00 65.35
ATOM   3210  O   ALA A 419       1.635  36.391 -43.509  1.00 66.74
ATOM   3211  CB  ALA A 419      -0.129  37.611 -41.568  1.00 65.48
ATOM   3212  N   HIS A 420       3.001  35.947 -41.784  1.00 64.56
ATOM   3213  CA  HIS A 420       4.180  35.808 -42.614  1.00 65.13
ATOM   3214  C   HIS A 420       5.210  34.919 -41.929  1.00 64.85
ATOM   3215  O   HIS A 420       5.731  33.979 -42.531  1.00 64.35
ATOM   3216  CB  HIS A 420       4.802  37.180 -42.890  1.00 66.76
ATOM   3217  CG  HIS A 420       4.075  37.987 -43.921  1.00 67.50
ATOM   3218  ND1 HIS A 420       4.143  37.708 -45.268  1.00 67.13
ATOM   3219  CD2 HIS A 420       3.283  39.079 -43.802  1.00 67.42
ATOM   3220  CE1 HIS A 420       3.427  38.595 -45.935  1.00 68.47
ATOM   3221  NE2 HIS A 420       2.895  39.438 -45.068  1.00 67.34
ATOM   3222  N   TYR A 421       5.497  35.211 -40.665  1.00 64.23
ATOM   3223  CA  TYR A 421       6.493  34.442 -39.936  1.00 63.62
ATOM   3224  C   TYR A 421       5.956  33.783 -38.675  1.00 63.75
ATOM   3225  O   TYR A 421       6.721  33.385 -37.796  1.00 63.44
ATOM   3226  CB  TYR A 421       7.674  35.345 -39.605  1.00 62.79
ATOM   3227  CG  TYR A 421       8.010  36.277 -40.743  1.00 63.43
ATOM   3228  CD1 TYR A 421       7.602  37.610 -40.719  1.00 62.95
ATOM   3229  CD2 TYR A 421       8.713  35.820 -41.857  1.00 62.93
ATOM   3230  CE1 TYR A 421       7.888  38.465 -41.770  1.00 63.04
ATOM   3231  CE2 TYR A 421       9.005  36.664 -42.917  1.00 62.96
ATOM   3232  CZ  TYR A 421       8.592  37.988 -42.869  1.00 64.49
ATOM   3233  OH  TYR A 421       8.900  38.841 -43.910  1.00 63.05
ATOM   3234  N   LYS A 422       4.635  33.670 -38.595  1.00 64.01
ATOM   3235  CA  LYS A 422       3.991  33.036 -37.455  1.00 64.52
ATOM   3236  C   LYS A 422       4.360  31.560 -37.456  1.00 65.99
ATOM   3237  O   LYS A 422       4.276  30.888 -36.429  1.00 66.17
ATOM   3238  CB  LYS A 422       2.475  33.179 -37.558  1.00 64.81
ATOM   3239  CG  LYS A 422       1.689  32.480 -36.460  1.00 64.34
ATOM   3240  CD  LYS A 422       1.928  33.124 -35.111  1.00 66.12
ATOM   3241  CE  LYS A 422       0.926  32.628 -34.080  1.00 66.70
ATOM   3242  NZ  LYS A 422       1.035  31.163 -33.861  1.00 66.53
ATOM   3243  N   MET A 423       4.780  31.056 -38.610  1.00 66.76
ATOM   3244  CA  MET A 423       5.141  29.656 -38.699  1.00 69.14
ATOM   3245  C   MET A 423       6.317  29.350 -39.608  1.00 67.21
ATOM   3246  O   MET A 423       6.556  30.048 -40.591  1.00 65.88
ATOM   3247  CB  MET A 423       3.932  28.852 -39.135  1.00 74.86
ATOM   3248  CG  MET A 423       3.297  29.359 -40.392  1.00 81.07
ATOM   3249  SD  MET A 423       1.621  28.490 -40.569  1.00 91.94
ATOM   3250  CE  MET A 423       2.145  27.121 -41.839  1.00 88.84
ATOM   3251  N   MET A 424       7.029  28.279 -39.259  1.00 65.73
ATOM   3252  CA  MET A 424       8.220  27.820 -39.968  1.00 65.31
ATOM   3253  C   MET A 424       8.101  27.997 -41.472  1.00 65.20
ATOM   3254  O   MET A 424       9.086  28.283 -42.158  1.00 63.06
ATOM   3255  CB  MET A 424       8.475  26.350 -39.640  1.00 64.30
ATOM   3256  CG  MET A 424       9.933  25.954 -39.689  1.00 65.31
ATOM   3257  SD  MET A 424      10.975  26.918 -38.377  1.00 67.81
ATOM   3258  CE  MET A 424       9.658  26.996 -36.965  1.00 61.92
ATOM   3259  N   ASN A 425       6.880  27.815 -41.965  1.00 66.70
ATOM   3260  CA  ASN A 425       6.559  27.948 -43.382  1.00 68.80
ATOM   3261  C   ASN A 425       7.219  29.224 -43.912  1.00 68.77
ATOM   3262  O   ASN A 425       8.146  29.174 -44.727  1.00 69.37
ATOM   3263  CB  ASN A 425       5.034  28.034 -43.550  1.00 69.88
ATOM   3264  CG  ASN A 425       4.550  27.493 -44.886  1.00 70.20
ATOM   3265  OD1 ASN A 425       4.997  27.923 -45.949  1.00 70.45
ATOM   3266  ND2 ASN A 425       3.618  26.548 -44.832  1.00 72.13
ATOM   3267  N   GLY A 426       6.745  30.365 -43.421  1.00 67.75
ATOM   3268  CA  GLY A 426       7.287  31.639 -43.849  1.00 66.42
ATOM   3269  C   GLY A 426       8.611  32.021 -43.217  1.00 64.86
ATOM   3270  O   GLY A 426       9.453  32.623 -43.875  1.00 66.69
ATOM   3271  N   PHE A 427       8.809  31.671 -41.950  1.00 62.92
ATOM   3272  CA  PHE A 427      10.045  32.019 -41.260  1.00 61.71
ATOM   3273  C   PHE A 427      11.312  31.548 -41.947  1.00 62.55
ATOM   3274  O   PHE A 427      12.298  32.279 -41.994  1.00 61.79
ATOM   3275  CB  PHE A 427      10.048  31.475 -39.830  1.00 60.07
ATOM   3276  CG  PHE A 427      11.372  31.636 -39.130  1.00 57.59
ATOM   3277  CD1 PHE A 427      11.811  32.890 -38.719  1.00 56.90
ATOM   3278  CD2 PHE A 427      12.199  30.541 -38.918  1.00 54.47
ATOM   3279  CE1 PHE A 427      13.059  33.051 -38.107  1.00 56.31
ATOM   3280  CE2 PHE A 427      13.444  30.693 -38.309  1.00 55.04
ATOM   3281  CZ  PHE A 427      13.874  31.953 -37.903  1.00 54.82
ATOM   3282  N   GLU A 428      11.307  30.327 -42.467  1.00 65.62
ATOM   3283  CA  GLU A 428      12.506  29.816 -43.116  1.00 69.27
ATOM   3284  C   GLU A 428      12.798  30.632 -44.375  1.00 69.94
ATOM   3285  O   GLU A 428      13.950  30.729 -44.809  1.00 68.95
ATOM   3286  CB  GLU A 428      12.345  28.329 -43.443  1.00 72.23
ATOM   3287  CG  GLU A 428      13.660  27.516 -43.404  1.00 76.65
ATOM   3288  CD  GLU A 428      14.288  27.411 -42.005  1.00 78.53
ATOM   3289  OE1 GLU A 428      14.819  28.425 -41.505  1.00 80.41
ATOM   3290  OE2 GLU A 428      14.253  26.311 -41.403  1.00 78.57
ATOM   3291  N   LYS A 429      11.750  31.223 -44.951  1.00 70.61
ATOM   3292  CA  LYS A 429      11.899  32.068 -46.136  1.00 71.11
ATOM   3293  C   LYS A 429      12.717  33.286 -45.712  1.00 70.32
ATOM   3294  O   LYS A 429      13.798  33.545 -46.246  1.00 69.11
ATOM   3295  CB  LYS A 429      10.533  32.541 -46.650  1.00 72.90
ATOM   3296  CG  LYS A 429       9.576  31.424 -47.049  1.00 76.17
ATOM   3297  CD  LYS A 429       8.207  31.970 -47.467  1.00 78.33
ATOM   3298  CE  LYS A 429       7.225  30.836 -47.770  1.00 80.31
ATOM   3299  NZ  LYS A 429       5.866  31.326 -48.148  1.00 80.58
ATOM   3300  N   LEU A 430      12.186  34.018 -44.733  1.00 68.99
ATOM   3301  CA  LEU A 430      12.829  35.215 -44.202  1.00 67.05
ATOM   3302  C   LEU A 430      14.333  35.037 -44.022  1.00 66.51
ATOM   3303  O   LEU A 430      15.113  35.925 -44.364  1.00 65.77
ATOM   3304  CB  LEU A 430      12.199  35.598 -42.861  1.00 66.89
ATOM   3305  CG  LEU A 430      12.730  36.874 -42.201  1.00 66.58
ATOM   3306  CD1 LEU A 430      12.301  38.076 -43.015  1.00 66.84
ATOM   3307  CD2 LEU A 430      12.201  36.990 -40.791  1.00 66.48
ATOM   3308  N   VAL A 431      14.741  33.893 -43.485  1.00 66.92
ATOM   3309  CA  VAL A 431      16.162  33.633 -43.270  1.00 68.16
ATOM   3310  C   VAL A 431      16.767  32.736 -44.347  1.00 69.09
ATOM   3311  O   VAL A 431      17.911  32.306 -44.235  1.00 68.62
ATOM   3312  CB  VAL A 431      16.409  32.996 -41.884  1.00 67.65
ATOM   3313  CG1 VAL A 431      16.257  34.048 -40.802  1.00 68.09
ATOM   3314  CG2 VAL A 431      15.428  31.859 -41.649  1.00 66.14
ATOM   3315  N   GLN A 432      15.992  32.472 -45.394  1.00 71.03
ATOM   3316  CA  GLN A 432      16.432  31.634 -46.504  1.00 73.34
ATOM   3317  C   GLN A 432      17.891  31.866 -46.913  1.00 73.13
ATOM   3318  O   GLN A 432      18.693  30.936 -46.943  1.00 73.79
ATOM   3319  CB  GLN A 432      15.528  31.870 -47.722  1.00 75.49
ATOM   3320  CG  GLN A 432      15.721  30.869 -48.853  1.00 79.15
ATOM   3321  CD  GLN A 432      14.881  31.195 -50.078  1.00 80.64
ATOM   3322  OE1 GLN A 432      13.680  31.448 -49.974  1.00 81.37
ATOM   3323  NE2 GLN A 432      15.513  31.180 -51.250  1.00 81.63
ATOM   3324  N   HIS A 433      18.238  33.110 -47.215  1.00 72.66
ATOM   3325  CA  HIS A 433      19.589  33.426 -47.654  1.00 72.30
ATOM   3326  C   HIS A 433      20.583  33.671 -46.531  1.00 70.39
ATOM   3327  O   HIS A 433      21.753  33.953 -46.787  1.00 70.19
ATOM   3328  CB  HIS A 433      19.553  34.642 -48.577  1.00 76.29
ATOM   3329  CG  HIS A 433      18.416  34.623 -49.552  1.00 79.72
ATOM   3330  ND1 HIS A 433      18.177  33.560 -50.398  1.00 81.16
ATOM   3331  CD2 HIS A 433      17.443  35.531 -49.804  1.00 80.63
ATOM   3332  CE1 HIS A 433      17.104  33.813 -51.126  1.00 82.08
ATOM   3333  NE2 HIS A 433      16.640  35.003 -50.786  1.00 82.11
ATOM   3334  N   GLY A 434      20.123  33.567 -45.289  1.00 68.86
ATOM   3335  CA  GLY A 434      21.015  33.781 -44.162  1.00 65.93
ATOM   3336  C   GLY A 434      20.338  34.356 -42.930  1.00 63.80
ATOM   3337  O   GLY A 434      19.228  34.880 -42.998  1.00 64.03
ATOM   3338  N   VAL A 435      21.012  34.246 -41.792  1.00 61.85
ATOM   3339  CA  VAL A 435      20.493  34.765 -40.533  1.00 56.94
ATOM   3340  C   VAL A 435      21.320  35.995 -40.175  1.00 54.14
ATOM   3341  O   VAL A 435      22.525  35.907 -39.950  1.00 52.70
ATOM   3342  CB  VAL A 435      20.590  33.699 -39.424  1.00 57.02
ATOM   3343  CG1 VAL A 435      20.153  34.279 -38.092  1.00 56.15
ATOM   3344  CG2 VAL A 435      19.714  32.507 -39.788  1.00 55.05
ATOM   3345  N   PRO A 436      20.675  37.166 -40.128  1.00 51.80
ATOM   3346  CA  PRO A 436      21.358  38.422 -39.807  1.00 50.66
ATOM   3347  C   PRO A 436      22.016  38.407 -38.442  1.00 50.14
ATOM   3348  O   PRO A 436      21.552  37.723 -37.530  1.00 52.16
ATOM   3349  CB  PRO A 436      20.238  39.454 -39.905  1.00 50.30
ATOM   3350  CG  PRO A 436      19.042  38.680 -39.458  1.00 50.84
ATOM   3351  CD  PRO A 436      19.213  37.356 -40.167  1.00 50.92
ATOM   3352  N   SER A 437      23.107  39.152 -38.306  1.00 48.10
ATOM   3353  CA  SER A 437      23.818  39.238 -37.034  1.00 46.42
ATOM   3354  C   SER A 437      23.017  40.137 -36.086  1.00 46.09
ATOM   3355  O   SER A 437      22.718  41.287 -36.418  1.00 45.51
ATOM   3356  CB  SER A 437      25.216  39.821 -37.253  1.00 44.40
ATOM   3357  OG  SER A 437      25.801  40.206 -36.022  1.00 43.83
ATOM   3358  N   LEU A 438      22.671  39.619 -34.908  1.00 45.63
ATOM   3359  CA  LEU A 438      21.887  40.393 -33.947  1.00 42.53
ATOM   3360  C   LEU A 438      22.566  40.586 -32.597  1.00 43.34
ATOM   3361  O   LEU A 438      21.946  41.108 -31.667  1.00 44.51
ATOM   3362  CB  LEU A 438      20.535  39.718 -33.716  1.00 40.57
ATOM   3363  CG  LEU A 438      19.651  39.354 -34.913  1.00 40.46
ATOM   3364  CD1 LEU A 438      18.547  38.403 -34.456  1.00 37.79
ATOM   3365  CD2 LEU A 438      19.068  40.612 -35.534  1.00 38.88
ATOM   3366  N   VAL A 439      23.822  40.167 -32.469  1.00 41.97
ATOM   3367  CA  VAL A 439      24.519  40.311 -31.193  1.00 42.37
ATOM   3368  C   VAL A 439      24.577  41.767 -30.712  1.00 43.10
ATOM   3369  O   VAL A 439      24.600  42.029 -29.508  1.00 43.17
ATOM   3370  CB  VAL A 439      25.965  39.745 -31.267  1.00 44.13
ATOM   3371  CG1 VAL A 439      26.775  40.495 -32.319  1.00 44.29
ATOM   3372  CG2 VAL A 439      26.634  39.854 -29.902  1.00 41.44
ATOM   3373  N   GLU A 440      24.600  42.709 -31.649  1.00 42.85
ATOM   3374  CA  GLU A 440      24.653  44.129 -31.309  1.00 44.46
ATOM   3375  C   GLU A 440      23.298  44.789 -31.542  1.00 44.22
ATOM   3376  O   GLU A 440      23.185  46.014 -31.479  1.00 44.11
ATOM   3377  CB  GLU A 440      25.688  44.854 -32.172  1.00 46.65
ATOM   3378  CG  GLU A 440      27.123  44.371 -32.042  1.00 51.31
ATOM   3379  CD  GLU A 440      27.780  44.824 -30.758  1.00 54.71
ATOM   3380  OE1 GLU A 440      28.999  44.588 -30.600  1.00 55.12
ATOM   3381  OE2 GLU A 440      27.076  45.414 -29.907  1.00 57.20
ATOM   3382  N   CYS A 441      22.274  43.987 -31.825  1.00 42.17
ATOM   3383  CA  CYS A 441      20.947  44.531 -32.081  1.00 41.10
ATOM   3384  C   CYS A 441      20.023  44.524 -30.865  1.00 41.58
ATOM   3385  O   CYS A 441      19.794  43.487 -30.247  1.00 41.95
ATOM   3386  CB  CYS A 441      20.287  43.778 -33.233  1.00 39.79
ATOM   3387  SG  CYS A 441      18.614  44.328 -33.563  1.00 42.22
ATOM   3388  N   LYS A 442      19.483  45.692 -30.538  1.00 41.46
ATOM   3389  CA  LYS A 442      18.596  45.836 -29.389  1.00 42.94
ATOM   3390  C   LYS A 442      17.199  45.299 -29.692  1.00 43.17
ATOM   3391  O   LYS A 442      16.612  44.545 -28.903  1.00 40.32
ATOM   3392  CB  LYS A 442      18.515  47.314 -28.984  1.00 44.29
ATOM   3393  CG  LYS A 442      17.708  47.576 -27.724  1.00 49.07
ATOM   3394  CD  LYS A 442      17.910  49.002 -27.206  1.00 53.17
ATOM   3395  CE  LYS A 442      17.086  49.241 -25.941  1.00 55.35
ATOM   3396  NZ  LYS A 442      17.346  50.572 -25.328  1.00 57.27
ATOM   3397  N   ARG A 443      16.677  45.707 -30.842  1.00 42.12
ATOM   3398  CA  ARG A 443      15.363  45.291 -31.289  1.00 42.57
ATOM   3399  C   ARG A 443      15.312  45.288 -32.806  1.00 41.68
ATOM   3400  O   ARG A 443      15.884  46.156 -33.468  1.00 42.39
ATOM   3401  CB  ARG A 443      14.275  46.238 -30.761  1.00 44.44
ATOM   3402  CG  ARG A 443      12.859  45.856 -31.220  1.00 47.43
ATOM   3403  CD  ARG A 443      11.797  46.908 -30.875  1.00 51.44
ATOM   3404  NE  ARG A 443      11.063  46.620 -29.644  1.00 55.17
ATOM   3405  CZ  ARG A 443      11.536  46.809 -28.413  1.00 58.48
ATOM   3406  NH1 ARG A 443      12.761  47.296 -28.224  1.00 59.14
ATOM   3407  NH2 ARG A 443      10.782  46.501 -27.363  1.00 58.51
ATOM   3408  N   VAL A 444      14.641  44.284 -33.346  1.00 39.12
ATOM   3409  CA  VAL A 444      14.451  44.173 -34.775  1.00 39.04
ATOM   3410  C   VAL A 444      12.987  43.818 -34.962  1.00 40.36
ATOM   3411  O   VAL A 444      12.465  42.918 -34.301  1.00 39.71
ATOM   3412  CB  VAL A 444      15.320  43.075 -35.416  1.00 37.85
ATOM   3413  CG1 VAL A 444      15.126  41.751 -34.695  1.00 38.67
ATOM   3414  CG2 VAL A 444      14.930  42.928 -36.874  1.00 34.92
ATOM   3415  N   THR A 445      12.329  44.557 -35.845  1.00 42.48
ATOM   3416  CA  THR A 445      10.919  44.356 -36.149  1.00 44.24
ATOM   3417  C   THR A 445      10.793  44.147 -37.647  1.00 46.59
ATOM   3418  O   THR A 445      11.387  44.881 -38.435  1.00 47.12
ATOM   3419  CB  THR A 445      10.079  45.596 -35.786  1.00 43.68
ATOM   3420  OG1 THR A 445      10.156  45.842 -34.377  1.00 45.44
ATOM   3421  CG2 THR A 445       8.630  45.392 -36.193  1.00 43.78
ATOM   3422  N   VAL A 446      10.028  43.144 -38.049  1.00 48.01
ATOM   3423  CA  VAL A 446       9.851  42.898 -39.465  1.00 48.17
ATOM   3424  C   VAL A 446       8.370  42.959 -39.786  1.00 50.22
ATOM   3425  O   VAL A 446       7.576  42.165 -39.274  1.00 49.16
ATOM   3426  CB  VAL A 446      10.436  41.538 -39.867  1.00 47.69
ATOM   3427  CG1 VAL A 446      10.377  41.379 -41.377  1.00 44.32
ATOM   3428  CG2 VAL A 446      11.875  41.433 -39.370  1.00 45.62
ATOM   3429  N   LYS A 447       8.011  43.936 -40.617  1.00 51.69
ATOM   3430  CA  LYS A 447       6.629  44.160 -41.040  1.00 53.05
ATOM   3431  C   LYS A 447       6.506  43.891 -42.538  1.00 53.52
ATOM   3432  O   LYS A 447       7.302  44.403 -43.329  1.00 52.20
ATOM   3433  CB  LYS A 447       6.223  45.606 -40.757  1.00 52.57
ATOM   3434  CG  LYS A 447       6.252  45.990 -39.293  1.00 53.57
ATOM   3435  CD  LYS A 447       6.221  47.505 -39.132  1.00 54.37
ATOM   3436  CE  LYS A 447       6.087  47.918 -37.671  1.00 54.67
ATOM   3437  NZ  LYS A 447       4.740  47.585 -37.111  1.00 57.00
ATOM   3438  N   GLY A 448       5.507  43.094 -42.920  1.00 53.80
ATOM   3439  CA  GLY A 448       5.312  42.772 -44.323  1.00 53.55
ATOM   3440  C   GLY A 448       6.229  41.654 -44.783  1.00 54.82
ATOM   3441  O   GLY A 448       7.060  41.162 -44.019  1.00 55.06
ATOM   3442  N   LEU A 449       6.083  41.255 -46.041  1.00 55.68
ATOM   3443  CA  LEU A 449       6.889  40.183 -46.610  1.00 57.10
ATOM   3444  C   LEU A 449       8.327  40.653 -46.860  1.00 58.21
ATOM   3445  O   LEU A 449       8.583  41.447 -47.773  1.00 59.09
ATOM   3446  CB  LEU A 449       6.249  39.698 -47.915  1.00 57.62
ATOM   3447  CG  LEU A 449       6.722  38.348 -48.457  1.00 58.68
ATOM   3448  CD1 LEU A 449       6.535  37.284 -47.386  1.00 57.93
ATOM   3449  CD2 LEU A 449       5.935  37.985 -49.706  1.00 57.13
ATOM   3450  N   VAL A 450       9.257  40.144 -46.051  1.00 57.43
ATOM   3451  CA  VAL A 450      10.668  40.512 -46.141  1.00 54.84
ATOM   3452  C   VAL A 450      11.603  39.302 -46.229  1.00 55.92
ATOM   3453  O   VAL A 450      11.223  38.181 -45.887  1.00 54.09
ATOM   3454  CB  VAL A 450      11.078  41.347 -44.906  1.00 53.16
ATOM   3455  CG1 VAL A 450      12.497  41.864 -45.063  1.00 52.27
ATOM   3456  CG2 VAL A 450      10.100  42.491 -44.704  1.00 51.12
ATOM   3457  N   GLN A 451      12.828  39.547 -46.688  1.00 57.68
ATOM   3458  CA  GLN A 451      13.852  38.513 -46.815  1.00 60.31
ATOM   3459  C   GLN A 451      15.241  39.068 -46.523  1.00 61.12
ATOM   3460  O   GLN A 451      15.732  39.940 -47.240  1.00 61.57
ATOM   3461  CB  GLN A 451      13.869  37.921 -48.221  1.00 62.34
ATOM   3462  CG  GLN A 451      12.806  36.886 -48.501  1.00 65.85
ATOM   3463  CD  GLN A 451      13.010  36.232 -49.855  1.00 69.01
ATOM   3464  OE1 GLN A 451      14.105  35.751 -50.161  1.00 70.59
ATOM   3465  NE2 GLN A 451      11.961  36.210 -50.674  1.00 68.17
ATOM   3466  N   PHE A 452      15.881  38.559 -45.476  1.00 61.98
ATOM   3467  CA  PHE A 452      17.220  39.019 -45.140  1.00 62.16
ATOM   3468  C   PHE A 452      18.181  38.608 -46.240  1.00 62.65
ATOM   3469  O   PHE A 452      18.013  37.563 -46.868  1.00 64.46
ATOM   3470  CB  PHE A 452      17.694  38.426 -43.810  1.00 60.59
ATOM   3471  CG  PHE A 452      17.030  39.023 -42.609  1.00 58.15
ATOM   3472  CD1 PHE A 452      16.009  38.347 -41.954  1.00 57.52
ATOM   3473  CD2 PHE A 452      17.419  40.271 -42.140  1.00 57.79
ATOM   3474  CE1 PHE A 452      15.384  38.904 -40.846  1.00 57.17
ATOM   3475  CE2 PHE A 452      16.801  40.840 -41.033  1.00 58.33
ATOM   3476  CZ  PHE A 452      15.780  40.155 -40.384  1.00 57.57
ATOM   3477  N   GLY A 453      19.182  39.441 -46.482  1.00 62.68
ATOM   3478  CA  GLY A 453      20.154  39.118 -47.501  1.00 62.63
ATOM   3479  C   GLY A 453      21.067  38.064 -46.925  1.00 62.58
ATOM   3480  O   GLY A 453      20.604  37.016 -46.483  1.00 64.04
ATOM   3481  N   ALA A 454      22.363  38.350 -46.922  1.00 60.83
ATOM   3482  CA  ALA A 454      23.365  37.443 -46.380  1.00 58.48
ATOM   3483  C   ALA A 454      24.469  38.338 -45.831  1.00 57.49
ATOM   3484  O   ALA A 454      24.807  39.356 -46.436  1.00 56.21
ATOM   3485  CB  ALA A 454      23.902  36.535 -47.479  1.00 58.72
ATOM   3486  N   GLY A 455      25.033  37.975 -44.687  1.00 55.92
ATOM   3487  CA  GLY A 455      26.065  38.819 -44.117  1.00 56.75
ATOM   3488  C   GLY A 455      25.443  40.108 -43.597  1.00 57.31
ATOM   3489  O   GLY A 455      26.138  41.099 -43.358  1.00 58.01
ATOM   3490  N   ASN A 456      24.119  40.100 -43.437  1.00 55.98
ATOM   3491  CA  ASN A 456      23.407  41.260 -42.917  1.00 54.66
ATOM   3492  C   ASN A 456      23.805  41.440 -41.463  1.00 53.26
ATOM   3493  O   ASN A 456      23.942  40.461 -40.732  1.00 54.85
ATOM   3494  CB  ASN A 456      21.894  41.050 -42.992  1.00 54.12
ATOM   3495  CG  ASN A 456      21.361  41.152 -44.402  1.00 56.04
ATOM   3496  OD1 ASN A 456      20.153  41.045 -44.635  1.00 54.75
ATOM   3497  ND2 ASN A 456      22.257  41.364 -45.356  1.00 58.06
ATOM   3498  N   VAL A 457      23.995  42.685 -41.045  1.00 50.61
ATOM   3499  CA  VAL A 457      24.365  42.964 -39.666  1.00 49.36
ATOM   3500  C   VAL A 457      23.493  44.085 -39.103  1.00 50.18
ATOM   3501  O   VAL A 457      23.496  45.202 -39.614  1.00 51.48
ATOM   3502  CB  VAL A 457      25.832  43.384 -39.553  1.00 47.32
ATOM   3503  CG1 VAL A 457      26.205  43.513 -38.097  1.00 47.62
ATOM   3504  CG2 VAL A 457      26.726  42.370 -40.247  1.00 47.63
ATOM   3505  N   LEU A 458      22.754  43.786 -38.042  1.00 49.06
ATOM   3506  CA  LEU A 458      21.876  44.772 -37.428  1.00 48.48
ATOM   3507  C   LEU A 458      22.374  45.266 -36.063  1.00 46.87
ATOM   3508  O   LEU A 458      22.788  44.482 -35.214  1.00 46.76
ATOM   3509  CB  LEU A 458      20.458  44.190 -37.292  1.00 48.85
ATOM   3510  CG  LEU A 458      19.556  44.074 -38.536  1.00 50.16
ATOM   3511  CD1 LEU A 458      20.247  43.286 -39.638  1.00 48.47
ATOM   3512  CD2 LEU A 458      18.238  43.402 -38.143  1.00 49.21
ATOM   3513  N   THR A 459      22.337  46.579 -35.868  1.00 46.01
ATOM   3514  CA  THR A 459      22.758  47.188 -34.612  1.00 45.24
ATOM   3515  C   THR A 459      21.668  48.155 -34.153  1.00 43.13
ATOM   3516  O   THR A 459      20.849  48.597 -34.955  1.00 43.37
ATOM   3517  CB  THR A 459      24.116  47.941 -34.770  1.00 47.12
ATOM   3518  OG1 THR A 459      24.104  48.721 -35.971  1.00 46.07
ATOM   3519  CG2 THR A 459      25.279  46.947 -34.835  1.00 46.03
ATOM   3520  N   GLY A 460      21.649  48.471 -32.863  1.00 41.73
ATOM   3521  CA  GLY A 460      20.634  49.370 -32.344  1.00 39.09
ATOM   3522  C   GLY A 460      19.226  48.853 -32.610  1.00 39.94
ATOM   3523  O   GLY A 460      18.969  47.644 -32.565  1.00 38.96
ATOM   3524  N   THR A 461      18.311  49.776 -32.887  1.00 38.56
ATOM   3525  CA  THR A 461      16.927  49.440 -33.170  1.00 38.98
ATOM   3526  C   THR A 461      16.711  49.478 -34.682  1.00 40.17
ATOM   3527  O   THR A 461      17.022  50.478 -35.330  1.00 40.01
ATOM   3528  CB  THR A 461      15.961  50.452 -32.520  1.00 38.66
ATOM   3529  OG1 THR A 461      16.167  50.482 -31.102  1.00 39.08
ATOM   3530  CG2 THR A 461      14.525  50.070 -32.812  1.00 37.57
ATOM   3531  N   VAL A 462      16.167  48.402 -35.241  1.00 39.66
ATOM   3532  CA  VAL A 462      15.937  48.355 -36.672  1.00 41.18
ATOM   3533  C   VAL A 462      14.544  47.871 -37.043  1.00 44.08
ATOM   3534  O   VAL A 462      14.055  46.888 -36.491  1.00 45.98
ATOM   3535  CB  VAL A 462      16.961  47.437 -37.362  1.00 39.78
ATOM   3536  CG1 VAL A 462      16.711  47.424 -38.857  1.00 38.02
ATOM   3537  CG2 VAL A 462      18.379  47.908 -37.055  1.00 38.87
ATOM   3538  N   THR A 463      13.911  48.568 -37.981  1.00 45.05
ATOM   3539  CA  THR A 463      12.584  48.194 -38.459  1.00 47.91
ATOM   3540  C   THR A 463      12.666  47.952 -39.961  1.00 51.58
ATOM   3541  O   THR A 463      13.205  48.776 -40.693  1.00 54.01
ATOM   3542  CB  THR A 463      11.534  49.310 -38.222  1.00 46.67
ATOM   3543  OG1 THR A 463      11.383  49.553 -36.818  1.00 47.38
ATOM   3544  CG2 THR A 463      10.189  48.903 -38.799  1.00 43.26
ATOM   3545  N   ILE A 464      12.139  46.823 -40.417  1.00 55.13
ATOM   3546  CA  ILE A 464      12.141  46.496 -41.836  1.00 59.65
ATOM   3547  C   ILE A 464      10.697  46.246 -42.255  1.00 63.92
ATOM   3548  O   ILE A 464      10.133  45.189 -41.961  1.00 64.10
ATOM   3549  CB  ILE A 464      12.966  45.234 -42.118  1.00 59.34
ATOM   3550  CG1 ILE A 464      14.374  45.391 -41.548  1.00 59.43
ATOM   3551  CG2 ILE A 464      13.045  44.994 -43.614  1.00 60.84
ATOM   3552  CD1 ILE A 464      15.189  44.117 -41.603  1.00 58.15
ATOM   3553  N   GLU A 465      10.097  47.222 -42.933  1.00 69.24
ATOM   3554  CA  GLU A 465       8.710  47.097 -43.368  1.00 73.91
ATOM   3555  C   GLU A 465       8.494  47.304 -44.861  1.00 77.15
ATOM   3556  O   GLU A 465       9.088  48.188 -45.480  1.00 77.73
ATOM   3557  CB  GLU A 465       7.818  48.061 -42.580  1.00 73.93
ATOM   3558  CG  GLU A 465       8.116  49.535 -42.770  1.00 74.65
ATOM   3559  CD  GLU A 465       7.224  50.415 -41.903  1.00 76.08
ATOM   3560  OE1 GLU A 465       5.983  50.289 -42.001  1.00 76.27
ATOM   3561  OE2 GLU A 465       7.760  51.233 -41.123  1.00 76.62
ATOM   3562  N   ASN A 466       7.623  46.473 -45.424  1.00 80.99
ATOM   3563  CA  ASN A 466       7.294  46.512 -46.842  1.00 84.45
ATOM   3564  C   ASN A 466       6.141  47.480 -47.083  1.00 86.93
ATOM   3565  O   ASN A 466       5.026  47.251 -46.610  1.00 86.74
ATOM   3566  CB  ASN A 466       6.911  45.108 -47.315  1.00 84.45
ATOM   3567  CG  ASN A 466       6.808  45.006 -48.823  1.00 85.17
ATOM   3568  OD1 ASN A 466       5.932  45.610 -49.442  1.00 86.49
ATOM   3569  ND2 ASN A 466       7.710  44.239 -49.424  1.00 84.69
ATOM   3570  N   THR A 467       6.429  48.556 -47.818  1.00 89.84
ATOM   3571  CA  THR A 467       5.453  49.598 -48.147  1.00 92.63
ATOM   3572  C   THR A 467       4.008  49.111 -48.069  1.00 94.44
ATOM   3573  O   THR A 467       3.371  49.195 -47.018  1.00 94.81
ATOM   3574  CB  THR A 467       5.700  50.166 -49.561  1.00 92.65
ATOM   3575  OG1 THR A 467       7.060  50.602 -49.672  1.00 92.89
ATOM   3576  CG2 THR A 467       4.777  51.349 -49.827  1.00 92.88
ATOM   3577  N   ASP A 468       3.490  48.602 -49.181  1.00 96.20
ATOM   3578  CA  ASP A 468       2.123  48.111 -49.205  1.00 97.96
ATOM   3579  C   ASP A 468       2.034  46.742 -49.864  1.00 99.08
ATOM   3580  O   ASP A 468       1.127  46.476 -50.654  1.00 99.92
ATOM   3581  CB  ASP A 468       1.217  49.112 -49.926  1.00 98.21
ATOM   3582  CG  ASP A 468       1.139  50.446 -49.207  1.00 98.51
ATOM   3583  OD1 ASP A 468       0.725  50.464 -48.028  1.00 98.64
ATOM   3584  OD2 ASP A 468       1.493  51.476 -49.818  1.00 98.66
ATOM   3585  N   SER A 469       2.990  45.879 -49.531  1.00 99.49
ATOM   3586  CA  SER A 469       3.041  44.517 -50.056  1.00 99.36
ATOM   3587  C   SER A 469       3.284  44.425 -51.557  1.00 99.66
ATOM   3588  O   SER A 469       2.555  43.727 -52.267  1.00100.37
ATOM   3589  CB  SER A 469       1.751  43.762 -49.708  1.00 99.25
ATOM   3590  OG  SER A 469       1.761  42.449 -50.246  1.00 98.47
ATOM   3591  N   ALA A 470       4.302  45.127 -52.047  1.00 99.09
ATOM   3592  CA  ALA A 470       4.627  45.065 -53.468  1.00 98.00
ATOM   3593  C   ALA A 470       5.114  43.635 -53.717  1.00 97.19
ATOM   3594  O   ALA A 470       5.385  43.237 -54.852  1.00 97.60
ATOM   3595  CB  ALA A 470       5.722  46.074 -53.807  1.00 98.28
ATOM   3596  N   SER A 471       5.216  42.881 -52.620  1.00 95.51
ATOM   3597  CA  SER A 471       5.640  41.483 -52.608  1.00 92.51
ATOM   3598  C   SER A 471       7.133  41.234 -52.793  1.00 90.73
ATOM   3599  O   SER A 471       7.706  41.542 -53.840  1.00 90.25
ATOM   3600  CB  SER A 471       4.855  40.681 -53.651  1.00 92.05
ATOM   3601  OG  SER A 471       3.478  40.641 -53.320  1.00 91.14
ATOM   3602  N   ALA A 472       7.750  40.678 -51.753  1.00 87.95
ATOM   3603  CA  ALA A 472       9.165  40.326 -51.764  1.00 84.89
ATOM   3604  C   ALA A 472      10.157  41.475 -51.647  1.00 82.57
ATOM   3605  O   ALA A 472      10.685  41.947 -52.649  1.00 82.94
ATOM   3606  CB  ALA A 472       9.481  39.503 -53.017  1.00 85.71
ATOM   3607  N   PHE A 473      10.419  41.918 -50.422  1.00 80.41
ATOM   3608  CA  PHE A 473      11.391  42.985 -50.200  1.00 78.11
ATOM   3609  C   PHE A 473      12.683  42.332 -49.717  1.00 76.85
ATOM   3610  O   PHE A 473      12.877  42.110 -48.523  1.00 76.16
ATOM   3611  CB  PHE A 473      10.872  43.989 -49.162  1.00 77.99
ATOM   3612  CG  PHE A 473      11.886  45.038 -48.759  1.00 77.21
ATOM   3613  CD1 PHE A 473      12.790  45.555 -49.685  1.00 77.10
ATOM   3614  CD2 PHE A 473      11.923  45.520 -47.454  1.00 76.55
ATOM   3615  CE1 PHE A 473      13.714  46.535 -49.317  1.00 76.58
ATOM   3616  CE2 PHE A 473      12.842  46.499 -47.078  1.00 76.57
ATOM   3617  CZ  PHE A 473      13.740  47.006 -48.013  1.00 76.69
ATOM   3618  N   VAL A 474      13.557  42.012 -50.665  1.00 75.86
ATOM   3619  CA  VAL A 474      14.822  41.363 -50.358  1.00 74.90
ATOM   3620  C   VAL A 474      15.894  42.379 -50.003  1.00 75.09
ATOM   3621  O   VAL A 474      16.252  43.230 -50.815  1.00 76.33
ATOM   3622  CB  VAL A 474      15.309  40.521 -51.558  1.00 74.20
ATOM   3623  CG1 VAL A 474      16.538  39.701 -51.167  1.00 73.89
ATOM   3624  CG2 VAL A 474      14.181  39.623 -52.047  1.00 72.63
ATOM   3625  N   ILE A 475      16.406  42.286 -48.782  1.00 74.67
ATOM   3626  CA  ILE A 475      17.444  43.195 -48.320  1.00 74.35
ATOM   3627  C   ILE A 475      18.780  42.898 -48.994  1.00 75.17
ATOM   3628  O   ILE A 475      19.131  41.738 -49.219  1.00 76.19
ATOM   3629  CB  ILE A 475      17.623  43.090 -46.793  1.00 73.00
ATOM   3630  CG1 ILE A 475      16.418  43.713 -46.098  1.00 72.32
ATOM   3631  CG2 ILE A 475      18.913  43.766 -46.359  1.00 71.78
ATOM   3632  CD1 ILE A 475      16.498  43.662 -44.602  1.00 73.97
ATOM   3633  N   PRO A 476      19.538  43.949 -49.343  1.00 74.98
ATOM   3634  CA  PRO A 476      20.840  43.764 -49.989  1.00 74.32
ATOM   3635  C   PRO A 476      21.770  42.918 -49.116  1.00 73.38
ATOM   3636  O   PRO A 476      21.551  42.788 -47.911  1.00 74.08
ATOM   3637  CB  PRO A 476      21.338  45.196 -50.155  1.00 74.45
ATOM   3638  CG  PRO A 476      20.068  45.951 -50.396  1.00 74.88
ATOM   3639  CD  PRO A 476      19.154  45.371 -49.340  1.00 74.90
ATOM   3640  N   ASP A 477      22.801  42.340 -49.724  1.00 71.28
ATOM   3641  CA  ASP A 477      23.745  41.517 -48.982  1.00 69.07
ATOM   3642  C   ASP A 477      24.815  42.391 -48.357  1.00 67.79
ATOM   3643  O   ASP A 477      25.176  43.424 -48.912  1.00 68.51
ATOM   3644  CB  ASP A 477      24.388  40.481 -49.903  1.00 68.17
ATOM   3645  CG  ASP A 477      23.362  39.591 -50.573  1.00 69.02
ATOM   3646  OD1 ASP A 477      23.765  38.613 -51.239  1.00 70.00
ATOM   3647  OD2 ASP A 477      22.150  39.872 -50.436  1.00 66.82
ATOM   3648  N   GLY A 478      25.312  41.972 -47.196  1.00 67.60
ATOM   3649  CA  GLY A 478      26.341  42.732 -46.502  1.00 66.01
ATOM   3650  C   GLY A 478      25.762  43.996 -45.903  1.00 64.79
ATOM   3651  O   GLY A 478      26.470  44.787 -45.277  1.00 63.65
ATOM   3652  N   ALA A 479      24.458  44.173 -46.103  1.00 63.80
ATOM   3653  CA  ALA A 479      23.737  45.333 -45.605  1.00 63.07
ATOM   3654  C   ALA A 479      23.938  45.510 -44.105  1.00 62.57
ATOM   3655  O   ALA A 479      23.678  44.602 -43.319  1.00 62.75
ATOM   3656  CB  ALA A 479      22.252  45.195 -45.928  1.00 62.07
ATOM   3657  N   LYS A 480      24.410  46.687 -43.720  1.00 62.38
ATOM   3658  CA  LYS A 480      24.647  47.002 -42.321  1.00 61.86
ATOM   3659  C   LYS A 480      23.589  48.003 -41.841  1.00 61.43
ATOM   3660  O   LYS A 480      23.776  49.215 -41.970  1.00 60.87
ATOM   3661  CB  LYS A 480      26.043  47.596 -42.163  1.00 63.32
ATOM   3662  CG  LYS A 480      26.385  48.016 -40.751  1.00 67.24
ATOM   3663  CD  LYS A 480      26.649  46.816 -39.858  1.00 70.06
ATOM   3664  CE  LYS A 480      26.786  47.235 -38.397  1.00 71.23
ATOM   3665  NZ  LYS A 480      25.490  47.760 -37.860  1.00 71.83
ATOM   3666  N   LEU A 481      22.479  47.491 -41.305  1.00 59.43
ATOM   3667  CA  LEU A 481      21.393  48.336 -40.809  1.00 57.99
ATOM   3668  C   LEU A 481      21.630  48.742 -39.351  1.00 57.57
ATOM   3669  O   LEU A 481      21.720  47.897 -38.461  1.00 57.09
ATOM   3670  CB  LEU A 481      20.050  47.603 -40.931  1.00 56.92
ATOM   3671  CG  LEU A 481      19.661  47.059 -42.312  1.00 55.89
ATOM   3672  CD1 LEU A 481      18.316  46.358 -42.232  1.00 54.45
ATOM   3673  CD2 LEU A 481      19.601  48.191 -43.316  1.00 55.30
ATOM   3674  N   ASN A 482      21.726  50.045 -39.113  1.00 58.18
ATOM   3675  CA  ASN A 482      21.968  50.571 -37.774  1.00 57.45
ATOM   3676  C   ASN A 482      20.992  51.684 -37.412  1.00 56.05
ATOM   3677  O   ASN A 482      20.916  52.697 -38.112  1.00 54.92
ATOM   3678  CB  ASN A 482      23.401  51.096 -37.683  1.00 60.45
ATOM   3679  CG  ASN A 482      23.665  51.840 -36.392  1.00 64.67
ATOM   3680  OD1 ASN A 482      23.601  51.266 -35.297  1.00 64.69
ATOM   3681  ND2 ASN A 482      23.959  53.134 -36.510  1.00 66.96
ATOM   3682  N   ASP A 483      20.254  51.490 -36.316  1.00 54.39
ATOM   3683  CA  ASP A 483      19.268  52.468 -35.845  1.00 53.10
ATOM   3684  C   ASP A 483      18.455  53.050 -36.996  1.00 53.06
ATOM   3685  O   ASP A 483      18.216  54.255 -37.054  1.00 51.99
ATOM   3686  CB  ASP A 483      19.970  53.596 -35.101  1.00 51.94
ATOM   3687  CG  ASP A 483      20.242  53.250 -33.668  1.00 52.70
ATOM   3688  OD1 ASP A 483      21.111  53.893 -33.046  1.00 55.65
ATOM   3689  OD2 ASP A 483      19.575  52.335 -33.156  1.00 52.36
ATOM   3690  N   THR A 484      18.012  52.181 -37.895  1.00 52.75
ATOM   3691  CA  THR A 484      17.275  52.616 -39.066  1.00 54.50
ATOM   3692  C   THR A 484      15.956  51.897 -39.311  1.00 54.91
ATOM   3693  O   THR A 484      15.562  50.976 -38.592  1.00 54.52
ATOM   3694  CB  THR A 484      18.158  52.442 -40.333  1.00 53.92
ATOM   3695  OG1 THR A 484      17.436  52.849 -41.502  1.00 54.05
ATOM   3696  CG2 THR A 484      18.563  50.989 -40.489  1.00 54.72
ATOM   3697  N   THR A 485      15.276  52.360 -40.347  1.00 55.76
ATOM   3698  CA  THR A 485      14.028  51.782 -40.788  1.00 56.20
ATOM   3699  C   THR A 485      14.264  51.531 -42.264  1.00 57.23
ATOM   3700  O   THR A 485      14.243  52.462 -43.064  1.00 58.17
ATOM   3701  CB  THR A 485      12.855  52.756 -40.623  1.00 55.46
ATOM   3702  OG1 THR A 485      12.571  52.929 -39.230  1.00 55.20
ATOM   3703  CG2 THR A 485      11.621  52.221 -41.336  1.00 53.93
ATOM   3704  N   ALA A 486      14.532  50.279 -42.614  1.00 58.08
ATOM   3705  CA  ALA A 486      14.765  49.920 -44.001  1.00 59.10
ATOM   3706  C   ALA A 486      13.419  49.686 -44.666  1.00 60.73
ATOM   3707  O   ALA A 486      12.529  49.070 -44.083  1.00 60.61
ATOM   3708  CB  ALA A 486      15.623  48.667 -44.089  1.00 58.66
ATOM   3709  N   SER A 487      13.277  50.199 -45.883  1.00 63.48
ATOM   3710  CA  SER A 487      12.051  50.065 -46.660  1.00 65.72
ATOM   3711  C   SER A 487      12.340  50.277 -48.136  1.00 68.09
ATOM   3712  O   SER A 487      13.412  50.745 -48.516  1.00 68.80
ATOM   3713  CB  SER A 487      11.007  51.098 -46.218  1.00 64.82
ATOM   3714  OG  SER A 487      10.445  50.779 -44.958  1.00 65.09
ATOM   3715  N   PRO A 488      11.389  49.894 -48.993  1.00 71.02
ATOM   3716  CA  PRO A 488      11.572  50.068 -50.432  1.00 72.86
ATOM   3717  C   PRO A 488      10.700  51.214 -50.949  1.00 73.64
ATOM   3718  O   PRO A 488      11.025  51.838 -51.960  1.00 75.56
ATOM   3719  CB  PRO A 488      11.157  48.711 -50.986  1.00 73.61
ATOM   3720  CG  PRO A 488       9.971  48.387 -50.126  1.00 72.67
ATOM   3721  CD  PRO A 488      10.392  48.838 -48.721  1.00 71.91
TER    3722      PRO A 488
END



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