File: 3BZD.pdb

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ATOM      1  N   ALA A   2      33.763  52.112 -44.090  1.00 25.34
ATOM      2  CA  ALA A   2      33.403  52.722 -42.739  1.00 25.11
ATOM      3  C   ALA A   2      31.960  53.249 -42.614  1.00 24.76
ATOM      4  O   ALA A   2      31.694  54.512 -42.582  1.00 23.96
ATOM      5  CB  ALA A   2      34.416  53.856 -42.420  1.00 25.90
ATOM      6  N   ALA A   3      31.006  52.310 -42.598  1.00 22.94
ATOM      7  CA  ALA A   3      29.599  52.628 -42.417  1.00 20.08
ATOM      8  C   ALA A   3      29.149  54.015 -41.825  1.00 19.99
ATOM      9  O   ALA A   3      28.776  54.906 -42.573  1.00 20.00
ATOM     10  CB  ALA A   3      28.955  51.482 -41.644  1.00 23.26
ATOM     11  N   VAL A   4      29.035  54.170 -40.506  1.00 18.40
ATOM     12  CA  VAL A   4      28.549  55.423 -39.964  1.00 18.10
ATOM     13  C   VAL A   4      29.576  56.081 -38.981  1.00 20.17
ATOM     14  O   VAL A   4      30.137  55.401 -38.110  1.00 23.21
ATOM     15  CB  VAL A   4      27.169  55.298 -39.311  1.00 17.65
ATOM     16  CG1 VAL A   4      26.698  56.664 -38.801  1.00 15.66
ATOM     17  CG2 VAL A   4      26.087  54.720 -40.311  1.00 13.28
ATOM     18  N   THR A   5      29.873  57.358 -39.124  1.00 20.40
ATOM     19  CA  THR A   5      30.874  57.978 -38.197  1.00 20.85
ATOM     20  C   THR A   5      30.306  59.193 -37.579  1.00 20.88
ATOM     21  O   THR A   5      29.679  59.984 -38.291  1.00 23.01
ATOM     22  CB  THR A   5      32.105  58.415 -38.935  1.00 19.13
ATOM     23  OG1 THR A   5      31.701  59.319 -39.976  1.00 20.17
ATOM     24  CG2 THR A   5      32.793  57.235 -39.515  1.00 19.09
ATOM     25  N   GLN A   6      30.516  59.359 -36.266  1.00 22.20
ATOM     26  CA  GLN A   6      30.067  60.585 -35.579  1.00 23.92
ATOM     27  C   GLN A   6      31.183  61.576 -35.350  1.00 24.16
ATOM     28  O   GLN A   6      32.319  61.255 -35.567  1.00 24.44
ATOM     29  CB  GLN A   6      29.374  60.216 -34.293  1.00 24.31
ATOM     30  CG  GLN A   6      28.414  59.048 -34.567  1.00 26.83
ATOM     31  CD  GLN A   6      27.650  58.653 -33.341  1.00 33.51
ATOM     32  OE1 GLN A   6      27.159  57.489 -33.222  1.00 29.01
ATOM     33  NE2 GLN A   6      27.551  59.606 -32.387  1.00 30.50
ATOM     34  N   SER A   7      30.858  62.793 -34.915  1.00 24.73
ATOM     35  CA  SER A   7      31.873  63.763 -34.592  1.00 24.61
ATOM     36  C   SER A   7      31.252  64.844 -33.743  1.00 22.89
ATOM     37  O   SER A   7      30.226  65.374 -34.175  1.00 23.88
ATOM     38  CB  SER A   7      32.492  64.358 -35.868  1.00 24.52
ATOM     39  OG  SER A   7      32.873  65.718 -35.598  1.00 29.35
ATOM     40  N   PRO A   8      31.876  65.196 -32.575  1.00 21.61
ATOM     41  CA  PRO A   8      33.116  64.595 -32.127  1.00 23.90
ATOM     42  C   PRO A   8      32.855  63.370 -31.324  1.00 25.23
ATOM     43  O   PRO A   8      31.723  63.054 -31.034  1.00 26.87
ATOM     44  CB  PRO A   8      33.746  65.663 -31.273  1.00 21.34
ATOM     45  CG  PRO A   8      32.608  66.338 -30.689  1.00 20.62
ATOM     46  CD  PRO A   8      31.440  66.196 -31.594  1.00 21.05
ATOM     47  N   ARG A   9      33.912  62.635 -31.030  1.00 30.32
ATOM     48  CA  ARG A   9      33.769  61.344 -30.318  1.00 32.66
ATOM     49  C   ARG A   9      33.547  61.556 -28.814  1.00 34.51
ATOM     50  O   ARG A   9      32.676  60.886 -28.211  1.00 34.65
ATOM     51  CB  ARG A   9      34.960  60.411 -30.594  1.00 33.97
ATOM     52  CG  ARG A   9      34.579  58.965 -31.203  1.00 37.59
ATOM     53  CD  ARG A   9      34.574  57.847 -30.146  1.00 41.10
ATOM     54  NE  ARG A   9      33.525  57.998 -29.122  1.00 41.96
ATOM     55  CZ  ARG A   9      33.148  57.018 -28.288  1.00 46.33
ATOM     56  NH1 ARG A   9      33.734  55.823 -28.351  1.00 46.04
ATOM     57  NH2 ARG A   9      32.191  57.226 -27.381  1.00 45.03
ATOM     58  N   ASN A  10      34.255  62.538 -28.252  1.00 34.63
ATOM     59  CA  ASN A  10      34.322  62.770 -26.841  1.00 36.87
ATOM     60  C   ASN A  10      34.176  64.301 -26.619  1.00 37.49
ATOM     61  O   ASN A  10      34.952  65.100 -27.222  1.00 37.87
ATOM     62  CB  ASN A  10      35.728  62.350 -26.344  1.00 38.51
ATOM     63  CG  ASN A  10      35.808  60.909 -25.778  1.00 40.50
ATOM     64  OD1 ASN A  10      35.289  60.621 -24.690  1.00 42.89
ATOM     65  ND2 ASN A  10      36.562  60.024 -26.478  1.00 45.07
ATOM     66  N   LYS A  11      33.234  64.711 -25.756  1.00 37.13
ATOM     67  CA  LYS A  11      32.988  66.146 -25.513  1.00 37.05
ATOM     68  C   LYS A  11      32.611  66.551 -24.094  1.00 37.79
ATOM     69  O   LYS A  11      31.611  66.081 -23.547  1.00 38.26
ATOM     70  CB  LYS A  11      31.917  66.640 -26.461  1.00 36.57
ATOM     71  CG  LYS A  11      31.671  68.085 -26.434  1.00 34.46
ATOM     72  CD  LYS A  11      32.930  68.874 -26.804  1.00 34.83
ATOM     73  CE  LYS A  11      32.640  70.397 -26.761  1.00 30.64
ATOM     74  NZ  LYS A  11      31.514  70.805 -27.599  1.00 22.67
ATOM     75  N   VAL A  12      33.386  67.505 -23.554  1.00 38.60
ATOM     76  CA  VAL A  12      33.166  68.115 -22.222  1.00 38.63
ATOM     77  C   VAL A  12      32.833  69.600 -22.304  1.00 37.84
ATOM     78  O   VAL A  12      33.705  70.410 -22.575  1.00 37.68
ATOM     79  CB  VAL A  12      34.436  68.044 -21.367  1.00 38.68
ATOM     80  CG1 VAL A  12      34.455  66.783 -20.594  1.00 36.81
ATOM     81  CG2 VAL A  12      35.698  68.267 -22.244  1.00 39.25
ATOM     82  N   ALA A  13      31.582  69.958 -22.048  1.00 38.24
ATOM     83  CA  ALA A  13      31.154  71.334 -22.244  1.00 37.91
ATOM     84  C   ALA A  13      30.518  71.865 -20.969  1.00 38.80
ATOM     85  O   ALA A  13      29.977  71.078 -20.172  1.00 40.28
ATOM     86  CB  ALA A  13      30.206  71.429 -23.445  1.00 36.72
ATOM     87  N   VAL A  14      30.572  73.184 -20.774  1.00 38.57
ATOM     88  CA  VAL A  14      30.029  73.826 -19.562  1.00 37.61
ATOM     89  C   VAL A  14      28.509  74.033 -19.608  1.00 37.37
ATOM     90  O   VAL A  14      27.928  74.222 -20.657  1.00 37.41
ATOM     91  CB  VAL A  14      30.786  75.122 -19.224  1.00 37.15
ATOM     92  CG1 VAL A  14      32.258  74.813 -18.990  1.00 39.31
ATOM     93  CG2 VAL A  14      30.659  76.145 -20.333  1.00 36.96
ATOM     94  N   THR A  15      27.833  73.972 -18.484  1.00 37.50
ATOM     95  CA  THR A  15      26.374  74.084 -18.570  1.00 38.08
ATOM     96  C   THR A  15      26.081  75.446 -19.119  1.00 38.88
ATOM     97  O   THR A  15      26.546  76.448 -18.589  1.00 38.13
ATOM     98  CB  THR A  15      25.740  73.917 -17.219  1.00 38.28
ATOM     99  OG1 THR A  15      26.179  72.659 -16.708  1.00 37.16
ATOM    100  CG2 THR A  15      24.211  73.945 -17.270  1.00 33.98
ATOM    101  N   GLY A  16      25.378  75.454 -20.243  1.00 40.38
ATOM    102  CA  GLY A  16      25.006  76.708 -20.944  1.00 40.95
ATOM    103  C   GLY A  16      25.235  76.682 -22.453  1.00 41.28
ATOM    104  O   GLY A  16      24.284  76.759 -23.237  1.00 41.72
ATOM    105  N   GLU A  17      26.507  76.545 -22.845  1.00 40.82
ATOM    106  CA  GLU A  17      26.917  76.561 -24.222  1.00 39.97
ATOM    107  C   GLU A  17      26.090  75.713 -25.162  1.00 39.45
ATOM    108  O   GLU A  17      25.424  74.709 -24.773  1.00 41.25
ATOM    109  CB  GLU A  17      28.383  76.194 -24.313  1.00 39.94
ATOM    110  CG  GLU A  17      28.705  74.768 -24.699  1.00 42.31
ATOM    111  CD  GLU A  17      30.173  74.663 -25.044  1.00 46.41
ATOM    112  OE1 GLU A  17      30.997  74.973 -24.160  1.00 50.97
ATOM    113  OE2 GLU A  17      30.528  74.333 -26.192  1.00 47.31
ATOM    114  N   LYS A  18      26.162  76.106 -26.423  1.00 38.14
ATOM    115  CA  LYS A  18      25.390  75.490 -27.489  1.00 36.59
ATOM    116  C   LYS A  18      26.189  74.336 -28.077  1.00 35.70
ATOM    117  O   LYS A  18      27.186  74.553 -28.726  1.00 35.80
ATOM    118  CB  LYS A  18      25.078  76.547 -28.555  1.00 35.73
ATOM    119  CG  LYS A  18      24.642  75.967 -29.873  1.00 35.86
ATOM    120  CD  LYS A  18      24.304  77.030 -30.889  1.00 32.18
ATOM    121  CE  LYS A  18      23.847  76.454 -32.203  1.00 30.56
ATOM    122  NZ  LYS A  18      23.525  77.616 -33.110  1.00 28.09
ATOM    123  N   VAL A  19      25.740  73.104 -27.883  1.00 34.54
ATOM    124  CA  VAL A  19      26.489  72.024 -28.480  1.00 33.14
ATOM    125  C   VAL A  19      25.814  71.336 -29.702  1.00 31.93
ATOM    126  O   VAL A  19      24.659  70.939 -29.621  1.00 30.42
ATOM    127  CB  VAL A  19      26.948  71.030 -27.399  1.00 32.22
ATOM    128  CG1 VAL A  19      27.930  70.120 -27.985  1.00 33.61
ATOM    129  CG2 VAL A  19      27.634  71.795 -26.270  1.00 32.41
ATOM    130  N   THR A  20      26.586  71.154 -30.793  1.00 30.75
ATOM    131  CA  THR A  20      26.129  70.433 -32.017  1.00 30.63
ATOM    132  C   THR A  20      26.803  69.064 -32.325  1.00 29.61
ATOM    133  O   THR A  20      28.002  68.986 -32.412  1.00 28.29
ATOM    134  CB  THR A  20      26.358  71.321 -33.227  1.00 30.22
ATOM    135  OG1 THR A  20      26.098  72.665 -32.851  1.00 33.58
ATOM    136  CG2 THR A  20      25.454  70.942 -34.404  1.00 33.21
ATOM    137  N   LEU A  21      26.040  67.994 -32.533  1.00 29.29
ATOM    138  CA  LEU A  21      26.700  66.703 -32.864  1.00 27.84
ATOM    139  C   LEU A  21      26.557  66.244 -34.315  1.00 27.04
ATOM    140  O   LEU A  21      25.477  65.992 -34.733  1.00 27.86
ATOM    141  CB  LEU A  21      26.195  65.601 -31.949  1.00 27.07
ATOM    142  CG  LEU A  21      26.733  65.616 -30.538  1.00 26.22
ATOM    143  CD1 LEU A  21      26.467  64.263 -30.005  1.00 22.98
ATOM    144  CD2 LEU A  21      28.210  65.836 -30.545  1.00 24.93
ATOM    145  N   SER A  22      27.666  66.097 -35.041  1.00 26.93
ATOM    146  CA  SER A  22      27.686  65.831 -36.452  1.00 25.10
ATOM    147  C   SER A  22      27.878  64.323 -36.752  1.00 25.45
ATOM    148  O   SER A  22      28.824  63.705 -36.279  1.00 25.57
ATOM    149  CB  SER A  22      28.845  66.590 -37.029  1.00 25.68
ATOM    150  OG  SER A  22      30.064  66.188 -36.403  1.00 23.64
ATOM    151  N   CYS A  23      26.991  63.763 -37.572  1.00 24.02
ATOM    152  CA  CYS A  23      27.004  62.372 -37.923  1.00 22.83
ATOM    153  C   CYS A  23      26.979  62.271 -39.446  1.00 23.31
ATOM    154  O   CYS A  23      26.279  63.033 -40.098  1.00 23.51
ATOM    155  CB  CYS A  23      25.766  61.690 -37.327  1.00 21.98
ATOM    156  SG  CYS A  23      25.500  60.064 -38.017  1.00 27.28
ATOM    157  N   GLN A  24      27.724  61.334 -40.069  1.00 24.11
ATOM    158  CA  GLN A  24      27.667  61.306 -41.533  1.00 22.59
ATOM    159  C   GLN A  24      27.779  59.925 -42.002  1.00 21.63
ATOM    160  O   GLN A  24      28.489  59.172 -41.354  1.00 24.40
ATOM    161  CB  GLN A  24      28.770  62.176 -42.143  1.00 21.88
ATOM    162  CG  GLN A  24      30.159  61.762 -41.757  1.00 21.77
ATOM    163  CD  GLN A  24      31.178  62.618 -42.429  1.00 26.24
ATOM    164  OE1 GLN A  24      31.091  63.863 -42.343  1.00 29.92
ATOM    165  NE2 GLN A  24      32.140  61.991 -43.145  1.00 24.42
ATOM    166  N   GLN A  25      27.160  59.595 -43.134  1.00 20.02
ATOM    167  CA  GLN A  25      27.124  58.224 -43.673  1.00 21.13
ATOM    168  C   GLN A  25      27.819  58.088 -45.004  1.00 20.72
ATOM    169  O   GLN A  25      28.362  59.074 -45.564  1.00 22.35
ATOM    170  CB  GLN A  25      25.756  57.546 -43.767  1.00 19.39
ATOM    171  CG  GLN A  25      24.519  58.524 -43.955  1.00 20.36
ATOM    172  CD  GLN A  25      23.359  57.917 -44.753  1.00 23.09
ATOM    173  OE1 GLN A  25      22.679  56.907 -44.328  1.00 19.57
ATOM    174  NE2 GLN A  25      23.099  58.545 -45.937  1.00 16.66
ATOM    175  N   THR A  26      27.877  56.829 -45.457  1.00 18.37
ATOM    176  CA  THR A  26      28.528  56.500 -46.708  1.00 16.35
ATOM    177  C   THR A  26      27.721  55.440 -47.431  1.00 17.39
ATOM    178  O   THR A  26      27.938  55.242 -48.615  1.00 17.50
ATOM    179  CB  THR A  26      29.959  56.011 -46.482  1.00 16.16
ATOM    180  OG1 THR A  26      29.910  54.845 -45.647  1.00 11.99
ATOM    181  CG2 THR A  26      30.757  57.080 -45.751  1.00 13.64
ATOM    182  N   ASN A  27      26.734  54.815 -46.773  1.00 17.97
ATOM    183  CA  ASN A  27      25.938  53.826 -47.485  1.00 18.36
ATOM    184  C   ASN A  27      24.715  54.509 -47.983  1.00 18.04
ATOM    185  O   ASN A  27      23.783  53.876 -48.453  1.00 18.57
ATOM    186  CB  ASN A  27      25.558  52.683 -46.505  1.00 20.73
ATOM    187  CG  ASN A  27      25.725  51.289 -47.098  1.00 24.04
ATOM    188  OD1 ASN A  27      26.831  50.715 -47.091  1.00 29.48
ATOM    189  ND2 ASN A  27      24.608  50.706 -47.571  1.00 30.58
ATOM    190  N   ASN A  28      24.671  55.826 -47.792  1.00 20.40
ATOM    191  CA  ASN A  28      23.537  56.642 -48.189  1.00 19.02
ATOM    192  C   ASN A  28      22.188  55.904 -47.921  1.00 19.71
ATOM    193  O   ASN A  28      21.534  55.410 -48.886  1.00 19.66
ATOM    194  CB  ASN A  28      23.680  56.862 -49.657  1.00 20.31
ATOM    195  CG  ASN A  28      24.155  58.217 -50.032  1.00 20.99
ATOM    196  OD1 ASN A  28      23.445  59.211 -49.917  1.00 27.80
ATOM    197  ND2 ASN A  28      25.368  58.270 -50.570  1.00 24.27
ATOM    198  N   HIS A  29      21.795  55.744 -46.648  1.00 18.69
ATOM    199  CA  HIS A  29      20.457  55.153 -46.346  1.00 18.06
ATOM    200  C   HIS A  29      19.444  56.308 -46.121  1.00 16.73
ATOM    201  O   HIS A  29      19.811  57.331 -45.565  1.00 20.04
ATOM    202  CB  HIS A  29      20.507  54.337 -45.095  1.00 17.41
ATOM    203  CG  HIS A  29      21.021  52.959 -45.269  1.00 19.31
ATOM    204  ND1 HIS A  29      20.203  51.888 -45.553  1.00 16.65
ATOM    205  CD2 HIS A  29      22.258  52.452 -45.058  1.00 21.43
ATOM    206  CE1 HIS A  29      20.941  50.796 -45.604  1.00 25.33
ATOM    207  NE2 HIS A  29      22.191  51.109 -45.304  1.00 22.12
ATOM    208  N   ASN A  30      18.211  56.170 -46.565  1.00 16.43
ATOM    209  CA  ASN A  30      17.159  57.197 -46.310  1.00 17.97
ATOM    210  C   ASN A  30      17.031  57.559 -44.839  1.00 16.70
ATOM    211  O   ASN A  30      17.239  58.757 -44.450  1.00 17.12
ATOM    212  CB  ASN A  30      15.761  56.739 -46.736  1.00 17.02
ATOM    213  CG  ASN A  30      15.515  56.891 -48.242  1.00 22.50
ATOM    214  OD1 ASN A  30      15.136  57.977 -48.709  1.00 18.29
ATOM    215  ND2 ASN A  30      15.689  55.759 -49.011  1.00 22.63
ATOM    216  N   ASN A  31      16.761  56.515 -44.054  1.00 11.02
ATOM    217  CA  ASN A  31      16.530  56.652 -42.671  1.00  9.90
ATOM    218  C   ASN A  31      17.818  56.798 -41.902  1.00  6.58
ATOM    219  O   ASN A  31      18.694  55.898 -41.955  1.00  4.85
ATOM    220  CB  ASN A  31      15.760  55.424 -42.145  1.00  6.98
ATOM    221  CG  ASN A  31      14.467  55.180 -42.966  1.00 14.28
ATOM    222  OD1 ASN A  31      13.762  56.123 -43.321  1.00  7.84
ATOM    223  ND2 ASN A  31      14.218  53.914 -43.341  1.00 16.55
ATOM    224  N   MET A  32      17.807  57.813 -41.093  1.00  5.23
ATOM    225  CA  MET A  32      18.898  58.140 -40.201  1.00  7.27
ATOM    226  C   MET A  32      18.254  58.442 -38.836  1.00  8.07
ATOM    227  O   MET A  32      17.211  58.997 -38.766  1.00  8.99
ATOM    228  CB  MET A  32      19.672  59.387 -40.702  1.00  3.95
ATOM    229  CG  MET A  32      20.577  59.136 -41.919  1.00  5.49
ATOM    230  SD  MET A  32      21.698  60.644 -42.175  1.00  5.77
ATOM    231  CE  MET A  32      22.930  60.281 -40.924  1.00  2.69
ATOM    232  N   TYR A  33      18.939  58.049 -37.781  1.00 10.23
ATOM    233  CA  TYR A  33      18.485  58.134 -36.453  1.00 11.65
ATOM    234  C   TYR A  33      19.529  58.685 -35.519  1.00 13.00
ATOM    235  O   TYR A  33      20.745  58.482 -35.738  1.00 14.80
ATOM    236  CB  TYR A  33      18.183  56.755 -35.952  1.00  8.27
ATOM    237  CG  TYR A  33      17.172  55.995 -36.797  1.00  9.16
ATOM    238  CD1 TYR A  33      17.567  55.372 -37.947  1.00  9.60
ATOM    239  CD2 TYR A  33      15.875  55.813 -36.394  1.00  8.35
ATOM    240  CE1 TYR A  33      16.726  54.629 -38.655  1.00  8.48
ATOM    241  CE2 TYR A  33      14.994  55.044 -37.161  1.00  4.06
ATOM    242  CZ  TYR A  33      15.412  54.492 -38.272  1.00  2.00
ATOM    243  OH  TYR A  33      14.651  53.753 -39.062  1.00  2.00
ATOM    244  N   TRP A  34      19.017  59.313 -34.456  1.00 12.47
ATOM    245  CA  TRP A  34      19.789  59.833 -33.397  1.00 14.01
ATOM    246  C   TRP A  34      19.380  59.348 -32.091  1.00 14.80
ATOM    247  O   TRP A  34      18.295  59.679 -31.673  1.00 13.65
ATOM    248  CB  TRP A  34      19.719  61.354 -33.312  1.00 14.33
ATOM    249  CG  TRP A  34      21.039  62.043 -33.708  1.00 14.58
ATOM    250  CD1 TRP A  34      21.164  63.184 -34.489  1.00 21.03
ATOM    251  CD2 TRP A  34      22.393  61.706 -33.337  1.00 21.37
ATOM    252  NE1 TRP A  34      22.489  63.581 -34.609  1.00 18.93
ATOM    253  CE2 TRP A  34      23.268  62.656 -33.967  1.00 22.46
ATOM    254  CE3 TRP A  34      22.966  60.679 -32.611  1.00 22.42
ATOM    255  CZ2 TRP A  34      24.640  62.626 -33.817  1.00 16.69
ATOM    256  CZ3 TRP A  34      24.360  60.669 -32.487  1.00 19.46
ATOM    257  CH2 TRP A  34      25.156  61.624 -33.089  1.00 16.75
ATOM    258  N   TYR A  35      20.318  58.700 -31.373  1.00 16.59
ATOM    259  CA  TYR A  35      20.025  58.048 -30.110  1.00 19.53
ATOM    260  C   TYR A  35      20.770  58.434 -28.838  1.00 23.24
ATOM    261  O   TYR A  35      21.798  59.136 -28.807  1.00 23.03
ATOM    262  CB  TYR A  35      20.165  56.517 -30.238  1.00 19.62
ATOM    263  CG  TYR A  35      19.116  55.815 -31.007  1.00 17.41
ATOM    264  CD1 TYR A  35      19.385  55.211 -32.233  1.00 24.24
ATOM    265  CD2 TYR A  35      17.824  55.757 -30.540  1.00 26.35
ATOM    266  CE1 TYR A  35      18.329  54.539 -32.996  1.00 23.20
ATOM    267  CE2 TYR A  35      16.774  55.105 -31.289  1.00 23.93
ATOM    268  CZ  TYR A  35      17.047  54.502 -32.502  1.00 18.60
ATOM    269  OH  TYR A  35      16.022  53.857 -33.132  1.00 18.41
ATOM    270  N   ARG A  36      20.215  57.924 -27.745  1.00 26.23
ATOM    271  CA  ARG A  36      20.751  58.211 -26.419  1.00 28.69
ATOM    272  C   ARG A  36      20.212  57.170 -25.494  1.00 28.15
ATOM    273  O   ARG A  36      19.027  56.836 -25.571  1.00 28.01
ATOM    274  CB  ARG A  36      20.285  59.583 -25.939  1.00 27.85
ATOM    275  CG  ARG A  36      20.493  59.755 -24.462  1.00 31.16
ATOM    276  CD  ARG A  36      19.602  60.811 -23.864  1.00 33.89
ATOM    277  NE  ARG A  36      20.211  61.355 -22.672  1.00 36.37
ATOM    278  CZ  ARG A  36      19.768  62.446 -22.062  1.00 41.06
ATOM    279  NH1 ARG A  36      18.687  63.103 -22.518  1.00 39.15
ATOM    280  NH2 ARG A  36      20.414  62.881 -20.979  1.00 45.24
ATOM    281  N   GLN A  37      21.052  56.654 -24.618  1.00 27.73
ATOM    282  CA  GLN A  37      20.513  55.667 -23.666  1.00 29.93
ATOM    283  C   GLN A  37      20.937  55.839 -22.220  1.00 32.10
ATOM    284  O   GLN A  37      22.045  56.329 -21.956  1.00 31.45
ATOM    285  CB  GLN A  37      20.940  54.259 -24.103  1.00 28.84
ATOM    286  CG  GLN A  37      22.207  53.757 -23.477  1.00 28.69
ATOM    287  CD  GLN A  37      23.398  54.608 -23.778  1.00 28.99
ATOM    288  OE1 GLN A  37      23.312  55.848 -23.782  1.00 31.15
ATOM    289  NE2 GLN A  37      24.542  53.954 -23.997  1.00 31.03
ATOM    290  N   ASP A  38      20.091  55.359 -21.292  1.00 35.15
ATOM    291  CA  ASP A  38      20.347  55.510 -19.830  1.00 37.59
ATOM    292  C   ASP A  38      21.750  54.926 -19.513  1.00 39.77
ATOM    293  O   ASP A  38      22.144  53.892 -20.107  1.00 39.61
ATOM    294  CB  ASP A  38      19.246  54.830 -18.980  1.00 37.64
ATOM    295  CG  ASP A  38      17.786  55.219 -19.403  1.00 40.45
ATOM    296  OD1 ASP A  38      16.827  54.657 -18.785  1.00 43.63
ATOM    297  OD2 ASP A  38      17.596  56.075 -20.341  1.00 42.66
ATOM    298  N   THR A  39      22.522  55.610 -18.641  1.00 40.55
ATOM    299  CA  THR A  39      23.847  55.118 -18.192  1.00 40.95
ATOM    300  C   THR A  39      23.898  53.578 -18.042  1.00 40.92
ATOM    301  O   THR A  39      23.483  53.036 -17.009  1.00 41.40
ATOM    302  CB  THR A  39      24.208  55.719 -16.803  1.00 41.28
ATOM    303  OG1 THR A  39      23.294  55.208 -15.795  1.00 40.20
ATOM    304  CG2 THR A  39      24.172  57.241 -16.865  1.00 38.52
ATOM    305  N   GLY A  40      24.365  52.867 -19.061  1.00 40.84
ATOM    306  CA  GLY A  40      24.301  51.382 -19.003  1.00 39.24
ATOM    307  C   GLY A  40      22.895  50.808 -18.952  1.00 39.07
ATOM    308  O   GLY A  40      22.571  49.886 -18.168  1.00 38.71
ATOM    309  N   HIS A  41      22.035  51.322 -19.806  1.00 38.93
ATOM    310  CA  HIS A  41      20.732  50.721 -19.935  1.00 39.45
ATOM    311  C   HIS A  41      20.433  50.476 -21.375  1.00 38.06
ATOM    312  O   HIS A  41      21.288  49.913 -22.066  1.00 39.00
ATOM    313  CB  HIS A  41      19.656  51.558 -19.295  1.00 40.24
ATOM    314  CG  HIS A  41      19.886  51.795 -17.843  1.00 44.06
ATOM    315  ND1 HIS A  41      20.900  52.611 -17.378  1.00 44.73
ATOM    316  CD2 HIS A  41      19.210  51.352 -16.751  1.00 44.64
ATOM    317  CE1 HIS A  41      20.838  52.657 -16.056  1.00 48.20
ATOM    318  NE2 HIS A  41      19.828  51.897 -15.653  1.00 46.58
ATOM    319  N   GLY A  42      19.234  50.901 -21.798  1.00 36.92
ATOM    320  CA  GLY A  42      18.756  50.882 -23.205  1.00 33.98
ATOM    321  C   GLY A  42      18.650  52.260 -23.892  1.00 32.32
ATOM    322  O   GLY A  42      18.530  53.325 -23.203  1.00 30.64
ATOM    323  N   LEU A  43      18.686  52.201 -25.244  1.00 30.24
ATOM    324  CA  LEU A  43      18.813  53.349 -26.156  1.00 28.39
ATOM    325  C   LEU A  43      17.429  53.821 -26.436  1.00 26.43
ATOM    326  O   LEU A  43      16.610  53.017 -26.821  1.00 27.01
ATOM    327  CB  LEU A  43      19.447  52.940 -27.507  1.00 26.17
ATOM    328  CG  LEU A  43      20.808  52.296 -27.686  1.00 27.83
ATOM    329  CD1 LEU A  43      20.850  51.996 -29.120  1.00 20.60
ATOM    330  CD2 LEU A  43      22.063  53.200 -27.360  1.00 26.64
ATOM    331  N   ARG A  44      17.190  55.112 -26.282  1.00 25.05
ATOM    332  CA  ARG A  44      15.838  55.669 -26.456  1.00 21.42
ATOM    333  C   ARG A  44      15.875  56.773 -27.502  1.00 18.53
ATOM    334  O   ARG A  44      16.653  57.707 -27.355  1.00 15.20
ATOM    335  CB  ARG A  44      15.350  56.296 -25.153  1.00 21.90
ATOM    336  CG  ARG A  44      14.698  55.388 -24.124  1.00 25.18
ATOM    337  CD  ARG A  44      14.147  56.223 -22.980  1.00 25.46
ATOM    338  NE  ARG A  44      12.690  56.439 -23.148  1.00 32.69
ATOM    339  CZ  ARG A  44      11.874  57.006 -22.248  1.00 31.77
ATOM    340  NH1 ARG A  44      12.363  57.448 -21.079  1.00 32.00
ATOM    341  NH2 ARG A  44      10.555  57.108 -22.503  1.00 30.75
ATOM    342  N   LEU A  45      14.957  56.707 -28.469  1.00 16.07
ATOM    343  CA  LEU A  45      14.820  57.706 -29.550  1.00 16.26
ATOM    344  C   LEU A  45      14.482  59.159 -29.299  1.00 17.44
ATOM    345  O   LEU A  45      13.280  59.517 -29.108  1.00 17.07
ATOM    346  CB  LEU A  45      13.762  57.206 -30.568  1.00 16.13
ATOM    347  CG  LEU A  45      13.630  57.726 -32.009  1.00 13.95
ATOM    348  CD1 LEU A  45      14.927  58.143 -32.676  1.00  9.54
ATOM    349  CD2 LEU A  45      12.942  56.649 -32.893  1.00 15.48
ATOM    350  N   ILE A  46      15.475  60.026 -29.511  1.00 17.03
ATOM    351  CA  ILE A  46      15.239  61.497 -29.465  1.00 17.15
ATOM    352  C   ILE A  46      14.645  62.029 -30.738  1.00 17.84
ATOM    353  O   ILE A  46      13.578  62.589 -30.728  1.00 16.66
ATOM    354  CB  ILE A  46      16.535  62.247 -29.258  1.00 17.70
ATOM    355  CG1 ILE A  46      17.534  61.249 -28.731  1.00 17.56
ATOM    356  CG2 ILE A  46      16.338  63.315 -28.213  1.00 15.51
ATOM    357  CD1 ILE A  46      18.843  61.663 -29.077  1.00 31.46
ATOM    358  N   HIS A  47      15.366  61.844 -31.845  1.00 18.47
ATOM    359  CA  HIS A  47      14.915  62.350 -33.169  1.00 19.88
ATOM    360  C   HIS A  47      15.342  61.473 -34.313  1.00 19.68
ATOM    361  O   HIS A  47      16.442  60.924 -34.283  1.00 20.02
ATOM    362  CB  HIS A  47      15.493  63.749 -33.415  1.00 18.60
ATOM    363  CG  HIS A  47      14.717  64.794 -32.719  1.00 20.12
ATOM    364  ND1 HIS A  47      13.370  64.973 -32.962  1.00 19.16
ATOM    365  CD2 HIS A  47      15.052  65.676 -31.756  1.00 18.63
ATOM    366  CE1 HIS A  47      12.922  65.972 -32.223  1.00 21.23
ATOM    367  NE2 HIS A  47      13.925  66.433 -31.500  1.00 23.41
ATOM    368  N   TYR A  48      14.499  61.385 -35.333  1.00 21.16
ATOM    369  CA  TYR A  48      14.814  60.597 -36.549  1.00 20.65
ATOM    370  C   TYR A  48      14.527  61.357 -37.816  1.00 21.75
ATOM    371  O   TYR A  48      14.028  62.495 -37.743  1.00 23.47
ATOM    372  CB  TYR A  48      14.078  59.310 -36.601  1.00 19.65
ATOM    373  CG  TYR A  48      12.582  59.339 -36.698  1.00 15.57
ATOM    374  CD1 TYR A  48      11.852  59.965 -35.756  1.00 12.80
ATOM    375  CD2 TYR A  48      11.909  58.546 -37.644  1.00 13.82
ATOM    376  CE1 TYR A  48      10.495  59.958 -35.784  1.00 20.40
ATOM    377  CE2 TYR A  48      10.548  58.489 -37.674  1.00 20.23
ATOM    378  CZ  TYR A  48       9.848  59.245 -36.721  1.00 21.09
ATOM    379  OH  TYR A  48       8.507  59.262 -36.650  1.00 26.85
ATOM    380  N   SER A  49      14.874  60.783 -38.965  1.00 21.01
ATOM    381  CA  SER A  49      14.604  61.422 -40.248  1.00 21.90
ATOM    382  C   SER A  49      14.467  60.424 -41.392  1.00 23.43
ATOM    383  O   SER A  49      15.316  59.524 -41.525  1.00 25.88
ATOM    384  CB  SER A  49      15.683  62.458 -40.535  1.00 20.33
ATOM    385  OG  SER A  49      15.677  62.884 -41.871  1.00 20.71
ATOM    386  N   TYR A  50      13.399  60.596 -42.210  1.00 25.27
ATOM    387  CA  TYR A  50      13.154  59.850 -43.486  1.00 24.55
ATOM    388  C   TYR A  50      13.955  60.321 -44.693  1.00 23.16
ATOM    389  O   TYR A  50      14.199  59.547 -45.605  1.00 21.41
ATOM    390  CB  TYR A  50      11.662  59.878 -43.843  1.00 25.93
ATOM    391  CG  TYR A  50      10.801  59.254 -42.771  1.00 27.76
ATOM    392  CD1 TYR A  50      11.001  57.919 -42.349  1.00 23.84
ATOM    393  CD2 TYR A  50       9.786  60.020 -42.177  1.00 26.69
ATOM    394  CE1 TYR A  50      10.201  57.382 -41.364  1.00 29.67
ATOM    395  CE2 TYR A  50       9.017  59.535 -41.212  1.00 26.58
ATOM    396  CZ  TYR A  50       9.186  58.226 -40.810  1.00 31.34
ATOM    397  OH  TYR A  50       8.312  57.826 -39.836  1.00 30.53
ATOM    398  N   GLY A  51      14.382  61.599 -44.667  1.00 24.09
ATOM    399  CA  GLY A  51      15.044  62.217 -45.809  1.00 22.40
ATOM    400  C   GLY A  51      15.515  63.611 -45.560  1.00 23.82
ATOM    401  O   GLY A  51      14.961  64.313 -44.716  1.00 26.06
ATOM    402  N   ALA A  52      16.553  64.051 -46.281  1.00 23.19
ATOM    403  CA  ALA A  52      17.007  65.436 -46.141  1.00 23.91
ATOM    404  C   ALA A  52      15.881  66.444 -46.162  1.00 24.25
ATOM    405  O   ALA A  52      14.943  66.314 -46.916  1.00 25.89
ATOM    406  CB  ALA A  52      18.151  65.807 -47.227  1.00 22.66
ATOM    407  N   GLY A  53      16.015  67.459 -45.311  1.00 24.18
ATOM    408  CA  GLY A  53      15.035  68.450 -45.106  1.00 22.02
ATOM    409  C   GLY A  53      13.803  67.916 -44.403  1.00 22.81
ATOM    410  O   GLY A  53      12.703  68.347 -44.689  1.00 21.34
ATOM    411  N   SER A  54      13.971  66.935 -43.509  1.00 22.17
ATOM    412  CA  SER A  54      12.877  66.527 -42.671  1.00 21.55
ATOM    413  C   SER A  54      13.201  65.595 -41.507  1.00 21.71
ATOM    414  O   SER A  54      13.686  64.487 -41.696  1.00 20.84
ATOM    415  CB  SER A  54      11.802  65.882 -43.505  1.00 20.87
ATOM    416  OG  SER A  54      10.948  65.235 -42.602  1.00 23.65
ATOM    417  N   THR A  55      12.833  66.054 -40.303  1.00 22.12
ATOM    418  CA  THR A  55      12.933  65.303 -39.070  1.00 21.61
ATOM    419  C   THR A  55      11.540  65.066 -38.392  1.00 21.37
ATOM    420  O   THR A  55      10.504  65.776 -38.677  1.00 18.29
ATOM    421  CB  THR A  55      13.918  65.965 -38.099  1.00 21.00
ATOM    422  OG1 THR A  55      13.268  67.027 -37.418  1.00 22.30
ATOM    423  CG2 THR A  55      15.184  66.550 -38.840  1.00 24.47
ATOM    424  N   GLU A  56      11.513  64.052 -37.523  1.00 21.59
ATOM    425  CA  GLU A  56      10.357  63.828 -36.597  1.00 23.73
ATOM    426  C   GLU A  56      10.811  63.516 -35.181  1.00 23.29
ATOM    427  O   GLU A  56      11.898  62.891 -34.967  1.00 24.24
ATOM    428  CB  GLU A  56       9.366  62.757 -37.097  1.00 22.89
ATOM    429  CG  GLU A  56       8.972  62.899 -38.593  1.00 23.30
ATOM    430  CD  GLU A  56       7.966  63.975 -38.767  1.00 24.59
ATOM    431  OE1 GLU A  56       6.975  63.962 -38.004  1.00 24.30
ATOM    432  OE2 GLU A  56       8.173  64.864 -39.630  1.00 22.90
ATOM    433  N   LYS A  57       9.977  63.983 -34.260  1.00 21.97
ATOM    434  CA  LYS A  57      10.125  63.815 -32.851  1.00 21.74
ATOM    435  C   LYS A  57      10.046  62.357 -32.520  1.00 23.50
ATOM    436  O   LYS A  57       9.113  61.660 -33.019  1.00 24.08
ATOM    437  CB  LYS A  57       9.004  64.498 -32.131  1.00 21.29
ATOM    438  CG  LYS A  57       9.092  66.030 -32.143  1.00 22.47
ATOM    439  CD  LYS A  57       8.106  66.668 -31.228  1.00 17.06
ATOM    440  CE  LYS A  57       6.736  66.528 -31.850  1.00 19.31
ATOM    441  NZ  LYS A  57       5.969  67.741 -31.538  1.00 13.09
ATOM    442  N   GLY A  58      11.013  61.945 -31.675  1.00 22.52
ATOM    443  CA  GLY A  58      11.141  60.601 -31.144  1.00 23.14
ATOM    444  C   GLY A  58      10.491  60.439 -29.804  1.00 23.00
ATOM    445  O   GLY A  58       9.500  61.107 -29.477  1.00 25.96
ATOM    446  N   ASP A  59      11.057  59.544 -29.011  1.00 22.81
ATOM    447  CA  ASP A  59      10.479  59.219 -27.734  1.00 21.67
ATOM    448  C   ASP A  59      10.615  60.410 -26.766  1.00 20.59
ATOM    449  O   ASP A  59       9.570  60.910 -26.239  1.00 16.51
ATOM    450  CB  ASP A  59      11.204  58.085 -27.102  1.00 21.61
ATOM    451  CG  ASP A  59      10.902  56.820 -27.730  1.00 24.79
ATOM    452  OD1 ASP A  59       9.737  56.567 -28.095  1.00 31.31
ATOM    453  OD2 ASP A  59      11.864  56.042 -27.866  1.00 35.15
ATOM    454  N   ILE A  60      11.906  60.748 -26.535  1.00 14.01
ATOM    455  CA  ILE A  60      12.349  61.815 -25.704  1.00 12.85
ATOM    456  C   ILE A  60      12.806  63.151 -26.431  1.00 13.38
ATOM    457  O   ILE A  60      13.811  63.676 -26.085  1.00  7.88
ATOM    458  CB  ILE A  60      13.442  61.322 -24.741  1.00 11.10
ATOM    459  CG1 ILE A  60      14.791  61.088 -25.491  1.00  7.48
ATOM    460  CG2 ILE A  60      12.981  60.093 -24.170  1.00  7.33
ATOM    461  CD1 ILE A  60      15.782  60.438 -24.619  1.00  6.63
ATOM    462  N   PRO A  61      11.927  63.770 -27.291  1.00 15.12
ATOM    463  CA  PRO A  61      12.273  64.920 -28.126  1.00 15.69
ATOM    464  C   PRO A  61      12.844  66.019 -27.261  1.00 18.53
ATOM    465  O   PRO A  61      14.033  66.465 -27.424  1.00 17.03
ATOM    466  CB  PRO A  61      10.909  65.320 -28.776  1.00 18.22
ATOM    467  CG  PRO A  61       9.837  64.631 -28.044  1.00 14.90
ATOM    468  CD  PRO A  61      10.511  63.389 -27.425  1.00 15.95
ATOM    469  N   ASP A  62      12.055  66.359 -26.241  1.00 19.16
ATOM    470  CA  ASP A  62      12.335  67.506 -25.360  1.00 22.26
ATOM    471  C   ASP A  62      13.779  67.849 -25.121  1.00 22.45
ATOM    472  O   ASP A  62      14.600  66.976 -24.835  1.00 21.75
ATOM    473  CB  ASP A  62      11.652  67.288 -24.035  1.00 22.99
ATOM    474  CG  ASP A  62      10.145  67.026 -24.200  1.00 26.95
ATOM    475  OD1 ASP A  62       9.379  68.031 -24.343  1.00 27.55
ATOM    476  OD2 ASP A  62       9.751  65.812 -24.217  1.00 23.92
ATOM    477  N   GLY A  63      14.084  69.127 -25.257  1.00 23.31
ATOM    478  CA  GLY A  63      15.418  69.672 -24.964  1.00 23.00
ATOM    479  C   GLY A  63      16.459  69.321 -26.028  1.00 25.36
ATOM    480  O   GLY A  63      17.703  69.460 -25.831  1.00 24.68
ATOM    481  N   TYR A  65      15.959  68.720 -27.420  1.00 19.63
ATOM    482  CA  TYR A  65      16.878  68.607 -28.527  1.00 20.06
ATOM    483  C   TYR A  65      16.368  69.227 -29.784  1.00 20.64
ATOM    484  O   TYR A  65      15.126  69.419 -29.965  1.00 23.12
ATOM    485  CB  TYR A  65      17.234  67.148 -28.747  1.00 19.26
ATOM    486  CG  TYR A  65      18.014  66.628 -27.603  1.00 18.44
ATOM    487  CD1 TYR A  65      19.403  66.906 -27.457  1.00 16.23
ATOM    488  CD2 TYR A  65      17.393  65.948 -26.599  1.00 14.82
ATOM    489  CE1 TYR A  65      20.115  66.405 -26.338  1.00 17.23
ATOM    490  CE2 TYR A  65      18.076  65.465 -25.489  1.00 17.56
ATOM    491  CZ  TYR A  65      19.409  65.684 -25.339  1.00 20.74
ATOM    492  OH  TYR A  65      20.037  65.156 -24.211  1.00 24.31
ATOM    493  N   LYS A  66      17.332  69.545 -30.665  1.00 20.59
ATOM    494  CA  LYS A  66      17.100  70.052 -32.030  1.00 18.57
ATOM    495  C   LYS A  66      17.852  69.194 -32.963  1.00 17.77
ATOM    496  O   LYS A  66      18.948  68.800 -32.639  1.00 20.25
ATOM    497  CB  LYS A  66      17.584  71.478 -32.191  1.00 18.01
ATOM    498  CG  LYS A  66      16.390  72.410 -32.349  1.00 14.95
ATOM    499  CD  LYS A  66      15.674  72.462 -31.017  1.00 14.01
ATOM    500  CE  LYS A  66      14.751  73.705 -30.789  1.00 21.17
ATOM    501  NZ  LYS A  66      15.542  75.062 -30.712  1.00 20.26
ATOM    502  N   ALA A  67      17.283  68.861 -34.109  1.00 16.92
ATOM    503  CA  ALA A  67      18.016  68.067 -35.075  1.00 16.23
ATOM    504  C   ALA A  67      18.008  68.801 -36.409  1.00 15.26
ATOM    505  O   ALA A  67      17.425  69.935 -36.527  1.00 15.93
ATOM    506  CB  ALA A  67      17.514  66.589 -35.160  1.00 13.96
ATOM    507  N   SER A  68      18.698  68.217 -37.398  1.00 12.50
ATOM    508  CA  SER A  68      18.651  68.734 -38.754  1.00 10.06
ATOM    509  C   SER A  68      19.205  67.806 -39.812  1.00  9.01
ATOM    510  O   SER A  68      20.371  67.363 -39.695  1.00  9.10
ATOM    511  CB  SER A  68      19.462  70.011 -38.820  1.00  8.25
ATOM    512  OG  SER A  68      19.426  70.358 -40.171  1.00  9.36
ATOM    513  N   ARG A  69      18.460  67.575 -40.888  1.00  7.32
ATOM    514  CA  ARG A  69      18.987  66.675 -42.042  1.00  6.51
ATOM    515  C   ARG A  69      19.050  67.470 -43.266  1.00  6.32
ATOM    516  O   ARG A  69      18.025  67.776 -43.877  1.00  7.29
ATOM    517  CB  ARG A  69      18.025  65.512 -42.346  1.00  7.56
ATOM    518  CG  ARG A  69      18.425  64.404 -43.244  1.00  2.00
ATOM    519  CD  ARG A  69      19.062  63.260 -42.459  1.00  7.87
ATOM    520  NE  ARG A  69      19.565  62.159 -43.299  1.00  2.00
ATOM    521  CZ  ARG A  69      18.724  61.367 -43.970  1.00  9.88
ATOM    522  NH1 ARG A  69      19.189  60.339 -44.719  1.00  2.65
ATOM    523  NH2 ARG A  69      17.380  61.594 -43.841  1.00  6.65
ATOM    524  N   PRO A  70      20.233  67.879 -43.615  1.00  8.98
ATOM    525  CA  PRO A  70      20.571  68.724 -44.742  1.00  8.76
ATOM    526  C   PRO A  70      20.981  68.046 -45.986  1.00  8.00
ATOM    527  O   PRO A  70      21.057  68.718 -47.017  1.00  8.50
ATOM    528  CB  PRO A  70      21.709  69.611 -44.185  1.00 10.30
ATOM    529  CG  PRO A  70      22.478  68.558 -43.262  1.00 10.69
ATOM    530  CD  PRO A  70      21.396  67.681 -42.695  1.00 11.50
ATOM    531  N   SER A  71      21.092  66.704 -45.949  1.00 10.22
ATOM    532  CA  SER A  71      21.519  65.934 -47.038  1.00  7.07
ATOM    533  C   SER A  71      21.439  64.413 -46.663  1.00 10.49
ATOM    534  O   SER A  71      22.057  64.013 -45.654  1.00 12.31
ATOM    535  CB  SER A  71      22.961  66.344 -47.335  1.00  9.69
ATOM    536  OG  SER A  71      23.860  66.173 -46.280  1.00  6.34
ATOM    537  N   GLN A  72      20.687  63.610 -47.418  1.00  7.39
ATOM    538  CA  GLN A  72      20.667  62.122 -47.333  1.00 10.10
ATOM    539  C   GLN A  72      21.697  61.453 -46.511  1.00 10.83
ATOM    540  O   GLN A  72      21.357  60.718 -45.696  1.00 15.05
ATOM    541  CB  GLN A  72      20.553  61.480 -48.729  1.00  8.55
ATOM    542  CG  GLN A  72      19.132  60.903 -48.997  1.00  6.16
ATOM    543  CD  GLN A  72      18.945  59.442 -48.739  1.00  4.96
ATOM    544  OE1 GLN A  72      19.928  58.648 -48.743  1.00  7.54
ATOM    545  NE2 GLN A  72      17.665  59.032 -48.424  1.00  4.14
ATOM    546  N   GLU A  73      22.967  61.840 -46.616  1.00 18.10
ATOM    547  CA  GLU A  73      24.014  61.227 -45.813  1.00 20.45
ATOM    548  C   GLU A  73      24.460  62.009 -44.574  1.00 21.25
ATOM    549  O   GLU A  73      25.455  61.657 -43.906  1.00 22.74
ATOM    550  CB  GLU A  73      25.204  60.777 -46.715  1.00 21.37
ATOM    551  CG  GLU A  73      26.107  61.919 -47.214  1.00 25.91
ATOM    552  CD  GLU A  73      25.471  62.696 -48.296  1.00 30.33
ATOM    553  OE1 GLU A  73      25.819  63.890 -48.434  1.00 36.07
ATOM    554  OE2 GLU A  73      24.575  62.130 -48.985  1.00 37.75
ATOM    555  N   GLN A  74      23.753  63.069 -44.218  1.00 21.10
ATOM    556  CA  GLN A  74      24.223  63.914 -43.050  1.00 18.96
ATOM    557  C   GLN A  74      23.063  64.248 -42.126  1.00 19.32
ATOM    558  O   GLN A  74      21.965  64.539 -42.642  1.00 20.50
ATOM    559  CB  GLN A  74      24.840  65.155 -43.538  1.00 16.28
ATOM    560  CG  GLN A  74      25.188  66.134 -42.337  1.00 20.77
ATOM    561  CD  GLN A  74      26.198  65.514 -41.271  1.00 18.29
ATOM    562  OE1 GLN A  74      26.127  65.828 -40.078  1.00 18.61
ATOM    563  NE2 GLN A  74      27.109  64.603 -41.728  1.00 22.03
ATOM    564  N   PHE A  75      23.271  64.195 -40.802  1.00 20.12
ATOM    565  CA  PHE A  75      22.225  64.478 -39.692  1.00 20.28
ATOM    566  C   PHE A  75      23.044  65.020 -38.500  1.00 20.22
ATOM    567  O   PHE A  75      24.233  64.606 -38.304  1.00 21.49
ATOM    568  CB  PHE A  75      21.526  63.178 -39.228  1.00 19.63
ATOM    569  CG  PHE A  75      20.143  63.339 -38.633  1.00 19.51
ATOM    570  CD1 PHE A  75      19.429  64.541 -38.725  1.00 17.91
ATOM    571  CD2 PHE A  75      19.501  62.247 -38.086  1.00 15.80
ATOM    572  CE1 PHE A  75      18.126  64.640 -38.263  1.00 18.24
ATOM    573  CE2 PHE A  75      18.170  62.395 -37.596  1.00 18.85
ATOM    574  CZ  PHE A  75      17.509  63.600 -37.706  1.00 13.17
ATOM    575  N   SER A  76      22.438  65.895 -37.724  1.00 18.33
ATOM    576  CA  SER A  76      23.094  66.642 -36.635  1.00 19.06
ATOM    577  C   SER A  76      22.195  66.909 -35.418  1.00 19.81
ATOM    578  O   SER A  76      20.976  67.121 -35.561  1.00 21.88
ATOM    579  CB  SER A  76      23.724  67.957 -37.150  1.00 17.55
ATOM    580  OG  SER A  76      24.248  67.727 -38.459  1.00 15.12
ATOM    581  N   LEU A  77      22.764  66.836 -34.218  1.00 19.96
ATOM    582  CA  LEU A  77      21.937  66.978 -32.984  1.00 21.04
ATOM    583  C   LEU A  77      22.306  68.335 -32.408  1.00 22.72
ATOM    584  O   LEU A  77      23.515  68.564 -32.114  1.00 23.84
ATOM    585  CB  LEU A  77      22.267  65.859 -31.972  1.00 19.71
ATOM    586  CG  LEU A  77      21.254  65.468 -30.936  1.00 16.37
ATOM    587  CD1 LEU A  77      20.058  65.094 -31.704  1.00 23.34
ATOM    588  CD2 LEU A  77      21.653  64.259 -30.036  1.00 19.34
ATOM    589  N   ILE A  78      21.331  69.241 -32.370  1.00 24.76
ATOM    590  CA  ILE A  78      21.572  70.568 -31.829  1.00 28.07
ATOM    591  C   ILE A  78      21.116  70.641 -30.376  1.00 29.24
ATOM    592  O   ILE A  78      20.137  70.001 -29.992  1.00 29.48
ATOM    593  CB  ILE A  78      21.083  71.747 -32.771  1.00 28.37
ATOM    594  CG1 ILE A  78      21.845  71.695 -34.109  1.00 30.48
ATOM    595  CG2 ILE A  78      21.437  73.125 -32.176  1.00 25.48
ATOM    596  CD1 ILE A  78      21.085  72.241 -35.308  1.00 32.11
ATOM    597  N   LEU A  79      21.894  71.361 -29.572  1.00 31.09
ATOM    598  CA  LEU A  79      21.646  71.560 -28.153  1.00 33.06
ATOM    599  C   LEU A  79      21.943  72.998 -27.807  1.00 33.59
ATOM    600  O   LEU A  79      23.115  73.408 -27.776  1.00 34.79
ATOM    601  CB  LEU A  79      22.576  70.648 -27.361  1.00 33.63
ATOM    602  CG  LEU A  79      22.018  69.218 -27.316  1.00 33.58
ATOM    603  CD1 LEU A  79      22.503  68.427 -28.455  1.00 35.82
ATOM    604  CD2 LEU A  79      22.473  68.540 -26.077  1.00 32.36
ATOM    605  N   GLU A  80      20.890  73.777 -27.589  1.00 34.47
ATOM    606  CA  GLU A  80      21.055  75.212 -27.578  1.00 34.81
ATOM    607  C   GLU A  80      21.702  75.589 -26.248  1.00 35.80
ATOM    608  O   GLU A  80      22.928  75.889 -26.179  1.00 37.02
ATOM    609  CB  GLU A  80      19.721  75.882 -27.786  1.00 34.59
ATOM    610  CG  GLU A  80      19.770  77.292 -28.411  1.00 34.90
ATOM    611  CD  GLU A  80      19.674  77.291 -29.941  1.00 35.81
ATOM    612  OE1 GLU A  80      18.613  76.862 -30.493  1.00 33.77
ATOM    613  OE2 GLU A  80      20.666  77.723 -30.575  1.00 33.25
ATOM    614  N   SER A  81      20.928  75.517 -25.170  1.00 34.67
ATOM    615  CA  SER A  81      21.519  75.649 -23.834  1.00 33.28
ATOM    616  C   SER A  81      21.590  74.271 -23.172  1.00 32.90
ATOM    617  O   SER A  81      20.570  73.728 -22.759  1.00 32.83
ATOM    618  CB  SER A  81      20.715  76.626 -22.949  1.00 34.47
ATOM    619  OG  SER A  81      20.274  77.805 -23.635  1.00 33.38
ATOM    620  N   ALA A  82      22.800  73.708 -23.122  1.00 32.67
ATOM    621  CA  ALA A  82      23.068  72.434 -22.458  1.00 32.37
ATOM    622  C   ALA A  82      22.717  72.504 -21.007  1.00 32.22
ATOM    623  O   ALA A  82      22.595  73.598 -20.430  1.00 34.49
ATOM    624  CB  ALA A  82      24.509  72.063 -22.586  1.00 31.35
ATOM    625  N   THR A  83      22.610  71.333 -20.405  1.00 31.68
ATOM    626  CA  THR A  83      22.424  71.174 -18.960  1.00 31.76
ATOM    627  C   THR A  83      22.860  69.746 -18.549  1.00 31.96
ATOM    628  O   THR A  83      22.633  68.790 -19.318  1.00 32.23
ATOM    629  CB  THR A  83      20.925  71.301 -18.557  1.00 30.60
ATOM    630  OG1 THR A  83      20.235  70.118 -18.976  1.00 28.00
ATOM    631  CG2 THR A  83      20.285  72.495 -19.217  1.00 33.27
ATOM    632  N   PRO A  84      23.476  69.604 -17.357  1.00 31.47
ATOM    633  CA  PRO A  84      24.094  68.370 -16.921  1.00 30.69
ATOM    634  C   PRO A  84      23.235  67.208 -17.192  1.00 30.90
ATOM    635  O   PRO A  84      23.740  66.259 -17.733  1.00 32.14
ATOM    636  CB  PRO A  84      24.305  68.597 -15.458  1.00 31.44
ATOM    637  CG  PRO A  84      24.748  70.155 -15.443  1.00 30.69
ATOM    638  CD  PRO A  84      23.703  70.712 -16.399  1.00 32.64
ATOM    639  N   SER A  85      21.940  67.289 -16.909  1.00 30.74
ATOM    640  CA  SER A  85      20.986  66.254 -17.312  1.00 30.68
ATOM    641  C   SER A  85      21.299  65.585 -18.671  1.00 29.82
ATOM    642  O   SER A  85      21.387  64.336 -18.758  1.00 29.59
ATOM    643  CB  SER A  85      19.586  66.850 -17.402  1.00 31.56
ATOM    644  OG  SER A  85      19.367  67.736 -16.333  1.00 34.84
ATOM    645  N   GLN A  86      21.439  66.414 -19.717  1.00 27.94
ATOM    646  CA  GLN A  86      21.732  65.966 -21.084  1.00 26.08
ATOM    647  C   GLN A  86      23.091  65.288 -21.160  1.00 26.67
ATOM    648  O   GLN A  86      23.608  64.988 -22.240  1.00 28.23
ATOM    649  CB  GLN A  86      21.691  67.140 -22.047  1.00 25.17
ATOM    650  CG  GLN A  86      20.319  67.829 -22.172  1.00 20.93
ATOM    651  CD  GLN A  86      20.368  69.002 -23.076  1.00 21.62
ATOM    652  OE1 GLN A  86      21.401  69.744 -23.136  1.00 23.80
ATOM    653  NE2 GLN A  86      19.287  69.208 -23.820  1.00 23.26
ATOM    654  N   THR A  87      23.683  64.999 -20.023  1.00 26.64
ATOM    655  CA  THR A  87      25.012  64.384 -20.074  1.00 25.84
ATOM    656  C   THR A  87      24.914  62.912 -20.298  1.00 24.76
ATOM    657  O   THR A  87      24.318  62.224 -19.474  1.00 24.67
ATOM    658  CB  THR A  87      25.758  64.614 -18.804  1.00 25.33
ATOM    659  OG1 THR A  87      26.164  65.997 -18.742  1.00 28.64
ATOM    660  CG2 THR A  87      26.982  63.731 -18.783  1.00 27.86
ATOM    661  N   SER A  88      25.501  62.395 -21.391  1.00 24.36
ATOM    662  CA  SER A  88      25.407  60.952 -21.684  1.00 21.73
ATOM    663  C   SER A  88      26.274  60.418 -22.863  1.00 22.18
ATOM    664  O   SER A  88      27.319  61.007 -23.207  1.00 19.63
ATOM    665  CB  SER A  88      23.940  60.567 -21.884  1.00 20.91
ATOM    666  OG  SER A  88      23.838  59.253 -22.405  1.00 24.54
ATOM    667  N   VAL A  89      25.808  59.310 -23.478  1.00 21.23
ATOM    668  CA  VAL A  89      26.430  58.712 -24.647  1.00 20.48
ATOM    669  C   VAL A  89      25.371  58.628 -25.771  1.00 20.61
ATOM    670  O   VAL A  89      24.345  57.912 -25.598  1.00 19.43
ATOM    671  CB  VAL A  89      26.952  57.283 -24.320  1.00 19.60
ATOM    672  CG1 VAL A  89      27.430  56.704 -25.530  1.00 22.57
ATOM    673  CG2 VAL A  89      28.099  57.282 -23.399  1.00 17.69
ATOM    674  N   TYR A  90      25.614  59.411 -26.856  1.00 20.59
ATOM    675  CA  TYR A  90      24.821  59.476 -28.078  1.00 19.75
ATOM    676  C   TYR A  90      25.227  58.495 -29.234  1.00 19.70
ATOM    677  O   TYR A  90      26.435  58.282 -29.492  1.00 20.90
ATOM    678  CB  TYR A  90      24.762  60.934 -28.553  1.00 21.37
ATOM    679  CG  TYR A  90      24.112  61.839 -27.490  1.00 20.56
ATOM    680  CD1 TYR A  90      24.860  62.303 -26.407  1.00 19.91
ATOM    681  CD2 TYR A  90      22.802  62.251 -27.588  1.00 16.94
ATOM    682  CE1 TYR A  90      24.305  63.093 -25.447  1.00 17.31
ATOM    683  CE2 TYR A  90      22.245  63.063 -26.606  1.00 12.46
ATOM    684  CZ  TYR A  90      22.998  63.423 -25.533  1.00 17.07
ATOM    685  OH  TYR A  90      22.497  64.165 -24.526  1.00 18.29
ATOM    686  N   PHE A  91      24.268  57.943 -29.983  1.00 18.99
ATOM    687  CA  PHE A  91      24.676  56.971 -31.084  1.00 18.42
ATOM    688  C   PHE A  91      23.810  57.255 -32.288  1.00 17.15
ATOM    689  O   PHE A  91      22.624  57.554 -32.137  1.00 16.37
ATOM    690  CB  PHE A  91      24.418  55.526 -30.739  1.00 16.98
ATOM    691  CG  PHE A  91      25.403  54.914 -29.845  1.00 16.49
ATOM    692  CD1 PHE A  91      26.490  54.188 -30.362  1.00 19.19
ATOM    693  CD2 PHE A  91      25.190  54.910 -28.510  1.00 17.43
ATOM    694  CE1 PHE A  91      27.372  53.597 -29.593  1.00 15.02
ATOM    695  CE2 PHE A  91      26.066  54.366 -27.712  1.00 15.69
ATOM    696  CZ  PHE A  91      27.241  53.687 -28.268  1.00 17.74
ATOM    697  N   CYS A  92      24.399  57.129 -33.464  1.00 16.41
ATOM    698  CA  CYS A  92      23.771  57.517 -34.705  1.00 16.96
ATOM    699  C   CYS A  92      23.599  56.269 -35.504  1.00 15.72
ATOM    700  O   CYS A  92      24.488  55.435 -35.526  1.00 16.29
ATOM    701  CB  CYS A  92      24.678  58.472 -35.489  1.00 18.61
ATOM    702  SG  CYS A  92      23.944  59.212 -37.011  1.00 23.63
ATOM    703  N   ALA A  93      22.458  56.140 -36.165  1.00 13.99
ATOM    704  CA  ALA A  93      22.243  55.027 -37.068  1.00 11.57
ATOM    705  C   ALA A  93      21.548  55.415 -38.349  1.00 12.39
ATOM    706  O   ALA A  93      20.745  56.401 -38.424  1.00 11.49
ATOM    707  CB  ALA A  93      21.489  53.930 -36.413  1.00 10.15
ATOM    708  N   SER A  94      21.759  54.539 -39.329  1.00 12.18
ATOM    709  CA  SER A  94      21.044  54.576 -40.607  1.00  9.60
ATOM    710  C   SER A  94      20.648  53.183 -40.926  1.00  9.12
ATOM    711  O   SER A  94      21.406  52.166 -40.720  1.00  6.58
ATOM    712  CB  SER A  94      22.023  55.019 -41.649  1.00  7.65
ATOM    713  OG  SER A  94      23.207  54.268 -41.355  1.00 12.05
ATOM    714  N   GLY A  95      19.505  53.169 -41.543  1.00 11.63
ATOM    715  CA  GLY A  95      18.600  52.030 -41.608  1.00 12.49
ATOM    716  C   GLY A  95      17.878  52.015 -42.984  1.00 14.87
ATOM    717  O   GLY A  95      17.472  53.076 -43.480  1.00 14.59
ATOM    718  N   GLY A  96      17.720  50.808 -43.601  1.00 15.93
ATOM    719  CA  GLY A  96      17.256  50.745 -45.014  1.00 16.18
ATOM    720  C   GLY A  96      17.464  49.438 -45.734  1.00 17.00
ATOM    721  O   GLY A  96      18.383  48.692 -45.438  1.00 17.51
ATOM    722  N   GLY A  97      16.588  49.132 -46.678  1.00 18.28
ATOM    723  CA  GLY A  97      16.631  47.827 -47.309  1.00 17.77
ATOM    724  C   GLY A  97      17.089  46.726 -46.412  1.00 18.83
ATOM    725  O   GLY A  97      17.969  46.009 -46.752  1.00 20.47
ATOM    726  N   GLY A  98      16.462  46.553 -45.261  1.00 21.86
ATOM    727  CA  GLY A  98      16.840  45.474 -44.308  1.00 23.33
ATOM    728  C   GLY A  98      18.162  45.786 -43.608  1.00 25.81
ATOM    729  O   GLY A  98      19.022  44.886 -43.439  1.00 25.35
ATOM    730  N   THR A  99      18.368  47.057 -43.204  1.00 24.75
ATOM    731  CA  THR A  99      19.680  47.437 -42.682  1.00 25.00
ATOM    732  C   THR A  99      19.548  48.550 -41.602  1.00 24.87
ATOM    733  O   THR A  99      18.457  49.170 -41.491  1.00 24.41
ATOM    734  CB  THR A  99      20.609  47.780 -43.897  1.00 26.72
ATOM    735  OG1 THR A  99      20.607  46.656 -44.794  1.00 29.51
ATOM    736  CG2 THR A  99      22.060  48.119 -43.519  1.00 24.08
ATOM    737  N   LEU A 100      20.603  48.685 -40.770  1.00 22.07
ATOM    738  CA  LEU A 100      20.668  49.552 -39.620  1.00 21.67
ATOM    739  C   LEU A 100      22.149  49.677 -39.220  1.00 22.92
ATOM    740  O   LEU A 100      22.780  48.691 -38.892  1.00 22.85
ATOM    741  CB  LEU A 100      19.827  49.030 -38.442  1.00 22.58
ATOM    742  CG  LEU A 100      19.595  49.844 -37.168  1.00 21.21
ATOM    743  CD1 LEU A 100      19.535  51.364 -37.409  1.00 25.83
ATOM    744  CD2 LEU A 100      18.396  49.373 -36.361  1.00 20.40
ATOM    745  N   TYR A 101      22.715  50.878 -39.273  1.00 21.83
ATOM    746  CA  TYR A 101      24.121  50.939 -38.988  1.00 21.69
ATOM    747  C   TYR A 101      24.314  51.712 -37.736  1.00 20.75
ATOM    748  O   TYR A 101      23.656  52.703 -37.532  1.00 19.76
ATOM    749  CB  TYR A 101      24.890  51.480 -40.186  1.00 22.03
ATOM    750  CG  TYR A 101      25.320  50.372 -41.087  1.00 22.85
ATOM    751  CD1 TYR A 101      25.923  50.635 -42.288  1.00 25.76
ATOM    752  CD2 TYR A 101      25.099  49.037 -40.731  1.00 28.10
ATOM    753  CE1 TYR A 101      26.322  49.615 -43.147  1.00 29.14
ATOM    754  CE2 TYR A 101      25.478  47.958 -41.570  1.00 27.04
ATOM    755  CZ  TYR A 101      26.097  48.266 -42.799  1.00 28.81
ATOM    756  OH  TYR A 101      26.508  47.282 -43.689  1.00 25.17
ATOM    757  N   PHE A 108      25.796  51.509 -36.846  1.00 23.14
ATOM    758  CA  PHE A 108      25.593  52.538 -35.802  1.00 22.74
ATOM    759  C   PHE A 108      26.853  53.325 -35.788  1.00 23.97
ATOM    760  O   PHE A 108      27.890  52.816 -36.196  1.00 25.37
ATOM    761  CB  PHE A 108      25.475  51.881 -34.427  1.00 22.25
ATOM    762  CG  PHE A 108      24.058  51.459 -34.040  1.00 16.70
ATOM    763  CD1 PHE A 108      23.678  50.130 -34.142  1.00 15.08
ATOM    764  CD2 PHE A 108      23.131  52.378 -33.574  1.00 18.12
ATOM    765  CE1 PHE A 108      22.438  49.732 -33.768  1.00 16.12
ATOM    766  CE2 PHE A 108      21.855  51.997 -33.209  1.00  7.42
ATOM    767  CZ  PHE A 108      21.483  50.736 -33.298  1.00 12.82
ATOM    768  N   GLY A 109      26.807  54.533 -35.273  1.00 23.99
ATOM    769  CA  GLY A 109      28.025  55.292 -35.101  1.00 24.15
ATOM    770  C   GLY A 109      28.791  54.785 -33.905  1.00 24.01
ATOM    771  O   GLY A 109      28.454  53.768 -33.315  1.00 23.80
ATOM    772  N   ALA A 110      29.861  55.467 -33.547  1.00 25.49
ATOM    773  CA  ALA A 110      30.728  54.861 -32.550  1.00 25.77
ATOM    774  C   ALA A 110      30.348  55.522 -31.280  1.00 26.56
ATOM    775  O   ALA A 110      30.881  55.249 -30.243  1.00 28.13
ATOM    776  CB  ALA A 110      32.212  55.059 -32.896  1.00 26.23
ATOM    777  N   GLY A 111      29.351  56.381 -31.346  1.00 27.71
ATOM    778  CA  GLY A 111      28.863  56.987 -30.135  1.00 27.86
ATOM    779  C   GLY A 111      29.637  58.278 -29.814  1.00 27.73
ATOM    780  O   GLY A 111      30.829  58.413 -30.117  1.00 26.03
ATOM    781  N   THR A 112      28.935  59.222 -29.182  1.00 28.75
ATOM    782  CA  THR A 112      29.537  60.467 -28.644  1.00 28.28
ATOM    783  C   THR A 112      29.319  60.549 -27.147  1.00 28.92
ATOM    784  O   THR A 112      28.196  60.439 -26.702  1.00 30.00
ATOM    785  CB  THR A 112      28.947  61.626 -29.319  1.00 28.48
ATOM    786  OG1 THR A 112      29.185  61.457 -30.712  1.00 28.68
ATOM    787  CG2 THR A 112      29.594  62.918 -28.838  1.00 31.20
ATOM    788  N   ARG A 113      30.403  60.636 -26.377  1.00 30.74
ATOM    789  CA  ARG A 113      30.387  60.678 -24.924  1.00 32.03
ATOM    790  C   ARG A 113      30.446  62.132 -24.544  1.00 31.11
ATOM    791  O   ARG A 113      31.453  62.776 -24.809  1.00 32.54
ATOM    792  CB  ARG A 113      31.630  59.986 -24.374  1.00 32.00
ATOM    793  CG  ARG A 113      31.649  58.473 -24.550  1.00 35.71
ATOM    794  CD  ARG A 113      32.988  57.842 -24.112  1.00 37.55
ATOM    795  NE  ARG A 113      33.135  56.454 -24.554  1.00 44.07
ATOM    796  CZ  ARG A 113      34.213  55.711 -24.329  1.00 48.18
ATOM    797  NH1 ARG A 113      34.232  54.447 -24.748  1.00 49.96
ATOM    798  NH2 ARG A 113      35.280  56.233 -23.702  1.00 51.15
ATOM    799  N   LEU A 114      29.386  62.644 -23.908  1.00 30.65
ATOM    800  CA  LEU A 114      29.223  64.073 -23.619  1.00 29.44
ATOM    801  C   LEU A 114      29.274  64.390 -22.127  1.00 29.99
ATOM    802  O   LEU A 114      29.050  63.498 -21.318  1.00 29.03
ATOM    803  CB  LEU A 114      27.924  64.575 -24.216  1.00 29.38
ATOM    804  CG  LEU A 114      27.736  66.059 -23.995  1.00 27.56
ATOM    805  CD1 LEU A 114      28.957  66.681 -24.544  1.00 27.56
ATOM    806  CD2 LEU A 114      26.492  66.543 -24.706  1.00 25.50
ATOM    807  N   SER A 115      29.539  65.670 -21.765  1.00 30.00
ATOM    808  CA  SER A 115      29.621  66.072 -20.353  1.00 27.94
ATOM    809  C   SER A 115      29.199  67.512 -20.170  1.00 27.64
ATOM    810  O   SER A 115      29.829  68.465 -20.669  1.00 25.16
ATOM    811  CB  SER A 115      31.035  65.824 -19.800  1.00 27.42
ATOM    812  OG  SER A 115      31.646  64.723 -20.470  1.00 27.25
ATOM    813  N   VAL A 116      28.123  67.651 -19.401  1.00 28.68
ATOM    814  CA  VAL A 116      27.453  68.912 -19.238  1.00 29.51
ATOM    815  C   VAL A 116      27.605  69.348 -17.817  1.00 30.12
ATOM    816  O   VAL A 116      26.847  68.922 -16.934  1.00 30.98
ATOM    817  CB  VAL A 116      25.946  68.867 -19.510  1.00 29.62
ATOM    818  CG1 VAL A 116      25.479  70.293 -19.652  1.00 29.79
ATOM    819  CG2 VAL A 116      25.636  68.102 -20.793  1.00 30.72
ATOM    820  N   LEU A 117      28.600  70.205 -17.611  1.00 30.29
ATOM    821  CA  LEU A 117      29.021  70.664 -16.285  1.00 30.02
ATOM    822  C   LEU A 117      28.991  72.211 -16.238  1.00 31.55
ATOM    823  O   LEU A 117      28.115  72.739 -15.535  1.00 32.99
ATOM    824  CB  LEU A 117      30.402  70.080 -15.927  1.00 27.75
ATOM    825  CG  LEU A 117      31.582  70.437 -16.806  1.00 25.62
ATOM    826  CD1 LEU A 117      32.102  71.840 -16.433  1.00 25.56
ATOM    827  CD2 LEU A 117      32.699  69.428 -16.689  1.00 25.18
ATOM    828  OXT LEU A 117      29.765  72.971 -16.897  1.00 32.42
ATOM    830  N   SER B   2     -12.922  87.868 -57.323  1.00 49.46
ATOM    831  CA  SER B   2     -11.806  87.540 -56.402  1.00 48.79
ATOM    832  C   SER B   2     -12.055  86.351 -55.422  1.00 49.31
ATOM    833  O   SER B   2     -13.190  85.844 -55.322  1.00 48.83
ATOM    834  CB  SER B   2     -11.469  88.790 -55.623  1.00 48.77
ATOM    835  OG  SER B   2     -10.170  88.647 -55.125  1.00 48.31
ATOM    836  N   GLN B   3     -10.986  85.888 -54.740  1.00 49.19
ATOM    837  CA  GLN B   3     -11.064  84.920 -53.596  1.00 48.86
ATOM    838  C   GLN B   3     -11.487  85.698 -52.298  1.00 49.55
ATOM    839  O   GLN B   3     -10.695  86.513 -51.788  1.00 50.05
ATOM    840  CB  GLN B   3      -9.707  84.192 -53.388  1.00 48.33
ATOM    841  CG  GLN B   3      -9.746  82.913 -52.500  1.00 47.69
ATOM    842  CD  GLN B   3      -8.367  82.248 -52.242  1.00 46.58
ATOM    843  OE1 GLN B   3      -8.265  81.026 -52.113  1.00 42.58
ATOM    844  NE2 GLN B   3      -7.321  83.060 -52.145  1.00 42.62
ATOM    845  N   PRO B   4     -12.730  85.463 -51.772  1.00 49.48
ATOM    846  CA  PRO B   4     -13.194  86.135 -50.554  1.00 49.75
ATOM    847  C   PRO B   4     -12.220  85.975 -49.369  1.00 49.79
ATOM    848  O   PRO B   4     -11.565  84.909 -49.257  1.00 50.72
ATOM    849  CB  PRO B   4     -14.531  85.438 -50.253  1.00 49.38
ATOM    850  CG  PRO B   4     -14.546  84.264 -51.047  1.00 49.06
ATOM    851  CD  PRO B   4     -13.771  84.553 -52.267  1.00 49.45
ATOM    852  N   ASP B   5     -12.093  87.039 -48.555  1.00 48.69
ATOM    853  CA  ASP B   5     -11.260  87.080 -47.343  1.00 47.45
ATOM    854  C   ASP B   5     -11.474  85.845 -46.457  1.00 47.10
ATOM    855  O   ASP B   5     -12.635  85.374 -46.332  1.00 48.05
ATOM    856  CB  ASP B   5     -11.551  88.375 -46.572  1.00 48.22
ATOM    857  CG  ASP B   5     -10.393  89.390 -46.650  1.00 47.87
ATOM    858  OD1 ASP B   5     -10.500  90.526 -46.098  1.00 46.94
ATOM    859  OD2 ASP B   5      -9.356  89.014 -47.235  1.00 47.90
ATOM    860  N   PRO B   6     -10.389  85.287 -45.865  1.00 45.35
ATOM    861  CA  PRO B   6     -10.480  83.963 -45.209  1.00 44.40
ATOM    862  C   PRO B   6     -11.416  84.024 -44.032  1.00 43.68
ATOM    863  O   PRO B   6     -11.791  85.140 -43.617  1.00 43.26
ATOM    864  CB  PRO B   6      -9.066  83.745 -44.672  1.00 44.87
ATOM    865  CG  PRO B   6      -8.463  85.182 -44.538  1.00 45.39
ATOM    866  CD  PRO B   6      -9.042  85.878 -45.734  1.00 45.51
ATOM    867  N   MET B   7     -11.766  82.859 -43.482  1.00 43.29
ATOM    868  CA  MET B   7     -12.558  82.791 -42.235  1.00 43.42
ATOM    869  C   MET B   7     -11.817  82.205 -41.022  1.00 41.64
ATOM    870  O   MET B   7     -11.003  81.338 -41.176  1.00 41.74
ATOM    871  CB  MET B   7     -13.867  82.057 -42.472  1.00 43.12
ATOM    872  CG  MET B   7     -14.881  82.876 -43.309  1.00 44.63
ATOM    873  SD  MET B   7     -16.391  82.001 -43.780  1.00 46.00
ATOM    874  CE  MET B   7     -16.086  81.536 -45.474  1.00 45.38
ATOM    875  N   PRO B   8     -12.075  82.739 -39.824  1.00 40.58
ATOM    876  CA  PRO B   8     -11.602  82.269 -38.537  1.00 39.41
ATOM    877  C   PRO B   8     -11.354  80.759 -38.486  1.00 39.14
ATOM    878  O   PRO B   8     -10.205  80.297 -38.461  1.00 35.97
ATOM    879  CB  PRO B   8     -12.769  82.608 -37.614  1.00 40.15
ATOM    880  CG  PRO B   8     -13.805  83.511 -38.512  1.00 41.93
ATOM    881  CD  PRO B   8     -12.897  83.954 -39.673  1.00 40.17
ATOM    882  N   ASP B   9     -12.459  80.012 -38.473  1.00 37.97
ATOM    883  CA  ASP B   9     -12.404  78.567 -38.416  1.00 37.87
ATOM    884  C   ASP B   9     -12.072  78.072 -39.838  1.00 35.74
ATOM    885  O   ASP B   9     -12.058  76.906 -40.113  1.00 36.24
ATOM    886  CB  ASP B   9     -13.761  78.077 -37.934  1.00 37.93
ATOM    887  CG  ASP B   9     -14.883  78.722 -38.711  1.00 41.67
ATOM    888  OD1 ASP B   9     -15.393  79.807 -38.263  1.00 38.95
ATOM    889  OD2 ASP B   9     -15.217  78.135 -39.790  1.00 43.48
ATOM    890  N   ASP B  10     -11.808  78.983 -40.757  1.00 34.01
ATOM    891  CA  ASP B  10     -11.432  78.587 -42.104  1.00 31.00
ATOM    892  C   ASP B  10      -9.941  78.590 -42.281  1.00 28.13
ATOM    893  O   ASP B  10      -9.442  78.366 -43.405  1.00 27.56
ATOM    894  CB  ASP B  10     -12.089  79.467 -43.162  1.00 31.03
ATOM    895  CG  ASP B  10     -13.537  79.031 -43.497  1.00 34.41
ATOM    896  OD1 ASP B  10     -14.481  79.227 -42.651  1.00 34.30
ATOM    897  OD2 ASP B  10     -13.741  78.495 -44.632  1.00 35.04
ATOM    898  N   LEU B  11      -9.251  78.865 -41.178  1.00 25.86
ATOM    899  CA  LEU B  11      -7.741  78.964 -41.092  1.00 23.56
ATOM    900  C   LEU B  11      -7.166  77.868 -40.181  1.00 23.57
ATOM    901  O   LEU B  11      -7.882  77.367 -39.268  1.00 26.01
ATOM    902  CB  LEU B  11      -7.290  80.355 -40.609  1.00 20.63
ATOM    903  CG  LEU B  11      -7.653  81.528 -41.534  1.00 18.00
ATOM    904  CD1 LEU B  11      -7.544  82.846 -40.865  1.00 12.99
ATOM    905  CD2 LEU B  11      -6.781  81.594 -42.784  1.00 13.84
ATOM    906  N   HIS B  12      -5.936  77.438 -40.442  1.00 21.48
ATOM    907  CA  HIS B  12      -5.348  76.332 -39.727  1.00 20.33
ATOM    908  C   HIS B  12      -4.675  76.904 -38.512  1.00 21.48
ATOM    909  O   HIS B  12      -4.085  78.055 -38.515  1.00 25.05
ATOM    910  CB  HIS B  12      -4.281  75.644 -40.576  1.00 20.41
ATOM    911  CG  HIS B  12      -4.804  74.672 -41.605  1.00 17.84
ATOM    912  ND1 HIS B  12      -3.961  73.932 -42.413  1.00 16.88
ATOM    913  CD2 HIS B  12      -6.056  74.271 -41.914  1.00 14.19
ATOM    914  CE1 HIS B  12      -4.680  73.127 -43.182  1.00 19.53
ATOM    915  NE2 HIS B  12      -5.958  73.341 -42.930  1.00 11.77
ATOM    916  N   LYS B  13      -4.684  76.094 -37.478  1.00 19.87
ATOM    917  CA  LYS B  13      -4.274  76.539 -36.217  1.00 15.64
ATOM    918  C   LYS B  13      -3.105  75.722 -35.836  1.00 14.91
ATOM    919  O   LYS B  13      -3.162  74.456 -35.690  1.00 12.68
ATOM    920  CB  LYS B  13      -5.357  76.258 -35.218  1.00 16.55
ATOM    921  CG  LYS B  13      -6.629  77.068 -35.451  1.00 18.23
ATOM    922  CD  LYS B  13      -7.676  76.703 -34.429  1.00 17.83
ATOM    923  CE  LYS B  13      -9.096  77.253 -34.794  1.00 17.38
ATOM    924  NZ  LYS B  13      -9.703  76.685 -36.027  1.00 19.74
ATOM    925  N   SER B  14      -2.080  76.493 -35.533  1.00  9.93
ATOM    926  CA  SER B  14      -0.873  76.010 -34.961  1.00  7.98
ATOM    927  C   SER B  14      -1.060  75.122 -33.772  1.00  8.16
ATOM    928  O   SER B  14      -0.506  74.034 -33.780  1.00  7.79
ATOM    929  CB  SER B  14      -0.015  77.203 -34.554  1.00  7.92
ATOM    930  OG  SER B  14       1.229  76.758 -34.063  1.00 11.22
ATOM    931  N   SER B  15      -1.772  75.606 -32.717  1.00  9.50
ATOM    932  CA  SER B  15      -2.182  74.794 -31.569  1.00  8.75
ATOM    933  C   SER B  15      -2.690  73.367 -31.957  1.00  7.50
ATOM    934  O   SER B  15      -2.784  72.491 -31.119  1.00  2.00
ATOM    935  CB  SER B  15      -3.361  75.457 -30.840  1.00 10.06
ATOM    936  OG  SER B  15      -4.501  75.523 -31.686  1.00 11.48
ATOM    937  N   GLU B  16      -3.118  73.202 -33.202  1.00  8.28
ATOM    938  CA  GLU B  16      -3.663  71.873 -33.584  1.00  8.32
ATOM    939  C   GLU B  16      -2.693  70.973 -34.283  1.00  7.34
ATOM    940  O   GLU B  16      -3.077  69.906 -34.819  1.00  9.72
ATOM    941  CB  GLU B  16      -4.940  71.972 -34.384  1.00  6.90
ATOM    942  CG  GLU B  16      -6.110  72.774 -33.611  1.00 13.03
ATOM    943  CD  GLU B  16      -7.082  73.426 -34.592  1.00 15.44
ATOM    944  OE1 GLU B  16      -8.246  73.802 -34.204  1.00 14.49
ATOM    945  OE2 GLU B  16      -6.693  73.489 -35.802  1.00 15.33
ATOM    946  N   PHE B  17      -1.447  71.346 -34.309  1.00  5.54
ATOM    947  CA  PHE B  17      -0.477  70.537 -35.005  1.00  8.01
ATOM    948  C   PHE B  17       0.634  70.002 -34.046  1.00  8.60
ATOM    949  O   PHE B  17       1.639  70.697 -33.698  1.00 10.83
ATOM    950  CB  PHE B  17       0.093  71.335 -36.173  1.00  9.38
ATOM    951  CG  PHE B  17       1.388  70.796 -36.738  1.00  8.94
ATOM    952  CD1 PHE B  17       1.406  69.702 -37.581  1.00  8.04
ATOM    953  CD2 PHE B  17       2.592  71.437 -36.481  1.00 13.11
ATOM    954  CE1 PHE B  17       2.597  69.272 -38.139  1.00  3.89
ATOM    955  CE2 PHE B  17       3.797  70.956 -37.026  1.00  4.66
ATOM    956  CZ  PHE B  17       3.789  69.927 -37.838  1.00  6.54
ATOM    957  N   THR B  18       0.463  68.752 -33.636  1.00  5.37
ATOM    958  CA  THR B  18       1.315  68.198 -32.667  1.00  5.33
ATOM    959  C   THR B  18       2.629  67.818 -33.297  1.00  4.69
ATOM    960  O   THR B  18       3.511  67.445 -32.597  1.00  4.77
ATOM    961  CB  THR B  18       0.720  66.955 -32.010  1.00  6.54
ATOM    962  OG1 THR B  18       1.465  65.775 -32.431  1.00  3.09
ATOM    963  CG2 THR B  18      -0.787  66.747 -32.453  1.00  6.57
ATOM    964  N   GLY B  19       2.715  68.028 -34.598  1.00  5.78
ATOM    965  CA  GLY B  19       3.820  67.641 -35.507  1.00  6.84
ATOM    966  C   GLY B  19       5.073  68.363 -35.118  1.00  8.48
ATOM    967  O   GLY B  19       5.154  68.776 -33.959  1.00 10.21
ATOM    968  N   THR B  20       6.004  68.575 -36.076  1.00  8.52
ATOM    969  CA  THR B  20       7.187  69.354 -35.838  1.00  6.10
ATOM    970  C   THR B  20       7.286  70.595 -36.787  1.00  4.47
ATOM    971  O   THR B  20       7.777  70.493 -37.870  1.00  7.92
ATOM    972  CB  THR B  20       8.422  68.486 -36.181  1.00  7.30
ATOM    973  OG1 THR B  20       8.455  67.268 -35.411  1.00  4.45
ATOM    974  CG2 THR B  20       9.736  69.308 -35.881  1.00  5.58
ATOM    975  N   MET B  21       6.923  71.806 -36.425  1.00  7.84
ATOM    976  CA  MET B  21       6.991  72.951 -37.374  1.00  6.25
ATOM    977  C   MET B  21       8.347  73.215 -38.035  1.00  6.67
ATOM    978  O   MET B  21       8.460  74.145 -38.823  1.00  9.47
ATOM    979  CB  MET B  21       6.533  74.221 -36.666  1.00  9.03
ATOM    980  CG  MET B  21       6.240  75.448 -37.531  1.00  2.99
ATOM    981  SD  MET B  21       4.679  75.068 -38.286  1.00 12.32
ATOM    982  CE  MET B  21       3.576  75.454 -36.948  1.00  2.00
ATOM    983  N   GLY B  22       9.354  72.348 -37.848  1.00  5.67
ATOM    984  CA  GLY B  22      10.657  72.569 -38.394  1.00  5.46
ATOM    985  C   GLY B  22      10.691  72.137 -39.819  1.00  5.45
ATOM    986  O   GLY B  22      11.374  72.766 -40.666  1.00  4.30
ATOM    987  N   ASN B  23       9.894  71.108 -40.152  1.00  4.03
ATOM    988  CA  ASN B  23       9.755  70.722 -41.544  1.00  2.32
ATOM    989  C   ASN B  23       9.094  71.790 -42.450  1.00  3.97
ATOM    990  O   ASN B  23       9.135  71.699 -43.717  1.00  4.25
ATOM    991  CB  ASN B  23       8.988  69.480 -41.632  1.00  3.48
ATOM    992  CG  ASN B  23       9.503  68.445 -40.683  1.00  4.51
ATOM    993  OD1 ASN B  23       8.951  67.398 -40.603  1.00  2.00
ATOM    994  ND2 ASN B  23      10.684  68.724 -40.048  1.00  8.89
ATOM    995  N   MET B  24       8.413  72.746 -41.824  1.00  4.15
ATOM    996  CA  MET B  24       7.869  73.871 -42.604  1.00  6.07
ATOM    997  C   MET B  24       8.935  74.946 -42.606  1.00  8.10
ATOM    998  O   MET B  24       9.056  75.652 -43.569  1.00 11.97
ATOM    999  CB  MET B  24       6.585  74.375 -41.946  1.00  5.93
ATOM   1000  CG  MET B  24       6.282  75.875 -42.155  1.00  6.16
ATOM   1001  SD  MET B  24       5.399  76.020 -43.732  1.00 11.88
ATOM   1002  CE  MET B  24       4.033  74.884 -43.653  1.00 12.63
ATOM   1003  N   LYS B  25       9.591  75.196 -41.477  1.00  9.51
ATOM   1004  CA  LYS B  25      10.632  76.225 -41.474  1.00 12.64
ATOM   1005  C   LYS B  25      11.555  75.823 -42.623  1.00 12.16
ATOM   1006  O   LYS B  25      11.972  76.666 -43.399  1.00 10.17
ATOM   1007  CB  LYS B  25      11.449  76.210 -40.172  1.00 11.58
ATOM   1008  CG  LYS B  25      12.314  77.417 -39.928  1.00 13.23
ATOM   1009  CD  LYS B  25      13.033  77.369 -38.536  1.00 12.03
ATOM   1010  CE  LYS B  25      14.389  78.062 -38.522  1.00 11.09
ATOM   1011  NZ  LYS B  25      14.975  78.650 -37.246  1.00  9.14
ATOM   1012  N   TYR B  26      11.729  74.508 -42.790  1.00 12.78
ATOM   1013  CA  TYR B  26      12.779  73.942 -43.671  1.00 13.08
ATOM   1014  C   TYR B  26      12.727  74.501 -45.052  1.00 14.82
ATOM   1015  O   TYR B  26      13.768  74.870 -45.606  1.00 16.26
ATOM   1016  CB  TYR B  26      12.662  72.412 -43.825  1.00 15.17
ATOM   1017  CG  TYR B  26      13.626  71.883 -44.844  1.00 16.72
ATOM   1018  CD1 TYR B  26      14.993  72.051 -44.706  1.00 16.69
ATOM   1019  CD2 TYR B  26      13.154  71.284 -45.989  1.00 22.97
ATOM   1020  CE1 TYR B  26      15.922  71.599 -45.696  1.00 17.03
ATOM   1021  CE2 TYR B  26      14.042  70.807 -46.984  1.00 21.75
ATOM   1022  CZ  TYR B  26      15.423  71.017 -46.822  1.00 20.28
ATOM   1023  OH  TYR B  26      16.212  70.601 -47.826  1.00 22.50
ATOM   1024  N   LEU B  27      11.513  74.577 -45.606  1.00 15.13
ATOM   1025  CA  LEU B  27      11.258  74.998 -46.969  1.00 11.75
ATOM   1026  C   LEU B  27      11.462  76.511 -47.238  1.00 12.61
ATOM   1027  O   LEU B  27      11.363  76.924 -48.416  1.00 13.55
ATOM   1028  CB  LEU B  27       9.793  74.655 -47.240  1.00 11.96
ATOM   1029  CG  LEU B  27       9.249  73.293 -46.797  1.00 10.71
ATOM   1030  CD1 LEU B  27       7.846  73.236 -47.184  1.00  8.09
ATOM   1031  CD2 LEU B  27      10.048  72.234 -47.482  1.00 10.20
ATOM   1032  N   TYR B  28      11.605  77.351 -46.192  1.00 10.51
ATOM   1033  CA  TYR B  28      11.910  78.786 -46.430  1.00 12.26
ATOM   1034  C   TYR B  28      13.061  79.521 -45.738  1.00  9.88
ATOM   1035  O   TYR B  28      13.247  80.680 -45.994  1.00  9.05
ATOM   1036  CB  TYR B  28      10.688  79.632 -46.251  1.00 12.47
ATOM   1037  CG  TYR B  28       9.486  79.043 -46.815  1.00 16.52
ATOM   1038  CD1 TYR B  28       9.009  77.837 -46.342  1.00 17.14
ATOM   1039  CD2 TYR B  28       8.708  79.739 -47.700  1.00 17.99
ATOM   1040  CE1 TYR B  28       7.896  77.325 -46.807  1.00 19.39
ATOM   1041  CE2 TYR B  28       7.536  79.196 -48.149  1.00 18.75
ATOM   1042  CZ  TYR B  28       7.138  78.013 -47.697  1.00 14.71
ATOM   1043  OH  TYR B  28       5.988  77.435 -48.151  1.00 18.96
ATOM   1044  N   ASP B  29      13.834  78.889 -44.865  1.00 11.42
ATOM   1045  CA  ASP B  29      15.039  79.582 -44.329  1.00 12.07
ATOM   1046  C   ASP B  29      16.120  79.506 -45.382  1.00 12.70
ATOM   1047  O   ASP B  29      16.874  78.462 -45.477  1.00 13.45
ATOM   1048  CB  ASP B  29      15.478  79.013 -42.972  1.00 12.05
ATOM   1049  CG  ASP B  29      16.523  79.893 -42.233  1.00 20.40
ATOM   1050  OD1 ASP B  29      16.977  79.436 -41.118  1.00 25.56
ATOM   1051  OD2 ASP B  29      16.891  81.035 -42.722  1.00 21.98
ATOM   1052  N   ASP B  30      16.145  80.510 -46.279  1.00 10.97
ATOM   1053  CA  ASP B  30      17.227  80.571 -47.304  1.00 12.51
ATOM   1054  C   ASP B  30      17.311  79.226 -48.096  1.00 13.06
ATOM   1055  O   ASP B  30      18.435  78.724 -48.297  1.00 12.50
ATOM   1056  CB  ASP B  30      18.607  80.840 -46.658  1.00 12.06
ATOM   1057  CG  ASP B  30      19.697  81.234 -47.696  1.00 17.11
ATOM   1058  OD1 ASP B  30      19.489  82.195 -48.463  1.00 15.72
ATOM   1059  OD2 ASP B  30      20.774  80.600 -47.724  1.00 14.13
ATOM   1060  N   HIS B  31      16.132  78.730 -48.546  1.00  9.50
ATOM   1061  CA  HIS B  31      15.966  77.483 -49.319  1.00 11.12
ATOM   1062  C   HIS B  31      15.071  77.866 -50.454  1.00 11.29
ATOM   1063  O   HIS B  31      13.974  78.366 -50.185  1.00 16.56
ATOM   1064  CB  HIS B  31      15.131  76.527 -48.447  1.00  9.99
ATOM   1065  CG  HIS B  31      14.696  75.288 -49.095  1.00  7.73
ATOM   1066  ND1 HIS B  31      15.545  74.224 -49.295  1.00  2.00
ATOM   1067  CD2 HIS B  31      13.465  74.898 -49.547  1.00 14.99
ATOM   1068  CE1 HIS B  31      14.855  73.229 -49.825  1.00 11.39
ATOM   1069  NE2 HIS B  31      13.587  73.591 -49.959  1.00  5.47
ATOM   1070  N   TYR B  32      15.557  77.760 -51.681  1.00 11.92
ATOM   1071  CA  TYR B  32      14.771  77.896 -52.927  1.00 12.20
ATOM   1072  C   TYR B  32      15.646  77.342 -54.070  1.00 12.61
ATOM   1073  O   TYR B  32      16.857  77.145 -53.874  1.00 10.79
ATOM   1074  CB  TYR B  32      14.534  79.343 -53.236  1.00 12.35
ATOM   1075  CG  TYR B  32      15.805  80.063 -53.151  1.00 12.45
ATOM   1076  CD1 TYR B  32      16.803  79.780 -54.022  1.00  7.96
ATOM   1077  CD2 TYR B  32      16.029  81.005 -52.146  1.00 10.10
ATOM   1078  CE1 TYR B  32      18.015  80.430 -53.913  1.00 11.27
ATOM   1079  CE2 TYR B  32      17.196  81.659 -52.046  1.00 11.49
ATOM   1080  CZ  TYR B  32      18.206  81.364 -52.904  1.00 13.57
ATOM   1081  OH  TYR B  32      19.445  81.985 -52.705  1.00 15.12
ATOM   1082  N   VAL B  33      15.053  77.207 -55.268  1.00  9.92
ATOM   1083  CA  VAL B  33      15.792  76.815 -56.413  1.00  7.41
ATOM   1084  C   VAL B  33      15.738  77.982 -57.313  1.00  9.49
ATOM   1085  O   VAL B  33      14.617  78.528 -57.530  1.00  7.51
ATOM   1086  CB  VAL B  33      15.069  75.631 -57.030  1.00  7.08
ATOM   1087  CG1 VAL B  33      15.556  75.285 -58.414  1.00  2.45
ATOM   1088  CG2 VAL B  33      15.150  74.529 -56.135  1.00  5.59
ATOM   1089  N   SER B  34      16.898  78.390 -57.879  1.00  8.50
ATOM   1090  CA  SER B  34      16.866  79.564 -58.721  1.00  9.28
ATOM   1091  C   SER B  34      17.727  79.393 -59.896  1.00 10.37
ATOM   1092  O   SER B  34      18.939  79.451 -59.788  1.00 14.13
ATOM   1093  CB  SER B  34      17.181  80.861 -58.005  1.00 10.40
ATOM   1094  OG  SER B  34      16.973  81.971 -58.909  1.00  9.49
ATOM   1095  N   ALA B  35      17.098  79.261 -61.062  1.00 11.32
ATOM   1096  CA  ALA B  35      17.828  79.044 -62.324  1.00  9.78
ATOM   1097  C   ALA B  35      17.370  80.112 -63.260  1.00  8.82
ATOM   1098  O   ALA B  35      16.275  80.511 -63.151  1.00  6.77
ATOM   1099  CB  ALA B  35      17.474  77.737 -62.932  1.00  9.96
ATOM   1100  N   THR B  36      18.220  80.489 -64.208  1.00 10.12
ATOM   1101  CA  THR B  36      18.011  81.657 -65.118  1.00 11.05
ATOM   1102  C   THR B  36      18.294  81.320 -66.544  1.00 12.61
ATOM   1103  O   THR B  36      19.354  80.861 -66.853  1.00 10.92
ATOM   1104  CB  THR B  36      18.942  82.743 -64.777  1.00 11.66
ATOM   1105  OG1 THR B  36      18.747  82.955 -63.382  1.00 15.75
ATOM   1106  CG2 THR B  36      18.594  84.074 -65.630  1.00 11.27
ATOM   1107  N   LYS B  37      17.296  81.531 -67.430  1.00 14.89
ATOM   1108  CA  LYS B  37      17.543  81.310 -68.814  1.00 13.99
ATOM   1109  C   LYS B  37      17.984  79.844 -68.958  1.00 14.22
ATOM   1110  O   LYS B  37      19.196  79.574 -69.047  1.00 11.92
ATOM   1111  CB  LYS B  37      18.653  82.324 -69.197  1.00 14.69
ATOM   1112  CG  LYS B  37      19.098  82.350 -70.666  1.00 14.92
ATOM   1113  CD  LYS B  37      20.481  83.023 -70.818  1.00 15.90
ATOM   1114  CE  LYS B  37      21.493  82.531 -69.826  1.00 18.89
ATOM   1115  NZ  LYS B  37      22.701  83.497 -70.086  1.00 25.94
ATOM   1116  N   VAL B  38      17.018  78.889 -68.941  1.00 14.33
ATOM   1117  CA  VAL B  38      17.333  77.460 -69.217  1.00  8.47
ATOM   1118  C   VAL B  38      16.156  76.741 -69.917  1.00 11.64
ATOM   1119  O   VAL B  38      15.036  77.291 -70.018  1.00 11.70
ATOM   1120  CB  VAL B  38      17.549  76.692 -67.969  1.00  9.41
ATOM   1121  CG1 VAL B  38      18.761  77.135 -67.216  1.00  5.49
ATOM   1122  CG2 VAL B  38      16.192  76.623 -66.976  1.00  3.34
ATOM   1123  N   LYS B  39      16.348  75.481 -70.341  1.00  8.26
ATOM   1124  CA  LYS B  39      15.260  74.869 -70.996  1.00  7.03
ATOM   1125  C   LYS B  39      15.158  73.459 -70.546  1.00  7.23
ATOM   1126  O   LYS B  39      16.188  72.769 -70.251  1.00  4.87
ATOM   1127  CB  LYS B  39      15.431  74.849 -72.513  1.00  8.92
ATOM   1128  CG  LYS B  39      14.042  74.528 -73.349  1.00  8.95
ATOM   1129  CD  LYS B  39      14.417  74.176 -74.848  1.00  5.73
ATOM   1130  CE  LYS B  39      15.312  75.405 -75.341  1.00 11.99
ATOM   1131  NZ  LYS B  39      15.446  75.446 -76.803  1.00 16.06
ATOM   1132  N   SER B  40      13.887  73.080 -70.432  1.00  4.91
ATOM   1133  CA  SER B  40      13.521  71.755 -69.977  1.00  6.31
ATOM   1134  C   SER B  40      14.456  70.798 -70.680  1.00  4.19
ATOM   1135  O   SER B  40      14.844  71.105 -71.730  1.00  7.46
ATOM   1136  CB  SER B  40      12.115  71.366 -70.441  1.00  3.16
ATOM   1137  OG  SER B  40      12.137  69.930 -70.572  1.00  4.42
ATOM   1138  N   VAL B  41      14.734  69.669 -70.124  1.00  4.68
ATOM   1139  CA  VAL B  41      15.584  68.637 -70.775  1.00  5.16
ATOM   1140  C   VAL B  41      15.081  67.212 -70.608  1.00  6.17
ATOM   1141  O   VAL B  41      15.809  66.230 -70.835  1.00  8.77
ATOM   1142  CB  VAL B  41      16.973  68.667 -70.217  1.00  3.62
ATOM   1143  CG1 VAL B  41      17.543  70.203 -70.141  1.00  2.00
ATOM   1144  CG2 VAL B  41      16.981  68.059 -68.909  1.00  2.37
ATOM   1145  N   ASP B  42      13.868  67.049 -70.145  1.00  7.39
ATOM   1146  CA  ASP B  42      13.306  65.666 -70.092  1.00  9.19
ATOM   1147  C   ASP B  42      11.941  65.741 -69.522  1.00  8.29
ATOM   1148  O   ASP B  42      11.325  66.848 -69.425  1.00  9.02
ATOM   1149  CB  ASP B  42      14.161  64.741 -69.201  1.00  8.49
ATOM   1150  CG  ASP B  42      13.714  63.283 -69.281  1.00 12.22
ATOM   1151  OD1 ASP B  42      14.480  62.410 -68.854  1.00  9.11
ATOM   1152  OD2 ASP B  42      12.595  62.983 -69.819  1.00 14.09
ATOM   1153  N   LYS B  43      11.473  64.586 -69.038  1.00  8.95
ATOM   1154  CA  LYS B  43      10.139  64.519 -68.495  1.00  7.59
ATOM   1155  C   LYS B  43       9.684  63.146 -68.063  1.00 10.74
ATOM   1156  O   LYS B  43      10.015  62.135 -68.714  1.00 10.33
ATOM   1157  CB  LYS B  43       9.253  65.059 -69.569  1.00  5.57
ATOM   1158  CG  LYS B  43       7.828  64.484 -69.586  1.00 10.36
ATOM   1159  CD  LYS B  43       6.985  64.859 -70.881  1.00  3.92
ATOM   1160  CE  LYS B  43       6.779  66.394 -71.226  1.00 11.54
ATOM   1161  NZ  LYS B  43       5.771  67.268 -70.464  1.00 12.95
ATOM   1162  N   PHE B  44       8.899  63.089 -66.973  1.00 13.77
ATOM   1163  CA  PHE B  44       8.231  61.846 -66.431  1.00 13.20
ATOM   1164  C   PHE B  44       6.713  61.771 -66.767  1.00 13.65
ATOM   1165  O   PHE B  44       6.333  61.164 -67.764  1.00 14.30
ATOM   1166  CB  PHE B  44       8.265  61.820 -64.913  1.00 15.36
ATOM   1167  CG  PHE B  44       7.633  60.568 -64.303  1.00 18.19
ATOM   1168  CD1 PHE B  44       7.180  60.562 -63.004  1.00 25.22
ATOM   1169  CD2 PHE B  44       7.398  59.431 -65.070  1.00 23.88
ATOM   1170  CE1 PHE B  44       6.605  59.390 -62.409  1.00 26.02
ATOM   1171  CE2 PHE B  44       6.800  58.257 -64.475  1.00 24.48
ATOM   1172  CZ  PHE B  44       6.431  58.275 -63.141  1.00 25.14
ATOM   1173  N   LEU B  45       5.846  62.308 -65.937  1.00 10.95
ATOM   1174  CA  LEU B  45       4.420  62.211 -66.290  1.00 13.95
ATOM   1175  C   LEU B  45       4.007  63.403 -67.129  1.00 13.43
ATOM   1176  O   LEU B  45       4.714  64.387 -67.080  1.00 13.44
ATOM   1177  CB  LEU B  45       3.533  62.034 -65.052  1.00 12.98
ATOM   1178  CG  LEU B  45       3.491  60.557 -64.573  1.00 17.93
ATOM   1179  CD1 LEU B  45       2.605  60.444 -63.348  1.00 15.62
ATOM   1180  CD2 LEU B  45       2.989  59.653 -65.701  1.00 18.26
ATOM   1181  N   ALA B  46       2.807  63.332 -67.766  1.00 15.53
ATOM   1182  CA  ALA B  46       2.294  64.222 -68.816  1.00 13.36
ATOM   1183  C   ALA B  46       2.261  65.697 -68.384  1.00 14.37
ATOM   1184  O   ALA B  46       1.548  66.560 -68.990  1.00 16.33
ATOM   1185  CB  ALA B  46       0.974  63.805 -69.171  1.00 15.72
ATOM   1186  N   HIS B  47       2.986  65.981 -67.335  1.00 11.62
ATOM   1187  CA  HIS B  47       2.946  67.269 -66.763  1.00 12.15
ATOM   1188  C   HIS B  47       4.089  67.604 -65.841  1.00 12.13
ATOM   1189  O   HIS B  47       3.843  68.485 -65.023  1.00 16.78
ATOM   1190  CB  HIS B  47       1.627  67.475 -65.997  1.00 11.30
ATOM   1191  CG  HIS B  47       1.524  66.644 -64.769  1.00  8.04
ATOM   1192  ND1 HIS B  47       1.415  65.265 -64.818  1.00 11.28
ATOM   1193  CD2 HIS B  47       1.572  66.966 -63.462  1.00  9.91
ATOM   1194  CE1 HIS B  47       1.331  64.779 -63.591  1.00 12.14
ATOM   1195  NE2 HIS B  47       1.447  65.780 -62.744  1.00 11.10
ATOM   1196  N   ASP B  48       5.329  67.095 -66.039  1.00 10.44
ATOM   1197  CA  ASP B  48       6.482  67.608 -65.281  1.00 10.07
ATOM   1198  C   ASP B  48       7.732  67.723 -66.130  1.00 11.73
ATOM   1199  O   ASP B  48       8.044  66.806 -66.774  1.00 12.14
ATOM   1200  CB  ASP B  48       6.804  66.628 -64.196  1.00 10.01
ATOM   1201  CG  ASP B  48       7.151  65.308 -64.774  1.00 12.06
ATOM   1202  OD1 ASP B  48       6.255  64.716 -65.450  1.00 16.00
ATOM   1203  OD2 ASP B  48       8.334  64.933 -64.674  1.00 10.05
ATOM   1204  N   LEU B  49       8.419  68.874 -66.147  1.00 14.01
ATOM   1205  CA  LEU B  49       9.622  69.109 -66.936  1.00 11.39
ATOM   1206  C   LEU B  49      10.864  69.134 -66.050  1.00 10.43
ATOM   1207  O   LEU B  49      10.920  69.975 -65.207  1.00  8.63
ATOM   1208  CB  LEU B  49       9.471  70.402 -67.733  1.00 14.66
ATOM   1209  CG  LEU B  49       7.996  70.851 -67.931  1.00 11.19
ATOM   1210  CD1 LEU B  49       8.099  72.163 -68.333  1.00 10.92
ATOM   1211  CD2 LEU B  49       7.245  70.080 -68.995  1.00 11.02
ATOM   1212  N   ILE B  50      11.770  68.146 -66.209  1.00  8.25
ATOM   1213  CA  ILE B  50      13.045  68.051 -65.544  1.00  9.33
ATOM   1214  C   ILE B  50      14.068  69.010 -66.171  1.00 10.09
ATOM   1215  O   ILE B  50      14.155  69.097 -67.364  1.00 11.32
ATOM   1216  CB  ILE B  50      13.693  66.661 -65.734  1.00 10.94
ATOM   1217  CG1 ILE B  50      12.772  65.492 -65.444  1.00  7.35
ATOM   1218  CG2 ILE B  50      15.055  66.522 -64.894  1.00 15.10
ATOM   1219  CD1 ILE B  50      12.196  65.557 -64.237  1.00 19.03
ATOM   1220  N   TYR B  51      14.861  69.697 -65.394  1.00 10.16
ATOM   1221  CA  TYR B  51      15.858  70.595 -65.925  1.00 10.62
ATOM   1222  C   TYR B  51      17.190  70.100 -65.383  1.00 13.67
ATOM   1223  O   TYR B  51      17.173  69.256 -64.457  1.00 13.15
ATOM   1224  CB  TYR B  51      15.580  71.985 -65.381  1.00  9.74
ATOM   1225  CG  TYR B  51      14.372  72.680 -66.007  1.00  4.41
ATOM   1226  CD1 TYR B  51      13.066  72.166 -65.865  1.00  9.42
ATOM   1227  CD2 TYR B  51      14.534  73.789 -66.752  1.00  2.00
ATOM   1228  CE1 TYR B  51      11.920  72.867 -66.435  1.00  3.76
ATOM   1229  CE2 TYR B  51      13.431  74.465 -67.376  1.00  3.37
ATOM   1230  CZ  TYR B  51      12.132  73.991 -67.193  1.00  2.47
ATOM   1231  OH  TYR B  51      11.103  74.610 -67.833  1.00  2.40
ATOM   1232  N   ASN B  52      18.309  70.669 -65.826  1.00 11.97
ATOM   1233  CA  ASN B  52      19.512  70.170 -65.302  1.00 16.18
ATOM   1234  C   ASN B  52      20.011  71.357 -64.563  1.00 18.09
ATOM   1235  O   ASN B  52      20.932  72.001 -65.058  1.00 16.56
ATOM   1236  CB  ASN B  52      20.539  69.722 -66.381  1.00 14.82
ATOM   1237  CG  ASN B  52      20.068  68.591 -67.201  1.00 18.24
ATOM   1238  OD1 ASN B  52      19.771  67.528 -66.662  1.00 22.02
ATOM   1239  ND2 ASN B  52      19.954  68.790 -68.538  1.00 15.48
ATOM   1240  N   ILE B  53      19.397  71.620 -63.404  1.00 19.01
ATOM   1241  CA  ILE B  53      19.784  72.713 -62.507  1.00 18.95
ATOM   1242  C   ILE B  53      20.574  72.138 -61.328  1.00 19.83
ATOM   1243  O   ILE B  53      20.063  71.356 -60.587  1.00 18.44
ATOM   1244  CB  ILE B  53      18.514  73.413 -61.941  1.00 18.10
ATOM   1245  CG1 ILE B  53      17.650  74.111 -63.022  1.00 20.40
ATOM   1246  CG2 ILE B  53      18.850  74.429 -60.893  1.00 15.21
ATOM   1247  CD1 ILE B  53      18.495  74.743 -64.053  1.00 28.21
ATOM   1248  N   SER B  54      21.773  72.639 -61.067  1.00 20.41
ATOM   1249  CA  SER B  54      22.556  72.066 -59.997  1.00 19.93
ATOM   1250  C   SER B  54      22.663  72.786 -58.690  1.00 21.74
ATOM   1251  O   SER B  54      23.084  73.939 -58.644  1.00 22.49
ATOM   1252  CB  SER B  54      24.016  71.951 -60.412  1.00 19.12
ATOM   1253  OG  SER B  54      24.117  71.236 -61.577  1.00 19.90
ATOM   1254  N   ASP B  55      22.484  72.032 -57.619  1.00 24.40
ATOM   1255  CA  ASP B  55      22.631  72.525 -56.276  1.00 27.39
ATOM   1256  C   ASP B  55      23.850  73.400 -56.170  1.00 28.79
ATOM   1257  O   ASP B  55      24.937  72.900 -56.246  1.00 29.60
ATOM   1258  CB  ASP B  55      22.775  71.310 -55.333  1.00 28.70
ATOM   1259  CG  ASP B  55      22.622  71.670 -53.853  1.00 28.72
ATOM   1260  OD1 ASP B  55      22.728  70.776 -52.983  1.00 21.42
ATOM   1261  OD2 ASP B  55      22.423  72.871 -53.570  1.00 29.02
ATOM   1262  N   LYS B  56      23.689  74.715 -55.947  1.00 30.83
ATOM   1263  CA  LYS B  56      24.874  75.548 -55.684  1.00 30.73
ATOM   1264  C   LYS B  56      25.373  75.552 -54.230  1.00 30.90
ATOM   1265  O   LYS B  56      26.582  75.461 -53.950  1.00 32.61
ATOM   1266  CB  LYS B  56      24.687  76.960 -56.247  1.00 31.60
ATOM   1267  CG  LYS B  56      25.160  77.072 -57.720  1.00 32.82
ATOM   1268  CD  LYS B  56      26.585  76.462 -57.886  1.00 37.24
ATOM   1269  CE  LYS B  56      26.706  75.575 -59.119  1.00 35.70
ATOM   1270  NZ  LYS B  56      26.428  76.315 -60.371  1.00 35.95
ATOM   1271  N   LYS B  57      24.428  75.645 -53.310  1.00 31.60
ATOM   1272  CA  LYS B  57      24.639  75.634 -51.870  1.00 31.24
ATOM   1273  C   LYS B  57      25.322  74.360 -51.418  1.00 30.68
ATOM   1274  O   LYS B  57      26.396  74.421 -50.916  1.00 28.36
ATOM   1275  CB  LYS B  57      23.295  75.785 -51.152  1.00 31.97
ATOM   1276  CG  LYS B  57      22.915  77.245 -50.724  1.00 33.43
ATOM   1277  CD  LYS B  57      22.763  78.189 -51.967  1.00 38.46
ATOM   1278  CE  LYS B  57      21.830  79.384 -51.702  1.00 38.33
ATOM   1279  NZ  LYS B  57      20.614  78.991 -50.937  1.00 33.85
ATOM   1280  N   LEU B  58      24.698  73.204 -51.613  1.00 31.37
ATOM   1281  CA  LEU B  58      25.336  71.948 -51.168  1.00 31.93
ATOM   1282  C   LEU B  58      25.752  71.059 -52.354  1.00 31.95
ATOM   1283  O   LEU B  58      26.643  71.387 -53.145  1.00 32.26
ATOM   1284  CB  LEU B  58      24.392  71.172 -50.259  1.00 32.96
ATOM   1285  CG  LEU B  58      23.395  71.988 -49.404  1.00 32.02
ATOM   1286  CD1 LEU B  58      22.251  71.121 -48.917  1.00 36.53
ATOM   1287  CD2 LEU B  58      24.084  72.609 -48.210  1.00 34.80
ATOM   1288  N   LYS B  59      25.098  69.921 -52.485  1.00 31.56
ATOM   1289  CA  LYS B  59      25.498  68.925 -53.512  1.00 30.11
ATOM   1290  C   LYS B  59      24.412  67.847 -53.648  1.00 27.60
ATOM   1291  O   LYS B  59      24.633  66.702 -54.165  1.00 25.06
ATOM   1292  CB  LYS B  59      26.889  68.313 -53.230  1.00 30.42
ATOM   1293  CG  LYS B  59      27.120  67.821 -51.786  1.00 33.62
ATOM   1294  CD  LYS B  59      28.487  67.027 -51.655  1.00 32.10
ATOM   1295  CE  LYS B  59      28.596  66.317 -50.318  1.00 35.13
ATOM   1296  NZ  LYS B  59      29.742  65.287 -50.286  1.00 37.19
ATOM   1297  N   ASN B  60      23.215  68.265 -53.235  1.00 25.43
ATOM   1298  CA  ASN B  60      22.065  67.375 -53.182  1.00 25.07
ATOM   1299  C   ASN B  60      21.634  66.986 -54.603  1.00 23.02
ATOM   1300  O   ASN B  60      21.571  65.851 -54.845  1.00 23.53
ATOM   1301  CB  ASN B  60      20.943  67.975 -52.301  1.00 24.37
ATOM   1302  CG  ASN B  60      21.513  68.539 -51.004  1.00 29.91
ATOM   1303  OD1 ASN B  60      22.355  67.865 -50.312  1.00 22.22
ATOM   1304  ND2 ASN B  60      21.158  69.825 -50.702  1.00 26.60
ATOM   1305  N   TYR B  61      21.386  67.925 -55.539  1.00 22.28
ATOM   1306  CA  TYR B  61      20.766  67.595 -56.850  1.00 21.25
ATOM   1307  C   TYR B  61      21.603  68.088 -57.992  1.00 19.95
ATOM   1308  O   TYR B  61      22.388  68.957 -57.803  1.00 22.42
ATOM   1309  CB  TYR B  61      19.317  68.143 -56.927  1.00 20.47
ATOM   1310  CG  TYR B  61      19.231  69.645 -56.725  1.00 22.50
ATOM   1311  CD1 TYR B  61      19.603  70.503 -57.744  1.00 17.96
ATOM   1312  CD2 TYR B  61      18.819  70.185 -55.508  1.00 22.53
ATOM   1313  CE1 TYR B  61      19.552  71.866 -57.543  1.00 21.42
ATOM   1314  CE2 TYR B  61      18.791  71.524 -55.288  1.00 18.08
ATOM   1315  CZ  TYR B  61      19.175  72.338 -56.311  1.00 18.98
ATOM   1316  OH  TYR B  61      19.158  73.620 -56.151  1.00 23.27
ATOM   1317  N   ASP B  62      21.453  67.527 -59.165  1.00 18.98
ATOM   1318  CA  ASP B  62      21.948  68.124 -60.410  1.00 18.61
ATOM   1319  C   ASP B  62      20.707  68.334 -61.325  1.00 17.80
ATOM   1320  O   ASP B  62      20.795  68.945 -62.349  1.00 17.30
ATOM   1321  CB  ASP B  62      22.852  67.123 -61.091  1.00 19.51
ATOM   1322  CG  ASP B  62      22.099  65.851 -61.414  1.00 18.23
ATOM   1323  OD1 ASP B  62      22.010  64.964 -60.565  1.00 16.70
ATOM   1324  OD2 ASP B  62      21.558  65.780 -62.505  1.00 24.79
ATOM   1325  N   LYS B  63      19.526  67.848 -60.930  1.00 18.24
ATOM   1326  CA  LYS B  63      18.277  67.989 -61.726  1.00 17.27
ATOM   1327  C   LYS B  63      17.025  68.255 -60.877  1.00 16.44
ATOM   1328  O   LYS B  63      17.022  68.000 -59.702  1.00 16.35
ATOM   1329  CB  LYS B  63      18.004  66.723 -62.471  1.00 17.43
ATOM   1330  CG  LYS B  63      18.989  66.354 -63.557  1.00 18.56
ATOM   1331  CD  LYS B  63      18.273  65.328 -64.583  1.00 19.04
ATOM   1332  CE  LYS B  63      19.232  64.535 -65.499  1.00 22.68
ATOM   1333  NZ  LYS B  63      20.351  63.925 -64.725  1.00 20.82
ATOM   1334  N   VAL B  64      15.956  68.762 -61.466  1.00 14.94
ATOM   1335  CA  VAL B  64      14.918  69.428 -60.687  1.00 13.39
ATOM   1336  C   VAL B  64      13.690  69.204 -61.470  1.00 14.07
ATOM   1337  O   VAL B  64      13.659  69.610 -62.662  1.00 13.58
ATOM   1338  CB  VAL B  64      15.129  70.881 -60.563  1.00 13.23
ATOM   1339  CG1 VAL B  64      14.106  71.459 -59.685  1.00 13.27
ATOM   1340  CG2 VAL B  64      16.539  71.163 -59.937  1.00 14.70
ATOM   1341  N   LYS B  65      12.758  68.457 -60.862  1.00 11.22
ATOM   1342  CA  LYS B  65      11.479  68.023 -61.513  1.00 10.59
ATOM   1343  C   LYS B  65      10.399  68.943 -61.018  1.00  9.34
ATOM   1344  O   LYS B  65      10.124  68.893 -59.864  1.00 10.41
ATOM   1345  CB  LYS B  65      11.075  66.669 -61.027  1.00  9.02
ATOM   1346  CG  LYS B  65       9.850  66.003 -61.721  1.00 12.54
ATOM   1347  CD  LYS B  65       9.549  64.629 -60.972  1.00 10.08
ATOM   1348  CE  LYS B  65       8.240  64.021 -61.369  1.00 15.90
ATOM   1349  NZ  LYS B  65       6.934  64.371 -60.782  1.00 11.30
ATOM   1350  N   THR B  66       9.829  69.785 -61.846  1.00  5.88
ATOM   1351  CA  THR B  66       8.816  70.634 -61.359  1.00  7.32
ATOM   1352  C   THR B  66       7.519  70.173 -61.946  1.00  6.50
ATOM   1353  O   THR B  66       7.553  69.747 -63.109  1.00  7.78
ATOM   1354  CB  THR B  66       8.992  72.105 -61.878  1.00  7.09
ATOM   1355  OG1 THR B  66       7.855  72.831 -61.412  1.00  8.11
ATOM   1356  CG2 THR B  66       8.875  72.163 -63.350  1.00  2.38
ATOM   1357  N   GLU B  67       6.431  70.214 -61.200  1.00  4.69
ATOM   1358  CA  GLU B  67       5.170  69.577 -61.684  1.00  7.90
ATOM   1359  C   GLU B  67       4.184  70.675 -61.809  1.00  7.23
ATOM   1360  O   GLU B  67       4.206  71.534 -60.958  1.00 10.86
ATOM   1361  CB  GLU B  67       4.580  68.526 -60.696  1.00  7.73
ATOM   1362  CG  GLU B  67       5.458  67.338 -60.426  1.00  8.95
ATOM   1363  CD  GLU B  67       4.690  66.177 -59.888  1.00 11.55
ATOM   1364  OE1 GLU B  67       4.324  66.244 -58.729  1.00 16.77
ATOM   1365  OE2 GLU B  67       4.470  65.142 -60.591  1.00 16.26
ATOM   1366  N   LEU B  68       3.365  70.693 -62.850  1.00  8.84
ATOM   1367  CA  LEU B  68       2.462  71.833 -63.143  1.00  9.86
ATOM   1368  C   LEU B  68       1.027  71.385 -62.992  1.00 10.53
ATOM   1369  O   LEU B  68       0.791  70.184 -62.825  1.00 10.30
ATOM   1370  CB  LEU B  68       2.716  72.295 -64.551  1.00  9.24
ATOM   1371  CG  LEU B  68       4.027  73.070 -64.676  1.00  7.01
ATOM   1372  CD1 LEU B  68       5.248  72.234 -64.901  1.00 17.00
ATOM   1373  CD2 LEU B  68       4.025  74.132 -65.788  1.00 14.31
ATOM   1374  N   LEU B  69       0.099  72.328 -63.029  1.00 11.18
ATOM   1375  CA  LEU B  69      -1.315  72.050 -62.810  1.00 11.28
ATOM   1376  C   LEU B  69      -1.819  70.892 -63.672  1.00 10.82
ATOM   1377  O   LEU B  69      -2.476  69.979 -63.156  1.00  8.92
ATOM   1378  CB  LEU B  69      -2.130  73.341 -62.923  1.00 12.67
ATOM   1379  CG  LEU B  69      -3.627  73.149 -62.920  1.00 15.85
ATOM   1380  CD1 LEU B  69      -4.010  72.221 -61.839  1.00 18.69
ATOM   1381  CD2 LEU B  69      -4.286  74.471 -62.738  1.00 17.52
ATOM   1382  N   ASN B  70      -1.508  70.919 -64.968  1.00  9.53
ATOM   1383  CA  ASN B  70      -2.003  69.907 -65.903  1.00  9.06
ATOM   1384  C   ASN B  70      -1.073  69.825 -67.089  1.00  9.38
ATOM   1385  O   ASN B  70      -0.050  70.521 -67.152  1.00 10.04
ATOM   1386  CB  ASN B  70      -3.409  70.182 -66.411  1.00  6.28
ATOM   1387  CG  ASN B  70      -3.501  71.506 -66.983  1.00 13.91
ATOM   1388  OD1 ASN B  70      -2.579  71.916 -67.741  1.00 16.29
ATOM   1389  ND2 ASN B  70      -4.504  72.305 -66.529  1.00 11.11
ATOM   1390  N   GLU B  71      -1.424  68.960 -68.016  1.00  7.89
ATOM   1391  CA  GLU B  71      -0.676  68.737 -69.198  1.00  7.99
ATOM   1392  C   GLU B  71      -0.468  69.933 -70.108  1.00  9.63
ATOM   1393  O   GLU B  71       0.627  70.112 -70.552  1.00  8.93
ATOM   1394  CB  GLU B  71      -1.268  67.546 -69.978  1.00  7.88
ATOM   1395  CG  GLU B  71      -0.765  67.327 -71.345  1.00  8.94
ATOM   1396  CD  GLU B  71      -1.738  66.502 -72.194  1.00 19.55
ATOM   1397  OE1 GLU B  71      -2.182  65.417 -71.711  1.00 21.09
ATOM   1398  OE2 GLU B  71      -2.064  66.942 -73.327  1.00 22.55
ATOM   1399  N   ASP B  72      -1.517  70.679 -70.516  1.00 14.68
ATOM   1400  CA  ASP B  72      -1.301  71.873 -71.390  1.00 13.93
ATOM   1401  C   ASP B  72      -0.493  72.928 -70.793  1.00 14.66
ATOM   1402  O   ASP B  72       0.170  73.716 -71.506  1.00 17.22
ATOM   1403  CB  ASP B  72      -2.611  72.412 -71.915  1.00 17.39
ATOM   1404  CG  ASP B  72      -3.429  71.314 -72.501  1.00 19.78
ATOM   1405  OD1 ASP B  72      -2.947  70.643 -73.464  1.00 21.01
ATOM   1406  OD2 ASP B  72      -4.467  71.078 -71.921  1.00 18.49
ATOM   1407  N   LEU B  73      -0.450  72.988 -69.489  1.00 15.50
ATOM   1408  CA  LEU B  73       0.356  74.077 -68.854  1.00 16.88
ATOM   1409  C   LEU B  73       1.795  73.598 -68.994  1.00 17.13
ATOM   1410  O   LEU B  73       2.713  74.421 -68.993  1.00 14.55
ATOM   1411  CB  LEU B  73       0.041  74.280 -67.349  1.00 15.61
ATOM   1412  CG  LEU B  73       0.738  75.289 -66.451  1.00 14.47
ATOM   1413  CD1 LEU B  73       0.660  76.606 -67.087  1.00 15.56
ATOM   1414  CD2 LEU B  73      -0.027  75.293 -65.170  1.00 12.77
ATOM   1415  N   ALA B  74       1.958  72.262 -69.083  1.00 17.65
ATOM   1416  CA  ALA B  74       3.328  71.583 -69.197  1.00 18.93
ATOM   1417  C   ALA B  74       3.979  72.020 -70.515  1.00 17.88
ATOM   1418  O   ALA B  74       5.065  72.519 -70.526  1.00 19.26
ATOM   1419  CB  ALA B  74       3.180  70.088 -69.191  1.00 17.35
ATOM   1420  N   LYS B  75       3.242  71.878 -71.613  1.00 16.67
ATOM   1421  CA  LYS B  75       3.692  72.225 -72.929  1.00 14.00
ATOM   1422  C   LYS B  75       3.926  73.707 -73.032  1.00 14.30
ATOM   1423  O   LYS B  75       5.026  74.104 -73.441  1.00 15.59
ATOM   1424  CB  LYS B  75       2.679  71.749 -73.934  1.00 14.96
ATOM   1425  CG  LYS B  75       1.968  70.381 -73.562  1.00 14.40
ATOM   1426  CD  LYS B  75       2.272  69.253 -74.608  1.00 12.43
ATOM   1427  CE  LYS B  75       1.170  68.249 -74.842  1.00 15.68
ATOM   1428  NZ  LYS B  75      -0.199  68.762 -75.093  1.00 13.37
ATOM   1429  N   LYS B  76       2.984  74.553 -72.617  1.00 12.03
ATOM   1430  CA  LYS B  76       3.311  75.984 -72.654  1.00 10.80
ATOM   1431  C   LYS B  76       4.841  76.225 -72.391  1.00 10.78
ATOM   1432  O   LYS B  76       5.448  77.124 -72.943  1.00  9.45
ATOM   1433  CB  LYS B  76       2.462  76.752 -71.698  1.00  8.57
ATOM   1434  CG  LYS B  76       2.749  78.209 -71.763  1.00  8.38
ATOM   1435  CD  LYS B  76       1.966  78.906 -70.687  1.00  4.09
ATOM   1436  CE  LYS B  76       2.484  80.347 -70.386  1.00  2.00
ATOM   1437  NZ  LYS B  76       1.287  81.228 -69.885  1.00  6.42
ATOM   1438  N   TYR B  77       5.491  75.393 -71.582  1.00 10.61
ATOM   1439  CA  TYR B  77       6.872  75.670 -71.324  1.00 12.40
ATOM   1440  C   TYR B  77       7.830  74.629 -71.793  1.00 12.88
ATOM   1441  O   TYR B  77       9.057  74.842 -71.636  1.00 11.52
ATOM   1442  CB  TYR B  77       7.130  75.839 -69.871  1.00 12.86
ATOM   1443  CG  TYR B  77       6.508  77.058 -69.301  1.00 15.12
ATOM   1444  CD1 TYR B  77       5.163  77.019 -68.837  1.00 14.99
ATOM   1445  CD2 TYR B  77       7.157  78.239 -69.376  1.00  6.11
ATOM   1446  CE1 TYR B  77       4.582  78.144 -68.372  1.00 18.57
ATOM   1447  CE2 TYR B  77       6.584  79.388 -68.847  1.00 16.06
ATOM   1448  CZ  TYR B  77       5.311  79.335 -68.345  1.00  7.39
ATOM   1449  OH  TYR B  77       4.699  80.458 -67.889  1.00 14.02
ATOM   1450  N   LYS B  78       7.263  73.504 -72.250  1.00 14.19
ATOM   1451  CA  LYS B  78       8.003  72.249 -72.535  1.00 15.10
ATOM   1452  C   LYS B  78       9.323  72.472 -73.139  1.00 15.39
ATOM   1453  O   LYS B  78      10.278  71.866 -72.682  1.00 16.90
ATOM   1454  CB  LYS B  78       7.264  71.344 -73.514  1.00 15.32
ATOM   1455  CG  LYS B  78       7.999  69.995 -73.797  1.00 11.68
ATOM   1456  CD  LYS B  78       7.232  69.281 -74.934  1.00 16.61
ATOM   1457  CE  LYS B  78       8.095  68.285 -75.666  1.00 20.76
ATOM   1458  NZ  LYS B  78       9.032  67.580 -74.703  1.00 11.20
ATOM   1459  N   ASP B  79       9.423  73.322 -74.163  1.00 16.73
ATOM   1460  CA  ASP B  79      10.788  73.702 -74.750  1.00 18.74
ATOM   1461  C   ASP B  79      11.135  75.217 -74.946  1.00 20.66
ATOM   1462  O   ASP B  79      11.712  75.641 -76.009  1.00 20.48
ATOM   1463  CB  ASP B  79      10.968  73.054 -76.098  1.00 18.72
ATOM   1464  CG  ASP B  79       9.662  72.840 -76.800  1.00 21.57
ATOM   1465  OD1 ASP B  79       9.419  71.711 -77.346  1.00 25.37
ATOM   1466  OD2 ASP B  79       8.851  73.809 -76.783  1.00 24.82
ATOM   1467  N   GLU B  80      10.863  76.019 -73.924  1.00 19.44
ATOM   1468  CA  GLU B  80      11.144  77.436 -73.999  1.00 19.33
ATOM   1469  C   GLU B  80      12.226  77.796 -73.009  1.00 18.09
ATOM   1470  O   GLU B  80      12.434  77.108 -72.022  1.00 16.55
ATOM   1471  CB  GLU B  80       9.828  78.244 -73.719  1.00 20.36
ATOM   1472  CG  GLU B  80       8.704  78.003 -74.707  1.00 21.54
ATOM   1473  CD  GLU B  80       9.206  78.011 -76.179  1.00 30.53
ATOM   1474  OE1 GLU B  80       9.469  79.116 -76.782  1.00 31.76
ATOM   1475  OE2 GLU B  80       9.326  76.886 -76.746  1.00 31.31
ATOM   1476  N   VAL B  81      12.878  78.937 -73.238  1.00 17.57
ATOM   1477  CA  VAL B  81      13.940  79.359 -72.343  1.00 16.47
ATOM   1478  C   VAL B  81      13.323  80.074 -71.207  1.00 15.80
ATOM   1479  O   VAL B  81      12.771  81.152 -71.433  1.00 16.92
ATOM   1480  CB  VAL B  81      15.086  80.195 -73.045  1.00 17.46
ATOM   1481  CG1 VAL B  81      16.185  80.500 -72.069  1.00 13.61
ATOM   1482  CG2 VAL B  81      15.671  79.426 -74.271  1.00 17.65
ATOM   1483  N   VAL B  82      13.346  79.476 -69.990  1.00 14.23
ATOM   1484  CA  VAL B  82      12.610  80.098 -68.904  1.00 13.60
ATOM   1485  C   VAL B  82      13.534  80.375 -67.765  1.00 12.40
ATOM   1486  O   VAL B  82      14.676  79.967 -67.895  1.00 14.07
ATOM   1487  CB  VAL B  82      11.490  79.249 -68.382  1.00 12.61
ATOM   1488  CG1 VAL B  82      10.354  79.315 -69.282  1.00 10.09
ATOM   1489  CG2 VAL B  82      11.999  77.805 -68.150  1.00 11.70
ATOM   1490  N   ASP B  83      13.039  81.043 -66.689  1.00 10.60
ATOM   1491  CA  ASP B  83      13.762  81.172 -65.403  1.00 11.28
ATOM   1492  C   ASP B  83      13.062  80.297 -64.387  1.00  9.47
ATOM   1493  O   ASP B  83      11.936  79.906 -64.585  1.00  9.22
ATOM   1494  CB  ASP B  83      13.768  82.602 -64.944  1.00  9.92
ATOM   1495  CG  ASP B  83      14.390  83.537 -65.985  1.00 11.34
ATOM   1496  OD1 ASP B  83      15.623  83.444 -66.297  1.00 17.16
ATOM   1497  OD2 ASP B  83      13.664  84.379 -66.431  1.00  6.06
ATOM   1498  N   VAL B  84      13.691  80.060 -63.267  1.00  8.77
ATOM   1499  CA  VAL B  84      13.023  79.298 -62.188  1.00 10.37
ATOM   1500  C   VAL B  84      13.117  79.876 -60.767  1.00 11.30
ATOM   1501  O   VAL B  84      14.126  80.482 -60.456  1.00 13.92
ATOM   1502  CB  VAL B  84      13.628  77.883 -62.165  1.00 10.76
ATOM   1503  CG1 VAL B  84      12.884  77.064 -61.176  1.00  5.69
ATOM   1504  CG2 VAL B  84      13.564  77.266 -63.594  1.00  4.66
ATOM   1505  N   TYR B  85      12.108  79.666 -59.896  1.00  8.83
ATOM   1506  CA  TYR B  85      12.136  80.156 -58.546  1.00  9.12
ATOM   1507  C   TYR B  85      11.096  79.343 -57.815  1.00 10.75
ATOM   1508  O   TYR B  85       9.841  79.621 -57.969  1.00 10.81
ATOM   1509  CB  TYR B  85      11.767  81.683 -58.387  1.00 11.31
ATOM   1510  CG  TYR B  85      12.501  82.121 -57.168  1.00  9.98
ATOM   1511  CD1 TYR B  85      13.853  82.362 -57.238  1.00  8.95
ATOM   1512  CD2 TYR B  85      11.896  82.151 -55.943  1.00  5.62
ATOM   1513  CE1 TYR B  85      14.571  82.620 -56.105  1.00  9.81
ATOM   1514  CE2 TYR B  85      12.609  82.444 -54.793  1.00  5.27
ATOM   1515  CZ  TYR B  85      13.965  82.664 -54.887  1.00 10.35
ATOM   1516  OH  TYR B  85      14.728  83.004 -53.767  1.00 11.66
ATOM   1517  N   GLY B  86      11.541  78.354 -57.052  1.00  7.23
ATOM   1518  CA  GLY B  86      10.644  77.587 -56.266  1.00  7.38
ATOM   1519  C   GLY B  86      11.231  76.949 -55.037  1.00  6.94
ATOM   1520  O   GLY B  86      12.435  76.891 -54.965  1.00  8.25
ATOM   1521  N   SER B  87      10.382  76.472 -54.097  1.00  7.72
ATOM   1522  CA  SER B  87      10.844  75.599 -52.995  1.00  8.44
ATOM   1523  C   SER B  87      10.802  74.121 -53.322  1.00  8.90
ATOM   1524  O   SER B  87       9.713  73.546 -53.513  1.00  9.26
ATOM   1525  CB  SER B  87       9.983  75.747 -51.747  1.00  8.80
ATOM   1526  OG  SER B  87      10.728  75.763 -50.525  1.00  7.70
ATOM   1527  N   ASN B  88      11.982  73.491 -53.252  1.00  8.69
ATOM   1528  CA  ASN B  88      12.165  72.144 -53.582  1.00  7.11
ATOM   1529  C   ASN B  88      12.002  71.279 -52.338  1.00  8.13
ATOM   1530  O   ASN B  88      12.130  71.771 -51.217  1.00  4.36
ATOM   1531  CB  ASN B  88      13.499  71.970 -54.194  1.00  7.12
ATOM   1532  CG  ASN B  88      14.642  72.413 -53.287  1.00 10.18
ATOM   1533  OD1 ASN B  88      14.774  73.557 -53.002  1.00 11.23
ATOM   1534  ND2 ASN B  88      15.541  71.479 -52.920  1.00 14.47
ATOM   1535  N   TYR B  89      11.690  69.987 -52.544  1.00  6.65
ATOM   1536  CA  TYR B  89      11.737  69.031 -51.411  1.00  8.82
ATOM   1537  C   TYR B  89      12.318  67.674 -51.833  1.00  7.44
ATOM   1538  O   TYR B  89      12.585  67.502 -52.994  1.00 11.07
ATOM   1539  CB  TYR B  89      10.314  68.813 -50.904  1.00  8.27
ATOM   1540  CG  TYR B  89       9.512  68.177 -51.942  1.00 11.68
ATOM   1541  CD1 TYR B  89       8.875  68.985 -52.869  1.00 15.37
ATOM   1542  CD2 TYR B  89       9.322  66.799 -51.994  1.00 12.69
ATOM   1543  CE1 TYR B  89       8.097  68.485 -53.860  1.00 17.48
ATOM   1544  CE2 TYR B  89       8.426  66.252 -52.973  1.00 17.91
ATOM   1545  CZ  TYR B  89       7.807  67.121 -53.924  1.00 17.27
ATOM   1546  OH  TYR B  89       6.978  66.738 -55.040  1.00 15.30
ATOM   1547  N   TYR B  90      12.379  66.694 -50.953  1.00  6.70
ATOM   1548  CA  TYR B  90      12.874  65.401 -51.307  1.00  9.56
ATOM   1549  C   TYR B  90      11.972  64.287 -50.795  1.00 10.66
ATOM   1550  O   TYR B  90      11.441  63.521 -51.556  1.00  9.30
ATOM   1551  CB  TYR B  90      14.355  65.180 -50.866  1.00 11.84
ATOM   1552  CG  TYR B  90      15.304  66.388 -51.055  1.00  6.94
ATOM   1553  CD1 TYR B  90      15.061  67.617 -50.466  1.00 11.94
ATOM   1554  CD2 TYR B  90      16.488  66.267 -51.848  1.00 13.00
ATOM   1555  CE1 TYR B  90      16.035  68.788 -50.710  1.00 13.14
ATOM   1556  CE2 TYR B  90      17.361  67.346 -52.107  1.00  6.85
ATOM   1557  CZ  TYR B  90      17.158  68.564 -51.548  1.00 11.37
ATOM   1558  OH  TYR B  90      18.112  69.535 -51.834  1.00 13.49
ATOM   1559  N   VAL B  91      11.758  64.193 -49.511  1.00 12.20
ATOM   1560  CA  VAL B  91      10.935  63.129 -49.007  1.00 12.35
ATOM   1561  C   VAL B  91       9.624  63.043 -49.868  1.00 14.60
ATOM   1562  O   VAL B  91       8.783  63.939 -49.828  1.00 15.23
ATOM   1563  CB  VAL B  91      10.650  63.404 -47.531  1.00 11.92
ATOM   1564  CG1 VAL B  91       9.584  62.436 -46.988  1.00 15.42
ATOM   1565  CG2 VAL B  91      11.821  63.307 -46.758  1.00 10.19
ATOM   1566  N   ASN B  92       9.518  61.970 -50.668  1.00 17.21
ATOM   1567  CA  ASN B  92       8.487  61.746 -51.714  1.00 19.48
ATOM   1568  C   ASN B  92       8.707  62.480 -53.062  1.00 18.45
ATOM   1569  O   ASN B  92       7.691  62.951 -53.670  1.00 21.19
ATOM   1570  CB  ASN B  92       7.082  62.037 -51.126  1.00 19.37
ATOM   1571  CG  ASN B  92       7.038  61.674 -49.672  1.00 22.66
ATOM   1572  OD1 ASN B  92       7.620  60.637 -49.265  1.00 20.81
ATOM   1573  ND2 ASN B  92       6.391  62.518 -48.864  1.00 18.75
ATOM   1574  N   CYS B  93       9.980  62.605 -53.491  1.00 15.78
ATOM   1575  CA  CYS B  93      10.367  63.139 -54.805  1.00 13.75
ATOM   1576  C   CYS B  93      10.644  61.980 -55.647  1.00 13.70
ATOM   1577  O   CYS B  93      11.751  61.344 -55.527  1.00 10.79
ATOM   1578  CB  CYS B  93      11.636  63.954 -54.782  1.00 13.51
ATOM   1579  SG  CYS B  93      11.861  64.897 -56.272  1.00 14.61
ATOM   1580  N   TYR B  94       9.653  61.678 -56.486  1.00 13.67
ATOM   1581  CA  TYR B  94       9.621  60.421 -57.328  1.00 15.69
ATOM   1582  C   TYR B  94       9.675  60.669 -58.829  1.00 15.27
ATOM   1583  O   TYR B  94       9.286  61.762 -59.331  1.00 19.56
ATOM   1584  CB  TYR B  94       8.305  59.659 -57.057  1.00 15.20
ATOM   1585  CG  TYR B  94       7.031  60.478 -57.059  1.00 18.01
ATOM   1586  CD1 TYR B  94       7.022  61.873 -56.649  1.00 15.82
ATOM   1587  CD2 TYR B  94       5.785  59.875 -57.383  1.00 23.47
ATOM   1588  CE1 TYR B  94       5.877  62.615 -56.650  1.00 17.23
ATOM   1589  CE2 TYR B  94       4.621  60.606 -57.388  1.00 19.56
ATOM   1590  CZ  TYR B  94       4.679  62.004 -56.987  1.00 19.32
ATOM   1591  OH  TYR B  94       3.547  62.769 -56.927  1.00 17.22
ATOM   1592  N   PHE B  95       9.970  59.607 -59.527  1.00 17.97
ATOM   1593  CA  PHE B  95      10.083  59.509 -60.982  1.00 19.11
ATOM   1594  C   PHE B  95       9.652  58.228 -61.591  1.00 21.85
ATOM   1595  O   PHE B  95      10.132  57.878 -62.688  1.00 22.70
ATOM   1596  CB  PHE B  95      11.560  59.673 -61.375  1.00 17.11
ATOM   1597  CG  PHE B  95      12.114  61.023 -61.058  1.00 14.83
ATOM   1598  CD1 PHE B  95      12.667  61.299 -59.805  1.00 13.75
ATOM   1599  CD2 PHE B  95      12.203  61.974 -62.026  1.00 14.84
ATOM   1600  CE1 PHE B  95      13.252  62.604 -59.528  1.00  8.51
ATOM   1601  CE2 PHE B  95      12.822  63.262 -61.725  1.00 12.52
ATOM   1602  CZ  PHE B  95      13.338  63.488 -60.464  1.00  6.47
ATOM   1603  N   SER B  96       8.810  57.482 -60.875  1.00 25.99
ATOM   1604  CA  SER B  96       8.347  56.176 -61.296  1.00 28.59
ATOM   1605  C   SER B  96       7.024  55.902 -60.597  1.00 31.56
ATOM   1606  O   SER B  96       6.234  56.815 -60.366  1.00 33.73
ATOM   1607  CB  SER B  96       9.379  55.077 -60.951  1.00 29.62
ATOM   1608  OG  SER B  96       9.536  54.957 -59.559  1.00 28.29
ATOM   1609  N   SER B  97       6.788  54.675 -60.185  1.00 33.99
ATOM   1610  CA  SER B  97       5.468  54.366 -59.653  1.00 38.04
ATOM   1611  C   SER B  97       5.525  54.185 -58.124  1.00 39.63
ATOM   1612  O   SER B  97       4.625  54.625 -57.400  1.00 40.35
ATOM   1613  CB  SER B  97       4.880  53.118 -60.369  1.00 37.97
ATOM   1614  OG  SER B  97       5.813  52.017 -60.388  1.00 40.53
ATOM   1615  N   LYS B  98       6.578  53.505 -57.648  1.00 41.07
ATOM   1616  CA  LYS B  98       6.788  53.287 -56.228  1.00 41.19
ATOM   1617  C   LYS B  98       6.946  54.657 -55.566  1.00 40.42
ATOM   1618  O   LYS B  98       7.752  55.497 -56.014  1.00 40.75
ATOM   1619  CB  LYS B  98       8.019  52.418 -55.969  1.00 41.81
ATOM   1620  CG  LYS B  98       8.231  52.130 -54.448  1.00 46.39
ATOM   1621  CD  LYS B  98       8.799  50.694 -54.215  1.00 47.24
ATOM   1622  CE  LYS B  98       9.540  50.525 -52.875  1.00 44.71
ATOM   1623  NZ  LYS B  98      10.104  49.134 -52.858  1.00 43.05
ATOM   1624  N   ASP B  99       6.189  54.810 -54.474  1.00 38.39
ATOM   1625  CA  ASP B  99       5.901  56.066 -53.718  1.00 34.76
ATOM   1626  C   ASP B  99       7.036  56.611 -52.805  1.00 32.59
ATOM   1627  O   ASP B  99       7.281  57.835 -52.828  1.00 31.60
ATOM   1628  CB  ASP B  99       4.584  55.829 -52.926  1.00 34.67
ATOM   1629  CG  ASP B  99       4.399  54.356 -52.600  1.00 35.24
ATOM   1630  OD1 ASP B  99       5.420  53.669 -52.353  1.00 32.71
ATOM   1631  OD2 ASP B  99       3.253  53.869 -52.686  1.00 40.51
ATOM   1632  N   ASN B 100       7.685  55.702 -52.026  1.00 31.93
ATOM   1633  CA  ASN B 100       8.939  55.992 -51.232  1.00 30.10
ATOM   1634  C   ASN B 100      10.162  55.208 -51.702  1.00 27.75
ATOM   1635  O   ASN B 100      10.419  54.047 -51.296  1.00 26.05
ATOM   1636  CB  ASN B 100       8.766  55.841 -49.718  1.00 30.15
ATOM   1637  CG  ASN B 100       9.343  57.037 -48.930  1.00 33.53
ATOM   1638  OD1 ASN B 100       9.026  57.182 -47.760  1.00 37.67
ATOM   1639  ND2 ASN B 100      10.181  57.898 -49.571  1.00 36.67
ATOM   1640  N   VAL B 101      10.896  55.889 -52.579  1.00 23.52
ATOM   1641  CA  VAL B 101      12.030  55.317 -53.305  1.00 19.42
ATOM   1642  C   VAL B 101      13.074  56.460 -53.430  1.00 17.45
ATOM   1643  O   VAL B 101      12.697  57.638 -53.560  1.00 17.04
ATOM   1644  CB  VAL B 101      11.655  54.932 -54.680  1.00 19.06
ATOM   1645  CG1 VAL B 101      12.769  55.233 -55.580  1.00 16.25
ATOM   1646  CG2 VAL B 101      11.246  53.482 -54.761  1.00 16.36
ATOM   1647  N   TRP B 102      14.352  56.134 -53.434  1.00 13.17
ATOM   1648  CA  TRP B 102      15.408  57.181 -53.580  1.00 11.54
ATOM   1649  C   TRP B 102      16.058  57.307 -55.003  1.00 13.46
ATOM   1650  O   TRP B 102      15.952  56.363 -55.838  1.00 12.67
ATOM   1651  CB  TRP B 102      16.497  57.028 -52.477  1.00 10.48
ATOM   1652  CG  TRP B 102      17.507  58.185 -52.433  1.00  5.07
ATOM   1653  CD1 TRP B 102      17.217  59.462 -52.217  1.00  7.38
ATOM   1654  CD2 TRP B 102      18.941  58.100 -52.532  1.00  6.91
ATOM   1655  NE1 TRP B 102      18.339  60.232 -52.206  1.00 12.31
ATOM   1656  CE2 TRP B 102      19.437  59.423 -52.400  1.00 11.59
ATOM   1657  CE3 TRP B 102      19.844  57.047 -52.618  1.00  2.04
ATOM   1658  CZ2 TRP B 102      20.804  59.745 -52.437  1.00  9.18
ATOM   1659  CZ3 TRP B 102      21.225  57.372 -52.720  1.00 12.39
ATOM   1660  CH2 TRP B 102      21.678  58.744 -52.650  1.00  5.74
ATOM   1661  N   TRP B 103      16.737  58.440 -55.275  1.00 10.67
ATOM   1662  CA  TRP B 103      17.389  58.659 -56.531  1.00 11.92
ATOM   1663  C   TRP B 103      18.728  59.316 -56.402  1.00 12.65
ATOM   1664  O   TRP B 103      19.762  58.621 -56.390  1.00  9.75
ATOM   1665  CB  TRP B 103      16.594  59.594 -57.349  1.00 12.69
ATOM   1666  CG  TRP B 103      15.126  59.184 -57.268  1.00 16.33
ATOM   1667  CD1 TRP B 103      14.267  59.483 -56.223  1.00 18.14
ATOM   1668  CD2 TRP B 103      14.374  58.378 -58.206  1.00 10.68
ATOM   1669  NE1 TRP B 103      12.989  58.940 -56.488  1.00 21.88
ATOM   1670  CE2 TRP B 103      13.016  58.269 -57.681  1.00 16.85
ATOM   1671  CE3 TRP B 103      14.674  57.779 -59.411  1.00  9.65
ATOM   1672  CZ2 TRP B 103      12.003  57.597 -58.327  1.00  5.83
ATOM   1673  CZ3 TRP B 103      13.686  57.072 -60.073  1.00 14.50
ATOM   1674  CH2 TRP B 103      12.327  56.970 -59.508  1.00 16.82
ATOM   1675  N   HIS B 104      18.665  60.638 -56.254  1.00 12.02
ATOM   1676  CA  HIS B 104      19.857  61.491 -56.132  1.00 16.75
ATOM   1677  C   HIS B 104      20.012  62.383 -57.314  1.00 16.77
ATOM   1678  O   HIS B 104      19.530  62.037 -58.414  1.00 18.99
ATOM   1679  CB  HIS B 104      21.213  60.746 -55.925  1.00 16.62
ATOM   1680  CG  HIS B 104      22.336  61.642 -55.459  1.00 25.28
ATOM   1681  ND1 HIS B 104      23.120  62.390 -56.337  1.00 29.30
ATOM   1682  CD2 HIS B 104      22.773  61.953 -54.208  1.00 29.34
ATOM   1683  CE1 HIS B 104      23.952  63.152 -55.647  1.00 29.76
ATOM   1684  NE2 HIS B 104      23.782  62.891 -54.358  1.00 36.11
ATOM   1685  N   GLY B 105      20.739  63.493 -57.095  1.00 18.38
ATOM   1686  CA  GLY B 105      20.819  64.653 -58.034  1.00 16.22
ATOM   1687  C   GLY B 105      19.465  65.145 -58.513  1.00 16.19
ATOM   1688  O   GLY B 105      19.368  65.887 -59.512  1.00 19.12
ATOM   1689  N   LYS B 106      18.393  64.787 -57.799  1.00 14.02
ATOM   1690  CA  LYS B 106      17.084  65.062 -58.255  1.00 12.47
ATOM   1691  C   LYS B 106      16.345  65.731 -57.120  1.00 12.17
ATOM   1692  O   LYS B 106      16.776  65.679 -56.013  1.00 11.55
ATOM   1693  CB  LYS B 106      16.360  63.756 -58.710  1.00 13.14
ATOM   1694  CG  LYS B 106      16.797  63.278 -60.111  1.00  8.35
ATOM   1695  CD  LYS B 106      16.382  61.820 -60.425  1.00 11.82
ATOM   1696  CE  LYS B 106      17.092  61.326 -61.692  1.00 15.57
ATOM   1697  NZ  LYS B 106      18.235  60.490 -61.370  1.00  7.61
ATOM   1698  N   THR B 107      15.234  66.428 -57.401  1.00 13.15
ATOM   1699  CA  THR B 107      14.476  67.159 -56.381  1.00  8.49
ATOM   1700  C   THR B 107      13.231  67.590 -57.055  1.00  6.30
ATOM   1701  O   THR B 107      13.235  67.728 -58.277  1.00  5.01
ATOM   1702  CB  THR B 107      15.275  68.272 -55.782  1.00  8.54
ATOM   1703  OG1 THR B 107      14.660  68.602 -54.511  1.00 14.67
ATOM   1704  CG2 THR B 107      15.330  69.521 -56.648  1.00  9.67
ATOM   1705  N   CYS B 108      12.188  67.807 -56.306  1.00  4.27
ATOM   1706  CA  CYS B 108      10.876  68.141 -56.923  1.00  6.58
ATOM   1707  C   CYS B 108      10.353  69.553 -56.567  1.00  5.36
ATOM   1708  O   CYS B 108      10.907  70.226 -55.725  1.00  5.29
ATOM   1709  CB  CYS B 108       9.803  67.187 -56.465  1.00  6.72
ATOM   1710  SG  CYS B 108      10.094  65.385 -57.069  1.00  9.90
ATOM   1711  N   MET B 109       9.316  70.008 -57.246  1.00  5.12
ATOM   1712  CA  MET B 109       8.679  71.251 -56.801  1.00  7.91
ATOM   1713  C   MET B 109       7.433  71.379 -57.550  1.00  9.35
ATOM   1714  O   MET B 109       6.863  70.371 -58.066  1.00  8.73
ATOM   1715  CB  MET B 109       9.568  72.495 -57.063  1.00  4.69
ATOM   1716  CG  MET B 109      10.500  72.430 -58.287  1.00  4.57
ATOM   1717  SD  MET B 109      11.353  73.955 -58.699  1.00 14.05
ATOM   1718  CE  MET B 109      10.059  75.050 -58.966  1.00  5.69
ATOM   1719  N   TYR B 110       6.937  72.604 -57.591  1.00  9.58
ATOM   1720  CA  TYR B 110       5.757  72.850 -58.404  1.00 10.15
ATOM   1721  C   TYR B 110       5.902  74.323 -58.882  1.00  9.39
ATOM   1722  O   TYR B 110       6.311  75.097 -58.125  1.00  9.09
ATOM   1723  CB  TYR B 110       4.550  72.741 -57.565  1.00  7.44
ATOM   1724  CG  TYR B 110       4.372  71.414 -56.868  1.00  9.66
ATOM   1725  CD1 TYR B 110       4.965  71.150 -55.616  1.00  6.00
ATOM   1726  CD2 TYR B 110       3.577  70.425 -57.453  1.00  3.96
ATOM   1727  CE1 TYR B 110       4.778  69.920 -54.962  1.00 12.85
ATOM   1728  CE2 TYR B 110       3.408  69.212 -56.844  1.00 15.12
ATOM   1729  CZ  TYR B 110       3.977  68.950 -55.612  1.00 12.80
ATOM   1730  OH  TYR B 110       3.699  67.763 -55.123  1.00  5.30
ATOM   1731  N   GLY B 111       5.582  74.631 -60.131  1.00  8.70
ATOM   1732  CA  GLY B 111       5.484  75.996 -60.610  1.00  9.13
ATOM   1733  C   GLY B 111       6.866  76.655 -60.607  1.00  9.52
ATOM   1734  O   GLY B 111       7.889  75.991 -60.731  1.00  8.14
ATOM   1735  N   GLY B 112       6.873  77.960 -60.434  1.00 10.77
ATOM   1736  CA  GLY B 112       8.144  78.748 -60.544  1.00 13.18
ATOM   1737  C   GLY B 112       8.996  78.739 -61.797  1.00 11.17
ATOM   1738  O   GLY B 112      10.105  78.204 -61.791  1.00 13.11
ATOM   1739  N   ILE B 113       8.467  79.310 -62.878  1.00 11.24
ATOM   1740  CA  ILE B 113       9.169  79.449 -64.171  1.00  9.56
ATOM   1741  C   ILE B 113       8.519  80.518 -64.952  1.00 10.23
ATOM   1742  O   ILE B 113       7.281  80.661 -64.867  1.00 10.06
ATOM   1743  CB  ILE B 113       9.006  78.156 -64.984  1.00  8.61
ATOM   1744  CG1 ILE B 113       7.580  77.622 -64.832  1.00  8.65
ATOM   1745  CG2 ILE B 113       9.994  77.192 -64.406  1.00  6.90
ATOM   1746  CD1 ILE B 113       7.313  76.166 -65.516  1.00 12.96
ATOM   1747  N   THR B 114       9.325  81.256 -65.725  1.00 10.16
ATOM   1748  CA  THR B 114       8.774  82.257 -66.629  1.00 11.15
ATOM   1749  C   THR B 114       9.670  82.465 -67.835  1.00 10.54
ATOM   1750  O   THR B 114      10.912  82.234 -67.805  1.00 11.15
ATOM   1751  CB  THR B 114       8.550  83.601 -65.914  1.00 13.35
ATOM   1752  OG1 THR B 114       9.843  84.078 -65.478  1.00 16.18
ATOM   1753  CG2 THR B 114       7.606  83.380 -64.728  1.00  7.66
ATOM   1754  N   LYS B 115       9.050  82.879 -68.928  1.00  9.49
ATOM   1755  CA  LYS B 115       9.785  83.011 -70.168  1.00  9.70
ATOM   1756  C   LYS B 115      10.811  84.122 -69.895  1.00  9.23
ATOM   1757  O   LYS B 115      10.503  85.183 -69.354  1.00  9.06
ATOM   1758  CB  LYS B 115       8.908  83.301 -71.387  1.00 10.49
ATOM   1759  CG  LYS B 115       8.038  82.187 -72.012  1.00 19.64
ATOM   1760  CD  LYS B 115       8.699  80.880 -72.386  1.00 19.57
ATOM   1761  CE  LYS B 115       9.221  80.970 -73.805  1.00 21.13
ATOM   1762  NZ  LYS B 115       8.195  80.572 -74.876  1.00 17.94
ATOM   1763  N   HIS B 116      12.071  83.790 -70.094  1.00 10.99
ATOM   1764  CA  HIS B 116      13.201  84.707 -69.864  1.00 10.07
ATOM   1765  C   HIS B 116      13.223  85.943 -70.791  1.00 12.52
ATOM   1766  O   HIS B 116      13.477  87.033 -70.303  1.00  9.87
ATOM   1767  CB  HIS B 116      14.447  83.988 -70.149  1.00  9.39
ATOM   1768  CG  HIS B 116      15.634  84.874 -70.122  1.00 10.83
ATOM   1769  ND1 HIS B 116      15.658  86.065 -70.805  1.00 10.40
ATOM   1770  CD2 HIS B 116      16.854  84.727 -69.554  1.00  7.08
ATOM   1771  CE1 HIS B 116      16.851  86.627 -70.630  1.00 16.48
ATOM   1772  NE2 HIS B 116      17.600  85.809 -69.915  1.00 13.80
ATOM   1773  N   GLU B 117      12.954  85.711 -72.095  1.00 14.09
ATOM   1774  CA  GLU B 117      13.008  86.715 -73.119  1.00 18.84
ATOM   1775  C   GLU B 117      12.160  87.878 -72.715  1.00 20.59
ATOM   1776  O   GLU B 117      10.973  87.724 -72.412  1.00 18.17
ATOM   1777  CB  GLU B 117      12.507  86.212 -74.453  1.00 19.37
ATOM   1778  CG  GLU B 117      13.333  85.008 -74.997  1.00 25.78
ATOM   1779  CD  GLU B 117      13.310  83.843 -74.035  1.00 27.77
ATOM   1780  OE1 GLU B 117      12.223  83.466 -73.482  1.00 32.69
ATOM   1781  OE2 GLU B 117      14.401  83.336 -73.758  1.00 33.27
ATOM   1782  N   GLY B 118      12.817  89.041 -72.711  1.00 22.37
ATOM   1783  CA  GLY B 118      12.149  90.322 -72.498  1.00 24.73
ATOM   1784  C   GLY B 118      11.132  90.259 -71.360  1.00 26.71
ATOM   1785  O   GLY B 118       9.886  90.422 -71.592  1.00 27.33
ATOM   1786  N   ASN B 119      11.679  89.909 -70.183  1.00 27.51
ATOM   1787  CA  ASN B 119      10.988  89.869 -68.887  1.00 29.14
ATOM   1788  C   ASN B 119      11.884  90.374 -67.752  1.00 29.31
ATOM   1789  O   ASN B 119      11.366  90.684 -66.681  1.00 30.05
ATOM   1790  CB  ASN B 119      10.432  88.477 -68.527  1.00 28.85
ATOM   1791  CG  ASN B 119       9.737  88.451 -67.164  1.00 29.52
ATOM   1792  OD1 ASN B 119       8.930  89.342 -66.828  1.00 26.52
ATOM   1793  ND2 ASN B 119      10.089  87.441 -66.339  1.00 26.90
ATOM   1794  N   HIS B 120      13.196  90.450 -67.971  1.00 28.78
ATOM   1795  CA  HIS B 120      14.067  91.078 -66.995  1.00 29.01
ATOM   1796  C   HIS B 120      14.113  92.632 -67.214  1.00 29.57
ATOM   1797  O   HIS B 120      13.477  93.145 -68.150  1.00 28.35
ATOM   1798  CB  HIS B 120      15.447  90.446 -66.999  1.00 27.87
ATOM   1799  CG  HIS B 120      15.452  88.993 -66.670  1.00 27.03
ATOM   1800  ND1 HIS B 120      16.619  88.308 -66.412  1.00 24.92
ATOM   1801  CD2 HIS B 120      14.451  88.070 -66.614  1.00 27.21
ATOM   1802  CE1 HIS B 120      16.339  87.035 -66.170  1.00 25.59
ATOM   1803  NE2 HIS B 120      15.024  86.861 -66.280  1.00 24.73
ATOM   1804  N   PHE B 121      14.850  93.346 -66.342  1.00 30.72
ATOM   1805  CA  PHE B 121      14.986  94.839 -66.354  1.00 30.52
ATOM   1806  C   PHE B 121      16.146  95.390 -67.176  1.00 31.96
ATOM   1807  O   PHE B 121      17.125  94.668 -67.533  1.00 28.89
ATOM   1808  CB  PHE B 121      15.031  95.395 -64.915  1.00 30.37
ATOM   1809  CG  PHE B 121      13.773  95.020 -64.070  1.00 32.98
ATOM   1810  CD1 PHE B 121      13.731  93.846 -63.346  1.00 29.42
ATOM   1811  CD2 PHE B 121      12.650  95.835 -64.060  1.00 31.22
ATOM   1812  CE1 PHE B 121      12.612  93.474 -62.648  1.00 29.11
ATOM   1813  CE2 PHE B 121      11.490  95.513 -63.325  1.00 31.61
ATOM   1814  CZ  PHE B 121      11.449  94.340 -62.621  1.00 33.06
ATOM   1815  N   ASP B 122      16.012  96.696 -67.433  1.00 33.06
ATOM   1816  CA  ASP B 122      17.021  97.532 -68.102  1.00 35.47
ATOM   1817  C   ASP B 122      18.478  97.100 -67.971  1.00 36.30
ATOM   1818  O   ASP B 122      19.023  96.501 -68.922  1.00 36.41
ATOM   1819  CB  ASP B 122      16.832  98.948 -67.623  1.00 35.80
ATOM   1820  CG  ASP B 122      15.368  99.286 -67.473  1.00 37.96
ATOM   1821  OD1 ASP B 122      14.704  99.441 -68.516  1.00 33.41
ATOM   1822  OD2 ASP B 122      14.876  99.334 -66.319  1.00 41.53
ATOM   1823  N   ASN B 123      19.109  97.411 -66.826  1.00 36.90
ATOM   1824  CA  ASN B 123      20.581  97.164 -66.654  1.00 38.14
ATOM   1825  C   ASN B 123      20.949  96.369 -65.397  1.00 37.63
ATOM   1826  O   ASN B 123      21.938  96.646 -64.728  1.00 37.21
ATOM   1827  CB  ASN B 123      21.380  98.488 -66.751  1.00 38.59
ATOM   1828  CG  ASN B 123      20.858  99.394 -67.885  1.00 40.63
ATOM   1829  OD1 ASN B 123      20.748  98.955 -69.059  1.00 38.53
ATOM   1830  ND2 ASN B 123      20.479 100.644 -67.525  1.00 41.94
ATOM   1831  N   GLY B 124      20.147  95.340 -65.127  1.00 38.07
ATOM   1832  CA  GLY B 124      20.142  94.651 -63.830  1.00 36.81
ATOM   1833  C   GLY B 124      19.411  95.286 -62.633  1.00 35.66
ATOM   1834  O   GLY B 124      19.419  94.723 -61.534  1.00 36.43
ATOM   1835  N   ASN B 125      18.789  96.454 -62.805  1.00 34.47
ATOM   1836  CA  ASN B 125      17.963  97.006 -61.726  1.00 31.69
ATOM   1837  C   ASN B 125      16.999  95.950 -61.192  1.00 30.35
ATOM   1838  O   ASN B 125      16.532  95.069 -61.946  1.00 29.46
ATOM   1839  CB  ASN B 125      17.196  98.203 -62.233  1.00 31.89
ATOM   1840  CG  ASN B 125      18.067  99.117 -63.058  1.00 30.31
ATOM   1841  OD1 ASN B 125      19.126  99.578 -62.604  1.00 32.28
ATOM   1842  ND2 ASN B 125      17.651  99.357 -64.282  1.00 27.13
ATOM   1843  N   LEU B 126      16.716  96.038 -59.894  1.00 28.25
ATOM   1844  CA  LEU B 126      15.776  95.134 -59.194  1.00 25.70
ATOM   1845  C   LEU B 126      14.576  95.936 -58.726  1.00 25.19
ATOM   1846  O   LEU B 126      14.705  97.120 -58.351  1.00 24.59
ATOM   1847  CB  LEU B 126      16.428  94.546 -57.965  1.00 22.39
ATOM   1848  CG  LEU B 126      17.691  93.714 -58.205  1.00 25.21
ATOM   1849  CD1 LEU B 126      18.909  94.566 -57.829  1.00 21.63
ATOM   1850  CD2 LEU B 126      17.725  92.365 -57.395  1.00 14.86
ATOM   1851  N   GLN B 127      13.438  95.266 -58.681  1.00 24.03
ATOM   1852  CA  GLN B 127      12.162  95.869 -58.291  1.00 23.82
ATOM   1853  C   GLN B 127      11.867  95.662 -56.816  1.00 21.33
ATOM   1854  O   GLN B 127      12.310  94.690 -56.213  1.00 23.19
ATOM   1855  CB  GLN B 127      11.088  95.236 -59.159  1.00 24.51
ATOM   1856  CG  GLN B 127       9.693  95.720 -59.004  1.00 23.80
ATOM   1857  CD  GLN B 127       9.518  97.090 -59.486  1.00 19.47
ATOM   1858  OE1 GLN B 127       9.931  97.432 -60.602  1.00 16.64
ATOM   1859  NE2 GLN B 127       8.884  97.934 -58.638  1.00 18.42
ATOM   1860  N   ASN B 128      11.174  96.586 -56.197  1.00 18.24
ATOM   1861  CA  ASN B 128      10.876  96.414 -54.808  1.00 16.74
ATOM   1862  C   ASN B 128       9.400  96.250 -54.537  1.00 14.86
ATOM   1863  O   ASN B 128       8.579  96.911 -55.087  1.00 13.35
ATOM   1864  CB  ASN B 128      11.460  97.541 -54.027  1.00 17.06
ATOM   1865  CG  ASN B 128      12.946  97.437 -53.892  1.00 22.92
ATOM   1866  OD1 ASN B 128      13.540  96.484 -53.243  1.00 27.41
ATOM   1867  ND2 ASN B 128      13.598  98.411 -54.478  1.00 23.80
ATOM   1868  N   VAL B 129       9.079  95.342 -53.647  1.00 15.83
ATOM   1869  CA  VAL B 129       7.672  94.996 -53.374  1.00 12.49
ATOM   1870  C   VAL B 129       7.427  95.137 -51.888  1.00 12.76
ATOM   1871  O   VAL B 129       8.068  94.511 -51.012  1.00 12.57
ATOM   1872  CB  VAL B 129       7.312  93.651 -53.890  1.00 11.86
ATOM   1873  CG1 VAL B 129       5.859  93.312 -53.630  1.00 13.98
ATOM   1874  CG2 VAL B 129       7.557  93.552 -55.345  1.00 12.23
ATOM   1875  N   LEU B 130       6.505  96.028 -51.600  1.00 12.53
ATOM   1876  CA  LEU B 130       6.116  96.238 -50.255  1.00 14.17
ATOM   1877  C   LEU B 130       5.396  95.053 -49.567  1.00 15.01
ATOM   1878  O   LEU B 130       4.605  94.357 -50.183  1.00 12.94
ATOM   1879  CB  LEU B 130       5.234  97.449 -50.208  1.00 13.01
ATOM   1880  CG  LEU B 130       4.670  97.861 -48.845  1.00 13.37
ATOM   1881  CD1 LEU B 130       5.718  98.086 -47.935  1.00 17.50
ATOM   1882  CD2 LEU B 130       3.956  99.214 -49.054  1.00 14.42
ATOM   1883  N   VAL B 131       5.654  94.887 -48.273  1.00 15.72
ATOM   1884  CA  VAL B 131       4.900  93.944 -47.502  1.00 17.44
ATOM   1885  C   VAL B 131       4.422  94.588 -46.227  1.00 17.65
ATOM   1886  O   VAL B 131       5.232  94.875 -45.390  1.00 18.45
ATOM   1887  CB  VAL B 131       5.732  92.787 -47.129  1.00 17.83
ATOM   1888  CG1 VAL B 131       4.857  91.621 -46.696  1.00 20.26
ATOM   1889  CG2 VAL B 131       6.479  92.304 -48.370  1.00 21.52
ATOM   1890  N   ARG B 132       3.096  94.764 -46.065  1.00 17.10
ATOM   1891  CA  ARG B 132       2.514  95.230 -44.837  1.00 16.49
ATOM   1892  C   ARG B 132       2.250  94.041 -43.951  1.00 16.38
ATOM   1893  O   ARG B 132       1.486  93.128 -44.288  1.00 17.66
ATOM   1894  CB  ARG B 132       1.233  96.053 -45.158  1.00 17.64
ATOM   1895  CG  ARG B 132       1.533  97.451 -45.817  1.00 19.05
ATOM   1896  CD  ARG B 132       0.175  98.171 -46.138  1.00 22.16
ATOM   1897  NE  ARG B 132       0.272  99.465 -46.820  1.00 26.61
ATOM   1898  CZ  ARG B 132       1.090 100.473 -46.477  1.00 28.63
ATOM   1899  NH1 ARG B 132       1.978 100.343 -45.482  1.00 24.59
ATOM   1900  NH2 ARG B 132       1.025 101.621 -47.167  1.00 26.04
ATOM   1901  N   VAL B 133       2.899  93.957 -42.793  1.00 17.40
ATOM   1902  CA  VAL B 133       2.578  92.864 -41.856  1.00 17.03
ATOM   1903  C   VAL B 133       1.515  93.263 -40.800  1.00 18.71
ATOM   1904  O   VAL B 133       1.548  94.406 -40.251  1.00 20.36
ATOM   1905  CB  VAL B 133       3.822  92.297 -41.244  1.00 16.70
ATOM   1906  CG1 VAL B 133       3.556  90.928 -40.665  1.00 16.96
ATOM   1907  CG2 VAL B 133       4.932  92.191 -42.356  1.00 16.40
ATOM   1908  N   TYR B 134       0.524  92.392 -40.573  1.00 15.25
ATOM   1909  CA  TYR B 134      -0.435  92.626 -39.494  1.00 14.39
ATOM   1910  C   TYR B 134      -0.391  91.550 -38.377  1.00 14.65
ATOM   1911  O   TYR B 134      -0.665  90.379 -38.641  1.00 16.82
ATOM   1912  CB  TYR B 134      -1.813  92.708 -40.093  1.00 12.80
ATOM   1913  CG  TYR B 134      -1.924  93.732 -41.220  1.00 11.35
ATOM   1914  CD1 TYR B 134      -1.179  93.601 -42.391  1.00 13.80
ATOM   1915  CD2 TYR B 134      -2.725  94.806 -41.095  1.00  9.74
ATOM   1916  CE1 TYR B 134      -1.221  94.530 -43.377  1.00 12.88
ATOM   1917  CE2 TYR B 134      -2.824  95.757 -42.071  1.00 12.15
ATOM   1918  CZ  TYR B 134      -2.126  95.645 -43.251  1.00 15.95
ATOM   1919  OH  TYR B 134      -2.229  96.681 -44.278  1.00 10.49
ATOM   1920  N   GLU B 135      -0.109  91.959 -37.145  1.00 12.49
ATOM   1921  CA  GLU B 135      -0.117  91.142 -35.939  1.00 11.29
ATOM   1922  C   GLU B 135      -1.349  91.598 -35.210  1.00 11.63
ATOM   1923  O   GLU B 135      -1.486  92.793 -34.824  1.00 11.38
ATOM   1924  CB  GLU B 135       1.158  91.467 -35.102  1.00  6.45
ATOM   1925  CG  GLU B 135       2.327  91.503 -35.961  1.00  9.85
ATOM   1926  CD  GLU B 135       3.631  91.477 -35.138  1.00 15.83
ATOM   1927  OE1 GLU B 135       3.927  90.356 -34.611  1.00 17.06
ATOM   1928  OE2 GLU B 135       4.251  92.551 -34.974  1.00  8.29
ATOM   1929  N   ASN B 136      -2.278  90.671 -35.064  1.00 13.39
ATOM   1930  CA  ASN B 136      -3.520  90.942 -34.395  1.00 14.33
ATOM   1931  C   ASN B 136      -4.244  92.175 -34.980  1.00 15.19
ATOM   1932  O   ASN B 136      -4.798  92.970 -34.222  1.00 15.12
ATOM   1933  CB  ASN B 136      -3.238  91.057 -32.887  1.00 13.00
ATOM   1934  CG  ASN B 136      -2.793  89.706 -32.317  1.00 15.23
ATOM   1935  OD1 ASN B 136      -3.528  88.730 -32.438  1.00 16.81
ATOM   1936  ND2 ASN B 136      -1.577  89.630 -31.783  1.00  8.97
ATOM   1937  N   LYS B 137      -4.207  92.305 -36.305  1.00 15.54
ATOM   1938  CA  LYS B 137      -4.813  93.461 -36.993  1.00 16.83
ATOM   1939  C   LYS B 137      -4.002  94.796 -36.861  1.00 17.35
ATOM   1940  O   LYS B 137      -4.584  95.859 -36.880  1.00 17.81
ATOM   1941  CB  LYS B 137      -6.211  93.705 -36.484  1.00 16.90
ATOM   1942  CG  LYS B 137      -7.126  92.573 -36.869  1.00 17.32
ATOM   1943  CD  LYS B 137      -8.365  92.709 -36.102  1.00 16.98
ATOM   1944  CE  LYS B 137      -9.354  91.606 -36.404  1.00 13.15
ATOM   1945  NZ  LYS B 137      -9.922  91.819 -37.745  1.00 15.50
ATOM   1946  N   ARG B 138      -2.684  94.771 -36.745  1.00 16.45
ATOM   1947  CA  ARG B 138      -2.027  96.073 -36.683  1.00 16.54
ATOM   1948  C   ARG B 138      -0.818  96.168 -37.593  1.00 15.22
ATOM   1949  O   ARG B 138      -0.110  95.183 -37.825  1.00 11.80
ATOM   1950  CB  ARG B 138      -1.701  96.347 -35.235  1.00 18.53
ATOM   1951  CG  ARG B 138      -2.889  96.118 -34.246  1.00 17.08
ATOM   1952  CD  ARG B 138      -2.777  97.008 -32.987  1.00 23.06
ATOM   1953  NE  ARG B 138      -3.823  96.655 -32.002  1.00 22.86
ATOM   1954  CZ  ARG B 138      -4.245  97.403 -31.003  1.00 20.73
ATOM   1955  NH1 ARG B 138      -3.748  98.619 -30.789  1.00 28.49
ATOM   1956  NH2 ARG B 138      -5.168  96.938 -30.191  1.00 21.56
ATOM   1957  N   ASN B 139      -0.613  97.325 -38.231  1.00 14.96
ATOM   1958  CA  ASN B 139       0.519  97.337 -39.218  1.00 12.56
ATOM   1959  C   ASN B 139       1.790  97.520 -38.443  1.00 12.18
ATOM   1960  O   ASN B 139       2.277  98.658 -38.204  1.00 12.06
ATOM   1961  CB  ASN B 139       0.269  98.289 -40.419  1.00 12.40
ATOM   1962  CG  ASN B 139       1.417  98.285 -41.448  1.00 12.13
ATOM   1963  OD1 ASN B 139       1.525  99.198 -42.291  1.00  5.69
ATOM   1964  ND2 ASN B 139       2.212  97.187 -41.462  1.00  8.79
ATOM   1965  N   THR B 140       2.331  96.396 -37.975  1.00  9.99
ATOM   1966  CA  THR B 140       3.434  96.455 -37.026  1.00 10.22
ATOM   1967  C   THR B 140       4.735  96.731 -37.764  1.00 10.78
ATOM   1968  O   THR B 140       5.424  97.718 -37.508  1.00 10.37
ATOM   1969  CB  THR B 140       3.592  95.116 -36.234  1.00 11.20
ATOM   1970  OG1 THR B 140       3.922  94.053 -37.120  1.00 10.26
ATOM   1971  CG2 THR B 140       2.394  94.746 -35.594  1.00  2.00
ATOM   1972  N   ILE B 141       4.992  95.880 -38.747  1.00 11.81
ATOM   1973  CA  ILE B 141       6.255  95.790 -39.452  1.00 10.72
ATOM   1974  C   ILE B 141       5.875  95.830 -40.951  1.00 12.42
ATOM   1975  O   ILE B 141       4.781  95.385 -41.355  1.00  7.30
ATOM   1976  CB  ILE B 141       7.065  94.510 -39.006  1.00 11.91
ATOM   1977  CG1 ILE B 141       8.147  94.211 -40.039  1.00  8.86
ATOM   1978  CG2 ILE B 141       6.128  93.292 -38.739  1.00 12.28
ATOM   1979  CD1 ILE B 141       9.167  95.493 -40.257  1.00  3.62
ATOM   1980  N   SER B 142       6.709  96.523 -41.742  1.00 14.48
ATOM   1981  CA  SER B 142       6.628  96.591 -43.249  1.00 13.70
ATOM   1982  C   SER B 142       8.025  96.659 -43.904  1.00 13.12
ATOM   1983  O   SER B 142       8.828  97.511 -43.611  1.00 11.14
ATOM   1984  CB  SER B 142       5.924  97.861 -43.653  1.00 15.53
ATOM   1985  OG  SER B 142       4.702  98.005 -42.923  1.00 14.03
ATOM   1986  N   PHE B 143       8.274  95.801 -44.875  1.00 11.99
ATOM   1987  CA  PHE B 143       9.587  95.706 -45.468  1.00 11.37
ATOM   1988  C   PHE B 143       9.326  95.531 -46.924  1.00 11.45
ATOM   1989  O   PHE B 143       8.239  95.761 -47.315  1.00 12.79
ATOM   1990  CB  PHE B 143      10.301  94.526 -44.890  1.00 10.71
ATOM   1991  CG  PHE B 143       9.560  93.219 -45.002  1.00  9.49
ATOM   1992  CD1 PHE B 143      10.106  92.186 -45.648  1.00 18.65
ATOM   1993  CD2 PHE B 143       8.331  93.022 -44.396  1.00 19.43
ATOM   1994  CE1 PHE B 143       9.481  90.991 -45.773  1.00 12.40
ATOM   1995  CE2 PHE B 143       7.697  91.820 -44.463  1.00 19.98
ATOM   1996  CZ  PHE B 143       8.272  90.796 -45.184  1.00 14.91
ATOM   1997  N   GLU B 144      10.294  95.092 -47.693  1.00 13.00
ATOM   1998  CA  GLU B 144      10.170  94.924 -49.116  1.00 14.00
ATOM   1999  C   GLU B 144      10.976  93.757 -49.637  1.00 15.25
ATOM   2000  O   GLU B 144      11.881  93.239 -49.002  1.00 15.56
ATOM   2001  CB  GLU B 144      10.675  96.141 -49.862  1.00 15.88
ATOM   2002  CG  GLU B 144       9.759  97.382 -49.850  1.00 16.61
ATOM   2003  CD  GLU B 144      10.582  98.650 -50.076  1.00 25.88
ATOM   2004  OE1 GLU B 144      10.004  99.734 -50.402  1.00 24.45
ATOM   2005  OE2 GLU B 144      11.836  98.527 -49.921  1.00 27.33
ATOM   2006  N   VAL B 145      10.655  93.342 -50.842  1.00 16.09
ATOM   2007  CA  VAL B 145      11.274  92.161 -51.363  1.00 16.73
ATOM   2008  C   VAL B 145      11.813  92.517 -52.690  1.00 16.25
ATOM   2009  O   VAL B 145      11.346  93.406 -53.306  1.00 17.89
ATOM   2010  CB  VAL B 145      10.275  91.022 -51.474  1.00 14.60
ATOM   2011  CG1 VAL B 145       9.897  90.667 -50.134  1.00 16.65
ATOM   2012  CG2 VAL B 145       8.988  91.435 -52.283  1.00 15.99
ATOM   2013  N   GLN B 146      12.814  91.803 -53.152  1.00 17.11
ATOM   2014  CA  GLN B 146      13.408  92.204 -54.403  1.00 15.52
ATOM   2015  C   GLN B 146      13.434  91.066 -55.360  1.00 14.76
ATOM   2016  O   GLN B 146      13.734  89.925 -54.991  1.00 12.62
ATOM   2017  CB  GLN B 146      14.852  92.695 -54.164  1.00 15.29
ATOM   2018  CG  GLN B 146      14.915  93.883 -53.203  1.00 15.56
ATOM   2019  CD  GLN B 146      16.273  94.492 -53.179  1.00 18.50
ATOM   2020  OE1 GLN B 146      17.342  93.781 -53.079  1.00 18.79
ATOM   2021  NE2 GLN B 146      16.291  95.800 -53.332  1.00 18.71
ATOM   2022  N   THR B 147      13.218  91.384 -56.629  1.00 14.53
ATOM   2023  CA  THR B 147      13.246  90.289 -57.663  1.00 12.61
ATOM   2024  C   THR B 147      13.786  90.853 -59.005  1.00 11.23
ATOM   2025  O   THR B 147      13.910  92.079 -59.168  1.00 10.99
ATOM   2026  CB  THR B 147      11.877  89.794 -57.949  1.00 11.13
ATOM   2027  OG1 THR B 147      11.982  88.639 -58.863  1.00 11.61
ATOM   2028  CG2 THR B 147      11.081  90.946 -58.616  1.00  5.83
ATOM   2029  N   ASP B 148      14.115  89.978 -59.937  1.00 10.18
ATOM   2030  CA  ASP B 148      14.563  90.373 -61.257  1.00 10.48
ATOM   2031  C   ASP B 148      13.474  90.219 -62.298  1.00 11.60
ATOM   2032  O   ASP B 148      13.622  90.804 -63.393  1.00 12.41
ATOM   2033  CB  ASP B 148      15.841  89.592 -61.685  1.00  9.84
ATOM   2034  CG  ASP B 148      15.558  88.075 -61.807  1.00 11.48
ATOM   2035  OD1 ASP B 148      16.421  87.265 -62.192  1.00  4.81
ATOM   2036  OD2 ASP B 148      14.466  87.683 -61.423  1.00  7.10
ATOM   2037  N   LYS B 149      12.332  89.534 -61.997  1.00 11.88
ATOM   2038  CA  LYS B 149      11.258  89.381 -62.974  1.00 10.08
ATOM   2039  C   LYS B 149      10.382  90.661 -63.193  1.00 11.09
ATOM   2040  O   LYS B 149      10.161  91.470 -62.235  1.00 12.10
ATOM   2041  CB  LYS B 149      10.389  88.174 -62.594  1.00 11.55
ATOM   2042  CG  LYS B 149      11.188  87.045 -61.819  1.00  7.50
ATOM   2043  CD  LYS B 149      12.368  86.532 -62.637  1.00  2.00
ATOM   2044  CE  LYS B 149      12.881  85.112 -62.243  1.00  3.24
ATOM   2045  NZ  LYS B 149      13.152  84.927 -60.827  1.00  2.00
ATOM   2046  N   LYS B 150       9.764  90.813 -64.379  1.00 10.58
ATOM   2047  CA  LYS B 150       8.923  92.106 -64.677  1.00  9.53
ATOM   2048  C   LYS B 150       7.539  91.632 -64.457  1.00 11.23
ATOM   2049  O   LYS B 150       6.500  92.418 -64.529  1.00 10.14
ATOM   2050  CB  LYS B 150       9.052  92.532 -66.136  1.00  4.52
ATOM   2051  CG  LYS B 150       8.851  94.008 -66.451  1.00 13.20
ATOM   2052  CD  LYS B 150       9.400  94.300 -67.839  1.00  9.55
ATOM   2053  CE  LYS B 150      10.997  94.288 -67.822  1.00  4.98
ATOM   2054  NZ  LYS B 150      11.424  94.556 -69.223  1.00  4.30
ATOM   2055  N   SER B 151       7.503  90.300 -64.323  1.00  9.23
ATOM   2056  CA  SER B 151       6.316  89.645 -63.928  1.00 10.30
ATOM   2057  C   SER B 151       6.768  88.289 -63.338  1.00 11.72
ATOM   2058  O   SER B 151       7.337  87.448 -64.084  1.00  8.10
ATOM   2059  CB  SER B 151       5.377  89.450 -65.116  1.00 10.96
ATOM   2060  OG  SER B 151       4.585  88.212 -64.909  1.00 14.65
ATOM   2061  N   VAL B 152       6.455  88.057 -62.037  1.00 11.10
ATOM   2062  CA  VAL B 152       7.048  86.941 -61.284  1.00  9.74
ATOM   2063  C   VAL B 152       6.031  86.059 -60.641  1.00 10.99
ATOM   2064  O   VAL B 152       4.885  86.505 -60.445  1.00  6.61
ATOM   2065  CB  VAL B 152       7.801  87.481 -60.116  1.00  9.35
ATOM   2066  CG1 VAL B 152       6.878  88.376 -59.353  1.00 11.35
ATOM   2067  CG2 VAL B 152       8.253  86.384 -59.300  1.00 13.03
ATOM   2068  N   THR B 153       6.510  84.848 -60.248  1.00 11.20
ATOM   2069  CA  THR B 153       5.698  83.768 -59.709  1.00 11.26
ATOM   2070  C   THR B 153       5.340  84.185 -58.299  1.00 12.21
ATOM   2071  O   THR B 153       6.251  84.416 -57.503  1.00 12.96
ATOM   2072  CB  THR B 153       6.433  82.432 -59.655  1.00 11.29
ATOM   2073  OG1 THR B 153       7.814  82.597 -59.311  1.00 11.34
ATOM   2074  CG2 THR B 153       6.466  81.805 -60.952  1.00 12.78
ATOM   2075  N   ALA B 154       4.019  84.290 -57.955  1.00 12.08
ATOM   2076  CA  ALA B 154       3.649  84.533 -56.565  1.00  9.26
ATOM   2077  C   ALA B 154       4.533  83.702 -55.618  1.00 11.16
ATOM   2078  O   ALA B 154       4.940  84.181 -54.553  1.00 12.36
ATOM   2079  CB  ALA B 154       2.205  84.209 -56.320  1.00  9.88
ATOM   2080  N   GLN B 155       4.785  82.440 -55.964  1.00 12.24
ATOM   2081  CA  GLN B 155       5.619  81.588 -55.156  1.00 11.20
ATOM   2082  C   GLN B 155       6.899  82.299 -54.858  1.00 11.78
ATOM   2083  O   GLN B 155       7.191  82.525 -53.686  1.00 12.77
ATOM   2084  CB  GLN B 155       5.908  80.251 -55.863  1.00 11.22
ATOM   2085  CG  GLN B 155       6.855  79.389 -55.121  1.00  9.44
ATOM   2086  CD  GLN B 155       6.851  78.024 -55.598  1.00 12.25
ATOM   2087  OE1 GLN B 155       7.563  77.137 -55.072  1.00 14.74
ATOM   2088  NE2 GLN B 155       6.021  77.785 -56.576  1.00 12.35
ATOM   2089  N   GLU B 156       7.640  82.714 -55.879  1.00 12.68
ATOM   2090  CA  GLU B 156       8.891  83.439 -55.654  1.00 11.50
ATOM   2091  C   GLU B 156       8.637  84.443 -54.618  1.00 10.38
ATOM   2092  O   GLU B 156       9.384  84.522 -53.634  1.00 12.43
ATOM   2093  CB  GLU B 156       9.405  84.209 -56.862  1.00 11.73
ATOM   2094  CG  GLU B 156      10.798  84.824 -56.532  1.00 10.22
ATOM   2095  CD  GLU B 156      11.506  85.410 -57.710  1.00 10.70
ATOM   2096  OE1 GLU B 156      12.296  86.337 -57.499  1.00 10.68
ATOM   2097  OE2 GLU B 156      11.198  85.056 -58.862  1.00 10.69
ATOM   2098  N   LEU B 157       7.605  85.247 -54.803  1.00  9.38
ATOM   2099  CA  LEU B 157       7.452  86.402 -53.926  1.00  6.92
ATOM   2100  C   LEU B 157       7.151  85.981 -52.523  1.00  9.33
ATOM   2101  O   LEU B 157       7.821  86.443 -51.555  1.00  7.71
ATOM   2102  CB  LEU B 157       6.296  87.275 -54.392  1.00  7.19
ATOM   2103  CG  LEU B 157       6.432  88.273 -55.528  1.00  4.70
ATOM   2104  CD1 LEU B 157       5.233  89.109 -55.484  1.00  9.57
ATOM   2105  CD2 LEU B 157       7.750  89.060 -55.364  1.00  2.23
ATOM   2106  N   ASP B 158       6.125  85.108 -52.393  1.00  6.81
ATOM   2107  CA  ASP B 158       5.819  84.524 -51.116  1.00  9.26
ATOM   2108  C   ASP B 158       7.054  84.005 -50.379  1.00  9.19
ATOM   2109  O   ASP B 158       7.252  84.374 -49.231  1.00  8.82
ATOM   2110  CB  ASP B 158       4.784  83.418 -51.365  1.00 11.98
ATOM   2111  CG  ASP B 158       4.422  82.679 -50.145  1.00 16.30
ATOM   2112  OD1 ASP B 158       3.748  83.262 -49.219  1.00 14.32
ATOM   2113  OD2 ASP B 158       4.880  81.525 -50.123  1.00 19.46
ATOM   2114  N   ILE B 159       7.863  83.122 -51.007  1.00  9.30
ATOM   2115  CA  ILE B 159       8.998  82.477 -50.346  1.00  8.37
ATOM   2116  C   ILE B 159       9.803  83.588 -49.644  1.00 10.33
ATOM   2117  O   ILE B 159       9.997  83.623 -48.443  1.00  7.57
ATOM   2118  CB  ILE B 159       9.929  81.735 -51.351  1.00 11.06
ATOM   2119  CG1 ILE B 159       9.363  80.388 -51.909  1.00  7.96
ATOM   2120  CG2 ILE B 159      11.177  81.314 -50.633  1.00  9.39
ATOM   2121  CD1 ILE B 159       7.844  80.183 -51.454  1.00 17.04
ATOM   2122  N   LYS B 160      10.165  84.572 -50.452  1.00 11.82
ATOM   2123  CA  LYS B 160      11.039  85.659 -50.114  1.00 11.64
ATOM   2124  C   LYS B 160      10.470  86.359 -48.872  1.00 11.98
ATOM   2125  O   LYS B 160      11.216  86.627 -47.920  1.00 12.74
ATOM   2126  CB  LYS B 160      11.194  86.610 -51.340  1.00 12.67
ATOM   2127  CG  LYS B 160      12.181  86.122 -52.431  1.00  9.61
ATOM   2128  CD  LYS B 160      12.580  87.203 -53.487  1.00 11.23
ATOM   2129  CE  LYS B 160      13.616  86.635 -54.541  1.00  9.99
ATOM   2130  NZ  LYS B 160      14.115  87.376 -55.820  1.00  5.35
ATOM   2131  N   ALA B 161       9.146  86.534 -48.838  1.00 12.01
ATOM   2132  CA  ALA B 161       8.426  87.120 -47.715  1.00 11.13
ATOM   2133  C   ALA B 161       8.716  86.295 -46.441  1.00 11.55
ATOM   2134  O   ALA B 161       9.305  86.799 -45.452  1.00  9.66
ATOM   2135  CB  ALA B 161       6.886  87.065 -48.056  1.00 12.32
ATOM   2136  N   ARG B 162       8.197  85.055 -46.442  1.00 11.54
ATOM   2137  CA  ARG B 162       8.422  84.079 -45.400  1.00  9.79
ATOM   2138  C   ARG B 162       9.892  83.993 -44.978  1.00  9.42
ATOM   2139  O   ARG B 162      10.168  84.068 -43.811  1.00 10.61
ATOM   2140  CB  ARG B 162       7.896  82.740 -45.885  1.00 10.88
ATOM   2141  CG  ARG B 162       6.352  82.681 -45.804  1.00 13.06
ATOM   2142  CD  ARG B 162       5.850  81.273 -46.220  1.00 10.66
ATOM   2143  NE  ARG B 162       4.394  81.194 -46.520  1.00 10.75
ATOM   2144  CZ  ARG B 162       3.785  80.040 -46.788  1.00  9.56
ATOM   2145  NH1 ARG B 162       4.494  78.951 -46.798  1.00  8.33
ATOM   2146  NH2 ARG B 162       2.508  79.945 -47.064  1.00 10.35
ATOM   2147  N   ASN B 163      10.835  83.795 -45.876  1.00 10.21
ATOM   2148  CA  ASN B 163      12.235  83.716 -45.525  1.00 12.67
ATOM   2149  C   ASN B 163      12.604  84.864 -44.587  1.00 15.05
ATOM   2150  O   ASN B 163      13.316  84.622 -43.558  1.00 17.57
ATOM   2151  CB  ASN B 163      13.070  83.786 -46.788  1.00 14.36
ATOM   2152  CG  ASN B 163      14.512  83.980 -46.551  1.00 14.15
ATOM   2153  OD1 ASN B 163      15.211  83.055 -46.280  1.00 11.96
ATOM   2154  ND2 ASN B 163      15.004  85.206 -46.822  1.00 24.48
ATOM   2155  N   PHE B 164      12.080  86.093 -44.849  1.00 15.44
ATOM   2156  CA  PHE B 164      12.399  87.286 -44.019  1.00 15.88
ATOM   2157  C   PHE B 164      11.749  87.102 -42.681  1.00 16.37
ATOM   2158  O   PHE B 164      12.455  87.126 -41.657  1.00 16.67
ATOM   2159  CB  PHE B 164      11.861  88.609 -44.588  1.00 17.00
ATOM   2160  CG  PHE B 164      12.462  89.877 -43.968  1.00 14.90
ATOM   2161  CD1 PHE B 164      13.725  90.325 -44.338  1.00 13.56
ATOM   2162  CD2 PHE B 164      11.668  90.727 -43.203  1.00 15.63
ATOM   2163  CE1 PHE B 164      14.224  91.559 -43.866  1.00 13.87
ATOM   2164  CE2 PHE B 164      12.157  91.868 -42.730  1.00 19.60
ATOM   2165  CZ  PHE B 164      13.479  92.294 -43.064  1.00 18.93
ATOM   2166  N   LEU B 165      10.410  86.953 -42.669  1.00 15.37
ATOM   2167  CA  LEU B 165       9.702  86.666 -41.401  1.00 13.55
ATOM   2168  C   LEU B 165      10.424  85.562 -40.539  1.00 13.06
ATOM   2169  O   LEU B 165      10.520  85.713 -39.307  1.00 11.08
ATOM   2170  CB  LEU B 165       8.245  86.377 -41.674  1.00 13.17
ATOM   2171  CG  LEU B 165       7.361  87.729 -41.740  1.00 13.02
ATOM   2172  CD1 LEU B 165       8.178  89.013 -41.878  1.00 11.78
ATOM   2173  CD2 LEU B 165       6.474  87.628 -42.851  1.00  6.61
ATOM   2174  N   ILE B 166      10.884  84.469 -41.152  1.00 11.42
ATOM   2175  CA  ILE B 166      11.692  83.493 -40.416  1.00 11.67
ATOM   2176  C   ILE B 166      12.885  84.313 -39.938  1.00 10.13
ATOM   2177  O   ILE B 166      13.040  84.607 -38.744  1.00 10.32
ATOM   2178  CB  ILE B 166      12.252  82.345 -41.291  1.00 11.20
ATOM   2179  CG1 ILE B 166      11.249  81.284 -41.675  1.00 11.84
ATOM   2180  CG2 ILE B 166      13.248  81.641 -40.507  1.00 11.60
ATOM   2181  CD1 ILE B 166       9.884  81.831 -42.041  1.00 22.91
ATOM   2182  N   ASN B 167      13.770  84.714 -40.837  1.00 11.87
ATOM   2183  CA  ASN B 167      14.978  85.474 -40.340  1.00 14.05
ATOM   2184  C   ASN B 167      14.829  86.695 -39.391  1.00 12.90
ATOM   2185  O   ASN B 167      15.831  87.273 -38.896  1.00 13.51
ATOM   2186  CB  ASN B 167      15.834  85.843 -41.520  1.00 14.78
ATOM   2187  CG  ASN B 167      16.375  84.558 -42.230  1.00 19.05
ATOM   2188  OD1 ASN B 167      15.645  83.560 -42.347  1.00 14.46
ATOM   2189  ND2 ASN B 167      17.676  84.566 -42.610  1.00 19.30
ATOM   2190  N   LYS B 168      13.615  87.148 -39.125  1.00 11.26
ATOM   2191  CA  LYS B 168      13.500  88.395 -38.258  1.00 11.77
ATOM   2192  C   LYS B 168      12.337  88.450 -37.256  1.00 12.15
ATOM   2193  O   LYS B 168      12.322  89.311 -36.316  1.00 12.84
ATOM   2194  CB  LYS B 168      13.505  89.680 -39.095  1.00  9.20
ATOM   2195  CG  LYS B 168      14.681  89.812 -40.078  1.00 10.37
ATOM   2196  CD  LYS B 168      15.794  90.757 -39.535  1.00  8.01
ATOM   2197  CE  LYS B 168      17.213  90.346 -40.138  1.00 15.79
ATOM   2198  NZ  LYS B 168      17.281  88.821 -40.091  1.00 16.18
ATOM   2199  N   LYS B 169      11.339  87.613 -37.467  1.00 13.05
ATOM   2200  CA  LYS B 169      10.094  87.567 -36.613  1.00 12.54
ATOM   2201  C   LYS B 169       9.630  86.120 -36.246  1.00 13.48
ATOM   2202  O   LYS B 169       8.418  85.868 -35.965  1.00 10.89
ATOM   2203  CB  LYS B 169       8.916  88.327 -37.262  1.00 13.42
ATOM   2204  CG  LYS B 169       8.749  89.804 -36.680  1.00 17.03
ATOM   2205  CD  LYS B 169       7.947  89.896 -35.456  1.00 14.89
ATOM   2206  CE  LYS B 169       7.454  91.335 -35.199  1.00 16.37
ATOM   2207  NZ  LYS B 169       6.425  91.315 -34.085  1.00 15.63
ATOM   2208  N   ASN B 170      10.593  85.201 -36.191  1.00 12.08
ATOM   2209  CA  ASN B 170      10.322  83.812 -35.828  1.00 12.48
ATOM   2210  C   ASN B 170       9.004  83.244 -36.324  1.00 12.71
ATOM   2211  O   ASN B 170       8.240  82.589 -35.537  1.00 14.21
ATOM   2212  CB  ASN B 170      10.468  83.548 -34.334  1.00 11.37
ATOM   2213  CG  ASN B 170      11.920  83.693 -33.827  1.00 17.78
ATOM   2214  OD1 ASN B 170      12.516  84.844 -33.851  1.00 15.93
ATOM   2215  ND2 ASN B 170      12.530  82.540 -33.361  1.00 15.97
ATOM   2216  N   LEU B 171       8.770  83.362 -37.618  1.00 12.00
ATOM   2217  CA  LEU B 171       7.446  82.934 -38.152  1.00 13.94
ATOM   2218  C   LEU B 171       7.249  81.443 -37.909  1.00 12.54
ATOM   2219  O   LEU B 171       6.137  81.008 -37.725  1.00 12.15
ATOM   2220  CB  LEU B 171       7.261  83.317 -39.637  1.00 13.40
ATOM   2221  CG  LEU B 171       6.274  82.567 -40.512  1.00 14.34
ATOM   2222  CD1 LEU B 171       4.844  83.009 -40.145  1.00  7.49
ATOM   2223  CD2 LEU B 171       6.735  82.999 -41.949  1.00  8.00
ATOM   2224  N   TYR B 172       8.341  80.728 -37.855  1.00 10.81
ATOM   2225  CA  TYR B 172       8.365  79.256 -37.737  1.00 11.68
ATOM   2226  C   TYR B 172       9.645  79.034 -36.906  1.00 12.20
ATOM   2227  O   TYR B 172      10.677  79.740 -37.096  1.00 10.17
ATOM   2228  CB  TYR B 172       8.570  78.541 -39.088  1.00 11.85
ATOM   2229  CG  TYR B 172       7.468  78.762 -40.131  1.00  9.76
ATOM   2230  CD1 TYR B 172       7.741  79.149 -41.451  1.00  7.06
ATOM   2231  CD2 TYR B 172       6.145  78.621 -39.779  1.00 10.34
ATOM   2232  CE1 TYR B 172       6.648  79.451 -42.338  1.00  9.66
ATOM   2233  CE2 TYR B 172       5.073  78.813 -40.713  1.00  4.52
ATOM   2234  CZ  TYR B 172       5.331  79.239 -41.922  1.00  7.82
ATOM   2235  OH  TYR B 172       4.253  79.404 -42.710  1.00  8.43
ATOM   2236  N   GLU B 173       9.500  78.171 -35.925  1.00 10.42
ATOM   2237  CA  GLU B 173      10.576  77.696 -35.098  1.00 10.75
ATOM   2238  C   GLU B 173      10.569  76.151 -35.102  1.00  8.85
ATOM   2239  O   GLU B 173       9.491  75.561 -35.281  1.00  8.01
ATOM   2240  CB  GLU B 173      10.446  78.222 -33.678  1.00 10.73
ATOM   2241  CG  GLU B 173      11.265  79.448 -33.450  1.00 12.19
ATOM   2242  CD  GLU B 173      11.168  80.039 -32.022  1.00 15.69
ATOM   2243  OE1 GLU B 173      10.013  80.268 -31.509  1.00 15.58
ATOM   2244  OE2 GLU B 173      12.274  80.389 -31.525  1.00 12.51
ATOM   2245  N   PHE B 174      11.758  75.549 -34.925  1.00  6.15
ATOM   2246  CA  PHE B 174      11.932  74.151 -34.929  1.00  8.07
ATOM   2247  C   PHE B 174      10.870  73.308 -34.207  1.00  9.68
ATOM   2248  O   PHE B 174      10.626  72.209 -34.646  1.00  9.78
ATOM   2249  CB  PHE B 174      13.303  73.732 -34.570  1.00  7.52
ATOM   2250  CG  PHE B 174      13.510  72.266 -34.568  1.00  5.79
ATOM   2251  CD1 PHE B 174      14.065  71.623 -35.663  1.00 14.25
ATOM   2252  CD2 PHE B 174      13.263  71.536 -33.446  1.00  9.44
ATOM   2253  CE1 PHE B 174      14.391  70.235 -35.653  1.00 10.77
ATOM   2254  CE2 PHE B 174      13.485  70.101 -33.390  1.00 10.57
ATOM   2255  CZ  PHE B 174      14.040  69.450 -34.497  1.00 12.18
ATOM   2256  N   ASN B 175      10.204  73.806 -33.170  1.00 12.47
ATOM   2257  CA  ASN B 175       9.083  73.005 -32.528  1.00 13.00
ATOM   2258  C   ASN B 175       7.697  73.473 -32.777  1.00 12.75
ATOM   2259  O   ASN B 175       6.675  72.740 -32.556  1.00 16.51
ATOM   2260  CB  ASN B 175       9.316  72.909 -31.030  1.00 12.93
ATOM   2261  CG  ASN B 175      10.835  72.902 -30.648  1.00 19.64
ATOM   2262  OD1 ASN B 175      11.562  73.894 -30.895  1.00 24.36
ATOM   2263  ND2 ASN B 175      11.309  71.787 -30.048  1.00 18.24
ATOM   2264  N   SER B 176       7.597  74.751 -33.083  1.00 12.74
ATOM   2265  CA  SER B 176       6.358  75.376 -33.393  1.00 12.21
ATOM   2266  C   SER B 176       6.504  76.858 -33.733  1.00 12.97
ATOM   2267  O   SER B 176       7.577  77.313 -34.215  1.00 13.11
ATOM   2268  CB  SER B 176       5.358  75.164 -32.278  1.00 14.14
ATOM   2269  OG  SER B 176       4.137  75.662 -32.658  1.00  7.94
ATOM   2270  N   SER B 177       5.427  77.594 -33.519  1.00 10.45
ATOM   2271  CA  SER B 177       5.393  79.010 -33.915  1.00 12.73
ATOM   2272  C   SER B 177       4.541  79.885 -32.965  1.00 12.63
ATOM   2273  O   SER B 177       3.448  79.464 -32.507  1.00 11.87
ATOM   2274  CB  SER B 177       4.833  79.114 -35.350  1.00 12.31
ATOM   2275  OG  SER B 177       5.052  80.370 -35.936  1.00 11.70
ATOM   2276  N   PRO B 178       5.080  81.076 -32.644  1.00 12.02
ATOM   2277  CA  PRO B 178       4.547  82.091 -31.802  1.00  9.04
ATOM   2278  C   PRO B 178       3.199  82.494 -32.270  1.00  8.64
ATOM   2279  O   PRO B 178       2.496  83.197 -31.526  1.00 10.15
ATOM   2280  CB  PRO B 178       5.504  83.279 -32.044  1.00  6.82
ATOM   2281  CG  PRO B 178       6.732  82.693 -32.542  1.00 10.75
ATOM   2282  CD  PRO B 178       6.362  81.497 -33.266  1.00 10.69
ATOM   2283  N   TYR B 179       2.828  82.127 -33.485  1.00  8.35
ATOM   2284  CA  TYR B 179       1.535  82.531 -34.083  1.00  7.55
ATOM   2285  C   TYR B 179       0.545  81.338 -34.147  1.00  9.22
ATOM   2286  O   TYR B 179       0.978  80.119 -34.091  1.00  7.45
ATOM   2287  CB  TYR B 179       1.749  83.185 -35.439  1.00  7.94
ATOM   2288  CG  TYR B 179       2.835  84.308 -35.407  1.00  9.55
ATOM   2289  CD1 TYR B 179       4.125  84.015 -35.696  1.00  4.63
ATOM   2290  CD2 TYR B 179       2.489  85.691 -35.052  1.00  5.68
ATOM   2291  CE1 TYR B 179       5.148  85.040 -35.661  1.00  9.84
ATOM   2292  CE2 TYR B 179       3.437  86.672 -35.060  1.00 10.92
ATOM   2293  CZ  TYR B 179       4.731  86.347 -35.363  1.00  7.69
ATOM   2294  OH  TYR B 179       5.601  87.296 -35.362  1.00 11.82
ATOM   2295  N   GLU B 180      -0.758  81.659 -34.154  1.00  7.58
ATOM   2296  CA  GLU B 180      -1.771  80.611 -34.103  1.00  8.20
ATOM   2297  C   GLU B 180      -2.225  80.392 -35.524  1.00  9.69
ATOM   2298  O   GLU B 180      -2.495  79.213 -35.937  1.00 12.55
ATOM   2299  CB  GLU B 180      -2.968  81.073 -33.226  1.00  9.88
ATOM   2300  CG  GLU B 180      -4.214  80.055 -33.074  1.00  7.74
ATOM   2301  CD  GLU B 180      -3.815  78.698 -32.652  1.00 14.00
ATOM   2302  OE1 GLU B 180      -4.718  77.859 -32.381  1.00 13.19
ATOM   2303  OE2 GLU B 180      -2.594  78.441 -32.539  1.00 14.28
ATOM   2304  N   THR B 181      -2.340  81.495 -36.291  1.00  7.35
ATOM   2305  CA  THR B 181      -2.758  81.443 -37.668  1.00  5.80
ATOM   2306  C   THR B 181      -2.063  82.479 -38.501  1.00  8.40
ATOM   2307  O   THR B 181      -1.553  83.505 -37.992  1.00  8.91
ATOM   2308  CB  THR B 181      -4.217  81.805 -37.857  1.00  6.75
ATOM   2309  OG1 THR B 181      -4.375  83.227 -37.709  1.00  3.57
ATOM   2310  CG2 THR B 181      -5.036  81.183 -36.781  1.00  9.08
ATOM   2311  N   GLY B 182      -2.142  82.311 -39.822  1.00 10.56
ATOM   2312  CA  GLY B 182      -1.544  83.286 -40.758  1.00 10.08
ATOM   2313  C   GLY B 182      -1.610  82.947 -42.226  1.00  9.33
ATOM   2314  O   GLY B 182      -1.493  81.779 -42.637  1.00 11.90
ATOM   2315  N   TYR B 183      -1.868  83.965 -43.020  1.00 10.65
ATOM   2316  CA  TYR B 183      -2.120  83.795 -44.454  1.00  9.89
ATOM   2317  C   TYR B 183      -1.543  84.942 -45.226  1.00  8.57
ATOM   2318  O   TYR B 183      -1.530  86.077 -44.750  1.00  9.83
ATOM   2319  CB  TYR B 183      -3.624  83.631 -44.720  1.00  9.39
ATOM   2320  CG  TYR B 183      -4.399  84.770 -44.286  1.00  8.52
ATOM   2321  CD1 TYR B 183      -4.479  85.875 -45.086  1.00 11.80
ATOM   2322  CD2 TYR B 183      -5.080  84.771 -43.095  1.00 10.88
ATOM   2323  CE1 TYR B 183      -5.115  86.953 -44.720  1.00  6.52
ATOM   2324  CE2 TYR B 183      -5.779  85.899 -42.704  1.00 12.75
ATOM   2325  CZ  TYR B 183      -5.731  87.021 -43.535  1.00 11.06
ATOM   2326  OH  TYR B 183      -6.374  88.211 -43.253  1.00  7.67
ATOM   2327  N   ILE B 184      -1.031  84.654 -46.405  1.00  9.90
ATOM   2328  CA  ILE B 184      -0.388  85.700 -47.205  1.00 10.65
ATOM   2329  C   ILE B 184      -1.317  86.012 -48.368  1.00 11.31
ATOM   2330  O   ILE B 184      -1.555  85.121 -49.199  1.00 11.43
ATOM   2331  CB  ILE B 184       1.035  85.376 -47.623  1.00  9.55
ATOM   2332  CG1 ILE B 184       1.540  86.523 -48.481  1.00 11.59
ATOM   2333  CG2 ILE B 184       1.133  84.079 -48.420  1.00  7.45
ATOM   2334  CD1 ILE B 184       3.055  86.502 -48.734  1.00  2.00
ATOM   2335  N   LYS B 185      -1.922  87.214 -48.352  1.00 11.47
ATOM   2336  CA  LYS B 185      -2.835  87.668 -49.404  1.00 10.17
ATOM   2337  C   LYS B 185      -2.159  88.672 -50.310  1.00 10.31
ATOM   2338  O   LYS B 185      -1.532  89.563 -49.758  1.00  9.95
ATOM   2339  CB  LYS B 185      -4.051  88.357 -48.798  1.00  9.79
ATOM   2340  CG  LYS B 185      -4.768  89.267 -49.747  1.00  6.30
ATOM   2341  CD  LYS B 185      -5.563  90.327 -48.982  1.00 10.91
ATOM   2342  CE  LYS B 185      -6.862  89.796 -48.284  1.00  7.86
ATOM   2343  NZ  LYS B 185      -7.989  89.703 -49.318  1.00  5.30
ATOM   2344  N   PHE B 186      -2.414  88.522 -51.635  1.00  9.12
ATOM   2345  CA  PHE B 186      -1.964  89.335 -52.784  1.00 10.62
ATOM   2346  C   PHE B 186      -3.098  90.156 -53.455  1.00 12.24
ATOM   2347  O   PHE B 186      -4.298  89.748 -53.549  1.00 10.76
ATOM   2348  CB  PHE B 186      -1.213  88.516 -53.906  1.00  9.75
ATOM   2349  CG  PHE B 186       0.022  87.762 -53.438  1.00  9.80
ATOM   2350  CD1 PHE B 186      -0.134  86.622 -52.682  1.00 11.65
ATOM   2351  CD2 PHE B 186       1.306  88.160 -53.817  1.00  3.11
ATOM   2352  CE1 PHE B 186       0.994  85.877 -52.255  1.00 16.27
ATOM   2353  CE2 PHE B 186       2.389  87.450 -53.410  1.00 15.26
ATOM   2354  CZ  PHE B 186       2.244  86.292 -52.600  1.00  6.63
ATOM   2355  N   ILE B 187      -2.700  91.335 -53.942  1.00 11.90
ATOM   2356  CA  ILE B 187      -3.582  92.250 -54.580  1.00 12.57
ATOM   2357  C   ILE B 187      -3.041  92.600 -55.941  1.00 14.79
ATOM   2358  O   ILE B 187      -1.846  93.039 -56.077  1.00 16.42
ATOM   2359  CB  ILE B 187      -3.715  93.431 -53.735  1.00 13.01
ATOM   2360  CG1 ILE B 187      -4.226  93.007 -52.311  1.00 16.00
ATOM   2361  CG2 ILE B 187      -4.758  94.386 -54.373  1.00 15.42
ATOM   2362  CD1 ILE B 187      -4.528  94.141 -51.308  1.00 10.51
ATOM   2363  N   GLU B 188      -3.836  92.355 -56.982  1.00 15.05
ATOM   2364  CA  GLU B 188      -3.408  92.707 -58.334  1.00 14.95
ATOM   2365  C   GLU B 188      -4.027  94.071 -58.816  1.00 19.36
ATOM   2366  O   GLU B 188      -5.206  94.374 -58.606  1.00 18.43
ATOM   2367  CB  GLU B 188      -3.804  91.576 -59.273  1.00 17.01
ATOM   2368  CG  GLU B 188      -2.806  90.476 -59.373  1.00 12.13
ATOM   2369  CD  GLU B 188      -3.221  89.365 -60.378  1.00 13.05
ATOM   2370  OE1 GLU B 188      -4.321  88.737 -60.229  1.00 10.21
ATOM   2371  OE2 GLU B 188      -2.443  89.176 -61.327  1.00 10.67
ATOM   2372  N   ASN B 189      -3.182  94.892 -59.418  1.00 19.45
ATOM   2373  CA  ASN B 189      -3.527  96.195 -59.949  1.00 20.35
ATOM   2374  C   ASN B 189      -4.976  96.278 -60.436  1.00 20.82
ATOM   2375  O   ASN B 189      -5.691  97.232 -60.105  1.00 20.40
ATOM   2376  CB  ASN B 189      -2.462  96.539 -61.019  1.00 20.40
ATOM   2377  CG  ASN B 189      -2.371  97.982 -61.313  1.00 22.90
ATOM   2378  OD1 ASN B 189      -1.446  98.399 -62.053  1.00 19.48
ATOM   2379  ND2 ASN B 189      -3.348  98.783 -60.807  1.00 20.53
ATOM   2380  N   ASN B 190      -5.448  95.201 -61.065  1.00 22.20
ATOM   2381  CA  ASN B 190      -6.825  95.098 -61.558  1.00 24.24
ATOM   2382  C   ASN B 190      -7.914  95.023 -60.459  1.00 24.69
ATOM   2383  O   ASN B 190      -9.077  95.542 -60.629  1.00 25.12
ATOM   2384  CB  ASN B 190      -6.974  93.922 -62.575  1.00 22.98
ATOM   2385  CG  ASN B 190      -6.899  92.603 -61.943  1.00 24.78
ATOM   2386  OD1 ASN B 190      -7.526  92.379 -60.912  1.00 22.45
ATOM   2387  ND2 ASN B 190      -6.111  91.662 -62.565  1.00 29.35
ATOM   2388  N   GLY B 191      -7.535  94.384 -59.353  1.00 23.82
ATOM   2389  CA  GLY B 191      -8.432  94.063 -58.212  1.00 23.15
ATOM   2390  C   GLY B 191      -8.493  92.564 -57.899  1.00 22.31
ATOM   2391  O   GLY B 191      -9.385  92.085 -57.250  1.00 22.97
ATOM   2392  N   ASN B 192      -7.533  91.811 -58.346  1.00 21.65
ATOM   2393  CA  ASN B 192      -7.634  90.412 -58.000  1.00 22.72
ATOM   2394  C   ASN B 192      -6.888  90.259 -56.722  1.00 21.77
ATOM   2395  O   ASN B 192      -5.828  90.871 -56.502  1.00 22.82
ATOM   2396  CB  ASN B 192      -7.213  89.485 -59.140  1.00 22.16
ATOM   2397  CG  ASN B 192      -7.340  88.019 -58.780  1.00 23.83
ATOM   2398  OD1 ASN B 192      -8.445  87.499 -58.582  1.00 28.16
ATOM   2399  ND2 ASN B 192      -6.202  87.341 -58.688  1.00 15.99
ATOM   2400  N   THR B 193      -7.516  89.556 -55.813  1.00 22.25
ATOM   2401  CA  THR B 193      -6.939  89.344 -54.528  1.00 23.00
ATOM   2402  C   THR B 193      -7.088  87.890 -54.172  1.00 22.98
ATOM   2403  O   THR B 193      -8.237  87.347 -54.187  1.00 23.92
ATOM   2404  CB  THR B 193      -7.653  90.154 -53.441  1.00 24.01
ATOM   2405  OG1 THR B 193      -9.071  89.922 -53.495  1.00 27.20
ATOM   2406  CG2 THR B 193      -7.330  91.673 -53.524  1.00 25.14
ATOM   2407  N   PHE B 194      -5.977  87.264 -53.775  1.00 20.38
ATOM   2408  CA  PHE B 194      -6.001  85.844 -53.397  1.00 19.18
ATOM   2409  C   PHE B 194      -5.067  85.592 -52.208  1.00 18.89
ATOM   2410  O   PHE B 194      -4.134  86.334 -51.997  1.00 21.99
ATOM   2411  CB  PHE B 194      -5.628  84.944 -54.586  1.00 17.29
ATOM   2412  CG  PHE B 194      -4.247  85.218 -55.194  1.00 18.77
ATOM   2413  CD1 PHE B 194      -3.169  84.380 -54.924  1.00 12.76
ATOM   2414  CD2 PHE B 194      -4.047  86.286 -56.084  1.00 13.96
ATOM   2415  CE1 PHE B 194      -1.951  84.623 -55.515  1.00 11.06
ATOM   2416  CE2 PHE B 194      -2.787  86.529 -56.635  1.00 12.71
ATOM   2417  CZ  PHE B 194      -1.763  85.671 -56.366  1.00  8.39
ATOM   2418  N   TRP B 195      -5.338  84.619 -51.381  1.00 17.64
ATOM   2419  CA  TRP B 195      -4.539  84.404 -50.150  1.00 16.18
ATOM   2420  C   TRP B 195      -4.153  82.918 -50.037  1.00 15.37
ATOM   2421  O   TRP B 195      -4.823  82.064 -50.592  1.00 17.63
ATOM   2422  CB  TRP B 195      -5.301  84.892 -48.904  1.00 15.52
ATOM   2423  CG  TRP B 195      -6.663  84.153 -48.565  1.00 13.57
ATOM   2424  CD1 TRP B 195      -7.938  84.485 -48.996  1.00 16.11
ATOM   2425  CD2 TRP B 195      -6.810  83.005 -47.748  1.00 13.94
ATOM   2426  NE1 TRP B 195      -8.883  83.587 -48.487  1.00 12.09
ATOM   2427  CE2 TRP B 195      -8.210  82.663 -47.730  1.00 11.99
ATOM   2428  CE3 TRP B 195      -5.912  82.179 -47.097  1.00 11.60
ATOM   2429  CZ2 TRP B 195      -8.672  81.627 -47.067  1.00 11.51
ATOM   2430  CZ3 TRP B 195      -6.395  81.122 -46.421  1.00 17.58
ATOM   2431  CH2 TRP B 195      -7.790  80.877 -46.369  1.00 14.64
ATOM   2432  N   TYR B 196      -3.187  82.614 -49.215  1.00 14.57
ATOM   2433  CA  TYR B 196      -2.660  81.260 -49.076  1.00 12.19
ATOM   2434  C   TYR B 196      -2.391  81.016 -47.588  1.00 13.35
ATOM   2435  O   TYR B 196      -1.703  81.832 -46.938  1.00 13.23
ATOM   2436  CB  TYR B 196      -1.325  81.064 -49.838  1.00 12.78
ATOM   2437  CG  TYR B 196      -1.362  81.122 -51.385  1.00 11.28
ATOM   2438  CD1 TYR B 196      -0.232  81.508 -52.105  1.00  7.94
ATOM   2439  CD2 TYR B 196      -2.517  80.777 -52.105  1.00 10.80
ATOM   2440  CE1 TYR B 196      -0.243  81.564 -53.451  1.00  9.77
ATOM   2441  CE2 TYR B 196      -2.571  80.869 -53.487  1.00  8.96
ATOM   2442  CZ  TYR B 196      -1.388  81.261 -54.156  1.00 14.65
ATOM   2443  OH  TYR B 196      -1.393  81.334 -55.542  1.00 12.98
ATOM   2444  N   ASP B 197      -2.894  79.903 -47.033  1.00 11.14
ATOM   2445  CA  ASP B 197      -2.708  79.655 -45.619  1.00 11.60
ATOM   2446  C   ASP B 197      -1.246  79.357 -45.326  1.00 11.07
ATOM   2447  O   ASP B 197      -0.588  78.761 -46.133  1.00 12.24
ATOM   2448  CB  ASP B 197      -3.616  78.517 -45.132  1.00 10.08
ATOM   2449  CG  ASP B 197      -3.393  78.176 -43.664  1.00 14.64
ATOM   2450  OD1 ASP B 197      -2.209  78.129 -43.204  1.00 19.92
ATOM   2451  OD2 ASP B 197      -4.376  77.867 -42.955  1.00 18.48
ATOM   2452  N   MET B 198      -0.742  79.757 -44.170  1.00 12.07
ATOM   2453  CA  MET B 198       0.727  79.527 -43.850  1.00 11.16
ATOM   2454  C   MET B 198       0.926  78.434 -42.884  1.00 11.82
ATOM   2455  O   MET B 198       2.065  77.960 -42.729  1.00  9.95
ATOM   2456  CB  MET B 198       1.388  80.779 -43.383  1.00  7.16
ATOM   2457  CG  MET B 198       0.996  81.883 -44.351  1.00  8.30
ATOM   2458  SD  MET B 198       1.492  83.513 -43.744  1.00  9.06
ATOM   2459  CE  MET B 198       3.287  83.563 -43.783  1.00  2.00
ATOM   2460  N   MET B 199      -0.184  78.031 -42.249  1.00 12.91
ATOM   2461  CA  MET B 199      -0.064  77.067 -41.224  1.00 15.02
ATOM   2462  C   MET B 199      -0.478  75.681 -41.652  1.00 16.65
ATOM   2463  O   MET B 199      -1.454  75.492 -42.412  1.00 19.44
ATOM   2464  CB  MET B 199      -0.720  77.528 -39.935  1.00 13.49
ATOM   2465  CG  MET B 199      -0.201  78.796 -39.427  1.00 11.97
ATOM   2466  SD  MET B 199       1.350  78.591 -38.589  1.00 13.57
ATOM   2467  CE  MET B 199       1.680  80.312 -38.301  1.00  8.73
ATOM   2468  N   PRO B 200       0.288  74.679 -41.195  1.00 17.16
ATOM   2469  CA  PRO B 200       0.032  73.273 -41.338  1.00 16.01
ATOM   2470  C   PRO B 200      -1.377  72.760 -41.071  1.00 17.27
ATOM   2471  O   PRO B 200      -2.319  73.473 -40.633  1.00 17.12
ATOM   2472  CB  PRO B 200       1.001  72.626 -40.355  1.00 16.46
ATOM   2473  CG  PRO B 200       2.214  73.558 -40.387  1.00 14.67
ATOM   2474  CD  PRO B 200       1.551  74.971 -40.464  1.00 17.02
ATOM   2475  N   ALA B 201      -1.540  71.493 -41.378  1.00 15.58
ATOM   2476  CA  ALA B 201      -2.863  70.939 -41.396  1.00 17.17
ATOM   2477  C   ALA B 201      -3.114  70.473 -39.966  1.00 18.46
ATOM   2478  O   ALA B 201      -2.181  69.919 -39.361  1.00 20.88
ATOM   2479  CB  ALA B 201      -2.815  69.737 -42.273  1.00 17.09
ATOM   2480  N   PRO B 202      -4.355  70.567 -39.454  1.00 16.86
ATOM   2481  CA  PRO B 202      -4.566  70.282 -38.124  1.00 16.02
ATOM   2482  C   PRO B 202      -4.383  68.790 -37.988  1.00 16.82
ATOM   2483  O   PRO B 202      -5.291  68.064 -38.297  1.00 17.69
ATOM   2484  CB  PRO B 202      -6.027  70.705 -37.918  1.00 12.96
ATOM   2485  CG  PRO B 202      -6.672  70.356 -39.075  1.00 13.52
ATOM   2486  CD  PRO B 202      -5.649  70.868 -40.091  1.00 20.01
ATOM   2487  N   GLY B 203      -3.168  68.355 -37.621  1.00 18.95
ATOM   2488  CA  GLY B 203      -2.881  66.987 -37.126  1.00 19.31
ATOM   2489  C   GLY B 203      -1.470  66.626 -36.655  1.00 20.74
ATOM   2490  O   GLY B 203      -0.637  67.490 -36.252  1.00 21.35
ATOM   2491  N   ASP B 204      -1.169  65.332 -36.660  1.00 21.37
ATOM   2492  CA  ASP B 204       0.117  64.865 -36.115  1.00 22.31
ATOM   2493  C   ASP B 204       1.356  65.057 -36.952  1.00 21.10
ATOM   2494  O   ASP B 204       2.421  65.302 -36.395  1.00 20.39
ATOM   2495  CB  ASP B 204       0.038  63.364 -35.820  1.00 23.43
ATOM   2496  CG  ASP B 204       1.406  62.788 -35.466  1.00 29.29
ATOM   2497  OD1 ASP B 204       2.103  63.400 -34.634  1.00 25.43
ATOM   2498  OD2 ASP B 204       1.788  61.713 -36.016  1.00 35.50
ATOM   2499  N   LYS B 205       1.253  64.780 -38.266  1.00 21.26
ATOM   2500  CA  LYS B 205       2.385  64.893 -39.228  1.00 19.07
ATOM   2501  C   LYS B 205       2.184  65.936 -40.311  1.00 16.65
ATOM   2502  O   LYS B 205       1.121  66.441 -40.483  1.00 14.45
ATOM   2503  CB  LYS B 205       2.831  63.549 -39.839  1.00 20.05
ATOM   2504  CG  LYS B 205       1.670  62.561 -40.116  1.00 24.18
ATOM   2505  CD  LYS B 205       1.331  61.766 -38.850  1.00 21.21
ATOM   2506  CE  LYS B 205       0.100  60.838 -39.050  1.00 23.66
ATOM   2507  NZ  LYS B 205       0.010  59.948 -37.824  1.00 18.16
ATOM   2508  N   PHE B 206       3.242  66.235 -41.061  1.00 14.82
ATOM   2509  CA  PHE B 206       3.137  67.215 -42.131  1.00 13.57
ATOM   2510  C   PHE B 206       3.690  66.705 -43.463  1.00 13.13
ATOM   2511  O   PHE B 206       4.897  66.556 -43.586  1.00 14.61
ATOM   2512  CB  PHE B 206       3.972  68.471 -41.702  1.00 11.00
ATOM   2513  CG  PHE B 206       4.048  69.531 -42.709  1.00 10.52
ATOM   2514  CD1 PHE B 206       2.886  70.012 -43.328  1.00  5.52
ATOM   2515  CD2 PHE B 206       5.278  70.093 -43.038  1.00  8.57
ATOM   2516  CE1 PHE B 206       2.972  71.070 -44.134  1.00  9.40
ATOM   2517  CE2 PHE B 206       5.354  71.122 -43.857  1.00  5.77
ATOM   2518  CZ  PHE B 206       4.172  71.631 -44.437  1.00  4.76
ATOM   2519  N   ASP B 207       2.852  66.444 -44.474  1.00 14.31
ATOM   2520  CA  ASP B 207       3.382  66.066 -45.781  1.00 12.10
ATOM   2521  C   ASP B 207       3.919  67.366 -46.431  1.00 13.28
ATOM   2522  O   ASP B 207       3.152  68.192 -46.951  1.00 11.62
ATOM   2523  CB  ASP B 207       2.239  65.477 -46.568  1.00 11.84
ATOM   2524  CG  ASP B 207       2.604  65.072 -47.969  1.00 14.12
ATOM   2525  OD1 ASP B 207       3.819  65.021 -48.280  1.00 20.54
ATOM   2526  OD2 ASP B 207       1.653  64.838 -48.794  1.00 16.80
ATOM   2527  N   GLN B 208       5.249  67.519 -46.462  1.00 12.94
ATOM   2528  CA  GLN B 208       5.846  68.678 -47.079  1.00 12.07
ATOM   2529  C   GLN B 208       5.292  68.909 -48.441  1.00 14.28
ATOM   2530  O   GLN B 208       4.488  69.855 -48.699  1.00 16.38
ATOM   2531  CB  GLN B 208       7.343  68.518 -47.118  1.00 13.83
ATOM   2532  CG  GLN B 208       8.076  69.250 -45.963  1.00  8.93
ATOM   2533  CD  GLN B 208       9.522  68.700 -45.880  1.00  7.81
ATOM   2534  OE1 GLN B 208      10.449  69.331 -45.329  1.00  2.00
ATOM   2535  NE2 GLN B 208       9.706  67.572 -46.534  1.00  7.76
ATOM   2536  N   SER B 209       5.549  67.949 -49.281  1.00 13.28
ATOM   2537  CA  SER B 209       4.976  67.974 -50.609  1.00 14.95
ATOM   2538  C   SER B 209       3.596  68.558 -50.733  1.00 15.05
ATOM   2539  O   SER B 209       3.413  69.708 -51.100  1.00 15.66
ATOM   2540  CB  SER B 209       4.884  66.623 -51.212  1.00 14.51
ATOM   2541  OG  SER B 209       4.184  66.790 -52.450  1.00 20.02
ATOM   2542  N   LYS B 210       2.629  67.688 -50.540  1.00 13.77
ATOM   2543  CA  LYS B 210       1.213  68.094 -50.713  1.00 12.46
ATOM   2544  C   LYS B 210       0.881  69.486 -50.315  1.00  8.67
ATOM   2545  O   LYS B 210      -0.174  69.981 -50.687  1.00  8.86
ATOM   2546  CB  LYS B 210       0.316  67.149 -49.895  1.00 10.27
ATOM   2547  CG  LYS B 210      -1.092  67.083 -50.390  1.00 10.90
ATOM   2548  CD  LYS B 210      -2.095  66.676 -49.232  1.00 11.44
ATOM   2549  CE  LYS B 210      -3.580  66.439 -49.764  1.00 14.70
ATOM   2550  NZ  LYS B 210      -4.473  66.155 -48.636  1.00 13.56
ATOM   2551  N   TYR B 211       1.706  70.096 -49.468  1.00 10.54
ATOM   2552  CA  TYR B 211       1.443  71.515 -49.057  1.00  7.88
ATOM   2553  C   TYR B 211       1.711  72.318 -50.290  1.00  8.59
ATOM   2554  O   TYR B 211       0.925  73.263 -50.746  1.00 11.87
ATOM   2555  CB  TYR B 211       2.347  71.974 -47.907  1.00  7.91
ATOM   2556  CG  TYR B 211       2.248  73.541 -47.516  1.00  9.48
ATOM   2557  CD1 TYR B 211       1.033  74.114 -47.060  1.00  2.42
ATOM   2558  CD2 TYR B 211       3.315  74.389 -47.688  1.00  5.30
ATOM   2559  CE1 TYR B 211       0.899  75.421 -46.669  1.00  2.05
ATOM   2560  CE2 TYR B 211       3.187  75.795 -47.393  1.00  7.64
ATOM   2561  CZ  TYR B 211       1.964  76.276 -46.875  1.00  8.61
ATOM   2562  OH  TYR B 211       1.790  77.577 -46.600  1.00  7.48
ATOM   2563  N   LEU B 212       2.870  72.048 -50.850  1.00  7.58
ATOM   2564  CA  LEU B 212       3.405  72.839 -51.971  1.00  5.40
ATOM   2565  C   LEU B 212       2.632  72.655 -53.177  1.00  8.42
ATOM   2566  O   LEU B 212       2.670  73.494 -54.063  1.00 12.22
ATOM   2567  CB  LEU B 212       4.817  72.454 -52.247  1.00  4.90
ATOM   2568  CG  LEU B 212       5.906  72.763 -51.202  1.00  2.14
ATOM   2569  CD1 LEU B 212       7.193  72.208 -51.542  1.00 10.84
ATOM   2570  CD2 LEU B 212       6.169  74.388 -51.135  1.00  5.79
ATOM   2571  N   MET B 213       1.842  71.572 -53.271  1.00  9.17
ATOM   2572  CA  MET B 213       1.198  71.298 -54.517  1.00  5.98
ATOM   2573  C   MET B 213       0.358  72.535 -54.882  1.00  6.67
ATOM   2574  O   MET B 213      -0.136  72.676 -55.997  1.00  8.57
ATOM   2575  CB  MET B 213       0.327  70.158 -54.313  1.00  2.70
ATOM   2576  CG  MET B 213      -0.485  69.890 -55.450  1.00  5.38
ATOM   2577  SD  MET B 213      -1.040  68.218 -55.292  1.00 10.00
ATOM   2578  CE  MET B 213       0.675  67.411 -55.231  1.00  7.05
ATOM   2579  N   MET B 214       0.114  73.410 -53.931  1.00  6.76
ATOM   2580  CA  MET B 214      -0.600  74.596 -54.245  1.00  5.62
ATOM   2581  C   MET B 214       0.100  75.546 -55.204  1.00  8.62
ATOM   2582  O   MET B 214      -0.545  76.605 -55.666  1.00  7.46
ATOM   2583  CB  MET B 214      -0.940  75.403 -53.004  1.00  7.43
ATOM   2584  CG  MET B 214       0.189  75.926 -52.127  1.00  5.09
ATOM   2585  SD  MET B 214      -0.177  76.922 -50.685  1.00  3.90
ATOM   2586  CE  MET B 214       0.893  78.406 -51.057  1.00  7.67
ATOM   2587  N   TYR B 215       1.355  75.241 -55.536  1.00  6.55
ATOM   2588  CA  TYR B 215       2.067  76.214 -56.352  1.00  8.24
ATOM   2589  C   TYR B 215       2.055  75.738 -57.767  1.00 10.44
ATOM   2590  O   TYR B 215       2.719  76.301 -58.669  1.00  9.45
ATOM   2591  CB  TYR B 215       3.489  76.556 -55.873  1.00  9.46
ATOM   2592  CG  TYR B 215       3.640  77.347 -54.574  1.00  9.98
ATOM   2593  CD1 TYR B 215       4.463  76.871 -53.521  1.00 13.26
ATOM   2594  CD2 TYR B 215       2.891  78.498 -54.349  1.00 12.80
ATOM   2595  CE1 TYR B 215       4.586  77.611 -52.313  1.00 11.10
ATOM   2596  CE2 TYR B 215       3.009  79.237 -53.144  1.00  7.24
ATOM   2597  CZ  TYR B 215       3.863  78.800 -52.158  1.00  6.83
ATOM   2598  OH  TYR B 215       3.966  79.535 -50.972  1.00  6.01
ATOM   2599  N   ASN B 216       1.207  74.743 -58.027  1.00 10.11
ATOM   2600  CA  ASN B 216       1.243  74.184 -59.366  1.00 10.42
ATOM   2601  C   ASN B 216       0.340  74.921 -60.396  1.00 11.37
ATOM   2602  O   ASN B 216       0.157  74.494 -61.556  1.00 12.14
ATOM   2603  CB  ASN B 216       1.003  72.660 -59.234  1.00 10.99
ATOM   2604  CG  ASN B 216      -0.493  72.295 -58.845  1.00  7.94
ATOM   2605  OD1 ASN B 216      -0.880  71.187 -59.046  1.00  8.88
ATOM   2606  ND2 ASN B 216      -1.276  73.223 -58.348  1.00  7.90
ATOM   2607  N   ASP B 217      -0.208  76.049 -59.971  1.00 13.41
ATOM   2608  CA  ASP B 217      -1.109  76.814 -60.818  1.00 13.47
ATOM   2609  C   ASP B 217      -0.190  77.876 -61.500  1.00 13.44
ATOM   2610  O   ASP B 217      -0.605  78.774 -62.232  1.00  8.95
ATOM   2611  CB  ASP B 217      -2.173  77.474 -59.928  1.00 14.77
ATOM   2612  CG  ASP B 217      -1.604  78.561 -59.073  1.00 18.29
ATOM   2613  OD1 ASP B 217      -0.357  78.599 -59.004  1.00 25.18
ATOM   2614  OD2 ASP B 217      -2.360  79.387 -58.522  1.00 15.38
ATOM   2615  N   ASN B 218       1.119  77.716 -61.246  1.00 13.79
ATOM   2616  CA  ASN B 218       2.083  78.640 -61.731  1.00 11.63
ATOM   2617  C   ASN B 218       1.623  80.062 -61.868  1.00 14.18
ATOM   2618  O   ASN B 218       1.977  80.681 -62.792  1.00 16.15
ATOM   2619  CB  ASN B 218       2.554  78.205 -63.054  1.00 12.01
ATOM   2620  CG  ASN B 218       3.987  78.680 -63.272  1.00 13.18
ATOM   2621  OD1 ASN B 218       4.903  78.223 -62.578  1.00 10.21
ATOM   2622  ND2 ASN B 218       4.161  79.674 -64.107  1.00  7.20
ATOM   2623  N   LYS B 219       0.784  80.555 -60.967  1.00 13.83
ATOM   2624  CA  LYS B 219       0.125  81.773 -61.130  1.00 13.39
ATOM   2625  C   LYS B 219       1.207  82.778 -60.997  1.00 14.08
ATOM   2626  O   LYS B 219       2.116  82.609 -60.161  1.00 16.86
ATOM   2627  CB  LYS B 219      -0.855  82.027 -59.962  1.00 13.32
ATOM   2628  CG  LYS B 219      -1.266  83.523 -59.806  1.00 10.67
ATOM   2629  CD  LYS B 219      -1.971  84.122 -61.071  1.00  2.64
ATOM   2630  CE  LYS B 219      -2.428  85.720 -60.820  1.00  6.33
ATOM   2631  NZ  LYS B 219      -3.811  85.804 -60.273  1.00  9.10
ATOM   2632  N   THR B 220       1.132  83.796 -61.845  1.00 12.34
ATOM   2633  CA  THR B 220       2.051  84.948 -61.885  1.00 13.14
ATOM   2634  C   THR B 220       1.331  86.328 -61.557  1.00 11.83
ATOM   2635  O   THR B 220       0.035  86.521 -61.610  1.00  6.57
ATOM   2636  CB  THR B 220       2.628  85.189 -63.283  1.00 11.29
ATOM   2637  OG1 THR B 220       1.735  84.675 -64.246  1.00 16.36
ATOM   2638  CG2 THR B 220       4.031  84.648 -63.482  1.00 15.28
ATOM   2639  N   VAL B 221       2.205  87.279 -61.336  1.00  9.47
ATOM   2640  CA  VAL B 221       1.804  88.642 -60.939  1.00  8.96
ATOM   2641  C   VAL B 221       2.805  89.735 -61.425  1.00  9.26
ATOM   2642  O   VAL B 221       3.969  89.454 -61.744  1.00  7.29
ATOM   2643  CB  VAL B 221       1.740  88.729 -59.432  1.00  8.07
ATOM   2644  CG1 VAL B 221       0.413  88.178 -58.892  1.00  6.23
ATOM   2645  CG2 VAL B 221       2.885  88.058 -58.844  1.00  8.07
ATOM   2646  N   ASP B 222       2.354  90.999 -61.458  1.00 11.10
ATOM   2647  CA  ASP B 222       3.230  92.030 -62.042  1.00 11.38
ATOM   2648  C   ASP B 222       3.928  92.799 -60.967  1.00 10.59
ATOM   2649  O   ASP B 222       3.290  93.658 -60.236  1.00 10.88
ATOM   2650  CB  ASP B 222       2.458  92.942 -62.994  1.00 11.31
ATOM   2651  CG  ASP B 222       3.159  94.290 -63.216  1.00 18.61
ATOM   2652  OD1 ASP B 222       4.402  94.328 -63.651  1.00 12.76
ATOM   2653  OD2 ASP B 222       2.437  95.315 -62.949  1.00 20.55
ATOM   2654  N   SER B 223       5.202  92.484 -60.775  1.00 11.01
ATOM   2655  CA  SER B 223       6.008  93.167 -59.706  1.00 10.81
ATOM   2656  C   SER B 223       5.680  94.662 -59.588  1.00 13.01
ATOM   2657  O   SER B 223       4.861  95.098 -58.779  1.00 12.28
ATOM   2658  CB  SER B 223       7.431  92.954 -60.035  1.00 12.80
ATOM   2659  OG  SER B 223       7.714  93.692 -61.198  1.00 17.99
ATOM   2660  N   LYS B 224       6.293  95.493 -60.391  1.00 16.57
ATOM   2661  CA  LYS B 224       6.027  96.970 -60.347  1.00 18.61
ATOM   2662  C   LYS B 224       4.662  97.474 -59.806  1.00 17.45
ATOM   2663  O   LYS B 224       4.496  98.671 -59.496  1.00 22.39
ATOM   2664  CB  LYS B 224       6.328  97.627 -61.715  1.00 17.57
ATOM   2665  CG  LYS B 224       5.840  99.108 -61.832  1.00 22.56
ATOM   2666  CD  LYS B 224       6.607 100.035 -60.888  1.00 30.04
ATOM   2667  CE  LYS B 224       8.134  99.942 -61.100  1.00 30.69
ATOM   2668  NZ  LYS B 224       8.574 100.785 -62.276  1.00 30.96
ATOM   2669  N   SER B 225       3.700  96.620 -59.636  1.00 15.93
ATOM   2670  CA  SER B 225       2.383  97.129 -59.155  1.00 16.39
ATOM   2671  C   SER B 225       1.743  96.430 -58.047  1.00 13.02
ATOM   2672  O   SER B 225       1.368  97.084 -57.074  1.00 16.98
ATOM   2673  CB  SER B 225       1.304  97.240 -60.229  1.00 15.75
ATOM   2674  OG  SER B 225       0.888  95.949 -60.640  1.00 23.80
ATOM   2675  N   VAL B 226       1.532  95.163 -58.206  1.00 12.07
ATOM   2676  CA  VAL B 226       1.080  94.194 -57.144  1.00 12.12
ATOM   2677  C   VAL B 226       1.634  94.647 -55.829  1.00 13.26
ATOM   2678  O   VAL B 226       2.795  95.206 -55.740  1.00 15.27
ATOM   2679  CB  VAL B 226       1.664  92.740 -57.401  1.00 10.62
ATOM   2680  CG1 VAL B 226       3.105  92.644 -57.014  1.00 12.40
ATOM   2681  CG2 VAL B 226       0.975  91.629 -56.666  1.00 12.97
ATOM   2682  N   LYS B 227       0.829  94.417 -54.801  1.00 14.79
ATOM   2683  CA  LYS B 227       1.127  94.757 -53.375  1.00 13.32
ATOM   2684  C   LYS B 227       0.797  93.482 -52.514  1.00 11.92
ATOM   2685  O   LYS B 227      -0.144  92.773 -52.855  1.00  9.07
ATOM   2686  CB  LYS B 227       0.244  95.971 -52.941  1.00 10.36
ATOM   2687  CG  LYS B 227      -1.236  95.816 -53.245  1.00 12.29
ATOM   2688  CD  LYS B 227      -2.001  97.269 -53.303  1.00 16.29
ATOM   2689  CE  LYS B 227      -1.117  98.384 -54.076  1.00 17.98
ATOM   2690  NZ  LYS B 227      -1.848  99.652 -54.281  1.00 21.46
ATOM   2691  N   ILE B 228       1.511  93.278 -51.387  1.00 12.84
ATOM   2692  CA  ILE B 228       1.363  92.065 -50.474  1.00 12.66
ATOM   2693  C   ILE B 228       0.868  92.391 -49.090  1.00 11.62
ATOM   2694  O   ILE B 228       1.163  93.494 -48.570  1.00  9.82
ATOM   2695  CB  ILE B 228       2.649  91.385 -50.356  1.00 11.44
ATOM   2696  CG1 ILE B 228       3.085  91.087 -51.804  1.00 17.05
ATOM   2697  CG2 ILE B 228       2.432  90.020 -49.796  1.00 14.63
ATOM   2698  CD1 ILE B 228       4.582  90.906 -51.983  1.00 27.71
ATOM   2699  N   GLU B 229       0.051  91.488 -48.552  1.00  8.09
ATOM   2700  CA  GLU B 229      -0.319  91.548 -47.203  1.00  8.55
ATOM   2701  C   GLU B 229      -0.230  90.210 -46.470  1.00 10.16
ATOM   2702  O   GLU B 229      -0.815  89.166 -46.918  1.00  8.76
ATOM   2703  CB  GLU B 229      -1.793  92.008 -47.080  1.00  8.11
ATOM   2704  CG  GLU B 229      -1.987  93.457 -47.591  1.00  5.95
ATOM   2705  CD  GLU B 229      -3.473  94.015 -47.374  1.00  9.38
ATOM   2706  OE1 GLU B 229      -4.138  93.522 -46.464  1.00  4.16
ATOM   2707  OE2 GLU B 229      -3.928  94.948 -48.149  1.00  5.72
ATOM   2708  N   VAL B 230       0.441  90.271 -45.317  1.00  9.23
ATOM   2709  CA  VAL B 230       0.472  89.129 -44.411  1.00 10.18
ATOM   2710  C   VAL B 230      -0.299  89.382 -43.165  1.00 10.18
ATOM   2711  O   VAL B 230      -0.392  90.540 -42.669  1.00  7.88
ATOM   2712  CB  VAL B 230       1.900  88.713 -44.098  1.00  9.33
ATOM   2713  CG1 VAL B 230       1.911  87.345 -43.637  1.00 11.38
ATOM   2714  CG2 VAL B 230       2.678  88.721 -45.378  1.00  6.10
ATOM   2715  N   HIS B 231      -0.999  88.328 -42.715  1.00 10.47
ATOM   2716  CA  HIS B 231      -1.878  88.492 -41.562  1.00  7.93
ATOM   2717  C   HIS B 231      -1.788  87.438 -40.479  1.00  9.90
ATOM   2718  O   HIS B 231      -2.104  86.235 -40.706  1.00  7.96
ATOM   2719  CB  HIS B 231      -3.308  88.687 -42.003  1.00 10.05
ATOM   2720  CG  HIS B 231      -3.514  89.873 -42.884  1.00  4.45
ATOM   2721  ND1 HIS B 231      -3.540  91.167 -42.386  1.00 14.17
ATOM   2722  CD2 HIS B 231      -3.743  89.978 -44.205  1.00  8.07
ATOM   2723  CE1 HIS B 231      -3.814  92.023 -43.367  1.00 11.46
ATOM   2724  NE2 HIS B 231      -3.921  91.338 -44.496  1.00  9.52
ATOM   2725  N   LEU B 232      -1.347  87.908 -39.281  1.00  9.33
ATOM   2726  CA  LEU B 232      -1.211  87.048 -38.168  1.00 10.79
ATOM   2727  C   LEU B 232      -1.990  87.322 -36.867  1.00 11.53
ATOM   2728  O   LEU B 232      -2.351  88.432 -36.581  1.00  9.61
ATOM   2729  CB  LEU B 232       0.289  86.905 -37.838  1.00  6.58
ATOM   2730  CG  LEU B 232       1.204  87.014 -39.059  1.00  6.26
ATOM   2731  CD1 LEU B 232       2.639  87.509 -38.690  1.00  2.00
ATOM   2732  CD2 LEU B 232       1.300  85.699 -39.770  1.00  8.32
ATOM   2733  N   THR B 233      -2.050  86.274 -36.041  1.00 13.55
ATOM   2734  CA  THR B 233      -2.766  86.244 -34.802  1.00 17.69
ATOM   2735  C   THR B 233      -1.963  85.429 -33.839  1.00 18.51
ATOM   2736  O   THR B 233      -1.586  84.272 -34.110  1.00 18.86
ATOM   2737  CB  THR B 233      -4.114  85.683 -34.921  1.00 15.29
ATOM   2738  OG1 THR B 233      -4.012  84.454 -35.648  1.00 22.65
ATOM   2739  CG2 THR B 233      -5.033  86.635 -35.675  1.00 16.54
ATOM   2740  N   THR B 234      -1.686  86.088 -32.721  1.00 21.39
ATOM   2741  CA  THR B 234      -0.809  85.565 -31.717  1.00 24.25
ATOM   2742  C   THR B 234      -1.483  84.491 -30.955  1.00 24.47
ATOM   2743  O   THR B 234      -2.715  84.347 -30.992  1.00 26.05
ATOM   2744  CB  THR B 234      -0.389  86.652 -30.788  1.00 24.84
ATOM   2745  OG1 THR B 234       0.167  87.710 -31.570  1.00 25.92
ATOM   2746  CG2 THR B 234       0.698  86.127 -29.884  1.00 31.82
ATOM   2747  N   LYS B 235      -0.671  83.665 -30.317  1.00 26.23
ATOM   2748  CA  LYS B 235      -1.160  82.497 -29.579  1.00 25.36
ATOM   2749  C   LYS B 235      -1.798  83.077 -28.343  1.00 26.05
ATOM   2750  O   LYS B 235      -2.684  83.934 -28.437  1.00 26.41
ATOM   2751  CB  LYS B 235       0.022  81.665 -29.110  1.00 24.60
ATOM   2752  CG  LYS B 235       0.453  80.518 -30.001  1.00 28.91
ATOM   2753  CD  LYS B 235      -0.485  79.259 -29.947  1.00 27.15
ATOM   2754  CE  LYS B 235       0.151  78.062 -30.780  1.00 23.19
ATOM   2755  NZ  LYS B 235       1.588  77.709 -30.374  1.00 24.48