CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 20012010283022702

Job options:

ID        	=	 20012010283022702
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

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


A second structure was input as follows:


ATOM      1  N   SER A   7      24.979  19.508  69.674  1.00 36.62
ATOM      2  CA  SER A   7      26.357  18.962  69.515  1.00 36.81
ATOM      3  C   SER A   7      26.711  18.693  68.063  1.00 35.50
ATOM      4  O   SER A   7      26.083  17.856  67.410  1.00 34.51
ATOM      5  CB  SER A   7      26.508  17.664  70.291  1.00 38.73
ATOM      6  OG  SER A   7      27.801  17.134  70.074  1.00 41.05
ATOM      7  N   LEU A   8      27.741  19.377  67.571  1.00 35.36
ATOM      8  CA  LEU A   8      28.174  19.246  66.181  1.00 34.44
ATOM      9  C   LEU A   8      28.990  18.013  65.851  1.00 34.19
ATOM     10  O   LEU A   8      29.780  17.533  66.662  1.00 34.30
ATOM     11  CB  LEU A   8      28.981  20.481  65.774  1.00 33.11
ATOM     12  CG  LEU A   8      28.265  21.777  65.357  1.00 34.77
ATOM     13  CD1 LEU A   8      26.808  21.748  65.733  1.00 33.47
ATOM     14  CD2 LEU A   8      28.973  22.940  66.020  1.00 33.97
ATOM     15  N   SER A   9      28.778  17.508  64.643  1.00 33.04
ATOM     16  CA  SER A   9      29.522  16.367  64.159  1.00 32.60
ATOM     17  C   SER A   9      30.941  16.876  64.006  1.00 31.48
ATOM     18  O   SER A   9      31.176  18.091  63.982  1.00 32.44
ATOM     19  CB  SER A   9      29.033  15.945  62.786  1.00 33.59
ATOM     20  OG  SER A   9      29.348  16.969  61.852  1.00 37.02
ATOM     21  N   ALA A  10      31.878  15.945  63.890  1.00 28.70
ATOM     22  CA  ALA A  10      33.280  16.278  63.730  1.00 27.19
ATOM     23  C   ALA A  10      33.495  17.236  62.561  1.00 24.20
ATOM     24  O   ALA A  10      34.243  18.204  62.671  1.00 23.53
ATOM     25  CB  ALA A  10      34.079  15.000  63.504  1.00 28.47
ATOM     26  N   ALA A  11      32.843  16.935  61.443  1.00 23.69
ATOM     27  CA  ALA A  11      32.951  17.730  60.226  1.00 22.48
ATOM     28  C   ALA A  11      32.541  19.186  60.463  1.00 22.75
ATOM     29  O   ALA A  11      33.278  20.116  60.135  1.00 24.43
ATOM     30  CB  ALA A  11      32.093  17.117  59.150  1.00 20.57
ATOM     31  N   ALA A  12      31.366  19.375  61.047  1.00 22.12
ATOM     32  CA  ALA A  12      30.859  20.709  61.323  1.00 21.96
ATOM     33  C   ALA A  12      31.827  21.436  62.244  1.00 21.97
ATOM     34  O   ALA A  12      32.158  22.595  62.023  1.00 19.10
ATOM     35  CB  ALA A  12      29.482  20.612  61.962  1.00 21.45
ATOM     36  N   GLN A  13      32.293  20.722  63.262  1.00 22.94
ATOM     37  CA  GLN A  13      33.225  21.258  64.246  1.00 23.72
ATOM     38  C   GLN A  13      34.554  21.663  63.578  1.00 23.16
ATOM     39  O   GLN A  13      35.245  22.584  64.038  1.00 21.75
ATOM     40  CB  GLN A  13      33.449  20.199  65.339  1.00 26.78
ATOM     41  CG  GLN A  13      33.697  20.768  66.731  1.00 33.61
ATOM     42  CD  GLN A  13      33.260  19.838  67.877  1.00 36.19
ATOM     43  OE1 GLN A  13      33.368  20.209  69.049  1.00 38.03
ATOM     44  NE2 GLN A  13      32.764  18.641  67.545  1.00 36.42
ATOM     45  N   ALA A  14      34.900  20.980  62.488  1.00 20.13
ATOM     46  CA  ALA A  14      36.126  21.278  61.746  1.00 19.62
ATOM     47  C   ALA A  14      35.962  22.587  60.958  1.00 18.35
ATOM     48  O   ALA A  14      36.914  23.358  60.792  1.00 17.44
ATOM     49  CB  ALA A  14      36.452  20.128  60.789  1.00 19.65
ATOM     50  N   CYS A  15      34.751  22.820  60.466  1.00 17.73
ATOM     51  CA  CYS A  15      34.435  24.042  59.733  1.00 17.99
ATOM     52  C   CYS A  15      34.503  25.217  60.698  1.00 17.76
ATOM     53  O   CYS A  15      35.086  26.257  60.395  1.00 19.34
ATOM     54  CB  CYS A  15      33.032  23.948  59.137  1.00 18.04
ATOM     55  SG  CYS A  15      32.863  22.750  57.795  1.00 19.47
ATOM     56  N   VAL A  16      33.892  25.050  61.864  1.00 17.81
ATOM     57  CA  VAL A  16      33.909  26.087  62.885  1.00 19.03
ATOM     58  C   VAL A  16      35.356  26.429  63.227  1.00 20.24
ATOM     59  O   VAL A  16      35.742  27.595  63.266  1.00 21.14
ATOM     60  CB  VAL A  16      33.203  25.603  64.166  1.00 19.27
ATOM     61  CG1 VAL A  16      33.592  26.482  65.350  1.00 16.54
ATOM     62  CG2 VAL A  16      31.699  25.610  63.947  1.00 19.24
ATOM     63  N   LYS A  17      36.159  25.398  63.464  1.00 22.04
ATOM     64  CA  LYS A  17      37.558  25.603  63.812  1.00 21.92
ATOM     65  C   LYS A  17      38.295  26.324  62.689  1.00 21.56
ATOM     66  O   LYS A  17      39.076  27.252  62.938  1.00 22.47
ATOM     67  CB  LYS A  17      38.240  24.267  64.095  1.00 24.59
ATOM     68  CG  LYS A  17      39.695  24.436  64.507  1.00 30.57
ATOM     69  CD  LYS A  17      40.392  23.104  64.708  1.00 32.33
ATOM     70  CE  LYS A  17      41.811  23.318  65.222  1.00 36.11
ATOM     71  NZ  LYS A  17      42.619  24.215  64.343  1.00 36.99
ATOM     72  N   LYS A  18      38.052  25.904  61.451  1.00 19.33
ATOM     73  CA  LYS A  18      38.707  26.549  60.323  1.00 17.24
ATOM     74  C   LYS A  18      38.295  28.024  60.239  1.00 18.21
ATOM     75  O   LYS A  18      39.125  28.892  59.984  1.00 16.22
ATOM     76  CB  LYS A  18      38.347  25.846  59.009  1.00 17.79
ATOM     77  CG  LYS A  18      39.226  26.302  57.838  1.00 17.68
ATOM     78  CD  LYS A  18      38.958  25.568  56.522  1.00 16.01
ATOM     79  CE  LYS A  18      39.974  26.053  55.478  1.00 17.72
ATOM     80  NZ  LYS A  18      39.783  25.494  54.115  1.00 18.21
ATOM     81  N   MET A  19      37.010  28.300  60.453  1.00 17.59
ATOM     82  CA  MET A  19      36.512  29.668  60.387  1.00 18.52
ATOM     83  C   MET A  19      37.020  30.526  61.538  1.00 18.69
ATOM     84  O   MET A  19      37.300  31.706  61.352  1.00 17.26
ATOM     85  CB  MET A  19      34.980  29.664  60.345  1.00 19.72
ATOM     86  CG  MET A  19      34.444  29.067  59.045  1.00 19.14
ATOM     87  SD  MET A  19      32.547  28.683  59.051  1.00 25.09
ATOM     88  CE  MET A  19      31.865  30.334  58.375  1.00 12.67
ATOM     89  N   ARG A  20      37.139  29.940  62.725  1.00 20.39
ATOM     90  CA  ARG A  20      37.652  30.687  63.866  1.00 22.06
ATOM     91  C   ARG A  20      39.101  31.044  63.573  1.00 22.36
ATOM     92  O   ARG A  20      39.500  32.203  63.685  1.00 21.27
ATOM     93  CB  ARG A  20      37.585  29.856  65.142  1.00 21.73
ATOM     94  CG  ARG A  20      36.195  29.725  65.713  1.00 24.17
ATOM     95  CD  ARG A  20      35.907  30.797  66.742  1.00 25.99
ATOM     96  NE  ARG A  20      34.510  30.766  67.182  1.00 28.53
ATOM     97  CZ  ARG A  20      33.904  29.711  67.719  1.00 27.42
ATOM     98  NH1 ARG A  20      34.566  28.578  67.895  1.00 30.87
ATOM     99  NH2 ARG A  20      32.629  29.780  68.073  1.00 27.01
ATOM    100  N   ASP A  21      39.887  30.048  63.178  1.00 24.06
ATOM    101  CA  ASP A  21      41.296  30.288  62.874  1.00 25.71
ATOM    102  C   ASP A  21      41.459  31.405  61.850  1.00 25.45
ATOM    103  O   ASP A  21      42.364  32.224  61.952  1.00 23.72
ATOM    104  CB  ASP A  21      41.964  29.026  62.325  1.00 29.31
ATOM    105  CG  ASP A  21      42.044  27.905  63.345  1.00 32.80
ATOM    106  OD1 ASP A  21      42.139  28.195  64.558  1.00 33.18
ATOM    107  OD2 ASP A  21      42.040  26.724  62.923  1.00 35.98
ATOM    108  N   ALA A  22      40.572  31.441  60.863  1.00 24.10
ATOM    109  CA  ALA A  22      40.660  32.455  59.832  1.00 23.26
ATOM    110  C   ALA A  22      39.993  33.759  60.249  1.00 24.15
ATOM    111  O   ALA A  22      39.814  34.664  59.428  1.00 24.85
ATOM    112  CB  ALA A  22      40.056  31.938  58.548  1.00 24.12
ATOM    113  N   LYS A  23      39.639  33.853  61.525  1.00 23.45
ATOM    114  CA  LYS A  23      39.012  35.056  62.073  1.00 25.20
ATOM    115  C   LYS A  23      37.673  35.404  61.441  1.00 23.98
ATOM    116  O   LYS A  23      37.327  36.580  61.315  1.00 22.84
ATOM    117  CB  LYS A  23      39.935  36.280  61.922  1.00 26.95
ATOM    118  CG  LYS A  23      41.362  36.085  62.407  1.00 30.58
ATOM    119  CD  LYS A  23      41.428  35.875  63.913  1.00 33.56
ATOM    120  CE  LYS A  23      42.878  35.913  64.401  1.00 36.63
ATOM    121  NZ  LYS A  23      43.565  37.203  64.053  1.00 36.26
ATOM    122  N   VAL A  24      36.915  34.398  61.033  1.00 23.44
ATOM    123  CA  VAL A  24      35.628  34.682  60.433  1.00 21.75
ATOM    124  C   VAL A  24      34.694  35.175  61.524  1.00 23.46
ATOM    125  O   VAL A  24      34.725  34.698  62.661  1.00 22.98
ATOM    126  CB  VAL A  24      35.034  33.449  59.757  1.00 19.81
ATOM    127  CG1 VAL A  24      33.615  33.725  59.336  1.00 15.35
ATOM    128  CG2 VAL A  24      35.863  33.105  58.538  1.00 21.59
ATOM    129  N   ASN A  25      33.890  36.163  61.164  1.00 23.46
ATOM    130  CA  ASN A  25      32.934  36.779  62.060  1.00 24.77
ATOM    131  C   ASN A  25      32.029  35.704  62.678  1.00 22.75
ATOM    132  O   ASN A  25      31.584  34.788  61.983  1.00 21.17
ATOM    133  CB  ASN A  25      32.127  37.803  61.248  1.00 27.56
ATOM    134  CG  ASN A  25      31.134  38.538  62.076  1.00 30.60
ATOM    135  OD1 ASN A  25      30.089  38.001  62.425  1.00 34.30
ATOM    136  ND2 ASN A  25      31.450  39.783  62.410  1.00 33.64
ATOM    137  N   GLU A  26      31.765  35.816  63.980  1.00 21.07
ATOM    138  CA  GLU A  26      30.931  34.835  64.682  1.00 20.83
ATOM    139  C   GLU A  26      29.543  34.649  64.103  1.00 18.94
ATOM    140  O   GLU A  26      29.036  33.536  64.069  1.00 19.64
ATOM    141  CB  GLU A  26      30.791  35.192  66.166  1.00 20.84
ATOM    142  CG  GLU A  26      31.958  34.728  67.027  1.00 21.51
ATOM    143  CD  GLU A  26      32.286  33.259  66.812  1.00 24.44
ATOM    144  OE1 GLU A  26      31.372  32.399  66.922  1.00 25.63
ATOM    145  OE2 GLU A  26      33.466  32.967  66.532  1.00 24.41
ATOM    146  N   ALA A  27      28.920  35.746  63.680  1.00 17.65
ATOM    147  CA  ALA A  27      27.578  35.698  63.098  1.00 16.27
ATOM    148  C   ALA A  27      27.576  34.861  61.835  1.00 13.75
ATOM    149  O   ALA A  27      26.645  34.111  61.581  1.00 13.82
ATOM    150  CB  ALA A  27      27.086  37.113  62.777  1.00 15.15
ATOM    151  N   CYS A  28      28.621  35.005  61.037  1.00 14.40
ATOM    152  CA  CYS A  28      28.727  34.254  59.797  1.00 16.73
ATOM    153  C   CYS A  28      28.904  32.770  60.099  1.00 16.84
ATOM    154  O   CYS A  28      28.342  31.918  59.406  1.00 16.84
ATOM    155  CB  CYS A  28      29.900  34.765  58.959  1.00 18.11
ATOM    156  SG  CYS A  28      30.248  33.724  57.526  1.00 18.28
ATOM    157  N   ILE A  29      29.663  32.470  61.144  1.00 16.62
ATOM    158  CA  ILE A  29      29.894  31.077  61.531  1.00 18.05
ATOM    159  C   ILE A  29      28.595  30.447  62.018  1.00 18.61
ATOM    160  O   ILE A  29      28.236  29.338  61.595  1.00 15.56
ATOM    161  CB  ILE A  29      30.956  30.965  62.658  1.00 18.26
ATOM    162  CG1 ILE A  29      32.309  31.481  62.150  1.00 19.54
ATOM    163  CG2 ILE A  29      31.065  29.511  63.135  1.00 19.66
ATOM    164  CD1 ILE A  29      33.422  31.537  63.222  1.00 18.39
ATOM    165  N   ARG A  30      27.885  31.152  62.903  1.00 18.18
ATOM    166  CA  ARG A  30      26.625  30.627  63.411  1.00 17.93
ATOM    167  C   ARG A  30      25.671  30.382  62.252  1.00 18.13
ATOM    168  O   ARG A  30      24.983  29.375  62.216  1.00 20.11
ATOM    169  CB  ARG A  30      25.974  31.603  64.410  1.00 20.92
ATOM    170  CG  ARG A  30      26.646  31.666  65.794  1.00 23.40
ATOM    171  CD  ARG A  30      25.740  32.357  66.838  1.00 24.56
ATOM    172  NE  ARG A  30      25.415  33.730  66.462  1.00 24.17
ATOM    173  CZ  ARG A  30      26.197  34.777  66.709  1.00 25.86
ATOM    174  NH1 ARG A  30      27.354  34.619  67.347  1.00 24.09
ATOM    175  NH2 ARG A  30      25.836  35.980  66.290  1.00 27.33
ATOM    176  N   THR A  31      25.631  31.306  61.297  1.00 17.42
ATOM    177  CA  THR A  31      24.734  31.170  60.148  1.00 18.05
ATOM    178  C   THR A  31      25.140  30.003  59.250  1.00 17.04
ATOM    179  O   THR A  31      24.298  29.191  58.850  1.00 16.97
ATOM    180  CB  THR A  31      24.711  32.471  59.324  1.00 18.29
ATOM    181  OG1 THR A  31      24.201  33.528  60.143  1.00 20.38
ATOM    182  CG2 THR A  31      23.848  32.326  58.087  1.00 16.58
ATOM    183  N   PHE A  32      26.427  29.917  58.940  1.00 16.42
ATOM    184  CA  PHE A  32      26.922  28.835  58.095  1.00 16.81
ATOM    185  C   PHE A  32      26.700  27.467  58.754  1.00 16.73
ATOM    186  O   PHE A  32      26.276  26.521  58.107  1.00 17.60
ATOM    187  CB  PHE A  32      28.408  29.019  57.812  1.00 14.80
ATOM    188  CG  PHE A  32      29.043  27.845  57.099  1.00 12.88
ATOM    189  CD1 PHE A  32      29.003  27.750  55.708  1.00 12.55
ATOM    190  CD2 PHE A  32      29.674  26.827  57.829  1.00 12.49
ATOM    191  CE1 PHE A  32      29.580  26.652  55.043  1.00 11.31
ATOM    192  CE2 PHE A  32      30.255  25.732  57.188  1.00  8.77
ATOM    193  CZ  PHE A  32      30.203  25.648  55.779  1.00 10.27
ATOM    194  N   ILE A  33      26.982  27.373  60.043  1.00 16.71
ATOM    195  CA  ILE A  33      26.824  26.113  60.755  1.00 17.88
ATOM    196  C   ILE A  33      25.390  25.583  60.744  1.00 18.45
ATOM    197  O   ILE A  33      25.167  24.390  60.552  1.00 16.70
ATOM    198  CB  ILE A  33      27.313  26.266  62.194  1.00 17.21
ATOM    199  CG1 ILE A  33      28.842  26.385  62.197  1.00 18.98
ATOM    200  CG2 ILE A  33      26.803  25.126  63.048  1.00 23.48
ATOM    201  CD1 ILE A  33      29.583  25.213  61.556  1.00 21.15
ATOM    202  N   ALA A  34      24.420  26.468  60.956  1.00 17.92
ATOM    203  CA  ALA A  34      23.016  26.062  60.951  1.00 18.54
ATOM    204  C   ALA A  34      22.667  25.511  59.575  1.00 17.62
ATOM    205  O   ALA A  34      21.812  24.629  59.437  1.00 19.41
ATOM    206  CB  ALA A  34      22.107  27.255  61.304  1.00 17.32
ATOM    207  N   GLN A  35      23.332  26.029  58.550  1.00 17.74
ATOM    208  CA  GLN A  35      23.101  25.549  57.191  1.00 16.53
ATOM    209  C   GLN A  35      23.744  24.160  57.038  1.00 16.92
ATOM    210  O   GLN A  35      23.180  23.271  56.405  1.00 18.40
ATOM    211  CB  GLN A  35      23.717  26.517  56.180  1.00 15.85
ATOM    212  CG  GLN A  35      23.025  27.874  56.078  1.00 15.65
ATOM    213  CD  GLN A  35      23.787  28.845  55.179  1.00 17.68
ATOM    214  OE1 GLN A  35      23.323  29.952  54.899  1.00 20.89
ATOM    215  NE2 GLN A  35      24.968  28.434  54.731  1.00 16.83
ATOM    216  N   HIS A  36      24.933  24.004  57.611  1.00 16.68
ATOM    217  CA  HIS A  36      25.684  22.751  57.583  1.00 19.43
ATOM    218  C   HIS A  36      24.878  21.659  58.299  1.00 20.51
ATOM    219  O   HIS A  36      24.873  20.504  57.878  1.00 21.88
ATOM    220  CB  HIS A  36      27.036  22.956  58.274  1.00 17.18
ATOM    221  CG  HIS A  36      28.036  21.878  58.003  1.00 17.75
ATOM    222  ND1 HIS A  36      27.945  20.616  58.551  1.00 17.25
ATOM    223  CD2 HIS A  36      29.174  21.888  57.270  1.00 17.74
ATOM    224  CE1 HIS A  36      28.986  19.898  58.173  1.00 15.59
ATOM    225  NE2 HIS A  36      29.747  20.645  57.395  1.00 15.66
ATOM    226  N   VAL A  37      24.193  22.029  59.380  1.00 22.89
ATOM    227  CA  VAL A  37      23.378  21.076  60.117  1.00 23.26
ATOM    228  C   VAL A  37      22.260  20.578  59.202  1.00 25.87
ATOM    229  O   VAL A  37      21.957  19.382  59.172  1.00 26.05
ATOM    230  CB  VAL A  37      22.751  21.719  61.367  1.00 24.44
ATOM    231  CG1 VAL A  37      21.795  20.732  62.037  1.00 22.55
ATOM    232  CG2 VAL A  37      23.846  22.138  62.345  1.00 24.32
ATOM    233  N   MET A  38      21.654  21.501  58.457  1.00 26.72
ATOM    234  CA  MET A  38      20.584  21.154  57.532  1.00 29.05
ATOM    235  C   MET A  38      21.109  20.169  56.495  1.00 27.96
ATOM    236  O   MET A  38      20.579  19.074  56.347  1.00 28.27
ATOM    237  CB  MET A  38      20.050  22.400  56.816  1.00 32.24
ATOM    238  CG  MET A  38      19.347  23.426  57.716  1.00 39.81
ATOM    239  SD  MET A  38      17.692  22.790  58.531  1.00 50.98
ATOM    240  CE  MET A  38      18.360  22.161  60.235  1.00 47.14
ATOM    241  N   VAL A  39      22.157  20.565  55.784  1.00 26.36
ATOM    242  CA  VAL A  39      22.739  19.718  54.761  1.00 25.80
ATOM    243  C   VAL A  39      23.043  18.304  55.269  1.00 24.80
ATOM    244  O   VAL A  39      22.654  17.326  54.644  1.00 24.54
ATOM    245  CB  VAL A  39      24.016  20.368  54.180  1.00 25.93
ATOM    246  CG1 VAL A  39      24.773  19.370  53.286  1.00 24.87
ATOM    247  CG2 VAL A  39      23.622  21.589  53.355  1.00 25.49
ATOM    248  N   SER A  40      23.729  18.204  56.399  1.00 26.26
ATOM    249  CA  SER A  40      24.060  16.905  56.986  1.00 29.32
ATOM    250  C   SER A  40      22.820  16.034  57.222  1.00 31.57
ATOM    251  O   SER A  40      22.919  14.803  57.276  1.00 33.39
ATOM    252  CB  SER A  40      24.797  17.102  58.306  1.00 28.70
ATOM    253  OG  SER A  40      24.043  17.904  59.194  1.00 29.92
ATOM    254  N   LYS A  41      21.660  16.670  57.360  1.00 32.20
ATOM    255  CA  LYS A  41      20.417  15.940  57.580  1.00 33.68
ATOM    256  C   LYS A  41      19.656  15.596  56.307  1.00 33.30
ATOM    257  O   LYS A  41      18.566  15.042  56.376  1.00 32.99
ATOM    258  CB  LYS A  41      19.497  16.706  58.530  1.00 33.05
ATOM    259  CG  LYS A  41      19.872  16.493  59.985  1.00 36.22
ATOM    260  CD  LYS A  41      18.799  16.999  60.944  1.00 39.26
ATOM    261  CE  LYS A  41      18.865  18.509  61.128  1.00 42.04
ATOM    262  NZ  LYS A  41      18.013  18.972  62.263  1.00 42.68
ATOM    263  N   GLY A  42      20.226  15.917  55.149  1.00 32.75
ATOM    264  CA  GLY A  42      19.551  15.600  53.899  1.00 32.75
ATOM    265  C   GLY A  42      19.019  16.779  53.098  1.00 31.99
ATOM    266  O   GLY A  42      18.652  16.618  51.937  1.00 30.24
ATOM    267  N   GLU A  43      18.964  17.958  53.709  1.00 32.12
ATOM    268  CA  GLU A  43      18.480  19.151  53.009  1.00 33.21
ATOM    269  C   GLU A  43      19.323  19.401  51.762  1.00 34.01
ATOM    270  O   GLU A  43      20.538  19.588  51.870  1.00 34.19
ATOM    271  CB  GLU A  43      18.580  20.372  53.919  1.00 34.02
ATOM    272  CG  GLU A  43      18.102  21.668  53.285  1.00 35.37
ATOM    273  CD  GLU A  43      16.644  21.605  52.884  1.00 36.80
ATOM    274  OE1 GLU A  43      16.354  21.428  51.679  1.00 34.77
ATOM    275  OE2 GLU A  43      15.783  21.715  53.785  1.00 38.04
ATOM    276  N   THR A  44      18.684  19.412  50.590  1.00 34.34
ATOM    277  CA  THR A  44      19.383  19.648  49.319  1.00 34.55
ATOM    278  C   THR A  44      19.177  21.086  48.865  1.00 34.65
ATOM    279  O   THR A  44      19.927  21.602  48.029  1.00 36.54
ATOM    280  CB  THR A  44      18.858  18.737  48.191  1.00 35.15
ATOM    281  OG1 THR A  44      17.479  19.040  47.947  1.00 33.88
ATOM    282  CG2 THR A  44      18.983  17.260  48.580  1.00 35.93
ATOM    283  N   GLY A  45      18.148  21.718  49.417  1.00 33.26
ATOM    284  CA  GLY A  45      17.840  23.092  49.077  1.00 33.14
ATOM    285  C   GLY A  45      16.666  23.181  48.125  1.00 32.96
ATOM    286  O   GLY A  45      16.043  24.240  47.995  1.00 32.85
ATOM    287  N   SER A  46      16.354  22.059  47.477  1.00 31.34
ATOM    288  CA  SER A  46      15.269  21.995  46.505  1.00 30.55
ATOM    289  C   SER A  46      13.886  22.240  47.096  1.00 28.44
ATOM    290  O   SER A  46      13.582  21.846  48.222  1.00 28.60
ATOM    291  CB  SER A  46      15.289  20.636  45.779  1.00 31.72
ATOM    292  OG  SER A  46      14.270  19.767  46.254  1.00 32.39
ATOM    293  N   ILE A  47      13.058  22.921  46.319  1.00 26.73
ATOM    294  CA  ILE A  47      11.684  23.232  46.701  1.00 25.92
ATOM    295  C   ILE A  47      10.833  22.624  45.576  1.00 26.08
ATOM    296  O   ILE A  47      10.744  23.181  44.476  1.00 23.97
ATOM    297  CB  ILE A  47      11.468  24.774  46.782  1.00 26.02
ATOM    298  CG1 ILE A  47      12.334  25.363  47.913  1.00 25.44
ATOM    299  CG2 ILE A  47       9.978  25.087  46.979  1.00 24.49
ATOM    300  CD1 ILE A  47      12.374  26.897  47.952  1.00 25.39
ATOM    301  N   PRO A  48      10.230  21.451  45.830  1.00 25.76
ATOM    302  CA  PRO A  48       9.413  20.807  44.799  1.00 26.27
ATOM    303  C   PRO A  48       8.120  21.524  44.469  1.00 26.49
ATOM    304  O   PRO A  48       7.530  22.188  45.312  1.00 26.47
ATOM    305  CB  PRO A  48       9.175  19.410  45.368  1.00 26.66
ATOM    306  CG  PRO A  48       9.126  19.675  46.883  1.00 25.62
ATOM    307  CD  PRO A  48      10.293  20.630  47.058  1.00 25.05
ATOM    308  N   ASP A  49       7.697  21.375  43.222  1.00 28.70
ATOM    309  CA  ASP A  49       6.468  21.971  42.722  1.00 31.50
ATOM    310  C   ASP A  49       5.248  21.618  43.575  1.00 30.78
ATOM    311  O   ASP A  49       4.345  22.440  43.745  1.00 29.86
ATOM    312  CB  ASP A  49       6.235  21.498  41.284  1.00 34.66
ATOM    313  CG  ASP A  49       6.145  22.639  40.302  1.00 38.83
ATOM    314  OD1 ASP A  49       5.009  23.105  40.063  1.00 42.26
ATOM    315  OD2 ASP A  49       7.204  23.074  39.783  1.00 40.35
ATOM    316  N   SER A  50       5.229  20.402  44.115  1.00 30.96
ATOM    317  CA  SER A  50       4.102  19.941  44.924  1.00 31.51
ATOM    318  C   SER A  50       4.004  20.695  46.245  1.00 30.69
ATOM    319  O   SER A  50       2.950  20.707  46.888  1.00 31.99
ATOM    320  CB  SER A  50       4.233  18.435  45.211  1.00 32.14
ATOM    321  OG  SER A  50       5.239  18.173  46.178  1.00 30.30
ATOM    322  N   ALA A  51       5.101  21.333  46.637  1.00 28.79
ATOM    323  CA  ALA A  51       5.139  22.057  47.898  1.00 27.11
ATOM    324  C   ALA A  51       4.792  23.540  47.818  1.00 26.73
ATOM    325  O   ALA A  51       4.754  24.217  48.847  1.00 27.28
ATOM    326  CB  ALA A  51       6.510  21.880  48.540  1.00 26.19
ATOM    327  N   ILE A  52       4.539  24.051  46.617  1.00 26.08
ATOM    328  CA  ILE A  52       4.218  25.468  46.465  1.00 26.09
ATOM    329  C   ILE A  52       3.027  25.736  45.541  1.00 28.02
ATOM    330  O   ILE A  52       2.571  24.848  44.834  1.00 27.59
ATOM    331  CB  ILE A  52       5.445  26.263  45.940  1.00 24.24
ATOM    332  CG1 ILE A  52       5.879  25.722  44.572  1.00 22.06
ATOM    333  CG2 ILE A  52       6.585  26.173  46.949  1.00 21.41
ATOM    334  CD1 ILE A  52       6.963  26.560  43.903  1.00 19.61
ATOM    335  N   MET A  53       2.534  26.972  45.554  1.00 30.66
ATOM    336  CA  MET A  53       1.392  27.354  44.732  1.00 34.27
ATOM    337  C   MET A  53       1.604  28.756  44.142  1.00 33.27
ATOM    338  O   MET A  53       2.358  29.556  44.685  1.00 31.92
ATOM    339  CB  MET A  53       0.117  27.314  45.581  1.00 40.32
ATOM    340  CG  MET A  53      -1.109  26.733  44.861  1.00 49.48
ATOM    341  SD  MET A  53      -1.094  24.794  44.546  1.00 61.17
ATOM    342  CE  MET A  53      -0.038  24.700  42.931  1.00 56.43
ATOM    343  N   PRO A  54       0.941  29.069  43.017  1.00 32.80
ATOM    344  CA  PRO A  54       1.111  30.393  42.406  1.00 32.08
ATOM    345  C   PRO A  54       0.484  31.524  43.212  1.00 31.26
ATOM    346  O   PRO A  54      -0.399  31.300  44.044  1.00 30.42
ATOM    347  CB  PRO A  54       0.439  30.248  41.035  1.00 32.79
ATOM    348  CG  PRO A  54       0.356  28.746  40.819  1.00 35.20
ATOM    349  CD  PRO A  54       0.070  28.219  42.190  1.00 32.69
ATOM    350  N   VAL A  55       0.958  32.739  42.953  1.00 30.59
ATOM    351  CA  VAL A  55       0.457  33.943  43.609  1.00 29.47
ATOM    352  C   VAL A  55      -0.439  34.600  42.581  1.00 30.15
ATOM    353  O   VAL A  55       0.026  34.928  41.486  1.00 30.14
ATOM    354  CB  VAL A  55       1.603  34.896  43.948  1.00 28.19
ATOM    355  CG1 VAL A  55       1.050  36.237  44.397  1.00 25.57
ATOM    356  CG2 VAL A  55       2.483  34.270  45.026  1.00 27.03
ATOM    357  N   ASP A  56      -1.711  34.795  42.918  1.00 30.97
ATOM    358  CA  ASP A  56      -2.652  35.381  41.958  1.00 32.32
ATOM    359  C   ASP A  56      -3.070  36.809  42.209  1.00 32.62
ATOM    360  O   ASP A  56      -3.800  37.393  41.401  1.00 36.14
ATOM    361  CB  ASP A  56      -3.933  34.548  41.873  1.00 33.48
ATOM    362  CG  ASP A  56      -3.677  33.133  41.430  1.00 35.68
ATOM    363  OD1 ASP A  56      -2.889  32.948  40.480  1.00 36.92
ATOM    364  OD2 ASP A  56      -4.273  32.207  42.027  1.00 37.61
ATOM    365  N   SER A  57      -2.629  37.394  43.309  1.00 30.19
ATOM    366  CA  SER A  57      -3.068  38.740  43.571  1.00 27.68
ATOM    367  C   SER A  57      -2.086  39.554  44.391  1.00 26.25
ATOM    368  O   SER A  57      -1.801  39.213  45.542  1.00 25.36
ATOM    369  CB  SER A  57      -4.427  38.671  44.275  1.00 28.75
ATOM    370  OG  SER A  57      -4.954  39.956  44.520  1.00 31.58
ATOM    371  N   LEU A  58      -1.575  40.628  43.790  1.00 21.43
ATOM    372  CA  LEU A  58      -0.656  41.530  44.466  1.00 19.86
ATOM    373  C   LEU A  58      -1.038  42.965  44.132  1.00 19.96
ATOM    374  O   LEU A  58      -1.589  43.230  43.062  1.00 18.80
ATOM    375  CB  LEU A  58       0.787  41.288  44.009  1.00 18.18
ATOM    376  CG  LEU A  58       1.391  39.918  44.339  1.00 18.36
ATOM    377  CD1 LEU A  58       2.791  39.813  43.758  1.00 15.03
ATOM    378  CD2 LEU A  58       1.406  39.722  45.840  1.00 12.29
ATOM    379  N   ASP A  59      -0.760  43.894  45.041  1.00 20.05
ATOM    380  CA  ASP A  59      -1.045  45.297  44.750  1.00 20.20
ATOM    381  C   ASP A  59      -0.030  45.685  43.688  1.00 18.99
ATOM    382  O   ASP A  59       0.987  45.013  43.526  1.00 19.12
ATOM    383  CB  ASP A  59      -0.861  46.195  45.983  1.00 21.79
ATOM    384  CG  ASP A  59      -2.003  46.074  46.977  1.00 23.38
ATOM    385  OD1 ASP A  59      -3.131  45.779  46.535  1.00 28.14
ATOM    386  OD2 ASP A  59      -1.786  46.287  48.194  1.00 22.88
ATOM    387  N   ALA A  60      -0.301  46.766  42.971  1.00 19.08
ATOM    388  CA  ALA A  60       0.598  47.218  41.926  1.00 19.52
ATOM    389  C   ALA A  60       1.127  48.608  42.232  1.00 20.32
ATOM    390  O   ALA A  60       0.388  49.492  42.676  1.00 20.92
ATOM    391  CB  ALA A  60      -0.126  47.206  40.571  1.00 19.30
ATOM    392  N   LEU A  61       2.418  48.802  42.004  1.00 20.72
ATOM    393  CA  LEU A  61       3.021  50.095  42.269  1.00 22.10
ATOM    394  C   LEU A  61       2.342  51.186  41.429  1.00 23.98
ATOM    395  O   LEU A  61       2.274  52.338  41.852  1.00 23.24
ATOM    396  CB  LEU A  61       4.523  50.025  41.988  1.00 20.20
ATOM    397  CG  LEU A  61       5.473  51.172  42.360  1.00 21.42
ATOM    398  CD1 LEU A  61       5.774  51.973  41.131  1.00 23.29
ATOM    399  CD2 LEU A  61       4.905  52.050  43.445  1.00 20.00
ATOM    400  N   ASP A  62       1.819  50.813  40.259  1.00 25.90
ATOM    401  CA  ASP A  62       1.142  51.753  39.349  1.00 29.14
ATOM    402  C   ASP A  62      -0.114  52.390  39.935  1.00 27.71
ATOM    403  O   ASP A  62      -0.550  53.446  39.479  1.00 28.01
ATOM    404  CB  ASP A  62       0.751  51.049  38.041  1.00 33.84
ATOM    405  CG  ASP A  62       1.935  50.798  37.140  1.00 38.11
ATOM    406  OD1 ASP A  62       1.835  49.923  36.253  1.00 41.30
ATOM    407  OD2 ASP A  62       2.965  51.481  37.310  1.00 41.86
ATOM    408  N   SER A  63      -0.696  51.736  40.932  1.00 26.55
ATOM    409  CA  SER A  63      -1.904  52.231  41.580  1.00 26.95
ATOM    410  C   SER A  63      -1.585  53.202  42.713  1.00 26.96
ATOM    411  O   SER A  63      -2.479  53.869  43.243  1.00 28.03
ATOM    412  CB  SER A  63      -2.698  51.055  42.156  1.00 27.80
ATOM    413  OG  SER A  63      -3.097  50.154  41.149  1.00 27.88
ATOM    414  N   LEU A  64      -0.318  53.273  43.103  1.00 25.11
ATOM    415  CA  LEU A  64       0.070  54.152  44.196  1.00 23.39
ATOM    416  C   LEU A  64       0.316  55.570  43.716  1.00 22.72
ATOM    417  O   LEU A  64       0.678  55.792  42.562  1.00 23.06
ATOM    418  CB  LEU A  64       1.320  53.599  44.887  1.00 23.64
ATOM    419  CG  LEU A  64       1.233  52.144  45.369  1.00 23.44
ATOM    420  CD1 LEU A  64       2.462  51.798  46.195  1.00 20.72
ATOM    421  CD2 LEU A  64      -0.032  51.949  46.193  1.00 23.05
ATOM    422  N   THR A  65       0.122  56.540  44.601  1.00 23.08
ATOM    423  CA  THR A  65       0.328  57.940  44.224  1.00 23.45
ATOM    424  C   THR A  65       0.961  58.774  45.328  1.00 23.26
ATOM    425  O   THR A  65       1.727  59.701  45.055  1.00 22.12
ATOM    426  CB  THR A  65      -1.002  58.609  43.810  1.00 22.69
ATOM    427  OG1 THR A  65      -1.934  58.536  44.900  1.00 24.40
ATOM    428  CG2 THR A  65      -1.591  57.909  42.585  1.00 21.16
ATOM    429  N   ILE A  66       0.651  58.436  46.573  1.00 24.12
ATOM    430  CA  ILE A  66       1.179  59.176  47.712  1.00 26.12
ATOM    431  C   ILE A  66       2.658  58.918  47.983  1.00 27.95
ATOM    432  O   ILE A  66       3.108  57.767  48.022  1.00 27.31
ATOM    433  CB  ILE A  66       0.369  58.867  48.999  1.00 25.80
ATOM    434  CG1 ILE A  66      -1.122  59.123  48.749  1.00 25.43
ATOM    435  CG2 ILE A  66       0.825  59.773  50.136  1.00 26.90
ATOM    436  CD1 ILE A  66      -2.014  58.710  49.892  1.00 25.33
ATOM    437  N   GLU A  67       3.408  60.004  48.159  1.00 29.78
ATOM    438  CA  GLU A  67       4.837  59.921  48.448  1.00 32.66
ATOM    439  C   GLU A  67       5.046  60.030  49.950  1.00 33.36
ATOM    440  O   GLU A  67       4.250  60.665  50.650  1.00 34.63
ATOM    441  CB  GLU A  67       5.607  61.052  47.765  1.00 33.66
ATOM    442  CG  GLU A  67       5.515  61.088  46.252  1.00 37.15
ATOM    443  CD  GLU A  67       6.325  62.236  45.670  1.00 40.28
ATOM    444  OE1 GLU A  67       6.265  63.355  46.236  1.00 40.68
ATOM    445  OE2 GLU A  67       7.017  62.023  44.648  1.00 41.22
ATOM    446  N   CYS A  68       6.121  59.415  50.438  1.00 32.06
ATOM    447  CA  CYS A  68       6.453  59.443  51.861  1.00 31.58
ATOM    448  C   CYS A  68       6.866  60.849  52.303  1.00 32.72
ATOM    449  O   CYS A  68       7.212  61.687  51.471  1.00 31.73
ATOM    450  CB  CYS A  68       7.605  58.471  52.146  1.00 28.34
ATOM    451  SG  CYS A  68       9.188  58.920  51.394  1.00 21.61
ATOM    452  N   ASP A  69       6.843  61.102  53.610  1.00 35.61
ATOM    453  CA  ASP A  69       7.251  62.411  54.128  1.00 38.16
ATOM    454  C   ASP A  69       8.775  62.503  54.184  1.00 38.52
ATOM    455  O   ASP A  69       9.478  61.492  54.070  1.00 38.80
ATOM    456  CB  ASP A  69       6.645  62.678  55.515  1.00 41.03
ATOM    457  CG  ASP A  69       6.972  61.595  56.526  1.00 43.83
ATOM    458  OD1 ASP A  69       8.170  61.294  56.720  1.00 46.48
ATOM    459  OD2 ASP A  69       6.026  61.054  57.140  1.00 45.88
ATOM    460  N   ASN A  70       9.286  63.714  54.353  1.00 37.74
ATOM    461  CA  ASN A  70      10.724  63.929  54.375  1.00 37.18
ATOM    462  C   ASN A  70      11.455  63.051  55.385  1.00 36.01
ATOM    463  O   ASN A  70      12.520  62.500  55.098  1.00 35.11
ATOM    464  CB  ASN A  70      11.030  65.393  54.666  1.00 37.81
ATOM    465  CG  ASN A  70      12.496  65.701  54.530  1.00 40.56
ATOM    466  OD1 ASN A  70      13.147  66.151  55.479  1.00 41.54
ATOM    467  ND2 ASN A  70      13.038  65.449  53.343  1.00 42.06
ATOM    468  N   ALA A  71      10.881  62.936  56.573  1.00 34.18
ATOM    469  CA  ALA A  71      11.476  62.131  57.627  1.00 32.81
ATOM    470  C   ALA A  71      11.783  60.713  57.120  1.00 31.52
ATOM    471  O   ALA A  71      12.936  60.268  57.126  1.00 30.04
ATOM    472  CB  ALA A  71      10.534  62.079  58.818  1.00 30.57
ATOM    473  N   VAL A  72      10.744  60.018  56.671  1.00 30.42
ATOM    474  CA  VAL A  72      10.892  58.661  56.167  1.00 28.05
ATOM    475  C   VAL A  72      11.950  58.565  55.082  1.00 28.64
ATOM    476  O   VAL A  72      12.815  57.681  55.123  1.00 27.44
ATOM    477  CB  VAL A  72       9.560  58.135  55.619  1.00 26.03
ATOM    478  CG1 VAL A  72       9.761  56.794  54.928  1.00 23.68
ATOM    479  CG2 VAL A  72       8.568  57.994  56.769  1.00 25.10
ATOM    480  N   LEU A  73      11.905  59.483  54.124  1.00 27.81
ATOM    481  CA  LEU A  73      12.873  59.442  53.042  1.00 29.03
ATOM    482  C   LEU A  73      14.294  59.591  53.579  1.00 29.57
ATOM    483  O   LEU A  73      15.215  58.896  53.133  1.00 29.23
ATOM    484  CB  LEU A  73      12.586  60.547  52.022  1.00 30.60
ATOM    485  CG  LEU A  73      13.364  60.560  50.691  1.00 32.13
ATOM    486  CD1 LEU A  73      14.813  60.901  50.927  1.00 32.92
ATOM    487  CD2 LEU A  73      13.248  59.207  49.992  1.00 33.16
ATOM    488  N   GLN A  74      14.468  60.486  54.544  1.00 27.74
ATOM    489  CA  GLN A  74      15.785  60.728  55.099  1.00 27.59
ATOM    490  C   GLN A  74      16.338  59.511  55.832  1.00 24.88
ATOM    491  O   GLN A  74      17.549  59.357  55.958  1.00 24.21
ATOM    492  CB  GLN A  74      15.728  61.914  56.054  1.00 31.78
ATOM    493  CG  GLN A  74      16.921  62.814  55.940  1.00 36.31
ATOM    494  CD  GLN A  74      17.035  63.422  54.560  1.00 39.44
ATOM    495  OE1 GLN A  74      16.099  64.054  54.057  1.00 40.96
ATOM    496  NE2 GLN A  74      18.188  63.239  53.940  1.00 40.41
ATOM    497  N   SER A  75      15.446  58.642  56.290  1.00 21.13
ATOM    498  CA  SER A  75      15.834  57.460  57.043  1.00 20.20
ATOM    499  C   SER A  75      16.082  56.251  56.153  1.00 19.79
ATOM    500  O   SER A  75      16.169  55.131  56.660  1.00 19.25
ATOM    501  CB  SER A  75      14.727  57.106  58.035  1.00 21.24
ATOM    502  OG  SER A  75      13.536  56.744  57.348  1.00 20.30
ATOM    503  N   THR A  76      16.197  56.482  54.842  1.00 18.11
ATOM    504  CA  THR A  76      16.393  55.401  53.886  1.00 16.51
ATOM    505  C   THR A  76      17.804  55.291  53.334  1.00 16.67
ATOM    506  O   THR A  76      18.361  56.252  52.802  1.00 19.84
ATOM    507  CB  THR A  76      15.392  55.533  52.699  1.00 17.00
ATOM    508  OG1 THR A  76      14.057  55.601  53.216  1.00 15.73
ATOM    509  CG2 THR A  76      15.478  54.321  51.756  1.00 15.64
ATOM    510  N   VAL A  77      18.376  54.102  53.472  1.00 15.07
ATOM    511  CA  VAL A  77      19.713  53.797  52.967  1.00 13.34
ATOM    512  C   VAL A  77      19.610  53.064  51.620  1.00 11.48
ATOM    513  O   VAL A  77      18.710  52.241  51.434  1.00  8.79
ATOM    514  CB  VAL A  77      20.468  52.850  53.915  1.00 14.59
ATOM    515  CG1 VAL A  77      21.851  52.536  53.343  1.00 17.15
ATOM    516  CG2 VAL A  77      20.591  53.468  55.281  1.00 17.70
ATOM    517  N   VAL A  78      20.534  53.355  50.704  1.00  9.39
ATOM    518  CA  VAL A  78      20.567  52.706  49.404  1.00 11.40
ATOM    519  C   VAL A  78      21.786  51.777  49.317  1.00 12.56
ATOM    520  O   VAL A  78      22.914  52.180  49.603  1.00 11.29
ATOM    521  CB  VAL A  78      20.689  53.719  48.241  1.00 12.60
ATOM    522  CG1 VAL A  78      20.885  52.955  46.942  1.00 13.96
ATOM    523  CG2 VAL A  78      19.442  54.599  48.152  1.00 12.43
ATOM    524  N   LEU A  79      21.563  50.527  48.944  1.00 12.10
ATOM    525  CA  LEU A  79      22.686  49.618  48.814  1.00 11.99
ATOM    526  C   LEU A  79      22.602  48.864  47.493  1.00 11.33
ATOM    527  O   LEU A  79      21.526  48.411  47.076  1.00 10.21
ATOM    528  CB  LEU A  79      22.737  48.639  49.994  1.00 11.17
ATOM    529  CG  LEU A  79      23.992  47.745  50.103  1.00 12.77
ATOM    530  CD1 LEU A  79      24.236  47.374  51.564  1.00 11.95
ATOM    531  CD2 LEU A  79      23.839  46.494  49.266  1.00 12.25
ATOM    532  N   LYS A  80      23.750  48.773  46.835  1.00 12.34
ATOM    533  CA  LYS A  80      23.906  48.066  45.576  1.00 13.24
ATOM    534  C   LYS A  80      24.792  46.839  45.816  1.00 13.83
ATOM    535  O   LYS A  80      25.888  46.974  46.351  1.00 14.24
ATOM    536  CB  LYS A  80      24.580  48.970  44.550  1.00 11.86
ATOM    537  CG  LYS A  80      23.639  49.857  43.743  1.00 16.93
ATOM    538  CD  LYS A  80      22.817  49.006  42.777  1.00 19.27
ATOM    539  CE  LYS A  80      22.003  49.841  41.800  1.00 20.87
ATOM    540  NZ  LYS A  80      21.075  48.965  41.017  1.00 18.92
ATOM    541  N   LEU A  81      24.316  45.651  45.438  1.00 13.13
ATOM    542  CA  LEU A  81      25.101  44.423  45.558  1.00 10.42
ATOM    543  C   LEU A  81      26.213  44.497  44.543  1.00 11.77
ATOM    544  O   LEU A  81      25.971  44.904  43.393  1.00 10.22
ATOM    545  CB  LEU A  81      24.227  43.181  45.329  1.00  8.69
ATOM    546  CG  LEU A  81      22.975  43.019  46.194  1.00  5.01
ATOM    547  CD1 LEU A  81      22.148  41.824  45.746  1.00  7.43
ATOM    548  CD2 LEU A  81      23.341  42.874  47.662  1.00  4.24
ATOM    549  N   ASN A  82      27.426  44.111  44.917  1.00 12.18
ATOM    550  CA  ASN A  82      28.545  44.211  43.983  1.00 13.25
ATOM    551  C   ASN A  82      29.649  43.202  44.299  1.00 14.73
ATOM    552  O   ASN A  82      30.808  43.475  44.039  1.00 14.36
ATOM    553  CB  ASN A  82      29.107  45.646  44.071  1.00 14.09
ATOM    554  CG  ASN A  82      30.104  45.976  42.970  1.00 16.45
ATOM    555  OD1 ASN A  82      29.815  45.809  41.788  1.00 18.25
ATOM    556  ND2 ASN A  82      31.279  46.475  43.357  1.00 14.70
ATOM    557  N   GLY A  83      29.311  42.039  44.853  1.00 16.49
ATOM    558  CA  GLY A  83      30.368  41.096  45.184  1.00 20.33
ATOM    559  C   GLY A  83      30.387  39.760  44.453  1.00 23.17
ATOM    560  O   GLY A  83      31.114  38.832  44.828  1.00 22.86
ATOM    561  N   GLY A  84      29.596  39.646  43.400  1.00 25.53
ATOM    562  CA  GLY A  84      29.559  38.387  42.690  1.00 29.27
ATOM    563  C   GLY A  84      30.571  38.266  41.569  1.00 31.13
ATOM    564  O   GLY A  84      31.257  39.222  41.211  1.00 30.70
ATOM    565  N   LEU A  85      30.662  37.061  41.026  1.00 33.83
ATOM    566  CA  LEU A  85      31.552  36.767  39.920  1.00 37.37
ATOM    567  C   LEU A  85      30.668  36.661  38.703  1.00 39.19
ATOM    568  O   LEU A  85      29.503  36.293  38.810  1.00 41.58
ATOM    569  CB  LEU A  85      32.243  35.432  40.145  1.00 39.61
ATOM    570  CG  LEU A  85      33.406  35.449  41.126  1.00 40.23
ATOM    571  CD1 LEU A  85      33.676  34.039  41.626  1.00 41.97
ATOM    572  CD2 LEU A  85      34.627  36.042  40.428  1.00 41.48
ATOM    573  N   GLY A  86      31.205  37.000  37.545  1.00 40.51
ATOM    574  CA  GLY A  86      30.416  36.886  36.337  1.00 41.16
ATOM    575  C   GLY A  86      30.938  35.678  35.586  1.00 41.60
ATOM    576  O   GLY A  86      30.988  35.677  34.361  1.00 40.77
ATOM    577  N   THR A  87      31.338  34.655  36.338  1.00 41.32
ATOM    578  CA  THR A  87      31.886  33.430  35.768  1.00 42.64
ATOM    579  C   THR A  87      31.197  33.001  34.474  1.00 41.35
ATOM    580  O   THR A  87      31.865  32.707  33.482  1.00 40.69
ATOM    581  CB  THR A  87      31.806  32.272  36.780  1.00 44.27
ATOM    582  OG1 THR A  87      30.444  32.085  37.180  1.00 47.84
ATOM    583  CG2 THR A  87      32.663  32.571  38.008  1.00 44.04
ATOM    584  N   GLY A  88      29.864  32.976  34.495  1.00 41.33
ATOM    585  CA  GLY A  88      29.085  32.587  33.328  1.00 39.88
ATOM    586  C   GLY A  88      29.334  33.422  32.082  1.00 39.48
ATOM    587  O   GLY A  88      29.132  32.938  30.967  1.00 40.73
ATOM    588  N   MET A  89      29.756  34.673  32.268  1.00 37.30
ATOM    589  CA  MET A  89      30.052  35.581  31.161  1.00 36.70
ATOM    590  C   MET A  89      31.567  35.694  30.950  1.00 37.92
ATOM    591  O   MET A  89      32.043  36.588  30.247  1.00 37.17
ATOM    592  CB  MET A  89      29.482  36.975  31.441  1.00 35.43
ATOM    593  CG  MET A  89      27.968  37.064  31.416  1.00 34.42
ATOM    594  SD  MET A  89      27.300  38.800  31.981  1.00 32.70
ATOM    595  CE  MET A  89      27.573  39.843  30.410  1.00 30.82
ATOM    596  N   GLY A  90      32.320  34.788  31.569  1.00 39.52
ATOM    597  CA  GLY A  90      33.769  34.801  31.429  1.00 41.22
ATOM    598  C   GLY A  90      34.446  36.035  31.997  1.00 43.23
ATOM    599  O   GLY A  90      35.518  36.430  31.530  1.00 42.53
ATOM    600  N   LEU A  91      33.822  36.648  33.002  1.00 44.26
ATOM    601  CA  LEU A  91      34.382  37.836  33.630  1.00 46.20
ATOM    602  C   LEU A  91      35.349  37.400  34.710  1.00 47.99
ATOM    603  O   LEU A  91      35.267  36.271  35.202  1.00 49.74
ATOM    604  CB  LEU A  91      33.283  38.684  34.273  1.00 45.36
ATOM    605  CG  LEU A  91      32.159  39.229  33.397  1.00 45.43
ATOM    606  CD1 LEU A  91      31.157  39.957  34.275  1.00 44.05
ATOM    607  CD2 LEU A  91      32.724  40.158  32.339  1.00 45.07
ATOM    608  N   CYS A  92      36.255  38.296  35.086  1.00 49.02
ATOM    609  CA  CYS A  92      37.223  37.997  36.130  1.00 50.75
ATOM    610  C   CYS A  92      37.230  39.078  37.203  1.00 48.73
ATOM    611  O   CYS A  92      37.908  38.944  38.220  1.00 49.94
ATOM    612  CB  CYS A  92      38.622  37.854  35.532  1.00 53.79
ATOM    613  SG  CYS A  92      39.872  37.367  36.740  1.00 62.41
ATOM    614  N   ASP A  93      36.477  40.151  36.973  1.00 45.92
ATOM    615  CA  ASP A  93      36.399  41.248  37.937  1.00 41.68
ATOM    616  C   ASP A  93      34.960  41.732  38.045  1.00 37.54
ATOM    617  O   ASP A  93      34.056  41.110  37.494  1.00 36.54
ATOM    618  CB  ASP A  93      37.321  42.401  37.520  1.00 43.40
ATOM    619  CG  ASP A  93      37.783  43.252  38.710  1.00 44.50
ATOM    620  OD1 ASP A  93      38.698  44.084  38.519  1.00 45.39
ATOM    621  OD2 ASP A  93      37.241  43.101  39.829  1.00 42.89
ATOM    622  N   ALA A  94      34.754  42.838  38.754  1.00 33.48
ATOM    623  CA  ALA A  94      33.412  43.376  38.965  1.00 29.11
ATOM    624  C   ALA A  94      32.653  43.610  37.668  1.00 26.39
ATOM    625  O   ALA A  94      33.132  44.296  36.764  1.00 24.77
ATOM    626  CB  ALA A  94      33.482  44.671  39.777  1.00 26.71
ATOM    627  N   LYS A  95      31.457  43.038  37.586  1.00 23.86
ATOM    628  CA  LYS A  95      30.645  43.189  36.394  1.00 22.30
ATOM    629  C   LYS A  95      30.280  44.652  36.165  1.00 21.70
ATOM    630  O   LYS A  95      30.173  45.110  35.027  1.00 20.69
ATOM    631  CB  LYS A  95      29.363  42.356  36.508  1.00 20.49
ATOM    632  CG  LYS A  95      28.459  42.488  35.275  1.00 16.98
ATOM    633  CD  LYS A  95      27.166  41.704  35.412  1.00 16.51
ATOM    634  CE  LYS A  95      27.401  40.216  35.473  1.00 20.07
ATOM    635  NZ  LYS A  95      26.111  39.482  35.593  1.00 23.88
ATOM    636  N   THR A  96      30.118  45.383  37.259  1.00 21.48
ATOM    637  CA  THR A  96      29.743  46.781  37.207  1.00 21.25
ATOM    638  C   THR A  96      30.758  47.688  36.532  1.00 22.92
ATOM    639  O   THR A  96      30.448  48.844  36.239  1.00 22.80
ATOM    640  CB  THR A  96      29.482  47.309  38.609  1.00 21.15
ATOM    641  OG1 THR A  96      30.639  47.079  39.420  1.00 20.89
ATOM    642  CG2 THR A  96      28.265  46.605  39.221  1.00 18.81
ATOM    643  N   LEU A  97      31.958  47.172  36.278  1.00 23.10
ATOM    644  CA  LEU A  97      32.998  47.968  35.627  1.00 24.51
ATOM    645  C   LEU A  97      32.925  47.873  34.099  1.00 24.98
ATOM    646  O   LEU A  97      33.726  48.483  33.385  1.00 25.33
ATOM    647  CB  LEU A  97      34.378  47.528  36.115  1.00 26.43
ATOM    648  CG  LEU A  97      34.625  47.739  37.613  1.00 27.24
ATOM    649  CD1 LEU A  97      35.810  46.888  38.064  1.00 28.59
ATOM    650  CD2 LEU A  97      34.859  49.212  37.886  1.00 24.30
ATOM    651  N   LEU A  98      31.966  47.097  33.606  1.00 23.41
ATOM    652  CA  LEU A  98      31.771  46.942  32.173  1.00 22.64
ATOM    653  C   LEU A  98      31.006  48.147  31.646  1.00 21.98
ATOM    654  O   LEU A  98      30.227  48.752  32.370  1.00 23.17
ATOM    655  CB  LEU A  98      30.957  45.670  31.874  1.00 21.20
ATOM    656  CG  LEU A  98      31.564  44.312  32.237  1.00 20.08
ATOM    657  CD1 LEU A  98      30.566  43.206  31.895  1.00 21.09
ATOM    658  CD2 LEU A  98      32.863  44.112  31.477  1.00 16.65
ATOM    659  N   GLU A  99      31.222  48.492  30.385  1.00 24.10
ATOM    660  CA  GLU A  99      30.515  49.618  29.786  1.00 27.16
ATOM    661  C   GLU A  99      29.063  49.247  29.469  1.00 26.29
ATOM    662  O   GLU A  99      28.772  48.115  29.086  1.00 24.33
ATOM    663  CB  GLU A  99      31.226  50.075  28.506  1.00 28.80
ATOM    664  CG  GLU A  99      32.328  51.100  28.741  1.00 35.55
ATOM    665  CD  GLU A  99      32.967  51.576  27.444  1.00 38.68
ATOM    666  OE1 GLU A  99      32.216  51.925  26.504  1.00 39.77
ATOM    667  OE2 GLU A  99      34.219  51.605  27.368  1.00 41.28
ATOM    668  N   VAL A 100      28.161  50.211  29.639  1.00 27.54
ATOM    669  CA  VAL A 100      26.731  50.021  29.380  1.00 28.87
ATOM    670  C   VAL A 100      26.314  50.897  28.196  1.00 28.31
ATOM    671  O   VAL A 100      25.526  50.482  27.344  1.00 30.17
ATOM    672  CB  VAL A 100      25.901  50.381  30.648  1.00 28.95
ATOM    673  CG1 VAL A 100      24.416  50.523  30.303  1.00 30.37
ATOM    674  CG2 VAL A 100      26.089  49.295  31.695  1.00 29.11
ATOM    675  N   LYS A 101      26.847  52.114  28.173  1.00 27.76
ATOM    676  CA  LYS A 101      26.623  53.084  27.100  1.00 28.70
ATOM    677  C   LYS A 101      28.014  53.658  26.835  1.00 29.03
ATOM    678  O   LYS A 101      28.896  53.555  27.691  1.00 30.47
ATOM    679  CB  LYS A 101      25.658  54.208  27.523  1.00 26.38
ATOM    680  CG  LYS A 101      24.194  53.784  27.688  1.00 24.49
ATOM    681  CD  LYS A 101      23.618  53.125  26.416  1.00 24.88
ATOM    682  CE  LYS A 101      22.134  52.798  26.576  1.00 24.20
ATOM    683  NZ  LYS A 101      21.587  51.972  25.462  1.00 24.32
ATOM    684  N   ASP A 102      28.217  54.253  25.665  1.00 29.00
ATOM    685  CA  ASP A 102      29.520  54.806  25.321  1.00 28.69
ATOM    686  C   ASP A 102      30.183  55.574  26.469  1.00 27.43
ATOM    687  O   ASP A 102      29.683  56.597  26.922  1.00 27.29
ATOM    688  CB  ASP A 102      29.407  55.693  24.068  1.00 29.53
ATOM    689  CG  ASP A 102      30.753  56.314  23.649  1.00 31.81
ATOM    690  OD1 ASP A 102      31.817  55.682  23.852  1.00 30.29
ATOM    691  OD2 ASP A 102      30.740  57.436  23.098  1.00 32.90
ATOM    692  N   GLY A 103      31.310  55.043  26.943  1.00 27.54
ATOM    693  CA  GLY A 103      32.060  55.675  28.015  1.00 25.79
ATOM    694  C   GLY A 103      31.480  55.629  29.419  1.00 25.67
ATOM    695  O   GLY A 103      32.016  56.282  30.317  1.00 25.55
ATOM    696  N   LYS A 104      30.397  54.879  29.623  1.00 24.40
ATOM    697  CA  LYS A 104      29.790  54.795  30.949  1.00 23.94
ATOM    698  C   LYS A 104      29.593  53.349  31.390  1.00 22.21
ATOM    699  O   LYS A 104      29.046  52.526  30.656  1.00 22.56
ATOM    700  CB  LYS A 104      28.447  55.537  30.968  1.00 24.33
ATOM    701  CG  LYS A 104      28.550  57.033  30.676  1.00 27.76
ATOM    702  CD  LYS A 104      29.206  57.780  31.827  1.00 29.40
ATOM    703  CE  LYS A 104      29.361  59.265  31.531  1.00 32.35
ATOM    704  NZ  LYS A 104      30.407  59.537  30.507  1.00 34.53
ATOM    705  N   THR A 105      30.040  53.052  32.601  1.00 21.69
ATOM    706  CA  THR A 105      29.931  51.713  33.168  1.00 18.80
ATOM    707  C   THR A 105      28.719  51.658  34.085  1.00 18.58
ATOM    708  O   THR A 105      28.077  52.685  34.342  1.00 16.23
ATOM    709  CB  THR A 105      31.160  51.393  34.021  1.00 19.73
ATOM    710  OG1 THR A 105      31.083  52.138  35.248  1.00 19.63
ATOM    711  CG2 THR A 105      32.447  51.780  33.272  1.00 17.96
ATOM    712  N   PHE A 106      28.397  50.464  34.576  1.00 17.55
ATOM    713  CA  PHE A 106      27.287  50.318  35.508  1.00 18.08
ATOM    714  C   PHE A 106      27.573  51.201  36.717  1.00 19.35
ATOM    715  O   PHE A 106      26.679  51.849  37.260  1.00 19.63
ATOM    716  CB  PHE A 106      27.167  48.878  36.011  1.00 16.55
ATOM    717  CG  PHE A 106      26.754  47.893  34.973  1.00 17.07
ATOM    718  CD1 PHE A 106      27.688  47.320  34.137  1.00 15.67
ATOM    719  CD2 PHE A 106      25.424  47.497  34.868  1.00 17.72
ATOM    720  CE1 PHE A 106      27.312  46.358  33.212  1.00 18.12
ATOM    721  CE2 PHE A 106      25.035  46.537  33.947  1.00 17.69
ATOM    722  CZ  PHE A 106      25.984  45.967  33.116  1.00 17.84
ATOM    723  N   LEU A 107      28.836  51.203  37.127  1.00 21.39
ATOM    724  CA  LEU A 107      29.287  51.974  38.281  1.00 22.60
ATOM    725  C   LEU A 107      29.095  53.457  38.037  1.00 21.99
ATOM    726  O   LEU A 107      28.776  54.202  38.960  1.00 22.35
ATOM    727  CB  LEU A 107      30.765  51.681  38.560  1.00 22.01
ATOM    728  CG  LEU A 107      31.183  51.383  39.995  1.00 24.88
ATOM    729  CD1 LEU A 107      30.207  50.395  40.638  1.00 26.55
ATOM    730  CD2 LEU A 107      32.594  50.804  40.002  1.00 23.30
ATOM    731  N   ASP A 108      29.303  53.877  36.790  1.00 22.01
ATOM    732  CA  ASP A 108      29.149  55.273  36.399  1.00 20.53
ATOM    733  C   ASP A 108      27.707  55.728  36.627  1.00 19.79
ATOM    734  O   ASP A 108      27.458  56.747  37.280  1.00 19.75
ATOM    735  CB  ASP A 108      29.505  55.461  34.912  1.00 22.84
ATOM    736  CG  ASP A 108      31.004  55.686  34.674  1.00 23.84
ATOM    737  OD1 ASP A 108      31.592  56.541  35.358  1.00 25.96
ATOM    738  OD2 ASP A 108      31.592  55.024  33.792  1.00 26.00
ATOM    739  N   PHE A 109      26.762  54.964  36.084  1.00 18.36
ATOM    740  CA  PHE A 109      25.350  55.281  36.217  1.00 17.12
ATOM    741  C   PHE A 109      24.859  55.162  37.656  1.00 17.18
ATOM    742  O   PHE A 109      23.986  55.910  38.081  1.00 18.82
ATOM    743  CB  PHE A 109      24.521  54.390  35.292  1.00 18.70
ATOM    744  CG  PHE A 109      24.582  54.807  33.840  1.00 21.66
ATOM    745  CD1 PHE A 109      25.287  54.047  32.905  1.00 22.05
ATOM    746  CD2 PHE A 109      23.953  55.983  33.413  1.00 21.84
ATOM    747  CE1 PHE A 109      25.371  54.447  31.560  1.00 22.30
ATOM    748  CE2 PHE A 109      24.032  56.397  32.073  1.00 23.67
ATOM    749  CZ  PHE A 109      24.743  55.625  31.146  1.00 21.54
ATOM    750  N   THR A 110      25.419  54.230  38.413  1.00 14.83
ATOM    751  CA  THR A 110      25.013  54.094  39.800  1.00 15.83
ATOM    752  C   THR A 110      25.321  55.384  40.551  1.00 14.02
ATOM    753  O   THR A 110      24.459  55.935  41.224  1.00 15.07
ATOM    754  CB  THR A 110      25.747  52.928  40.498  1.00 16.51
ATOM    755  OG1 THR A 110      25.514  51.718  39.773  1.00 17.39
ATOM    756  CG2 THR A 110      25.235  52.752  41.916  1.00 16.87
ATOM    757  N   ALA A 111      26.555  55.853  40.426  1.00 14.93
ATOM    758  CA  ALA A 111      27.009  57.077  41.092  1.00 17.45
ATOM    759  C   ALA A 111      26.209  58.296  40.646  1.00 17.10
ATOM    760  O   ALA A 111      25.859  59.154  41.454  1.00 19.10
ATOM    761  CB  ALA A 111      28.497  57.306  40.804  1.00 16.45
ATOM    762  N   LEU A 112      25.928  58.372  39.353  1.00 18.71
ATOM    763  CA  LEU A 112      25.157  59.483  38.818  1.00 19.89
ATOM    764  C   LEU A 112      23.779  59.445  39.460  1.00 21.06
ATOM    765  O   LEU A 112      23.179  60.489  39.749  1.00 20.63
ATOM    766  CB  LEU A 112      25.062  59.363  37.293  1.00 21.46
ATOM    767  CG  LEU A 112      26.385  59.696  36.594  1.00 21.04
ATOM    768  CD1 LEU A 112      26.341  59.364  35.108  1.00 20.28
ATOM    769  CD2 LEU A 112      26.656  61.199  36.797  1.00 23.12
ATOM    770  N   GLN A 113      23.285  58.234  39.704  1.00 20.93
ATOM    771  CA  GLN A 113      21.983  58.069  40.340  1.00 21.38
ATOM    772  C   GLN A 113      22.042  58.608  41.758  1.00 21.76
ATOM    773  O   GLN A 113      21.183  59.371  42.181  1.00 23.82
ATOM    774  CB  GLN A 113      21.581  56.597  40.361  1.00 21.73
ATOM    775  CG  GLN A 113      21.032  56.093  39.029  1.00 22.84
ATOM    776  CD  GLN A 113      20.973  54.574  38.932  1.00 22.49
ATOM    777  OE1 GLN A 113      20.897  53.872  39.941  1.00 22.57
ATOM    778  NE2 GLN A 113      20.989  54.066  37.707  1.00 22.31
ATOM    779  N   VAL A 114      23.067  58.215  42.497  1.00 22.98
ATOM    780  CA  VAL A 114      23.212  58.686  43.865  1.00 21.49
ATOM    781  C   VAL A 114      23.298  60.213  43.854  1.00 21.89
ATOM    782  O   VAL A 114      22.551  60.888  44.554  1.00 21.58
ATOM    783  CB  VAL A 114      24.476  58.097  44.516  1.00 19.11
ATOM    784  CG1 VAL A 114      24.636  58.639  45.916  1.00 17.94
ATOM    785  CG2 VAL A 114      24.379  56.568  44.531  1.00 18.59
ATOM    786  N   GLN A 115      24.201  60.746  43.038  1.00 23.32
ATOM    787  CA  GLN A 115      24.397  62.188  42.916  1.00 25.33
ATOM    788  C   GLN A 115      23.095  62.924  42.649  1.00 25.10
ATOM    789  O   GLN A 115      22.780  63.899  43.313  1.00 25.50
ATOM    790  CB  GLN A 115      25.384  62.464  41.793  1.00 27.25
ATOM    791  CG  GLN A 115      25.698  63.921  41.566  1.00 28.92
ATOM    792  CD  GLN A 115      26.799  64.094  40.531  1.00 31.03
ATOM    793  OE1 GLN A 115      26.619  63.782  39.350  1.00 30.37
ATOM    794  NE2 GLN A 115      27.953  64.583  40.975  1.00 31.60
ATOM    795  N   TYR A 116      22.331  62.440  41.680  1.00 26.71
ATOM    796  CA  TYR A 116      21.057  63.053  41.339  1.00 27.58
ATOM    797  C   TYR A 116      20.145  63.142  42.555  1.00 28.70
ATOM    798  O   TYR A 116      19.519  64.186  42.808  1.00 28.51
ATOM    799  CB  TYR A 116      20.343  62.245  40.255  1.00 27.48
ATOM    800  CG  TYR A 116      19.039  62.866  39.822  1.00 28.44
ATOM    801  CD1 TYR A 116      18.993  63.771  38.760  1.00 29.33
ATOM    802  CD2 TYR A 116      17.855  62.583  40.496  1.00 29.08
ATOM    803  CE1 TYR A 116      17.802  64.376  38.381  1.00 29.12
ATOM    804  CE2 TYR A 116      16.653  63.190  40.126  1.00 31.21
ATOM    805  CZ  TYR A 116      16.638  64.085  39.066  1.00 29.86
ATOM    806  OH  TYR A 116      15.454  64.684  38.692  1.00 33.00
ATOM    807  N   LEU A 117      20.042  62.041  43.296  1.00 28.23
ATOM    808  CA  LEU A 117      19.188  62.041  44.478  1.00 28.76
ATOM    809  C   LEU A 117      19.726  62.964  45.577  1.00 27.74
ATOM    810  O   LEU A 117      18.945  63.561  46.315  1.00 24.75
ATOM    811  CB  LEU A 117      18.995  60.621  45.028  1.00 27.68
ATOM    812  CG  LEU A 117      18.057  59.731  44.204  1.00 28.41
ATOM    813  CD1 LEU A 117      17.783  58.463  44.970  1.00 28.43
ATOM    814  CD2 LEU A 117      16.750  60.441  43.926  1.00 28.22
ATOM    815  N   ARG A 118      21.046  63.092  45.677  1.00 28.40
ATOM    816  CA  ARG A 118      21.610  63.965  46.691  1.00 32.18
ATOM    817  C   ARG A 118      21.412  65.441  46.310  1.00 33.55
ATOM    818  O   ARG A 118      21.446  66.320  47.169  1.00 34.90
ATOM    819  CB  ARG A 118      23.099  63.669  46.911  1.00 30.66
ATOM    820  CG  ARG A 118      23.363  62.481  47.820  1.00 32.41
ATOM    821  CD  ARG A 118      24.818  62.373  48.227  1.00 32.79
ATOM    822  NE  ARG A 118      25.106  61.051  48.773  1.00 35.98
ATOM    823  CZ  ARG A 118      26.272  60.688  49.298  1.00 36.05
ATOM    824  NH1 ARG A 118      27.269  61.556  49.349  1.00 37.45
ATOM    825  NH2 ARG A 118      26.436  59.459  49.776  1.00 36.52
ATOM    826  N   GLN A 119      21.202  65.717  45.030  1.00 34.81
ATOM    827  CA  GLN A 119      21.000  67.093  44.618  1.00 37.27
ATOM    828  C   GLN A 119      19.530  67.432  44.667  1.00 37.22
ATOM    829  O   GLN A 119      19.156  68.587  44.849  1.00 36.41
ATOM    830  CB  GLN A 119      21.585  67.323  43.215  1.00 38.83
ATOM    831  CG  GLN A 119      23.106  67.278  43.217  1.00 41.50
ATOM    832  CD  GLN A 119      23.729  67.187  41.828  1.00 42.58
ATOM    833  OE1 GLN A 119      23.100  66.758  40.866  1.00 43.18
ATOM    834  NE2 GLN A 119      24.993  67.565  41.736  1.00 43.14
ATOM    835  N   HIS A 120      18.686  66.414  44.568  1.00 38.95
ATOM    836  CA  HIS A 120      17.248  66.653  44.585  1.00 41.15
ATOM    837  C   HIS A 120      16.502  66.153  45.814  1.00 42.36
ATOM    838  O   HIS A 120      15.916  66.955  46.538  1.00 45.53
ATOM    839  CB  HIS A 120      16.631  66.065  43.331  1.00 43.31
ATOM    840  CG  HIS A 120      17.159  66.689  42.076  1.00 45.51
ATOM    841  ND1 HIS A 120      16.736  67.921  41.627  1.00 46.83
ATOM    842  CD2 HIS A 120      18.132  66.292  41.222  1.00 46.32
ATOM    843  CE1 HIS A 120      17.423  68.258  40.547  1.00 47.39
ATOM    844  NE2 HIS A 120      18.277  67.286  40.280  1.00 46.59
ATOM    845  N   CYS A 121      16.514  64.850  46.073  1.00 42.85
ATOM    846  CA  CYS A 121      15.775  64.323  47.224  1.00 43.40
ATOM    847  C   CYS A 121      16.368  64.601  48.606  1.00 42.28
ATOM    848  O   CYS A 121      15.796  65.362  49.382  1.00 42.93
ATOM    849  CB  CYS A 121      15.550  62.822  47.049  1.00 44.65
ATOM    850  SG  CYS A 121      14.515  62.453  45.630  1.00 52.07
ATOM    851  N   SER A 122      17.494  63.971  48.924  1.00 40.56
ATOM    852  CA  SER A 122      18.129  64.159  50.225  1.00 38.70
ATOM    853  C   SER A 122      19.627  64.276  50.049  1.00 37.77
ATOM    854  O   SER A 122      20.290  63.304  49.669  1.00 35.39
ATOM    855  CB  SER A 122      17.813  62.973  51.134  1.00 40.80
ATOM    856  OG  SER A 122      18.111  61.749  50.493  1.00 39.31
ATOM    857  N   GLU A 123      20.163  65.457  50.342  1.00 36.92
ATOM    858  CA  GLU A 123      21.588  65.701  50.161  1.00 38.00
ATOM    859  C   GLU A 123      22.532  64.752  50.893  1.00 36.45
ATOM    860  O   GLU A 123      23.669  64.570  50.465  1.00 34.88
ATOM    861  CB  GLU A 123      21.931  67.159  50.521  1.00 41.73
ATOM    862  CG  GLU A 123      21.695  67.552  51.973  1.00 45.35
ATOM    863  CD  GLU A 123      22.152  68.979  52.281  1.00 48.13
ATOM    864  OE1 GLU A 123      23.347  69.292  52.073  1.00 49.68
ATOM    865  OE2 GLU A 123      21.315  69.787  52.735  1.00 48.45
ATOM    866  N   HIS A 124      22.070  64.141  51.981  1.00 35.26
ATOM    867  CA  HIS A 124      22.916  63.224  52.740  1.00 35.00
ATOM    868  C   HIS A 124      22.522  61.764  52.562  1.00 31.96
ATOM    869  O   HIS A 124      22.734  60.945  53.453  1.00 32.53
ATOM    870  CB  HIS A 124      22.861  63.581  54.223  1.00 38.19
ATOM    871  CG  HIS A 124      23.159  65.019  54.499  1.00 41.60
ATOM    872  ND1 HIS A 124      24.400  65.575  54.279  1.00 42.70
ATOM    873  CD2 HIS A 124      22.365  66.025  54.936  1.00 42.11
ATOM    874  CE1 HIS A 124      24.358  66.864  54.567  1.00 44.33
ATOM    875  NE2 HIS A 124      23.134  67.163  54.968  1.00 44.42
ATOM    876  N   LEU A 125      21.942  61.438  51.416  1.00 30.01
ATOM    877  CA  LEU A 125      21.526  60.066  51.145  1.00 28.18
ATOM    878  C   LEU A 125      22.675  59.096  51.390  1.00 25.41
ATOM    879  O   LEU A 125      23.772  59.283  50.863  1.00 23.84
ATOM    880  CB  LEU A 125      21.066  59.922  49.695  1.00 30.34
ATOM    881  CG  LEU A 125      20.755  58.474  49.313  1.00 32.44
ATOM    882  CD1 LEU A 125      19.461  58.065  49.977  1.00 32.35
ATOM    883  CD2 LEU A 125      20.646  58.336  47.815  1.00 32.29
ATOM    884  N   ARG A 126      22.418  58.069  52.196  1.00 22.70
ATOM    885  CA  ARG A 126      23.431  57.066  52.493  1.00 20.91
ATOM    886  C   ARG A 126      23.424  55.997  51.403  1.00 19.61
ATOM    887  O   ARG A 126      22.426  55.301  51.188  1.00 17.62
ATOM    888  CB  ARG A 126      23.178  56.420  53.854  1.00 20.70
ATOM    889  CG  ARG A 126      24.141  55.267  54.206  1.00 22.95
ATOM    890  CD  ARG A 126      25.618  55.693  54.265  1.00 23.55
ATOM    891  NE  ARG A 126      25.882  56.726  55.266  1.00 26.54
ATOM    892  CZ  ARG A 126      26.064  56.507  56.568  1.00 29.50
ATOM    893  NH1 ARG A 126      26.021  55.273  57.062  1.00 27.48
ATOM    894  NH2 ARG A 126      26.284  57.533  57.387  1.00 31.24
ATOM    895  N   PHE A 127      24.546  55.896  50.705  1.00 17.79
ATOM    896  CA  PHE A 127      24.718  54.926  49.635  1.00 16.85
ATOM    897  C   PHE A 127      25.774  53.898  50.018  1.00 15.56
ATOM    898  O   PHE A 127      26.832  54.252  50.530  1.00 14.62
ATOM    899  CB  PHE A 127      25.154  55.628  48.344  1.00 17.90
ATOM    900  CG  PHE A 127      25.548  54.679  47.244  1.00 19.79
ATOM    901  CD1 PHE A 127      24.590  53.888  46.610  1.00 18.74
ATOM    902  CD2 PHE A 127      26.882  54.552  46.863  1.00 19.38
ATOM    903  CE1 PHE A 127      24.957  52.982  45.614  1.00 19.45
ATOM    904  CE2 PHE A 127      27.256  53.650  45.870  1.00 20.99
ATOM    905  CZ  PHE A 127      26.291  52.862  45.246  1.00 19.16
ATOM    906  N   MET A 128      25.489  52.631  49.736  1.00 14.74
ATOM    907  CA  MET A 128      26.418  51.556  50.039  1.00 14.62
ATOM    908  C   MET A 128      26.568  50.550  48.891  1.00 14.12
ATOM    909  O   MET A 128      25.719  50.470  47.995  1.00 13.36
ATOM    910  CB  MET A 128      25.973  50.809  51.298  1.00 14.41
ATOM    911  CG  MET A 128      25.845  51.666  52.551  1.00 17.33
ATOM    912  SD  MET A 128      25.438  50.605  54.162  1.00 25.12
ATOM    913  CE  MET A 128      27.259  50.207  54.693  1.00 20.64
ATOM    914  N   LEU A 129      27.675  49.812  48.935  1.00 12.49
ATOM    915  CA  LEU A 129      28.001  48.760  47.978  1.00 12.39
ATOM    916  C   LEU A 129      28.543  47.555  48.754  1.00 12.19
ATOM    917  O   LEU A 129      29.464  47.689  49.578  1.00 11.34
ATOM    918  CB  LEU A 129      29.089  49.204  46.996  1.00 10.73
ATOM    919  CG  LEU A 129      28.725  50.209  45.905  1.00 12.62
ATOM    920  CD1 LEU A 129      29.975  50.929  45.439  1.00  8.92
ATOM    921  CD2 LEU A 129      28.034  49.483  44.746  1.00 10.07
ATOM    922  N   MET A 130      27.972  46.381  48.512  1.00 11.30
ATOM    923  CA  MET A 130      28.484  45.198  49.174  1.00 12.51
ATOM    924  C   MET A 130      29.502  44.642  48.198  1.00 13.04
ATOM    925  O   MET A 130      29.165  44.345  47.043  1.00 12.38
ATOM    926  CB  MET A 130      27.379  44.174  49.437  1.00 13.73
ATOM    927  CG  MET A 130      27.923  42.906  50.095  1.00 16.54
ATOM    928  SD  MET A 130      26.567  41.740  50.825  1.00 24.92
ATOM    929  CE  MET A 130      26.315  40.577  49.274  1.00 16.66
ATOM    930  N   ASP A 131      30.749  44.537  48.643  1.00 12.15
ATOM    931  CA  ASP A 131      31.821  44.028  47.792  1.00 14.67
ATOM    932  C   ASP A 131      32.378  42.718  48.334  1.00 16.96
ATOM    933  O   ASP A 131      32.162  42.393  49.503  1.00 17.35
ATOM    934  CB  ASP A 131      32.980  45.030  47.728  1.00 12.27
ATOM    935  CG  ASP A 131      32.573  46.361  47.132  1.00 15.29
ATOM    936  OD1 ASP A 131      31.595  46.345  46.361  1.00 14.94
ATOM    937  OD2 ASP A 131      33.235  47.400  47.414  1.00 12.29
ATOM    938  N   SER A 132      33.090  41.988  47.476  1.00 17.97
ATOM    939  CA  SER A 132      33.747  40.734  47.849  1.00 23.90
ATOM    940  C   SER A 132      35.207  41.153  47.781  1.00 26.84
ATOM    941  O   SER A 132      35.483  42.245  47.273  1.00 26.48
ATOM    942  CB  SER A 132      33.482  39.640  46.814  1.00 24.19
ATOM    943  OG  SER A 132      34.089  39.971  45.573  1.00 21.55
ATOM    944  N   PHE A 133      36.159  40.351  48.259  1.00 31.46
ATOM    945  CA  PHE A 133      37.527  40.859  48.159  1.00 36.92
ATOM    946  C   PHE A 133      37.939  40.880  46.706  1.00 37.54
ATOM    947  O   PHE A 133      38.822  41.633  46.308  1.00 38.87
ATOM    948  CB  PHE A 133      38.543  40.051  48.963  1.00 41.74
ATOM    949  CG  PHE A 133      39.841  40.798  49.168  1.00 47.13
ATOM    950  CD1 PHE A 133      39.879  41.937  49.986  1.00 49.24
ATOM    951  CD2 PHE A 133      40.991  40.454  48.455  1.00 48.75
ATOM    952  CE1 PHE A 133      41.039  42.726  50.085  1.00 50.16
ATOM    953  CE2 PHE A 133      42.158  41.234  48.545  1.00 51.03
ATOM    954  CZ  PHE A 133      42.179  42.377  49.362  1.00 50.81
ATOM    955  N   ASN A 134      37.280  40.053  45.910  1.00 37.73
ATOM    956  CA  ASN A 134      37.575  40.011  44.494  1.00 38.14
ATOM    957  C   ASN A 134      37.197  41.321  43.779  1.00 36.26
ATOM    958  O   ASN A 134      37.879  41.745  42.840  1.00 37.95
ATOM    959  CB  ASN A 134      36.840  38.845  43.841  1.00 40.68
ATOM    960  CG  ASN A 134      36.967  38.859  42.329  1.00 45.59
ATOM    961  OD1 ASN A 134      38.074  38.966  41.788  1.00 47.67
ATOM    962  ND2 ASN A 134      35.832  38.752  41.633  1.00 46.72
ATOM    963  N   THR A 135      36.127  41.976  44.226  1.00 31.79
ATOM    964  CA  THR A 135      35.670  43.202  43.567  1.00 27.26
ATOM    965  C   THR A 135      35.974  44.506  44.304  1.00 25.95
ATOM    966  O   THR A 135      35.791  45.589  43.754  1.00 26.06
ATOM    967  CB  THR A 135      34.138  43.164  43.347  1.00 26.25
ATOM    968  OG1 THR A 135      33.477  43.357  44.598  1.00 22.33
ATOM    969  CG2 THR A 135      33.699  41.828  42.801  1.00 24.39
ATOM    970  N   SER A 136      36.430  44.398  45.545  1.00 24.66
ATOM    971  CA  SER A 136      36.699  45.567  46.380  1.00 23.47
ATOM    972  C   SER A 136      37.685  46.593  45.835  1.00 23.88
ATOM    973  O   SER A 136      37.339  47.763  45.633  1.00 23.69
ATOM    974  CB  SER A 136      37.164  45.099  47.763  1.00 22.98
ATOM    975  OG  SER A 136      37.294  46.180  48.658  1.00 23.79
ATOM    976  N   ALA A 137      38.914  46.152  45.604  1.00 23.60
ATOM    977  CA  ALA A 137      39.970  47.027  45.116  1.00 25.14
ATOM    978  C   ALA A 137      39.637  47.743  43.800  1.00 25.41
ATOM    979  O   ALA A 137      39.858  48.947  43.658  1.00 24.37
ATOM    980  CB  ALA A 137      41.271  46.223  44.967  1.00 24.86
ATOM    981  N   SER A 138      39.102  46.992  42.846  1.00 26.42
ATOM    982  CA  SER A 138      38.757  47.529  41.537  1.00 27.58
ATOM    983  C   SER A 138      37.708  48.617  41.657  1.00 26.96
ATOM    984  O   SER A 138      37.785  49.659  40.990  1.00 26.74
ATOM    985  CB  SER A 138      38.215  46.407  40.650  1.00 29.94
ATOM    986  OG  SER A 138      38.851  45.181  40.955  1.00 34.37
ATOM    987  N   THR A 139      36.722  48.358  42.511  1.00 25.36
ATOM    988  CA  THR A 139      35.628  49.292  42.727  1.00 24.10
ATOM    989  C   THR A 139      36.153  50.572  43.372  1.00 24.39
ATOM    990  O   THR A 139      35.867  51.682  42.905  1.00 24.18
ATOM    991  CB  THR A 139      34.535  48.670  43.642  1.00 23.47
ATOM    992  OG1 THR A 139      34.029  47.469  43.043  1.00 21.18
ATOM    993  CG2 THR A 139      33.389  49.645  43.847  1.00 20.96
ATOM    994  N   LYS A 140      36.927  50.413  44.439  1.00 24.00
ATOM    995  CA  LYS A 140      37.475  51.564  45.139  1.00 25.78
ATOM    996  C   LYS A 140      38.287  52.451  44.203  1.00 25.76
ATOM    997  O   LYS A 140      38.057  53.659  44.122  1.00 24.30
ATOM    998  CB  LYS A 140      38.349  51.105  46.304  1.00 27.36
ATOM    999  CG  LYS A 140      38.754  52.227  47.249  1.00 30.39
ATOM   1000  CD  LYS A 140      39.351  51.659  48.528  1.00 33.03
ATOM   1001  CE  LYS A 140      39.775  52.759  49.497  1.00 35.19
ATOM   1002  NZ  LYS A 140      40.283  52.170  50.775  1.00 35.50
ATOM   1003  N   SER A 141      39.228  51.849  43.483  1.00 25.39
ATOM   1004  CA  SER A 141      40.068  52.611  42.567  1.00 27.16
ATOM   1005  C   SER A 141      39.259  53.339  41.488  1.00 27.23
ATOM   1006  O   SER A 141      39.606  54.445  41.082  1.00 26.78
ATOM   1007  CB  SER A 141      41.084  51.682  41.917  1.00 27.68
ATOM   1008  OG  SER A 141      40.416  50.580  41.342  1.00 34.22
ATOM   1009  N   PHE A 142      38.181  52.719  41.022  1.00 28.20
ATOM   1010  CA  PHE A 142      37.358  53.356  40.005  1.00 28.37
ATOM   1011  C   PHE A 142      36.764  54.646  40.592  1.00 29.26
ATOM   1012  O   PHE A 142      36.883  55.719  39.999  1.00 30.09
ATOM   1013  CB  PHE A 142      36.234  52.414  39.537  1.00 24.61
ATOM   1014  CG  PHE A 142      35.334  53.030  38.506  1.00 22.66
ATOM   1015  CD1 PHE A 142      35.704  53.056  37.170  1.00 24.91
ATOM   1016  CD2 PHE A 142      34.160  53.659  38.880  1.00 23.06
ATOM   1017  CE1 PHE A 142      34.916  53.709  36.216  1.00 25.55
ATOM   1018  CE2 PHE A 142      33.361  54.317  37.939  1.00 23.25
ATOM   1019  CZ  PHE A 142      33.741  54.343  36.603  1.00 24.42
ATOM   1020  N   LEU A 143      36.138  54.536  41.765  1.00 29.21
ATOM   1021  CA  LEU A 143      35.533  55.693  42.419  1.00 29.58
ATOM   1022  C   LEU A 143      36.573  56.775  42.724  1.00 31.10
ATOM   1023  O   LEU A 143      36.294  57.970  42.575  1.00 30.42
ATOM   1024  CB  LEU A 143      34.838  55.280  43.724  1.00 25.57
ATOM   1025  CG  LEU A 143      33.708  54.250  43.609  1.00 26.04
ATOM   1026  CD1 LEU A 143      33.166  53.904  44.986  1.00 24.45
ATOM   1027  CD2 LEU A 143      32.604  54.800  42.741  1.00 22.17
ATOM   1028  N   LYS A 144      37.763  56.353  43.152  1.00 32.14
ATOM   1029  CA  LYS A 144      38.823  57.297  43.485  1.00 35.01
ATOM   1030  C   LYS A 144      39.177  58.189  42.303  1.00 35.23
ATOM   1031  O   LYS A 144      39.359  59.402  42.456  1.00 34.50
ATOM   1032  CB  LYS A 144      40.084  56.564  43.954  1.00 35.66
ATOM   1033  CG  LYS A 144      41.184  57.522  44.393  1.00 37.54
ATOM   1034  CD  LYS A 144      42.369  56.792  44.996  1.00 40.57
ATOM   1035  CE  LYS A 144      43.356  57.779  45.623  1.00 42.58
ATOM   1036  NZ  LYS A 144      44.568  57.104  46.166  1.00 42.12
ATOM   1037  N   ALA A 145      39.264  57.577  41.128  1.00 35.53
ATOM   1038  CA  ALA A 145      39.606  58.293  39.910  1.00 36.00
ATOM   1039  C   ALA A 145      38.424  59.027  39.270  1.00 36.32
ATOM   1040  O   ALA A 145      38.617  60.057  38.614  1.00 36.19
ATOM   1041  CB  ALA A 145      40.216  57.319  38.900  1.00 34.89
ATOM   1042  N   ARG A 146      37.207  58.516  39.465  1.00 35.69
ATOM   1043  CA  ARG A 146      36.025  59.122  38.844  1.00 35.33
ATOM   1044  C   ARG A 146      35.042  59.858  39.754  1.00 34.27
ATOM   1045  O   ARG A 146      34.479  60.869  39.350  1.00 34.18
ATOM   1046  CB  ARG A 146      35.251  58.057  38.054  1.00 37.02
ATOM   1047  CG  ARG A 146      36.074  57.288  37.013  1.00 39.69
ATOM   1048  CD  ARG A 146      36.681  58.222  35.965  1.00 41.68
ATOM   1049  NE  ARG A 146      37.371  57.491  34.901  1.00 45.01
ATOM   1050  CZ  ARG A 146      36.767  56.887  33.877  1.00 45.42
ATOM   1051  NH1 ARG A 146      35.446  56.920  33.758  1.00 45.27
ATOM   1052  NH2 ARG A 146      37.490  56.248  32.965  1.00 44.86
ATOM   1053  N   TYR A 147      34.811  59.351  40.964  1.00 34.28
ATOM   1054  CA  TYR A 147      33.857  59.986  41.887  1.00 33.73
ATOM   1055  C   TYR A 147      34.444  60.129  43.295  1.00 33.71
ATOM   1056  O   TYR A 147      33.956  59.520  44.252  1.00 34.60
ATOM   1057  CB  TYR A 147      32.545  59.169  41.933  1.00 31.72
ATOM   1058  CG  TYR A 147      31.896  58.998  40.577  1.00 29.14
ATOM   1059  CD1 TYR A 147      32.238  57.937  39.738  1.00 27.10
ATOM   1060  CD2 TYR A 147      31.006  59.958  40.093  1.00 29.70
ATOM   1061  CE1 TYR A 147      31.724  57.848  38.448  1.00 28.04
ATOM   1062  CE2 TYR A 147      30.481  59.878  38.806  1.00 30.31
ATOM   1063  CZ  TYR A 147      30.843  58.819  37.986  1.00 30.13
ATOM   1064  OH  TYR A 147      30.316  58.749  36.710  1.00 31.52
ATOM   1065  N   PRO A 148      35.484  60.965  43.440  1.00 34.02
ATOM   1066  CA  PRO A 148      36.164  61.202  44.716  1.00 32.89
ATOM   1067  C   PRO A 148      35.266  61.462  45.917  1.00 32.14
ATOM   1068  O   PRO A 148      35.610  61.081  47.029  1.00 30.68
ATOM   1069  CB  PRO A 148      37.080  62.381  44.401  1.00 35.15
ATOM   1070  CG  PRO A 148      36.299  63.133  43.375  1.00 36.45
ATOM   1071  CD  PRO A 148      35.856  62.006  42.467  1.00 34.24
ATOM   1072  N   TRP A 149      34.114  62.093  45.712  1.00 31.99
ATOM   1073  CA  TRP A 149      33.230  62.367  46.844  1.00 31.60
ATOM   1074  C   TRP A 149      32.745  61.054  47.487  1.00 31.16
ATOM   1075  O   TRP A 149      32.384  61.025  48.668  1.00 30.41
ATOM   1076  CB  TRP A 149      32.040  63.234  46.401  1.00 33.75
ATOM   1077  CG  TRP A 149      30.846  62.464  45.878  1.00 36.45
ATOM   1078  CD1 TRP A 149      29.933  61.748  46.613  1.00 37.12
ATOM   1079  CD2 TRP A 149      30.459  62.315  44.511  1.00 36.56
ATOM   1080  NE1 TRP A 149      29.007  61.158  45.783  1.00 36.75
ATOM   1081  CE2 TRP A 149      29.309  61.485  44.487  1.00 37.35
ATOM   1082  CE3 TRP A 149      30.978  62.789  43.302  1.00 36.96
ATOM   1083  CZ2 TRP A 149      28.663  61.134  43.301  1.00 37.39
ATOM   1084  CZ3 TRP A 149      30.337  62.441  42.123  1.00 38.75
ATOM   1085  CH2 TRP A 149      29.193  61.614  42.133  1.00 38.76
ATOM   1086  N   LEU A 150      32.734  59.977  46.703  1.00 29.90
ATOM   1087  CA  LEU A 150      32.322  58.658  47.193  1.00 30.30
ATOM   1088  C   LEU A 150      33.523  57.933  47.766  1.00 30.54
ATOM   1089  O   LEU A 150      33.425  57.235  48.771  1.00 28.84
ATOM   1090  CB  LEU A 150      31.734  57.814  46.064  1.00 31.81
ATOM   1091  CG  LEU A 150      30.256  58.039  45.755  1.00 33.71
ATOM   1092  CD1 LEU A 150      29.810  57.097  44.640  1.00 31.79
ATOM   1093  CD2 LEU A 150      29.441  57.803  47.033  1.00 32.21
ATOM   1094  N   TYR A 151      34.665  58.103  47.108  1.00 32.12
ATOM   1095  CA  TYR A 151      35.912  57.489  47.549  1.00 32.96
ATOM   1096  C   TYR A 151      36.308  57.916  48.972  1.00 33.34
ATOM   1097  O   TYR A 151      36.693  57.086  49.801  1.00 33.47
ATOM   1098  CB  TYR A 151      37.036  57.868  46.582  1.00 34.09
ATOM   1099  CG  TYR A 151      38.404  57.452  47.058  1.00 35.64
ATOM   1100  CD1 TYR A 151      38.792  56.116  47.020  1.00 36.55
ATOM   1101  CD2 TYR A 151      39.293  58.386  47.601  1.00 36.07
ATOM   1102  CE1 TYR A 151      40.026  55.708  47.514  1.00 37.75
ATOM   1103  CE2 TYR A 151      40.535  57.987  48.101  1.00 37.62
ATOM   1104  CZ  TYR A 151      40.891  56.642  48.053  1.00 38.47
ATOM   1105  OH  TYR A 151      42.103  56.214  48.544  1.00 40.79
ATOM   1106  N   GLN A 152      36.216  59.216  49.246  1.00 34.55
ATOM   1107  CA  GLN A 152      36.593  59.760  50.547  1.00 36.04
ATOM   1108  C   GLN A 152      35.853  59.178  51.747  1.00 35.59
ATOM   1109  O   GLN A 152      36.324  59.287  52.876  1.00 36.39
ATOM   1110  CB  GLN A 152      36.461  61.289  50.543  1.00 37.86
ATOM   1111  CG  GLN A 152      37.745  62.005  50.126  1.00 42.71
ATOM   1112  CD  GLN A 152      37.621  62.734  48.792  1.00 46.43
ATOM   1113  OE1 GLN A 152      36.893  63.730  48.675  1.00 48.28
ATOM   1114  NE2 GLN A 152      38.333  62.240  47.776  1.00 46.58
ATOM   1115  N   VAL A 153      34.704  58.560  51.510  1.00 34.56
ATOM   1116  CA  VAL A 153      33.942  57.954  52.592  1.00 33.88
ATOM   1117  C   VAL A 153      33.669  56.484  52.275  1.00 33.13
ATOM   1118  O   VAL A 153      32.744  55.877  52.817  1.00 32.60
ATOM   1119  CB  VAL A 153      32.607  58.684  52.799  1.00 35.03
ATOM   1120  CG1 VAL A 153      32.870  60.134  53.210  1.00 36.41
ATOM   1121  CG2 VAL A 153      31.786  58.638  51.514  1.00 34.68
ATOM   1122  N   PHE A 154      34.490  55.922  51.393  1.00 31.97
ATOM   1123  CA  PHE A 154      34.362  54.530  50.976  1.00 31.28
ATOM   1124  C   PHE A 154      34.429  53.580  52.165  1.00 31.51
ATOM   1125  O   PHE A 154      33.534  52.758  52.373  1.00 31.03
ATOM   1126  CB  PHE A 154      35.475  54.166  49.985  1.00 29.42
ATOM   1127  CG  PHE A 154      35.322  52.795  49.366  1.00 28.92
ATOM   1128  CD1 PHE A 154      34.411  52.574  48.335  1.00 28.76
ATOM   1129  CD2 PHE A 154      36.081  51.722  49.828  1.00 28.01
ATOM   1130  CE1 PHE A 154      34.258  51.299  47.771  1.00 28.95
ATOM   1131  CE2 PHE A 154      35.941  50.448  49.277  1.00 27.98
ATOM   1132  CZ  PHE A 154      35.028  50.234  48.246  1.00 28.70
ATOM   1133  N   ASP A 155      35.492  53.694  52.947  1.00 30.94
ATOM   1134  CA  ASP A 155      35.667  52.812  54.087  1.00 32.69
ATOM   1135  C   ASP A 155      34.699  53.114  55.206  1.00 31.87
ATOM   1136  O   ASP A 155      34.137  52.205  55.812  1.00 31.41
ATOM   1137  CB  ASP A 155      37.099  52.900  54.622  1.00 36.72
ATOM   1138  CG  ASP A 155      38.122  52.347  53.648  1.00 40.11
ATOM   1139  OD1 ASP A 155      38.434  53.031  52.653  1.00 43.34
ATOM   1140  OD2 ASP A 155      38.609  51.218  53.876  1.00 44.07
ATOM   1141  N   SER A 156      34.497  54.397  55.472  1.00 30.74
ATOM   1142  CA  SER A 156      33.615  54.811  56.552  1.00 29.21
ATOM   1143  C   SER A 156      32.141  54.506  56.388  1.00 27.87
ATOM   1144  O   SER A 156      31.497  54.050  57.330  1.00 29.72
ATOM   1145  CB  SER A 156      33.773  56.312  56.812  1.00 29.36
ATOM   1146  OG  SER A 156      33.555  57.067  55.627  1.00 30.41
ATOM   1147  N   GLU A 157      31.586  54.741  55.207  1.00 24.84
ATOM   1148  CA  GLU A 157      30.157  54.524  55.078  1.00 24.16
ATOM   1149  C   GLU A 157      29.637  53.772  53.873  1.00 21.15
ATOM   1150  O   GLU A 157      28.505  53.321  53.887  1.00 22.62
ATOM   1151  CB  GLU A 157      29.441  55.875  55.151  1.00 26.56
ATOM   1152  CG  GLU A 157      29.976  56.912  54.176  1.00 27.71
ATOM   1153  CD  GLU A 157      29.147  58.196  54.155  1.00 30.65
ATOM   1154  OE1 GLU A 157      28.181  58.292  53.357  1.00 29.88
ATOM   1155  OE2 GLU A 157      29.464  59.112  54.948  1.00 30.10
ATOM   1156  N   VAL A 158      30.445  53.618  52.835  1.00 16.66
ATOM   1157  CA  VAL A 158      29.952  52.958  51.650  1.00 15.44
ATOM   1158  C   VAL A 158      30.098  51.445  51.554  1.00 15.14
ATOM   1159  O   VAL A 158      29.121  50.732  51.295  1.00 15.20
ATOM   1160  CB  VAL A 158      30.580  53.566  50.397  1.00 15.43
ATOM   1161  CG1 VAL A 158      30.174  52.751  49.177  1.00 10.27
ATOM   1162  CG2 VAL A 158      30.149  55.037  50.246  1.00 14.21
ATOM   1163  N   GLU A 159      31.303  50.947  51.784  1.00 15.10
ATOM   1164  CA  GLU A 159      31.530  49.532  51.636  1.00 16.16
ATOM   1165  C   GLU A 159      31.127  48.595  52.745  1.00 16.70
ATOM   1166  O   GLU A 159      31.445  48.803  53.906  1.00 16.41
ATOM   1167  CB  GLU A 159      32.994  49.263  51.288  1.00 18.89
ATOM   1168  CG  GLU A 159      33.292  47.762  51.072  1.00 22.26
ATOM   1169  CD  GLU A 159      34.730  47.487  50.651  1.00 25.07
ATOM   1170  OE1 GLU A 159      35.643  47.608  51.507  1.00 23.19
ATOM   1171  OE2 GLU A 159      34.941  47.161  49.456  1.00 25.21
ATOM   1172  N   LEU A 160      30.412  47.554  52.334  1.00 15.89
ATOM   1173  CA  LEU A 160      30.017  46.475  53.213  1.00 15.15
ATOM   1174  C   LEU A 160      30.776  45.297  52.588  1.00 16.14
ATOM   1175  O   LEU A 160      30.610  44.999  51.404  1.00 16.98
ATOM   1176  CB  LEU A 160      28.517  46.206  53.157  1.00 12.82
ATOM   1177  CG  LEU A 160      28.146  44.970  53.983  1.00 13.16
ATOM   1178  CD1 LEU A 160      28.235  45.330  55.462  1.00 12.66
ATOM   1179  CD2 LEU A 160      26.741  44.470  53.627  1.00 11.13
ATOM   1180  N   MET A 161      31.660  44.666  53.345  1.00 18.58
ATOM   1181  CA  MET A 161      32.412  43.548  52.802  1.00 18.51
ATOM   1182  C   MET A 161      31.658  42.263  53.091  1.00 17.30
ATOM   1183  O   MET A 161      31.330  42.000  54.235  1.00 17.51
ATOM   1184  CB  MET A 161      33.795  43.490  53.443  1.00 22.90
ATOM   1185  CG  MET A 161      34.885  44.164  52.615  1.00 32.22
ATOM   1186  SD  MET A 161      35.259  43.135  51.020  1.00 38.48
ATOM   1187  CE  MET A 161      36.093  41.607  51.833  1.00 39.12
ATOM   1188  N   GLN A 162      31.372  41.461  52.072  1.00 15.38
ATOM   1189  CA  GLN A 162      30.666  40.210  52.329  1.00 17.81
ATOM   1190  C   GLN A 162      31.599  39.221  53.003  1.00 16.22
ATOM   1191  O   GLN A 162      32.809  39.427  53.042  1.00 16.14
ATOM   1192  CB  GLN A 162      30.107  39.596  51.038  1.00 18.70
ATOM   1193  CG  GLN A 162      31.144  39.193  50.017  1.00 20.77
ATOM   1194  CD  GLN A 162      30.516  38.590  48.766  1.00 24.57
ATOM   1195  OE1 GLN A 162      29.382  38.933  48.390  1.00 22.67
ATOM   1196  NE2 GLN A 162      31.258  37.695  48.102  1.00 25.79
ATOM   1197  N   ASN A 163      31.026  38.165  53.566  1.00 17.00
ATOM   1198  CA  ASN A 163      31.819  37.139  54.237  1.00 16.79
ATOM   1199  C   ASN A 163      32.316  36.112  53.225  1.00 16.03
ATOM   1200  O   ASN A 163      31.965  36.157  52.044  1.00 13.41
ATOM   1201  CB  ASN A 163      30.989  36.404  55.289  1.00 17.59
ATOM   1202  CG  ASN A 163      30.663  37.268  56.504  1.00 19.28
ATOM   1203  OD1 ASN A 163      31.544  37.667  57.277  1.00 20.59
ATOM   1204  ND2 ASN A 163      29.392  37.551  56.678  1.00 17.25
ATOM   1205  N   GLN A 164      33.111  35.181  53.733  1.00 15.34
ATOM   1206  CA  GLN A 164      33.687  34.100  52.961  1.00 16.26
ATOM   1207  C   GLN A 164      33.448  32.857  53.792  1.00 14.72
ATOM   1208  O   GLN A 164      33.698  32.883  54.996  1.00 12.25
ATOM   1209  CB  GLN A 164      35.186  34.295  52.830  1.00 20.43
ATOM   1210  CG  GLN A 164      35.677  34.561  51.447  1.00 26.65
ATOM   1211  CD  GLN A 164      37.187  34.639  51.409  1.00 29.94
ATOM   1212  OE1 GLN A 164      37.793  34.664  50.342  1.00 30.75
ATOM   1213  NE2 GLN A 164      37.801  34.683  52.585  1.00 29.35
ATOM   1214  N   VAL A 165      32.958  31.787  53.164  1.00 13.36
ATOM   1215  CA  VAL A 165      32.686  30.536  53.857  1.00 12.48
ATOM   1216  C   VAL A 165      33.438  29.406  53.185  1.00 13.62
ATOM   1217  O   VAL A 165      33.738  29.463  51.988  1.00 12.53
ATOM   1218  CB  VAL A 165      31.190  30.211  53.879  1.00 12.27
ATOM   1219  CG1 VAL A 165      30.450  31.225  54.757  1.00 12.76
ATOM   1220  CG2 VAL A 165      30.643  30.221  52.475  1.00 11.99
ATOM   1221  N   PRO A 166      33.755  28.357  53.953  1.00 14.53
ATOM   1222  CA  PRO A 166      34.495  27.225  53.403  1.00 14.16
ATOM   1223  C   PRO A 166      33.710  26.248  52.544  1.00 13.92
ATOM   1224  O   PRO A 166      32.613  25.835  52.906  1.00 14.35
ATOM   1225  CB  PRO A 166      35.081  26.560  54.653  1.00 14.62
ATOM   1226  CG  PRO A 166      34.020  26.803  55.697  1.00 15.43
ATOM   1227  CD  PRO A 166      33.595  28.239  55.419  1.00 14.56
ATOM   1228  N   LYS A 167      34.277  25.899  51.392  1.00 13.51
ATOM   1229  CA  LYS A 167      33.667  24.903  50.509  1.00 14.92
ATOM   1230  C   LYS A 167      33.823  23.588  51.292  1.00 14.43
ATOM   1231  O   LYS A 167      34.832  23.389  51.966  1.00 13.09
ATOM   1232  CB  LYS A 167      34.434  24.834  49.184  1.00 16.11
ATOM   1233  CG  LYS A 167      34.486  26.162  48.423  1.00 13.38
ATOM   1234  CD  LYS A 167      35.284  25.997  47.124  1.00 14.77
ATOM   1235  CE  LYS A 167      35.271  27.298  46.318  1.00 14.33
ATOM   1236  NZ  LYS A 167      36.301  27.357  45.262  1.00 13.70
ATOM   1237  N   ILE A 168      32.830  22.712  51.235  1.00 12.91
ATOM   1238  CA  ILE A 168      32.894  21.475  51.997  1.00 16.04
ATOM   1239  C   ILE A 168      32.808  20.230  51.119  1.00 16.19
ATOM   1240  O   ILE A 168      32.037  20.181  50.164  1.00 17.22
ATOM   1241  CB  ILE A 168      31.764  21.431  53.083  1.00 16.40
ATOM   1242  CG1 ILE A 168      30.387  21.503  52.430  1.00 14.40
ATOM   1243  CG2 ILE A 168      31.916  22.605  54.051  1.00 18.72
ATOM   1244  CD1 ILE A 168      29.230  21.385  53.414  1.00 13.77
ATOM   1245  N   LEU A 169      33.619  19.233  51.447  1.00 16.75
ATOM   1246  CA  LEU A 169      33.656  17.983  50.689  1.00 17.70
ATOM   1247  C   LEU A 169      32.263  17.374  50.659  1.00 17.09
ATOM   1248  O   LEU A 169      31.592  17.282  51.687  1.00 16.81
ATOM   1249  CB  LEU A 169      34.661  17.013  51.327  1.00 15.45
ATOM   1250  CG  LEU A 169      36.094  17.568  51.372  1.00 18.66
ATOM   1251  CD1 LEU A 169      37.019  16.630  52.149  1.00 17.27
ATOM   1252  CD2 LEU A 169      36.608  17.764  49.949  1.00 17.85
ATOM   1253  N   GLN A 170      31.834  16.977  49.469  1.00 19.53
ATOM   1254  CA  GLN A 170      30.516  16.385  49.272  1.00 23.31
ATOM   1255  C   GLN A 170      30.201  15.162  50.126  1.00 25.80
ATOM   1256  O   GLN A 170      29.061  14.970  50.543  1.00 26.47
ATOM   1257  CB  GLN A 170      30.318  16.030  47.799  1.00 22.67
ATOM   1258  CG  GLN A 170      29.974  17.233  46.913  1.00 25.94
ATOM   1259  CD  GLN A 170      29.417  16.814  45.564  1.00 27.33
ATOM   1260  OE1 GLN A 170      28.863  15.719  45.428  1.00 28.98
ATOM   1261  NE2 GLN A 170      29.542  17.687  44.565  1.00 27.43
ATOM   1262  N   ASP A 171      31.205  14.340  50.401  1.00 29.36
ATOM   1263  CA  ASP A 171      30.976  13.133  51.188  1.00 32.23
ATOM   1264  C   ASP A 171      30.780  13.361  52.668  1.00 31.80
ATOM   1265  O   ASP A 171      29.683  13.187  53.198  1.00 33.00
ATOM   1266  CB  ASP A 171      32.131  12.151  51.008  1.00 35.28
ATOM   1267  CG  ASP A 171      32.239  11.648  49.590  1.00 39.44
ATOM   1268  OD1 ASP A 171      31.165  11.424  48.975  1.00 40.65
ATOM   1269  OD2 ASP A 171      33.385  11.469  49.101  1.00 39.20
ATOM   1270  N   THR A 172      31.865  13.759  53.319  1.00 29.82
ATOM   1271  CA  THR A 172      31.914  13.975  54.753  1.00 25.83
ATOM   1272  C   THR A 172      31.485  15.355  55.243  1.00 25.03
ATOM   1273  O   THR A 172      31.276  15.551  56.445  1.00 25.83
ATOM   1274  CB  THR A 172      33.333  13.736  55.224  1.00 25.94
ATOM   1275  OG1 THR A 172      34.156  14.795  54.732  1.00 24.45
ATOM   1276  CG2 THR A 172      33.868  12.414  54.647  1.00 24.78
ATOM   1277  N   LEU A 173      31.368  16.316  54.333  1.00 21.82
ATOM   1278  CA  LEU A 173      30.997  17.680  54.712  1.00 21.51
ATOM   1279  C   LEU A 173      32.106  18.354  55.500  1.00 21.35
ATOM   1280  O   LEU A 173      31.842  19.293  56.259  1.00 21.58
ATOM   1281  CB  LEU A 173      29.710  17.694  55.544  1.00 19.78
ATOM   1282  CG  LEU A 173      28.541  17.007  54.858  1.00 19.48
ATOM   1283  CD1 LEU A 173      27.264  17.224  55.674  1.00 20.90
ATOM   1284  CD2 LEU A 173      28.394  17.551  53.427  1.00 18.47
ATOM   1285  N   GLU A 174      33.335  17.858  55.337  1.00 20.34
ATOM   1286  CA  GLU A 174      34.497  18.433  56.014  1.00 20.19
ATOM   1287  C   GLU A 174      34.965  19.589  55.150  1.00 17.88
ATOM   1288  O   GLU A 174      34.723  19.600  53.940  1.00 17.05
ATOM   1289  CB  GLU A 174      35.642  17.422  56.101  1.00 21.97
ATOM   1290  CG  GLU A 174      35.342  16.164  56.882  1.00 28.43
ATOM   1291  CD  GLU A 174      36.401  15.076  56.669  1.00 31.84
ATOM   1292  OE1 GLU A 174      36.696  14.732  55.496  1.00 34.09
ATOM   1293  OE2 GLU A 174      36.930  14.558  57.680  1.00 33.56
ATOM   1294  N   PRO A 175      35.643  20.577  55.741  1.00 16.95
ATOM   1295  CA  PRO A 175      36.084  21.671  54.874  1.00 18.24
ATOM   1296  C   PRO A 175      37.120  21.138  53.910  1.00 19.21
ATOM   1297  O   PRO A 175      37.969  20.341  54.300  1.00 21.05
ATOM   1298  CB  PRO A 175      36.655  22.703  55.860  1.00 16.43
ATOM   1299  CG  PRO A 175      37.012  21.898  57.060  1.00 15.90
ATOM   1300  CD  PRO A 175      35.893  20.889  57.151  1.00 16.94
ATOM   1301  N   ALA A 176      37.041  21.539  52.647  1.00 20.10
ATOM   1302  CA  ALA A 176      37.999  21.064  51.654  1.00 20.80
ATOM   1303  C   ALA A 176      39.323  21.828  51.696  1.00 22.27
ATOM   1304  O   ALA A 176      39.363  23.021  52.018  1.00 22.24
ATOM   1305  CB  ALA A 176      37.385  21.151  50.264  1.00 20.52
ATOM   1306  N   ALA A 177      40.404  21.125  51.372  1.00 21.59
ATOM   1307  CA  ALA A 177      41.733  21.723  51.330  1.00 22.36
ATOM   1308  C   ALA A 177      42.235  21.686  49.876  1.00 22.42
ATOM   1309  O   ALA A 177      41.915  20.768  49.118  1.00 24.35
ATOM   1310  CB  ALA A 177      42.701  20.954  52.261  1.00 18.72
ATOM   1311  N   TRP A 178      42.990  22.699  49.484  1.00 21.21
ATOM   1312  CA  TRP A 178      43.531  22.754  48.133  1.00 24.84
ATOM   1313  C   TRP A 178      44.943  23.313  48.256  1.00 25.17
ATOM   1314  O   TRP A 178      45.139  24.535  48.206  1.00 25.76
ATOM   1315  CB  TRP A 178      42.684  23.671  47.236  1.00 24.98
ATOM   1316  CG  TRP A 178      43.018  23.567  45.770  1.00 25.38
ATOM   1317  CD1 TRP A 178      43.281  24.596  44.918  1.00 27.56
ATOM   1318  CD2 TRP A 178      43.135  22.367  44.995  1.00 25.73
ATOM   1319  NE1 TRP A 178      43.558  24.115  43.663  1.00 27.69
ATOM   1320  CE2 TRP A 178      43.474  22.750  43.681  1.00 25.27
ATOM   1321  CE3 TRP A 178      42.978  21.003  45.282  1.00 25.54
ATOM   1322  CZ2 TRP A 178      43.672  21.817  42.651  1.00 27.20
ATOM   1323  CZ3 TRP A 178      43.172  20.070  44.252  1.00 25.12
ATOM   1324  CH2 TRP A 178      43.514  20.485  42.957  1.00 25.99
ATOM   1325  N   ALA A 179      45.908  22.407  48.434  1.00 23.85
ATOM   1326  CA  ALA A 179      47.319  22.760  48.591  1.00 25.40
ATOM   1327  C   ALA A 179      47.827  23.736  47.537  1.00 25.09
ATOM   1328  O   ALA A 179      48.497  24.709  47.854  1.00 27.08
ATOM   1329  CB  ALA A 179      48.177  21.487  48.577  1.00 23.21
ATOM   1330  N   GLU A 180      47.504  23.470  46.283  1.00 27.00
ATOM   1331  CA  GLU A 180      47.936  24.317  45.177  1.00 28.85
ATOM   1332  C   GLU A 180      47.564  25.798  45.325  1.00 27.33
ATOM   1333  O   GLU A 180      48.359  26.688  45.005  1.00 26.49
ATOM   1334  CB  GLU A 180      47.349  23.772  43.878  1.00 32.52
ATOM   1335  CG  GLU A 180      47.937  24.373  42.627  1.00 38.79
ATOM   1336  CD  GLU A 180      47.244  23.874  41.366  1.00 42.46
ATOM   1337  OE1 GLU A 180      46.996  22.646  41.262  1.00 44.02
ATOM   1338  OE2 GLU A 180      46.960  24.713  40.478  1.00 43.12
ATOM   1339  N   ASN A 181      46.355  26.063  45.807  1.00 26.05
ATOM   1340  CA  ASN A 181      45.883  27.435  45.972  1.00 23.20
ATOM   1341  C   ASN A 181      44.824  27.404  47.067  1.00 21.60
ATOM   1342  O   ASN A 181      43.634  27.255  46.796  1.00 20.10
ATOM   1343  CB  ASN A 181      45.264  27.928  44.656  1.00 25.12
ATOM   1344  CG  ASN A 181      44.984  29.434  44.649  1.00 27.73
ATOM   1345  OD1 ASN A 181      44.843  30.072  45.695  1.00 30.67
ATOM   1346  ND2 ASN A 181      44.883  29.999  43.456  1.00 28.54
ATOM   1347  N   PRO A 182      45.252  27.521  48.327  1.00 20.65
ATOM   1348  CA  PRO A 182      44.313  27.499  49.447  1.00 19.29
ATOM   1349  C   PRO A 182      43.194  28.549  49.383  1.00 19.45
ATOM   1350  O   PRO A 182      42.138  28.369  49.982  1.00 18.57
ATOM   1351  CB  PRO A 182      45.235  27.662  50.657  1.00 21.37
ATOM   1352  CG  PRO A 182      46.488  26.885  50.207  1.00 20.77
ATOM   1353  CD  PRO A 182      46.650  27.435  48.803  1.00 20.79
ATOM   1354  N   ALA A 183      43.403  29.643  48.662  1.00 19.44
ATOM   1355  CA  ALA A 183      42.344  30.648  48.565  1.00 20.08
ATOM   1356  C   ALA A 183      41.098  30.023  47.915  1.00 19.16
ATOM   1357  O   ALA A 183      39.989  30.545  48.064  1.00 18.89
ATOM   1358  CB  ALA A 183      42.821  31.846  47.751  1.00 18.99
ATOM   1359  N   TYR A 184      41.285  28.912  47.194  1.00 18.32
ATOM   1360  CA  TYR A 184      40.167  28.213  46.548  1.00 18.32
ATOM   1361  C   TYR A 184      39.341  27.386  47.540  1.00 17.45
ATOM   1362  O   TYR A 184      38.365  26.757  47.157  1.00 16.75
ATOM   1363  CB  TYR A 184      40.663  27.306  45.414  1.00 19.49
ATOM   1364  CG  TYR A 184      41.055  28.050  44.147  1.00 23.35
ATOM   1365  CD1 TYR A 184      41.557  27.364  43.035  1.00 25.28
ATOM   1366  CD2 TYR A 184      40.944  29.443  44.065  1.00 26.50
ATOM   1367  CE1 TYR A 184      41.942  28.047  41.872  1.00 26.98
ATOM   1368  CE2 TYR A 184      41.327  30.136  42.915  1.00 27.80
ATOM   1369  CZ  TYR A 184      41.826  29.431  41.822  1.00 28.86
ATOM   1370  OH  TYR A 184      42.220  30.116  40.693  1.00 30.81
ATOM   1371  N   GLU A 185      39.732  27.410  48.813  1.00 17.54
ATOM   1372  CA  GLU A 185      39.013  26.692  49.873  1.00 17.34
ATOM   1373  C   GLU A 185      37.871  27.549  50.424  1.00 16.91
ATOM   1374  O   GLU A 185      37.108  27.097  51.271  1.00 17.38
ATOM   1375  CB  GLU A 185      39.965  26.335  51.017  1.00 14.81
ATOM   1376  CG  GLU A 185      41.072  25.368  50.607  1.00 17.09
ATOM   1377  CD  GLU A 185      42.232  25.358  51.590  1.00 18.19
ATOM   1378  OE1 GLU A 185      42.083  25.947  52.681  1.00 16.55
ATOM   1379  OE2 GLU A 185      43.289  24.762  51.269  1.00 19.78
ATOM   1380  N   TRP A 186      37.751  28.779  49.932  1.00 16.79
ATOM   1381  CA  TRP A 186      36.694  29.688  50.384  1.00 17.37
ATOM   1382  C   TRP A 186      35.828  30.200  49.240  1.00 18.37
ATOM   1383  O   TRP A 186      36.323  30.457  48.141  1.00 19.55
ATOM   1384  CB  TRP A 186      37.303  30.889  51.108  1.00 16.43
ATOM   1385  CG  TRP A 186      38.175  30.501  52.246  1.00 15.95
ATOM   1386  CD1 TRP A 186      39.506  30.161  52.196  1.00 15.51
ATOM   1387  CD2 TRP A 186      37.778  30.365  53.613  1.00 14.06
ATOM   1388  NE1 TRP A 186      39.951  29.817  53.449  1.00 16.75
ATOM   1389  CE2 TRP A 186      38.907  29.923  54.335  1.00 14.56
ATOM   1390  CE3 TRP A 186      36.570  30.552  54.293  1.00 12.10
ATOM   1391  CZ2 TRP A 186      38.868  29.694  55.705  1.00 17.20
ATOM   1392  CZ3 TRP A 186      36.530  30.324  55.656  1.00 12.52
ATOM   1393  CH2 TRP A 186      37.665  29.888  56.346  1.00 16.94
ATOM   1394  N   ALA A 187      34.535  30.356  49.494  1.00 19.84
ATOM   1395  CA  ALA A 187      33.630  30.864  48.464  1.00 19.60
ATOM   1396  C   ALA A 187      32.641  31.878  49.020  1.00 20.25
ATOM   1397  O   ALA A 187      32.333  31.883  50.210  1.00 17.60
ATOM   1398  CB  ALA A 187      32.871  29.722  47.829  1.00 19.55
ATOM   1399  N   PRO A 188      32.142  32.775  48.158  1.00 22.94
ATOM   1400  CA  PRO A 188      31.177  33.759  48.648  1.00 22.40
ATOM   1401  C   PRO A 188      29.947  32.961  49.078  1.00 21.03
ATOM   1402  O   PRO A 188      29.715  31.855  48.584  1.00 20.25
ATOM   1403  CB  PRO A 188      30.937  34.641  47.421  1.00 24.33
ATOM   1404  CG  PRO A 188      31.126  33.695  46.281  1.00 23.77
ATOM   1405  CD  PRO A 188      32.366  32.935  46.710  1.00 24.23
ATOM   1406  N   PRO A 189      29.159  33.493  50.025  1.00 20.28
ATOM   1407  CA  PRO A 189      27.964  32.772  50.492  1.00 18.54
ATOM   1408  C   PRO A 189      26.627  33.172  49.859  1.00 16.58
ATOM   1409  O   PRO A 189      25.569  32.838  50.384  1.00 17.51
ATOM   1410  CB  PRO A 189      27.993  33.034  51.993  1.00 18.95
ATOM   1411  CG  PRO A 189      28.469  34.457  52.043  1.00 20.60
ATOM   1412  CD  PRO A 189      29.535  34.569  50.962  1.00 17.96
ATOM   1413  N   GLY A 190      26.672  33.857  48.722  1.00 15.54
ATOM   1414  CA  GLY A 190      25.436  34.295  48.083  1.00 13.84
ATOM   1415  C   GLY A 190      25.053  35.678  48.583  1.00 12.23
ATOM   1416  O   GLY A 190      25.561  36.116  49.633  1.00 12.62
ATOM   1417  N   HIS A 191      24.205  36.402  47.840  1.00 12.85
ATOM   1418  CA  HIS A 191      23.867  37.772  48.302  1.00 12.81
ATOM   1419  C   HIS A 191      23.044  37.734  49.591  1.00 13.71
ATOM   1420  O   HIS A 191      22.924  38.725  50.295  1.00 13.17
ATOM   1421  CB  HIS A 191      23.176  38.640  47.235  1.00 13.94
ATOM   1422  CG  HIS A 191      22.188  37.862  46.355  1.00 11.24
ATOM   1423  ND1 HIS A 191      20.982  37.386  46.814  1.00 13.40
ATOM   1424  CD2 HIS A 191      22.283  37.473  45.066  1.00  8.24
ATOM   1425  CE1 HIS A 191      20.368  36.736  45.843  1.00 14.11
ATOM   1426  NE2 HIS A 191      21.137  36.776  44.769  1.00 10.86
ATOM   1427  N   GLY A 192      22.461  36.583  49.905  1.00 13.13
ATOM   1428  CA  GLY A 192      21.679  36.432  51.121  1.00 12.46
ATOM   1429  C   GLY A 192      22.573  36.714  52.324  1.00 13.94
ATOM   1430  O   GLY A 192      22.108  36.873  53.449  1.00 12.83
ATOM   1431  N   ASP A 193      23.880  36.766  52.074  1.00 14.37
ATOM   1432  CA  ASP A 193      24.880  37.053  53.104  1.00 13.00
ATOM   1433  C   ASP A 193      24.840  38.510  53.578  1.00 12.21
ATOM   1434  O   ASP A 193      25.457  38.856  54.583  1.00 12.88
ATOM   1435  CB  ASP A 193      26.273  36.757  52.557  1.00 14.17
ATOM   1436  CG  ASP A 193      27.360  37.050  53.557  1.00 17.24
ATOM   1437  OD1 ASP A 193      28.244  37.892  53.265  1.00 17.86
ATOM   1438  OD2 ASP A 193      27.328  36.437  54.643  1.00 17.37
ATOM   1439  N   ILE A 194      24.141  39.372  52.844  1.00 11.35
ATOM   1440  CA  ILE A 194      24.050  40.780  53.225  1.00  9.81
ATOM   1441  C   ILE A 194      23.537  40.956  54.665  1.00 10.86
ATOM   1442  O   ILE A 194      24.086  41.738  55.435  1.00 11.03
ATOM   1443  CB  ILE A 194      23.107  41.567  52.252  1.00 11.51
ATOM   1444  CG1 ILE A 194      22.981  43.028  52.704  1.00 10.31
ATOM   1445  CG2 ILE A 194      21.722  40.933  52.210  1.00  7.33
ATOM   1446  CD1 ILE A 194      22.292  43.931  51.694  1.00 12.23
ATOM   1447  N   TYR A 195      22.494  40.220  55.039  1.00 12.17
ATOM   1448  CA  TYR A 195      21.935  40.360  56.382  1.00 12.72
ATOM   1449  C   TYR A 195      22.968  39.985  57.436  1.00 13.44
ATOM   1450  O   TYR A 195      23.159  40.686  58.432  1.00 13.89
ATOM   1451  CB  TYR A 195      20.682  39.488  56.537  1.00 13.08
ATOM   1452  CG  TYR A 195      19.640  39.704  55.458  1.00 13.44
ATOM   1453  CD1 TYR A 195      19.413  38.737  54.488  1.00 13.59
ATOM   1454  CD2 TYR A 195      18.914  40.893  55.383  1.00 13.09
ATOM   1455  CE1 TYR A 195      18.498  38.941  53.476  1.00 13.79
ATOM   1456  CE2 TYR A 195      17.991  41.107  54.357  1.00 12.75
ATOM   1457  CZ  TYR A 195      17.789  40.132  53.413  1.00 12.08
ATOM   1458  OH  TYR A 195      16.886  40.331  52.390  1.00 11.61
ATOM   1459  N   THR A 196      23.632  38.867  57.195  1.00 14.37
ATOM   1460  CA  THR A 196      24.658  38.359  58.083  1.00 13.83
ATOM   1461  C   THR A 196      25.815  39.346  58.223  1.00 13.05
ATOM   1462  O   THR A 196      26.262  39.614  59.332  1.00 15.30
ATOM   1463  CB  THR A 196      25.223  37.036  57.530  1.00 16.36
ATOM   1464  OG1 THR A 196      24.143  36.150  57.236  1.00 15.22
ATOM   1465  CG2 THR A 196      26.178  36.395  58.525  1.00 14.20
ATOM   1466  N   ALA A 197      26.315  39.863  57.099  1.00 12.65
ATOM   1467  CA  ALA A 197      27.449  40.802  57.130  1.00 13.38
ATOM   1468  C   ALA A 197      27.061  42.120  57.780  1.00 11.66
ATOM   1469  O   ALA A 197      27.866  42.721  58.494  1.00 11.02
ATOM   1470  CB  ALA A 197      27.985  41.066  55.717  1.00 11.97
ATOM   1471  N   LEU A 198      25.835  42.570  57.506  1.00 11.64
ATOM   1472  CA  LEU A 198      25.334  43.816  58.080  1.00  8.88
ATOM   1473  C   LEU A 198      25.280  43.660  59.579  1.00  9.07
ATOM   1474  O   LEU A 198      25.669  44.552  60.315  1.00  9.80
ATOM   1475  CB  LEU A 198      23.924  44.131  57.579  1.00  8.69
ATOM   1476  CG  LEU A 198      23.753  44.840  56.230  1.00 11.34
ATOM   1477  CD1 LEU A 198      22.279  45.002  55.923  1.00  7.54
ATOM   1478  CD2 LEU A 198      24.431  46.196  56.275  1.00  7.63
ATOM   1479  N   TYR A 199      24.797  42.506  60.025  1.00 11.08
ATOM   1480  CA  TYR A 199      24.646  42.232  61.446  1.00 10.86
ATOM   1481  C   TYR A 199      25.970  42.024  62.176  1.00 12.29
ATOM   1482  O   TYR A 199      26.249  42.679  63.192  1.00  9.03
ATOM   1483  CB  TYR A 199      23.780  40.992  61.639  1.00  9.65
ATOM   1484  CG  TYR A 199      23.463  40.685  63.090  1.00 10.94
ATOM   1485  CD1 TYR A 199      22.339  41.222  63.697  1.00 11.05
ATOM   1486  CD2 TYR A 199      24.297  39.861  63.856  1.00  9.80
ATOM   1487  CE1 TYR A 199      22.038  40.953  65.026  1.00 10.97
ATOM   1488  CE2 TYR A 199      24.003  39.582  65.193  1.00 10.07
ATOM   1489  CZ  TYR A 199      22.865  40.134  65.766  1.00 11.30
ATOM   1490  OH  TYR A 199      22.527  39.861  67.068  1.00 10.54
ATOM   1491  N   GLY A 200      26.776  41.110  61.636  1.00 12.74
ATOM   1492  CA  GLY A 200      28.044  40.765  62.242  1.00 14.99
ATOM   1493  C   GLY A 200      29.080  41.855  62.354  1.00 16.26
ATOM   1494  O   GLY A 200      29.839  41.895  63.325  1.00 18.39
ATOM   1495  N   SER A 201      29.116  42.742  61.369  1.00 16.20
ATOM   1496  CA  SER A 201      30.092  43.817  61.373  1.00 17.93
ATOM   1497  C   SER A 201      29.681  44.923  62.322  1.00 18.15
ATOM   1498  O   SER A 201      30.483  45.807  62.623  1.00 20.83
ATOM   1499  CB  SER A 201      30.249  44.394  59.958  1.00 17.70
ATOM   1500  OG  SER A 201      29.003  44.840  59.446  1.00 21.45
ATOM   1501  N   GLY A 202      28.434  44.874  62.779  1.00 18.95
ATOM   1502  CA  GLY A 202      27.914  45.900  63.672  1.00 18.70
ATOM   1503  C   GLY A 202      27.341  47.080  62.893  1.00 18.45
ATOM   1504  O   GLY A 202      26.895  48.070  63.462  1.00 17.89
ATOM   1505  N   LYS A 203      27.345  46.977  61.573  1.00 18.64
ATOM   1506  CA  LYS A 203      26.844  48.066  60.750  1.00 20.32
ATOM   1507  C   LYS A 203      25.320  48.195  60.853  1.00 19.71
ATOM   1508  O   LYS A 203      24.783  49.306  60.910  1.00 18.79
ATOM   1509  CB  LYS A 203      27.296  47.864  59.290  1.00 23.55
ATOM   1510  CG  LYS A 203      26.802  48.932  58.318  1.00 27.17
ATOM   1511  CD  LYS A 203      27.360  50.328  58.607  1.00 30.43
ATOM   1512  CE  LYS A 203      28.829  50.432  58.231  1.00 33.71
ATOM   1513  NZ  LYS A 203      29.267  51.851  58.112  1.00 34.71
ATOM   1514  N   LEU A 204      24.621  47.062  60.896  1.00 18.29
ATOM   1515  CA  LEU A 204      23.172  47.096  61.007  1.00 15.66
ATOM   1516  C   LEU A 204      22.779  47.859  62.265  1.00 15.60
ATOM   1517  O   LEU A 204      21.912  48.733  62.227  1.00 15.59
ATOM   1518  CB  LEU A 204      22.588  45.673  61.043  1.00 13.87
ATOM   1519  CG  LEU A 204      21.062  45.628  61.219  1.00 13.19
ATOM   1520  CD1 LEU A 204      20.405  46.458  60.120  1.00  8.89
ATOM   1521  CD2 LEU A 204      20.544  44.179  61.168  1.00 10.74
ATOM   1522  N   GLN A 205      23.416  47.535  63.387  1.00 16.96
ATOM   1523  CA  GLN A 205      23.110  48.217  64.638  1.00 17.57
ATOM   1524  C   GLN A 205      23.431  49.712  64.560  1.00 18.06
ATOM   1525  O   GLN A 205      22.677  50.551  65.060  1.00 17.20
ATOM   1526  CB  GLN A 205      23.896  47.612  65.801  1.00 20.37
ATOM   1527  CG  GLN A 205      23.602  48.374  67.098  1.00 24.60
ATOM   1528  CD  GLN A 205      23.993  47.629  68.357  1.00 28.12
ATOM   1529  OE1 GLN A 205      25.171  47.619  68.747  1.00 28.49
ATOM   1530  NE2 GLN A 205      23.002  46.990  69.006  1.00 24.08
ATOM   1531  N   GLU A 206      24.558  50.026  63.933  1.00 17.68
ATOM   1532  CA  GLU A 206      25.022  51.398  63.774  1.00 19.87
ATOM   1533  C   GLU A 206      24.026  52.254  62.973  1.00 18.82
ATOM   1534  O   GLU A 206      23.714  53.382  63.356  1.00 17.25
ATOM   1535  CB  GLU A 206      26.372  51.379  63.065  1.00 22.99
ATOM   1536  CG  GLU A 206      27.224  52.605  63.274  1.00 30.71
ATOM   1537  CD  GLU A 206      28.462  52.582  62.401  1.00 35.14
ATOM   1538  OE1 GLU A 206      28.417  53.177  61.299  1.00 36.86
ATOM   1539  OE2 GLU A 206      29.466  51.949  62.809  1.00 37.00
ATOM   1540  N   LEU A 207      23.530  51.708  61.866  1.00 16.86
ATOM   1541  CA  LEU A 207      22.580  52.426  61.028  1.00 16.85
ATOM   1542  C   LEU A 207      21.321  52.703  61.818  1.00 14.76
ATOM   1543  O   LEU A 207      20.806  53.818  61.810  1.00 15.97
ATOM   1544  CB  LEU A 207      22.243  51.616  59.776  1.00 15.76
ATOM   1545  CG  LEU A 207      23.351  51.476  58.737  1.00 17.01
ATOM   1546  CD1 LEU A 207      22.948  50.422  57.700  1.00 14.75
ATOM   1547  CD2 LEU A 207      23.613  52.824  58.070  1.00 14.67
ATOM   1548  N   VAL A 208      20.828  51.692  62.517  1.00 13.24
ATOM   1549  CA  VAL A 208      19.646  51.892  63.320  1.00 12.97
ATOM   1550  C   VAL A 208      19.877  52.921  64.450  1.00 14.15
ATOM   1551  O   VAL A 208      18.958  53.661  64.803  1.00 14.43
ATOM   1552  CB  VAL A 208      19.146  50.581  63.921  1.00 11.91
ATOM   1553  CG1 VAL A 208      18.003  50.879  64.864  1.00  8.02
ATOM   1554  CG2 VAL A 208      18.675  49.639  62.798  1.00  9.48
ATOM   1555  N   GLU A 209      21.081  52.964  65.021  1.00 14.39
ATOM   1556  CA  GLU A 209      21.370  53.936  66.081  1.00 15.82
ATOM   1557  C   GLU A 209      21.361  55.356  65.492  1.00 17.90
ATOM   1558  O   GLU A 209      20.908  56.309  66.130  1.00 18.37
ATOM   1559  CB  GLU A 209      22.740  53.675  66.716  1.00 11.80
ATOM   1560  CG  GLU A 209      22.858  52.342  67.455  1.00 15.45
ATOM   1561  CD  GLU A 209      24.269  52.060  67.923  1.00 12.83
ATOM   1562  OE1 GLU A 209      25.212  52.505  67.259  1.00 16.51
ATOM   1563  OE2 GLU A 209      24.445  51.384  68.946  1.00 18.11
ATOM   1564  N   GLN A 210      21.848  55.487  64.266  1.00 17.29
ATOM   1565  CA  GLN A 210      21.904  56.788  63.620  1.00 20.11
ATOM   1566  C   GLN A 210      20.567  57.247  63.060  1.00 19.72
ATOM   1567  O   GLN A 210      20.492  58.309  62.457  1.00 19.66
ATOM   1568  CB  GLN A 210      22.966  56.779  62.514  1.00 20.87
ATOM   1569  CG  GLN A 210      24.386  56.654  63.046  1.00 25.10
ATOM   1570  CD  GLN A 210      25.413  56.409  61.949  1.00 28.74
ATOM   1571  OE1 GLN A 210      25.092  56.429  60.756  1.00 30.41
ATOM   1572  NE2 GLN A 210      26.660  56.179  62.349  1.00 30.10
ATOM   1573  N   GLY A 211      19.516  56.448  63.250  1.00 20.73
ATOM   1574  CA  GLY A 211      18.198  56.838  62.765  1.00 19.01
ATOM   1575  C   GLY A 211      17.738  56.333  61.400  1.00 19.98
ATOM   1576  O   GLY A 211      16.720  56.801  60.875  1.00 20.15
ATOM   1577  N   TYR A 212      18.472  55.405  60.796  1.00 18.21
ATOM   1578  CA  TYR A 212      18.044  54.877  59.507  1.00 17.97
ATOM   1579  C   TYR A 212      16.965  53.860  59.803  1.00 18.34
ATOM   1580  O   TYR A 212      17.077  53.102  60.772  1.00 18.75
ATOM   1581  CB  TYR A 212      19.219  54.233  58.755  1.00 18.20
ATOM   1582  CG  TYR A 212      20.241  55.263  58.336  1.00 18.67
ATOM   1583  CD1 TYR A 212      21.376  55.499  59.098  1.00 19.55
ATOM   1584  CD2 TYR A 212      20.014  56.080  57.236  1.00 21.11
ATOM   1585  CE1 TYR A 212      22.269  56.532  58.772  1.00 20.44
ATOM   1586  CE2 TYR A 212      20.896  57.122  56.902  1.00 22.83
ATOM   1587  CZ  TYR A 212      22.015  57.338  57.675  1.00 22.10
ATOM   1588  OH  TYR A 212      22.877  58.351  57.341  1.00 23.55
ATOM   1589  N   ARG A 213      15.915  53.841  58.988  1.00 17.84
ATOM   1590  CA  ARG A 213      14.813  52.917  59.219  1.00 18.83
ATOM   1591  C   ARG A 213      14.533  51.970  58.056  1.00 19.61
ATOM   1592  O   ARG A 213      13.986  50.875  58.253  1.00 19.01
ATOM   1593  CB  ARG A 213      13.559  53.717  59.581  1.00 20.39
ATOM   1594  CG  ARG A 213      13.705  54.495  60.907  1.00 22.90
ATOM   1595  CD  ARG A 213      13.878  53.526  62.085  1.00 24.42
ATOM   1596  NE  ARG A 213      14.163  54.183  63.365  1.00 24.16
ATOM   1597  CZ  ARG A 213      15.379  54.356  63.892  1.00 25.56
ATOM   1598  NH1 ARG A 213      16.479  53.924  63.266  1.00 22.24
ATOM   1599  NH2 ARG A 213      15.493  54.964  65.069  1.00 25.32
ATOM   1600  N   TYR A 214      14.923  52.376  56.851  1.00 18.21
ATOM   1601  CA  TYR A 214      14.696  51.548  55.668  1.00 16.81
ATOM   1602  C   TYR A 214      15.933  51.394  54.812  1.00 15.90
ATOM   1603  O   TYR A 214      16.825  52.244  54.800  1.00 16.62
ATOM   1604  CB  TYR A 214      13.609  52.153  54.773  1.00 16.63
ATOM   1605  CG  TYR A 214      12.194  52.088  55.309  1.00 18.06
ATOM   1606  CD1 TYR A 214      11.624  53.177  55.971  1.00 19.05
ATOM   1607  CD2 TYR A 214      11.405  50.961  55.103  1.00 18.15
ATOM   1608  CE1 TYR A 214      10.299  53.149  56.407  1.00 17.32
ATOM   1609  CE2 TYR A 214      10.085  50.922  55.537  1.00 19.60
ATOM   1610  CZ  TYR A 214       9.537  52.024  56.188  1.00 19.80
ATOM   1611  OH  TYR A 214       8.228  51.983  56.631  1.00 21.06
ATOM   1612  N   MET A 215      15.982  50.299  54.079  1.00 14.99
ATOM   1613  CA  MET A 215      17.079  50.081  53.170  1.00 13.12
ATOM   1614  C   MET A 215      16.514  49.580  51.846  1.00 12.58
ATOM   1615  O   MET A 215      15.681  48.677  51.809  1.00 13.17
ATOM   1616  CB  MET A 215      18.076  49.065  53.724  1.00 12.60
ATOM   1617  CG  MET A 215      19.224  48.791  52.748  1.00 13.81
ATOM   1618  SD  MET A 215      20.522  47.495  53.414  1.00 19.77
ATOM   1619  CE  MET A 215      21.607  48.692  54.515  1.00 15.83
ATOM   1620  N   PHE A 216      16.957  50.187  50.758  1.00 12.54
ATOM   1621  CA  PHE A 216      16.517  49.771  49.443  1.00 12.58
ATOM   1622  C   PHE A 216      17.703  49.100  48.789  1.00 13.31
ATOM   1623  O   PHE A 216      18.702  49.760  48.506  1.00 12.46
ATOM   1624  CB  PHE A 216      16.107  50.960  48.592  1.00 11.19
ATOM   1625  CG  PHE A 216      15.792  50.585  47.180  1.00 12.71
ATOM   1626  CD1 PHE A 216      14.772  49.670  46.911  1.00 13.68
ATOM   1627  CD2 PHE A 216      16.528  51.105  46.121  1.00 12.29
ATOM   1628  CE1 PHE A 216      14.489  49.273  45.601  1.00 12.73
ATOM   1629  CE2 PHE A 216      16.256  50.715  44.806  1.00 12.35
ATOM   1630  CZ  PHE A 216      15.234  49.796  44.549  1.00 11.27
ATOM   1631  N   VAL A 217      17.596  47.793  48.553  1.00 13.94
ATOM   1632  CA  VAL A 217      18.679  47.042  47.936  1.00 13.30
ATOM   1633  C   VAL A 217      18.291  46.572  46.541  1.00 14.28
ATOM   1634  O   VAL A 217      17.129  46.266  46.288  1.00 15.27
ATOM   1635  CB  VAL A 217      19.037  45.788  48.776  1.00 14.96
ATOM   1636  CG1 VAL A 217      20.232  45.069  48.158  1.00 13.55
ATOM   1637  CG2 VAL A 217      19.321  46.188  50.202  1.00 13.67
ATOM   1638  N   SER A 218      19.265  46.501  45.639  1.00 13.99
ATOM   1639  CA  SER A 218      19.010  46.019  44.271  1.00 15.63
ATOM   1640  C   SER A 218      20.330  45.499  43.686  1.00 14.59
ATOM   1641  O   SER A 218      21.405  45.841  44.176  1.00 15.55
ATOM   1642  CB  SER A 218      18.423  47.139  43.384  1.00 13.27
ATOM   1643  OG  SER A 218      19.353  48.183  43.155  1.00 15.09
ATOM   1644  N   ASN A 219      20.251  44.665  42.657  1.00 15.16
ATOM   1645  CA  ASN A 219      21.455  44.103  42.043  1.00 13.83
ATOM   1646  C   ASN A 219      22.310  45.150  41.381  1.00 14.65
ATOM   1647  O   ASN A 219      21.797  46.142  40.859  1.00 16.36
ATOM   1648  CB  ASN A 219      21.104  43.078  40.983  1.00 13.87
ATOM   1649  CG  ASN A 219      20.299  41.946  41.523  1.00 13.73
ATOM   1650  OD1 ASN A 219      20.465  41.536  42.682  1.00 12.86
ATOM   1651  ND2 ASN A 219      19.424  41.410  40.686  1.00 10.39
ATOM   1652  N   GLY A 220      23.616  44.911  41.380  1.00 14.83
ATOM   1653  CA  GLY A 220      24.530  45.843  40.745  1.00 14.69
ATOM   1654  C   GLY A 220      24.336  45.924  39.230  1.00 14.48
ATOM   1655  O   GLY A 220      24.702  46.929  38.629  1.00 13.17
ATOM   1656  N   ASP A 221      23.749  44.889  38.618  1.00 13.62
ATOM   1657  CA  ASP A 221      23.540  44.873  37.159  1.00 15.34
ATOM   1658  C   ASP A 221      22.251  45.547  36.695  1.00 15.37
ATOM   1659  O   ASP A 221      22.098  45.879  35.520  1.00 17.40
ATOM   1660  CB  ASP A 221      23.557  43.436  36.640  1.00 14.75
ATOM   1661  CG  ASP A 221      22.468  42.580  37.262  1.00 16.36
ATOM   1662  OD1 ASP A 221      21.314  42.615  36.783  1.00 16.66
ATOM   1663  OD2 ASP A 221      22.767  41.881  38.245  1.00 14.88
ATOM   1664  N   ASN A 222      21.330  45.761  37.624  1.00 15.03
ATOM   1665  CA  ASN A 222      20.052  46.369  37.304  1.00 14.22
ATOM   1666  C   ASN A 222      20.047  47.885  37.521  1.00 13.41
ATOM   1667  O   ASN A 222      19.941  48.364  38.650  1.00 15.19
ATOM   1668  CB  ASN A 222      18.956  45.697  38.142  1.00 14.84
ATOM   1669  CG  ASN A 222      17.590  46.224  37.817  1.00 14.07
ATOM   1670  OD1 ASN A 222      17.350  46.669  36.693  1.00 18.16
ATOM   1671  ND2 ASN A 222      16.679  46.168  38.781  1.00 11.33
ATOM   1672  N   LEU A 223      20.141  48.639  36.432  1.00 11.81
ATOM   1673  CA  LEU A 223      20.173  50.096  36.516  1.00 11.98
ATOM   1674  C   LEU A 223      18.807  50.775  36.371  1.00 12.45
ATOM   1675  O   LEU A 223      18.726  51.990  36.233  1.00 11.20
ATOM   1676  CB  LEU A 223      21.146  50.645  35.473  1.00 13.24
ATOM   1677  CG  LEU A 223      22.615  50.231  35.613  1.00 12.01
ATOM   1678  CD1 LEU A 223      23.339  50.452  34.295  1.00 14.05
ATOM   1679  CD2 LEU A 223      23.268  51.030  36.743  1.00 12.10
ATOM   1680  N   GLY A 224      17.738  49.987  36.398  1.00 12.95
ATOM   1681  CA  GLY A 224      16.408  50.554  36.309  1.00 13.66
ATOM   1682  C   GLY A 224      15.846  50.776  37.698  1.00 15.90
ATOM   1683  O   GLY A 224      14.774  51.358  37.873  1.00 17.08
ATOM   1684  N   ALA A 225      16.592  50.331  38.702  1.00 16.90
ATOM   1685  CA  ALA A 225      16.145  50.438  40.079  1.00 17.06
ATOM   1686  C   ALA A 225      16.716  51.549  40.958  1.00 17.88
ATOM   1687  O   ALA A 225      17.916  51.580  41.233  1.00 17.68
ATOM   1688  CB  ALA A 225      16.356  49.097  40.776  1.00 17.40
ATOM   1689  N   THR A 226      15.833  52.449  41.385  1.00 17.70
ATOM   1690  CA  THR A 226      16.165  53.516  42.317  1.00 21.08
ATOM   1691  C   THR A 226      14.972  53.634  43.265  1.00 21.07
ATOM   1692  O   THR A 226      13.932  52.992  43.080  1.00 21.84
ATOM   1693  CB  THR A 226      16.394  54.906  41.656  1.00 22.65
ATOM   1694  OG1 THR A 226      15.196  55.333  40.998  1.00 26.86
ATOM   1695  CG2 THR A 226      17.550  54.857  40.685  1.00 22.07
ATOM   1696  N   ILE A 227      15.130  54.463  44.280  1.00 21.45
ATOM   1697  CA  ILE A 227      14.097  54.678  45.272  1.00 21.49
ATOM   1698  C   ILE A 227      12.831  55.327  44.751  1.00 21.73
ATOM   1699  O   ILE A 227      12.873  56.312  44.033  1.00 20.67
ATOM   1700  CB  ILE A 227      14.621  55.559  46.415  1.00 21.45
ATOM   1701  CG1 ILE A 227      15.527  54.741  47.332  1.00 22.46
ATOM   1702  CG2 ILE A 227      13.459  56.122  47.217  1.00 22.28
ATOM   1703  CD1 ILE A 227      16.116  55.567  48.458  1.00 23.52
ATOM   1704  N   ASP A 228      11.694  54.770  45.129  1.00 23.06
ATOM   1705  CA  ASP A 228      10.435  55.362  44.743  1.00 23.05
ATOM   1706  C   ASP A 228       9.727  55.680  46.057  1.00 22.89
ATOM   1707  O   ASP A 228       9.369  54.774  46.816  1.00 22.65
ATOM   1708  CB  ASP A 228       9.615  54.402  43.878  1.00 24.90
ATOM   1709  CG  ASP A 228       8.340  55.053  43.335  1.00 25.53
ATOM   1710  OD1 ASP A 228       7.925  54.722  42.199  1.00 25.28
ATOM   1711  OD2 ASP A 228       7.749  55.891  44.058  1.00 27.43
ATOM   1712  N   LYS A 229       9.548  56.972  46.320  1.00 21.38
ATOM   1713  CA  LYS A 229       8.925  57.440  47.552  1.00 21.97
ATOM   1714  C   LYS A 229       7.518  56.906  47.787  1.00 19.64
ATOM   1715  O   LYS A 229       7.017  56.952  48.904  1.00 21.45
ATOM   1716  CB  LYS A 229       8.923  58.973  47.592  1.00 22.54
ATOM   1717  CG  LYS A 229      10.314  59.597  47.397  1.00 28.28
ATOM   1718  CD  LYS A 229      10.275  61.116  47.601  1.00 31.72
ATOM   1719  CE  LYS A 229      11.150  61.861  46.595  1.00 34.67
ATOM   1720  NZ  LYS A 229      10.676  61.695  45.178  1.00 37.52
ATOM   1721  N   ARG A 230       6.876  56.393  46.748  1.00 18.28
ATOM   1722  CA  ARG A 230       5.536  55.843  46.927  1.00 18.96
ATOM   1723  C   ARG A 230       5.619  54.509  47.661  1.00 17.29
ATOM   1724  O   ARG A 230       4.738  54.189  48.453  1.00 20.06
ATOM   1725  CB  ARG A 230       4.831  55.650  45.577  1.00 16.74
ATOM   1726  CG  ARG A 230       4.536  56.954  44.861  1.00 19.71
ATOM   1727  CD  ARG A 230       3.943  56.680  43.484  1.00 23.02
ATOM   1728  NE  ARG A 230       4.907  56.039  42.590  1.00 20.44
ATOM   1729  CZ  ARG A 230       4.586  55.433  41.453  1.00 22.36
ATOM   1730  NH1 ARG A 230       3.319  55.379  41.067  1.00 20.50
ATOM   1731  NH2 ARG A 230       5.535  54.883  40.695  1.00 22.54
ATOM   1732  N   VAL A 231       6.670  53.733  47.389  1.00 15.95
ATOM   1733  CA  VAL A 231       6.873  52.437  48.047  1.00 15.54
ATOM   1734  C   VAL A 231       7.016  52.623  49.554  1.00 15.36
ATOM   1735  O   VAL A 231       6.459  51.857  50.348  1.00 15.77
ATOM   1736  CB  VAL A 231       8.154  51.734  47.535  1.00 15.27
ATOM   1737  CG1 VAL A 231       8.368  50.443  48.298  1.00 16.21
ATOM   1738  CG2 VAL A 231       8.045  51.464  46.046  1.00 13.49
ATOM   1739  N   LEU A 232       7.775  53.648  49.936  1.00 14.42
ATOM   1740  CA  LEU A 232       7.999  53.969  51.339  1.00 16.89
ATOM   1741  C   LEU A 232       6.706  54.355  52.059  1.00 18.73
ATOM   1742  O   LEU A 232       6.468  53.914  53.187  1.00 18.75
ATOM   1743  CB  LEU A 232       9.022  55.102  51.446  1.00 16.58
ATOM   1744  CG  LEU A 232      10.455  54.690  51.074  1.00 15.56
ATOM   1745  CD1 LEU A 232      11.304  55.924  50.854  1.00 14.72
ATOM   1746  CD2 LEU A 232      11.049  53.810  52.184  1.00 12.35
ATOM   1747  N   ALA A 233       5.876  55.177  51.411  1.00 20.22
ATOM   1748  CA  ALA A 233       4.601  55.606  51.998  1.00 20.02
ATOM   1749  C   ALA A 233       3.689  54.405  52.182  1.00 19.83
ATOM   1750  O   ALA A 233       3.008  54.274  53.199  1.00 20.15
ATOM   1751  CB  ALA A 233       3.920  56.632  51.094  1.00 21.67
ATOM   1752  N   TYR A 234       3.676  53.538  51.173  1.00 20.49
ATOM   1753  CA  TYR A 234       2.875  52.312  51.184  1.00 20.31
ATOM   1754  C   TYR A 234       3.365  51.436  52.339  1.00 20.13
ATOM   1755  O   TYR A 234       2.571  50.928  53.129  1.00 20.05
ATOM   1756  CB  TYR A 234       3.038  51.587  49.836  1.00 20.16
ATOM   1757  CG  TYR A 234       2.384  50.224  49.700  1.00 20.84
ATOM   1758  CD1 TYR A 234       1.002  50.096  49.517  1.00 22.07
ATOM   1759  CD2 TYR A 234       3.160  49.054  49.692  1.00 21.68
ATOM   1760  CE1 TYR A 234       0.411  48.842  49.321  1.00 19.31
ATOM   1761  CE2 TYR A 234       2.574  47.791  49.496  1.00 20.47
ATOM   1762  CZ  TYR A 234       1.201  47.696  49.310  1.00 21.60
ATOM   1763  OH  TYR A 234       0.618  46.462  49.107  1.00 21.45
ATOM   1764  N   MET A 235       4.676  51.274  52.456  1.00 21.25
ATOM   1765  CA  MET A 235       5.209  50.457  53.536  1.00 23.82
ATOM   1766  C   MET A 235       4.870  51.020  54.911  1.00 24.87
ATOM   1767  O   MET A 235       4.519  50.277  55.837  1.00 22.90
ATOM   1768  CB  MET A 235       6.720  50.300  53.376  1.00 23.23
ATOM   1769  CG  MET A 235       7.087  49.295  52.305  1.00 23.36
ATOM   1770  SD  MET A 235       8.956  49.115  52.074  1.00 23.39
ATOM   1771  CE  MET A 235       9.339  47.844  53.479  1.00 20.54
ATOM   1772  N   GLU A 236       4.992  52.334  55.044  1.00 25.45
ATOM   1773  CA  GLU A 236       4.677  53.019  56.307  1.00 28.91
ATOM   1774  C   GLU A 236       3.234  52.767  56.726  1.00 28.97
ATOM   1775  O   GLU A 236       2.941  52.459  57.875  1.00 29.51
ATOM   1776  CB  GLU A 236       4.857  54.532  56.131  1.00 29.87
ATOM   1777  CG  GLU A 236       6.287  55.010  56.195  1.00 32.47
ATOM   1778  CD  GLU A 236       6.813  54.953  57.608  1.00 35.71
ATOM   1779  OE1 GLU A 236       6.927  53.834  58.160  1.00 35.06
ATOM   1780  OE2 GLU A 236       7.101  56.035  58.161  1.00 37.44
ATOM   1781  N   LYS A 237       2.343  52.925  55.765  1.00 28.84
ATOM   1782  CA  LYS A 237       0.925  52.761  55.977  1.00 30.71
ATOM   1783  C   LYS A 237       0.453  51.339  56.179  1.00 30.02
ATOM   1784  O   LYS A 237      -0.294  51.059  57.107  1.00 31.86
ATOM   1785  CB  LYS A 237       0.209  53.346  54.787  1.00 33.24
ATOM   1786  CG  LYS A 237      -1.187  52.842  54.594  1.00 36.97
ATOM   1787  CD  LYS A 237      -1.672  53.317  53.253  1.00 38.23
ATOM   1788  CE  LYS A 237      -3.106  52.952  53.003  1.00 40.73
ATOM   1789  NZ  LYS A 237      -3.484  53.558  51.703  1.00 44.60
ATOM   1790  N   GLU A 238       0.855  50.455  55.280  1.00 29.64
ATOM   1791  CA  GLU A 238       0.462  49.058  55.360  1.00 30.40
ATOM   1792  C   GLU A 238       1.287  48.359  56.412  1.00 30.14
ATOM   1793  O   GLU A 238       1.102  47.171  56.663  1.00 30.66
ATOM   1794  CB  GLU A 238       0.647  48.369  54.006  1.00 29.20
ATOM   1795  CG  GLU A 238      -0.279  48.913  52.931  1.00 33.17
ATOM   1796  CD  GLU A 238      -1.744  48.866  53.352  1.00 36.91
ATOM   1797  OE1 GLU A 238      -2.271  47.753  53.586  1.00 38.63
ATOM   1798  OE2 GLU A 238      -2.367  49.947  53.460  1.00 39.51
ATOM   1799  N   LYS A 239       2.202  49.104  57.030  1.00 29.84
ATOM   1800  CA  LYS A 239       3.061  48.545  58.073  1.00 30.62
ATOM   1801  C   LYS A 239       3.760  47.260  57.606  1.00 27.71
ATOM   1802  O   LYS A 239       3.684  46.219  58.266  1.00 25.91
ATOM   1803  CB  LYS A 239       2.227  48.259  59.331  1.00 33.69
ATOM   1804  CG  LYS A 239       1.742  49.516  60.045  1.00 38.07
ATOM   1805  CD  LYS A 239       0.673  49.190  61.079  1.00 42.47
ATOM   1806  CE  LYS A 239       0.299  50.426  61.884  1.00 44.87
ATOM   1807  NZ  LYS A 239       0.095  51.617  61.005  1.00 47.20
ATOM   1808  N   ILE A 240       4.439  47.344  56.466  1.00 24.64
ATOM   1809  CA  ILE A 240       5.141  46.198  55.921  1.00 20.67
ATOM   1810  C   ILE A 240       6.602  46.314  56.289  1.00 19.96
ATOM   1811  O   ILE A 240       7.201  47.377  56.171  1.00 20.68
ATOM   1812  CB  ILE A 240       4.952  46.131  54.397  1.00 20.43
ATOM   1813  CG1 ILE A 240       3.466  45.925  54.088  1.00 19.03
ATOM   1814  CG2 ILE A 240       5.762  44.968  53.795  1.00 20.08
ATOM   1815  CD1 ILE A 240       3.138  46.000  52.594  1.00 19.78
ATOM   1816  N   ASP A 241       7.181  45.222  56.761  1.00 19.09
ATOM   1817  CA  ASP A 241       8.577  45.253  57.161  1.00 18.53
ATOM   1818  C   ASP A 241       9.549  44.809  56.066  1.00 17.38
ATOM   1819  O   ASP A 241      10.744  45.102  56.123  1.00 17.37
ATOM   1820  CB  ASP A 241       8.763  44.411  58.423  1.00 18.93
ATOM   1821  CG  ASP A 241       7.901  44.899  59.579  1.00 22.45
ATOM   1822  OD1 ASP A 241       7.851  46.127  59.830  1.00 26.05
ATOM   1823  OD2 ASP A 241       7.280  44.058  60.248  1.00 23.04
ATOM   1824  N   PHE A 242       9.034  44.119  55.058  1.00 15.89
ATOM   1825  CA  PHE A 242       9.870  43.642  53.969  1.00 15.52
ATOM   1826  C   PHE A 242       9.034  43.651  52.709  1.00 16.13
ATOM   1827  O   PHE A 242       7.910  43.145  52.698  1.00 18.47
ATOM   1828  CB  PHE A 242      10.341  42.216  54.269  1.00 17.09
ATOM   1829  CG  PHE A 242      11.163  41.608  53.176  1.00 16.45
ATOM   1830  CD1 PHE A 242      12.547  41.622  53.241  1.00 18.11
ATOM   1831  CD2 PHE A 242      10.554  41.014  52.090  1.00 13.51
ATOM   1832  CE1 PHE A 242      13.311  41.049  52.240  1.00 15.55
ATOM   1833  CE2 PHE A 242      11.310  40.441  51.087  1.00 15.03
ATOM   1834  CZ  PHE A 242      12.688  40.459  51.163  1.00 14.25
ATOM   1835  N   LEU A 243       9.578  44.213  51.638  1.00 15.76
ATOM   1836  CA  LEU A 243       8.829  44.270  50.396  1.00 14.16
ATOM   1837  C   LEU A 243       9.663  43.897  49.188  1.00 14.58
ATOM   1838  O   LEU A 243      10.697  44.525  48.909  1.00 15.05
ATOM   1839  CB  LEU A 243       8.249  45.675  50.178  1.00 14.53
ATOM   1840  CG  LEU A 243       7.211  45.757  49.053  1.00 14.08
ATOM   1841  CD1 LEU A 243       6.006  44.897  49.431  1.00 13.24
ATOM   1842  CD2 LEU A 243       6.759  47.194  48.852  1.00 14.85
ATOM   1843  N   MET A 244       9.198  42.886  48.460  1.00 13.27
ATOM   1844  CA  MET A 244       9.876  42.448  47.256  1.00 14.17
ATOM   1845  C   MET A 244       9.197  43.002  46.017  1.00 13.37
ATOM   1846  O   MET A 244       7.980  42.880  45.856  1.00 12.65
ATOM   1847  CB  MET A 244       9.877  40.916  47.147  1.00 15.82
ATOM   1848  CG  MET A 244      10.384  40.395  45.793  1.00 16.91
ATOM   1849  SD  MET A 244      10.184  38.452  45.619  1.00 21.46
ATOM   1850  CE  MET A 244      11.491  37.971  46.953  1.00 16.53
ATOM   1851  N   GLU A 245       9.979  43.608  45.135  1.00 13.56
ATOM   1852  CA  GLU A 245       9.414  44.101  43.888  1.00 13.65
ATOM   1853  C   GLU A 245       9.488  42.958  42.864  1.00 15.12
ATOM   1854  O   GLU A 245      10.568  42.426  42.597  1.00 15.53
ATOM   1855  CB  GLU A 245      10.211  45.301  43.381  1.00 12.31
ATOM   1856  CG  GLU A 245      10.035  46.551  44.221  1.00 12.26
ATOM   1857  CD  GLU A 245      10.778  47.742  43.648  1.00 12.05
ATOM   1858  OE1 GLU A 245      10.980  47.775  42.417  1.00 10.50
ATOM   1859  OE2 GLU A 245      11.143  48.651  44.424  1.00 13.09
ATOM   1860  N   VAL A 246       8.340  42.574  42.312  1.00 16.04
ATOM   1861  CA  VAL A 246       8.284  41.523  41.301  1.00 15.72
ATOM   1862  C   VAL A 246       7.741  42.083  39.983  1.00 16.15
ATOM   1863  O   VAL A 246       6.945  43.030  39.976  1.00 14.34
ATOM   1864  CB  VAL A 246       7.381  40.350  41.753  1.00 15.92
ATOM   1865  CG1 VAL A 246       7.934  39.714  43.032  1.00 14.43
ATOM   1866  CG2 VAL A 246       5.971  40.849  41.970  1.00 14.30
ATOM   1867  N   CYS A 247       8.179  41.505  38.870  1.00 15.48
ATOM   1868  CA  CYS A 247       7.723  41.928  37.547  1.00 18.30
ATOM   1869  C   CYS A 247       6.952  40.790  36.877  1.00 19.51
ATOM   1870  O   CYS A 247       7.193  39.628  37.188  1.00 19.53
ATOM   1871  CB  CYS A 247       8.917  42.276  36.660  1.00 17.45
ATOM   1872  SG  CYS A 247       9.513  43.979  36.747  1.00 25.40
ATOM   1873  N   ARG A 248       6.031  41.127  35.976  1.00 20.44
ATOM   1874  CA  ARG A 248       5.274  40.126  35.224  1.00 23.29
ATOM   1875  C   ARG A 248       6.352  39.407  34.424  1.00 23.29
ATOM   1876  O   ARG A 248       7.091  40.048  33.674  1.00 23.37
ATOM   1877  CB  ARG A 248       4.315  40.786  34.228  1.00 27.84
ATOM   1878  CG  ARG A 248       2.845  40.482  34.443  1.00 34.76
ATOM   1879  CD  ARG A 248       2.603  39.031  34.816  1.00 37.26
ATOM   1880  NE  ARG A 248       1.315  38.863  35.496  1.00 40.85
ATOM   1881  CZ  ARG A 248       0.737  39.793  36.260  1.00 42.57
ATOM   1882  NH1 ARG A 248       1.312  40.975  36.449  1.00 45.09
ATOM   1883  NH2 ARG A 248      -0.412  39.544  36.859  1.00 41.36
ATOM   1884  N   ARG A 249       6.444  38.090  34.563  1.00 21.96
ATOM   1885  CA  ARG A 249       7.490  37.337  33.882  1.00 23.31
ATOM   1886  C   ARG A 249       7.396  37.330  32.369  1.00 24.84
ATOM   1887  O   ARG A 249       6.328  37.097  31.800  1.00 27.85
ATOM   1888  CB  ARG A 249       7.499  35.910  34.403  1.00 22.17
ATOM   1889  CG  ARG A 249       8.778  35.173  34.142  1.00 20.97
ATOM   1890  CD  ARG A 249       8.721  33.834  34.850  1.00 21.14
ATOM   1891  NE  ARG A 249       9.947  33.053  34.695  1.00 21.72
ATOM   1892  CZ  ARG A 249      10.170  31.906  35.330  1.00 21.53
ATOM   1893  NH1 ARG A 249       9.254  31.419  36.155  1.00 17.67
ATOM   1894  NH2 ARG A 249      11.303  31.243  35.144  1.00 21.56
ATOM   1895  N   THR A 250       8.525  37.591  31.721  1.00 24.34
ATOM   1896  CA  THR A 250       8.600  37.584  30.269  1.00 26.08
ATOM   1897  C   THR A 250       9.431  36.386  29.829  1.00 27.51
ATOM   1898  O   THR A 250       9.953  35.638  30.666  1.00 28.55
ATOM   1899  CB  THR A 250       9.282  38.838  29.722  1.00 27.58
ATOM   1900  OG1 THR A 250      10.634  38.880  30.202  1.00 27.90
ATOM   1901  CG2 THR A 250       8.508  40.103  30.138  1.00 26.19
ATOM   1902  N   GLU A 251       9.555  36.215  28.516  1.00 28.21
ATOM   1903  CA  GLU A 251      10.312  35.108  27.934  1.00 30.28
ATOM   1904  C   GLU A 251      11.800  35.182  28.310  1.00 29.83
ATOM   1905  O   GLU A 251      12.458  34.146  28.453  1.00 29.89
ATOM   1906  CB  GLU A 251      10.169  35.127  26.400  1.00 32.13
ATOM   1907  CG  GLU A 251      10.419  33.774  25.724  1.00 34.39
ATOM   1908  CD  GLU A 251      10.442  33.863  24.192  1.00 37.28
ATOM   1909  OE1 GLU A 251       9.604  34.610  23.632  1.00 35.24
ATOM   1910  OE2 GLU A 251      11.287  33.178  23.552  1.00 35.78
ATOM   1911  N   SER A 252      12.309  36.410  28.467  1.00 30.01
ATOM   1912  CA  SER A 252      13.710  36.679  28.817  1.00 28.70
ATOM   1913  C   SER A 252      14.082  36.379  30.274  1.00 28.36
ATOM   1914  O   SER A 252      15.264  36.385  30.627  1.00 30.13
ATOM   1915  CB  SER A 252      14.038  38.142  28.548  1.00 29.03
ATOM   1916  OG  SER A 252      13.581  38.553  27.275  1.00 31.54
ATOM   1917  N   ASP A 253      13.092  36.137  31.129  1.00 26.65
ATOM   1918  CA  ASP A 253      13.382  35.850  32.537  1.00 26.39
ATOM   1919  C   ASP A 253      13.553  34.351  32.768  1.00 26.55
ATOM   1920  O   ASP A 253      12.602  33.646  33.095  1.00 25.56
ATOM   1921  CB  ASP A 253      12.277  36.395  33.440  1.00 23.03
ATOM   1922  CG  ASP A 253      11.979  37.845  33.168  1.00 21.02
ATOM   1923  OD1 ASP A 253      12.940  38.626  32.987  1.00 20.60
ATOM   1924  OD2 ASP A 253      10.786  38.208  33.134  1.00 19.58
ATOM   1925  N   LYS A 254      14.792  33.896  32.608  1.00 28.59
ATOM   1926  CA  LYS A 254      15.157  32.497  32.754  1.00 29.57
ATOM   1927  C   LYS A 254      16.153  32.263  33.882  1.00 28.01
ATOM   1928  O   LYS A 254      16.202  31.175  34.450  1.00 27.09
ATOM   1929  CB  LYS A 254      15.749  32.005  31.436  1.00 33.31
ATOM   1930  CG  LYS A 254      14.883  32.354  30.239  1.00 37.72
ATOM   1931  CD  LYS A 254      15.338  31.635  28.981  1.00 42.57
ATOM   1932  CE  LYS A 254      14.244  31.656  27.920  1.00 43.96
ATOM   1933  NZ  LYS A 254      14.577  30.761  26.776  1.00 46.24
ATOM   1934  N   LYS A 255      16.961  33.276  34.188  1.00 27.23
ATOM   1935  CA  LYS A 255      17.951  33.178  35.260  1.00 26.58
ATOM   1936  C   LYS A 255      17.578  34.135  36.384  1.00 24.30
ATOM   1937  O   LYS A 255      17.670  35.348  36.235  1.00 24.43
ATOM   1938  CB  LYS A 255      19.357  33.521  34.758  1.00 29.12
ATOM   1939  CG  LYS A 255      20.103  32.385  34.072  1.00 34.04
ATOM   1940  CD  LYS A 255      21.612  32.695  34.059  1.00 36.49
ATOM   1941  CE  LYS A 255      22.429  31.562  33.446  1.00 38.12
ATOM   1942  NZ  LYS A 255      22.193  31.429  31.972  1.00 39.99
ATOM   1943  N   GLY A 256      17.169  33.570  37.512  1.00 21.86
ATOM   1944  CA  GLY A 256      16.751  34.363  38.649  1.00 19.70
ATOM   1945  C   GLY A 256      15.793  33.520  39.473  1.00 20.14
ATOM   1946  O   GLY A 256      15.933  32.288  39.527  1.00 21.54
ATOM   1947  N   GLY A 257      14.825  34.163  40.118  1.00 18.22
ATOM   1948  CA  GLY A 257      13.868  33.426  40.928  1.00 15.29
ATOM   1949  C   GLY A 257      12.457  33.951  40.761  1.00 16.44
ATOM   1950  O   GLY A 257      12.243  35.073  40.289  1.00 14.46
ATOM   1951  N   HIS A 258      11.478  33.144  41.141  1.00 15.44
ATOM   1952  CA  HIS A 258      10.104  33.583  41.026  1.00 14.57
ATOM   1953  C   HIS A 258       9.435  33.511  42.379  1.00 14.95
ATOM   1954  O   HIS A 258       9.893  32.803  43.280  1.00 14.72
ATOM   1955  CB  HIS A 258       9.347  32.718  40.009  1.00 14.55
ATOM   1956  CG  HIS A 258       9.118  31.305  40.460  1.00 15.77
ATOM   1957  ND1 HIS A 258       8.130  30.961  41.357  1.00 13.25
ATOM   1958  CD2 HIS A 258       9.744  30.151  40.127  1.00 13.77
ATOM   1959  CE1 HIS A 258       8.154  29.654  41.555  1.00 14.47
ATOM   1960  NE2 HIS A 258       9.124  29.140  40.821  1.00 16.00
ATOM   1961  N   LEU A 259       8.342  34.251  42.509  1.00 14.40
ATOM   1962  CA  LEU A 259       7.569  34.294  43.743  1.00 13.89
ATOM   1963  C   LEU A 259       6.653  33.075  43.807  1.00 14.93
ATOM   1964  O   LEU A 259       6.374  32.443  42.787  1.00 14.57
ATOM   1965  CB  LEU A 259       6.715  35.571  43.760  1.00 13.41
ATOM   1966  CG  LEU A 259       5.950  35.911  45.039  1.00 15.12
ATOM   1967  CD1 LEU A 259       6.946  36.141  46.177  1.00 14.15
ATOM   1968  CD2 LEU A 259       5.095  37.158  44.823  1.00 13.66
ATOM   1969  N   ALA A 260       6.183  32.750  45.005  1.00 14.80
ATOM   1970  CA  ALA A 260       5.275  31.631  45.190  1.00 15.98
ATOM   1971  C   ALA A 260       4.688  31.744  46.580  1.00 16.79
ATOM   1972  O   ALA A 260       5.155  32.544  47.398  1.00 16.35
ATOM   1973  CB  ALA A 260       6.010  30.301  45.043  1.00 16.28
ATOM   1974  N   ARG A 261       3.689  30.921  46.855  1.00 16.99
ATOM   1975  CA  ARG A 261       3.046  30.936  48.159  1.00 21.88
ATOM   1976  C   ARG A 261       2.804  29.530  48.695  1.00 23.05
ATOM   1977  O   ARG A 261       2.866  28.545  47.962  1.00 22.01
ATOM   1978  CB  ARG A 261       1.690  31.647  48.062  1.00 21.14
ATOM   1979  CG  ARG A 261       0.688  30.948  47.116  1.00 24.53
ATOM   1980  CD  ARG A 261      -0.741  31.521  47.243  1.00 23.87
ATOM   1981  NE  ARG A 261      -1.338  31.153  48.522  1.00 26.39
ATOM   1982  CZ  ARG A 261      -2.373  31.775  49.079  1.00 28.48
ATOM   1983  NH1 ARG A 261      -2.935  32.811  48.467  1.00 26.72
ATOM   1984  NH2 ARG A 261      -2.843  31.362  50.256  1.00 28.53
ATOM   1985  N   GLN A 262       2.526  29.464  49.987  1.00 25.46
ATOM   1986  CA  GLN A 262       2.175  28.234  50.665  1.00 30.08
ATOM   1987  C   GLN A 262       1.042  28.733  51.572  1.00 32.21
ATOM   1988  O   GLN A 262       0.831  29.943  51.707  1.00 31.30
ATOM   1989  CB  GLN A 262       3.351  27.669  51.480  1.00 29.94
ATOM   1990  CG  GLN A 262       4.524  27.276  50.619  1.00 32.60
ATOM   1991  CD  GLN A 262       5.662  26.598  51.378  1.00 33.94
ATOM   1992  OE1 GLN A 262       6.016  26.956  52.498  1.00 34.72
ATOM   1993  NE2 GLN A 262       6.258  25.627  50.734  1.00 33.99
ATOM   1994  N   THR A 263       0.274  27.827  52.150  1.00 35.74
ATOM   1995  CA  THR A 263      -0.813  28.261  53.009  1.00 39.53
ATOM   1996  C   THR A 263      -0.577  27.739  54.396  1.00 42.82
ATOM   1997  O   THR A 263      -0.338  26.546  54.585  1.00 43.12
ATOM   1998  CB  THR A 263      -2.177  27.749  52.519  1.00 39.10
ATOM   1999  OG1 THR A 263      -2.465  28.326  51.242  1.00 37.50
ATOM   2000  CG2 THR A 263      -3.284  28.141  53.507  1.00 38.36
ATOM   2001  N   VAL A 264      -0.639  28.653  55.356  1.00 46.53
ATOM   2002  CA  VAL A 264      -0.442  28.329  56.758  1.00 50.67
ATOM   2003  C   VAL A 264      -1.765  28.523  57.484  1.00 54.63
ATOM   2004  O   VAL A 264      -2.495  29.475  57.201  1.00 54.12
ATOM   2005  CB  VAL A 264       0.618  29.246  57.370  1.00 49.95
ATOM   2006  CG1 VAL A 264       0.671  29.056  58.869  1.00 50.38
ATOM   2007  CG2 VAL A 264       1.974  28.943  56.745  1.00 51.13
ATOM   2008  N   TYR A 265      -2.074  27.616  58.411  1.00 59.19
ATOM   2009  CA  TYR A 265      -3.323  27.688  59.168  1.00 63.26
ATOM   2010  C   TYR A 265      -3.157  28.224  60.575  1.00 64.75
ATOM   2011  O   TYR A 265      -2.528  27.594  61.427  1.00 65.68
ATOM   2012  CB  TYR A 265      -3.987  26.314  59.219  1.00 64.79
ATOM   2013  CG  TYR A 265      -4.375  25.835  57.849  1.00 67.59
ATOM   2014  CD1 TYR A 265      -3.425  25.284  56.987  1.00 68.65
ATOM   2015  CD2 TYR A 265      -5.680  25.996  57.383  1.00 69.12
ATOM   2016  CE1 TYR A 265      -3.764  24.910  55.690  1.00 69.95
ATOM   2017  CE2 TYR A 265      -6.032  25.626  56.090  1.00 70.20
ATOM   2018  CZ  TYR A 265      -5.069  25.085  55.249  1.00 70.52
ATOM   2019  OH  TYR A 265      -5.409  24.729  53.966  1.00 72.14
ATOM   2020  N   VAL A 266      -3.725  29.400  60.805  1.00 66.23
ATOM   2021  CA  VAL A 266      -3.660  30.034  62.108  1.00 68.27
ATOM   2022  C   VAL A 266      -5.016  29.929  62.777  1.00 69.84
ATOM   2023  O   VAL A 266      -5.847  30.829  62.650  1.00 70.83
ATOM   2024  CB  VAL A 266      -3.282  31.521  61.998  1.00 68.09
ATOM   2025  CG1 VAL A 266      -1.771  31.691  62.112  1.00 68.49
ATOM   2026  CG2 VAL A 266      -3.784  32.076  60.675  1.00 68.42
ATOM   2027  N   LYS A 267      -5.249  28.821  63.475  1.00 71.24
ATOM   2028  CA  LYS A 267      -6.517  28.636  64.165  1.00 72.42
ATOM   2029  C   LYS A 267      -6.550  29.552  65.381  1.00 72.73
ATOM   2030  O   LYS A 267      -6.457  29.103  66.531  1.00 73.06
ATOM   2031  CB  LYS A 267      -6.711  27.179  64.586  1.00 72.87
ATOM   2032  CG  LYS A 267      -7.932  26.534  63.935  1.00 74.07
ATOM   2033  CD  LYS A 267      -9.158  27.434  64.083  1.00 74.31
ATOM   2034  CE  LYS A 267      -9.487  27.675  65.557  1.00 75.59
ATOM   2035  NZ  LYS A 267      -9.737  29.114  65.877  1.00 75.78
ATOM   2036  N   GLY A 268      -6.678  30.847  65.103  1.00 72.67
ATOM   2037  CA  GLY A 268      -6.713  31.845  66.151  1.00 73.00
ATOM   2038  C   GLY A 268      -8.118  32.137  66.631  1.00 73.62
ATOM   2039  O   GLY A 268      -9.052  32.282  65.833  1.00 73.49
ATOM   2040  N   LYS A 269      -8.252  32.205  67.953  1.00 73.33
ATOM   2041  CA  LYS A 269      -9.509  32.498  68.633  1.00 72.44
ATOM   2042  C   LYS A 269     -10.484  31.364  68.930  1.00 71.41
ATOM   2043  O   LYS A 269     -10.364  30.231  68.449  1.00 70.51
ATOM   2044  CB  LYS A 269     -10.274  33.613  67.911  1.00 73.23
ATOM   2045  CG  LYS A 269      -9.811  35.014  68.258  1.00 73.68
ATOM   2046  CD  LYS A 269     -10.716  36.041  67.605  1.00 74.04
ATOM   2047  CE  LYS A 269     -12.170  35.828  68.011  1.00 74.28
ATOM   2048  NZ  LYS A 269     -13.093  36.724  67.256  1.00 74.87
ATOM   2049  N   ASP A 270     -11.460  31.736  69.749  1.00 70.03
ATOM   2050  CA  ASP A 270     -12.525  30.880  70.231  1.00 68.04
ATOM   2051  C   ASP A 270     -13.806  31.251  69.488  1.00 66.43
ATOM   2052  O   ASP A 270     -14.262  32.398  69.541  1.00 65.54
ATOM   2053  CB  ASP A 270     -12.677  31.124  71.728  1.00 69.35
ATOM   2054  CG  ASP A 270     -11.955  32.389  72.178  1.00 69.72
ATOM   2055  OD1 ASP A 270     -12.296  33.480  71.668  1.00 71.13
ATOM   2056  OD2 ASP A 270     -11.040  32.297  73.024  1.00 69.52
ATOM   2057  N   GLY A 271     -14.386  30.275  68.800  1.00 64.54
ATOM   2058  CA  GLY A 271     -15.585  30.532  68.026  1.00 62.16
ATOM   2059  C   GLY A 271     -15.215  30.682  66.558  1.00 60.72
ATOM   2060  O   GLY A 271     -15.744  29.970  65.698  1.00 60.45
ATOM   2061  N   GLN A 272     -14.297  31.606  66.275  1.00 58.61
ATOM   2062  CA  GLN A 272     -13.845  31.843  64.912  1.00 56.66
ATOM   2063  C   GLN A 272     -13.186  30.565  64.414  1.00 56.79
ATOM   2064  O   GLN A 272     -12.542  29.845  65.176  1.00 57.13
ATOM   2065  CB  GLN A 272     -12.841  32.993  64.870  1.00 54.29
ATOM   2066  CG  GLN A 272     -13.435  34.354  65.109  1.00 51.92
ATOM   2067  CD  GLN A 272     -14.442  34.737  64.052  1.00 50.76
ATOM   2068  OE1 GLN A 272     -14.143  34.750  62.861  1.00 49.58
ATOM   2069  NE2 GLN A 272     -15.643  35.057  64.487  1.00 48.52
ATOM   2070  N   PRO A 273     -13.349  30.254  63.127  1.00 57.08
ATOM   2071  CA  PRO A 273     -12.751  29.039  62.575  1.00 58.06
ATOM   2072  C   PRO A 273     -11.371  29.192  61.922  1.00 59.25
ATOM   2073  O   PRO A 273     -10.697  30.218  62.053  1.00 58.42
ATOM   2074  CB  PRO A 273     -13.803  28.587  61.582  1.00 57.41
ATOM   2075  CG  PRO A 273     -14.246  29.901  60.996  1.00 57.36
ATOM   2076  CD  PRO A 273     -14.367  30.803  62.214  1.00 56.48
ATOM   2077  N   ASP A 274     -10.977  28.133  61.221  1.00 61.23
ATOM   2078  CA  ASP A 274      -9.708  28.058  60.508  1.00 62.68
ATOM   2079  C   ASP A 274      -9.413  29.275  59.647  1.00 62.37
ATOM   2080  O   ASP A 274      -9.996  29.442  58.575  1.00 63.27
ATOM   2081  CB  ASP A 274      -9.691  26.820  59.612  1.00 64.44
ATOM   2082  CG  ASP A 274      -9.343  25.563  60.366  1.00 67.18
ATOM   2083  OD1 ASP A 274      -9.949  25.316  61.434  1.00 68.91
ATOM   2084  OD2 ASP A 274      -8.463  24.817  59.884  1.00 68.74
ATOM   2085  N   ALA A 275      -8.500  30.118  60.111  1.00 61.58
ATOM   2086  CA  ALA A 275      -8.116  31.300  59.355  1.00 60.23
ATOM   2087  C   ALA A 275      -6.920  30.916  58.491  1.00 59.06
ATOM   2088  O   ALA A 275      -5.882  30.494  59.011  1.00 59.35
ATOM   2089  CB  ALA A 275      -7.742  32.436  60.305  1.00 61.27
ATOM   2090  N   GLU A 276      -7.073  31.039  57.175  1.00 56.82
ATOM   2091  CA  GLU A 276      -5.988  30.706  56.260  1.00 54.80
ATOM   2092  C   GLU A 276      -5.066  31.897  56.108  1.00 52.13
ATOM   2093  O   GLU A 276      -5.523  33.041  56.008  1.00 52.04
ATOM   2094  CB  GLU A 276      -6.527  30.303  54.895  1.00 55.98
ATOM   2095  CG  GLU A 276      -7.292  29.011  54.913  1.00 58.65
ATOM   2096  CD  GLU A 276      -7.736  28.597  53.533  1.00 60.76
ATOM   2097  OE1 GLU A 276      -8.423  29.403  52.868  1.00 61.73
ATOM   2098  OE2 GLU A 276      -7.397  27.467  53.114  1.00 61.82
ATOM   2099  N   LYS A 277      -3.767  31.621  56.092  1.00 47.92
ATOM   2100  CA  LYS A 277      -2.772  32.671  55.975  1.00 43.83
ATOM   2101  C   LYS A 277      -1.755  32.328  54.894  1.00 40.47
ATOM   2102  O   LYS A 277      -1.032  31.331  54.983  1.00 37.45
ATOM   2103  CB  LYS A 277      -2.060  32.874  57.319  1.00 45.06
ATOM   2104  CG  LYS A 277      -1.147  34.092  57.369  1.00 46.91
ATOM   2105  CD  LYS A 277      -0.218  34.078  58.585  1.00 48.15
ATOM   2106  CE  LYS A 277      -0.996  33.941  59.896  1.00 50.55
ATOM   2107  NZ  LYS A 277      -2.106  34.937  60.033  1.00 50.81
ATOM   2108  N   ARG A 278      -1.724  33.174  53.871  1.00 37.31
ATOM   2109  CA  ARG A 278      -0.813  33.019  52.752  1.00 35.46
ATOM   2110  C   ARG A 278       0.576  33.500  53.145  1.00 33.63
ATOM   2111  O   ARG A 278       0.728  34.616  53.646  1.00 34.71
ATOM   2112  CB  ARG A 278      -1.308  33.842  51.551  1.00 34.98
ATOM   2113  CG  ARG A 278      -0.315  33.917  50.398  1.00 32.79
ATOM   2114  CD  ARG A 278       0.086  35.354  50.110  1.00 33.96
ATOM   2115  NE  ARG A 278      -0.512  35.823  48.871  1.00 33.36
ATOM   2116  CZ  ARG A 278      -0.564  37.093  48.474  1.00 32.96
ATOM   2117  NH1 ARG A 278      -0.052  38.067  49.221  1.00 32.76
ATOM   2118  NH2 ARG A 278      -1.137  37.385  47.311  1.00 29.66
ATOM   2119  N   VAL A 279       1.579  32.649  52.939  1.00 30.20
ATOM   2120  CA  VAL A 279       2.964  33.012  53.219  1.00 26.51
ATOM   2121  C   VAL A 279       3.674  32.972  51.868  1.00 24.32
ATOM   2122  O   VAL A 279       3.416  32.085  51.051  1.00 24.14
ATOM   2123  CB  VAL A 279       3.652  32.024  54.195  1.00 26.32
ATOM   2124  CG1 VAL A 279       2.949  32.058  55.546  1.00 25.08
ATOM   2125  CG2 VAL A 279       3.653  30.619  53.607  1.00 26.16
ATOM   2126  N   LEU A 280       4.552  33.938  51.624  1.00 20.93
ATOM   2127  CA  LEU A 280       5.252  34.003  50.349  1.00 19.08
ATOM   2128  C   LEU A 280       6.642  33.461  50.520  1.00 17.66
ATOM   2129  O   LEU A 280       7.133  33.371  51.639  1.00 18.32
ATOM   2130  CB  LEU A 280       5.325  35.445  49.856  1.00 18.00
ATOM   2131  CG  LEU A 280       3.978  36.195  49.791  1.00 20.17
ATOM   2132  CD1 LEU A 280       4.204  37.696  49.643  1.00 15.95
ATOM   2133  CD2 LEU A 280       3.152  35.652  48.639  1.00 17.57
ATOM   2134  N   LEU A 281       7.267  33.096  49.407  1.00 16.57
ATOM   2135  CA  LEU A 281       8.625  32.565  49.422  1.00 16.94
ATOM   2136  C   LEU A 281       9.245  32.718  48.041  1.00 15.00
ATOM   2137  O   LEU A 281       8.550  32.938  47.056  1.00 16.13
ATOM   2138  CB  LEU A 281       8.644  31.085  49.858  1.00 17.16
ATOM   2139  CG  LEU A 281       7.931  30.027  48.993  1.00 21.51
ATOM   2140  CD1 LEU A 281       8.506  28.645  49.286  1.00 23.45
ATOM   2141  CD2 LEU A 281       6.432  30.026  49.272  1.00 19.92
ATOM   2142  N   LEU A 282      10.564  32.617  47.982  1.00 14.72
ATOM   2143  CA  LEU A 282      11.295  32.754  46.735  1.00 13.95
ATOM   2144  C   LEU A 282      11.841  31.393  46.314  1.00 14.18
ATOM   2145  O   LEU A 282      12.241  30.602  47.155  1.00  9.74
ATOM   2146  CB  LEU A 282      12.482  33.699  46.942  1.00 13.13
ATOM   2147  CG  LEU A 282      13.179  34.402  45.773  1.00 16.07
ATOM   2148  CD1 LEU A 282      14.669  34.576  46.086  1.00 15.12
ATOM   2149  CD2 LEU A 282      13.010  33.633  44.516  1.00 17.21
ATOM   2150  N   ARG A 283      11.834  31.111  45.016  1.00 15.89
ATOM   2151  CA  ARG A 283      12.425  29.873  44.529  1.00 16.55
ATOM   2152  C   ARG A 283      13.352  30.229  43.375  1.00 16.38
ATOM   2153  O   ARG A 283      12.907  30.598  42.283  1.00 16.95
ATOM   2154  CB  ARG A 283      11.379  28.849  44.062  1.00 16.58
ATOM   2155  CG  ARG A 283      12.038  27.523  43.586  1.00 15.40
ATOM   2156  CD  ARG A 283      11.036  26.391  43.283  1.00 13.86
ATOM   2157  NE  ARG A 283      10.286  26.593  42.041  1.00 17.18
ATOM   2158  CZ  ARG A 283       9.639  25.630  41.379  1.00 15.81
ATOM   2159  NH1 ARG A 283       9.645  24.386  41.824  1.00 16.01
ATOM   2160  NH2 ARG A 283       8.965  25.914  40.274  1.00 13.39
ATOM   2161  N   GLU A 284      14.649  30.153  43.654  1.00 15.90
ATOM   2162  CA  GLU A 284      15.683  30.423  42.676  1.00 14.11
ATOM   2163  C   GLU A 284      15.702  29.247  41.722  1.00 16.48
ATOM   2164  O   GLU A 284      15.233  28.153  42.053  1.00 15.66
ATOM   2165  CB  GLU A 284      17.055  30.487  43.360  1.00 17.74
ATOM   2166  CG  GLU A 284      17.270  31.659  44.264  1.00 17.99
ATOM   2167  CD  GLU A 284      17.092  32.948  43.503  1.00 21.75
ATOM   2168  OE1 GLU A 284      15.942  33.394  43.422  1.00 22.54
ATOM   2169  OE2 GLU A 284      18.084  33.494  42.965  1.00 20.10
ATOM   2170  N   SER A 285      16.270  29.464  40.549  1.00 17.42
ATOM   2171  CA  SER A 285      16.393  28.402  39.571  1.00 21.52
ATOM   2172  C   SER A 285      17.084  27.198  40.231  1.00 22.34
ATOM   2173  O   SER A 285      16.636  26.056  40.095  1.00 20.98
ATOM   2174  CB  SER A 285      17.224  28.899  38.387  1.00 23.52
ATOM   2175  OG  SER A 285      17.556  27.836  37.520  1.00 29.19
ATOM   2176  N   ALA A 286      18.159  27.471  40.966  1.00 22.93
ATOM   2177  CA  ALA A 286      18.924  26.422  41.646  1.00 24.96
ATOM   2178  C   ALA A 286      18.125  25.640  42.701  1.00 26.45
ATOM   2179  O   ALA A 286      18.556  24.569  43.150  1.00 27.85
ATOM   2180  CB  ALA A 286      20.189  27.026  42.286  1.00 24.67
ATOM   2181  N   GLN A 287      16.967  26.164  43.098  1.00 25.68
ATOM   2182  CA  GLN A 287      16.146  25.485  44.094  1.00 24.26
ATOM   2183  C   GLN A 287      15.097  24.578  43.482  1.00 25.42
ATOM   2184  O   GLN A 287      14.375  23.879  44.196  1.00 26.74
ATOM   2185  CB  GLN A 287      15.464  26.494  45.020  1.00 22.27
ATOM   2186  CG  GLN A 287      16.353  26.943  46.153  1.00 19.61
ATOM   2187  CD  GLN A 287      15.782  28.109  46.911  1.00 19.13
ATOM   2188  OE1 GLN A 287      15.530  29.165  46.341  1.00 20.00
ATOM   2189  NE2 GLN A 287      15.576  27.928  48.202  1.00 19.71
ATOM   2190  N   CYS A 288      14.997  24.594  42.160  1.00 26.23
ATOM   2191  CA  CYS A 288      14.038  23.725  41.494  1.00 26.75
ATOM   2192  C   CYS A 288      14.695  22.381  41.235  1.00 25.29
ATOM   2193  O   CYS A 288      15.789  22.325  40.673  1.00 24.98
ATOM   2194  CB  CYS A 288      13.598  24.309  40.161  1.00 26.05
ATOM   2195  SG  CYS A 288      12.420  23.213  39.319  1.00 31.23
ATOM   2196  N   PRO A 289      14.052  21.279  41.655  1.00 25.71
ATOM   2197  CA  PRO A 289      14.677  19.974  41.399  1.00 25.67
ATOM   2198  C   PRO A 289      15.081  19.901  39.932  1.00 26.95
ATOM   2199  O   PRO A 289      14.262  20.133  39.040  1.00 25.40
ATOM   2200  CB  PRO A 289      13.585  18.967  41.790  1.00 25.74
ATOM   2201  CG  PRO A 289      12.315  19.793  41.923  1.00 25.35
ATOM   2202  CD  PRO A 289      12.784  21.136  42.385  1.00 24.04
ATOM   2203  N   LYS A 290      16.360  19.618  39.698  1.00 29.14
ATOM   2204  CA  LYS A 290      16.917  19.562  38.349  1.00 31.37
ATOM   2205  C   LYS A 290      16.035  18.905  37.305  1.00 32.29
ATOM   2206  O   LYS A 290      15.957  19.387  36.179  1.00 33.05
ATOM   2207  CB  LYS A 290      18.284  18.861  38.366  1.00 34.61
ATOM   2208  CG  LYS A 290      18.320  17.579  39.197  1.00 37.26
ATOM   2209  CD  LYS A 290      19.452  16.617  38.783  1.00 40.78
ATOM   2210  CE  LYS A 290      20.864  17.154  39.034  1.00 41.28
ATOM   2211  NZ  LYS A 290      21.319  18.130  38.003  1.00 43.32
ATOM   2212  N   ALA A 291      15.361  17.818  37.677  1.00 33.02
ATOM   2213  CA  ALA A 291      14.507  17.088  36.742  1.00 34.12
ATOM   2214  C   ALA A 291      13.060  17.577  36.627  1.00 35.54
ATOM   2215  O   ALA A 291      12.215  16.875  36.071  1.00 34.99
ATOM   2216  CB  ALA A 291      14.524  15.602  37.093  1.00 32.62
ATOM   2217  N   ASP A 292      12.785  18.772  37.144  1.00 37.55
ATOM   2218  CA  ASP A 292      11.447  19.367  37.112  1.00 38.80
ATOM   2219  C   ASP A 292      11.550  20.801  36.651  1.00 38.97
ATOM   2220  O   ASP A 292      10.633  21.592  36.854  1.00 36.59
ATOM   2221  CB  ASP A 292      10.836  19.382  38.508  1.00 42.71
ATOM   2222  CG  ASP A 292      10.061  18.140  38.816  1.00 44.67
ATOM   2223  OD1 ASP A 292      10.297  17.558  39.894  1.00 48.90
ATOM   2224  OD2 ASP A 292       9.207  17.756  37.991  1.00 47.84
ATOM   2225  N   MET A 293      12.683  21.127  36.046  1.00 40.08
ATOM   2226  CA  MET A 293      12.958  22.470  35.570  1.00 42.26
ATOM   2227  C   MET A 293      11.926  23.110  34.645  1.00 42.92
ATOM   2228  O   MET A 293      11.745  24.332  34.670  1.00 40.45
ATOM   2229  CB  MET A 293      14.337  22.489  34.916  1.00 44.00
ATOM   2230  CG  MET A 293      15.466  22.628  35.918  1.00 47.18
ATOM   2231  SD  MET A 293      15.394  24.364  36.793  1.00 54.58
ATOM   2232  CE  MET A 293      15.687  25.480  35.247  1.00 49.64
ATOM   2233  N   GLU A 294      11.245  22.306  33.832  1.00 44.00
ATOM   2234  CA  GLU A 294      10.251  22.867  32.919  1.00 45.73
ATOM   2235  C   GLU A 294       9.161  23.625  33.673  1.00 44.00
ATOM   2236  O   GLU A 294       8.650  24.631  33.187  1.00 43.77
ATOM   2237  CB  GLU A 294       9.628  21.773  32.042  1.00 48.94
ATOM   2238  CG  GLU A 294       8.823  20.722  32.794  1.00 55.39
ATOM   2239  CD  GLU A 294       8.339  19.582  31.888  1.00 59.84
ATOM   2240  OE1 GLU A 294       8.700  19.559  30.685  1.00 61.90
ATOM   2241  OE2 GLU A 294       7.598  18.703  32.388  1.00 60.81
ATOM   2242  N   SER A 295       8.804  23.148  34.860  1.00 41.55
ATOM   2243  CA  SER A 295       7.792  23.836  35.654  1.00 39.84
ATOM   2244  C   SER A 295       8.312  25.214  36.117  1.00 37.74
ATOM   2245  O   SER A 295       7.545  26.177  36.179  1.00 37.18
ATOM   2246  CB  SER A 295       7.397  22.988  36.865  1.00 40.42
ATOM   2247  OG  SER A 295       8.499  22.785  37.728  1.00 42.36
ATOM   2248  N   PHE A 296       9.602  25.302  36.451  1.00 34.08
ATOM   2249  CA  PHE A 296      10.200  26.573  36.866  1.00 30.66
ATOM   2250  C   PHE A 296      10.229  27.480  35.639  1.00 31.41
ATOM   2251  O   PHE A 296      10.098  28.699  35.749  1.00 31.27
ATOM   2252  CB  PHE A 296      11.644  26.365  37.363  1.00 26.36
ATOM   2253  CG  PHE A 296      12.415  27.656  37.599  1.00 22.02
ATOM   2254  CD1 PHE A 296      12.429  28.269  38.855  1.00 19.45
ATOM   2255  CD2 PHE A 296      13.089  28.279  36.550  1.00 17.77
ATOM   2256  CE1 PHE A 296      13.098  29.483  39.063  1.00 17.65
ATOM   2257  CE2 PHE A 296      13.756  29.486  36.738  1.00 17.58
ATOM   2258  CZ  PHE A 296      13.763  30.099  38.003  1.00 18.46
ATOM   2259  N   GLN A 297      10.404  26.869  34.470  1.00 31.46
ATOM   2260  CA  GLN A 297      10.500  27.607  33.200  1.00 32.75
ATOM   2261  C   GLN A 297       9.181  28.104  32.607  1.00 30.90
ATOM   2262  O   GLN A 297       9.170  28.959  31.713  1.00 30.13
ATOM   2263  CB  GLN A 297      11.201  26.738  32.148  1.00 34.93
ATOM   2264  CG  GLN A 297      12.710  26.585  32.330  1.00 41.12
ATOM   2265  CD  GLN A 297      13.302  25.516  31.409  1.00 44.95
ATOM   2266  OE1 GLN A 297      12.893  25.368  30.245  1.00 47.32
ATOM   2267  NE2 GLN A 297      14.276  24.774  31.924  1.00 46.25
ATOM   2268  N   ASP A 298       8.078  27.546  33.087  1.00 28.88
ATOM   2269  CA  ASP A 298       6.761  27.914  32.602  1.00 27.64
ATOM   2270  C   ASP A 298       6.412  29.284  33.164  1.00 25.61
ATOM   2271  O   ASP A 298       6.093  29.418  34.353  1.00 24.99
ATOM   2272  CB  ASP A 298       5.751  26.849  33.047  1.00 29.68
ATOM   2273  CG  ASP A 298       4.317  27.243  32.767  1.00 32.41
ATOM   2274  OD1 ASP A 298       4.099  28.221  32.023  1.00 36.03
ATOM   2275  OD2 ASP A 298       3.405  26.566  33.288  1.00 34.32
ATOM   2276  N   ILE A 299       6.486  30.302  32.315  1.00 24.48
ATOM   2277  CA  ILE A 299       6.199  31.658  32.757  1.00 25.31
ATOM   2278  C   ILE A 299       4.722  31.966  32.977  1.00 26.74
ATOM   2279  O   ILE A 299       4.363  33.090  33.331  1.00 27.04
ATOM   2280  CB  ILE A 299       6.793  32.715  31.799  1.00 24.24
ATOM   2281  CG1 ILE A 299       6.021  32.762  30.487  1.00 24.80
ATOM   2282  CG2 ILE A 299       8.248  32.394  31.509  1.00 22.03
ATOM   2283  CD1 ILE A 299       6.527  33.889  29.563  1.00 24.91
ATOM   2284  N   ASN A 300       3.861  30.977  32.774  1.00 27.64
ATOM   2285  CA  ASN A 300       2.439  31.187  32.996  1.00 28.88
ATOM   2286  C   ASN A 300       2.104  30.696  34.392  1.00 29.57
ATOM   2287  O   ASN A 300       1.379  31.361  35.137  1.00 29.34
ATOM   2288  CB  ASN A 300       1.623  30.433  31.949  1.00 30.66
ATOM   2289  CG  ASN A 300       1.906  30.924  30.550  1.00 32.83
ATOM   2290  OD1 ASN A 300       2.292  30.153  29.667  1.00 36.72
ATOM   2291  ND2 ASN A 300       1.730  32.219  30.341  1.00 33.08
ATOM   2292  N   LYS A 301       2.648  29.537  34.752  1.00 28.94
ATOM   2293  CA  LYS A 301       2.403  28.977  36.073  1.00 29.32
ATOM   2294  C   LYS A 301       2.951  29.916  37.155  1.00 28.00
ATOM   2295  O   LYS A 301       2.289  30.165  38.157  1.00 28.34
ATOM   2296  CB  LYS A 301       3.062  27.605  36.188  1.00 32.76
ATOM   2297  CG  LYS A 301       2.712  26.830  37.457  1.00 36.72
ATOM   2298  CD  LYS A 301       3.115  25.354  37.310  1.00 40.52
ATOM   2299  CE  LYS A 301       2.600  24.481  38.455  1.00 41.86
ATOM   2300  NZ  LYS A 301       2.980  23.051  38.233  1.00 41.43
ATOM   2301  N   TYR A 302       4.159  30.433  36.951  1.00 25.39
ATOM   2302  CA  TYR A 302       4.766  31.357  37.912  1.00 23.95
ATOM   2303  C   TYR A 302       5.146  32.609  37.159  1.00 21.29
ATOM   2304  O   TYR A 302       6.272  32.739  36.671  1.00 18.69
ATOM   2305  CB  TYR A 302       6.014  30.739  38.559  1.00 25.80
ATOM   2306  CG  TYR A 302       5.734  29.443  39.284  1.00 27.48
ATOM   2307  CD1 TYR A 302       6.161  28.227  38.759  1.00 28.58
ATOM   2308  CD2 TYR A 302       5.024  29.431  40.485  1.00 29.84
ATOM   2309  CE1 TYR A 302       5.896  27.032  39.405  1.00 29.35
ATOM   2310  CE2 TYR A 302       4.747  28.233  41.142  1.00 30.69
ATOM   2311  CZ  TYR A 302       5.190  27.039  40.591  1.00 30.76
ATOM   2312  OH  TYR A 302       4.934  25.844  41.221  1.00 34.98
ATOM   2313  N   SER A 303       4.197  33.534  37.073  1.00 20.53
ATOM   2314  CA  SER A 303       4.404  34.762  36.323  1.00 19.44
ATOM   2315  C   SER A 303       4.990  35.931  37.077  1.00 19.57
ATOM   2316  O   SER A 303       5.155  37.003  36.503  1.00 20.45
ATOM   2317  CB  SER A 303       3.088  35.189  35.677  1.00 22.00
ATOM   2318  OG  SER A 303       2.035  35.131  36.617  1.00 23.09
ATOM   2319  N   PHE A 304       5.293  35.744  38.356  1.00 18.64
ATOM   2320  CA  PHE A 304       5.885  36.828  39.135  1.00 18.12
ATOM   2321  C   PHE A 304       7.355  36.540  39.410  1.00 17.48
ATOM   2322  O   PHE A 304       7.712  35.688  40.236  1.00 16.10
ATOM   2323  CB  PHE A 304       5.093  37.045  40.422  1.00 16.86
ATOM   2324  CG  PHE A 304       3.766  37.739  40.194  1.00 19.55
ATOM   2325  CD1 PHE A 304       2.563  37.129  40.560  1.00 18.63
ATOM   2326  CD2 PHE A 304       3.727  39.005  39.616  1.00 18.67
ATOM   2327  CE1 PHE A 304       1.328  37.774  40.355  1.00 20.52
ATOM   2328  CE2 PHE A 304       2.510  39.658  39.405  1.00 21.89
ATOM   2329  CZ  PHE A 304       1.302  39.037  39.779  1.00 21.04
ATOM   2330  N   PHE A 305       8.195  37.276  38.690  1.00 15.33
ATOM   2331  CA  PHE A 305       9.639  37.129  38.735  1.00 14.42
ATOM   2332  C   PHE A 305      10.247  38.174  39.649  1.00 14.27
ATOM   2333  O   PHE A 305       9.934  39.357  39.548  1.00 15.87
ATOM   2334  CB  PHE A 305      10.200  37.303  37.313  1.00 14.74
ATOM   2335  CG  PHE A 305      11.549  36.649  37.083  1.00 15.64
ATOM   2336  CD1 PHE A 305      11.665  35.259  37.019  1.00 14.86
ATOM   2337  CD2 PHE A 305      12.701  37.425  36.921  1.00 14.33
ATOM   2338  CE1 PHE A 305      12.908  34.647  36.799  1.00 15.70
ATOM   2339  CE2 PHE A 305      13.947  36.829  36.699  1.00 14.62
ATOM   2340  CZ  PHE A 305      14.057  35.439  36.639  1.00 14.96
ATOM   2341  N   ASN A 306      11.125  37.729  40.533  1.00 12.37
ATOM   2342  CA  ASN A 306      11.806  38.617  41.461  1.00 13.69
ATOM   2343  C   ASN A 306      12.813  39.514  40.740  1.00 12.80
ATOM   2344  O   ASN A 306      13.641  39.036  39.955  1.00  9.92
ATOM   2345  CB  ASN A 306      12.521  37.787  42.537  1.00 13.76
ATOM   2346  CG  ASN A 306      13.333  38.636  43.486  1.00 16.81
ATOM   2347  OD1 ASN A 306      12.921  39.742  43.857  1.00 19.19
ATOM   2348  ND2 ASN A 306      14.485  38.117  43.908  1.00 12.04
ATOM   2349  N   THR A 307      12.735  40.815  41.005  1.00 11.52
ATOM   2350  CA  THR A 307      13.660  41.771  40.393  1.00 11.52
ATOM   2351  C   THR A 307      14.860  41.967  41.312  1.00 10.10
ATOM   2352  O   THR A 307      15.873  42.507  40.899  1.00 10.83
ATOM   2353  CB  THR A 307      13.016  43.167  40.226  1.00 13.02
ATOM   2354  OG1 THR A 307      12.837  43.757  41.524  1.00 11.55
ATOM   2355  CG2 THR A 307      11.682  43.059  39.518  1.00 12.71
ATOM   2356  N   ASN A 308      14.714  41.511  42.552  1.00 10.39
ATOM   2357  CA  ASN A 308      15.708  41.644  43.616  1.00 13.59
ATOM   2358  C   ASN A 308      15.774  43.111  44.064  1.00 13.85
ATOM   2359  O   ASN A 308      16.768  43.539  44.669  1.00 14.43
ATOM   2360  CB  ASN A 308      17.112  41.112  43.202  1.00 17.34
ATOM   2361  CG  ASN A 308      17.663  40.066  44.175  1.00 19.92
ATOM   2362  OD1 ASN A 308      17.628  40.266  45.375  1.00 22.76
ATOM   2363  ND2 ASN A 308      18.178  38.963  43.653  1.00 29.81
ATOM   2364  N   ASN A 309      14.752  43.875  43.731  1.00 12.19
ATOM   2365  CA  ASN A 309      14.610  45.228  44.221  1.00 13.05
ATOM   2366  C   ASN A 309      13.875  45.043  45.529  1.00 12.32
ATOM   2367  O   ASN A 309      12.667  44.886  45.563  1.00 14.50
ATOM   2368  CB  ASN A 309      13.764  46.115  43.302  1.00 12.54
ATOM   2369  CG  ASN A 309      14.332  46.306  41.924  1.00 14.32
ATOM   2370  OD1 ASN A 309      15.516  46.050  41.698  1.00 15.71
ATOM   2371  ND2 ASN A 309      13.511  46.745  40.990  1.00 14.55
ATOM   2372  N   LEU A 310      14.619  45.053  46.628  1.00 12.37
ATOM   2373  CA  LEU A 310      14.055  44.789  47.949  1.00 12.34
ATOM   2374  C   LEU A 310      14.155  45.958  48.905  1.00 10.93
ATOM   2375  O   LEU A 310      15.125  46.712  48.885  1.00  9.27
ATOM   2376  CB  LEU A 310      14.758  43.586  48.603  1.00 11.59
ATOM   2377  CG  LEU A 310      14.414  42.138  48.250  1.00 14.37
ATOM   2378  CD1 LEU A 310      13.886  42.012  46.844  1.00 10.11
ATOM   2379  CD2 LEU A 310      15.661  41.302  48.460  1.00 12.21
ATOM   2380  N   TRP A 311      13.131  46.064  49.743  1.00 12.44
ATOM   2381  CA  TRP A 311      13.014  47.091  50.762  1.00 14.75
ATOM   2382  C   TRP A 311      12.893  46.369  52.093  1.00 14.94
ATOM   2383  O   TRP A 311      12.095  45.429  52.244  1.00 15.35
ATOM   2384  CB  TRP A 311      11.756  47.925  50.549  1.00 11.94
ATOM   2385  CG  TRP A 311      11.684  48.583  49.226  1.00 14.74
ATOM   2386  CD1 TRP A 311      11.337  48.007  48.037  1.00 13.38
ATOM   2387  CD2 TRP A 311      11.894  49.971  48.958  1.00 12.94
ATOM   2388  NE1 TRP A 311      11.312  48.958  47.041  1.00 15.43
ATOM   2389  CE2 TRP A 311      11.656  50.172  47.579  1.00 16.06
ATOM   2390  CE3 TRP A 311      12.270  51.063  49.748  1.00 15.00
ATOM   2391  CZ2 TRP A 311      11.761  51.432  46.972  1.00 15.04
ATOM   2392  CZ3 TRP A 311      12.378  52.316  49.148  1.00 15.57
ATOM   2393  CH2 TRP A 311      12.126  52.486  47.768  1.00 13.66
ATOM   2394  N   ILE A 312      13.685  46.815  53.054  1.00 16.04
ATOM   2395  CA  ILE A 312      13.686  46.217  54.375  1.00 15.83
ATOM   2396  C   ILE A 312      13.710  47.269  55.466  1.00 15.30
ATOM   2397  O   ILE A 312      14.470  48.242  55.383  1.00 15.21
ATOM   2398  CB  ILE A 312      14.924  45.314  54.597  1.00 17.90
ATOM   2399  CG1 ILE A 312      15.115  44.366  53.402  1.00 21.45
ATOM   2400  CG2 ILE A 312      14.730  44.484  55.883  1.00 18.93
ATOM   2401  CD1 ILE A 312      16.074  44.874  52.347  1.00 21.42
ATOM   2402  N   ARG A 313      12.873  47.061  56.481  1.00 14.62
ATOM   2403  CA  ARG A 313      12.809  47.949  57.628  1.00 14.26
ATOM   2404  C   ARG A 313      13.885  47.437  58.577  1.00 13.45
ATOM   2405  O   ARG A 313      13.775  46.349  59.165  1.00 12.75
ATOM   2406  CB  ARG A 313      11.423  47.902  58.282  1.00 15.93
ATOM   2407  CG  ARG A 313      11.387  48.600  59.624  1.00 22.90
ATOM   2408  CD  ARG A 313      10.027  49.198  59.974  1.00 26.97
ATOM   2409  NE  ARG A 313       8.998  48.947  58.967  1.00 32.12
ATOM   2410  CZ  ARG A 313       7.945  49.738  58.777  1.00 34.91
ATOM   2411  NH1 ARG A 313       7.794  50.829  59.527  1.00 35.76
ATOM   2412  NH2 ARG A 313       7.046  49.448  57.842  1.00 34.39
ATOM   2413  N   LEU A 314      14.945  48.228  58.677  1.00 13.14
ATOM   2414  CA  LEU A 314      16.119  47.930  59.476  1.00 11.64
ATOM   2415  C   LEU A 314      15.934  47.577  60.956  1.00 12.94
ATOM   2416  O   LEU A 314      16.533  46.623  61.442  1.00 12.86
ATOM   2417  CB  LEU A 314      17.097  49.092  59.322  1.00 12.06
ATOM   2418  CG  LEU A 314      17.454  49.304  57.849  1.00 15.50
ATOM   2419  CD1 LEU A 314      18.345  50.540  57.660  1.00 12.98
ATOM   2420  CD2 LEU A 314      18.141  48.044  57.346  1.00 12.33
ATOM   2421  N   PRO A 315      15.126  48.346  61.699  1.00 11.70
ATOM   2422  CA  PRO A 315      14.964  47.987  63.114  1.00 13.33
ATOM   2423  C   PRO A 315      14.378  46.588  63.298  1.00 12.64
ATOM   2424  O   PRO A 315      14.753  45.855  64.217  1.00 10.93
ATOM   2425  CB  PRO A 315      14.023  49.070  63.654  1.00 11.37
ATOM   2426  CG  PRO A 315      14.313  50.230  62.762  1.00 15.28
ATOM   2427  CD  PRO A 315      14.491  49.636  61.397  1.00 10.32
ATOM   2428  N   VAL A 316      13.442  46.241  62.424  1.00 12.33
ATOM   2429  CA  VAL A 316      12.772  44.957  62.487  1.00 12.00
ATOM   2430  C   VAL A 316      13.719  43.830  62.108  1.00 13.90
ATOM   2431  O   VAL A 316      13.713  42.773  62.721  1.00 13.40
ATOM   2432  CB  VAL A 316      11.536  44.950  61.565  1.00 12.29
ATOM   2433  CG1 VAL A 316      10.819  43.608  61.650  1.00 10.59
ATOM   2434  CG2 VAL A 316      10.586  46.086  61.967  1.00 12.96
ATOM   2435  N   LEU A 317      14.537  44.065  61.094  1.00 13.42
ATOM   2436  CA  LEU A 317      15.486  43.059  60.672  1.00 13.43
ATOM   2437  C   LEU A 317      16.425  42.796  61.830  1.00 13.37
ATOM   2438  O   LEU A 317      16.685  41.643  62.197  1.00 17.30
ATOM   2439  CB  LEU A 317      16.289  43.567  59.475  1.00 11.33
ATOM   2440  CG  LEU A 317      17.507  42.744  59.091  1.00 10.30
ATOM   2441  CD1 LEU A 317      17.071  41.411  58.458  1.00  9.21
ATOM   2442  CD2 LEU A 317      18.344  43.564  58.126  1.00  9.37
ATOM   2443  N   LEU A 318      16.921  43.875  62.416  1.00 12.00
ATOM   2444  CA  LEU A 318      17.859  43.779  63.516  1.00 13.19
ATOM   2445  C   LEU A 318      17.257  43.016  64.692  1.00 14.79
ATOM   2446  O   LEU A 318      17.904  42.128  65.263  1.00 13.55
ATOM   2447  CB  LEU A 318      18.308  45.188  63.940  1.00 12.02
ATOM   2448  CG  LEU A 318      19.269  45.335  65.132  1.00 13.92
ATOM   2449  CD1 LEU A 318      20.560  44.525  64.922  1.00  9.85
ATOM   2450  CD2 LEU A 318      19.589  46.817  65.322  1.00 11.77
ATOM   2451  N   GLU A 319      16.021  43.343  65.058  1.00 15.90
ATOM   2452  CA  GLU A 319      15.407  42.644  66.182  1.00 19.26
ATOM   2453  C   GLU A 319      15.099  41.176  65.886  1.00 17.50
ATOM   2454  O   GLU A 319      15.335  40.332  66.740  1.00 12.69
ATOM   2455  CB  GLU A 319      14.137  43.378  66.684  1.00 20.65
ATOM   2456  CG  GLU A 319      12.969  43.439  65.716  1.00 30.02
ATOM   2457  CD  GLU A 319      11.805  44.303  66.230  1.00 35.49
ATOM   2458  OE1 GLU A 319      11.996  45.066  67.210  1.00 37.23
ATOM   2459  OE2 GLU A 319      10.704  44.222  65.634  1.00 36.40
ATOM   2460  N   THR A 320      14.586  40.848  64.697  1.00 16.93
ATOM   2461  CA  THR A 320      14.306  39.430  64.483  1.00 18.08
ATOM   2462  C   THR A 320      15.592  38.610  64.423  1.00 17.19
ATOM   2463  O   THR A 320      15.588  37.449  64.805  1.00 15.42
ATOM   2464  CB  THR A 320      13.389  39.107  63.250  1.00 18.21
ATOM   2465  OG1 THR A 320      14.156  38.487  62.218  1.00 20.38
ATOM   2466  CG2 THR A 320      12.688  40.325  62.748  1.00 10.23
ATOM   2467  N   MET A 321      16.694  39.210  63.976  1.00 17.46
ATOM   2468  CA  MET A 321      17.963  38.478  63.937  1.00 18.60
ATOM   2469  C   MET A 321      18.460  38.280  65.368  1.00 18.57
ATOM   2470  O   MET A 321      18.998  37.222  65.719  1.00 16.94
ATOM   2471  CB  MET A 321      19.013  39.234  63.106  1.00 17.96
ATOM   2472  CG  MET A 321      18.785  39.096  61.595  1.00 16.66
ATOM   2473  SD  MET A 321      20.107  39.967  60.504  1.00 19.08
ATOM   2474  CE  MET A 321      21.499  38.594  60.531  1.00 16.24
ATOM   2475  N   GLN A 322      18.266  39.303  66.194  1.00 17.33
ATOM   2476  CA  GLN A 322      18.680  39.233  67.589  1.00 18.31
ATOM   2477  C   GLN A 322      17.930  38.122  68.298  1.00 18.93
ATOM   2478  O   GLN A 322      18.534  37.341  69.023  1.00 20.48
ATOM   2479  CB  GLN A 322      18.418  40.573  68.307  1.00 14.58
ATOM   2480  CG  GLN A 322      19.483  41.578  67.996  1.00 13.41
ATOM   2481  CD  GLN A 322      19.150  43.015  68.367  1.00  8.82
ATOM   2482  OE1 GLN A 322      20.043  43.849  68.365  1.00 14.00
ATOM   2483  NE2 GLN A 322      17.891  43.312  68.678  1.00  9.21
ATOM   2484  N   GLU A 323      16.622  38.045  68.079  1.00 21.51
ATOM   2485  CA  GLU A 323      15.814  37.023  68.743  1.00 26.11
ATOM   2486  C   GLU A 323      16.076  35.641  68.215  1.00 25.34
ATOM   2487  O   GLU A 323      15.666  34.658  68.821  1.00 27.29
ATOM   2488  CB  GLU A 323      14.308  37.302  68.615  1.00 28.39
ATOM   2489  CG  GLU A 323      13.723  37.366  67.189  1.00 37.10
ATOM   2490  CD  GLU A 323      13.515  36.001  66.482  1.00 41.18
ATOM   2491  OE1 GLU A 323      12.643  35.906  65.588  1.00 44.39
ATOM   2492  OE2 GLU A 323      14.213  35.014  66.779  1.00 47.03
ATOM   2493  N   HIS A 324      16.751  35.559  67.081  1.00 26.82
ATOM   2494  CA  HIS A 324      17.016  34.277  66.487  1.00 27.46
ATOM   2495  C   HIS A 324      18.487  33.894  66.543  1.00 26.88
ATOM   2496  O   HIS A 324      19.041  33.409  65.562  1.00 27.43
ATOM   2497  CB  HIS A 324      16.531  34.288  65.045  1.00 30.11
ATOM   2498  CG  HIS A 324      16.145  32.936  64.549  1.00 36.83
ATOM   2499  ND1 HIS A 324      17.056  31.911  64.414  1.00 38.79
ATOM   2500  CD2 HIS A 324      14.932  32.409  64.265  1.00 37.76
ATOM   2501  CE1 HIS A 324      16.420  30.803  64.074  1.00 39.63
ATOM   2502  NE2 HIS A 324      15.130  31.078  63.979  1.00 41.18
ATOM   2503  N   GLY A 325      19.121  34.141  67.681  1.00 25.43
ATOM   2504  CA  GLY A 325      20.516  33.781  67.836  1.00 22.25
ATOM   2505  C   GLY A 325      21.511  34.603  67.054  1.00 20.23
ATOM   2506  O   GLY A 325      22.664  34.211  66.905  1.00 20.11
ATOM   2507  N   GLY A 326      21.076  35.741  66.537  1.00 20.00
ATOM   2508  CA  GLY A 326      21.982  36.587  65.777  1.00 17.76
ATOM   2509  C   GLY A 326      22.231  36.078  64.370  1.00 17.60
ATOM   2510  O   GLY A 326      23.362  36.073  63.890  1.00 19.41
ATOM   2511  N   THR A 327      21.164  35.649  63.706  1.00 17.18
ATOM   2512  CA  THR A 327      21.241  35.132  62.341  1.00 16.26
ATOM   2513  C   THR A 327      19.869  35.259  61.708  1.00 14.87
ATOM   2514  O   THR A 327      18.885  35.505  62.380  1.00 14.58
ATOM   2515  CB  THR A 327      21.607  33.611  62.284  1.00 18.08
ATOM   2516  OG1 THR A 327      20.502  32.838  62.770  1.00 19.96
ATOM   2517  CG2 THR A 327      22.825  33.301  63.129  1.00 17.46
ATOM   2518  N   LEU A 328      19.810  35.093  60.403  1.00 15.37
ATOM   2519  CA  LEU A 328      18.546  35.120  59.695  1.00 17.11
ATOM   2520  C   LEU A 328      18.566  33.744  59.055  1.00 17.19
ATOM   2521  O   LEU A 328      19.345  33.479  58.154  1.00 20.25
ATOM   2522  CB  LEU A 328      18.523  36.217  58.632  1.00 17.57
ATOM   2523  CG  LEU A 328      17.121  36.489  58.067  1.00 17.34
ATOM   2524  CD1 LEU A 328      16.230  37.017  59.193  1.00 17.54
ATOM   2525  CD2 LEU A 328      17.196  37.512  56.929  1.00 17.68
ATOM   2526  N   PRO A 329      17.723  32.835  59.542  1.00 19.01
ATOM   2527  CA  PRO A 329      17.671  31.478  59.007  1.00 18.60
ATOM   2528  C   PRO A 329      17.086  31.337  57.615  1.00 19.13
ATOM   2529  O   PRO A 329      16.023  30.746  57.452  1.00 21.83
ATOM   2530  CB  PRO A 329      16.843  30.748  60.043  1.00 20.74
ATOM   2531  CG  PRO A 329      15.834  31.821  60.433  1.00 21.11
ATOM   2532  CD  PRO A 329      16.750  33.009  60.636  1.00 18.64
ATOM   2533  N   LEU A 330      17.782  31.864  56.610  1.00 17.82
ATOM   2534  CA  LEU A 330      17.327  31.777  55.227  1.00 15.03
ATOM   2535  C   LEU A 330      17.500  30.352  54.741  1.00 17.19
ATOM   2536  O   LEU A 330      18.441  29.665  55.152  1.00 14.56
ATOM   2537  CB  LEU A 330      18.146  32.710  54.335  1.00 12.38
ATOM   2538  CG  LEU A 330      18.061  34.211  54.651  1.00 14.20
ATOM   2539  CD1 LEU A 330      18.841  34.992  53.602  1.00 11.10
ATOM   2540  CD2 LEU A 330      16.615  34.668  54.674  1.00  8.81
ATOM   2541  N   PRO A 331      16.596  29.887  53.853  1.00 18.56
ATOM   2542  CA  PRO A 331      16.696  28.520  53.328  1.00 20.41
ATOM   2543  C   PRO A 331      17.988  28.329  52.534  1.00 21.99
ATOM   2544  O   PRO A 331      18.278  29.081  51.589  1.00 21.78
ATOM   2545  CB  PRO A 331      15.437  28.375  52.458  1.00 19.50
ATOM   2546  CG  PRO A 331      15.091  29.785  52.088  1.00 18.66
ATOM   2547  CD  PRO A 331      15.386  30.560  53.346  1.00 17.02
ATOM   2548  N   VAL A 332      18.758  27.313  52.929  1.00 22.14
ATOM   2549  CA  VAL A 332      20.037  27.013  52.294  1.00 21.16
ATOM   2550  C   VAL A 332      19.929  26.547  50.849  1.00 22.39
ATOM   2551  O   VAL A 332      18.991  25.829  50.475  1.00 24.34
ATOM   2552  CB  VAL A 332      20.798  25.919  53.062  1.00 22.29
ATOM   2553  CG1 VAL A 332      20.138  24.566  52.816  1.00 22.63
ATOM   2554  CG2 VAL A 332      22.263  25.892  52.630  1.00 20.89
ATOM   2555  N   ILE A 333      20.897  26.971  50.042  1.00 20.85
ATOM   2556  CA  ILE A 333      20.983  26.568  48.654  1.00 20.23
ATOM   2557  C   ILE A 333      22.313  25.802  48.555  1.00 21.81
ATOM   2558  O   ILE A 333      23.388  26.343  48.827  1.00 19.57
ATOM   2559  CB  ILE A 333      20.982  27.774  47.714  1.00 20.59
ATOM   2560  CG1 ILE A 333      19.627  28.497  47.797  1.00 21.41
ATOM   2561  CG2 ILE A 333      21.249  27.306  46.278  1.00 21.10
ATOM   2562  CD1 ILE A 333      19.505  29.758  46.911  1.00 16.23
ATOM   2563  N   ARG A 334      22.222  24.529  48.193  1.00 23.20
ATOM   2564  CA  ARG A 334      23.390  23.660  48.099  1.00 24.51
ATOM   2565  C   ARG A 334      23.963  23.627  46.701  1.00 25.26
ATOM   2566  O   ARG A 334      23.527  22.841  45.857  1.00 26.94
ATOM   2567  CB  ARG A 334      23.008  22.240  48.514  1.00 27.38
ATOM   2568  CG  ARG A 334      24.134  21.426  49.127  1.00 28.50
ATOM   2569  CD  ARG A 334      23.685  19.988  49.324  1.00 28.37
ATOM   2570  NE  ARG A 334      23.473  19.310  48.044  1.00 31.11
ATOM   2571  CZ  ARG A 334      23.147  18.024  47.928  1.00 32.43
ATOM   2572  NH1 ARG A 334      22.987  17.283  49.017  1.00 30.99
ATOM   2573  NH2 ARG A 334      23.005  17.471  46.727  1.00 32.88
ATOM   2574  N   ASN A 335      24.953  24.477  46.463  1.00 25.42
ATOM   2575  CA  ASN A 335      25.599  24.559  45.165  1.00 24.99
ATOM   2576  C   ASN A 335      26.736  23.518  45.048  1.00 24.20
ATOM   2577  O   ASN A 335      27.579  23.401  45.925  1.00 23.39
ATOM   2578  CB  ASN A 335      26.116  25.986  44.980  1.00 26.48
ATOM   2579  CG  ASN A 335      26.731  26.217  43.621  1.00 29.20
ATOM   2580  OD1 ASN A 335      26.493  25.464  42.679  1.00 30.56
ATOM   2581  ND2 ASN A 335      27.519  27.279  43.505  1.00 30.98
ATOM   2582  N   GLU A 336      26.736  22.751  43.966  1.00 24.92
ATOM   2583  CA  GLU A 336      27.753  21.727  43.743  1.00 25.74
ATOM   2584  C   GLU A 336      28.797  22.226  42.763  1.00 24.75
ATOM   2585  O   GLU A 336      28.459  22.742  41.705  1.00 24.69
ATOM   2586  CB  GLU A 336      27.121  20.458  43.164  1.00 26.98
ATOM   2587  CG  GLU A 336      25.778  20.109  43.758  1.00 30.49
ATOM   2588  CD  GLU A 336      25.208  18.825  43.193  1.00 33.67
ATOM   2589  OE1 GLU A 336      25.600  18.431  42.071  1.00 35.77
ATOM   2590  OE2 GLU A 336      24.353  18.218  43.866  1.00 34.81
ATOM   2591  N   LYS A 337      30.065  22.066  43.122  1.00 25.22
ATOM   2592  CA  LYS A 337      31.180  22.470  42.268  1.00 25.40
ATOM   2593  C   LYS A 337      32.409  21.680  42.677  1.00 23.60
ATOM   2594  O   LYS A 337      32.293  20.719  43.436  1.00 23.18
ATOM   2595  CB  LYS A 337      31.433  23.980  42.397  1.00 28.58
ATOM   2596  CG  LYS A 337      30.386  24.784  41.649  1.00 31.61
ATOM   2597  CD  LYS A 337      30.674  26.253  41.563  1.00 36.80
ATOM   2598  CE  LYS A 337      29.632  26.918  40.663  1.00 39.69
ATOM   2599  NZ  LYS A 337      29.603  28.407  40.777  1.00 44.19
ATOM   2600  N   THR A 338      33.574  22.042  42.152  1.00 22.98
ATOM   2601  CA  THR A 338      34.812  21.361  42.547  1.00 22.13
ATOM   2602  C   THR A 338      35.668  22.461  43.173  1.00 22.65
ATOM   2603  O   THR A 338      35.563  23.613  42.756  1.00 21.02
ATOM   2604  CB  THR A 338      35.546  20.712  41.335  1.00 22.36
ATOM   2605  OG1 THR A 338      35.833  21.707  40.344  1.00 20.71
ATOM   2606  CG2 THR A 338      34.696  19.604  40.723  1.00 18.49
ATOM   2607  N   VAL A 339      36.490  22.120  44.169  1.00 24.20
ATOM   2608  CA  VAL A 339      37.306  23.124  44.864  1.00 27.38
ATOM   2609  C   VAL A 339      37.963  24.102  43.902  1.00 29.42
ATOM   2610  O   VAL A 339      38.026  25.307  44.163  1.00 29.20
ATOM   2611  CB  VAL A 339      38.428  22.504  45.723  1.00 28.51
ATOM   2612  CG1 VAL A 339      38.578  23.308  47.007  1.00 25.18
ATOM   2613  CG2 VAL A 339      38.140  21.056  46.009  1.00 30.08
ATOM   2614  N   ASP A 340      38.481  23.570  42.803  1.00 30.97
ATOM   2615  CA  ASP A 340      39.090  24.393  41.778  1.00 33.78
ATOM   2616  C   ASP A 340      38.070  24.322  40.648  1.00 35.02
ATOM   2617  O   ASP A 340      38.062  23.356  39.876  1.00 35.04
ATOM   2618  CB  ASP A 340      40.423  23.795  41.326  1.00 34.61
ATOM   2619  CG  ASP A 340      41.142  24.671  40.316  1.00 36.46
ATOM   2620  OD1 ASP A 340      40.463  25.416  39.574  1.00 35.28
ATOM   2621  OD2 ASP A 340      42.389  24.599  40.259  1.00 37.61
ATOM   2622  N   SER A 341      37.198  25.329  40.573  1.00 35.74
ATOM   2623  CA  SER A 341      36.146  25.365  39.555  1.00 37.58
ATOM   2624  C   SER A 341      36.645  24.941  38.177  1.00 38.23
ATOM   2625  O   SER A 341      35.972  24.182  37.482  1.00 39.17
ATOM   2626  CB  SER A 341      35.519  26.763  39.484  1.00 36.82
ATOM   2627  OG  SER A 341      36.497  27.750  39.216  1.00 38.91
ATOM   2628  N   SER A 342      37.831  25.413  37.803  1.00 39.20
ATOM   2629  CA  SER A 342      38.443  25.104  36.504  1.00 40.42
ATOM   2630  C   SER A 342      38.771  23.621  36.326  1.00 40.86
ATOM   2631  O   SER A 342      38.431  23.006  35.311  1.00 43.13
ATOM   2632  CB  SER A 342      39.741  25.902  36.334  1.00 39.94
ATOM   2633  OG  SER A 342      39.601  27.230  36.807  1.00 41.09
ATOM   2634  N   ASN A 343      39.449  23.061  37.318  1.00 40.10
ATOM   2635  CA  ASN A 343      39.868  21.669  37.287  1.00 39.06
ATOM   2636  C   ASN A 343      38.784  20.701  37.769  1.00 39.92
ATOM   2637  O   ASN A 343      38.362  20.747  38.927  1.00 38.91
ATOM   2638  CB  ASN A 343      41.118  21.523  38.146  1.00 38.74
ATOM   2639  CG  ASN A 343      41.619  20.112  38.206  1.00 38.82
ATOM   2640  OD1 ASN A 343      41.040  19.208  37.603  1.00 37.83
ATOM   2641  ND2 ASN A 343      42.711  19.905  38.936  1.00 38.07
ATOM   2642  N   SER A 344      38.346  19.812  36.882  1.00 39.75
ATOM   2643  CA  SER A 344      37.317  18.840  37.229  1.00 39.30
ATOM   2644  C   SER A 344      37.889  17.570  37.823  1.00 38.70
ATOM   2645  O   SER A 344      37.172  16.595  38.044  1.00 39.16
ATOM   2646  CB  SER A 344      36.462  18.506  36.010  1.00 40.72
ATOM   2647  OG  SER A 344      35.568  19.574  35.744  1.00 42.35
ATOM   2648  N   ALA A 345      39.191  17.579  38.073  1.00 37.74
ATOM   2649  CA  ALA A 345      39.847  16.439  38.687  1.00 36.31
ATOM   2650  C   ALA A 345      39.935  16.756  40.175  1.00 34.71
ATOM   2651  O   ALA A 345      40.212  15.875  40.996  1.00 34.16
ATOM   2652  CB  ALA A 345      41.250  16.244  38.105  1.00 36.48
ATOM   2653  N   SER A 346      39.716  18.027  40.516  1.00 32.89
ATOM   2654  CA  SER A 346      39.766  18.451  41.915  1.00 30.12
ATOM   2655  C   SER A 346      38.526  17.900  42.607  1.00 28.20
ATOM   2656  O   SER A 346      37.520  17.607  41.965  1.00 29.06
ATOM   2657  CB  SER A 346      39.830  19.979  42.029  1.00 29.91
ATOM   2658  OG  SER A 346      38.736  20.601  41.378  1.00 29.90
ATOM   2659  N   PRO A 347      38.593  17.727  43.929  1.00 26.80
ATOM   2660  CA  PRO A 347      37.483  17.194  44.727  1.00 24.67
ATOM   2661  C   PRO A 347      36.152  17.941  44.577  1.00 25.70
ATOM   2662  O   PRO A 347      36.123  19.174  44.420  1.00 23.95
ATOM   2663  CB  PRO A 347      38.016  17.272  46.155  1.00 24.31
ATOM   2664  CG  PRO A 347      39.516  17.169  45.972  1.00 25.12
ATOM   2665  CD  PRO A 347      39.757  18.043  44.779  1.00 25.35
ATOM   2666  N   LYS A 348      35.057  17.182  44.649  1.00 23.60
ATOM   2667  CA  LYS A 348      33.717  17.732  44.554  1.00 23.40
ATOM   2668  C   LYS A 348      33.369  18.371  45.887  1.00 21.54
ATOM   2669  O   LYS A 348      33.728  17.859  46.942  1.00 21.35
ATOM   2670  CB  LYS A 348      32.711  16.632  44.216  1.00 26.48
ATOM   2671  CG  LYS A 348      32.979  16.000  42.866  1.00 30.93
ATOM   2672  CD  LYS A 348      31.903  15.013  42.469  1.00 33.58
ATOM   2673  CE  LYS A 348      32.119  14.585  41.033  1.00 36.01
ATOM   2674  NZ  LYS A 348      32.335  15.808  40.201  1.00 35.67
ATOM   2675  N   VAL A 349      32.670  19.495  45.834  1.00 18.30
ATOM   2676  CA  VAL A 349      32.319  20.205  47.047  1.00 16.31
ATOM   2677  C   VAL A 349      30.920  20.809  46.981  1.00 15.20
ATOM   2678  O   VAL A 349      30.307  20.904  45.925  1.00 13.82
ATOM   2679  CB  VAL A 349      33.293  21.362  47.295  1.00 15.31
ATOM   2680  CG1 VAL A 349      34.716  20.842  47.343  1.00 12.50
ATOM   2681  CG2 VAL A 349      33.147  22.419  46.184  1.00 14.60
ATOM   2682  N   TYR A 350      30.432  21.206  48.140  1.00 15.72
ATOM   2683  CA  TYR A 350      29.154  21.870  48.244  1.00 17.27
ATOM   2684  C   TYR A 350      29.550  23.278  48.677  1.00 17.64
ATOM   2685  O   TYR A 350      30.494  23.446  49.454  1.00 16.54
ATOM   2686  CB  TYR A 350      28.277  21.231  49.328  1.00 18.23
ATOM   2687  CG  TYR A 350      27.684  19.881  48.957  1.00 20.66
ATOM   2688  CD1 TYR A 350      27.641  18.841  49.888  1.00 22.71
ATOM   2689  CD2 TYR A 350      27.132  19.655  47.693  1.00 19.80
ATOM   2690  CE1 TYR A 350      27.064  17.607  49.576  1.00 23.38
ATOM   2691  CE2 TYR A 350      26.550  18.428  47.372  1.00 24.09
ATOM   2692  CZ  TYR A 350      26.520  17.405  48.326  1.00 24.18
ATOM   2693  OH  TYR A 350      25.940  16.186  48.031  1.00 26.00
ATOM   2694  N   GLN A 351      28.869  24.283  48.142  1.00 17.44
ATOM   2695  CA  GLN A 351      29.122  25.666  48.528  1.00 17.79
ATOM   2696  C   GLN A 351      27.755  26.139  48.960  1.00 18.43
ATOM   2697  O   GLN A 351      26.860  26.297  48.128  1.00 20.33
ATOM   2698  CB  GLN A 351      29.636  26.485  47.335  1.00 17.88
ATOM   2699  CG  GLN A 351      30.956  25.954  46.830  1.00 19.14
ATOM   2700  CD  GLN A 351      31.568  26.746  45.692  1.00 19.96
ATOM   2701  OE1 GLN A 351      31.212  27.903  45.431  1.00 21.69
ATOM   2702  NE2 GLN A 351      32.520  26.128  45.022  1.00 19.02
ATOM   2703  N   LEU A 352      27.588  26.323  50.265  1.00 16.99
ATOM   2704  CA  LEU A 352      26.313  26.765  50.821  1.00 17.44
ATOM   2705  C   LEU A 352      26.093  28.262  50.612  1.00 17.92
ATOM   2706  O   LEU A 352      26.966  29.080  50.912  1.00 17.27
ATOM   2707  CB  LEU A 352      26.255  26.415  52.303  1.00 14.33
ATOM   2708  CG  LEU A 352      26.760  24.994  52.552  1.00 15.76
ATOM   2709  CD1 LEU A 352      26.565  24.616  54.015  1.00 13.57
ATOM   2710  CD2 LEU A 352      26.003  24.033  51.636  1.00 15.37
ATOM   2711  N   GLU A 353      24.919  28.605  50.091  1.00 17.94
ATOM   2712  CA  GLU A 353      24.585  29.988  49.806  1.00 17.39
ATOM   2713  C   GLU A 353      23.140  30.251  50.123  1.00 16.08
ATOM   2714  O   GLU A 353      22.358  29.331  50.356  1.00 14.84
ATOM   2715  CB  GLU A 353      24.795  30.294  48.323  1.00 19.34
ATOM   2716  CG  GLU A 353      25.904  29.492  47.671  1.00 24.56
ATOM   2717  CD  GLU A 353      25.888  29.599  46.159  1.00 25.15
ATOM   2718  OE1 GLU A 353      24.779  29.584  45.581  1.00 27.03
ATOM   2719  OE2 GLU A 353      26.980  29.680  45.553  1.00 25.42
ATOM   2720  N   THR A 354      22.787  31.529  50.118  1.00 15.14
ATOM   2721  CA  THR A 354      21.412  31.934  50.346  1.00 13.90
ATOM   2722  C   THR A 354      21.151  33.127  49.437  1.00 13.96
ATOM   2723  O   THR A 354      22.070  33.834  49.044  1.00 14.68
ATOM   2724  CB  THR A 354      21.161  32.330  51.817  1.00 13.30
ATOM   2725  OG1 THR A 354      22.036  33.404  52.198  1.00 15.60
ATOM   2726  CG2 THR A 354      21.388  31.129  52.728  1.00 11.90
ATOM   2727  N   ALA A 355      19.896  33.332  49.085  1.00 12.60
ATOM   2728  CA  ALA A 355      19.527  34.439  48.239  1.00 13.07
ATOM   2729  C   ALA A 355      18.799  35.485  49.108  1.00 14.46
ATOM   2730  O   ALA A 355      17.932  35.158  49.921  1.00 15.77
ATOM   2731  CB  ALA A 355      18.615  33.958  47.121  1.00 12.36
ATOM   2732  N   MET A 356      19.182  36.737  48.927  1.00 13.89
ATOM   2733  CA  MET A 356      18.618  37.890  49.624  1.00 14.34
ATOM   2734  C   MET A 356      17.089  37.928  49.657  1.00 14.17
ATOM   2735  O   MET A 356      16.493  38.257  50.685  1.00 14.73
ATOM   2736  CB  MET A 356      19.139  39.147  48.947  1.00 16.30
ATOM   2737  CG  MET A 356      18.625  40.390  49.529  1.00 21.87
ATOM   2738  SD  MET A 356      19.588  41.739  48.599  1.00 19.82
ATOM   2739  CE  MET A 356      18.434  41.994  47.054  1.00 13.88
ATOM   2740  N   GLY A 357      16.454  37.574  48.545  1.00 12.54
ATOM   2741  CA  GLY A 357      15.003  37.605  48.500  1.00 13.22
ATOM   2742  C   GLY A 357      14.281  36.569  49.350  1.00 15.08
ATOM   2743  O   GLY A 357      13.104  36.736  49.665  1.00 14.23
ATOM   2744  N   ALA A 358      14.985  35.504  49.727  1.00 14.16
ATOM   2745  CA  ALA A 358      14.396  34.454  50.538  1.00 15.55
ATOM   2746  C   ALA A 358      13.898  35.011  51.869  1.00 15.83
ATOM   2747  O   ALA A 358      13.089  34.375  52.544  1.00 18.21
ATOM   2748  CB  ALA A 358      15.428  33.324  50.783  1.00 11.11
ATOM   2749  N   ALA A 359      14.376  36.193  52.249  1.00 15.30
ATOM   2750  CA  ALA A 359      13.962  36.814  53.511  1.00 14.70
ATOM   2751  C   ALA A 359      12.465  37.114  53.542  1.00 13.86
ATOM   2752  O   ALA A 359      11.895  37.289  54.603  1.00 13.88
ATOM   2753  CB  ALA A 359      14.764  38.107  53.756  1.00 13.90
ATOM   2754  N   ILE A 360      11.830  37.151  52.375  1.00 15.66
ATOM   2755  CA  ILE A 360      10.393  37.425  52.290  1.00 15.22
ATOM   2756  C   ILE A 360       9.571  36.450  53.123  1.00 15.36
ATOM   2757  O   ILE A 360       8.409  36.718  53.447  1.00 14.55
ATOM   2758  CB  ILE A 360       9.885  37.367  50.820  1.00 14.07
ATOM   2759  CG1 ILE A 360       8.486  37.988  50.723  1.00 13.64
ATOM   2760  CG2 ILE A 360       9.845  35.912  50.327  1.00 13.03
ATOM   2761  CD1 ILE A 360       7.980  38.118  49.284  1.00 10.39
ATOM   2762  N   ALA A 361      10.174  35.318  53.471  1.00 16.06
ATOM   2763  CA  ALA A 361       9.487  34.307  54.266  1.00 19.23
ATOM   2764  C   ALA A 361       9.759  34.543  55.737  1.00 19.96
ATOM   2765  O   ALA A 361       9.163  33.889  56.565  1.00 20.18
ATOM   2766  CB  ALA A 361       9.981  32.886  53.889  1.00 17.59
ATOM   2767  N   MET A 362      10.645  35.473  56.072  1.00 21.60
ATOM   2768  CA  MET A 362      10.973  35.661  57.477  1.00 23.84
ATOM   2769  C   MET A 362      10.263  36.700  58.314  1.00 22.82
ATOM   2770  O   MET A 362      10.565  36.843  59.482  1.00 20.89
ATOM   2771  CB  MET A 362      12.444  35.931  57.642  1.00 26.17
ATOM   2772  CG  MET A 362      13.031  35.072  58.723  1.00 34.10
ATOM   2773  SD  MET A 362      13.989  33.693  57.757  1.00 38.66
ATOM   2774  CE  MET A 362      12.475  32.636  57.261  1.00 34.74
ATOM   2775  N   PHE A 363       9.349  37.448  57.735  1.00 22.73
ATOM   2776  CA  PHE A 363       8.657  38.458  58.510  1.00 22.34
ATOM   2777  C   PHE A 363       7.163  38.277  58.343  1.00 23.00
ATOM   2778  O   PHE A 363       6.675  38.097  57.234  1.00 22.49
ATOM   2779  CB  PHE A 363       9.063  39.856  58.048  1.00 18.85
ATOM   2780  CG  PHE A 363      10.535  40.100  58.079  1.00 18.76
ATOM   2781  CD1 PHE A 363      11.309  39.914  56.933  1.00 15.97
ATOM   2782  CD2 PHE A 363      11.154  40.524  59.253  1.00 18.57
ATOM   2783  CE1 PHE A 363      12.667  40.151  56.952  1.00 15.21
ATOM   2784  CE2 PHE A 363      12.519  40.759  59.283  1.00 17.42
ATOM   2785  CZ  PHE A 363      13.278  40.571  58.120  1.00 15.95
ATOM   2786  N   GLU A 364       6.447  38.316  59.455  1.00 25.32
ATOM   2787  CA  GLU A 364       5.000  38.172  59.432  1.00 27.55
ATOM   2788  C   GLU A 364       4.348  39.119  58.419  1.00 26.04
ATOM   2789  O   GLU A 364       3.453  38.719  57.683  1.00 28.13
ATOM   2790  CB  GLU A 364       4.433  38.438  60.838  1.00 30.70
ATOM   2791  CG  GLU A 364       2.903  38.552  60.918  1.00 37.05
ATOM   2792  CD  GLU A 364       2.175  37.215  60.749  1.00 42.58
ATOM   2793  OE1 GLU A 364       0.924  37.235  60.645  1.00 43.71
ATOM   2794  OE2 GLU A 364       2.842  36.147  60.726  1.00 45.82
ATOM   2795  N   SER A 365       4.813  40.364  58.353  1.00 24.81
ATOM   2796  CA  SER A 365       4.205  41.338  57.444  1.00 24.29
ATOM   2797  C   SER A 365       4.916  41.525  56.110  1.00 22.96
ATOM   2798  O   SER A 365       4.773  42.564  55.463  1.00 25.62
ATOM   2799  CB  SER A 365       4.098  42.705  58.120  1.00 20.55
ATOM   2800  OG  SER A 365       5.358  43.350  58.064  1.00 24.13
ATOM   2801  N   ALA A 366       5.682  40.531  55.694  1.00 22.50
ATOM   2802  CA  ALA A 366       6.387  40.631  54.427  1.00 20.84
ATOM   2803  C   ALA A 366       5.367  40.607  53.286  1.00 21.27
ATOM   2804  O   ALA A 366       4.250  40.095  53.433  1.00 19.85
ATOM   2805  CB  ALA A 366       7.363  39.482  54.293  1.00 19.63
ATOM   2806  N   SER A 367       5.736  41.190  52.153  1.00 20.38
ATOM   2807  CA  SER A 367       4.838  41.181  51.008  1.00 19.95
ATOM   2808  C   SER A 367       5.622  41.467  49.743  1.00 18.87
ATOM   2809  O   SER A 367       6.837  41.687  49.790  1.00 16.39
ATOM   2810  CB  SER A 367       3.721  42.220  51.186  1.00 21.43
ATOM   2811  OG  SER A 367       2.604  41.922  50.354  1.00 24.04
ATOM   2812  N   ALA A 368       4.918  41.432  48.616  1.00 18.90
ATOM   2813  CA  ALA A 368       5.503  41.697  47.305  1.00 18.72
ATOM   2814  C   ALA A 368       4.603  42.700  46.607  1.00 19.34
ATOM   2815  O   ALA A 368       3.444  42.857  46.977  1.00 20.45
ATOM   2816  CB  ALA A 368       5.576  40.420  46.480  1.00 16.71
ATOM   2817  N   ILE A 369       5.132  43.381  45.602  1.00 19.52
ATOM   2818  CA  ILE A 369       4.340  44.349  44.870  1.00 20.13
ATOM   2819  C   ILE A 369       4.744  44.261  43.406  1.00 19.65
ATOM   2820  O   ILE A 369       5.933  44.184  43.094  1.00 18.52
ATOM   2821  CB  ILE A 369       4.598  45.772  45.415  1.00 22.81
ATOM   2822  CG1 ILE A 369       3.613  46.762  44.807  1.00 24.02
ATOM   2823  CG2 ILE A 369       6.015  46.197  45.106  1.00 20.33
ATOM   2824  CD1 ILE A 369       3.747  48.172  45.360  1.00 25.05
ATOM   2825  N   VAL A 370       3.763  44.239  42.507  1.00 18.92
ATOM   2826  CA  VAL A 370       4.079  44.173  41.087  1.00 17.53
ATOM   2827  C   VAL A 370       4.526  45.563  40.660  1.00 16.26
ATOM   2828  O   VAL A 370       3.844  46.538  40.958  1.00 17.89
ATOM   2829  CB  VAL A 370       2.848  43.765  40.227  1.00 18.35
ATOM   2830  CG1 VAL A 370       3.292  43.481  38.807  1.00 18.51
ATOM   2831  CG2 VAL A 370       2.162  42.531  40.802  1.00 18.63
ATOM   2832  N   VAL A 371       5.674  45.658  39.989  1.00 15.39
ATOM   2833  CA  VAL A 371       6.191  46.941  39.513  1.00 14.08
ATOM   2834  C   VAL A 371       6.344  46.902  37.991  1.00 17.18
ATOM   2835  O   VAL A 371       6.463  45.818  37.392  1.00 17.28
ATOM   2836  CB  VAL A 371       7.576  47.285  40.140  1.00 13.21
ATOM   2837  CG1 VAL A 371       7.476  47.267  41.665  1.00 14.84
ATOM   2838  CG2 VAL A 371       8.639  46.306  39.681  1.00 11.22
ATOM   2839  N   PRO A 372       6.312  48.076  37.334  1.00 17.45
ATOM   2840  CA  PRO A 372       6.461  48.077  35.873  1.00 19.17
ATOM   2841  C   PRO A 372       7.842  47.556  35.492  1.00 19.22
ATOM   2842  O   PRO A 372       8.737  47.505  36.330  1.00 19.55
ATOM   2843  CB  PRO A 372       6.257  49.547  35.494  1.00 19.59
ATOM   2844  CG  PRO A 372       6.662  50.291  36.750  1.00 20.97
ATOM   2845  CD  PRO A 372       6.086  49.436  37.851  1.00 19.48
ATOM   2846  N   ARG A 373       8.007  47.163  34.235  1.00 18.44
ATOM   2847  CA  ARG A 373       9.284  46.630  33.754  1.00 17.81
ATOM   2848  C   ARG A 373      10.429  47.657  33.769  1.00 16.68
ATOM   2849  O   ARG A 373      11.601  47.285  33.743  1.00 16.30
ATOM   2850  CB  ARG A 373       9.103  46.083  32.333  1.00 20.50
ATOM   2851  CG  ARG A 373      10.305  45.313  31.776  1.00 23.24
ATOM   2852  CD  ARG A 373      10.333  43.899  32.302  1.00 23.14
ATOM   2853  NE  ARG A 373      11.541  43.180  31.918  1.00 23.34
ATOM   2854  CZ  ARG A 373      11.752  41.901  32.201  1.00 25.33
ATOM   2855  NH1 ARG A 373      10.824  41.210  32.864  1.00 24.05
ATOM   2856  NH2 ARG A 373      12.889  41.319  31.841  1.00 24.51
ATOM   2857  N   SER A 374      10.092  48.942  33.809  1.00 15.86
ATOM   2858  CA  SER A 374      11.102  50.003  33.821  1.00 16.73
ATOM   2859  C   SER A 374      12.029  49.951  35.039  1.00 16.99
ATOM   2860  O   SER A 374      13.118  50.524  35.014  1.00 17.70
ATOM   2861  CB  SER A 374      10.426  51.388  33.758  1.00 17.98
ATOM   2862  OG  SER A 374       9.540  51.580  34.847  1.00 19.55
ATOM   2863  N   ARG A 375      11.599  49.272  36.099  1.00 16.18
ATOM   2864  CA  ARG A 375      12.410  49.146  37.314  1.00 16.88
ATOM   2865  C   ARG A 375      13.252  47.859  37.273  1.00 17.73
ATOM   2866  O   ARG A 375      13.860  47.477  38.275  1.00 17.59
ATOM   2867  CB  ARG A 375      11.508  49.146  38.570  1.00 13.77
ATOM   2868  CG  ARG A 375      10.819  50.509  38.851  1.00 16.65
ATOM   2869  CD  ARG A 375       9.972  50.521  40.140  1.00 15.55
ATOM   2870  NE  ARG A 375      10.777  50.236  41.330  1.00 15.66
ATOM   2871  CZ  ARG A 375      11.632  51.090  41.888  1.00 17.76
ATOM   2872  NH1 ARG A 375      11.800  52.313  41.378  1.00 16.56
ATOM   2873  NH2 ARG A 375      12.345  50.710  42.942  1.00 15.01
ATOM   2874  N   PHE A 376      13.290  47.199  36.115  1.00 17.42
ATOM   2875  CA  PHE A 376      14.056  45.960  35.976  1.00 16.42
ATOM   2876  C   PHE A 376      14.713  45.791  34.594  1.00 17.08
ATOM   2877  O   PHE A 376      14.060  45.400  33.629  1.00 16.71
ATOM   2878  CB  PHE A 376      13.129  44.778  36.275  1.00 16.25
ATOM   2879  CG  PHE A 376      13.826  43.446  36.360  1.00 16.75
ATOM   2880  CD1 PHE A 376      14.933  43.271  37.174  1.00 14.84
ATOM   2881  CD2 PHE A 376      13.359  42.359  35.632  1.00 16.72
ATOM   2882  CE1 PHE A 376      15.570  42.041  37.263  1.00 12.26
ATOM   2883  CE2 PHE A 376      13.994  41.117  35.715  1.00 17.92
ATOM   2884  CZ  PHE A 376      15.106  40.962  36.535  1.00 15.83
ATOM   2885  N   ALA A 377      16.004  46.109  34.507  1.00 16.58
ATOM   2886  CA  ALA A 377      16.784  45.955  33.273  1.00 15.84
ATOM   2887  C   ALA A 377      17.958  45.045  33.662  1.00 15.18
ATOM   2888  O   ALA A 377      19.071  45.512  33.863  1.00 14.64
ATOM   2889  CB  ALA A 377      17.306  47.315  32.809  1.00 17.37
ATOM   2890  N   PRO A 378      17.719  43.729  33.769  1.00 15.63
ATOM   2891  CA  PRO A 378      18.779  42.783  34.156  1.00 16.92
ATOM   2892  C   PRO A 378      19.891  42.489  33.152  1.00 17.94
ATOM   2893  O   PRO A 378      19.694  42.557  31.941  1.00 19.25
ATOM   2894  CB  PRO A 378      17.993  41.513  34.506  1.00 16.54
ATOM   2895  CG  PRO A 378      16.859  41.549  33.484  1.00 14.46
ATOM   2896  CD  PRO A 378      16.431  43.028  33.569  1.00 17.09
ATOM   2897  N   VAL A 379      21.066  42.157  33.675  1.00 18.25
ATOM   2898  CA  VAL A 379      22.203  41.785  32.845  1.00 16.20
ATOM   2899  C   VAL A 379      22.860  40.554  33.463  1.00 16.97
ATOM   2900  O   VAL A 379      23.803  40.683  34.239  1.00 18.63
ATOM   2901  CB  VAL A 379      23.253  42.907  32.752  1.00 16.29
ATOM   2902  CG1 VAL A 379      24.475  42.402  31.978  1.00 16.12
ATOM   2903  CG2 VAL A 379      22.668  44.130  32.050  1.00 15.68
ATOM   2904  N   LYS A 380      22.342  39.372  33.131  1.00 17.01
ATOM   2905  CA  LYS A 380      22.876  38.094  33.626  1.00 19.88
ATOM   2906  C   LYS A 380      23.755  37.392  32.584  1.00 21.59
ATOM   2907  O   LYS A 380      24.585  36.551  32.928  1.00 24.28
ATOM   2908  CB  LYS A 380      21.743  37.124  33.994  1.00 19.26
ATOM   2909  CG  LYS A 380      20.707  37.701  34.928  1.00 22.46
ATOM   2910  CD  LYS A 380      21.376  38.229  36.170  1.00 22.95
ATOM   2911  CE  LYS A 380      20.463  39.161  36.917  1.00 23.16
ATOM   2912  NZ  LYS A 380      21.133  39.715  38.120  1.00 22.75
ATOM   2913  N   THR A 381      23.555  37.723  31.311  1.00 22.14
ATOM   2914  CA  THR A 381      24.307  37.092  30.229  1.00 21.97
ATOM   2915  C   THR A 381      24.793  38.152  29.252  1.00 21.82
ATOM   2916  O   THR A 381      24.443  39.316  29.381  1.00 22.16
ATOM   2917  CB  THR A 381      23.407  36.124  29.443  1.00 20.94
ATOM   2918  OG1 THR A 381      22.355  36.871  28.817  1.00 20.28
ATOM   2919  CG2 THR A 381      22.792  35.083  30.368  1.00 18.40
ATOM   2920  N   CYS A 382      25.604  37.754  28.279  1.00 21.41
ATOM   2921  CA  CYS A 382      26.072  38.711  27.277  1.00 22.01
ATOM   2922  C   CYS A 382      24.882  39.070  26.384  1.00 19.58
ATOM   2923  O   CYS A 382      24.837  40.133  25.791  1.00 18.87
ATOM   2924  CB  CYS A 382      27.207  38.110  26.444  1.00 20.78
ATOM   2925  SG  CYS A 382      28.752  37.930  27.367  1.00 27.49
ATOM   2926  N   ALA A 383      23.922  38.157  26.297  1.00 20.05
ATOM   2927  CA  ALA A 383      22.713  38.370  25.503  1.00 20.42
ATOM   2928  C   ALA A 383      21.939  39.565  26.086  1.00 20.14
ATOM   2929  O   ALA A 383      21.415  40.398  25.346  1.00 20.16
ATOM   2930  CB  ALA A 383      21.857  37.104  25.532  1.00 19.15
ATOM   2931  N   ASP A 384      21.878  39.636  27.419  1.00 18.92
ATOM   2932  CA  ASP A 384      21.210  40.729  28.107  1.00 18.99
ATOM   2933  C   ASP A 384      22.046  41.994  27.923  1.00 18.34
ATOM   2934  O   ASP A 384      21.513  43.097  27.779  1.00 18.18
ATOM   2935  CB  ASP A 384      21.072  40.440  29.608  1.00 20.48
ATOM   2936  CG  ASP A 384      20.104  39.305  29.908  1.00 24.79
ATOM   2937  OD1 ASP A 384      19.218  39.023  29.071  1.00 28.42
ATOM   2938  OD2 ASP A 384      20.212  38.703  30.998  1.00 25.09
ATOM   2939  N   LEU A 385      23.363  41.835  27.924  1.00 17.40
ATOM   2940  CA  LEU A 385      24.236  42.982  27.765  1.00 18.34
ATOM   2941  C   LEU A 385      24.035  43.621  26.399  1.00 20.20
ATOM   2942  O   LEU A 385      24.076  44.851  26.262  1.00 21.91
ATOM   2943  CB  LEU A 385      25.692  42.570  27.951  1.00 17.54
ATOM   2944  CG  LEU A 385      26.697  43.721  27.853  1.00 15.91
ATOM   2945  CD1 LEU A 385      26.326  44.842  28.810  1.00 11.12
ATOM   2946  CD2 LEU A 385      28.077  43.185  28.182  1.00 13.67
ATOM   2947  N   LEU A 386      23.811  42.787  25.390  1.00 20.34
ATOM   2948  CA  LEU A 386      23.576  43.283  24.038  1.00 22.10
ATOM   2949  C   LEU A 386      22.335  44.182  24.055  1.00 22.49
ATOM   2950  O   LEU A 386      22.337  45.290  23.525  1.00 23.37
ATOM   2951  CB  LEU A 386      23.312  42.118  23.080  1.00 21.71
ATOM   2952  CG  LEU A 386      23.686  42.331  21.608  1.00 22.29
ATOM   2953  CD1 LEU A 386      22.905  41.351  20.765  1.00 21.57
ATOM   2954  CD2 LEU A 386      23.400  43.760  21.170  1.00 23.09
ATOM   2955  N   ALA A 387      21.268  43.679  24.667  1.00 22.43
ATOM   2956  CA  ALA A 387      20.022  44.423  24.743  1.00 21.43
ATOM   2957  C   ALA A 387      20.231  45.755  25.437  1.00 21.05
ATOM   2958  O   ALA A 387      19.793  46.784  24.940  1.00 21.69
ATOM   2959  CB  ALA A 387      18.961  43.605  25.478  1.00 20.46
ATOM   2960  N   LEU A 388      20.908  45.732  26.582  1.00 21.83
ATOM   2961  CA  LEU A 388      21.167  46.946  27.350  1.00 22.66
ATOM   2962  C   LEU A 388      21.984  47.955  26.548  1.00 22.64
ATOM   2963  O   LEU A 388      21.758  49.164  26.627  1.00 22.54
ATOM   2964  CB  LEU A 388      21.928  46.608  28.639  1.00 24.71
ATOM   2965  CG  LEU A 388      21.398  47.092  29.997  1.00 26.80
ATOM   2966  CD1 LEU A 388      22.595  47.436  30.849  1.00 27.54
ATOM   2967  CD2 LEU A 388      20.486  48.321  29.882  1.00 27.42
ATOM   2968  N   ARG A 389      22.940  47.457  25.778  1.00 23.56
ATOM   2969  CA  ARG A 389      23.774  48.343  24.980  1.00 26.16
ATOM   2970  C   ARG A 389      23.069  48.932  23.760  1.00 25.39
ATOM   2971  O   ARG A 389      23.341  50.072  23.388  1.00 23.90
ATOM   2972  CB  ARG A 389      25.051  47.618  24.538  1.00 26.67
ATOM   2973  CG  ARG A 389      26.011  47.337  25.690  1.00 27.20
ATOM   2974  CD  ARG A 389      27.388  46.901  25.191  1.00 29.45
ATOM   2975  NE  ARG A 389      28.329  46.701  26.292  1.00 28.64
ATOM   2976  CZ  ARG A 389      29.587  46.294  26.147  1.00 29.97
ATOM   2977  NH1 ARG A 389      30.075  46.035  24.940  1.00 30.49
ATOM   2978  NH2 ARG A 389      30.359  46.148  27.215  1.00 32.00
ATOM   2979  N   SER A 390      22.165  48.165  23.150  1.00 25.64
ATOM   2980  CA  SER A 390      21.448  48.630  21.959  1.00 25.78
ATOM   2981  C   SER A 390      20.525  49.790  22.292  1.00 27.69
ATOM   2982  O   SER A 390      20.278  50.080  23.467  1.00 29.01
ATOM   2983  CB  SER A 390      20.623  47.499  21.347  1.00 26.63
ATOM   2984  OG  SER A 390      19.506  47.188  22.158  1.00 25.55
ATOM   2985  N   ASP A 391      20.004  50.451  21.263  1.00 28.15
ATOM   2986  CA  ASP A 391      19.129  51.587  21.490  1.00 29.38
ATOM   2987  C   ASP A 391      17.820  51.166  22.138  1.00 29.89
ATOM   2988  O   ASP A 391      16.996  52.010  22.479  1.00 31.24
ATOM   2989  CB  ASP A 391      18.877  52.366  20.182  1.00 30.71
ATOM   2990  CG  ASP A 391      18.207  51.529  19.095  1.00 30.01
ATOM   2991  OD1 ASP A 391      17.840  50.360  19.343  1.00 30.74
ATOM   2992  OD2 ASP A 391      18.043  52.060  17.974  1.00 31.76
ATOM   2993  N   ALA A 392      17.628  49.862  22.322  1.00 29.92
ATOM   2994  CA  ALA A 392      16.415  49.377  22.969  1.00 29.19
ATOM   2995  C   ALA A 392      16.276  50.029  24.352  1.00 29.31
ATOM   2996  O   ALA A 392      15.165  50.342  24.782  1.00 30.04
ATOM   2997  CB  ALA A 392      16.447  47.858  23.097  1.00 30.38
ATOM   2998  N   TYR A 393      17.396  50.236  25.046  1.00 27.71
ATOM   2999  CA  TYR A 393      17.367  50.878  26.367  1.00 27.15
ATOM   3000  C   TYR A 393      17.810  52.329  26.309  1.00 26.73
ATOM   3001  O   TYR A 393      18.760  52.668  25.604  1.00 26.87
ATOM   3002  CB  TYR A 393      18.242  50.130  27.378  1.00 23.55
ATOM   3003  CG  TYR A 393      17.572  48.893  27.928  1.00 20.97
ATOM   3004  CD1 TYR A 393      17.576  47.704  27.214  1.00 20.77
ATOM   3005  CD2 TYR A 393      16.902  48.925  29.139  1.00 18.16
ATOM   3006  CE1 TYR A 393      16.925  46.578  27.692  1.00 20.02
ATOM   3007  CE2 TYR A 393      16.253  47.809  29.627  1.00 17.77
ATOM   3008  CZ  TYR A 393      16.262  46.637  28.900  1.00 18.80
ATOM   3009  OH  TYR A 393      15.577  45.529  29.356  1.00 19.41
ATOM   3010  N   VAL A 394      17.133  53.180  27.073  1.00 26.14
ATOM   3011  CA  VAL A 394      17.443  54.610  27.085  1.00 25.51
ATOM   3012  C   VAL A 394      17.807  55.111  28.477  1.00 25.03
ATOM   3013  O   VAL A 394      17.482  54.477  29.481  1.00 24.32
ATOM   3014  CB  VAL A 394      16.231  55.438  26.556  1.00 24.26
ATOM   3015  CG1 VAL A 394      15.924  55.044  25.105  1.00 25.47
ATOM   3016  CG2 VAL A 394      15.004  55.180  27.430  1.00 21.69
ATOM   3017  N   VAL A 395      18.480  56.256  28.523  1.00 25.40
ATOM   3018  CA  VAL A 395      18.892  56.872  29.784  1.00 25.65
ATOM   3019  C   VAL A 395      17.903  57.957  30.193  1.00 26.69
ATOM   3020  O   VAL A 395      17.582  58.843  29.396  1.00 27.83
ATOM   3021  CB  VAL A 395      20.270  57.537  29.661  1.00 25.37
ATOM   3022  CG1 VAL A 395      20.690  58.073  31.010  1.00 26.71
ATOM   3023  CG2 VAL A 395      21.291  56.550  29.135  1.00 24.25
ATOM   3024  N   THR A 396      17.426  57.903  31.432  1.00 26.85
ATOM   3025  CA  THR A 396      16.478  58.907  31.894  1.00 25.50
ATOM   3026  C   THR A 396      17.250  60.042  32.538  1.00 24.82
ATOM   3027  O   THR A 396      18.478  59.988  32.633  1.00 23.34
ATOM   3028  CB  THR A 396      15.481  58.326  32.913  1.00 26.35
ATOM   3029  OG1 THR A 396      16.188  57.892  34.084  1.00 27.09
ATOM   3030  CG2 THR A 396      14.722  57.149  32.296  1.00 24.04
ATOM   3031  N   ASP A 397      16.530  61.078  32.952  1.00 24.54
ATOM   3032  CA  ASP A 397      17.149  62.229  33.594  1.00 26.92
ATOM   3033  C   ASP A 397      17.756  61.883  34.964  1.00 25.65
ATOM   3034  O   ASP A 397      18.810  62.404  35.314  1.00 25.58
ATOM   3035  CB  ASP A 397      16.126  63.354  33.729  1.00 30.82
ATOM   3036  CG  ASP A 397      15.819  64.011  32.399  1.00 35.88
ATOM   3037  OD1 ASP A 397      15.893  63.308  31.367  1.00 38.55
ATOM   3038  OD2 ASP A 397      15.496  65.219  32.382  1.00 38.90
ATOM   3039  N   ASP A 398      17.100  61.015  35.734  1.00 22.84
ATOM   3040  CA  ASP A 398      17.641  60.617  37.028  1.00 24.70
ATOM   3041  C   ASP A 398      18.621  59.450  36.862  1.00 25.00
ATOM   3042  O   ASP A 398      18.950  58.741  37.815  1.00 26.49
ATOM   3043  CB  ASP A 398      16.528  60.253  38.012  1.00 25.79
ATOM   3044  CG  ASP A 398      15.521  59.286  37.430  1.00 27.95
ATOM   3045  OD1 ASP A 398      14.744  58.725  38.228  1.00 28.25
ATOM   3046  OD2 ASP A 398      15.498  59.095  36.190  1.00 32.26
ATOM   3047  N   PHE A 399      19.069  59.277  35.619  1.00 23.71
ATOM   3048  CA  PHE A 399      20.066  58.285  35.202  1.00 21.96
ATOM   3049  C   PHE A 399      19.810  56.784  35.317  1.00 21.99
ATOM   3050  O   PHE A 399      20.725  55.998  35.574  1.00 19.36
ATOM   3051  CB  PHE A 399      21.405  58.629  35.843  1.00 21.71
ATOM   3052  CG  PHE A 399      21.831  60.044  35.588  1.00 22.54
ATOM   3053  CD1 PHE A 399      21.512  61.058  36.482  1.00 23.47
ATOM   3054  CD2 PHE A 399      22.501  60.375  34.415  1.00 24.50
ATOM   3055  CE1 PHE A 399      21.856  62.390  36.213  1.00 25.88
ATOM   3056  CE2 PHE A 399      22.850  61.701  34.133  1.00 26.70
ATOM   3057  CZ  PHE A 399      22.525  62.710  35.035  1.00 25.52
ATOM   3058  N   ARG A 400      18.564  56.385  35.107  1.00 23.47
ATOM   3059  CA  ARG A 400      18.227  54.983  35.119  1.00 24.07
ATOM   3060  C   ARG A 400      18.175  54.522  33.667  1.00 25.03
ATOM   3061  O   ARG A 400      17.926  55.317  32.754  1.00 25.27
ATOM   3062  CB  ARG A 400      16.874  54.758  35.777  1.00 24.33
ATOM   3063  CG  ARG A 400      16.799  55.275  37.179  1.00 24.96
ATOM   3064  CD  ARG A 400      15.705  54.583  37.944  1.00 26.54
ATOM   3065  NE  ARG A 400      14.495  54.441  37.155  1.00 25.79
ATOM   3066  CZ  ARG A 400      13.848  55.458  36.612  1.00 27.89
ATOM   3067  NH1 ARG A 400      14.313  56.684  36.789  1.00 26.46
ATOM   3068  NH2 ARG A 400      12.754  55.244  35.886  1.00 24.80
ATOM   3069  N   LEU A 401      18.433  53.239  33.459  1.00 24.44
ATOM   3070  CA  LEU A 401      18.383  52.670  32.124  1.00 24.80
ATOM   3071  C   LEU A 401      17.048  51.971  31.967  1.00 24.67
ATOM   3072  O   LEU A 401      16.793  50.950  32.610  1.00 24.92
ATOM   3073  CB  LEU A 401      19.525  51.674  31.916  1.00 24.23
ATOM   3074  CG  LEU A 401      20.855  52.295  31.498  1.00 27.27
ATOM   3075  CD1 LEU A 401      20.704  52.899  30.113  1.00 30.07
ATOM   3076  CD2 LEU A 401      21.289  53.363  32.494  1.00 25.60
ATOM   3077  N   VAL A 402      16.179  52.530  31.130  1.00 24.01
ATOM   3078  CA  VAL A 402      14.879  51.914  30.922  1.00 24.11
ATOM   3079  C   VAL A 402      14.621  51.599  29.462  1.00 23.93
ATOM   3080  O   VAL A 402      15.170  52.221  28.557  1.00 20.91
ATOM   3081  CB  VAL A 402      13.707  52.803  31.436  1.00 23.40
ATOM   3082  CG1 VAL A 402      13.970  53.241  32.854  1.00 21.44
ATOM   3083  CG2 VAL A 402      13.490  54.009  30.506  1.00 22.30
ATOM   3084  N   LEU A 403      13.766  50.612  29.261  1.00 26.01
ATOM   3085  CA  LEU A 403      13.382  50.166  27.942  1.00 27.38
ATOM   3086  C   LEU A 403      12.763  51.361  27.224  1.00 28.71
ATOM   3087  O   LEU A 403      12.159  52.231  27.851  1.00 28.06
ATOM   3088  CB  LEU A 403      12.354  49.047  28.102  1.00 28.43
ATOM   3089  CG  LEU A 403      12.315  47.783  27.252  1.00 30.99
ATOM   3090  CD1 LEU A 403      13.702  47.214  27.041  1.00 29.74
ATOM   3091  CD2 LEU A 403      11.429  46.777  27.972  1.00 29.43
ATOM   3092  N   ASP A 404      12.928  51.410  25.909  1.00 30.84
ATOM   3093  CA  ASP A 404      12.350  52.483  25.107  1.00 32.74
ATOM   3094  C   ASP A 404      10.826  52.354  25.189  1.00 33.57
ATOM   3095  O   ASP A 404      10.307  51.252  25.374  1.00 32.93
ATOM   3096  CB  ASP A 404      12.817  52.356  23.652  1.00 33.41
ATOM   3097  CG  ASP A 404      12.331  53.492  22.779  1.00 33.52
ATOM   3098  OD1 ASP A 404      11.103  53.570  22.535  1.00 34.55
ATOM   3099  OD2 ASP A 404      13.178  54.308  22.346  1.00 34.93
ATOM   3100  N   ASP A 405      10.111  53.469  25.065  1.00 34.76
ATOM   3101  CA  ASP A 405       8.647  53.443  25.135  1.00 37.65
ATOM   3102  C   ASP A 405       8.029  52.571  24.045  1.00 37.65
ATOM   3103  O   ASP A 405       6.982  51.952  24.249  1.00 38.10
ATOM   3104  CB  ASP A 405       8.078  54.862  25.036  1.00 39.07
ATOM   3105  CG  ASP A 405       8.432  55.719  26.239  1.00 40.80
ATOM   3106  OD1 ASP A 405       8.222  55.260  27.383  1.00 40.47
ATOM   3107  OD2 ASP A 405       8.912  56.855  26.039  1.00 43.71
ATOM   3108  N   ARG A 406       8.688  52.508  22.896  1.00 38.33
ATOM   3109  CA  ARG A 406       8.194  51.708  21.785  1.00 39.24
ATOM   3110  C   ARG A 406       8.142  50.209  22.094  1.00 39.99
ATOM   3111  O   ARG A 406       7.395  49.463  21.452  1.00 40.52
ATOM   3112  CB  ARG A 406       9.068  51.939  20.553  1.00 40.01
ATOM   3113  CG  ARG A 406       9.271  53.403  20.223  1.00 39.54
ATOM   3114  CD  ARG A 406      10.003  53.574  18.909  1.00 40.23
ATOM   3115  NE  ARG A 406      11.315  54.188  19.075  1.00 38.66
ATOM   3116  CZ  ARG A 406      12.053  54.638  18.066  1.00 38.80
ATOM   3117  NH1 ARG A 406      11.609  54.546  16.818  1.00 38.12
ATOM   3118  NH2 ARG A 406      13.240  55.178  18.300  1.00 40.72
ATOM   3119  N   CYS A 407       8.917  49.768  23.081  1.00 38.36
ATOM   3120  CA  CYS A 407       8.955  48.352  23.433  1.00 36.93
ATOM   3121  C   CYS A 407       7.749  47.826  24.209  1.00 36.42
ATOM   3122  O   CYS A 407       7.498  46.611  24.233  1.00 34.87
ATOM   3123  CB  CYS A 407      10.235  48.050  24.223  1.00 37.83
ATOM   3124  SG  CYS A 407      11.768  48.337  23.302  1.00 35.93
ATOM   3125  N   HIS A 408       7.010  48.734  24.845  1.00 36.81
ATOM   3126  CA  HIS A 408       5.839  48.366  25.646  1.00 36.85
ATOM   3127  C   HIS A 408       6.159  47.403  26.780  1.00 35.28
ATOM   3128  O   HIS A 408       5.424  46.445  27.007  1.00 33.10
ATOM   3129  CB  HIS A 408       4.758  47.756  24.757  1.00 40.26
ATOM   3130  CG  HIS A 408       3.953  48.773  24.016  1.00 43.62
ATOM   3131  ND1 HIS A 408       4.527  49.856  23.387  1.00 43.75
ATOM   3132  CD2 HIS A 408       2.619  48.876  23.807  1.00 44.21
ATOM   3133  CE1 HIS A 408       3.580  50.584  22.821  1.00 45.13
ATOM   3134  NE2 HIS A 408       2.414  50.011  23.060  1.00 44.90
ATOM   3135  N   GLY A 409       7.254  47.666  27.493  1.00 35.22
ATOM   3136  CA  GLY A 409       7.652  46.805  28.600  1.00 34.78
ATOM   3137  C   GLY A 409       8.151  45.447  28.132  1.00 35.13
ATOM   3138  O   GLY A 409       8.352  44.528  28.934  1.00 34.39
ATOM   3139  N   HIS A 410       8.353  45.322  26.823  1.00 35.10
ATOM   3140  CA  HIS A 410       8.820  44.075  26.230  1.00 35.68
ATOM   3141  C   HIS A 410      10.246  44.184  25.716  1.00 33.80
ATOM   3142  O   HIS A 410      10.493  44.750  24.650  1.00 34.67
ATOM   3143  CB  HIS A 410       7.887  43.666  25.088  1.00 38.26
ATOM   3144  CG  HIS A 410       6.549  43.188  25.553  1.00 40.93
ATOM   3145  ND1 HIS A 410       5.398  43.361  24.816  1.00 41.70
ATOM   3146  CD2 HIS A 410       6.180  42.542  26.685  1.00 42.02
ATOM   3147  CE1 HIS A 410       4.377  42.843  25.475  1.00 42.73
ATOM   3148  NE2 HIS A 410       4.824  42.341  26.612  1.00 42.32
ATOM   3149  N   PRO A 411      11.210  43.651  26.474  1.00 32.80
ATOM   3150  CA  PRO A 411      12.598  43.728  26.018  1.00 32.57
ATOM   3151  C   PRO A 411      12.829  42.738  24.873  1.00 32.00
ATOM   3152  O   PRO A 411      12.172  41.702  24.795  1.00 30.89
ATOM   3153  CB  PRO A 411      13.385  43.379  27.274  1.00 32.73
ATOM   3154  CG  PRO A 411      12.470  42.393  27.970  1.00 32.66
ATOM   3155  CD  PRO A 411      11.118  43.029  27.810  1.00 32.08
ATOM   3156  N   PRO A 412      13.746  43.066  23.950  1.00 31.50
ATOM   3157  CA  PRO A 412      14.049  42.189  22.816  1.00 30.89
ATOM   3158  C   PRO A 412      14.466  40.802  23.282  1.00 30.29
ATOM   3159  O   PRO A 412      15.255  40.669  24.209  1.00 32.22
ATOM   3160  CB  PRO A 412      15.183  42.927  22.121  1.00 31.10
ATOM   3161  CG  PRO A 412      14.825  44.359  22.366  1.00 31.00
ATOM   3162  CD  PRO A 412      14.439  44.360  23.814  1.00 30.48
ATOM   3163  N   VAL A 413      13.934  39.760  22.661  1.00 30.43
ATOM   3164  CA  VAL A 413      14.321  38.416  23.065  1.00 29.95
ATOM   3165  C   VAL A 413      15.586  38.042  22.303  1.00 31.84
ATOM   3166  O   VAL A 413      15.541  37.653  21.136  1.00 32.16
ATOM   3167  CB  VAL A 413      13.200  37.399  22.796  1.00 30.32
ATOM   3168  CG1 VAL A 413      13.685  35.988  23.134  1.00 29.96
ATOM   3169  CG2 VAL A 413      11.966  37.756  23.647  1.00 26.75
ATOM   3170  N   VAL A 414      16.721  38.185  22.978  1.00 32.59
ATOM   3171  CA  VAL A 414      18.017  37.901  22.380  1.00 32.75
ATOM   3172  C   VAL A 414      18.511  36.498  22.668  1.00 33.58
ATOM   3173  O   VAL A 414      18.409  36.016  23.799  1.00 35.78
ATOM   3174  CB  VAL A 414      19.064  38.887  22.889  1.00 31.88
ATOM   3175  CG1 VAL A 414      20.386  38.630  22.201  1.00 30.81
ATOM   3176  CG2 VAL A 414      18.579  40.325  22.656  1.00 30.86
ATOM   3177  N   ASP A 415      19.048  35.842  21.643  1.00 32.61
ATOM   3178  CA  ASP A 415      19.571  34.488  21.804  1.00 32.58
ATOM   3179  C   ASP A 415      20.852  34.338  20.999  1.00 30.62
ATOM   3180  O   ASP A 415      20.832  34.281  19.770  1.00 29.45
ATOM   3181  CB  ASP A 415      18.527  33.442  21.382  1.00 34.53
ATOM   3182  CG  ASP A 415      19.091  32.020  21.341  1.00 38.10
ATOM   3183  OD1 ASP A 415      20.048  31.708  22.091  1.00 40.49
ATOM   3184  OD2 ASP A 415      18.564  31.197  20.562  1.00 39.97
ATOM   3185  N   LEU A 416      21.970  34.282  21.714  1.00 29.60
ATOM   3186  CA  LEU A 416      23.272  34.175  21.081  1.00 29.44
ATOM   3187  C   LEU A 416      23.866  32.795  21.252  1.00 29.14
ATOM   3188  O   LEU A 416      23.772  32.193  22.321  1.00 29.74
ATOM   3189  CB  LEU A 416      24.217  35.222  21.671  1.00 28.95
ATOM   3190  CG  LEU A 416      23.605  36.621  21.786  1.00 28.99
ATOM   3191  CD1 LEU A 416      24.637  37.584  22.349  1.00 27.01
ATOM   3192  CD2 LEU A 416      23.096  37.095  20.422  1.00 26.06
ATOM   3193  N   ASP A 417      24.477  32.301  20.182  1.00 29.50
ATOM   3194  CA  ASP A 417      25.111  30.986  20.184  1.00 28.55
ATOM   3195  C   ASP A 417      26.063  30.887  21.384  1.00 28.36
ATOM   3196  O   ASP A 417      27.043  31.622  21.475  1.00 27.17
ATOM   3197  CB  ASP A 417      25.883  30.799  18.874  1.00 29.52
ATOM   3198  CG  ASP A 417      26.380  29.381  18.681  1.00 29.36
ATOM   3199  OD1 ASP A 417      27.092  28.868  19.570  1.00 29.98
ATOM   3200  OD2 ASP A 417      26.061  28.785  17.630  1.00 30.34
ATOM   3201  N   SER A 418      25.775  29.980  22.309  1.00 29.22
ATOM   3202  CA  SER A 418      26.623  29.833  23.484  1.00 30.57
ATOM   3203  C   SER A 418      28.085  29.502  23.149  1.00 30.93
ATOM   3204  O   SER A 418      28.981  29.766  23.954  1.00 30.87
ATOM   3205  CB  SER A 418      26.048  28.753  24.409  1.00 32.78
ATOM   3206  OG  SER A 418      26.111  27.469  23.811  1.00 37.14
ATOM   3207  N   ALA A 419      28.331  28.933  21.971  1.00 29.20
ATOM   3208  CA  ALA A 419      29.691  28.562  21.591  1.00 29.64
ATOM   3209  C   ALA A 419      30.567  29.745  21.199  1.00 28.36
ATOM   3210  O   ALA A 419      31.792  29.661  21.270  1.00 28.67
ATOM   3211  CB  ALA A 419      29.668  27.528  20.442  1.00 29.23
ATOM   3212  N   HIS A 420      29.958  30.852  20.800  1.00 27.72
ATOM   3213  CA  HIS A 420      30.751  32.010  20.389  1.00 26.80
ATOM   3214  C   HIS A 420      30.517  33.275  21.195  1.00 27.54
ATOM   3215  O   HIS A 420      31.369  34.160  21.214  1.00 27.38
ATOM   3216  CB  HIS A 420      30.488  32.338  18.914  1.00 28.13
ATOM   3217  CG  HIS A 420      30.835  31.228  17.976  1.00 29.88
ATOM   3218  ND1 HIS A 420      29.994  30.161  17.744  1.00 32.06
ATOM   3219  CD2 HIS A 420      31.957  30.987  17.259  1.00 30.07
ATOM   3220  CE1 HIS A 420      30.585  29.308  16.926  1.00 31.98
ATOM   3221  NE2 HIS A 420      31.779  29.785  16.618  1.00 31.11
ATOM   3222  N   TYR A 421      29.379  33.374  21.869  1.00 27.02
ATOM   3223  CA  TYR A 421      29.102  34.592  22.600  1.00 30.24
ATOM   3224  C   TYR A 421      28.865  34.517  24.107  1.00 30.06
ATOM   3225  O   TYR A 421      28.718  35.557  24.756  1.00 29.50
ATOM   3226  CB  TYR A 421      27.929  35.298  21.924  1.00 32.08
ATOM   3227  CG  TYR A 421      28.032  35.238  20.418  1.00 32.99
ATOM   3228  CD1 TYR A 421      27.387  34.229  19.695  1.00 33.01
ATOM   3229  CD2 TYR A 421      28.832  36.144  19.720  1.00 32.51
ATOM   3230  CE1 TYR A 421      27.544  34.124  18.315  1.00 32.66
ATOM   3231  CE2 TYR A 421      28.998  36.047  18.340  1.00 31.72
ATOM   3232  CZ  TYR A 421      28.353  35.035  17.648  1.00 31.86
ATOM   3233  OH  TYR A 421      28.531  34.912  16.294  1.00 32.68
ATOM   3234  N   LYS A 422      28.839  33.315  24.675  1.00 30.45
ATOM   3235  CA  LYS A 422      28.606  33.195  26.107  1.00 30.95
ATOM   3236  C   LYS A 422      29.665  33.952  26.908  1.00 31.79
ATOM   3237  O   LYS A 422      29.350  34.572  27.921  1.00 32.71
ATOM   3238  CB  LYS A 422      28.582  31.728  26.525  1.00 30.72
ATOM   3239  CG  LYS A 422      27.972  31.494  27.903  1.00 31.44
ATOM   3240  CD  LYS A 422      28.084  30.027  28.301  1.00 34.36
ATOM   3241  CE  LYS A 422      27.402  29.746  29.634  1.00 35.80
ATOM   3242  NZ  LYS A 422      27.971  30.533  30.758  1.00 37.56
ATOM   3243  N   MET A 423      30.911  33.907  26.442  1.00 32.52
ATOM   3244  CA  MET A 423      32.035  34.586  27.094  1.00 34.20
ATOM   3245  C   MET A 423      32.144  36.033  26.617  1.00 32.95
ATOM   3246  O   MET A 423      31.888  36.329  25.453  1.00 33.25
ATOM   3247  CB  MET A 423      33.345  33.852  26.779  1.00 38.39
ATOM   3248  CG  MET A 423      33.361  32.374  27.178  1.00 43.07
ATOM   3249  SD  MET A 423      33.539  32.008  29.096  1.00 51.18
ATOM   3250  CE  MET A 423      31.689  32.129  29.640  1.00 47.66
ATOM   3251  N   MET A 424      32.546  36.936  27.504  1.00 32.51
ATOM   3252  CA  MET A 424      32.660  38.341  27.136  1.00 33.79
ATOM   3253  C   MET A 424      33.588  38.589  25.953  1.00 33.42
ATOM   3254  O   MET A 424      33.349  39.511  25.161  1.00 31.75
ATOM   3255  CB  MET A 424      33.143  39.173  28.324  1.00 36.71
ATOM   3256  CG  MET A 424      33.001  40.686  28.117  1.00 38.39
ATOM   3257  SD  MET A 424      31.127  41.232  28.091  1.00 41.82
ATOM   3258  CE  MET A 424      30.514  39.960  29.390  1.00 41.40
ATOM   3259  N   ASN A 425      34.650  37.789  25.843  1.00 33.32
ATOM   3260  CA  ASN A 425      35.605  37.930  24.740  1.00 34.12
ATOM   3261  C   ASN A 425      34.919  37.599  23.416  1.00 32.88
ATOM   3262  O   ASN A 425      35.186  38.229  22.391  1.00 33.39
ATOM   3263  CB  ASN A 425      36.821  37.009  24.932  1.00 37.69
ATOM   3264  CG  ASN A 425      37.700  37.423  26.112  1.00 41.73
ATOM   3265  OD1 ASN A 425      37.654  38.571  26.578  1.00 44.48
ATOM   3266  ND2 ASN A 425      38.524  36.489  26.587  1.00 42.10
ATOM   3267  N   GLY A 426      34.037  36.606  23.437  1.00 29.86
ATOM   3268  CA  GLY A 426      33.321  36.254  22.226  1.00 29.08
ATOM   3269  C   GLY A 426      32.307  37.338  21.902  1.00 29.56
ATOM   3270  O   GLY A 426      32.298  37.882  20.807  1.00 30.33
ATOM   3271  N   PHE A 427      31.446  37.666  22.859  1.00 29.35
ATOM   3272  CA  PHE A 427      30.454  38.714  22.644  1.00 28.24
ATOM   3273  C   PHE A 427      31.087  40.035  22.201  1.00 28.55
ATOM   3274  O   PHE A 427      30.543  40.740  21.351  1.00 27.54
ATOM   3275  CB  PHE A 427      29.653  38.965  23.924  1.00 27.17
ATOM   3276  CG  PHE A 427      28.861  40.245  23.898  1.00 26.46
ATOM   3277  CD1 PHE A 427      27.740  40.370  23.086  1.00 27.83
ATOM   3278  CD2 PHE A 427      29.263  41.342  24.651  1.00 27.20
ATOM   3279  CE1 PHE A 427      27.029  41.575  23.023  1.00 27.54
ATOM   3280  CE2 PHE A 427      28.560  42.551  24.595  1.00 27.70
ATOM   3281  CZ  PHE A 427      27.442  42.664  23.778  1.00 27.62
ATOM   3282  N   GLU A 428      32.231  40.380  22.775  1.00 29.40
ATOM   3283  CA  GLU A 428      32.872  41.641  22.418  1.00 31.16
ATOM   3284  C   GLU A 428      33.269  41.737  20.944  1.00 31.28
ATOM   3285  O   GLU A 428      33.299  42.830  20.385  1.00 31.38
ATOM   3286  CB  GLU A 428      34.099  41.887  23.293  1.00 33.10
ATOM   3287  CG  GLU A 428      34.654  43.294  23.151  1.00 36.39
ATOM   3288  CD  GLU A 428      34.420  44.146  24.394  1.00 38.87
ATOM   3289  OE1 GLU A 428      33.261  44.215  24.874  1.00 38.19
ATOM   3290  OE2 GLU A 428      35.401  44.755  24.885  1.00 38.30
ATOM   3291  N   LYS A 429      33.581  40.608  20.312  1.00 30.99
ATOM   3292  CA  LYS A 429      33.943  40.640  18.898  1.00 32.33
ATOM   3293  C   LYS A 429      32.678  40.685  18.013  1.00 31.12
ATOM   3294  O   LYS A 429      32.731  41.045  16.838  1.00 29.39
ATOM   3295  CB  LYS A 429      34.823  39.429  18.538  1.00 36.16
ATOM   3296  CG  LYS A 429      34.140  38.348  17.709  1.00 39.90
ATOM   3297  CD  LYS A 429      33.403  37.349  18.574  1.00 41.80
ATOM   3298  CE  LYS A 429      32.425  36.525  17.757  1.00 44.45
ATOM   3299  NZ  LYS A 429      31.796  35.460  18.585  1.00 46.71
ATOM   3300  N   LEU A 430      31.539  40.319  18.592  1.00 30.24
ATOM   3301  CA  LEU A 430      30.276  40.348  17.866  1.00 29.30
ATOM   3302  C   LEU A 430      29.828  41.782  17.611  1.00 28.48
ATOM   3303  O   LEU A 430      29.233  42.071  16.571  1.00 29.48
ATOM   3304  CB  LEU A 430      29.186  39.613  18.650  1.00 28.11
ATOM   3305  CG  LEU A 430      27.738  39.799  18.172  1.00 25.99
ATOM   3306  CD1 LEU A 430      27.558  39.311  16.726  1.00 24.91
ATOM   3307  CD2 LEU A 430      26.822  39.023  19.121  1.00 24.69
ATOM   3308  N   VAL A 431      30.108  42.678  18.555  1.00 27.79
ATOM   3309  CA  VAL A 431      29.723  44.086  18.404  1.00 27.12
ATOM   3310  C   VAL A 431      30.919  44.984  18.155  1.00 27.78
ATOM   3311  O   VAL A 431      30.827  46.211  18.240  1.00 27.23
ATOM   3312  CB  VAL A 431      28.969  44.615  19.643  1.00 26.83
ATOM   3313  CG1 VAL A 431      27.604  43.961  19.727  1.00 24.35
ATOM   3314  CG2 VAL A 431      29.794  44.364  20.910  1.00 25.57
ATOM   3315  N   GLN A 432      32.037  44.353  17.828  1.00 30.92
ATOM   3316  CA  GLN A 432      33.287  45.040  17.544  1.00 35.05
ATOM   3317  C   GLN A 432      33.110  46.239  16.604  1.00 35.31
ATOM   3318  O   GLN A 432      33.745  47.279  16.783  1.00 34.06
ATOM   3319  CB  GLN A 432      34.273  44.048  16.914  1.00 37.89
ATOM   3320  CG  GLN A 432      35.712  44.532  16.835  1.00 43.44
ATOM   3321  CD  GLN A 432      36.607  43.575  16.055  1.00 48.08
ATOM   3322  OE1 GLN A 432      36.558  42.353  16.246  1.00 49.43
ATOM   3323  NE2 GLN A 432      37.436  44.129  15.173  1.00 49.92
ATOM   3324  N   HIS A 433      32.245  46.087  15.607  1.00 36.40
ATOM   3325  CA  HIS A 433      32.025  47.134  14.620  1.00 39.18
ATOM   3326  C   HIS A 433      30.795  48.000  14.849  1.00 39.53
ATOM   3327  O   HIS A 433      30.477  48.866  14.026  1.00 39.43
ATOM   3328  CB  HIS A 433      31.966  46.498  13.234  1.00 42.13
ATOM   3329  CG  HIS A 433      33.234  45.810  12.846  1.00 46.58
ATOM   3330  ND1 HIS A 433      33.263  44.701  12.026  1.00 48.74
ATOM   3331  CD2 HIS A 433      34.521  46.057  13.193  1.00 48.09
ATOM   3332  CE1 HIS A 433      34.514  44.292  11.890  1.00 49.99
ATOM   3333  NE2 HIS A 433      35.296  45.097  12.588  1.00 49.12
ATOM   3334  N   GLY A 434      30.104  47.765  15.960  1.00 38.96
ATOM   3335  CA  GLY A 434      28.926  48.550  16.265  1.00 37.26
ATOM   3336  C   GLY A 434      27.824  47.712  16.862  1.00 36.71
ATOM   3337  O   GLY A 434      27.767  46.502  16.632  1.00 36.74
ATOM   3338  N   VAL A 435      26.960  48.355  17.646  1.00 36.05
ATOM   3339  CA  VAL A 435      25.829  47.676  18.278  1.00 34.86
ATOM   3340  C   VAL A 435      24.580  47.931  17.432  1.00 34.64
ATOM   3341  O   VAL A 435      24.173  49.076  17.233  1.00 33.69
ATOM   3342  CB  VAL A 435      25.565  48.194  19.718  1.00 34.19
ATOM   3343  CG1 VAL A 435      24.333  47.507  20.292  1.00 32.58
ATOM   3344  CG2 VAL A 435      26.778  47.928  20.610  1.00 33.02
ATOM   3345  N   PRO A 436      23.955  46.856  16.930  1.00 34.04
ATOM   3346  CA  PRO A 436      22.753  46.941  16.100  1.00 33.53
ATOM   3347  C   PRO A 436      21.541  47.516  16.818  1.00 33.55
ATOM   3348  O   PRO A 436      21.286  47.185  17.982  1.00 32.67
ATOM   3349  CB  PRO A 436      22.531  45.492  15.683  1.00 34.66
ATOM   3350  CG  PRO A 436      23.007  44.739  16.897  1.00 34.67
ATOM   3351  CD  PRO A 436      24.300  45.448  17.202  1.00 33.47
ATOM   3352  N   SER A 437      20.806  48.386  16.123  1.00 32.80
ATOM   3353  CA  SER A 437      19.590  48.976  16.676  1.00 31.56
ATOM   3354  C   SER A 437      18.638  47.805  16.909  1.00 31.23
ATOM   3355  O   SER A 437      18.418  46.996  16.011  1.00 31.35
ATOM   3356  CB  SER A 437      18.972  49.959  15.684  1.00 32.93
ATOM   3357  OG  SER A 437      17.654  50.304  16.071  1.00 31.69
ATOM   3358  N   LEU A 438      18.085  47.706  18.114  1.00 30.32
ATOM   3359  CA  LEU A 438      17.186  46.606  18.451  1.00 28.89
ATOM   3360  C   LEU A 438      15.848  47.103  18.944  1.00 29.73
ATOM   3361  O   LEU A 438      14.935  46.309  19.174  1.00 30.96
ATOM   3362  CB  LEU A 438      17.814  45.731  19.544  1.00 26.52
ATOM   3363  CG  LEU A 438      18.477  44.384  19.228  1.00 26.38
ATOM   3364  CD1 LEU A 438      19.258  44.423  17.925  1.00 25.18
ATOM   3365  CD2 LEU A 438      19.377  44.005  20.402  1.00 25.96
ATOM   3366  N   VAL A 439      15.737  48.412  19.122  1.00 29.47
ATOM   3367  CA  VAL A 439      14.501  48.995  19.622  1.00 31.46
ATOM   3368  C   VAL A 439      13.245  48.424  18.937  1.00 33.63
ATOM   3369  O   VAL A 439      12.271  48.059  19.621  1.00 31.75
ATOM   3370  CB  VAL A 439      14.531  50.543  19.482  1.00 29.97
ATOM   3371  CG1 VAL A 439      14.614  50.933  18.007  1.00 28.38
ATOM   3372  CG2 VAL A 439      13.299  51.161  20.161  1.00 28.75
ATOM   3373  N   GLU A 440      13.278  48.324  17.604  1.00 34.91
ATOM   3374  CA  GLU A 440      12.141  47.811  16.836  1.00 36.19
ATOM   3375  C   GLU A 440      12.267  46.320  16.580  1.00 36.84
ATOM   3376  O   GLU A 440      11.557  45.755  15.736  1.00 36.88
ATOM   3377  CB  GLU A 440      12.023  48.552  15.499  1.00 38.09
ATOM   3378  CG  GLU A 440      11.845  50.061  15.628  1.00 39.78
ATOM   3379  CD  GLU A 440      10.435  50.468  16.024  1.00 42.55
ATOM   3380  OE1 GLU A 440       9.686  49.617  16.555  1.00 43.14
ATOM   3381  OE2 GLU A 440      10.081  51.652  15.816  1.00 42.81
ATOM   3382  N   CYS A 441      13.169  45.678  17.313  1.00 36.02
ATOM   3383  CA  CYS A 441      13.384  44.245  17.157  1.00 35.38
ATOM   3384  C   CYS A 441      12.758  43.477  18.315  1.00 35.86
ATOM   3385  O   CYS A 441      13.041  43.757  19.475  1.00 36.73
ATOM   3386  CB  CYS A 441      14.878  43.941  17.085  1.00 33.47
ATOM   3387  SG  CYS A 441      15.219  42.189  16.962  1.00 35.71
ATOM   3388  N   LYS A 442      11.910  42.507  17.989  1.00 35.60
ATOM   3389  CA  LYS A 442      11.233  41.701  18.992  1.00 36.63
ATOM   3390  C   LYS A 442      11.997  40.435  19.348  1.00 36.53
ATOM   3391  O   LYS A 442      11.873  39.905  20.457  1.00 35.64
ATOM   3392  CB  LYS A 442       9.832  41.295  18.525  1.00 38.95
ATOM   3393  CG  LYS A 442       9.373  39.985  19.169  1.00 42.36
ATOM   3394  CD  LYS A 442       7.941  39.591  18.854  1.00 46.04
ATOM   3395  CE  LYS A 442       7.670  38.183  19.383  1.00 47.53
ATOM   3396  NZ  LYS A 442       6.228  37.931  19.654  1.00 52.10
ATOM   3397  N   ARG A 443      12.773  39.934  18.402  1.00 36.00
ATOM   3398  CA  ARG A 443      13.538  38.726  18.646  1.00 36.76
ATOM   3399  C   ARG A 443      14.683  38.632  17.660  1.00 36.05
ATOM   3400  O   ARG A 443      14.499  38.760  16.454  1.00 35.91
ATOM   3401  CB  ARG A 443      12.632  37.496  18.527  1.00 37.64
ATOM   3402  CG  ARG A 443      13.255  36.211  19.030  1.00 38.61
ATOM   3403  CD  ARG A 443      12.344  35.040  18.732  1.00 41.37
ATOM   3404  NE  ARG A 443      11.069  35.197  19.420  1.00 43.73
ATOM   3405  CZ  ARG A 443      10.792  34.667  20.606  1.00 44.33
ATOM   3406  NH1 ARG A 443      11.700  33.930  21.238  1.00 43.89
ATOM   3407  NH2 ARG A 443       9.615  34.898  21.169  1.00 44.01
ATOM   3408  N   VAL A 444      15.870  38.419  18.202  1.00 35.38
ATOM   3409  CA  VAL A 444      17.070  38.292  17.404  1.00 35.07
ATOM   3410  C   VAL A 444      17.865  37.095  17.897  1.00 35.08
ATOM   3411  O   VAL A 444      18.187  36.976  19.085  1.00 35.84
ATOM   3412  CB  VAL A 444      17.951  39.563  17.475  1.00 34.86
ATOM   3413  CG1 VAL A 444      18.120  40.014  18.918  1.00 35.74
ATOM   3414  CG2 VAL A 444      19.311  39.279  16.845  1.00 35.12
ATOM   3415  N   THR A 445      18.164  36.196  16.973  1.00 34.30
ATOM   3416  CA  THR A 445      18.923  35.009  17.296  1.00 34.09
ATOM   3417  C   THR A 445      20.168  35.047  16.423  1.00 34.53
ATOM   3418  O   THR A 445      20.140  35.570  15.312  1.00 34.86
ATOM   3419  CB  THR A 445      18.098  33.734  16.998  1.00 34.82
ATOM   3420  OG1 THR A 445      16.876  33.774  17.746  1.00 33.80
ATOM   3421  CG2 THR A 445      18.877  32.474  17.386  1.00 34.91
ATOM   3422  N   VAL A 446      21.273  34.536  16.943  1.00 34.62
ATOM   3423  CA  VAL A 446      22.512  34.499  16.177  1.00 33.04
ATOM   3424  C   VAL A 446      23.074  33.101  16.341  1.00 32.61
ATOM   3425  O   VAL A 446      23.323  32.640  17.458  1.00 33.28
ATOM   3426  CB  VAL A 446      23.531  35.542  16.674  1.00 32.43
ATOM   3427  CG1 VAL A 446      24.780  35.518  15.802  1.00 31.59
ATOM   3428  CG2 VAL A 446      22.901  36.922  16.649  1.00 32.75
ATOM   3429  N   LYS A 447      23.223  32.415  15.219  1.00 31.57
ATOM   3430  CA  LYS A 447      23.741  31.063  15.208  1.00 32.60
ATOM   3431  C   LYS A 447      25.075  31.088  14.481  1.00 32.22
ATOM   3432  O   LYS A 447      25.228  31.791  13.482  1.00 31.81
ATOM   3433  CB  LYS A 447      22.760  30.145  14.488  1.00 35.18
ATOM   3434  CG  LYS A 447      21.348  30.205  15.055  1.00 38.38
ATOM   3435  CD  LYS A 447      20.431  29.191  14.379  1.00 41.17
ATOM   3436  CE  LYS A 447      19.118  29.034  15.142  1.00 43.04
ATOM   3437  NZ  LYS A 447      18.270  27.919  14.609  1.00 44.47
ATOM   3438  N   GLY A 448      26.042  30.335  14.993  1.00 31.62
ATOM   3439  CA  GLY A 448      27.354  30.305  14.371  1.00 31.91
ATOM   3440  C   GLY A 448      28.085  31.622  14.558  1.00 31.78
ATOM   3441  O   GLY A 448      27.548  32.565  15.142  1.00 28.88
ATOM   3442  N   LEU A 449      29.314  31.684  14.051  1.00 32.80
ATOM   3443  CA  LEU A 449      30.140  32.875  14.170  1.00 31.67
ATOM   3444  C   LEU A 449      29.643  33.977  13.259  1.00 32.88
ATOM   3445  O   LEU A 449      29.481  33.784  12.058  1.00 33.77
ATOM   3446  CB  LEU A 449      31.596  32.546  13.840  1.00 31.15
ATOM   3447  CG  LEU A 449      32.569  33.724  13.977  1.00 30.24
ATOM   3448  CD1 LEU A 449      32.581  34.216  15.408  1.00 28.90
ATOM   3449  CD2 LEU A 449      33.962  33.292  13.564  1.00 30.48
ATOM   3450  N   VAL A 450      29.414  35.146  13.841  1.00 33.73
ATOM   3451  CA  VAL A 450      28.916  36.291  13.097  1.00 33.16
ATOM   3452  C   VAL A 450      29.500  37.572  13.664  1.00 33.41
ATOM   3453  O   VAL A 450      29.980  37.604  14.793  1.00 34.19
ATOM   3454  CB  VAL A 450      27.377  36.369  13.189  1.00 33.16
ATOM   3455  CG1 VAL A 450      26.873  37.684  12.596  1.00 31.26
ATOM   3456  CG2 VAL A 450      26.759  35.179  12.480  1.00 33.10
ATOM   3457  N   GLN A 451      29.438  38.633  12.877  1.00 33.71
ATOM   3458  CA  GLN A 451      29.960  39.912  13.304  1.00 35.21
ATOM   3459  C   GLN A 451      29.089  41.039  12.761  1.00 34.72
ATOM   3460  O   GLN A 451      28.930  41.173  11.545  1.00 35.13
ATOM   3461  CB  GLN A 451      31.394  40.065  12.804  1.00 37.39
ATOM   3462  CG  GLN A 451      32.179  41.150  13.506  1.00 41.08
ATOM   3463  CD  GLN A 451      33.660  41.106  13.171  1.00 42.79
ATOM   3464  OE1 GLN A 451      34.482  41.764  13.827  1.00 44.31
ATOM   3465  NE2 GLN A 451      34.010  40.333  12.148  1.00 42.27
ATOM   3466  N   PHE A 452      28.513  41.842  13.655  1.00 33.66
ATOM   3467  CA  PHE A 452      27.682  42.952  13.207  1.00 33.38
ATOM   3468  C   PHE A 452      28.553  43.988  12.516  1.00 33.78
ATOM   3469  O   PHE A 452      29.744  44.124  12.818  1.00 32.24
ATOM   3470  CB  PHE A 452      26.945  43.632  14.370  1.00 32.45
ATOM   3471  CG  PHE A 452      25.817  42.814  14.947  1.00 32.35
ATOM   3472  CD1 PHE A 452      25.937  42.221  16.205  1.00 32.04
ATOM   3473  CD2 PHE A 452      24.645  42.620  14.232  1.00 31.33
ATOM   3474  CE1 PHE A 452      24.908  41.443  16.738  1.00 30.42
ATOM   3475  CE2 PHE A 452      23.603  41.841  14.759  1.00 32.15
ATOM   3476  CZ  PHE A 452      23.739  41.251  16.015  1.00 31.28
ATOM   3477  N   GLY A 453      27.940  44.689  11.566  1.00 34.52
ATOM   3478  CA  GLY A 453      28.621  45.747  10.853  1.00 35.71
ATOM   3479  C   GLY A 453      28.095  47.019  11.483  1.00 36.65
ATOM   3480  O   GLY A 453      27.411  46.954  12.506  1.00 37.88
ATOM   3481  N   ALA A 454      28.395  48.171  10.900  1.00 37.41
ATOM   3482  CA  ALA A 454      27.915  49.427  11.463  1.00 38.07
ATOM   3483  C   ALA A 454      26.480  49.674  11.007  1.00 38.98
ATOM   3484  O   ALA A 454      26.003  49.035  10.064  1.00 39.94
ATOM   3485  CB  ALA A 454      28.818  50.569  11.024  1.00 37.23
ATOM   3486  N   GLY A 455      25.794  50.585  11.694  1.00 39.64
ATOM   3487  CA  GLY A 455      24.419  50.925  11.352  1.00 39.39
ATOM   3488  C   GLY A 455      23.422  49.790  11.157  1.00 39.67
ATOM   3489  O   GLY A 455      22.360  49.996  10.567  1.00 40.66
ATOM   3490  N   ASN A 456      23.746  48.591  11.630  1.00 39.16
ATOM   3491  CA  ASN A 456      22.828  47.458  11.510  1.00 38.71
ATOM   3492  C   ASN A 456      21.512  47.791  12.244  1.00 38.61
ATOM   3493  O   ASN A 456      21.533  48.191  13.412  1.00 38.45
ATOM   3494  CB  ASN A 456      23.466  46.201  12.117  1.00 39.78
ATOM   3495  CG  ASN A 456      24.556  45.604  11.236  1.00 39.40
ATOM   3496  OD1 ASN A 456      25.277  46.321  10.543  1.00 40.02
ATOM   3497  ND2 ASN A 456      24.688  44.282  11.276  1.00 37.32
ATOM   3498  N   VAL A 457      20.380  47.629  11.554  1.00 37.62
ATOM   3499  CA  VAL A 457      19.061  47.918  12.117  1.00 36.27
ATOM   3500  C   VAL A 457      18.137  46.712  11.999  1.00 37.12
ATOM   3501  O   VAL A 457      17.733  46.339  10.896  1.00 38.52
ATOM   3502  CB  VAL A 457      18.382  49.100  11.381  1.00 35.77
ATOM   3503  CG1 VAL A 457      16.980  49.300  11.917  1.00 35.21
ATOM   3504  CG2 VAL A 457      19.207  50.382  11.547  1.00 34.71
ATOM   3505  N   LEU A 458      17.785  46.098  13.123  1.00 36.30
ATOM   3506  CA  LEU A 458      16.901  44.945  13.060  1.00 36.02
ATOM   3507  C   LEU A 458      15.470  45.332  13.423  1.00 37.80
ATOM   3508  O   LEU A 458      15.239  46.245  14.220  1.00 37.10
ATOM   3509  CB  LEU A 458      17.406  43.829  13.981  1.00 35.24
ATOM   3510  CG  LEU A 458      18.905  43.478  13.912  1.00 34.24
ATOM   3511  CD1 LEU A 458      19.098  42.027  14.330  1.00 32.14
ATOM   3512  CD2 LEU A 458      19.450  43.687  12.516  1.00 35.00
ATOM   3513  N   THR A 459      14.513  44.641  12.811  1.00 38.92
ATOM   3514  CA  THR A 459      13.098  44.895  13.041  1.00 39.05
ATOM   3515  C   THR A 459      12.334  43.578  12.985  1.00 39.56
ATOM   3516  O   THR A 459      12.658  42.695  12.186  1.00 39.32
ATOM   3517  CB  THR A 459      12.536  45.859  11.974  1.00 40.09
ATOM   3518  OG1 THR A 459      13.033  47.186  12.212  1.00 40.33
ATOM   3519  CG2 THR A 459      11.016  45.867  12.004  1.00 41.74
ATOM   3520  N   GLY A 460      11.316  43.449  13.830  1.00 39.24
ATOM   3521  CA  GLY A 460      10.536  42.227  13.853  1.00 38.85
ATOM   3522  C   GLY A 460      11.412  41.070  14.284  1.00 39.56
ATOM   3523  O   GLY A 460      12.402  41.274  14.980  1.00 40.97
ATOM   3524  N   THR A 461      11.061  39.857  13.874  1.00 38.93
ATOM   3525  CA  THR A 461      11.836  38.677  14.235  1.00 39.14
ATOM   3526  C   THR A 461      12.978  38.441  13.247  1.00 40.62
ATOM   3527  O   THR A 461      12.744  38.166  12.066  1.00 40.14
ATOM   3528  CB  THR A 461      10.934  37.434  14.285  1.00 38.28
ATOM   3529  OG1 THR A 461       9.940  37.617  15.300  1.00 37.61
ATOM   3530  CG2 THR A 461      11.748  36.181  14.595  1.00 37.79
ATOM   3531  N   VAL A 462      14.212  38.540  13.745  1.00 41.11
ATOM   3532  CA  VAL A 462      15.412  38.358  12.925  1.00 39.97
ATOM   3533  C   VAL A 462      16.380  37.273  13.401  1.00 41.54
ATOM   3534  O   VAL A 462      16.801  37.265  14.554  1.00 43.16
ATOM   3535  CB  VAL A 462      16.211  39.663  12.839  1.00 38.65
ATOM   3536  CG1 VAL A 462      17.506  39.425  12.081  1.00 38.77
ATOM   3537  CG2 VAL A 462      15.381  40.740  12.169  1.00 35.96
ATOM   3538  N   THR A 463      16.732  36.354  12.510  1.00 41.37
ATOM   3539  CA  THR A 463      17.686  35.304  12.842  1.00 41.73
ATOM   3540  C   THR A 463      18.860  35.473  11.908  1.00 43.47
ATOM   3541  O   THR A 463      18.687  35.804  10.740  1.00 44.70
ATOM   3542  CB  THR A 463      17.126  33.883  12.626  1.00 41.13
ATOM   3543  OG1 THR A 463      16.215  33.556  13.679  1.00 42.13
ATOM   3544  CG2 THR A 463      18.248  32.866  12.627  1.00 40.01
ATOM   3545  N   ILE A 464      20.059  35.261  12.427  1.00 45.12
ATOM   3546  CA  ILE A 464      21.260  35.370  11.619  1.00 46.45
ATOM   3547  C   ILE A 464      21.996  34.042  11.729  1.00 48.85
ATOM   3548  O   ILE A 464      22.481  33.673  12.800  1.00 48.47
ATOM   3549  CB  ILE A 464      22.151  36.535  12.097  1.00 43.99
ATOM   3550  CG1 ILE A 464      21.394  37.852  11.926  1.00 43.79
ATOM   3551  CG2 ILE A 464      23.445  36.576  11.301  1.00 43.36
ATOM   3552  CD1 ILE A 464      22.162  39.069  12.359  1.00 42.76
ATOM   3553  N   GLU A 465      22.035  33.305  10.621  1.00 51.81
ATOM   3554  CA  GLU A 465      22.698  32.010  10.599  1.00 54.64
ATOM   3555  C   GLU A 465      24.022  32.003   9.875  1.00 56.31
ATOM   3556  O   GLU A 465      24.179  32.608   8.820  1.00 56.84
ATOM   3557  CB  GLU A 465      21.808  30.942   9.969  1.00 55.74
ATOM   3558  CG  GLU A 465      20.765  30.376  10.908  1.00 58.99
ATOM   3559  CD  GLU A 465      20.352  28.961  10.538  1.00 60.09
ATOM   3560  OE1 GLU A 465      19.914  28.747   9.386  1.00 60.60
ATOM   3561  OE2 GLU A 465      20.469  28.063  11.406  1.00 60.26
ATOM   3562  N   ASN A 466      24.968  31.298  10.475  1.00 59.39
ATOM   3563  CA  ASN A 466      26.305  31.135   9.941  1.00 62.06
ATOM   3564  C   ASN A 466      26.502  29.626   9.978  1.00 63.43
ATOM   3565  O   ASN A 466      27.227  29.095  10.821  1.00 62.96
ATOM   3566  CB  ASN A 466      27.333  31.823  10.845  1.00 63.67
ATOM   3567  CG  ASN A 466      28.747  31.728  10.302  1.00 65.26
ATOM   3568  OD1 ASN A 466      29.112  32.435   9.361  1.00 65.77
ATOM   3569  ND2 ASN A 466      29.546  30.838  10.884  1.00 65.79
ATOM   3570  N   THR A 467      25.815  28.942   9.070  1.00 65.47
ATOM   3571  CA  THR A 467      25.884  27.487   8.971  1.00 67.69
ATOM   3572  C   THR A 467      27.277  27.082   8.513  1.00 68.64
ATOM   3573  O   THR A 467      27.753  25.990   8.824  1.00 67.88
ATOM   3574  CB  THR A 467      24.872  26.968   7.947  1.00 68.72
ATOM   3575  OG1 THR A 467      23.625  27.656   8.119  1.00 69.16
ATOM   3576  CG2 THR A 467      24.652  25.473   8.134  1.00 69.35
ATOM   3577  N   ASP A 468      27.912  27.988   7.769  1.00 70.35
ATOM   3578  CA  ASP A 468      29.257  27.801   7.227  1.00 71.13
ATOM   3579  C   ASP A 468      30.278  27.383   8.281  1.00 70.61
ATOM   3580  O   ASP A 468      30.995  26.401   8.090  1.00 70.67
ATOM   3581  CB  ASP A 468      29.712  29.090   6.534  1.00 73.26
ATOM   3582  CG  ASP A 468      29.394  30.334   7.347  1.00 75.14
ATOM   3583  OD1 ASP A 468      28.723  30.198   8.390  1.00 74.88
ATOM   3584  OD2 ASP A 468      29.807  31.442   6.939  1.00 76.16
ATOM   3585  N   SER A 469      30.350  28.145   9.373  1.00 69.54
ATOM   3586  CA  SER A 469      31.251  27.870  10.497  1.00 68.46
ATOM   3587  C   SER A 469      32.661  28.459  10.436  1.00 67.63
ATOM   3588  O   SER A 469      32.947  29.485  11.055  1.00 67.67
ATOM   3589  CB  SER A 469      31.358  26.355  10.736  1.00 68.87
ATOM   3590  OG  SER A 469      30.120  25.804  11.156  1.00 68.59
ATOM   3591  N   ALA A 470      33.538  27.790   9.697  1.00 65.86
ATOM   3592  CA  ALA A 470      34.936  28.189   9.559  1.00 63.65
ATOM   3593  C   ALA A 470      35.227  29.640   9.156  1.00 62.25
ATOM   3594  O   ALA A 470      36.379  30.076   9.226  1.00 62.13
ATOM   3595  CB  ALA A 470      35.632  27.240   8.585  1.00 63.52
ATOM   3596  N   SER A 471      34.204  30.384   8.739  1.00 59.81
ATOM   3597  CA  SER A 471      34.402  31.774   8.321  1.00 56.89
ATOM   3598  C   SER A 471      33.368  32.712   8.917  1.00 54.71
ATOM   3599  O   SER A 471      32.171  32.489   8.767  1.00 53.99
ATOM   3600  CB  SER A 471      34.348  31.889   6.795  1.00 56.32
ATOM   3601  OG  SER A 471      35.380  31.138   6.181  1.00 57.23
ATOM   3602  N   ALA A 472      33.844  33.772   9.566  1.00 52.18
ATOM   3603  CA  ALA A 472      32.977  34.762  10.196  1.00 50.64
ATOM   3604  C   ALA A 472      32.113  35.513   9.190  1.00 49.72
ATOM   3605  O   ALA A 472      32.618  36.298   8.387  1.00 50.54
ATOM   3606  CB  ALA A 472      33.816  35.751  10.988  1.00 48.74
ATOM   3607  N   PHE A 473      30.808  35.267   9.242  1.00 48.26
ATOM   3608  CA  PHE A 473      29.859  35.931   8.355  1.00 48.40
ATOM   3609  C   PHE A 473      29.697  37.389   8.794  1.00 47.79
ATOM   3610  O   PHE A 473      28.907  37.681   9.690  1.00 48.04
ATOM   3611  CB  PHE A 473      28.507  35.226   8.429  1.00 48.22
ATOM   3612  CG  PHE A 473      27.416  35.926   7.678  1.00 50.89
ATOM   3613  CD1 PHE A 473      26.122  35.951   8.181  1.00 51.38
ATOM   3614  CD2 PHE A 473      27.675  36.555   6.465  1.00 52.08
ATOM   3615  CE1 PHE A 473      25.099  36.595   7.488  1.00 51.52
ATOM   3616  CE2 PHE A 473      26.660  37.202   5.764  1.00 52.56
ATOM   3617  CZ  PHE A 473      25.369  37.222   6.277  1.00 52.22
ATOM   3618  N   VAL A 474      30.442  38.298   8.169  1.00 46.37
ATOM   3619  CA  VAL A 474      30.369  39.710   8.531  1.00 46.04
ATOM   3620  C   VAL A 474      29.230  40.428   7.831  1.00 46.23
ATOM   3621  O   VAL A 474      29.202  40.549   6.609  1.00 46.05
ATOM   3622  CB  VAL A 474      31.677  40.450   8.202  1.00 46.86
ATOM   3623  CG1 VAL A 474      31.560  41.925   8.601  1.00 46.72
ATOM   3624  CG2 VAL A 474      32.838  39.785   8.925  1.00 47.20
ATOM   3625  N   ILE A 475      28.290  40.913   8.625  1.00 46.05
ATOM   3626  CA  ILE A 475      27.145  41.619   8.087  1.00 45.40
ATOM   3627  C   ILE A 475      27.581  42.998   7.615  1.00 44.86
ATOM   3628  O   ILE A 475      28.307  43.698   8.311  1.00 44.43
ATOM   3629  CB  ILE A 475      26.046  41.738   9.153  1.00 44.74
ATOM   3630  CG1 ILE A 475      25.632  40.333   9.595  1.00 44.68
ATOM   3631  CG2 ILE A 475      24.857  42.510   8.599  1.00 44.01
ATOM   3632  CD1 ILE A 475      24.804  40.293  10.842  1.00 44.97
ATOM   3633  N   PRO A 476      27.156  43.389   6.404  1.00 45.33
ATOM   3634  CA  PRO A 476      27.463  44.675   5.766  1.00 45.45
ATOM   3635  C   PRO A 476      27.057  45.869   6.620  1.00 45.62
ATOM   3636  O   PRO A 476      26.205  45.746   7.497  1.00 44.37
ATOM   3637  CB  PRO A 476      26.657  44.616   4.471  1.00 45.05
ATOM   3638  CG  PRO A 476      26.642  43.152   4.153  1.00 45.30
ATOM   3639  CD  PRO A 476      26.364  42.535   5.499  1.00 45.78
ATOM   3640  N   ASP A 477      27.665  47.020   6.356  1.00 46.23
ATOM   3641  CA  ASP A 477      27.331  48.226   7.091  1.00 47.90
ATOM   3642  C   ASP A 477      25.983  48.750   6.624  1.00 48.49
ATOM   3643  O   ASP A 477      25.550  48.448   5.516  1.00 49.38
ATOM   3644  CB  ASP A 477      28.401  49.294   6.882  1.00 48.91
ATOM   3645  CG  ASP A 477      29.702  48.951   7.576  1.00 51.33
ATOM   3646  OD1 ASP A 477      30.618  49.804   7.585  1.00 53.22
ATOM   3647  OD2 ASP A 477      29.809  47.824   8.114  1.00 51.53
ATOM   3648  N   GLY A 478      25.319  49.519   7.482  1.00 48.74
ATOM   3649  CA  GLY A 478      24.027  50.087   7.143  1.00 48.74
ATOM   3650  C   GLY A 478      22.947  49.068   6.849  1.00 49.62
ATOM   3651  O   GLY A 478      21.817  49.425   6.511  1.00 49.53
ATOM   3652  N   ALA A 479      23.293  47.793   6.976  1.00 50.52
ATOM   3653  CA  ALA A 479      22.343  46.715   6.717  1.00 51.20
ATOM   3654  C   ALA A 479      21.018  46.939   7.448  1.00 51.44
ATOM   3655  O   ALA A 479      20.972  47.603   8.486  1.00 52.38
ATOM   3656  CB  ALA A 479      22.949  45.384   7.138  1.00 51.15
ATOM   3657  N   LYS A 480      19.946  46.388   6.891  1.00 50.51
ATOM   3658  CA  LYS A 480      18.622  46.498   7.486  1.00 50.29
ATOM   3659  C   LYS A 480      17.965  45.137   7.374  1.00 50.21
ATOM   3660  O   LYS A 480      17.749  44.625   6.273  1.00 51.06
ATOM   3661  CB  LYS A 480      17.800  47.569   6.772  1.00 49.35
ATOM   3662  CG  LYS A 480      18.419  48.942   6.908  1.00 49.75
ATOM   3663  CD  LYS A 480      17.669  50.005   6.134  1.00 50.03
ATOM   3664  CE  LYS A 480      18.461  51.299   6.162  1.00 49.58
ATOM   3665  NZ  LYS A 480      18.812  51.656   7.565  1.00 49.00
ATOM   3666  N   LEU A 481      17.668  44.541   8.522  1.00 50.19
ATOM   3667  CA  LEU A 481      17.075  43.213   8.562  1.00 49.80
ATOM   3668  C   LEU A 481      15.702  43.177   9.244  1.00 49.72
ATOM   3669  O   LEU A 481      15.590  43.351  10.458  1.00 50.50
ATOM   3670  CB  LEU A 481      18.047  42.259   9.271  1.00 50.22
ATOM   3671  CG  LEU A 481      19.531  42.518   8.995  1.00 50.49
ATOM   3672  CD1 LEU A 481      20.400  41.501   9.730  1.00 49.74
ATOM   3673  CD2 LEU A 481      19.802  42.454   7.501  1.00 51.04
ATOM   3674  N   ASN A 482      14.668  42.944   8.442  1.00 49.08
ATOM   3675  CA  ASN A 482      13.303  42.864   8.915  1.00 48.72
ATOM   3676  C   ASN A 482      12.854  41.418   8.766  1.00 48.47
ATOM   3677  O   ASN A 482      13.262  40.745   7.830  1.00 49.04
ATOM   3678  CB  ASN A 482      12.397  43.750   8.065  1.00 49.58
ATOM   3679  CG  ASN A 482      12.855  45.198   8.015  1.00 50.94
ATOM   3680  OD1 ASN A 482      14.005  45.501   7.692  1.00 51.60
ATOM   3681  ND2 ASN A 482      11.941  46.105   8.333  1.00 52.22
ATOM   3682  N   ASP A 483      12.015  40.957   9.689  1.00 47.94
ATOM   3683  CA  ASP A 483      11.493  39.587   9.692  1.00 48.13
ATOM   3684  C   ASP A 483      12.158  38.633   8.691  1.00 47.14
ATOM   3685  O   ASP A 483      11.496  38.095   7.802  1.00 46.21
ATOM   3686  CB  ASP A 483       9.982  39.603   9.434  1.00 49.42
ATOM   3687  CG  ASP A 483       9.201  40.262  10.554  1.00 50.08
ATOM   3688  OD1 ASP A 483       8.071  40.724  10.303  1.00 52.21
ATOM   3689  OD2 ASP A 483       9.708  40.303  11.692  1.00 50.42
ATOM   3690  N   THR A 484      13.457  38.405   8.854  1.00 46.48
ATOM   3691  CA  THR A 484      14.187  37.535   7.951  1.00 46.50
ATOM   3692  C   THR A 484      15.223  36.661   8.665  1.00 46.35
ATOM   3693  O   THR A 484      15.410  36.763   9.878  1.00 46.47
ATOM   3694  CB  THR A 484      14.879  38.383   6.836  1.00 46.54
ATOM   3695  OG1 THR A 484      15.530  37.515   5.906  1.00 48.03
ATOM   3696  CG2 THR A 484      15.914  39.327   7.435  1.00 46.24
ATOM   3697  N   THR A 485      15.868  35.787   7.897  1.00 45.94
ATOM   3698  CA  THR A 485      16.916  34.894   8.391  1.00 45.54
ATOM   3699  C   THR A 485      18.084  35.159   7.444  1.00 45.66
ATOM   3700  O   THR A 485      18.146  34.602   6.350  1.00 46.33
ATOM   3701  CB  THR A 485      16.482  33.387   8.316  1.00 45.31
ATOM   3702  OG1 THR A 485      15.637  33.067   9.430  1.00 45.03
ATOM   3703  CG2 THR A 485      17.693  32.456   8.333  1.00 44.03
ATOM   3704  N   ALA A 486      18.984  36.046   7.853  1.00 45.95
ATOM   3705  CA  ALA A 486      20.135  36.394   7.029  1.00 45.77
ATOM   3706  C   ALA A 486      21.290  35.435   7.266  1.00 46.01
ATOM   3707  O   ALA A 486      21.611  35.086   8.406  1.00 46.38
ATOM   3708  CB  ALA A 486      20.573  37.820   7.314  1.00 44.18
ATOM   3709  N   SER A 487      21.907  35.003   6.176  1.00 45.19
ATOM   3710  CA  SER A 487      23.031  34.086   6.249  1.00 44.59
ATOM   3711  C   SER A 487      23.884  34.269   4.998  1.00 43.99
ATOM   3712  O   SER A 487      23.491  34.980   4.072  1.00 43.09
ATOM   3713  CB  SER A 487      22.527  32.639   6.373  1.00 44.57
ATOM   3714  OG  SER A 487      21.603  32.309   5.353  1.00 45.23
ATOM   3715  N   PRO A 488      25.076  33.653   4.964  1.00 43.54
ATOM   3716  CA  PRO A 488      25.944  33.790   3.788  1.00 44.26
ATOM   3717  C   PRO A 488      25.438  32.996   2.569  1.00 44.26
ATOM   3718  O   PRO A 488      25.084  33.639   1.556  1.00 45.52
ATOM   3719  CB  PRO A 488      27.294  33.298   4.308  1.00 43.73
ATOM   3720  CG  PRO A 488      26.893  32.232   5.291  1.00 43.33
ATOM   3721  CD  PRO A 488      25.728  32.860   6.023  1.00 43.00
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.