CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 220512180416120799

Job options:

ID        	=	 220512180416120799
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


CRYST1  163.298  169.764   55.664  90.00  90.00  90.00 P 21 21 2    16
ATOM      1  N   SER A  94     113.553  67.781 -31.126  1.00 80.20      A    N  
ATOM      2  CA  SER A  94     113.639  69.247 -31.376  1.00 80.31      A    C  
ATOM      3  C   SER A  94     113.347  69.565 -32.838  1.00 79.59      A    C  
ATOM      4  O   SER A  94     113.511  68.713 -33.712  1.00 79.99      A    O  
ATOM      5  CB  SER A  94     115.032  69.765 -31.003  1.00 81.74      A    C  
ATOM      6  OG  SER A  94     115.251  69.690 -29.604  1.00 83.85      A    O  
ATOM      7  N   SER A  95     112.920  70.800 -33.093  1.00 78.00      A    N  
ATOM      8  CA  SER A  95     112.597  71.250 -34.447  1.00 75.88      A    C  
ATOM      9  C   SER A  95     112.950  72.726 -34.648  1.00 72.87      A    C  
ATOM     10  O   SER A  95     112.987  73.495 -33.686  1.00 73.30      A    O  
ATOM     11  CB  SER A  95     111.113  71.025 -34.715  1.00 75.33      A    C  
ATOM     12  OG  SER A  95     110.344  71.521 -33.637  1.00 76.82      A    O  
ATOM     13  N   SER A  96     113.203  73.115 -35.898  1.00 69.61      A    N  
ATOM     14  CA  SER A  96     113.576  74.497 -36.214  1.00 64.54      A    C  
ATOM     15  C   SER A  96     112.584  75.499 -35.650  1.00 60.01      A    C  
ATOM     16  O   SER A  96     111.377  75.257 -35.625  1.00 58.83      A    O  
ATOM     17  CB  SER A  96     113.705  74.693 -37.730  1.00 62.40      A    C  
ATOM     18  OG  SER A  96     112.506  74.351 -38.390  1.00 64.79      A    O  
ATOM     19  N   VAL A  97     113.112  76.633 -35.207  1.00 55.51      A    N  
ATOM     20  CA  VAL A  97     112.306  77.688 -34.615  1.00 51.82      A    C  
ATOM     21  C   VAL A  97     111.841  78.742 -35.620  1.00 49.47      A    C  
ATOM     22  O   VAL A  97     112.653  79.370 -36.292  1.00 47.70      A    O  
ATOM     23  CB  VAL A  97     113.096  78.404 -33.510  1.00 52.57      A    C  
ATOM     24  CG1 VAL A  97     112.191  79.349 -32.745  1.00 50.89      A    C  
ATOM     25  CG2 VAL A  97     113.724  77.386 -32.587  1.00 52.86      A    C  
ATOM     26  N   PRO A  98     110.518  78.945 -35.735  1.00 47.99      A    N  
ATOM     27  CA  PRO A  98     109.998  79.945 -36.672  1.00 46.21      A    C  
ATOM     28  C   PRO A  98     110.331  81.349 -36.164  1.00 45.24      A    C  
ATOM     29  O   PRO A  98     110.346  81.593 -34.956  1.00 43.54      A    O  
ATOM     30  CB  PRO A  98     108.499  79.664 -36.670  1.00 46.27      A    C  
ATOM     31  CG  PRO A  98     108.254  79.217 -35.265  1.00 48.00      A    C  
ATOM     32  CD  PRO A  98     109.414  78.266 -35.033  1.00 47.17      A    C  
ATOM     33  N   SER A  99     110.605  82.267 -37.083  1.00 44.17      A    N  
ATOM     34  CA  SER A  99     110.943  83.633 -36.703  1.00 43.05      A    C  
ATOM     35  C   SER A  99     109.849  84.265 -35.863  1.00 41.08      A    C  
ATOM     36  O   SER A  99     108.682  83.935 -36.013  1.00 40.77      A    O  
ATOM     37  CB  SER A  99     111.159  84.498 -37.939  1.00 45.49      A    C  
ATOM     38  OG  SER A  99     111.378  85.852 -37.564  1.00 47.93      A    O  
ATOM     39  N   GLN A 100     110.234  85.183 -34.986  1.00 39.57      A    N  
ATOM     40  CA  GLN A 100     109.269  85.867 -34.140  1.00 41.22      A    C  
ATOM     41  C   GLN A 100     109.464  87.373 -34.271  1.00 38.10      A    C  
ATOM     42  O   GLN A 100     108.870  88.156 -33.533  1.00 34.79      A    O  
ATOM     43  CB  GLN A 100     109.452  85.456 -32.680  1.00 42.21      A    C  
ATOM     44  CG  GLN A 100     110.713  86.020 -32.040  1.00 48.02      A    C  
ATOM     45  CD  GLN A 100     110.937  85.483 -30.638  1.00 52.31      A    C  
ATOM     46  NE2 GLN A 100     110.690  86.321 -29.636  1.00 43.35      A    N  
ATOM     47  OE1 GLN A 100     111.315  84.320 -30.459  1.00 52.22      A    O  
ATOM     48  N   LYS A 101     110.294  87.782 -35.222  1.00 36.33      A    N  
ATOM     49  CA  LYS A 101     110.544  89.205 -35.396  1.00 37.93      A    C  
ATOM     50  C   LYS A 101     109.367  89.958 -36.000  1.00 35.95      A    C  
ATOM     51  O   LYS A 101     108.835  89.578 -37.042  1.00 34.60      A    O  
ATOM     52  CB  LYS A 101     111.778  89.451 -36.266  1.00 40.34      A    C  
ATOM     53  CG  LYS A 101     112.282  90.879 -36.137  1.00 44.04      A    C  
ATOM     54  CD  LYS A 101     113.290  91.234 -37.203  1.00 51.76      A    C  
ATOM     55  CE  LYS A 101     113.670  92.707 -37.108  1.00 53.26      A    C  
ATOM     56  NZ  LYS A 101     114.336  93.184 -38.353  1.00 54.17      A    N1+
ATOM     57  N   THR A 102     108.974  91.035 -35.334  1.00 34.37      A    N  
ATOM     58  CA  THR A 102     107.877  91.859 -35.798  1.00 35.44      A    C  
ATOM     59  C   THR A 102     108.225  92.411 -37.177  1.00 38.30      A    C  
ATOM     60  O   THR A 102     109.347  92.861 -37.421  1.00 37.93      A    O  
ATOM     61  CB  THR A 102     107.621  93.002 -34.814  1.00 36.19      A    C  
ATOM     62  CG2 THR A 102     106.409  93.819 -35.246  1.00 33.54      A    C  
ATOM     63  OG1 THR A 102     107.382  92.451 -33.510  1.00 38.33      A    O  
ATOM     64  N   TYR A 103     107.251  92.363 -38.075  1.00 37.34      A    N  
ATOM     65  CA  TYR A 103     107.429  92.813 -39.447  1.00 37.97      A    C  
ATOM     66  C   TYR A 103     106.065  93.299 -39.959  1.00 37.82      A    C  
ATOM     67  O   TYR A 103     105.162  92.498 -40.192  1.00 37.19      A    O  
ATOM     68  CB  TYR A 103     107.953  91.632 -40.277  1.00 36.19      A    C  
ATOM     69  CG  TYR A 103     108.087  91.882 -41.757  1.00 42.94      A    C  
ATOM     70  CD1 TYR A 103     108.954  92.864 -42.247  1.00 41.66      A    C  
ATOM     71  CD2 TYR A 103     107.356  91.124 -42.680  1.00 45.30      A    C  
ATOM     72  CE1 TYR A 103     109.091  93.087 -43.617  1.00 42.27      A    C  
ATOM     73  CE2 TYR A 103     107.488  91.340 -44.060  1.00 46.56      A    C  
ATOM     74  CZ  TYR A 103     108.354  92.322 -44.517  1.00 45.55      A    C  
ATOM     75  OH  TYR A 103     108.467  92.555 -45.868  1.00 50.76      A    O  
ATOM     76  N   GLN A 104     105.909  94.610 -40.115  1.00 35.71      A    N  
ATOM     77  CA  GLN A 104     104.640  95.158 -40.584  1.00 37.26      A    C  
ATOM     78  C   GLN A 104     104.373  94.891 -42.058  1.00 37.15      A    C  
ATOM     79  O   GLN A 104     103.218  94.778 -42.477  1.00 35.53      A    O  
ATOM     80  CB  GLN A 104     104.559  96.660 -40.298  1.00 35.92      A    C  
ATOM     81  CG  GLN A 104     104.465  96.965 -38.814  1.00 42.06      A    C  
ATOM     82  CD  GLN A 104     103.811  98.298 -38.518  1.00 44.47      A    C  
ATOM     83  NE2 GLN A 104     103.551  99.076 -39.558  1.00 47.18      A    N  
ATOM     84  OE1 GLN A 104     103.540  98.625 -37.361  1.00 52.08      A    O  
ATOM     85  N   GLY A 105     105.438  94.779 -42.840  1.00 37.42      A    N  
ATOM     86  CA  GLY A 105     105.282  94.496 -44.256  1.00 38.59      A    C  
ATOM     87  C   GLY A 105     104.633  95.608 -45.055  1.00 37.91      A    C  
ATOM     88  O   GLY A 105     104.419  96.709 -44.550  1.00 39.48      A    O  
ATOM     89  N   SER A 106     104.305  95.312 -46.306  1.00 36.64      A    N  
ATOM     90  CA  SER A 106     103.697  96.301 -47.184  1.00 40.02      A    C  
ATOM     91  C   SER A 106     102.333  96.773 -46.719  1.00 40.69      A    C  
ATOM     92  O   SER A 106     101.906  97.871 -47.075  1.00 42.78      A    O  
ATOM     93  CB  SER A 106     103.550  95.742 -48.596  1.00 38.71      A    C  
ATOM     94  OG  SER A 106     104.789  95.260 -49.074  1.00 47.26      A    O  
ATOM     95  N   TYR A 107     101.653  95.958 -45.920  1.00 40.44      A    N  
ATOM     96  CA  TYR A 107     100.312  96.314 -45.474  1.00 36.76      A    C  
ATOM     97  C   TYR A 107     100.211  96.911 -44.079  1.00 37.20      A    C  
ATOM     98  O   TYR A 107      99.110  97.152 -43.588  1.00 39.46      A    O  
ATOM     99  CB  TYR A 107      99.408  95.084 -45.603  1.00 34.61      A    C  
ATOM    100  CG  TYR A 107      99.363  94.559 -47.024  1.00 36.30      A    C  
ATOM    101  CD1 TYR A 107      98.599  95.201 -47.996  1.00 35.65      A    C  
ATOM    102  CD2 TYR A 107     100.140  93.468 -47.414  1.00 29.64      A    C  
ATOM    103  CE1 TYR A 107      98.609  94.773 -49.318  1.00 33.72      A    C  
ATOM    104  CE2 TYR A 107     100.158  93.031 -48.729  1.00 33.24      A    C  
ATOM    105  CZ  TYR A 107      99.389  93.690 -49.678  1.00 34.52      A    C  
ATOM    106  OH  TYR A 107      99.411  93.268 -50.988  1.00 40.52      A    O  
ATOM    107  N   GLY A 108     101.347  97.166 -43.444  1.00 36.68      A    N  
ATOM    108  CA  GLY A 108     101.310  97.748 -42.111  1.00 38.30      A    C  
ATOM    109  C   GLY A 108     100.537  96.878 -41.139  1.00 39.17      A    C  
ATOM    110  O   GLY A 108      99.727  97.366 -40.349  1.00 43.68      A    O  
ATOM    111  N   PHE A 109     100.804  95.581 -41.198  1.00 37.61      A    N  
ATOM    112  CA  PHE A 109     100.152  94.599 -40.347  1.00 34.90      A    C  
ATOM    113  C   PHE A 109     100.595  94.679 -38.884  1.00 36.37      A    C  
ATOM    114  O   PHE A 109     101.784  94.777 -38.590  1.00 35.65      A    O  
ATOM    115  CB  PHE A 109     100.443  93.195 -40.897  1.00 32.34      A    C  
ATOM    116  CG  PHE A 109      99.760  92.092 -40.148  1.00 35.39      A    C  
ATOM    117  CD1 PHE A 109      98.376  91.927 -40.237  1.00 32.87      A    C  
ATOM    118  CD2 PHE A 109     100.496  91.217 -39.345  1.00 33.14      A    C  
ATOM    119  CE1 PHE A 109      97.730  90.909 -39.541  1.00 34.20      A    C  
ATOM    120  CE2 PHE A 109      99.860  90.195 -38.643  1.00 36.14      A    C  
ATOM    121  CZ  PHE A 109      98.471  90.039 -38.741  1.00 38.03      A    C  
ATOM    122  N   ARG A 110      99.629  94.645 -37.969  1.00 36.21      A    N  
ATOM    123  CA  ARG A 110      99.929  94.664 -36.539  1.00 38.98      A    C  
ATOM    124  C   ARG A 110      98.685  94.250 -35.757  1.00 38.16      A    C  
ATOM    125  O   ARG A 110      97.572  94.313 -36.269  1.00 38.14      A    O  
ATOM    126  CB  ARG A 110     100.426  96.046 -36.073  1.00 39.23      A    C  
ATOM    127  CG  ARG A 110      99.370  97.132 -35.947  1.00 44.61      A    C  
ATOM    128  CD  ARG A 110      99.168  97.888 -37.238  1.00 46.14      A    C  
ATOM    129  NE  ARG A 110      98.274  99.027 -37.041  1.00 51.30      A    N  
ATOM    130  CZ  ARG A 110      97.831  99.811 -38.021  1.00 52.84      A    C  
ATOM    131  NH1 ARG A 110      98.196  99.584 -39.278  1.00 47.73      A    N1+
ATOM    132  NH2 ARG A 110      97.019 100.822 -37.743  1.00 50.91      A    N  
ATOM    133  N   LEU A 111      98.875  93.806 -34.523  1.00 36.69      A    N  
ATOM    134  CA  LEU A 111      97.751  93.372 -33.710  1.00 38.60      A    C  
ATOM    135  C   LEU A 111      97.288  94.438 -32.726  1.00 40.27      A    C  
ATOM    136  O   LEU A 111      98.025  95.384 -32.409  1.00 42.13      A    O  
ATOM    137  CB  LEU A 111      98.124  92.113 -32.923  1.00 35.41      A    C  
ATOM    138  CG  LEU A 111      98.673  90.916 -33.696  1.00 37.15      A    C  
ATOM    139  CD1 LEU A 111      99.174  89.877 -32.706  1.00 31.83      A    C  
ATOM    140  CD2 LEU A 111      97.596  90.334 -34.602  1.00 29.75      A    C  
ATOM    141  N   GLY A 112      96.062  94.258 -32.244  1.00 37.57      A    N  
ATOM    142  CA  GLY A 112      95.479  95.160 -31.270  1.00 39.83      A    C  
ATOM    143  C   GLY A 112      94.619  94.332 -30.331  1.00 41.55      A    C  
ATOM    144  O   GLY A 112      94.047  93.325 -30.746  1.00 41.11      A    O  
ATOM    145  N   PHE A 113      94.526  94.734 -29.069  1.00 44.16      A    N  
ATOM    146  CA  PHE A 113      93.720  93.998 -28.106  1.00 48.86      A    C  
ATOM    147  C   PHE A 113      92.752  94.948 -27.409  1.00 55.91      A    C  
ATOM    148  O   PHE A 113      92.960  96.162 -27.398  1.00 58.84      A    O  
ATOM    149  CB  PHE A 113      94.625  93.297 -27.087  1.00 42.58      A    C  
ATOM    150  CG  PHE A 113      95.716  92.472 -27.717  1.00 39.92      A    C  
ATOM    151  CD1 PHE A 113      96.928  93.052 -28.073  1.00 32.80      A    C  
ATOM    152  CD2 PHE A 113      95.503  91.130 -28.023  1.00 39.30      A    C  
ATOM    153  CE1 PHE A 113      97.909  92.312 -28.721  1.00 35.82      A    C  
ATOM    154  CE2 PHE A 113      96.480  90.379 -28.672  1.00 35.33      A    C  
ATOM    155  CZ  PHE A 113      97.681  90.969 -29.025  1.00 35.64      A    C  
ATOM    156  N   LEU A 114      91.685  94.396 -26.844  1.00 62.73      A    N  
ATOM    157  CA  LEU A 114      90.688  95.212 -26.159  1.00 71.63      A    C  
ATOM    158  C   LEU A 114      91.096  95.445 -24.711  1.00 76.80      A    C  
ATOM    159  O   LEU A 114      91.893  94.686 -24.157  1.00 78.94      A    O  
ATOM    160  CB  LEU A 114      89.320  94.519 -26.208  1.00 70.04      A    C  
ATOM    161  CG  LEU A 114      88.686  94.354 -27.594  1.00 69.59      A    C  
ATOM    162  CD1 LEU A 114      87.449  93.464 -27.504  1.00 67.71      A    C  
ATOM    163  CD2 LEU A 114      88.330  95.721 -28.153  1.00 68.31      A    C  
ATOM    164  N   HIS A 115      90.560  96.503 -24.105  1.00 82.75      A    N  
ATOM    165  CA  HIS A 115      90.854  96.816 -22.708  1.00 88.79      A    C  
ATOM    166  C   HIS A 115      89.765  96.210 -21.816  1.00 91.23      A    C  
ATOM    167  O   HIS A 115      88.843  96.904 -21.371  1.00 91.86      A    O  
ATOM    168  CB  HIS A 115      90.930  98.334 -22.501  1.00 90.81      A    C  
ATOM    169  CG  HIS A 115      92.066  98.987 -23.230  1.00 94.57      A    C  
ATOM    170  CD2 HIS A 115      92.079  99.967 -24.167  1.00 95.33      A    C  
ATOM    171  ND1 HIS A 115      93.382  98.639 -23.021  1.00 95.33      A    N  
ATOM    172  CE1 HIS A 115      94.160  99.374 -23.796  1.00 95.33      A    C  
ATOM    173  NE2 HIS A 115      93.394 100.188 -24.502  1.00 95.33      A    N  
ATOM    174  N   SER A 116      89.885  94.905 -21.570  1.00 93.76      A    N  
ATOM    175  CA  SER A 116      88.935  94.149 -20.753  1.00 95.06      A    C  
ATOM    176  C   SER A 116      88.667  94.773 -19.385  1.00 95.33      A    C  
ATOM    177  O   SER A 116      89.552  94.824 -18.523  1.00 95.33      A    O  
ATOM    178  CB  SER A 116      89.438  92.713 -20.571  1.00 95.09      A    C  
ATOM    179  OG  SER A 116      90.722  92.696 -19.969  1.00 95.33      A    O  
ATOM    180  N   GLY A 117      87.432  95.235 -19.196  1.00 95.33      A    N  
ATOM    181  CA  GLY A 117      87.043  95.850 -17.940  1.00 95.33      A    C  
ATOM    182  C   GLY A 117      85.573  96.232 -17.934  1.00 95.33      A    C  
ATOM    183  O   GLY A 117      85.216  97.349 -17.546  1.00 95.33      A    O  
ATOM    184  N   THR A 118      84.721  95.304 -18.367  1.00 95.33      A    N  
ATOM    185  CA  THR A 118      83.278  95.536 -18.418  1.00 95.33      A    C  
ATOM    186  C   THR A 118      82.464  94.388 -17.802  1.00 95.33      A    C  
ATOM    187  O   THR A 118      81.800  94.572 -16.778  1.00 95.01      A    O  
ATOM    188  CB  THR A 118      82.793  95.770 -19.885  1.00 95.33      A    C  
ATOM    189  CG2 THR A 118      83.389  97.059 -20.450  1.00 94.69      A    C  
ATOM    190  OG1 THR A 118      83.181  94.661 -20.711  1.00 95.33      A    O  
ATOM    191  N   ALA A 119      82.519  93.212 -18.428  1.00 95.33      A    N  
ATOM    192  CA  ALA A 119      81.780  92.047 -17.943  1.00 95.33      A    C  
ATOM    193  C   ALA A 119      82.610  90.760 -17.950  1.00 95.33      A    C  
ATOM    194  O   ALA A 119      82.810  90.138 -16.902  1.00 95.33      A    O  
ATOM    195  CB  ALA A 119      80.509  91.855 -18.776  1.00 94.63      A    C  
ATOM    196  N   LYS A 120      83.087  90.360 -19.129  1.00 95.33      A    N  
ATOM    197  CA  LYS A 120      83.889  89.143 -19.269  1.00 95.33      A    C  
ATOM    198  C   LYS A 120      85.371  89.411 -19.012  1.00 95.33      A    C  
ATOM    199  O   LYS A 120      86.240  88.669 -19.478  1.00 95.26      A    O  
ATOM    200  CB  LYS A 120      83.708  88.550 -20.674  1.00 95.33      A    C  
ATOM    201  CG  LYS A 120      82.265  88.190 -21.019  1.00 95.33      A    C  
ATOM    202  CD  LYS A 120      82.159  87.560 -22.402  1.00 95.33      A    C  
ATOM    203  CE  LYS A 120      80.722  87.187 -22.740  1.00 93.93      A    C  
ATOM    204  NZ  LYS A 120      80.611  86.553 -24.087  1.00 92.54      A    N1+
ATOM    205  N   SER A 121      85.644  90.470 -18.252  1.00 94.78      A    N  
ATOM    206  CA  SER A 121      87.008  90.879 -17.920  1.00 93.73      A    C  
ATOM    207  C   SER A 121      87.664  90.046 -16.816  1.00 91.34      A    C  
ATOM    208  O   SER A 121      88.706  90.425 -16.278  1.00 90.79      A    O  
ATOM    209  CB  SER A 121      87.020  92.361 -17.519  1.00 95.33      A    C  
ATOM    210  OG  SER A 121      86.121  92.619 -16.450  1.00 95.33      A    O  
ATOM    211  N   VAL A 122      87.053  88.915 -16.479  1.00 89.03      A    N  
ATOM    212  CA  VAL A 122      87.597  88.041 -15.445  1.00 85.26      A    C  
ATOM    213  C   VAL A 122      88.143  86.770 -16.094  1.00 81.40      A    C  
ATOM    214  O   VAL A 122      89.079  86.150 -15.591  1.00 81.11      A    O  
ATOM    215  CB  VAL A 122      86.510  87.668 -14.391  1.00 85.94      A    C  
ATOM    216  CG1 VAL A 122      85.359  86.924 -15.059  1.00 85.74      A    C  
ATOM    217  CG2 VAL A 122      87.122  86.830 -13.275  1.00 85.96      A    C  
ATOM    218  N   THR A 123      87.556  86.405 -17.229  1.00 76.61      A    N  
ATOM    219  CA  THR A 123      87.957  85.212 -17.958  1.00 71.26      A    C  
ATOM    220  C   THR A 123      89.098  85.491 -18.924  1.00 67.64      A    C  
ATOM    221  O   THR A 123      89.748  84.559 -19.398  1.00 67.21      A    O  
ATOM    222  CB  THR A 123      86.790  84.650 -18.795  1.00 71.96      A    C  
ATOM    223  CG2 THR A 123      85.586  84.362 -17.913  1.00 72.64      A    C  
ATOM    224  OG1 THR A 123      86.421  85.606 -19.800  1.00 72.01      A    O  
ATOM    225  N   CYS A 124      89.344  86.765 -19.215  1.00 61.72      A    N  
ATOM    226  CA  CYS A 124      90.384  87.127 -20.172  1.00 57.56      A    C  
ATOM    227  C   CYS A 124      90.813  88.588 -20.082  1.00 52.87      A    C  
ATOM    228  O   CYS A 124      90.009  89.488 -20.303  1.00 52.46      A    O  
ATOM    229  CB  CYS A 124      89.865  86.825 -21.581  1.00 58.60      A    C  
ATOM    230  SG  CYS A 124      90.850  87.472 -22.928  1.00 66.36      A    S  
ATOM    231  N   THR A 125      92.084  88.828 -19.774  1.00 50.28      A    N  
ATOM    232  CA  THR A 125      92.582  90.200 -19.663  1.00 48.20      A    C  
ATOM    233  C   THR A 125      93.972  90.385 -20.258  1.00 46.35      A    C  
ATOM    234  O   THR A 125      94.838  89.522 -20.094  1.00 47.13      A    O  
ATOM    235  CB  THR A 125      92.623  90.662 -18.198  1.00 48.62      A    C  
ATOM    236  CG2 THR A 125      93.531  89.752 -17.372  1.00 47.01      A    C  
ATOM    237  OG1 THR A 125      93.117  92.004 -18.139  1.00 47.70      A    O  
ATOM    238  N   TYR A 126      94.176  91.525 -20.923  1.00 44.94      A    N  
ATOM    239  CA  TYR A 126      95.444  91.858 -21.588  1.00 43.47      A    C  
ATOM    240  C   TYR A 126      96.270  92.945 -20.897  1.00 44.58      A    C  
ATOM    241  O   TYR A 126      95.740  93.968 -20.473  1.00 45.96      A    O  
ATOM    242  CB  TYR A 126      95.168  92.305 -23.026  1.00 41.87      A    C  
ATOM    243  CG  TYR A 126      96.400  92.747 -23.792  1.00 40.68      A    C  
ATOM    244  CD1 TYR A 126      97.342  91.817 -24.230  1.00 38.12      A    C  
ATOM    245  CD2 TYR A 126      96.615  94.093 -24.091  1.00 39.41      A    C  
ATOM    246  CE1 TYR A 126      98.468  92.211 -24.951  1.00 38.73      A    C  
ATOM    247  CE2 TYR A 126      97.745  94.502 -24.811  1.00 38.30      A    C  
ATOM    248  CZ  TYR A 126      98.666  93.551 -25.238  1.00 41.59      A    C  
ATOM    249  OH  TYR A 126      99.785  93.930 -25.952  1.00 40.56      A    O  
ATOM    250  N   SER A 127      97.578  92.725 -20.818  1.00 46.15      A    N  
ATOM    251  CA  SER A 127      98.495  93.673 -20.193  1.00 45.63      A    C  
ATOM    252  C   SER A 127      99.367  94.364 -21.232  1.00 46.25      A    C  
ATOM    253  O   SER A 127     100.256  93.745 -21.814  1.00 45.79      A    O  
ATOM    254  CB  SER A 127      99.401  92.949 -19.191  1.00 46.85      A    C  
ATOM    255  OG  SER A 127     100.544  93.732 -18.888  1.00 44.18      A    O  
ATOM    256  N   PRO A 128      99.129  95.661 -21.476  1.00 45.65      A    N  
ATOM    257  CA  PRO A 128      99.942  96.371 -22.470  1.00 46.99      A    C  
ATOM    258  C   PRO A 128     101.385  96.489 -22.019  1.00 46.84      A    C  
ATOM    259  O   PRO A 128     102.304  96.412 -22.830  1.00 48.72      A    O  
ATOM    260  CB  PRO A 128      99.271  97.744 -22.564  1.00 44.61      A    C  
ATOM    261  CG  PRO A 128      97.865  97.480 -22.150  1.00 45.66      A    C  
ATOM    262  CD  PRO A 128      98.026  96.510 -21.000  1.00 47.38      A    C  
ATOM    263  N   ALA A 129     101.579  96.683 -20.718  1.00 48.12      A    N  
ATOM    264  CA  ALA A 129     102.916  96.836 -20.164  1.00 49.65      A    C  
ATOM    265  C   ALA A 129     103.789  95.617 -20.432  1.00 49.80      A    C  
ATOM    266  O   ALA A 129     104.989  95.748 -20.693  1.00 51.24      A    O  
ATOM    267  CB  ALA A 129     102.829  97.109 -18.670  1.00 50.51      A    C  
ATOM    268  N   LEU A 130     103.187  94.433 -20.381  1.00 48.14      A    N  
ATOM    269  CA  LEU A 130     103.930  93.196 -20.617  1.00 47.63      A    C  
ATOM    270  C   LEU A 130     103.709  92.621 -22.021  1.00 45.47      A    C  
ATOM    271  O   LEU A 130     104.449  91.734 -22.444  1.00 46.46      A    O  
ATOM    272  CB  LEU A 130     103.513  92.142 -19.585  1.00 46.01      A    C  
ATOM    273  CG  LEU A 130     103.692  92.457 -18.098  1.00 45.73      A    C  
ATOM    274  CD1 LEU A 130     102.724  91.636 -17.270  1.00 44.33      A    C  
ATOM    275  CD2 LEU A 130     105.117  92.167 -17.682  1.00 48.68      A    C  
ATOM    276  N   ASN A 131     102.707  93.142 -22.735  1.00 44.25      A    N  
ATOM    277  CA  ASN A 131     102.318  92.643 -24.069  1.00 42.21      A    C  
ATOM    278  C   ASN A 131     102.013  91.159 -23.884  1.00 41.12      A    C  
ATOM    279  O   ASN A 131     102.483  90.299 -24.634  1.00 39.21      A    O  
ATOM    280  CB  ASN A 131     103.428  92.825 -25.113  1.00 39.57      A    C  
ATOM    281  CG  ASN A 131     103.016  92.306 -26.492  1.00 41.64      A    C  
ATOM    282  ND2 ASN A 131     103.968  91.750 -27.233  1.00 42.78      A    N  
ATOM    283  OD1 ASN A 131     101.853  92.413 -26.882  1.00 43.82      A    O  
ATOM    284  N   LYS A 132     101.206  90.885 -22.863  1.00 39.12      A    N  
ATOM    285  CA  LYS A 132     100.852  89.531 -22.494  1.00 38.38      A    C  
ATOM    286  C   LYS A 132      99.363  89.359 -22.213  1.00 35.88      A    C  
ATOM    287  O   LYS A 132      98.763  90.143 -21.486  1.00 35.97      A    O  
ATOM    288  CB  LYS A 132     101.682  89.145 -21.264  1.00 36.00      A    C  
ATOM    289  CG  LYS A 132     101.496  87.732 -20.754  1.00 40.27      A    C  
ATOM    290  CD  LYS A 132     102.621  87.365 -19.786  1.00 41.75      A    C  
ATOM    291  CE  LYS A 132     102.347  86.044 -19.074  1.00 42.84      A    C  
ATOM    292  NZ  LYS A 132     103.487  85.641 -18.208  1.00 40.39      A    N1+
ATOM    293  N   MET A 133      98.783  88.315 -22.793  1.00 33.97      A    N  
ATOM    294  CA  MET A 133      97.373  88.007 -22.614  1.00 37.20      A    C  
ATOM    295  C   MET A 133      97.201  86.949 -21.511  1.00 36.68      A    C  
ATOM    296  O   MET A 133      97.881  85.922 -21.518  1.00 40.76      A    O  
ATOM    297  CB  MET A 133      96.798  87.490 -23.939  1.00 38.71      A    C  
ATOM    298  CG  MET A 133      95.304  87.200 -23.928  1.00 42.17      A    C  
ATOM    299  SD  MET A 133      94.274  88.668 -23.629  1.00 51.29      A    S  
ATOM    300  CE  MET A 133      94.405  89.494 -25.218  1.00 46.58      A    C  
ATOM    301  N   PHE A 134      96.313  87.214 -20.555  1.00 35.43      A    N  
ATOM    302  CA  PHE A 134      96.044  86.276 -19.464  1.00 33.50      A    C  
ATOM    303  C   PHE A 134      94.627  85.765 -19.686  1.00 35.25      A    C  
ATOM    304  O   PHE A 134      93.685  86.552 -19.742  1.00 33.93      A    O  
ATOM    305  CB  PHE A 134      96.139  86.975 -18.098  1.00 32.76      A    C  
ATOM    306  CG  PHE A 134      97.517  87.496 -17.769  1.00 30.94      A    C  
ATOM    307  CD1 PHE A 134      98.021  88.630 -18.401  1.00 28.89      A    C  
ATOM    308  CD2 PHE A 134      98.320  86.835 -16.835  1.00 30.67      A    C  
ATOM    309  CE1 PHE A 134      99.304  89.102 -18.110  1.00 31.91      A    C  
ATOM    310  CE2 PHE A 134      99.609  87.298 -16.530  1.00 29.06      A    C  
ATOM    311  CZ  PHE A 134     100.104  88.434 -17.170  1.00 29.62      A    C  
ATOM    312  N   VAL A 135      94.466  84.453 -19.802  1.00 35.66      A    N  
ATOM    313  CA  VAL A 135      93.145  83.899 -20.066  1.00 35.62      A    C  
ATOM    314  C   VAL A 135      92.921  82.500 -19.477  1.00 37.18      A    C  
ATOM    315  O   VAL A 135      93.870  81.760 -19.240  1.00 40.01      A    O  
ATOM    316  CB  VAL A 135      92.918  83.824 -21.583  1.00 35.80      A    C  
ATOM    317  CG1 VAL A 135      93.917  82.850 -22.191  1.00 29.30      A    C  
ATOM    318  CG2 VAL A 135      91.477  83.407 -21.891  1.00 35.37      A    C  
ATOM    319  N   GLN A 136      91.661  82.142 -19.252  1.00 37.85      A    N  
ATOM    320  CA  GLN A 136      91.333  80.832 -18.706  1.00 39.73      A    C  
ATOM    321  C   GLN A 136      91.309  79.769 -19.792  1.00 40.99      A    C  
ATOM    322  O   GLN A 136      91.123  80.064 -20.976  1.00 42.45      A    O  
ATOM    323  CB  GLN A 136      89.969  80.848 -18.016  1.00 39.73      A    C  
ATOM    324  CG  GLN A 136      89.887  81.719 -16.788  1.00 47.84      A    C  
ATOM    325  CD  GLN A 136      88.612  81.474 -15.998  1.00 52.37      A    C  
ATOM    326  NE2 GLN A 136      88.760  81.156 -14.716  1.00 55.38      A    N  
ATOM    327  OE1 GLN A 136      87.509  81.568 -16.534  1.00 55.25      A    O  
ATOM    328  N   LEU A 137      91.492  78.526 -19.371  1.00 38.95      A    N  
ATOM    329  CA  LEU A 137      91.492  77.389 -20.276  1.00 40.47      A    C  
ATOM    330  C   LEU A 137      90.217  77.309 -21.124  1.00 40.67      A    C  
ATOM    331  O   LEU A 137      89.104  77.389 -20.610  1.00 41.34      A    O  
ATOM    332  CB  LEU A 137      91.668  76.109 -19.453  1.00 40.56      A    C  
ATOM    333  CG  LEU A 137      91.388  74.738 -20.063  1.00 45.10      A    C  
ATOM    334  CD1 LEU A 137      92.105  74.597 -21.389  1.00 51.31      A    C  
ATOM    335  CD2 LEU A 137      91.842  73.660 -19.089  1.00 48.14      A    C  
ATOM    336  N   ALA A 138      90.394  77.168 -22.432  1.00 41.36      A    N  
ATOM    337  CA  ALA A 138      89.280  77.048 -23.366  1.00 43.25      A    C  
ATOM    338  C   ALA A 138      88.283  78.211 -23.404  1.00 42.66      A    C  
ATOM    339  O   ALA A 138      87.157  78.039 -23.861  1.00 44.99      A    O  
ATOM    340  CB  ALA A 138      88.537  75.740 -23.107  1.00 41.82      A    C  
ATOM    341  N   LYS A 139      88.684  79.385 -22.934  1.00 45.01      A    N  
ATOM    342  CA  LYS A 139      87.798  80.546 -22.972  1.00 44.78      A    C  
ATOM    343  C   LYS A 139      88.193  81.442 -24.140  1.00 44.73      A    C  
ATOM    344  O   LYS A 139      89.377  81.599 -24.451  1.00 42.55      A    O  
ATOM    345  CB  LYS A 139      87.875  81.336 -21.664  1.00 47.36      A    C  
ATOM    346  CG  LYS A 139      87.374  80.565 -20.443  1.00 56.74      A    C  
ATOM    347  CD  LYS A 139      85.867  80.331 -20.486  1.00 58.25      A    C  
ATOM    348  CE  LYS A 139      85.431  79.337 -19.412  1.00 61.03      A    C  
ATOM    349  NZ  LYS A 139      85.816  79.768 -18.034  1.00 64.80      A    N1+
ATOM    350  N   THR A 140      87.185  82.033 -24.769  1.00 44.88      A    N  
ATOM    351  CA  THR A 140      87.353  82.906 -25.923  1.00 44.38      A    C  
ATOM    352  C   THR A 140      88.311  84.068 -25.727  1.00 42.87      A    C  
ATOM    353  O   THR A 140      88.217  84.800 -24.744  1.00 45.10      A    O  
ATOM    354  CB  THR A 140      85.993  83.470 -26.353  1.00 45.76      A    C  
ATOM    355  CG2 THR A 140      86.116  84.255 -27.650  1.00 47.71      A    C  
ATOM    356  OG1 THR A 140      85.085  82.382 -26.551  1.00 44.33      A    O  
ATOM    357  N   VAL A 141      89.225  84.233 -26.678  1.00 40.44      A    N  
ATOM    358  CA  VAL A 141      90.202  85.321 -26.639  1.00 40.06      A    C  
ATOM    359  C   VAL A 141      90.093  86.123 -27.938  1.00 40.38      A    C  
ATOM    360  O   VAL A 141      90.459  85.638 -29.009  1.00 38.29      A    O  
ATOM    361  CB  VAL A 141      91.659  84.784 -26.517  1.00 38.40      A    C  
ATOM    362  CG1 VAL A 141      92.635  85.935 -26.426  1.00 43.41      A    C  
ATOM    363  CG2 VAL A 141      91.792  83.903 -25.298  1.00 41.00      A    C  
ATOM    364  N   PRO A 142      89.567  87.355 -27.864  1.00 41.23      A    N  
ATOM    365  CA  PRO A 142      89.452  88.152 -29.088  1.00 39.79      A    C  
ATOM    366  C   PRO A 142      90.720  88.926 -29.416  1.00 40.01      A    C  
ATOM    367  O   PRO A 142      91.306  89.567 -28.546  1.00 43.42      A    O  
ATOM    368  CB  PRO A 142      88.272  89.066 -28.787  1.00 38.03      A    C  
ATOM    369  CG  PRO A 142      88.403  89.295 -27.317  1.00 39.72      A    C  
ATOM    370  CD  PRO A 142      88.717  87.911 -26.795  1.00 40.78      A    C  
ATOM    371  N   VAL A 143      91.139  88.857 -30.677  1.00 40.44      A    N  
ATOM    372  CA  VAL A 143      92.332  89.555 -31.146  1.00 39.28      A    C  
ATOM    373  C   VAL A 143      91.972  90.379 -32.383  1.00 41.59      A    C  
ATOM    374  O   VAL A 143      91.203  89.930 -33.238  1.00 41.45      A    O  
ATOM    375  CB  VAL A 143      93.464  88.566 -31.508  1.00 42.11      A    C  
ATOM    376  CG1 VAL A 143      94.695  89.337 -31.969  1.00 37.72      A    C  
ATOM    377  CG2 VAL A 143      93.801  87.683 -30.301  1.00 37.23      A    C  
ATOM    378  N   GLN A 144      92.534  91.580 -32.476  1.00 40.10      A    N  
ATOM    379  CA  GLN A 144      92.247  92.477 -33.588  1.00 41.20      A    C  
ATOM    380  C   GLN A 144      93.379  92.577 -34.596  1.00 42.22      A    C  
ATOM    381  O   GLN A 144      94.549  92.729 -34.231  1.00 41.34      A    O  
ATOM    382  CB  GLN A 144      91.920  93.869 -33.048  1.00 39.24      A    C  
ATOM    383  CG  GLN A 144      90.701  93.896 -32.138  1.00 48.32      A    C  
ATOM    384  CD  GLN A 144      90.617  95.166 -31.298  1.00 54.82      A    C  
ATOM    385  NE2 GLN A 144      91.765  95.799 -31.054  1.00 54.84      A    N  
ATOM    386  OE1 GLN A 144      89.532  95.565 -30.866  1.00 60.99      A    O  
ATOM    387  N   LEU A 145      93.018  92.495 -35.871  1.00 42.17      A    N  
ATOM    388  CA  LEU A 145      93.984  92.586 -36.959  1.00 43.27      A    C  
ATOM    389  C   LEU A 145      93.855  93.944 -37.631  1.00 40.93      A    C  
ATOM    390  O   LEU A 145      92.770  94.329 -38.041  1.00 40.69      A    O  
ATOM    391  CB  LEU A 145      93.714  91.489 -37.992  1.00 42.78      A    C  
ATOM    392  CG  LEU A 145      94.311  90.092 -37.832  1.00 46.04      A    C  
ATOM    393  CD1 LEU A 145      94.379  89.677 -36.377  1.00 45.19      A    C  
ATOM    394  CD2 LEU A 145      93.463  89.130 -38.656  1.00 45.43      A    C  
ATOM    395  N   TYR A 146      94.953  94.677 -37.732  1.00 43.67      A    N  
ATOM    396  CA  TYR A 146      94.919  95.972 -38.398  1.00 44.81      A    C  
ATOM    397  C   TYR A 146      95.788  95.904 -39.644  1.00 47.35      A    C  
ATOM    398  O   TYR A 146      96.868  95.309 -39.632  1.00 49.10      A    O  
ATOM    399  CB  TYR A 146      95.443  97.088 -37.494  1.00 45.30      A    C  
ATOM    400  CG  TYR A 146      94.565  97.428 -36.312  1.00 47.91      A    C  
ATOM    401  CD1 TYR A 146      94.535  96.615 -35.183  1.00 44.65      A    C  
ATOM    402  CD2 TYR A 146      93.791  98.589 -36.308  1.00 45.93      A    C  
ATOM    403  CE1 TYR A 146      93.765  96.953 -34.077  1.00 48.43      A    C  
ATOM    404  CE2 TYR A 146      93.017  98.935 -35.206  1.00 48.60      A    C  
ATOM    405  CZ  TYR A 146      93.010  98.115 -34.093  1.00 48.74      A    C  
ATOM    406  OH  TYR A 146      92.260  98.465 -32.991  1.00 52.29      A    O  
ATOM    407  N   VAL A 147      95.319  96.528 -40.716  1.00 48.22      A    N  
ATOM    408  CA  VAL A 147      96.048  96.533 -41.968  1.00 47.72      A    C  
ATOM    409  C   VAL A 147      95.761  97.868 -42.664  1.00 50.46      A    C  
ATOM    410  O   VAL A 147      94.620  98.326 -42.688  1.00 51.58      A    O  
ATOM    411  CB  VAL A 147      95.610  95.309 -42.817  1.00 47.18      A    C  
ATOM    412  CG1 VAL A 147      94.726  95.735 -43.977  1.00 43.97      A    C  
ATOM    413  CG2 VAL A 147      96.824  94.540 -43.272  1.00 46.86      A    C  
ATOM    414  N   ASP A 148      96.805  98.497 -43.205  1.00 53.07      A    N  
ATOM    415  CA  ASP A 148      96.693  99.789 -43.887  1.00 51.26      A    C  
ATOM    416  C   ASP A 148      95.974  99.773 -45.233  1.00 52.50      A    C  
ATOM    417  O   ASP A 148      95.256 100.718 -45.564  1.00 53.72      A    O  
ATOM    418  CB  ASP A 148      98.083 100.393 -44.057  1.00 52.46      A    C  
ATOM    419  CG  ASP A 148      98.664 100.871 -42.747  1.00 52.40      A    C  
ATOM    420  OD1 ASP A 148      99.891 101.103 -42.679  1.00 53.93      A    O  
ATOM    421  OD2 ASP A 148      97.887 101.022 -41.783  1.00 49.62      A    O1-
ATOM    422  N   SER A 149      96.186  98.719 -46.014  1.00 52.79      A    N  
ATOM    423  CA  SER A 149      95.523  98.575 -47.308  1.00 55.21      A    C  
ATOM    424  C   SER A 149      95.076  97.129 -47.432  1.00 54.01      A    C  
ATOM    425  O   SER A 149      95.711  96.235 -46.883  1.00 56.79      A    O  
ATOM    426  CB  SER A 149      96.466  98.954 -48.455  1.00 55.95      A    C  
ATOM    427  OG  SER A 149      97.722  98.312 -48.330  1.00 60.50      A    O  
ATOM    428  N   THR A 150      93.980  96.901 -48.143  1.00 55.04      A    N  
ATOM    429  CA  THR A 150      93.443  95.559 -48.296  1.00 55.37      A    C  
ATOM    430  C   THR A 150      94.408  94.583 -48.959  1.00 53.12      A    C  
ATOM    431  O   THR A 150      94.847  94.795 -50.088  1.00 54.17      A    O  
ATOM    432  CB  THR A 150      92.123  95.585 -49.095  1.00 57.15      A    C  
ATOM    433  CG2 THR A 150      91.070  96.438 -48.368  1.00 57.99      A    C  
ATOM    434  OG1 THR A 150      92.365  96.145 -50.392  1.00 63.78      A    O  
ATOM    435  N   PRO A 151      94.752  93.495 -48.254  1.00 52.11      A    N  
ATOM    436  CA  PRO A 151      95.667  92.466 -48.761  1.00 51.95      A    C  
ATOM    437  C   PRO A 151      95.116  91.855 -50.047  1.00 50.16      A    C  
ATOM    438  O   PRO A 151      93.935  91.990 -50.340  1.00 47.52      A    O  
ATOM    439  CB  PRO A 151      95.708  91.450 -47.620  1.00 51.28      A    C  
ATOM    440  CG  PRO A 151      95.486  92.301 -46.408  1.00 52.31      A    C  
ATOM    441  CD  PRO A 151      94.379  93.222 -46.855  1.00 50.46      A    C  
ATOM    442  N   PRO A 152      95.964  91.155 -50.818  1.00 52.93      A    N  
ATOM    443  CA  PRO A 152      95.530  90.532 -52.075  1.00 51.78      A    C  
ATOM    444  C   PRO A 152      94.623  89.313 -51.888  1.00 53.81      A    C  
ATOM    445  O   PRO A 152      94.560  88.722 -50.808  1.00 53.85      A    O  
ATOM    446  CB  PRO A 152      96.850  90.168 -52.741  1.00 49.42      A    C  
ATOM    447  CG  PRO A 152      97.697  89.769 -51.560  1.00 52.99      A    C  
ATOM    448  CD  PRO A 152      97.389  90.874 -50.556  1.00 51.39      A    C  
ATOM    449  N   PRO A 153      93.901  88.923 -52.950  1.00 54.86      A    N  
ATOM    450  CA  PRO A 153      93.002  87.765 -52.889  1.00 52.19      A    C  
ATOM    451  C   PRO A 153      93.741  86.515 -52.431  1.00 50.05      A    C  
ATOM    452  O   PRO A 153      94.831  86.226 -52.928  1.00 51.86      A    O  
ATOM    453  CB  PRO A 153      92.515  87.633 -54.331  1.00 52.80      A    C  
ATOM    454  CG  PRO A 153      92.494  89.055 -54.808  1.00 55.75      A    C  
ATOM    455  CD  PRO A 153      93.805  89.596 -54.261  1.00 56.12      A    C  
ATOM    456  N   GLY A 154      93.154  85.783 -51.486  1.00 46.43      A    N  
ATOM    457  CA  GLY A 154      93.781  84.560 -51.013  1.00 41.72      A    C  
ATOM    458  C   GLY A 154      94.769  84.723 -49.872  1.00 41.90      A    C  
ATOM    459  O   GLY A 154      95.551  83.815 -49.595  1.00 40.44      A    O  
ATOM    460  N   THR A 155      94.755  85.879 -49.218  1.00 40.11      A    N  
ATOM    461  CA  THR A 155      95.645  86.113 -48.084  1.00 39.33      A    C  
ATOM    462  C   THR A 155      95.095  85.336 -46.885  1.00 39.28      A    C  
ATOM    463  O   THR A 155      93.880  85.257 -46.685  1.00 35.09      A    O  
ATOM    464  CB  THR A 155      95.718  87.618 -47.721  1.00 38.82      A    C  
ATOM    465  CG2 THR A 155      96.419  87.822 -46.396  1.00 35.91      A    C  
ATOM    466  OG1 THR A 155      96.433  88.324 -48.745  1.00 44.23      A    O  
ATOM    467  N   ARG A 156      95.988  84.751 -46.095  1.00 39.19      A    N  
ATOM    468  CA  ARG A 156      95.563  83.988 -44.930  1.00 38.17      A    C  
ATOM    469  C   ARG A 156      96.209  84.506 -43.649  1.00 38.54      A    C  
ATOM    470  O   ARG A 156      97.182  85.267 -43.686  1.00 37.59      A    O  
ATOM    471  CB  ARG A 156      95.917  82.518 -45.107  1.00 35.43      A    C  
ATOM    472  CG  ARG A 156      95.276  81.845 -46.307  1.00 38.22      A    C  
ATOM    473  CD  ARG A 156      95.948  80.495 -46.539  1.00 38.93      A    C  
ATOM    474  NE  ARG A 156      95.138  79.370 -46.085  1.00 41.96      A    N  
ATOM    475  CZ  ARG A 156      95.588  78.124 -45.971  1.00 42.12      A    C  
ATOM    476  NH1 ARG A 156      96.854  77.837 -46.263  1.00 34.25      A    N1+
ATOM    477  NH2 ARG A 156      94.758  77.153 -45.603  1.00 41.21      A    N  
ATOM    478  N   VAL A 157      95.651  84.084 -42.520  1.00 36.35      A    N  
ATOM    479  CA  VAL A 157      96.158  84.464 -41.213  1.00 33.35      A    C  
ATOM    480  C   VAL A 157      96.434  83.170 -40.455  1.00 34.12      A    C  
ATOM    481  O   VAL A 157      95.542  82.330 -40.323  1.00 37.68      A    O  
ATOM    482  CB  VAL A 157      95.122  85.298 -40.433  1.00 38.44      A    C  
ATOM    483  CG1 VAL A 157      95.724  85.767 -39.112  1.00 34.20      A    C  
ATOM    484  CG2 VAL A 157      94.661  86.495 -41.277  1.00 34.38      A    C  
ATOM    485  N   ARG A 158      97.659  83.006 -39.962  1.00 30.06      A    N  
ATOM    486  CA  ARG A 158      98.041  81.802 -39.237  1.00 27.38      A    C  
ATOM    487  C   ARG A 158      98.493  82.120 -37.813  1.00 30.67      A    C  
ATOM    488  O   ARG A 158      99.103  83.164 -37.562  1.00 29.56      A    O  
ATOM    489  CB  ARG A 158      99.178  81.099 -39.987  1.00 30.52      A    C  
ATOM    490  CG  ARG A 158      99.638  79.767 -39.393  1.00 29.61      A    C  
ATOM    491  CD  ARG A 158     100.873  79.235 -40.130  1.00 26.28      A    C  
ATOM    492  NE  ARG A 158     100.631  79.078 -41.559  1.00 34.31      A    N  
ATOM    493  CZ  ARG A 158      99.996  78.045 -42.117  1.00 39.26      A    C  
ATOM    494  NH1 ARG A 158      99.534  77.046 -41.372  1.00 35.21      A    N1+
ATOM    495  NH2 ARG A 158      99.795  78.024 -43.427  1.00 39.48      A    N  
ATOM    496  N   ALA A 159      98.189  81.215 -36.884  1.00 30.59      A    N  
ATOM    497  CA  ALA A 159      98.590  81.374 -35.481  1.00 30.13      A    C  
ATOM    498  C   ALA A 159      99.407  80.152 -35.048  1.00 30.23      A    C  
ATOM    499  O   ALA A 159      99.035  79.003 -35.324  1.00 28.71      A    O  
ATOM    500  CB  ALA A 159      97.359  81.538 -34.579  1.00 29.97      A    C  
ATOM    501  N   MET A 160     100.523  80.406 -34.372  1.00 29.89      A    N  
ATOM    502  CA  MET A 160     101.418  79.339 -33.930  1.00 28.65      A    C  
ATOM    503  C   MET A 160     102.041  79.721 -32.599  1.00 30.40      A    C  
ATOM    504  O   MET A 160     102.368  80.882 -32.376  1.00 33.20      A    O  
ATOM    505  CB  MET A 160     102.517  79.132 -34.973  1.00 26.80      A    C  
ATOM    506  CG  MET A 160     103.484  78.005 -34.684  1.00 30.98      A    C  
ATOM    507  SD  MET A 160     104.850  78.022 -35.895  1.00 37.16      A    S  
ATOM    508  CE  MET A 160     104.094  77.238 -37.302  1.00 31.83      A    C  
ATOM    509  N   ALA A 161     102.205  78.748 -31.709  1.00 30.61      A    N  
ATOM    510  CA  ALA A 161     102.802  79.035 -30.415  1.00 27.98      A    C  
ATOM    511  C   ALA A 161     104.211  78.470 -30.351  1.00 27.67      A    C  
ATOM    512  O   ALA A 161     104.496  77.438 -30.953  1.00 28.00      A    O  
ATOM    513  CB  ALA A 161     101.951  78.439 -29.310  1.00 27.60      A    C  
ATOM    514  N   ILE A 162     105.099  79.167 -29.646  1.00 28.54      A    N  
ATOM    515  CA  ILE A 162     106.474  78.707 -29.455  1.00 26.55      A    C  
ATOM    516  C   ILE A 162     106.851  79.045 -28.026  1.00 27.22      A    C  
ATOM    517  O   ILE A 162     106.305  79.979 -27.442  1.00 27.86      A    O  
ATOM    518  CB  ILE A 162     107.493  79.411 -30.384  1.00 28.49      A    C  
ATOM    519  CG1 ILE A 162     107.600  80.887 -30.026  1.00 28.43      A    C  
ATOM    520  CG2 ILE A 162     107.096  79.239 -31.835  1.00 31.73      A    C  
ATOM    521  CD1 ILE A 162     108.780  81.560 -30.693  1.00 34.71      A    C  
ATOM    522  N   TYR A 163     107.770  78.289 -27.447  1.00 28.84      A    N  
ATOM    523  CA  TYR A 163     108.180  78.581 -26.081  1.00 29.30      A    C  
ATOM    524  C   TYR A 163     109.031  79.838 -26.107  1.00 29.26      A    C  
ATOM    525  O   TYR A 163     109.809  80.041 -27.029  1.00 29.49      A    O  
ATOM    526  CB  TYR A 163     108.955  77.397 -25.503  1.00 31.59      A    C  
ATOM    527  CG  TYR A 163     108.054  76.253 -25.101  1.00 27.12      A    C  
ATOM    528  CD1 TYR A 163     107.150  76.400 -24.062  1.00 28.08      A    C  
ATOM    529  CD2 TYR A 163     108.071  75.040 -25.794  1.00 28.85      A    C  
ATOM    530  CE1 TYR A 163     106.276  75.382 -23.712  1.00 27.28      A    C  
ATOM    531  CE2 TYR A 163     107.193  74.009 -25.450  1.00 29.28      A    C  
ATOM    532  CZ  TYR A 163     106.297  74.192 -24.404  1.00 28.16      A    C  
ATOM    533  OH  TYR A 163     105.416  73.190 -24.040  1.00 32.51      A    O  
ATOM    534  N   LYS A 164     108.872  80.684 -25.099  1.00 32.67      A    N  
ATOM    535  CA  LYS A 164     109.600  81.951 -25.013  1.00 35.30      A    C  
ATOM    536  C   LYS A 164     111.065  81.839 -24.570  1.00 35.32      A    C  
ATOM    537  O   LYS A 164     111.920  82.565 -25.064  1.00 39.39      A    O  
ATOM    538  CB  LYS A 164     108.844  82.893 -24.072  1.00 38.41      A    C  
ATOM    539  CG  LYS A 164     109.485  84.246 -23.855  1.00 41.37      A    C  
ATOM    540  CD  LYS A 164     108.740  85.015 -22.775  1.00 46.02      A    C  
ATOM    541  CE  LYS A 164     109.369  86.372 -22.510  1.00 47.83      A    C  
ATOM    542  NZ  LYS A 164     108.797  87.011 -21.291  1.00 50.76      A    N1+
ATOM    543  N   GLN A 165     111.356  80.939 -23.638  1.00 37.29      A    N  
ATOM    544  CA  GLN A 165     112.722  80.757 -23.146  1.00 35.14      A    C  
ATOM    545  C   GLN A 165     113.600  80.035 -24.162  1.00 38.73      A    C  
ATOM    546  O   GLN A 165     113.153  79.121 -24.855  1.00 39.93      A    O  
ATOM    547  CB  GLN A 165     112.700  79.987 -21.827  1.00 32.82      A    C  
ATOM    548  CG  GLN A 165     111.979  80.733 -20.714  1.00 35.42      A    C  
ATOM    549  CD  GLN A 165     111.479  79.816 -19.611  1.00 41.45      A    C  
ATOM    550  NE2 GLN A 165     111.879  80.102 -18.377  1.00 46.11      A    N  
ATOM    551  OE1 GLN A 165     110.730  78.866 -19.863  1.00 44.52      A    O  
ATOM    552  N   SER A 166     114.860  80.453 -24.248  1.00 40.11      A    N  
ATOM    553  CA  SER A 166     115.811  79.872 -25.191  1.00 40.26      A    C  
ATOM    554  C   SER A 166     116.028  78.373 -25.025  1.00 38.09      A    C  
ATOM    555  O   SER A 166     116.138  77.656 -26.016  1.00 37.85      A    O  
ATOM    556  CB  SER A 166     117.158  80.578 -25.077  1.00 41.34      A    C  
ATOM    557  OG  SER A 166     117.722  80.352 -23.800  1.00 40.93      A    O  
ATOM    558  N   GLN A 167     116.089  77.894 -23.784  1.00 37.24      A    N  
ATOM    559  CA  GLN A 167     116.316  76.473 -23.563  1.00 39.27      A    C  
ATOM    560  C   GLN A 167     115.154  75.581 -23.986  1.00 40.12      A    C  
ATOM    561  O   GLN A 167     115.285  74.358 -23.994  1.00 41.43      A    O  
ATOM    562  CB  GLN A 167     116.687  76.178 -22.096  1.00 39.74      A    C  
ATOM    563  CG  GLN A 167     115.615  76.435 -21.036  1.00 43.90      A    C  
ATOM    564  CD  GLN A 167     115.660  77.853 -20.448  1.00 48.97      A    C  
ATOM    565  NE2 GLN A 167     116.158  78.812 -21.227  1.00 41.23      A    N  
ATOM    566  OE1 GLN A 167     115.234  78.077 -19.309  1.00 46.29      A    O  
ATOM    567  N   HIS A 168     114.032  76.182 -24.364  1.00 38.45      A    N  
ATOM    568  CA  HIS A 168     112.868  75.404 -24.779  1.00 36.97      A    C  
ATOM    569  C   HIS A 168     112.362  75.740 -26.179  1.00 38.08      A    C  
ATOM    570  O   HIS A 168     111.479  75.058 -26.702  1.00 40.82      A    O  
ATOM    571  CB  HIS A 168     111.742  75.598 -23.764  1.00 35.17      A    C  
ATOM    572  CG  HIS A 168     112.088  75.120 -22.388  1.00 38.20      A    C  
ATOM    573  CD2 HIS A 168     112.545  73.921 -21.949  1.00 33.38      A    C  
ATOM    574  ND1 HIS A 168     111.963  75.915 -21.267  1.00 38.71      A    N  
ATOM    575  CE1 HIS A 168     112.325  75.227 -20.199  1.00 34.79      A    C  
ATOM    576  NE2 HIS A 168     112.682  74.015 -20.584  1.00 32.25      A    N  
ATOM    577  N   MET A 169     112.935  76.773 -26.788  1.00 38.03      A    N  
ATOM    578  CA  MET A 169     112.529  77.219 -28.116  1.00 38.29      A    C  
ATOM    579  C   MET A 169     112.378  76.123 -29.141  1.00 36.63      A    C  
ATOM    580  O   MET A 169     111.442  76.147 -29.936  1.00 35.54      A    O  
ATOM    581  CB  MET A 169     113.512  78.258 -28.668  1.00 44.81      A    C  
ATOM    582  CG  MET A 169     113.502  79.589 -27.937  1.00 52.17      A    C  
ATOM    583  SD  MET A 169     114.405  80.869 -28.841  1.00 63.15      A    S  
ATOM    584  CE  MET A 169     113.117  81.456 -29.945  1.00 55.69      A    C  
ATOM    585  N   THR A 170     113.296  75.163 -29.123  1.00 36.59      A    N  
ATOM    586  CA  THR A 170     113.283  74.066 -30.091  1.00 35.66      A    C  
ATOM    587  C   THR A 170     112.232  72.993 -29.841  1.00 34.63      A    C  
ATOM    588  O   THR A 170     112.032  72.112 -30.678  1.00 32.00      A    O  
ATOM    589  CB  THR A 170     114.668  73.379 -30.171  1.00 38.11      A    C  
ATOM    590  CG2 THR A 170     115.694  74.325 -30.775  1.00 33.90      A    C  
ATOM    591  OG1 THR A 170     115.087  72.992 -28.852  1.00 35.43      A    O  
ATOM    592  N   GLU A 171     111.562  73.046 -28.698  1.00 31.14      A    N  
ATOM    593  CA  GLU A 171     110.542  72.042 -28.423  1.00 34.47      A    C  
ATOM    594  C   GLU A 171     109.157  72.503 -28.907  1.00 33.81      A    C  
ATOM    595  O   GLU A 171     108.728  73.634 -28.645  1.00 31.42      A    O  
ATOM    596  CB  GLU A 171     110.489  71.714 -26.928  1.00 33.84      A    C  
ATOM    597  CG  GLU A 171     109.583  70.533 -26.608  1.00 41.63      A    C  
ATOM    598  CD  GLU A 171     109.547  70.189 -25.126  1.00 48.33      A    C  
ATOM    599  OE1 GLU A 171     110.632  70.150 -24.499  1.00 50.59      A    O  
ATOM    600  OE2 GLU A 171     108.438  69.947 -24.594  1.00 42.34      A    O1-
ATOM    601  N   VAL A 172     108.471  71.618 -29.621  1.00 31.79      A    N  
ATOM    602  CA  VAL A 172     107.139  71.909 -30.146  1.00 32.17      A    C  
ATOM    603  C   VAL A 172     106.115  72.059 -29.025  1.00 31.31      A    C  
ATOM    604  O   VAL A 172     106.064  71.238 -28.106  1.00 35.22      A    O  
ATOM    605  CB  VAL A 172     106.684  70.783 -31.090  1.00 33.52      A    C  
ATOM    606  CG1 VAL A 172     105.280  71.047 -31.587  1.00 33.53      A    C  
ATOM    607  CG2 VAL A 172     107.656  70.679 -32.256  1.00 32.90      A    C  
ATOM    608  N   VAL A 173     105.304  73.108 -29.096  1.00 30.71      A    N  
ATOM    609  CA  VAL A 173     104.277  73.339 -28.085  1.00 29.06      A    C  
ATOM    610  C   VAL A 173     103.062  72.473 -28.414  1.00 34.43      A    C  
ATOM    611  O   VAL A 173     102.525  72.543 -29.525  1.00 32.16      A    O  
ATOM    612  CB  VAL A 173     103.833  74.805 -28.074  1.00 29.01      A    C  
ATOM    613  CG1 VAL A 173     102.774  75.020 -26.992  1.00 27.74      A    C  
ATOM    614  CG2 VAL A 173     105.043  75.713 -27.855  1.00 25.36      A    C  
ATOM    615  N   ARG A 174     102.643  71.645 -27.459  1.00 32.98      A    N  
ATOM    616  CA  ARG A 174     101.490  70.773 -27.667  1.00 36.10      A    C  
ATOM    617  C   ARG A 174     100.663  70.594 -26.405  1.00 38.08      A    C  
ATOM    618  O   ARG A 174     101.026  71.097 -25.337  1.00 38.87      A    O  
ATOM    619  CB  ARG A 174     101.944  69.405 -28.184  1.00 36.80      A    C  
ATOM    620  CG  ARG A 174     103.315  68.979 -27.708  1.00 41.34      A    C  
ATOM    621  CD  ARG A 174     103.653  67.550 -28.125  1.00 43.17      A    C  
ATOM    622  NE  ARG A 174     103.579  67.332 -29.572  1.00 47.21      A    N  
ATOM    623  CZ  ARG A 174     104.630  67.096 -30.351  1.00 46.54      A    C  
ATOM    624  NH1 ARG A 174     105.851  67.050 -29.829  1.00 52.12      A    N1+
ATOM    625  NH2 ARG A 174     104.463  66.895 -31.652  1.00 43.45      A    N  
ATOM    626  N   ARG A 175      99.540  69.895 -26.532  1.00 36.49      A    N  
ATOM    627  CA  ARG A 175      98.681  69.640 -25.382  1.00 36.92      A    C  
ATOM    628  C   ARG A 175      99.227  68.473 -24.585  1.00 32.77      A    C  
ATOM    629  O   ARG A 175      99.822  67.561 -25.140  1.00 35.47      A    O  
ATOM    630  CB  ARG A 175      97.262  69.295 -25.818  1.00 39.74      A    C  
ATOM    631  CG  ARG A 175      96.466  70.458 -26.341  1.00 42.42      A    C  
ATOM    632  CD  ARG A 175      95.069  69.988 -26.659  1.00 42.42      A    C  
ATOM    633  NE  ARG A 175      94.123  70.195 -25.568  1.00 40.54      A    N  
ATOM    634  CZ  ARG A 175      92.916  69.650 -25.553  1.00 35.15      A    C  
ATOM    635  NH1 ARG A 175      92.557  68.867 -26.557  1.00 32.24      A    N1+
ATOM    636  NH2 ARG A 175      92.061  69.922 -24.579  1.00 35.50      A    N  
ATOM    637  N   CYS A 176      99.013  68.503 -23.279  1.00 35.19      A    N  
ATOM    638  CA  CYS A 176      99.481  67.432 -22.406  1.00 35.60      A    C  
ATOM    639  C   CYS A 176      98.672  66.154 -22.661  1.00 38.98      A    C  
ATOM    640  O   CYS A 176      97.565  66.201 -23.196  1.00 39.14      A    O  
ATOM    641  CB  CYS A 176      99.318  67.844 -20.951  1.00 31.04      A    C  
ATOM    642  SG  CYS A 176      97.601  67.887 -20.416  1.00 37.39      A    S  
ATOM    643  N   PRO A 177      99.217  64.992 -22.282  1.00 41.46      A    N  
ATOM    644  CA  PRO A 177      98.478  63.748 -22.509  1.00 41.76      A    C  
ATOM    645  C   PRO A 177      97.067  63.732 -21.925  1.00 42.03      A    C  
ATOM    646  O   PRO A 177      96.141  63.228 -22.556  1.00 45.15      A    O  
ATOM    647  CB  PRO A 177      99.382  62.697 -21.871  1.00 43.77      A    C  
ATOM    648  CG  PRO A 177     100.754  63.252 -22.145  1.00 43.56      A    C  
ATOM    649  CD  PRO A 177     100.579  64.713 -21.787  1.00 38.96      A    C  
ATOM    650  N   HIS A 178      96.889  64.289 -20.734  1.00 41.78      A    N  
ATOM    651  CA  HIS A 178      95.565  64.279 -20.116  1.00 43.49      A    C  
ATOM    652  C   HIS A 178      94.473  64.958 -20.937  1.00 43.88      A    C  
ATOM    653  O   HIS A 178      93.465  64.338 -21.257  1.00 46.32      A    O  
ATOM    654  CB  HIS A 178      95.602  64.913 -18.724  1.00 43.48      A    C  
ATOM    655  CG  HIS A 178      94.255  65.010 -18.075  1.00 47.56      A    C  
ATOM    656  CD2 HIS A 178      93.309  64.070 -17.838  1.00 45.27      A    C  
ATOM    657  ND1 HIS A 178      93.741  66.199 -17.596  1.00 48.91      A    N  
ATOM    658  CE1 HIS A 178      92.537  65.985 -17.093  1.00 46.80      A    C  
ATOM    659  NE2 HIS A 178      92.251  64.702 -17.227  1.00 45.48      A    N  
ATOM    660  N   HIS A 179      94.659  66.232 -21.260  1.00 44.93      A    N  
ATOM    661  CA  HIS A 179      93.663  66.965 -22.030  1.00 45.67      A    C  
ATOM    662  C   HIS A 179      93.574  66.503 -23.478  1.00 48.34      A    C  
ATOM    663  O   HIS A 179      92.567  66.723 -24.152  1.00 49.90      A    O  
ATOM    664  CB  HIS A 179      93.952  68.465 -21.970  1.00 38.82      A    C  
ATOM    665  CG  HIS A 179      93.513  69.106 -20.691  1.00 42.73      A    C  
ATOM    666  CD2 HIS A 179      92.286  69.215 -20.126  1.00 41.90      A    C  
ATOM    667  ND1 HIS A 179      94.389  69.721 -19.823  1.00 39.32      A    N  
ATOM    668  CE1 HIS A 179      93.722  70.181 -18.779  1.00 43.16      A    C  
ATOM    669  NE2 HIS A 179      92.445  69.886 -18.938  1.00 45.72      A    N  
ATOM    670  N   GLU A 180      94.625  65.854 -23.955  1.00 51.34      A    N  
ATOM    671  CA  GLU A 180      94.648  65.373 -25.328  1.00 58.51      A    C  
ATOM    672  C   GLU A 180      93.574  64.314 -25.538  1.00 63.38      A    C  
ATOM    673  O   GLU A 180      92.947  64.256 -26.599  1.00 64.37      A    O  
ATOM    674  CB  GLU A 180      96.014  64.782 -25.640  1.00 57.00      A    C  
ATOM    675  CG  GLU A 180      96.262  64.521 -27.096  1.00 60.80      A    C  
ATOM    676  CD  GLU A 180      97.627  63.916 -27.316  1.00 64.75      A    C  
ATOM    677  OE1 GLU A 180      97.793  62.717 -27.012  1.00 67.47      A    O  
ATOM    678  OE2 GLU A 180      98.539  64.642 -27.770  1.00 67.96      A    O1-
ATOM    679  N   ARG A 181      93.364  63.476 -24.526  1.00 67.81      A    N  
ATOM    680  CA  ARG A 181      92.361  62.419 -24.614  1.00 72.88      A    C  
ATOM    681  C   ARG A 181      90.995  62.878 -24.115  1.00 74.09      A    C  
ATOM    682  O   ARG A 181      90.086  62.067 -23.947  1.00 73.47      A    O  
ATOM    683  CB  ARG A 181      92.806  61.189 -23.820  1.00 73.41      A    C  
ATOM    684  CG  ARG A 181      92.882  61.405 -22.319  1.00 77.81      A    C  
ATOM    685  CD  ARG A 181      93.129  60.091 -21.596  1.00 80.14      A    C  
ATOM    686  NE  ARG A 181      94.329  59.420 -22.085  1.00 81.54      A    N  
ATOM    687  CZ  ARG A 181      94.773  58.256 -21.624  1.00 82.68      A    C  
ATOM    688  NH1 ARG A 181      94.115  57.629 -20.655  1.00 82.46      A    N1+
ATOM    689  NH2 ARG A 181      95.877  57.722 -22.128  1.00 82.05      A    N  
ATOM    690  N   SER A 182      90.854  64.177 -23.880  1.00 77.89      A    N  
ATOM    691  CA  SER A 182      89.591  64.733 -23.408  1.00 82.69      A    C  
ATOM    692  C   SER A 182      88.552  64.691 -24.523  1.00 85.43      A    C  
ATOM    693  O   SER A 182      88.858  64.317 -25.655  1.00 86.93      A    O  
ATOM    694  CB  SER A 182      89.790  66.176 -22.945  1.00 82.78      A    C  
ATOM    695  OG  SER A 182      88.595  66.708 -22.401  1.00 85.76      A    O  
ATOM    696  N   SER A 183      87.321  65.076 -24.199  1.00 88.60      A    N  
ATOM    697  CA  SER A 183      86.240  65.077 -25.177  1.00 91.91      A    C  
ATOM    698  C   SER A 183      85.697  66.486 -25.387  1.00 93.06      A    C  
ATOM    699  O   SER A 183      84.485  66.692 -25.463  1.00 93.52      A    O  
ATOM    700  CB  SER A 183      85.112  64.149 -24.715  1.00 93.03      A    C  
ATOM    701  OG  SER A 183      84.608  64.547 -23.451  1.00 93.68      A    O  
ATOM    702  N   ASP A 184      86.607  67.451 -25.479  1.00 94.38      A    N  
ATOM    703  CA  ASP A 184      86.238  68.851 -25.680  1.00 95.30      A    C  
ATOM    704  C   ASP A 184      86.390  69.257 -27.142  1.00 94.75      A    C  
ATOM    705  O   ASP A 184      86.020  70.365 -27.531  1.00 94.85      A    O  
ATOM    706  CB  ASP A 184      87.107  69.758 -24.795  1.00 95.33      A    C  
ATOM    707  CG  ASP A 184      88.601  69.549 -25.020  1.00 95.32      A    C  
ATOM    708  OD1 ASP A 184      89.403  70.185 -24.306  1.00 95.33      A    O  
ATOM    709  OD2 ASP A 184      88.978  68.752 -25.908  1.00 95.21      A    O1-
ATOM    710  N   SER A 185      86.936  68.344 -27.940  1.00 94.14      A    N  
ATOM    711  CA  SER A 185      87.157  68.572 -29.363  1.00 93.64      A    C  
ATOM    712  C   SER A 185      85.885  68.949 -30.119  1.00 93.14      A    C  
ATOM    713  O   SER A 185      84.831  68.335 -29.929  1.00 92.28      A    O  
ATOM    714  CB  SER A 185      87.783  67.323 -29.982  1.00 94.58      A    C  
ATOM    715  OG  SER A 185      87.163  66.153 -29.472  1.00 95.33      A    O  
ATOM    716  N   ASP A 186      85.996  69.963 -30.977  1.00 92.22      A    N  
ATOM    717  CA  ASP A 186      84.870  70.449 -31.777  1.00 90.88      A    C  
ATOM    718  C   ASP A 186      84.673  69.644 -33.057  1.00 88.30      A    C  
ATOM    719  O   ASP A 186      83.725  69.883 -33.809  1.00 86.40      A    O  
ATOM    720  CB  ASP A 186      85.074  71.924 -32.146  1.00 93.00      A    C  
ATOM    721  CG  ASP A 186      84.835  72.862 -30.975  1.00 95.33      A    C  
ATOM    722  OD1 ASP A 186      85.575  72.773 -29.970  1.00 95.33      A    O  
ATOM    723  OD2 ASP A 186      83.903  73.691 -31.062  1.00 95.14      A    O1-
ATOM    724  N   GLY A 187      85.575  68.694 -33.295  1.00 85.44      A    N  
ATOM    725  CA  GLY A 187      85.491  67.864 -34.484  1.00 79.89      A    C  
ATOM    726  C   GLY A 187      86.388  68.379 -35.588  1.00 75.68      A    C  
ATOM    727  O   GLY A 187      86.980  67.604 -36.342  1.00 76.66      A    O  
ATOM    728  N   LEU A 188      86.496  69.700 -35.677  1.00 71.28      A    N  
ATOM    729  CA  LEU A 188      87.319  70.341 -36.690  1.00 66.80      A    C  
ATOM    730  C   LEU A 188      88.799  70.397 -36.296  1.00 62.86      A    C  
ATOM    731  O   LEU A 188      89.672  70.238 -37.146  1.00 64.52      A    O  
ATOM    732  CB  LEU A 188      86.791  71.755 -36.953  1.00 68.85      A    C  
ATOM    733  CG  LEU A 188      87.445  72.590 -38.059  1.00 70.02      A    C  
ATOM    734  CD1 LEU A 188      87.302  71.879 -39.394  1.00 69.64      A    C  
ATOM    735  CD2 LEU A 188      86.790  73.971 -38.111  1.00 67.21      A    C  
ATOM    736  N   ALA A 189      89.075  70.606 -35.009  1.00 58.22      A    N  
ATOM    737  CA  ALA A 189      90.451  70.695 -34.509  1.00 52.19      A    C  
ATOM    738  C   ALA A 189      90.999  69.391 -33.931  1.00 47.93      A    C  
ATOM    739  O   ALA A 189      90.353  68.738 -33.120  1.00 46.11      A    O  
ATOM    740  CB  ALA A 189      90.547  71.793 -33.450  1.00 49.55      A    C  
ATOM    741  N   PRO A 190      92.209  68.996 -34.350  1.00 46.13      A    N  
ATOM    742  CA  PRO A 190      92.810  67.760 -33.838  1.00 46.26      A    C  
ATOM    743  C   PRO A 190      92.997  67.873 -32.329  1.00 46.43      A    C  
ATOM    744  O   PRO A 190      93.267  68.953 -31.805  1.00 45.44      A    O  
ATOM    745  CB  PRO A 190      94.134  67.685 -34.584  1.00 45.58      A    C  
ATOM    746  CG  PRO A 190      93.800  68.323 -35.897  1.00 47.48      A    C  
ATOM    747  CD  PRO A 190      93.003  69.538 -35.463  1.00 47.57      A    C  
ATOM    748  N   PRO A 191      92.862  66.756 -31.607  1.00 47.87      A    N  
ATOM    749  CA  PRO A 191      93.019  66.810 -30.152  1.00 44.76      A    C  
ATOM    750  C   PRO A 191      94.372  67.293 -29.631  1.00 44.00      A    C  
ATOM    751  O   PRO A 191      94.452  67.816 -28.523  1.00 44.69      A    O  
ATOM    752  CB  PRO A 191      92.697  65.378 -29.723  1.00 43.78      A    C  
ATOM    753  CG  PRO A 191      93.137  64.563 -30.900  1.00 44.12      A    C  
ATOM    754  CD  PRO A 191      92.626  65.373 -32.065  1.00 44.92      A    C  
ATOM    755  N   GLN A 192      95.425  67.151 -30.424  1.00 44.06      A    N  
ATOM    756  CA  GLN A 192      96.748  67.567 -29.965  1.00 44.23      A    C  
ATOM    757  C   GLN A 192      97.083  69.066 -30.070  1.00 43.19      A    C  
ATOM    758  O   GLN A 192      98.080  69.522 -29.498  1.00 41.69      A    O  
ATOM    759  CB  GLN A 192      97.835  66.750 -30.678  1.00 44.74      A    C  
ATOM    760  CG  GLN A 192      98.094  67.118 -32.139  1.00 51.18      A    C  
ATOM    761  CD  GLN A 192      97.109  66.498 -33.124  1.00 55.18      A    C  
ATOM    762  NE2 GLN A 192      96.073  65.834 -32.603  1.00 54.95      A    N  
ATOM    763  OE1 GLN A 192      97.281  66.618 -34.342  1.00 50.05      A    O  
ATOM    764  N   HIS A 193      96.262  69.834 -30.780  1.00 39.64      A    N  
ATOM    765  CA  HIS A 193      96.525  71.262 -30.937  1.00 39.00      A    C  
ATOM    766  C   HIS A 193      96.120  72.099 -29.733  1.00 38.42      A    C  
ATOM    767  O   HIS A 193      95.025  71.950 -29.198  1.00 39.63      A    O  
ATOM    768  CB  HIS A 193      95.809  71.824 -32.174  1.00 38.48      A    C  
ATOM    769  CG  HIS A 193      96.419  71.407 -33.476  1.00 37.37      A    C  
ATOM    770  CD2 HIS A 193      96.881  70.208 -33.904  1.00 40.72      A    C  
ATOM    771  ND1 HIS A 193      96.591  72.282 -34.530  1.00 36.09      A    N  
ATOM    772  CE1 HIS A 193      97.135  71.641 -35.549  1.00 37.69      A    C  
ATOM    773  NE2 HIS A 193      97.321  70.381 -35.197  1.00 41.09      A    N  
ATOM    774  N   LEU A 194      97.014  72.992 -29.323  1.00 34.76      A    N  
ATOM    775  CA  LEU A 194      96.767  73.891 -28.205  1.00 29.87      A    C  
ATOM    776  C   LEU A 194      95.853  75.034 -28.621  1.00 30.48      A    C  
ATOM    777  O   LEU A 194      94.922  75.395 -27.899  1.00 32.20      A    O  
ATOM    778  CB  LEU A 194      98.078  74.508 -27.721  1.00 27.57      A    C  
ATOM    779  CG  LEU A 194      97.921  75.654 -26.718  1.00 28.42      A    C  
ATOM    780  CD1 LEU A 194      97.504  75.089 -25.355  1.00 31.92      A    C  
ATOM    781  CD2 LEU A 194      99.238  76.413 -26.597  1.00 30.64      A    C  
ATOM    782  N   ILE A 195      96.145  75.616 -29.779  1.00 28.19      A    N  
ATOM    783  CA  ILE A 195      95.387  76.759 -30.269  1.00 32.16      A    C  
ATOM    784  C   ILE A 195      94.278  76.406 -31.254  1.00 36.31      A    C  
ATOM    785  O   ILE A 195      94.508  75.707 -32.253  1.00 37.16      A    O  
ATOM    786  CB  ILE A 195      96.319  77.778 -30.972  1.00 32.31      A    C  
ATOM    787  CG1 ILE A 195      97.471  78.162 -30.043  1.00 29.50      A    C  
ATOM    788  CG2 ILE A 195      95.529  79.019 -31.395  1.00 26.89      A    C  
ATOM    789  CD1 ILE A 195      98.476  79.108 -30.690  1.00 23.19      A    C  
ATOM    790  N   ARG A 196      93.083  76.917 -30.975  1.00 34.23      A    N  
ATOM    791  CA  ARG A 196      91.934  76.702 -31.850  1.00 36.69      A    C  
ATOM    792  C   ARG A 196      91.339  78.043 -32.234  1.00 34.68      A    C  
ATOM    793  O   ARG A 196      91.458  79.022 -31.493  1.00 34.03      A    O  
ATOM    794  CB  ARG A 196      90.835  75.901 -31.150  1.00 32.86      A    C  
ATOM    795  CG  ARG A 196      91.175  74.464 -30.864  1.00 40.47      A    C  
ATOM    796  CD  ARG A 196      90.028  73.814 -30.136  1.00 37.84      A    C  
ATOM    797  NE  ARG A 196      90.328  72.448 -29.728  1.00 38.70      A    N  
ATOM    798  CZ  ARG A 196      89.524  71.715 -28.965  1.00 40.80      A    C  
ATOM    799  NH1 ARG A 196      88.373  72.219 -28.528  1.00 39.56      A    N1+
ATOM    800  NH2 ARG A 196      89.873  70.481 -28.640  1.00 39.66      A    N  
ATOM    801  N   VAL A 197      90.697  78.083 -33.395  1.00 32.47      A    N  
ATOM    802  CA  VAL A 197      90.030  79.297 -33.814  1.00 32.76      A    C  
ATOM    803  C   VAL A 197      88.563  79.029 -33.523  1.00 33.11      A    C  
ATOM    804  O   VAL A 197      88.079  77.926 -33.757  1.00 33.65      A    O  
ATOM    805  CB  VAL A 197      90.247  79.572 -35.303  1.00 30.11      A    C  
ATOM    806  CG1 VAL A 197      89.222  80.576 -35.814  1.00 30.40      A    C  
ATOM    807  CG2 VAL A 197      91.636  80.115 -35.504  1.00 27.36      A    C  
ATOM    808  N   GLU A 198      87.872  80.023 -32.987  1.00 35.65      A    N  
ATOM    809  CA  GLU A 198      86.464  79.880 -32.649  1.00 39.59      A    C  
ATOM    810  C   GLU A 198      85.563  80.710 -33.558  1.00 41.35      A    C  
ATOM    811  O   GLU A 198      85.919  81.825 -33.954  1.00 40.07      A    O  
ATOM    812  CB  GLU A 198      86.236  80.314 -31.199  1.00 43.64      A    C  
ATOM    813  CG  GLU A 198      84.796  80.200 -30.739  1.00 51.59      A    C  
ATOM    814  CD  GLU A 198      84.523  80.972 -29.457  1.00 60.87      A    C  
ATOM    815  OE1 GLU A 198      83.350  80.988 -29.012  1.00 65.51      A    O  
ATOM    816  OE2 GLU A 198      85.477  81.564 -28.896  1.00 60.83      A    O1-
ATOM    817  N   GLY A 199      84.391  80.156 -33.878  1.00 43.07      A    N  
ATOM    818  CA  GLY A 199      83.419  80.854 -34.703  1.00 40.33      A    C  
ATOM    819  C   GLY A 199      83.769  81.009 -36.170  1.00 41.96      A    C  
ATOM    820  O   GLY A 199      83.346  81.980 -36.797  1.00 42.25      A    O  
ATOM    821  N   ASN A 200      84.519  80.056 -36.725  1.00 40.77      A    N  
ATOM    822  CA  ASN A 200      84.916  80.121 -38.128  1.00 38.11      A    C  
ATOM    823  C   ASN A 200      85.161  78.729 -38.698  1.00 40.16      A    C  
ATOM    824  O   ASN A 200      86.212  78.137 -38.471  1.00 35.91      A    O  
ATOM    825  CB  ASN A 200      86.189  80.946 -38.263  1.00 40.36      A    C  
ATOM    826  CG  ASN A 200      86.487  81.337 -39.702  1.00 43.28      A    C  
ATOM    827  ND2 ASN A 200      86.916  82.576 -39.894  1.00 40.90      A    N  
ATOM    828  OD1 ASN A 200      86.347  80.529 -40.628  1.00 45.65      A    O  
ATOM    829  N   LEU A 201      84.197  78.214 -39.455  1.00 42.66      A    N  
ATOM    830  CA  LEU A 201      84.324  76.880 -40.032  1.00 43.54      A    C  
ATOM    831  C   LEU A 201      85.311  76.790 -41.190  1.00 43.49      A    C  
ATOM    832  O   LEU A 201      85.487  75.721 -41.778  1.00 44.17      A    O  
ATOM    833  CB  LEU A 201      82.945  76.347 -40.453  1.00 47.39      A    C  
ATOM    834  CG  LEU A 201      82.096  75.616 -39.391  1.00 51.35      A    C  
ATOM    835  CD1 LEU A 201      82.732  74.266 -39.071  1.00 53.19      A    C  
ATOM    836  CD2 LEU A 201      81.988  76.444 -38.122  1.00 52.22      A    C  
ATOM    837  N   ARG A 202      85.965  77.901 -41.521  1.00 44.15      A    N  
ATOM    838  CA  ARG A 202      86.967  77.882 -42.592  1.00 43.02      A    C  
ATOM    839  C   ARG A 202      88.355  77.612 -41.991  1.00 41.00      A    C  
ATOM    840  O   ARG A 202      89.322  77.373 -42.716  1.00 42.30      A    O  
ATOM    841  CB  ARG A 202      86.967  79.207 -43.351  1.00 42.49      A    C  
ATOM    842  CG  ARG A 202      85.678  79.477 -44.123  1.00 48.16      A    C  
ATOM    843  CD  ARG A 202      85.602  80.933 -44.567  1.00 46.00      A    C  
ATOM    844  NE  ARG A 202      86.134  81.146 -45.910  1.00 43.70      A    N  
ATOM    845  CZ  ARG A 202      86.399  82.346 -46.418  1.00 43.16      A    C  
ATOM    846  NH1 ARG A 202      86.194  83.439 -45.690  1.00 36.10      A    N1+
ATOM    847  NH2 ARG A 202      86.838  82.455 -47.666  1.00 42.66      A    N  
ATOM    848  N   ALA A 203      88.444  77.647 -40.663  1.00 38.15      A    N  
ATOM    849  CA  ALA A 203      89.702  77.385 -39.971  1.00 40.08      A    C  
ATOM    850  C   ALA A 203      90.295  76.059 -40.427  1.00 40.26      A    C  
ATOM    851  O   ALA A 203      89.595  75.052 -40.527  1.00 42.58      A    O  
ATOM    852  CB  ALA A 203      89.480  77.356 -38.459  1.00 38.45      A    C  
ATOM    853  N   GLU A 204      91.596  76.061 -40.678  1.00 40.46      A    N  
ATOM    854  CA  GLU A 204      92.294  74.865 -41.123  1.00 41.04      A    C  
ATOM    855  C   GLU A 204      93.444  74.573 -40.130  1.00 39.54      A    C  
ATOM    856  O   GLU A 204      94.086  75.498 -39.637  1.00 39.24      A    O  
ATOM    857  CB  GLU A 204      92.798  75.128 -42.538  1.00 44.16      A    C  
ATOM    858  CG  GLU A 204      93.376  73.959 -43.277  1.00 52.60      A    C  
ATOM    859  CD  GLU A 204      93.685  74.330 -44.720  1.00 60.85      A    C  
ATOM    860  OE1 GLU A 204      92.732  74.685 -45.457  1.00 57.14      A    O  
ATOM    861  OE2 GLU A 204      94.876  74.276 -45.112  1.00 61.67      A    O1-
ATOM    862  N   TYR A 205      93.682  73.297 -39.827  1.00 36.44      A    N  
ATOM    863  CA  TYR A 205      94.718  72.898 -38.875  1.00 35.24      A    C  
ATOM    864  C   TYR A 205      95.860  72.121 -39.504  1.00 37.21      A    C  
ATOM    865  O   TYR A 205      95.642  71.137 -40.217  1.00 34.52      A    O  
ATOM    866  CB  TYR A 205      94.099  72.067 -37.750  1.00 33.28      A    C  
ATOM    867  CG  TYR A 205      93.179  72.874 -36.869  1.00 30.99      A    C  
ATOM    868  CD1 TYR A 205      93.652  73.492 -35.714  1.00 29.34      A    C  
ATOM    869  CD2 TYR A 205      91.854  73.087 -37.232  1.00 30.97      A    C  
ATOM    870  CE1 TYR A 205      92.825  74.306 -34.946  1.00 27.31      A    C  
ATOM    871  CE2 TYR A 205      91.021  73.900 -36.475  1.00 30.26      A    C  
ATOM    872  CZ  TYR A 205      91.514  74.508 -35.336  1.00 25.20      A    C  
ATOM    873  OH  TYR A 205      90.700  75.351 -34.613  1.00 36.97      A    O  
ATOM    874  N   LEU A 206      97.082  72.554 -39.207  1.00 38.62      A    N  
ATOM    875  CA  LEU A 206      98.274  71.939 -39.768  1.00 42.71      A    C  
ATOM    876  C   LEU A 206      99.253  71.314 -38.779  1.00 44.57      A    C  
ATOM    877  O   LEU A 206      99.504  71.850 -37.698  1.00 47.01      A    O  
ATOM    878  CB  LEU A 206      99.025  72.969 -40.611  1.00 40.42      A    C  
ATOM    879  CG  LEU A 206     100.372  72.554 -41.214  1.00 45.17      A    C  
ATOM    880  CD1 LEU A 206     100.158  71.465 -42.272  1.00 37.58      A    C  
ATOM    881  CD2 LEU A 206     101.049  73.782 -41.834  1.00 40.15      A    C  
ATOM    882  N   ASP A 207      99.790  70.164 -39.179  1.00 48.68      A    N  
ATOM    883  CA  ASP A 207     100.796  69.419 -38.426  1.00 50.12      A    C  
ATOM    884  C   ASP A 207     101.957  69.357 -39.399  1.00 53.00      A    C  
ATOM    885  O   ASP A 207     102.079  68.397 -40.159  1.00 54.51      A    O  
ATOM    886  CB  ASP A 207     100.335  67.994 -38.134  1.00 52.67      A    C  
ATOM    887  CG  ASP A 207      99.936  67.797 -36.694  1.00 56.27      A    C  
ATOM    888  OD1 ASP A 207      98.807  68.198 -36.331  1.00 57.37      A    O  
ATOM    889  OD2 ASP A 207     100.760  67.249 -35.925  1.00 55.11      A    O1-
ATOM    890  N   ASP A 208     102.795  70.387 -39.391  1.00 53.38      A    N  
ATOM    891  CA  ASP A 208     103.922  70.453 -40.307  1.00 52.87      A    C  
ATOM    892  C   ASP A 208     104.675  69.133 -40.415  1.00 53.91      A    C  
ATOM    893  O   ASP A 208     105.241  68.641 -39.445  1.00 53.70      A    O  
ATOM    894  CB  ASP A 208     104.873  71.563 -39.886  1.00 52.99      A    C  
ATOM    895  CG  ASP A 208     105.848  71.925 -40.980  1.00 53.79      A    C  
ATOM    896  OD1 ASP A 208     106.689  71.073 -41.326  1.00 54.34      A    O  
ATOM    897  OD2 ASP A 208     105.762  73.056 -41.504  1.00 55.62      A    O1-
ATOM    898  N   PRO A 209     104.693  68.544 -41.616  1.00 56.25      A    N  
ATOM    899  CA  PRO A 209     105.382  67.270 -41.844  1.00 57.35      A    C  
ATOM    900  C   PRO A 209     106.896  67.309 -41.652  1.00 57.97      A    C  
ATOM    901  O   PRO A 209     107.533  66.265 -41.559  1.00 58.91      A    O  
ATOM    902  CB  PRO A 209     104.989  66.926 -43.278  1.00 57.22      A    C  
ATOM    903  CG  PRO A 209     104.888  68.273 -43.916  1.00 59.05      A    C  
ATOM    904  CD  PRO A 209     104.126  69.066 -42.872  1.00 56.22      A    C  
ATOM    905  N   ASN A 210     107.472  68.505 -41.584  1.00 59.66      A    N  
ATOM    906  CA  ASN A 210     108.915  68.631 -41.412  1.00 58.33      A    C  
ATOM    907  C   ASN A 210     109.360  69.210 -40.072  1.00 58.14      A    C  
ATOM    908  O   ASN A 210     110.318  68.720 -39.471  1.00 60.89      A    O  
ATOM    909  CB  ASN A 210     109.498  69.467 -42.549  1.00 60.10      A    C  
ATOM    910  CG  ASN A 210     109.206  68.870 -43.906  1.00 63.34      A    C  
ATOM    911  ND2 ASN A 210     110.228  68.296 -44.531  1.00 66.46      A    N  
ATOM    912  OD1 ASN A 210     108.073  68.912 -44.385  1.00 66.88      A    O  
ATOM    913  N   THR A 211     108.677  70.252 -39.604  1.00 54.50      A    N  
ATOM    914  CA  THR A 211     109.030  70.872 -38.335  1.00 49.68      A    C  
ATOM    915  C   THR A 211     108.171  70.319 -37.202  1.00 48.69      A    C  
ATOM    916  O   THR A 211     108.468  70.528 -36.029  1.00 49.72      A    O  
ATOM    917  CB  THR A 211     108.856  72.409 -38.393  1.00 50.07      A    C  
ATOM    918  CG2 THR A 211     109.601  72.985 -39.593  1.00 47.54      A    C  
ATOM    919  OG1 THR A 211     107.463  72.735 -38.510  1.00 49.60      A    O  
ATOM    920  N   PHE A 212     107.104  69.616 -37.561  1.00 44.62      A    N  
ATOM    921  CA  PHE A 212     106.201  69.031 -36.580  1.00 42.76      A    C  
ATOM    922  C   PHE A 212     105.471  70.085 -35.757  1.00 39.19      A    C  
ATOM    923  O   PHE A 212     104.823  69.757 -34.767  1.00 38.49      A    O  
ATOM    924  CB  PHE A 212     106.976  68.098 -35.640  1.00 48.47      A    C  
ATOM    925  CG  PHE A 212     107.665  66.960 -36.344  1.00 53.50      A    C  
ATOM    926  CD1 PHE A 212     106.930  65.913 -36.899  1.00 57.45      A    C  
ATOM    927  CD2 PHE A 212     109.049  66.951 -36.480  1.00 56.71      A    C  
ATOM    928  CE1 PHE A 212     107.568  64.875 -37.586  1.00 59.36      A    C  
ATOM    929  CE2 PHE A 212     109.696  65.922 -37.163  1.00 60.30      A    C  
ATOM    930  CZ  PHE A 212     108.954  64.881 -37.718  1.00 57.82      A    C  
ATOM    931  N   ARG A 213     105.571  71.345 -36.168  1.00 34.46      A    N  
ATOM    932  CA  ARG A 213     104.920  72.444 -35.448  1.00 32.92      A    C  
ATOM    933  C   ARG A 213     103.439  72.491 -35.784  1.00 32.68      A    C  
ATOM    934  O   ARG A 213     103.045  72.205 -36.911  1.00 33.70      A    O  
ATOM    935  CB  ARG A 213     105.529  73.792 -35.843  1.00 32.52      A    C  
ATOM    936  CG  ARG A 213     106.999  73.961 -35.574  1.00 32.98      A    C  
ATOM    937  CD  ARG A 213     107.236  74.638 -34.247  1.00 30.91      A    C  
ATOM    938  NE  ARG A 213     108.660  74.751 -33.960  1.00 34.53      A    N  
ATOM    939  CZ  ARG A 213     109.153  75.125 -32.788  1.00 32.88      A    C  
ATOM    940  NH1 ARG A 213     108.333  75.426 -31.792  1.00 34.44      A    N1+
ATOM    941  NH2 ARG A 213     110.463  75.178 -32.610  1.00 36.51      A    N  
ATOM    942  N   HIS A 214     102.618  72.875 -34.814  1.00 32.51      A    N  
ATOM    943  CA  HIS A 214     101.182  72.973 -35.035  1.00 29.91      A    C  
ATOM    944  C   HIS A 214     100.819  74.408 -35.329  1.00 29.83      A    C  
ATOM    945  O   HIS A 214     101.492  75.332 -34.874  1.00 32.48      A    O  
ATOM    946  CB  HIS A 214     100.410  72.545 -33.789  1.00 30.44      A    C  
ATOM    947  CG  HIS A 214     100.689  71.143 -33.352  1.00 34.55      A    C  
ATOM    948  CD2 HIS A 214     101.323  70.123 -33.978  1.00 31.71      A    C  
ATOM    949  ND1 HIS A 214     100.303  70.659 -32.120  1.00 29.22      A    N  
ATOM    950  CE1 HIS A 214     100.691  69.401 -32.004  1.00 32.06      A    C  
ATOM    951  NE2 HIS A 214     101.312  69.052 -33.117  1.00 36.74      A    N  
ATOM    952  N   SER A 215      99.743  74.594 -36.079  1.00 28.46      A    N  
ATOM    953  CA  SER A 215      99.255  75.928 -36.397  1.00 29.51      A    C  
ATOM    954  C   SER A 215      97.837  75.845 -36.927  1.00 28.30      A    C  
ATOM    955  O   SER A 215      97.398  74.797 -37.397  1.00 27.07      A    O  
ATOM    956  CB  SER A 215     100.150  76.618 -37.438  1.00 32.82      A    C  
ATOM    957  OG  SER A 215     100.194  75.899 -38.660  1.00 32.23      A    O  
ATOM    958  N   VAL A 216      97.116  76.955 -36.819  1.00 28.12      A    N  
ATOM    959  CA  VAL A 216      95.757  77.046 -37.318  1.00 27.32      A    C  
ATOM    960  C   VAL A 216      95.710  78.231 -38.292  1.00 30.04      A    C  
ATOM    961  O   VAL A 216      96.265  79.289 -38.006  1.00 31.62      A    O  
ATOM    962  CB  VAL A 216      94.760  77.266 -36.162  1.00 29.08      A    C  
ATOM    963  CG1 VAL A 216      95.104  78.534 -35.388  1.00 28.41      A    C  
ATOM    964  CG2 VAL A 216      93.342  77.350 -36.712  1.00 32.35      A    C  
ATOM    965  N   VAL A 217      95.064  78.052 -39.443  1.00 34.90      A    N  
ATOM    966  CA  VAL A 217      94.965  79.118 -40.448  1.00 36.80      A    C  
ATOM    967  C   VAL A 217      93.545  79.403 -40.903  1.00 36.82      A    C  
ATOM    968  O   VAL A 217      92.753  78.483 -41.070  1.00 38.05      A    O  
ATOM    969  CB  VAL A 217      95.717  78.785 -41.755  1.00 36.64      A    C  
ATOM    970  CG1 VAL A 217      96.601  79.950 -42.140  1.00 39.90      A    C  
ATOM    971  CG2 VAL A 217      96.488  77.495 -41.624  1.00 40.27      A    C  
ATOM    972  N   VAL A 218      93.248  80.679 -41.136  1.00 35.87      A    N  
ATOM    973  CA  VAL A 218      91.939  81.100 -41.623  1.00 38.08      A    C  
ATOM    974  C   VAL A 218      92.137  82.123 -42.748  1.00 40.32      A    C  
ATOM    975  O   VAL A 218      93.148  82.820 -42.798  1.00 39.11      A    O  
ATOM    976  CB  VAL A 218      91.084  81.775 -40.524  1.00 37.15      A    C  
ATOM    977  CG1 VAL A 218      90.866  80.821 -39.361  1.00 38.44      A    C  
ATOM    978  CG2 VAL A 218      91.749  83.067 -40.070  1.00 35.00      A    C  
ATOM    979  N   PRO A 219      91.177  82.211 -43.678  1.00 43.29      A    N  
ATOM    980  CA  PRO A 219      91.326  83.181 -44.763  1.00 41.70      A    C  
ATOM    981  C   PRO A 219      91.189  84.596 -44.212  1.00 40.89      A    C  
ATOM    982  O   PRO A 219      90.444  84.823 -43.257  1.00 39.20      A    O  
ATOM    983  CB  PRO A 219      90.178  82.823 -45.702  1.00 43.63      A    C  
ATOM    984  CG  PRO A 219      90.016  81.341 -45.483  1.00 46.24      A    C  
ATOM    985  CD  PRO A 219      90.103  81.246 -43.981  1.00 46.41      A    C  
ATOM    986  N   TYR A 220      91.916  85.546 -44.795  1.00 37.74      A    N  
ATOM    987  CA  TYR A 220      91.821  86.929 -44.347  1.00 37.51      A    C  
ATOM    988  C   TYR A 220      90.473  87.495 -44.781  1.00 39.79      A    C  
ATOM    989  O   TYR A 220      90.033  87.276 -45.909  1.00 41.06      A    O  
ATOM    990  CB  TYR A 220      92.933  87.797 -44.955  1.00 36.79      A    C  
ATOM    991  CG  TYR A 220      92.736  89.273 -44.662  1.00 37.78      A    C  
ATOM    992  CD1 TYR A 220      93.107  89.819 -43.427  1.00 35.23      A    C  
ATOM    993  CD2 TYR A 220      92.092  90.110 -45.585  1.00 34.36      A    C  
ATOM    994  CE1 TYR A 220      92.835  91.155 -43.113  1.00 35.33      A    C  
ATOM    995  CE2 TYR A 220      91.814  91.450 -45.279  1.00 33.13      A    C  
ATOM    996  CZ  TYR A 220      92.188  91.962 -44.040  1.00 36.33      A    C  
ATOM    997  OH  TYR A 220      91.896  93.269 -43.716  1.00 36.49      A    O  
ATOM    998  N   GLU A 221      89.825  88.230 -43.887  1.00 41.30      A    N  
ATOM    999  CA  GLU A 221      88.536  88.836 -44.180  1.00 42.27      A    C  
ATOM   1000  C   GLU A 221      88.656  90.310 -43.810  1.00 43.44      A    C  
ATOM   1001  O   GLU A 221      89.190  90.658 -42.750  1.00 40.77      A    O  
ATOM   1002  CB  GLU A 221      87.432  88.144 -43.366  1.00 45.36      A    C  
ATOM   1003  CG  GLU A 221      87.251  86.655 -43.714  1.00 55.93      A    C  
ATOM   1004  CD  GLU A 221      86.309  85.897 -42.759  1.00 63.82      A    C  
ATOM   1005  OE1 GLU A 221      86.099  84.677 -42.975  1.00 65.74      A    O  
ATOM   1006  OE2 GLU A 221      85.785  86.508 -41.797  1.00 62.79      A    O1-
ATOM   1007  N   PRO A 222      88.183  91.203 -44.694  1.00 43.40      A    N  
ATOM   1008  CA  PRO A 222      88.239  92.651 -44.467  1.00 41.91      A    C  
ATOM   1009  C   PRO A 222      87.434  93.036 -43.249  1.00 41.20      A    C  
ATOM   1010  O   PRO A 222      86.553  92.295 -42.827  1.00 42.19      A    O  
ATOM   1011  CB  PRO A 222      87.627  93.224 -45.742  1.00 43.97      A    C  
ATOM   1012  CG  PRO A 222      87.896  92.171 -46.762  1.00 42.26      A    C  
ATOM   1013  CD  PRO A 222      87.577  90.915 -46.003  1.00 43.74      A    C  
ATOM   1014  N   PRO A 223      87.729  94.204 -42.663  1.00 44.04      A    N  
ATOM   1015  CA  PRO A 223      86.993  94.655 -41.478  1.00 47.54      A    C  
ATOM   1016  C   PRO A 223      85.519  94.812 -41.820  1.00 52.92      A    C  
ATOM   1017  O   PRO A 223      85.156  94.924 -42.992  1.00 54.07      A    O  
ATOM   1018  CB  PRO A 223      87.633  96.001 -41.159  1.00 44.60      A    C  
ATOM   1019  CG  PRO A 223      89.033  95.835 -41.657  1.00 46.05      A    C  
ATOM   1020  CD  PRO A 223      88.833  95.126 -42.976  1.00 43.36      A    C  
ATOM   1021  N   GLU A 224      84.674  94.814 -40.796  1.00 58.61      A    N  
ATOM   1022  CA  GLU A 224      83.248  94.981 -41.003  1.00 62.36      A    C  
ATOM   1023  C   GLU A 224      83.047  96.457 -41.324  1.00 63.38      A    C  
ATOM   1024  O   GLU A 224      83.794  97.305 -40.835  1.00 63.49      A    O  
ATOM   1025  CB  GLU A 224      82.483  94.610 -39.728  1.00 66.22      A    C  
ATOM   1026  CG  GLU A 224      81.175  93.884 -39.993  1.00 74.85      A    C  
ATOM   1027  CD  GLU A 224      81.391  92.496 -40.588  1.00 78.38      A    C  
ATOM   1028  OE1 GLU A 224      80.422  91.919 -41.133  1.00 79.56      A    O  
ATOM   1029  OE2 GLU A 224      82.529  91.982 -40.501  1.00 79.05      A    O1-
ATOM   1030  N   VAL A 225      82.050  96.765 -42.147  1.00 65.66      A    N  
ATOM   1031  CA  VAL A 225      81.773  98.154 -42.518  1.00 65.39      A    C  
ATOM   1032  C   VAL A 225      81.648  99.034 -41.277  1.00 64.10      A    C  
ATOM   1033  O   VAL A 225      80.868  98.737 -40.368  1.00 63.98      A    O  
ATOM   1034  CB  VAL A 225      80.465  98.260 -43.337  1.00 67.29      A    C  
ATOM   1035  CG1 VAL A 225      80.246  99.696 -43.786  1.00 65.85      A    C  
ATOM   1036  CG2 VAL A 225      80.527  97.329 -44.535  1.00 66.05      A    C  
ATOM   1037  N   GLY A 226      82.423 100.113 -41.240  1.00 64.48      A    N  
ATOM   1038  CA  GLY A 226      82.374 101.015 -40.101  1.00 66.60      A    C  
ATOM   1039  C   GLY A 226      83.529 100.851 -39.127  1.00 67.45      A    C  
ATOM   1040  O   GLY A 226      83.711 101.670 -38.221  1.00 68.00      A    O  
ATOM   1041  N   SER A 227      84.315  99.794 -39.310  1.00 66.43      A    N  
ATOM   1042  CA  SER A 227      85.455  99.531 -38.441  1.00 65.54      A    C  
ATOM   1043  C   SER A 227      86.743  99.429 -39.247  1.00 63.06      A    C  
ATOM   1044  O   SER A 227      86.711  99.210 -40.459  1.00 63.04      A    O  
ATOM   1045  CB  SER A 227      85.233  98.238 -37.656  1.00 66.71      A    C  
ATOM   1046  OG  SER A 227      86.291  98.024 -36.739  1.00 72.19      A    O  
ATOM   1047  N   ASP A 228      87.878  99.586 -38.574  1.00 60.23      A    N  
ATOM   1048  CA  ASP A 228      89.170  99.517 -39.246  1.00 59.30      A    C  
ATOM   1049  C   ASP A 228      90.018  98.302 -38.842  1.00 56.31      A    C  
ATOM   1050  O   ASP A 228      91.231  98.275 -39.070  1.00 54.77      A    O  
ATOM   1051  CB  ASP A 228      89.945 100.817 -39.002  1.00 62.34      A    C  
ATOM   1052  CG  ASP A 228      90.123 101.127 -37.528  1.00 66.28      A    C  
ATOM   1053  OD1 ASP A 228      89.142 100.984 -36.760  1.00 68.43      A    O  
ATOM   1054  OD2 ASP A 228      91.244 101.526 -37.141  1.00 67.68      A    O1-
ATOM   1055  N   TYR A 229      89.374  97.293 -38.260  1.00 52.80      A    N  
ATOM   1056  CA  TYR A 229      90.070  96.083 -37.834  1.00 50.35      A    C  
ATOM   1057  C   TYR A 229      89.217  94.833 -38.030  1.00 48.65      A    C  
ATOM   1058  O   TYR A 229      87.987  94.906 -38.081  1.00 46.88      A    O  
ATOM   1059  CB  TYR A 229      90.475  96.195 -36.356  1.00 48.74      A    C  
ATOM   1060  CG  TYR A 229      89.307  96.346 -35.399  1.00 52.53      A    C  
ATOM   1061  CD1 TYR A 229      88.501  95.255 -35.064  1.00 52.99      A    C  
ATOM   1062  CD2 TYR A 229      88.988  97.589 -34.853  1.00 51.90      A    C  
ATOM   1063  CE1 TYR A 229      87.403  95.399 -34.213  1.00 51.05      A    C  
ATOM   1064  CE2 TYR A 229      87.894  97.743 -34.003  1.00 52.51      A    C  
ATOM   1065  CZ  TYR A 229      87.105  96.647 -33.688  1.00 52.57      A    C  
ATOM   1066  OH  TYR A 229      86.012  96.803 -32.859  1.00 48.88      A    O  
ATOM   1067  N   THR A 230      89.882  93.688 -38.147  1.00 46.14      A    N  
ATOM   1068  CA  THR A 230      89.201  92.412 -38.305  1.00 43.53      A    C  
ATOM   1069  C   THR A 230      89.436  91.622 -37.028  1.00 44.58      A    C  
ATOM   1070  O   THR A 230      90.561  91.552 -36.534  1.00 47.74      A    O  
ATOM   1071  CB  THR A 230      89.765  91.611 -39.468  1.00 43.09      A    C  
ATOM   1072  CG2 THR A 230      89.013  90.286 -39.599  1.00 41.73      A    C  
ATOM   1073  OG1 THR A 230      89.639  92.374 -40.678  1.00 45.08      A    O  
ATOM   1074  N   THR A 231      88.383  91.019 -36.496  1.00 41.78      A    N  
ATOM   1075  CA  THR A 231      88.505  90.262 -35.265  1.00 42.18      A    C  
ATOM   1076  C   THR A 231      88.591  88.765 -35.491  1.00 41.98      A    C  
ATOM   1077  O   THR A 231      87.859  88.209 -36.301  1.00 42.18      A    O  
ATOM   1078  CB  THR A 231      87.308  90.540 -34.322  1.00 44.03      A    C  
ATOM   1079  CG2 THR A 231      87.390  89.677 -33.067  1.00 44.72      A    C  
ATOM   1080  OG1 THR A 231      87.313  91.920 -33.940  1.00 48.90      A    O  
ATOM   1081  N   ILE A 232      89.504  88.121 -34.773  1.00 38.95      A    N  
ATOM   1082  CA  ILE A 232      89.660  86.684 -34.854  1.00 37.50      A    C  
ATOM   1083  C   ILE A 232      89.597  86.193 -33.403  1.00 36.29      A    C  
ATOM   1084  O   ILE A 232      90.148  86.825 -32.503  1.00 36.22      A    O  
ATOM   1085  CB  ILE A 232      91.001  86.293 -35.549  1.00 36.30      A    C  
ATOM   1086  CG1 ILE A 232      91.149  84.771 -35.578  1.00 38.89      A    C  
ATOM   1087  CG2 ILE A 232      92.180  86.908 -34.822  1.00 44.53      A    C  
ATOM   1088  CD1 ILE A 232      92.244  84.279 -36.518  1.00 40.92      A    C  
ATOM   1089  N   TYR A 233      88.893  85.092 -33.172  1.00 34.44      A    N  
ATOM   1090  CA  TYR A 233      88.748  84.561 -31.825  1.00 36.24      A    C  
ATOM   1091  C   TYR A 233      89.512  83.265 -31.619  1.00 35.98      A    C  
ATOM   1092  O   TYR A 233      89.412  82.336 -32.431  1.00 37.09      A    O  
ATOM   1093  CB  TYR A 233      87.271  84.316 -31.499  1.00 38.89      A    C  
ATOM   1094  CG  TYR A 233      86.391  85.541 -31.603  1.00 41.32      A    C  
ATOM   1095  CD1 TYR A 233      85.693  85.829 -32.779  1.00 42.73      A    C  
ATOM   1096  CD2 TYR A 233      86.244  86.404 -30.523  1.00 40.30      A    C  
ATOM   1097  CE1 TYR A 233      84.865  86.946 -32.868  1.00 44.95      A    C  
ATOM   1098  CE2 TYR A 233      85.425  87.523 -30.601  1.00 44.79      A    C  
ATOM   1099  CZ  TYR A 233      84.736  87.791 -31.775  1.00 45.68      A    C  
ATOM   1100  OH  TYR A 233      83.921  88.904 -31.854  1.00 48.56      A    O  
ATOM   1101  N   PHE A 234      90.263  83.206 -30.522  1.00 33.48      A    N  
ATOM   1102  CA  PHE A 234      91.044  82.016 -30.193  1.00 34.77      A    C  
ATOM   1103  C   PHE A 234      90.644  81.376 -28.865  1.00 34.86      A    C  
ATOM   1104  O   PHE A 234      90.012  82.002 -28.009  1.00 39.10      A    O  
ATOM   1105  CB  PHE A 234      92.534  82.356 -30.108  1.00 29.69      A    C  
ATOM   1106  CG  PHE A 234      93.128  82.865 -31.388  1.00 26.88      A    C  
ATOM   1107  CD1 PHE A 234      93.489  84.197 -31.512  1.00 23.53      A    C  
ATOM   1108  CD2 PHE A 234      93.388  82.002 -32.440  1.00 23.99      A    C  
ATOM   1109  CE1 PHE A 234      94.112  84.666 -32.666  1.00 26.53      A    C  
ATOM   1110  CE2 PHE A 234      94.014  82.464 -33.604  1.00 25.74      A    C  
ATOM   1111  CZ  PHE A 234      94.374  83.800 -33.712  1.00 24.85      A    C  
ATOM   1112  N   LYS A 235      91.030  80.117 -28.710  1.00 33.94      A    N  
ATOM   1113  CA  LYS A 235      90.793  79.363 -27.492  1.00 33.11      A    C  
ATOM   1114  C   LYS A 235      92.071  78.583 -27.247  1.00 33.83      A    C  
ATOM   1115  O   LYS A 235      92.625  77.997 -28.179  1.00 33.70      A    O  
ATOM   1116  CB  LYS A 235      89.635  78.372 -27.654  1.00 36.06      A    C  
ATOM   1117  CG  LYS A 235      88.248  78.960 -27.417  1.00 45.07      A    C  
ATOM   1118  CD  LYS A 235      87.203  77.870 -27.154  1.00 45.96      A    C  
ATOM   1119  CE  LYS A 235      87.078  76.900 -28.318  1.00 55.27      A    C  
ATOM   1120  NZ  LYS A 235      86.249  75.691 -27.989  1.00 59.64      A    N1+
ATOM   1121  N   PHE A 236      92.559  78.590 -26.009  1.00 31.49      A    N  
ATOM   1122  CA  PHE A 236      93.769  77.839 -25.681  1.00 32.84      A    C  
ATOM   1123  C   PHE A 236      93.354  76.641 -24.824  1.00 32.07      A    C  
ATOM   1124  O   PHE A 236      92.792  76.801 -23.742  1.00 33.21      A    O  
ATOM   1125  CB  PHE A 236      94.771  78.753 -24.977  1.00 27.04      A    C  
ATOM   1126  CG  PHE A 236      95.242  79.888 -25.849  1.00 30.13      A    C  
ATOM   1127  CD1 PHE A 236      94.471  81.030 -26.007  1.00 28.89      A    C  
ATOM   1128  CD2 PHE A 236      96.437  79.791 -26.555  1.00 31.79      A    C  
ATOM   1129  CE1 PHE A 236      94.874  82.056 -26.854  1.00 28.20      A    C  
ATOM   1130  CE2 PHE A 236      96.847  80.811 -27.408  1.00 32.88      A    C  
ATOM   1131  CZ  PHE A 236      96.062  81.950 -27.558  1.00 28.71      A    C  
ATOM   1132  N   MET A 237      93.643  75.444 -25.329  1.00 33.02      A    N  
ATOM   1133  CA  MET A 237      93.236  74.189 -24.704  1.00 33.79      A    C  
ATOM   1134  C   MET A 237      94.055  73.515 -23.589  1.00 39.78      A    C  
ATOM   1135  O   MET A 237      93.844  72.330 -23.301  1.00 41.41      A    O  
ATOM   1136  CB  MET A 237      92.983  73.173 -25.821  1.00 31.72      A    C  
ATOM   1137  CG  MET A 237      92.061  73.706 -26.929  1.00 35.01      A    C  
ATOM   1138  SD  MET A 237      90.519  74.457 -26.305  1.00 40.94      A    S  
ATOM   1139  CE  MET A 237      89.647  72.971 -25.742  1.00 35.00      A    C  
ATOM   1140  N   CYS A 238      94.987  74.238 -22.971  1.00 37.59      A    N  
ATOM   1141  CA  CYS A 238      95.775  73.689 -21.862  1.00 34.89      A    C  
ATOM   1142  C   CYS A 238      96.222  74.857 -21.015  1.00 33.44      A    C  
ATOM   1143  O   CYS A 238      96.434  75.951 -21.530  1.00 34.31      A    O  
ATOM   1144  CB  CYS A 238      97.033  72.945 -22.346  1.00 34.96      A    C  
ATOM   1145  SG  CYS A 238      96.880  71.166 -22.736  1.00 40.28      A    S  
ATOM   1146  N   ASN A 239      96.345  74.639 -19.713  1.00 33.15      A    N  
ATOM   1147  CA  ASN A 239      96.833  75.694 -18.844  1.00 33.54      A    C  
ATOM   1148  C   ASN A 239      98.338  75.729 -19.089  1.00 33.61      A    C  
ATOM   1149  O   ASN A 239      98.921  74.753 -19.573  1.00 31.37      A    O  
ATOM   1150  CB  ASN A 239      96.557  75.370 -17.369  1.00 37.54      A    C  
ATOM   1151  CG  ASN A 239      95.101  75.583 -16.986  1.00 40.38      A    C  
ATOM   1152  ND2 ASN A 239      94.495  74.571 -16.377  1.00 41.74      A    N  
ATOM   1153  OD1 ASN A 239      94.532  76.648 -17.227  1.00 38.37      A    O  
ATOM   1154  N   SER A 240      98.972  76.848 -18.775  1.00 31.44      A    N  
ATOM   1155  CA  SER A 240     100.408  76.935 -18.961  1.00 33.34      A    C  
ATOM   1156  C   SER A 240     101.116  75.990 -17.995  1.00 34.22      A    C  
ATOM   1157  O   SER A 240     102.284  75.682 -18.177  1.00 35.88      A    O  
ATOM   1158  CB  SER A 240     100.888  78.367 -18.723  1.00 33.35      A    C  
ATOM   1159  OG  SER A 240     100.372  79.249 -19.712  1.00 34.23      A    O  
ATOM   1160  N   SER A 241     100.392  75.503 -16.992  1.00 34.97      A    N  
ATOM   1161  CA  SER A 241     100.972  74.620 -15.982  1.00 37.29      A    C  
ATOM   1162  C   SER A 241     100.831  73.111 -16.209  1.00 37.39      A    C  
ATOM   1163  O   SER A 241     101.461  72.323 -15.508  1.00 41.23      A    O  
ATOM   1164  CB  SER A 241     100.386  74.967 -14.606  1.00 34.75      A    C  
ATOM   1165  OG  SER A 241      98.985  74.732 -14.579  1.00 38.43      A    O  
ATOM   1166  N   CYS A 242     100.016  72.699 -17.171  1.00 37.13      A    N  
ATOM   1167  CA  CYS A 242      99.827  71.268 -17.427  1.00 36.55      A    C  
ATOM   1168  C   CYS A 242     101.122  70.459 -17.559  1.00 37.96      A    C  
ATOM   1169  O   CYS A 242     101.948  70.717 -18.444  1.00 35.78      A    O  
ATOM   1170  CB  CYS A 242      98.985  71.057 -18.690  1.00 30.50      A    C  
ATOM   1171  SG  CYS A 242      97.277  71.660 -18.605  1.00 39.45      A    S  
ATOM   1172  N   MET A 243     101.305  69.468 -16.690  1.00 37.23      A    N  
ATOM   1173  CA  MET A 243     102.501  68.654 -16.798  1.00 43.54      A    C  
ATOM   1174  C   MET A 243     102.311  67.732 -17.988  1.00 41.62      A    C  
ATOM   1175  O   MET A 243     101.204  67.279 -18.265  1.00 40.76      A    O  
ATOM   1176  CB  MET A 243     102.763  67.847 -15.525  1.00 48.89      A    C  
ATOM   1177  CG  MET A 243     101.672  66.885 -15.120  1.00 59.07      A    C  
ATOM   1178  SD  MET A 243     102.315  65.719 -13.885  1.00 68.62      A    S  
ATOM   1179  CE  MET A 243     102.951  66.885 -12.624  1.00 67.89      A    C  
ATOM   1180  N   GLY A 244     103.398  67.462 -18.696  1.00 41.71      A    N  
ATOM   1181  CA  GLY A 244     103.313  66.628 -19.874  1.00 40.21      A    C  
ATOM   1182  C   GLY A 244     103.111  67.550 -21.059  1.00 39.27      A    C  
ATOM   1183  O   GLY A 244     103.281  67.145 -22.206  1.00 43.19      A    O  
ATOM   1184  N   GLY A 245     102.748  68.800 -20.771  1.00 37.52      A    N  
ATOM   1185  CA  GLY A 245     102.528  69.784 -21.820  1.00 33.02      A    C  
ATOM   1186  C   GLY A 245     103.408  71.015 -21.663  1.00 33.83      A    C  
ATOM   1187  O   GLY A 245     104.634  70.913 -21.681  1.00 34.54      A    O  
ATOM   1188  N   MET A 246     102.811  72.190 -21.502  1.00 30.47      A    N  
ATOM   1189  CA  MET A 246     103.641  73.381 -21.364  1.00 33.87      A    C  
ATOM   1190  C   MET A 246     104.491  73.345 -20.087  1.00 32.20      A    C  
ATOM   1191  O   MET A 246     105.563  73.954 -20.013  1.00 33.57      A    O  
ATOM   1192  CB  MET A 246     102.778  74.642 -21.470  1.00 26.86      A    C  
ATOM   1193  CG  MET A 246     102.214  74.806 -22.887  1.00 27.16      A    C  
ATOM   1194  SD  MET A 246     101.306  76.342 -23.174  1.00 33.30      A    S  
ATOM   1195  CE  MET A 246      99.724  75.946 -22.569  1.00 26.79      A    C  
ATOM   1196  N   ASN A 247     104.011  72.614 -19.091  1.00 32.77      A    N  
ATOM   1197  CA  ASN A 247     104.744  72.423 -17.843  1.00 33.95      A    C  
ATOM   1198  C   ASN A 247     105.314  73.699 -17.227  1.00 34.49      A    C  
ATOM   1199  O   ASN A 247     106.485  73.751 -16.866  1.00 35.03      A    O  
ATOM   1200  CB  ASN A 247     105.871  71.412 -18.095  1.00 32.65      A    C  
ATOM   1201  CG  ASN A 247     106.377  70.757 -16.816  1.00 40.92      A    C  
ATOM   1202  ND2 ASN A 247     107.694  70.745 -16.642  1.00 40.96      A    N  
ATOM   1203  OD1 ASN A 247     105.595  70.254 -16.002  1.00 44.35      A    O  
ATOM   1204  N   ARG A 248     104.473  74.723 -17.124  1.00 35.69      A    N  
ATOM   1205  CA  ARG A 248     104.837  76.011 -16.544  1.00 35.34      A    C  
ATOM   1206  C   ARG A 248     105.795  76.857 -17.369  1.00 37.16      A    C  
ATOM   1207  O   ARG A 248     106.320  77.852 -16.878  1.00 40.39      A    O  
ATOM   1208  CB  ARG A 248     105.391  75.804 -15.129  1.00 38.37      A    C  
ATOM   1209  CG  ARG A 248     104.433  75.020 -14.251  1.00 40.23      A    C  
ATOM   1210  CD  ARG A 248     104.897  74.840 -12.816  1.00 46.63      A    C  
ATOM   1211  NE  ARG A 248     103.854  74.158 -12.042  1.00 56.92      A    N  
ATOM   1212  CZ  ARG A 248     103.727  74.204 -10.715  1.00 60.80      A    C  
ATOM   1213  NH1 ARG A 248     104.584  74.904  -9.975  1.00 60.55      A    N1+
ATOM   1214  NH2 ARG A 248     102.727  73.559 -10.127  1.00 58.33      A    N  
ATOM   1215  N   ARG A 249     106.019  76.478 -18.623  1.00 34.96      A    N  
ATOM   1216  CA  ARG A 249     106.911  77.247 -19.493  1.00 34.13      A    C  
ATOM   1217  C   ARG A 249     106.121  78.307 -20.265  1.00 33.82      A    C  
ATOM   1218  O   ARG A 249     105.136  77.998 -20.932  1.00 36.68      A    O  
ATOM   1219  CB  ARG A 249     107.618  76.310 -20.479  1.00 30.29      A    C  
ATOM   1220  CG  ARG A 249     108.538  75.311 -19.811  1.00 33.28      A    C  
ATOM   1221  CD  ARG A 249     109.067  74.269 -20.782  1.00 30.52      A    C  
ATOM   1222  NE  ARG A 249     108.026  73.364 -21.261  1.00 28.19      A    N  
ATOM   1223  CZ  ARG A 249     108.248  72.354 -22.100  1.00 29.89      A    C  
ATOM   1224  NH1 ARG A 249     109.473  72.119 -22.547  1.00 28.36      A    N1+
ATOM   1225  NH2 ARG A 249     107.248  71.579 -22.502  1.00 27.47      A    N  
ATOM   1226  N   PRO A 250     106.544  79.574 -20.194  1.00 33.87      A    N  
ATOM   1227  CA  PRO A 250     105.820  80.629 -20.916  1.00 30.86      A    C  
ATOM   1228  C   PRO A 250     105.886  80.459 -22.431  1.00 30.91      A    C  
ATOM   1229  O   PRO A 250     106.883  79.976 -22.972  1.00 29.84      A    O  
ATOM   1230  CB  PRO A 250     106.528  81.908 -20.468  1.00 35.37      A    C  
ATOM   1231  CG  PRO A 250     107.150  81.530 -19.142  1.00 36.20      A    C  
ATOM   1232  CD  PRO A 250     107.661  80.143 -19.423  1.00 34.56      A    C  
ATOM   1233  N   ILE A 251     104.827  80.870 -23.118  1.00 28.14      A    N  
ATOM   1234  CA  ILE A 251     104.799  80.761 -24.565  1.00 30.47      A    C  
ATOM   1235  C   ILE A 251     104.535  82.097 -25.247  1.00 31.10      A    C  
ATOM   1236  O   ILE A 251     104.037  83.054 -24.647  1.00 33.47      A    O  
ATOM   1237  CB  ILE A 251     103.718  79.764 -25.050  1.00 29.21      A    C  
ATOM   1238  CG1 ILE A 251     102.330  80.251 -24.623  1.00 26.54      A    C  
ATOM   1239  CG2 ILE A 251     103.989  78.385 -24.485  1.00 30.25      A    C  
ATOM   1240  CD1 ILE A 251     101.193  79.461 -25.242  1.00 24.58      A    C  
ATOM   1241  N   LEU A 252     104.863  82.138 -26.523  1.00 30.38      A    N  
ATOM   1242  CA  LEU A 252     104.667  83.319 -27.340  1.00 34.61      A    C  
ATOM   1243  C   LEU A 252     103.792  82.890 -28.526  1.00 33.74      A    C  
ATOM   1244  O   LEU A 252     104.047  81.853 -29.144  1.00 32.77      A    O  
ATOM   1245  CB  LEU A 252     106.026  83.798 -27.837  1.00 38.00      A    C  
ATOM   1246  CG  LEU A 252     106.115  85.095 -28.615  1.00 43.24      A    C  
ATOM   1247  CD1 LEU A 252     105.710  86.249 -27.719  1.00 51.29      A    C  
ATOM   1248  CD2 LEU A 252     107.545  85.278 -29.103  1.00 49.31      A    C  
ATOM   1249  N   VAL A 253     102.752  83.660 -28.834  1.00 32.17      A    N  
ATOM   1250  CA  VAL A 253     101.889  83.323 -29.963  1.00 29.44      A    C  
ATOM   1251  C   VAL A 253     102.267  84.196 -31.169  1.00 30.04      A    C  
ATOM   1252  O   VAL A 253     102.242  85.422 -31.087  1.00 30.53      A    O  
ATOM   1253  CB  VAL A 253     100.384  83.500 -29.588  1.00 30.33      A    C  
ATOM   1254  CG1 VAL A 253      99.508  83.368 -30.818  1.00 27.19      A    C  
ATOM   1255  CG2 VAL A 253      99.972  82.425 -28.580  1.00 25.77      A    C  
ATOM   1256  N   ILE A 254     102.646  83.550 -32.270  1.00 28.08      A    N  
ATOM   1257  CA  ILE A 254     103.040  84.235 -33.498  1.00 27.91      A    C  
ATOM   1258  C   ILE A 254     101.882  84.300 -34.500  1.00 31.03      A    C  
ATOM   1259  O   ILE A 254     101.398  83.263 -34.953  1.00 32.73      A    O  
ATOM   1260  CB  ILE A 254     104.199  83.493 -34.242  1.00 29.27      A    C  
ATOM   1261  CG1 ILE A 254     105.303  83.057 -33.270  1.00 30.22      A    C  
ATOM   1262  CG2 ILE A 254     104.783  84.394 -35.327  1.00 25.49      A    C  
ATOM   1263  CD1 ILE A 254     105.874  84.154 -32.452  1.00 40.35      A    C  
ATOM   1264  N   ILE A 255     101.452  85.509 -34.861  1.00 29.28      A    N  
ATOM   1265  CA  ILE A 255     100.381  85.678 -35.839  1.00 29.60      A    C  
ATOM   1266  C   ILE A 255     101.027  86.195 -37.133  1.00 31.81      A    C  
ATOM   1267  O   ILE A 255     101.621  87.273 -37.144  1.00 31.90      A    O  
ATOM   1268  CB  ILE A 255      99.327  86.722 -35.377  1.00 31.68      A    C  
ATOM   1269  CG1 ILE A 255      98.700  86.313 -34.036  1.00 28.55      A    C  
ATOM   1270  CG2 ILE A 255      98.259  86.885 -36.454  1.00 28.12      A    C  
ATOM   1271  CD1 ILE A 255      98.002  84.979 -34.051  1.00 29.66      A    C  
ATOM   1272  N   THR A 256     100.912  85.431 -38.215  1.00 31.71      A    N  
ATOM   1273  CA  THR A 256     101.501  85.829 -39.485  1.00 32.53      A    C  
ATOM   1274  C   THR A 256     100.468  86.058 -40.591  1.00 34.53      A    C  
ATOM   1275  O   THR A 256      99.444  85.380 -40.665  1.00 35.92      A    O  
ATOM   1276  CB  THR A 256     102.509  84.769 -39.994  1.00 33.47      A    C  
ATOM   1277  CG2 THR A 256     103.649  84.588 -39.011  1.00 32.71      A    C  
ATOM   1278  OG1 THR A 256     101.840  83.514 -40.167  1.00 41.52      A    O  
ATOM   1279  N   LEU A 257     100.737  87.034 -41.444  1.00 32.67      A    N  
ATOM   1280  CA  LEU A 257      99.864  87.313 -42.568  1.00 33.55      A    C  
ATOM   1281  C   LEU A 257     100.636  86.705 -43.731  1.00 32.50      A    C  
ATOM   1282  O   LEU A 257     101.806  87.005 -43.900  1.00 34.75      A    O  
ATOM   1283  CB  LEU A 257      99.721  88.823 -42.770  1.00 33.71      A    C  
ATOM   1284  CG  LEU A 257      98.634  89.280 -43.745  1.00 34.39      A    C  
ATOM   1285  CD1 LEU A 257      97.269  89.158 -43.084  1.00 33.28      A    C  
ATOM   1286  CD2 LEU A 257      98.893  90.716 -44.154  1.00 32.39      A    C  
ATOM   1287  N   GLU A 258     100.011  85.831 -44.513  1.00 35.08      A    N  
ATOM   1288  CA  GLU A 258     100.709  85.214 -45.638  1.00 39.22      A    C  
ATOM   1289  C   GLU A 258      99.859  85.155 -46.906  1.00 41.98      A    C  
ATOM   1290  O   GLU A 258      98.625  85.220 -46.835  1.00 43.97      A    O  
ATOM   1291  CB  GLU A 258     101.177  83.808 -45.253  1.00 39.60      A    C  
ATOM   1292  CG  GLU A 258     100.095  82.933 -44.647  1.00 46.31      A    C  
ATOM   1293  CD  GLU A 258     100.578  81.521 -44.328  1.00 48.55      A    C  
ATOM   1294  OE1 GLU A 258     101.461  81.357 -43.450  1.00 47.49      A    O  
ATOM   1295  OE2 GLU A 258     100.064  80.573 -44.964  1.00 50.40      A    O1-
ATOM   1296  N   ASP A 259     100.507  85.061 -48.068  1.00 43.93      A    N  
ATOM   1297  CA  ASP A 259      99.758  84.981 -49.322  1.00 44.58      A    C  
ATOM   1298  C   ASP A 259      99.251  83.554 -49.513  1.00 44.02      A    C  
ATOM   1299  O   ASP A 259      99.623  82.653 -48.760  1.00 41.82      A    O  
ATOM   1300  CB  ASP A 259     100.610  85.405 -50.529  1.00 46.08      A    C  
ATOM   1301  CG  ASP A 259     101.865  84.560 -50.704  1.00 52.51      A    C  
ATOM   1302  OD1 ASP A 259     101.881  83.388 -50.275  1.00 55.29      A    O  
ATOM   1303  OD2 ASP A 259     102.843  85.071 -51.298  1.00 57.03      A    O1-
ATOM   1304  N   SER A 260      98.407  83.354 -50.522  1.00 46.14      A    N  
ATOM   1305  CA  SER A 260      97.823  82.043 -50.808  1.00 49.10      A    C  
ATOM   1306  C   SER A 260      98.822  80.895 -50.854  1.00 48.55      A    C  
ATOM   1307  O   SER A 260      98.445  79.739 -50.663  1.00 49.78      A    O  
ATOM   1308  CB  SER A 260      97.055  82.080 -52.134  1.00 51.48      A    C  
ATOM   1309  OG  SER A 260      97.939  82.195 -53.239  1.00 61.57      A    O  
ATOM   1310  N   SER A 261     100.089  81.210 -51.100  1.00 48.67      A    N  
ATOM   1311  CA  SER A 261     101.132  80.191 -51.190  1.00 49.13      A    C  
ATOM   1312  C   SER A 261     101.959  80.035 -49.920  1.00 48.90      A    C  
ATOM   1313  O   SER A 261     102.874  79.213 -49.870  1.00 47.40      A    O  
ATOM   1314  CB  SER A 261     102.065  80.503 -52.361  1.00 50.52      A    C  
ATOM   1315  OG  SER A 261     101.334  80.598 -53.576  1.00 59.37      A    O  
ATOM   1316  N   GLY A 262     101.656  80.833 -48.903  1.00 47.36      A    N  
ATOM   1317  CA  GLY A 262     102.390  80.725 -47.653  1.00 47.21      A    C  
ATOM   1318  C   GLY A 262     103.586  81.646 -47.468  1.00 47.46      A    C  
ATOM   1319  O   GLY A 262     104.356  81.480 -46.515  1.00 45.46      A    O  
ATOM   1320  N   ASN A 263     103.755  82.613 -48.362  1.00 43.93      A    N  
ATOM   1321  CA  ASN A 263     104.871  83.537 -48.239  1.00 44.43      A    C  
ATOM   1322  C   ASN A 263     104.519  84.597 -47.202  1.00 43.11      A    C  
ATOM   1323  O   ASN A 263     103.374  85.049 -47.118  1.00 42.11      A    O  
ATOM   1324  CB  ASN A 263     105.176  84.189 -49.590  1.00 48.52      A    C  
ATOM   1325  CG  ASN A 263     105.572  83.174 -50.646  1.00 49.75      A    C  
ATOM   1326  ND2 ASN A 263     104.792  83.100 -51.720  1.00 50.41      A    N  
ATOM   1327  OD1 ASN A 263     106.565  82.461 -50.494  1.00 50.84      A    O  
ATOM   1328  N   LEU A 264     105.509  84.985 -46.410  1.00 40.12      A    N  
ATOM   1329  CA  LEU A 264     105.303  85.973 -45.366  1.00 39.67      A    C  
ATOM   1330  C   LEU A 264     104.998  87.380 -45.897  1.00 39.08      A    C  
ATOM   1331  O   LEU A 264     105.736  87.905 -46.737  1.00 43.75      A    O  
ATOM   1332  CB  LEU A 264     106.539  86.024 -44.468  1.00 35.12      A    C  
ATOM   1333  CG  LEU A 264     106.432  86.896 -43.216  1.00 40.08      A    C  
ATOM   1334  CD1 LEU A 264     105.563  86.198 -42.188  1.00 36.33      A    C  
ATOM   1335  CD2 LEU A 264     107.818  87.139 -42.635  1.00 42.15      A    C  
ATOM   1336  N   LEU A 265     103.910  87.975 -45.405  1.00 35.71      A    N  
ATOM   1337  CA  LEU A 265     103.514  89.331 -45.780  1.00 31.22      A    C  
ATOM   1338  C   LEU A 265     103.593  90.218 -44.544  1.00 32.04      A    C  
ATOM   1339  O   LEU A 265     103.833  91.425 -44.643  1.00 36.42      A    O  
ATOM   1340  CB  LEU A 265     102.080  89.361 -46.308  1.00 32.92      A    C  
ATOM   1341  CG  LEU A 265     101.777  88.610 -47.609  1.00 36.78      A    C  
ATOM   1342  CD1 LEU A 265     100.295  88.688 -47.898  1.00 33.16      A    C  
ATOM   1343  CD2 LEU A 265     102.579  89.214 -48.763  1.00 36.96      A    C  
ATOM   1344  N   GLY A 266     103.383  89.619 -43.373  1.00 31.74      A    N  
ATOM   1345  CA  GLY A 266     103.427  90.377 -42.134  1.00 27.52      A    C  
ATOM   1346  C   GLY A 266     103.500  89.463 -40.931  1.00 31.52      A    C  
ATOM   1347  O   GLY A 266     103.125  88.290 -41.014  1.00 29.46      A    O  
ATOM   1348  N   ARG A 267     103.970  90.000 -39.806  1.00 31.00      A    N  
ATOM   1349  CA  ARG A 267     104.096  89.224 -38.580  1.00 28.92      A    C  
ATOM   1350  C   ARG A 267     104.067  90.072 -37.312  1.00 32.64      A    C  
ATOM   1351  O   ARG A 267     104.632  91.166 -37.263  1.00 34.69      A    O  
ATOM   1352  CB  ARG A 267     105.398  88.429 -38.619  1.00 27.74      A    C  
ATOM   1353  CG  ARG A 267     105.641  87.529 -37.403  1.00 33.89      A    C  
ATOM   1354  CD  ARG A 267     106.765  86.528 -37.695  1.00 30.46      A    C  
ATOM   1355  NE  ARG A 267     107.955  87.242 -38.129  1.00 40.15      A    N  
ATOM   1356  CZ  ARG A 267     108.738  86.872 -39.131  1.00 38.70      A    C  
ATOM   1357  NH1 ARG A 267     108.473  85.774 -39.824  1.00 43.51      A    N1+
ATOM   1358  NH2 ARG A 267     109.782  87.619 -39.446  1.00 47.66      A    N  
ATOM   1359  N   ASP A 268     103.398  89.559 -36.287  1.00 30.65      A    N  
ATOM   1360  CA  ASP A 268     103.333  90.233 -35.007  1.00 29.92      A    C  
ATOM   1361  C   ASP A 268     103.134  89.136 -33.968  1.00 31.58      A    C  
ATOM   1362  O   ASP A 268     102.890  87.983 -34.334  1.00 32.66      A    O  
ATOM   1363  CB  ASP A 268     102.194  91.248 -34.969  1.00 29.85      A    C  
ATOM   1364  CG  ASP A 268     102.337  92.233 -33.815  1.00 34.92      A    C  
ATOM   1365  OD1 ASP A 268     103.378  92.184 -33.120  1.00 28.87      A    O  
ATOM   1366  OD2 ASP A 268     101.417  93.056 -33.604  1.00 36.92      A    O1-
ATOM   1367  N   SER A 269     103.241  89.468 -32.685  1.00 28.51      A    N  
ATOM   1368  CA  SER A 269     103.104  88.446 -31.660  1.00 29.26      A    C  
ATOM   1369  C   SER A 269     102.806  88.988 -30.275  1.00 31.39      A    C  
ATOM   1370  O   SER A 269     102.949  90.181 -30.008  1.00 33.20      A    O  
ATOM   1371  CB  SER A 269     104.386  87.625 -31.598  1.00 28.67      A    C  
ATOM   1372  OG  SER A 269     105.489  88.472 -31.334  1.00 33.26      A    O  
ATOM   1373  N   PHE A 270     102.391  88.091 -29.390  1.00 30.74      A    N  
ATOM   1374  CA  PHE A 270     102.080  88.450 -28.016  1.00 30.10      A    C  
ATOM   1375  C   PHE A 270     102.317  87.246 -27.131  1.00 31.63      A    C  
ATOM   1376  O   PHE A 270     102.288  86.113 -27.602  1.00 36.17      A    O  
ATOM   1377  CB  PHE A 270     100.626  88.943 -27.876  1.00 29.63      A    C  
ATOM   1378  CG  PHE A 270      99.573  87.975 -28.375  1.00 28.34      A    C  
ATOM   1379  CD1 PHE A 270      99.356  87.791 -29.735  1.00 29.10      A    C  
ATOM   1380  CD2 PHE A 270      98.742  87.310 -27.478  1.00 32.28      A    C  
ATOM   1381  CE1 PHE A 270      98.321  86.964 -30.194  1.00 29.65      A    C  
ATOM   1382  CE2 PHE A 270      97.697  86.474 -27.930  1.00 26.94      A    C  
ATOM   1383  CZ  PHE A 270      97.487  86.307 -29.282  1.00 28.33      A    C  
ATOM   1384  N   GLU A 271     102.569  87.491 -25.850  1.00 35.85      A    N  
ATOM   1385  CA  GLU A 271     102.817  86.412 -24.905  1.00 34.22      A    C  
ATOM   1386  C   GLU A 271     101.490  85.969 -24.341  1.00 35.48      A    C  
ATOM   1387  O   GLU A 271     100.563  86.771 -24.229  1.00 37.93      A    O  
ATOM   1388  CB  GLU A 271     103.725  86.885 -23.768  1.00 38.13      A    C  
ATOM   1389  CG  GLU A 271     104.335  85.742 -22.962  1.00 43.90      A    C  
ATOM   1390  CD  GLU A 271     105.173  86.223 -21.794  1.00 46.93      A    C  
ATOM   1391  OE1 GLU A 271     106.017  87.125 -21.990  1.00 48.16      A    O  
ATOM   1392  OE2 GLU A 271     104.991  85.689 -20.680  1.00 49.00      A    O1-
ATOM   1393  N   VAL A 272     101.397  84.694 -23.979  1.00 34.66      A    N  
ATOM   1394  CA  VAL A 272     100.159  84.158 -23.437  1.00 34.32      A    C  
ATOM   1395  C   VAL A 272     100.372  83.247 -22.245  1.00 34.53      A    C  
ATOM   1396  O   VAL A 272     101.229  82.369 -22.270  1.00 35.60      A    O  
ATOM   1397  CB  VAL A 272      99.391  83.323 -24.482  1.00 33.60      A    C  
ATOM   1398  CG1 VAL A 272      98.147  82.721 -23.841  1.00 33.90      A    C  
ATOM   1399  CG2 VAL A 272      99.020  84.180 -25.682  1.00 38.12      A    C  
ATOM   1400  N   ARG A 273      99.582  83.466 -21.201  1.00 34.80      A    N  
ATOM   1401  CA  ARG A 273      99.624  82.626 -20.020  1.00 32.20      A    C  
ATOM   1402  C   ARG A 273      98.193  82.152 -19.842  1.00 34.08      A    C  
ATOM   1403  O   ARG A 273      97.289  82.962 -19.649  1.00 34.48      A    O  
ATOM   1404  CB  ARG A 273     100.045  83.409 -18.777  1.00 30.69      A    C  
ATOM   1405  CG  ARG A 273      99.887  82.604 -17.479  1.00 28.94      A    C  
ATOM   1406  CD  ARG A 273     100.008  83.485 -16.244  1.00 28.21      A    C  
ATOM   1407  NE  ARG A 273      99.749  82.770 -14.991  1.00 30.33      A    N  
ATOM   1408  CZ  ARG A 273     100.608  81.937 -14.405  1.00 35.85      A    C  
ATOM   1409  NH1 ARG A 273     101.795  81.692 -14.953  1.00 32.49      A    N1+
ATOM   1410  NH2 ARG A 273     100.293  81.369 -13.250  1.00 32.28      A    N  
ATOM   1411  N   VAL A 274      97.986  80.846 -19.938  1.00 34.01      A    N  
ATOM   1412  CA  VAL A 274      96.664  80.277 -19.764  1.00 33.05      A    C  
ATOM   1413  C   VAL A 274      96.606  79.798 -18.318  1.00 37.09      A    C  
ATOM   1414  O   VAL A 274      97.320  78.869 -17.937  1.00 36.69      A    O  
ATOM   1415  CB  VAL A 274      96.448  79.086 -20.710  1.00 32.70      A    C  
ATOM   1416  CG1 VAL A 274      95.005  78.614 -20.630  1.00 27.01      A    C  
ATOM   1417  CG2 VAL A 274      96.810  79.484 -22.126  1.00 29.60      A    C  
ATOM   1418  N   CYS A 275      95.757  80.429 -17.515  1.00 39.12      A    N  
ATOM   1419  CA  CYS A 275      95.649  80.076 -16.102  1.00 42.94      A    C  
ATOM   1420  C   CYS A 275      94.233  80.145 -15.540  1.00 43.88      A    C  
ATOM   1421  O   CYS A 275      93.308  80.600 -16.205  1.00 45.57      A    O  
ATOM   1422  CB  CYS A 275      96.547  81.002 -15.287  1.00 40.95      A    C  
ATOM   1423  SG  CYS A 275      96.265  82.743 -15.657  1.00 49.83      A    S  
ATOM   1424  N   ALA A 276      94.086  79.709 -14.293  1.00 45.03      A    N  
ATOM   1425  CA  ALA A 276      92.794  79.703 -13.615  1.00 46.76      A    C  
ATOM   1426  C   ALA A 276      92.405  81.074 -13.062  1.00 44.43      A    C  
ATOM   1427  O   ALA A 276      91.221  81.342 -12.844  1.00 42.81      A    O  
ATOM   1428  CB  ALA A 276      92.809  78.672 -12.484  1.00 44.25      A    C  
ATOM   1429  N   CYS A 277      93.394  81.937 -12.846  1.00 43.09      A    N  
ATOM   1430  CA  CYS A 277      93.132  83.265 -12.297  1.00 43.31      A    C  
ATOM   1431  C   CYS A 277      93.861  84.400 -13.030  1.00 42.85      A    C  
ATOM   1432  O   CYS A 277      94.818  84.978 -12.513  1.00 42.99      A    O  
ATOM   1433  CB  CYS A 277      93.498  83.282 -10.807  1.00 43.02      A    C  
ATOM   1434  SG  CYS A 277      92.612  82.031  -9.808  1.00 52.52      A    S  
ATOM   1435  N   PRO A 278      93.397  84.748 -14.241  1.00 43.63      A    N  
ATOM   1436  CA  PRO A 278      94.015  85.819 -15.035  1.00 42.26      A    C  
ATOM   1437  C   PRO A 278      94.189  87.138 -14.273  1.00 42.31      A    C  
ATOM   1438  O   PRO A 278      95.264  87.734 -14.287  1.00 42.93      A    O  
ATOM   1439  CB  PRO A 278      93.061  85.960 -16.222  1.00 43.68      A    C  
ATOM   1440  CG  PRO A 278      92.524  84.565 -16.384  1.00 43.72      A    C  
ATOM   1441  CD  PRO A 278      92.247  84.161 -14.954  1.00 39.38      A    C  
ATOM   1442  N   GLY A 279      93.125  87.600 -13.623  1.00 44.29      A    N  
ATOM   1443  CA  GLY A 279      93.208  88.841 -12.867  1.00 43.83      A    C  
ATOM   1444  C   GLY A 279      94.322  88.813 -11.834  1.00 44.75      A    C  
ATOM   1445  O   GLY A 279      95.231  89.646 -11.855  1.00 43.28      A    O  
ATOM   1446  N   ARG A 280      94.256  87.851 -10.921  1.00 45.10      A    N  
ATOM   1447  CA  ARG A 280      95.276  87.707  -9.885  1.00 45.46      A    C  
ATOM   1448  C   ARG A 280      96.675  87.617 -10.488  1.00 46.47      A    C  
ATOM   1449  O   ARG A 280      97.590  88.331 -10.066  1.00 50.50      A    O  
ATOM   1450  CB  ARG A 280      95.018  86.449  -9.050  1.00 41.80      A    C  
ATOM   1451  CG  ARG A 280      96.124  86.146  -8.047  1.00 43.66      A    C  
ATOM   1452  CD  ARG A 280      95.943  84.784  -7.376  1.00 40.89      A    C  
ATOM   1453  NE  ARG A 280      96.292  83.674  -8.262  1.00 42.25      A    N  
ATOM   1454  CZ  ARG A 280      96.137  82.393  -7.940  1.00 43.04      A    C  
ATOM   1455  NH1 ARG A 280      95.637  82.058  -6.755  1.00 40.10      A    N1+
ATOM   1456  NH2 ARG A 280      96.492  81.443  -8.795  1.00 39.93      A    N  
ATOM   1457  N   ASP A 281      96.847  86.741 -11.476  1.00 45.39      A    N  
ATOM   1458  CA  ASP A 281      98.158  86.568 -12.086  1.00 42.43      A    C  
ATOM   1459  C   ASP A 281      98.621  87.807 -12.828  1.00 43.12      A    C  
ATOM   1460  O   ASP A 281      99.813  88.106 -12.843  1.00 43.61      A    O  
ATOM   1461  CB  ASP A 281      98.168  85.350 -13.012  1.00 42.22      A    C  
ATOM   1462  CG  ASP A 281      97.921  84.042 -12.264  1.00 42.67      A    C  
ATOM   1463  OD1 ASP A 281      97.940  82.973 -12.905  1.00 41.22      A    O  
ATOM   1464  OD2 ASP A 281      97.699  84.082 -11.033  1.00 48.05      A    O1-
ATOM   1465  N   ARG A 282      97.700  88.538 -13.446  1.00 45.21      A    N  
ATOM   1466  CA  ARG A 282      98.105  89.750 -14.141  1.00 47.31      A    C  
ATOM   1467  C   ARG A 282      98.584  90.774 -13.112  1.00 47.87      A    C  
ATOM   1468  O   ARG A 282      99.608  91.426 -13.306  1.00 48.59      A    O  
ATOM   1469  CB  ARG A 282      96.959  90.350 -14.951  1.00 48.50      A    C  
ATOM   1470  CG  ARG A 282      97.395  91.614 -15.693  1.00 47.34      A    C  
ATOM   1471  CD  ARG A 282      96.264  92.281 -16.454  1.00 49.86      A    C  
ATOM   1472  NE  ARG A 282      96.687  93.580 -16.968  1.00 47.11      A    N  
ATOM   1473  CZ  ARG A 282      95.872  94.478 -17.513  1.00 47.74      A    C  
ATOM   1474  NH1 ARG A 282      94.574  94.226 -17.631  1.00 40.24      A    N1+
ATOM   1475  NH2 ARG A 282      96.355  95.641 -17.923  1.00 47.34      A    N  
ATOM   1476  N   ARG A 283      97.845  90.910 -12.016  1.00 49.81      A    N  
ATOM   1477  CA  ARG A 283      98.229  91.849 -10.963  1.00 53.37      A    C  
ATOM   1478  C   ARG A 283      99.629  91.503 -10.460  1.00 51.63      A    C  
ATOM   1479  O   ARG A 283     100.507  92.364 -10.397  1.00 51.24      A    O  
ATOM   1480  CB  ARG A 283      97.244  91.783  -9.788  1.00 57.33      A    C  
ATOM   1481  CG  ARG A 283      95.829  92.223 -10.120  1.00 65.13      A    C  
ATOM   1482  CD  ARG A 283      94.842  91.762  -9.050  1.00 70.52      A    C  
ATOM   1483  NE  ARG A 283      93.472  91.750  -9.560  1.00 76.32      A    N  
ATOM   1484  CZ  ARG A 283      92.506  90.959  -9.098  1.00 81.10      A    C  
ATOM   1485  NH1 ARG A 283      92.758  90.107  -8.110  1.00 82.31      A    N1+
ATOM   1486  NH2 ARG A 283      91.291  91.010  -9.634  1.00 82.97      A    N  
ATOM   1487  N   THR A 284      99.832  90.235 -10.116  1.00 50.91      A    N  
ATOM   1488  CA  THR A 284     101.122  89.781  -9.607  1.00 51.49      A    C  
ATOM   1489  C   THR A 284     102.279  90.140 -10.529  1.00 51.79      A    C  
ATOM   1490  O   THR A 284     103.233  90.793 -10.107  1.00 51.69      A    O  
ATOM   1491  CB  THR A 284     101.129  88.250  -9.375  1.00 51.42      A    C  
ATOM   1492  CG2 THR A 284     102.466  87.805  -8.791  1.00 47.78      A    C  
ATOM   1493  OG1 THR A 284     100.078  87.899  -8.463  1.00 50.39      A    O  
ATOM   1494  N   GLU A 285     102.193  89.724 -11.788  1.00 54.05      A    N  
ATOM   1495  CA  GLU A 285     103.255  90.003 -12.752  1.00 54.21      A    C  
ATOM   1496  C   GLU A 285     103.485  91.484 -13.029  1.00 54.94      A    C  
ATOM   1497  O   GLU A 285     104.622  91.903 -13.228  1.00 54.98      A    O  
ATOM   1498  CB  GLU A 285     102.999  89.251 -14.064  1.00 52.25      A    C  
ATOM   1499  CG  GLU A 285     103.305  87.760 -13.945  1.00 56.89      A    C  
ATOM   1500  CD  GLU A 285     103.223  87.000 -15.265  1.00 58.42      A    C  
ATOM   1501  OE1 GLU A 285     103.731  87.511 -16.290  1.00 54.39      A    O  
ATOM   1502  OE2 GLU A 285     102.664  85.875 -15.262  1.00 57.00      A    O1-
ATOM   1503  N   GLU A 286     102.422  92.282 -13.044  1.00 58.14      A    N  
ATOM   1504  CA  GLU A 286     102.592  93.711 -13.292  1.00 61.68      A    C  
ATOM   1505  C   GLU A 286     103.239  94.388 -12.090  1.00 63.64      A    C  
ATOM   1506  O   GLU A 286     103.973  95.363 -12.240  1.00 63.08      A    O  
ATOM   1507  CB  GLU A 286     101.252  94.368 -13.626  1.00 60.15      A    C  
ATOM   1508  CG  GLU A 286     100.631  93.832 -14.907  1.00 61.42      A    C  
ATOM   1509  CD  GLU A 286      99.446  94.646 -15.381  1.00 62.30      A    C  
ATOM   1510  OE1 GLU A 286      98.621  95.044 -14.533  1.00 64.45      A    O  
ATOM   1511  OE2 GLU A 286      99.330  94.880 -16.604  1.00 62.79      A    O1-
ATOM   1512  N   GLU A 287     102.970  93.860 -10.898  1.00 66.75      A    N  
ATOM   1513  CA  GLU A 287     103.552  94.407  -9.678  1.00 70.18      A    C  
ATOM   1514  C   GLU A 287     105.037  94.066  -9.627  1.00 71.09      A    C  
ATOM   1515  O   GLU A 287     105.859  94.901  -9.248  1.00 73.10      A    O  
ATOM   1516  CB  GLU A 287     102.849  93.839  -8.439  1.00 72.27      A    C  
ATOM   1517  CG  GLU A 287     103.547  94.173  -7.119  1.00 76.95      A    C  
ATOM   1518  CD  GLU A 287     103.590  95.670  -6.811  1.00 81.25      A    C  
ATOM   1519  OE1 GLU A 287     104.331  96.060  -5.881  1.00 82.57      A    O  
ATOM   1520  OE2 GLU A 287     102.885  96.455  -7.483  1.00 81.80      A    O1-
ATOM   1521  N   ASN A 288     105.379  92.838 -10.010  1.00 70.90      A    N  
ATOM   1522  CA  ASN A 288     106.771  92.402 -10.011  1.00 71.68      A    C  
ATOM   1523  C   ASN A 288     107.570  93.190 -11.036  1.00 72.38      A    C  
ATOM   1524  O   ASN A 288     108.777  93.365 -10.893  1.00 73.21      A    O  
ATOM   1525  CB  ASN A 288     106.865  90.905 -10.317  1.00 70.88      A    C  
ATOM   1526  CG  ASN A 288     106.499  90.039  -9.123  1.00 73.20      A    C  
ATOM   1527  ND2 ASN A 288     107.297  89.007  -8.876  1.00 74.76      A    N  
ATOM   1528  OD1 ASN A 288     105.508  90.291  -8.436  1.00 74.52      A    O  
ATOM   1529  N   LEU A 289     106.892  93.664 -12.076  1.00 74.33      A    N  
ATOM   1530  CA  LEU A 289     107.553  94.447 -13.113  1.00 76.21      A    C  
ATOM   1531  C   LEU A 289     107.772  95.866 -12.595  1.00 77.97      A    C  
ATOM   1532  O   LEU A 289     108.767  96.514 -12.921  1.00 76.91      A    O  
ATOM   1533  CB  LEU A 289     106.696  94.490 -14.382  1.00 73.31      A    C  
ATOM   1534  CG  LEU A 289     107.258  95.325 -15.541  1.00 70.86      A    C  
ATOM   1535  CD1 LEU A 289     108.558  94.717 -16.040  1.00 69.38      A    C  
ATOM   1536  CD2 LEU A 289     106.241  95.391 -16.662  1.00 69.08      A    C  
ATOM   1537  N   ARG A 290     106.828  96.334 -11.785  1.00 79.98      A    N  
ATOM   1538  CA  ARG A 290     106.886  97.672 -11.212  1.00 83.39      A    C  
ATOM   1539  C   ARG A 290     108.042  97.777 -10.221  1.00 84.71      A    C  
ATOM   1540  O   ARG A 290     108.792  98.755 -10.224  1.00 84.52      A    O  
ATOM   1541  CB  ARG A 290     105.572  97.991 -10.497  1.00 85.34      A    C  
ATOM   1542  CG  ARG A 290     105.369  99.465 -10.189  1.00 88.80      A    C  
ATOM   1543  CD  ARG A 290     104.525  99.651  -8.942  1.00 90.96      A    C  
ATOM   1544  NE  ARG A 290     105.232  99.180  -7.756  1.00 92.61      A    N  
ATOM   1545  CZ  ARG A 290     104.730  99.200  -6.526  1.00 94.45      A    C  
ATOM   1546  NH1 ARG A 290     103.507  99.668  -6.313  1.00 95.33      A    N1+
ATOM   1547  NH2 ARG A 290     105.453  98.752  -5.508  1.00 95.33      A    N  
ATOM   1548  N   LYS A 291     108.179  96.764  -9.373  1.00 86.26      A    N  
ATOM   1549  CA  LYS A 291     109.242  96.743  -8.376  1.00 88.20      A    C  
ATOM   1550  C   LYS A 291     110.606  96.803  -9.052  1.00 89.42      A    C  
ATOM   1551  O   LYS A 291     111.537  97.426  -8.542  1.00 91.00      A    O  
ATOM   1552  CB  LYS A 291     109.152  95.470  -7.531  1.00 87.37      A    C  
ATOM   1553  CG  LYS A 291     107.874  95.341  -6.722  1.00 88.34      A    C  
ATOM   1554  CD  LYS A 291     107.874  94.052  -5.915  1.00 89.97      A    C  
ATOM   1555  CE  LYS A 291     106.596  93.909  -5.105  1.00 91.44      A    C  
ATOM   1556  NZ  LYS A 291     106.574  92.649  -4.306  1.00 92.93      A    N1+
ATOM   1557  N   LYS A 321     110.714  96.153 -10.205  1.00 90.68      A    N  
ATOM   1558  CA  LYS A 321     111.963  96.112 -10.955  1.00 92.05      A    C  
ATOM   1559  C   LYS A 321     112.310  97.475 -11.554  1.00 92.57      A    C  
ATOM   1560  O   LYS A 321     113.420  97.681 -12.041  1.00 93.33      A    O  
ATOM   1561  CB  LYS A 321     111.861  95.049 -12.054  1.00 93.40      A    C  
ATOM   1562  CG  LYS A 321     113.176  94.666 -12.710  1.00 92.92      A    C  
ATOM   1563  CD  LYS A 321     112.970  93.486 -13.650  1.00 93.98      A    C  
ATOM   1564  CE  LYS A 321     114.277  93.028 -14.272  1.00 95.33      A    C  
ATOM   1565  NZ  LYS A 321     114.081  91.828 -15.137  1.00 95.33      A    N1+
TER   
END


A second structure was input as follows:


CRYST1   64.999   71.057  105.099  90.00  90.00  90.00 P 21 21 21    8
ATOM      1  N   SER A  96     114.582  73.470 -35.930  1.00 32.91      A    N  
ANISOU    1  N   SER A  96     4210   4339   3957    387    834   -416  A    N  
ATOM      2  CA  SER A  96     114.474  74.882 -36.270  1.00 31.88      A    C  
ANISOU    2  CA  SER A  96     3962   4296   3854    457    684   -483  A    C  
ATOM      3  C   SER A  96     113.490  75.601 -35.354  1.00 27.76      A    C  
ANISOU    3  C   SER A  96     3167   3847   3535    510    505   -393  A    C  
ATOM      4  O   SER A  96     112.794  74.977 -34.541  1.00 26.43      A    O  
ANISOU    4  O   SER A  96     2857   3580   3606    396    397   -660  A    O  
ATOM      5  CB  SER A  96     114.062  75.063 -37.733  1.00 34.39      A    C  
ANISOU    5  CB  SER A  96     4298   4636   4132    267    667   -505  A    C  
ATOM      6  OG  SER A  96     112.709  74.696 -37.937  1.00 36.17      A    O  
ANISOU    6  OG  SER A  96     4618   4831   4296    147    638   -558  A    O  
ATOM      7  N   VAL A  97     113.450  76.923 -35.488  1.00 24.74      A    N  
ANISOU    7  N   VAL A  97     2683   3510   3206    680    305   -155  A    N  
ATOM      8  CA  VAL A  97     112.616  77.776 -34.647  1.00 21.66      A    C  
ANISOU    8  CA  VAL A  97     2228   3085   2917    692    136    154  A    C  
ATOM      9  C   VAL A  97     111.952  78.837 -35.518  1.00 19.91      A    C  
ANISOU    9  C   VAL A  97     1916   2999   2650    538    216    254  A    C  
ATOM     10  O   VAL A  97     112.641  79.536 -36.274  1.00 21.34      A    O  
ANISOU   10  O   VAL A  97     1929   3426   2752    441    454    387  A    O  
ATOM     11  CB  VAL A  97     113.437  78.443 -33.533  1.00 22.26      A    C  
ANISOU   11  CB  VAL A  97     2377   3032   3048    620   -180    375  A    C  
ATOM     12  CG1 VAL A  97     112.544  79.339 -32.709  1.00 24.71      A    C  
ANISOU   12  CG1 VAL A  97     2888   3298   3204    501   -215    347  A    C  
ATOM     13  CG2 VAL A  97     114.122  77.401 -32.650  1.00 21.51      A    C  
ANISOU   13  CG2 VAL A  97     2300   2843   3031    637   -423    572  A    C  
ATOM     14  N   PRO A  98     110.635  78.998 -35.441  1.00 17.60      A    N  
ANISOU   14  N   PRO A  98     1537   2723   2429    496    167    220  A    N  
ATOM     15  CA  PRO A  98     109.976  80.067 -36.200  1.00 18.58      A    C  
ANISOU   15  CA  PRO A  98     1743   2839   2478    427    -23    257  A    C  
ATOM     16  C   PRO A  98     110.424  81.438 -35.714  1.00 18.38      A    C  
ANISOU   16  C   PRO A  98     1938   2653   2392    557    -31    457  A    C  
ATOM     17  O   PRO A  98     110.623  81.659 -34.519  1.00 18.73      A    O  
ANISOU   17  O   PRO A  98     2157   2650   2311    316   -141    375  A    O  
ATOM     18  CB  PRO A  98     108.487  79.842 -35.905  1.00 19.79      A    C  
ANISOU   18  CB  PRO A  98     1783   3066   2670    218   -119    127  A    C  
ATOM     19  CG  PRO A  98     108.393  78.426 -35.418  1.00 19.86      A    C  
ANISOU   19  CG  PRO A  98     1710   3197   2640     37    -86    212  A    C  
ATOM     20  CD  PRO A  98     109.676  78.158 -34.705  1.00 17.91      A    C  
ANISOU   20  CD  PRO A  98     1504   2815   2484    167    -28    285  A    C  
ATOM     21  N   SER A  99     110.576  82.366 -36.656  1.00 18.22      A    N  
ANISOU   21  N   SER A  99     1946   2591   2385    560    245    449  A    N  
ATOM     22  CA  SER A  99     110.928  83.730 -36.296  1.00 19.21      A    C  
ANISOU   22  CA  SER A  99     2223   2634   2442    517    392    527  A    C  
ATOM     23  C   SER A  99     109.791  84.391 -35.526  1.00 18.23      A    C  
ANISOU   23  C   SER A  99     2201   2404   2323    506    344    454  A    C  
ATOM     24  O   SER A  99     108.608  84.132 -35.766  1.00 18.11      A    O  
ANISOU   24  O   SER A  99     2352   2210   2318    312    441    609  A    O  
ATOM     25  CB  SER A  99     111.218  84.546 -37.554  1.00 19.94      A    C  
ANISOU   25  CB  SER A  99     2359   2677   2540    466    544    592  A    C  
ATOM     26  OG  SER A  99     111.374  85.922 -37.244  1.00 20.70      A    O  
ANISOU   26  OG  SER A  99     2283   2903   2680    407    552    539  A    O  
ATOM     27  N   GLN A 100     110.165  85.258 -34.585  1.00 17.99      A    N  
ANISOU   27  N   GLN A 100     2231   2320   2283    598    182    569  A    N  
ATOM     28  CA  GLN A 100     109.202  86.055 -33.834  1.00 17.41      A    C  
ANISOU   28  CA  GLN A 100     2151   2171   2295    448    154    682  A    C  
ATOM     29  C   GLN A 100     109.387  87.545 -34.075  1.00 17.44      A    C  
ANISOU   29  C   GLN A 100     2094   2207   2324    338    260    714  A    C  
ATOM     30  O   GLN A 100     108.827  88.357 -33.332  1.00 19.35      A    O  
ANISOU   30  O   GLN A 100     2423   2473   2457    435    405    672  A    O  
ATOM     31  CB  GLN A 100     109.285  85.748 -32.335  1.00 18.85      A    C  
ANISOU   31  CB  GLN A 100     2340   2439   2382    260     28    669  A    C  
ATOM     32  CG  GLN A 100     110.630  86.075 -31.715  1.00 19.62      A    C  
ANISOU   32  CG  GLN A 100     2462   2558   2436    145     91    833  A    C  
ATOM     33  CD  GLN A 100     110.678  85.710 -30.249  1.00 20.59      A    C  
ANISOU   33  CD  GLN A 100     2639   2598   2585     22    153    833  A    C  
ATOM     34  NE2 GLN A 100     110.314  86.657 -29.395  1.00 20.55      A    N  
ANISOU   34  NE2 GLN A 100     2617   2665   2525    -60    256    712  A    N  
ATOM     35  OE1 GLN A 100     111.032  84.585 -29.885  1.00 22.05      A    O  
ANISOU   35  OE1 GLN A 100     2821   2687   2871    273     45    661  A    O  
ATOM     36  N   LYS A 101     110.153  87.921 -35.094  1.00 17.02      A    N  
ANISOU   36  N   LYS A 101     1825   2356   2288     91     41    760  A    N  
ATOM     37  CA  LYS A 101     110.438  89.324 -35.356  1.00 17.25      A    C  
ANISOU   37  CA  LYS A 101     1877   2374   2304    152    -24    650  A    C  
ATOM     38  C   LYS A 101     109.182  90.046 -35.834  1.00 15.60      A    C  
ANISOU   38  C   LYS A 101     1592   2275   2062    -51    -27    556  A    C  
ATOM     39  O   LYS A 101     108.549  89.640 -36.814  1.00 14.33      A    O  
ANISOU   39  O   LYS A 101     1451   2019   1976   -175    -91    545  A    O  
ATOM     40  CB  LYS A 101     111.530  89.415 -36.422  1.00 19.14      A    C  
ANISOU   40  CB  LYS A 101     2075   2640   2556      6    -68    682  A    C  
ATOM     41  CG  LYS A 101     111.807  90.807 -36.950  1.00 23.19      A    C  
ANISOU   41  CG  LYS A 101     2849   3091   2870     73   -181    656  A    C  
ATOM     42  CD  LYS A 101     112.605  91.635 -35.967  1.00 27.24      A    C  
ANISOU   42  CD  LYS A 101     3510   3627   3212    241   -152    704  A    C  
ATOM     43  CE  LYS A 101     113.105  92.913 -36.632  1.00 29.73      A    C  
ANISOU   43  CE  LYS A 101     3943   3972   3383    389   -150    760  A    C  
ATOM     44  NZ  LYS A 101     113.894  92.623 -37.861  1.00 32.27      A    N1+
ANISOU   44  NZ  LYS A 101     4328   4367   3566    425   -266    669  A    N1+
ATOM     45  N   THR A 102     108.824  91.127 -35.145  1.00 14.68      A    N  
ANISOU   45  N   THR A 102     1432   2363   1782   -124    135    587  A    N  
ATOM     46  CA  THR A 102     107.686  91.930 -35.571  1.00 14.35      A    C  
ANISOU   46  CA  THR A 102     1497   2227   1727    -31     47    416  A    C  
ATOM     47  C   THR A 102     107.971  92.520 -36.946  1.00 13.50      A    C  
ANISOU   47  C   THR A 102     1369   1993   1767    -36     -6    501  A    C  
ATOM     48  O   THR A 102     109.060  93.043 -37.196  1.00 15.23      A    O  
ANISOU   48  O   THR A 102     1465   2282   2039   -364     28    457  A    O  
ATOM     49  CB  THR A 102     107.439  93.043 -34.554  1.00 16.21      A    C  
ANISOU   49  CB  THR A 102     2046   2320   1793    -73      0    293  A    C  
ATOM     50  CG2 THR A 102     106.282  93.930 -34.988  1.00 16.30      A    C  
ANISOU   50  CG2 THR A 102     2113   2204   1878    -91    -55     65  A    C  
ATOM     51  OG1 THR A 102     107.119  92.456 -33.287  1.00 18.29      A    O  
ANISOU   51  OG1 THR A 102     2453   2654   1841    -13    -38    287  A    O  
ATOM     52  N   TYR A 103     106.991  92.429 -37.839  1.00 12.13      A    N  
ANISOU   52  N   TYR A 103     1534   1669   1404    -87    120    271  A    N  
ATOM     53  CA  TYR A 103     107.180  92.853 -39.222  1.00 12.30      A    C  
ANISOU   53  CA  TYR A 103     1707   1566   1401    216    195    248  A    C  
ATOM     54  C   TYR A 103     105.834  93.337 -39.742  1.00 11.53      A    C  
ANISOU   54  C   TYR A 103     1767   1240   1373     58    132    320  A    C  
ATOM     55  O   TYR A 103     104.943  92.527 -40.009  1.00 12.69      A    O  
ANISOU   55  O   TYR A 103     2178   1211   1434   -313     10    347  A    O  
ATOM     56  CB  TYR A 103     107.710  91.683 -40.049  1.00 14.98      A    C  
ANISOU   56  CB  TYR A 103     1998   2133   1562    427    487    263  A    C  
ATOM     57  CG  TYR A 103     107.791  91.934 -41.538  1.00 17.93      A    C  
ANISOU   57  CG  TYR A 103     2434   2736   1645    647    556    366  A    C  
ATOM     58  CD1 TYR A 103     108.512  93.006 -42.051  1.00 19.82      A    C  
ANISOU   58  CD1 TYR A 103     2762   3071   1698    740    741    530  A    C  
ATOM     59  CD2 TYR A 103     107.165  91.077 -42.437  1.00 19.32      A    C  
ANISOU   59  CD2 TYR A 103     2597   3102   1641    880    418    214  A    C  
ATOM     60  CE1 TYR A 103     108.589  93.219 -43.423  1.00 21.54      A    C  
ANISOU   60  CE1 TYR A 103     3082   3411   1690    786    593    621  A    C  
ATOM     61  CE2 TYR A 103     107.242  91.280 -43.798  1.00 21.42      A    C  
ANISOU   61  CE2 TYR A 103     2936   3465   1737    854    439    300  A    C  
ATOM     62  CZ  TYR A 103     107.951  92.348 -44.286  1.00 22.31      A    C  
ANISOU   62  CZ  TYR A 103     3233   3586   1656    982    572    618  A    C  
ATOM     63  OH  TYR A 103     108.020  92.540 -45.646  1.00 24.99      A    O  
ANISOU   63  OH  TYR A 103     3662   4046   1789   1133    560    678  A    O  
ATOM     64  N   GLN A 104     105.671  94.656 -39.875  1.00 11.14      A    N  
ANISOU   64  N   GLN A 104     1695   1147   1391     31    203    294  A    N  
ATOM     65  CA  GLN A 104     104.395  95.162 -40.377  1.00 11.33      A    C  
ANISOU   65  CA  GLN A 104     1816   1111   1378     68    229    115  A    C  
ATOM     66  C   GLN A 104     104.213  94.869 -41.860  1.00 11.96      A    C  
ANISOU   66  C   GLN A 104     1849   1353   1341    -69    303    153  A    C  
ATOM     67  O   GLN A 104     103.082  94.645 -42.307  1.00 12.86      A    O  
ANISOU   67  O   GLN A 104     1925   1576   1386    -70    167    115  A    O  
ATOM     68  CB  GLN A 104     104.257  96.656 -40.112  1.00 13.05      A    C  
ANISOU   68  CB  GLN A 104     2319   1201   1438   -210    163     43  A    C  
ATOM     69  CG  GLN A 104     104.054  96.989 -38.652  1.00 15.40      A    C  
ANISOU   69  CG  GLN A 104     2826   1542   1483     53    201    -12  A    C  
ATOM     70  CD  GLN A 104     103.236  98.246 -38.457  1.00 18.52      A    C  
ANISOU   70  CD  GLN A 104     3355   1927   1755    115    279     10  A    C  
ATOM     71  NE2 GLN A 104     102.797  98.473 -37.230  1.00 19.91      A    N  
ANISOU   71  NE2 GLN A 104     3357   2332   1876   -255    286   -239  A    N  
ATOM     72  OE1 GLN A 104     102.985  98.999 -39.405  1.00 21.58      A    O  
ANISOU   72  OE1 GLN A 104     3786   2270   2145    283    214   -131  A    O  
ATOM     73  N   GLY A 105     105.299  94.857 -42.631  1.00 13.41      A    N  
ANISOU   73  N   GLY A 105     2036   1708   1350     46    444    339  A    N  
ATOM     74  CA  GLY A 105     105.195  94.565 -44.051  1.00 14.21      A    C  
ANISOU   74  CA  GLY A 105     2153   1744   1503     94    437    296  A    C  
ATOM     75  C   GLY A 105     104.463  95.647 -44.841  1.00 15.02      A    C  
ANISOU   75  C   GLY A 105     2216   1815   1677    -11    531    333  A    C  
ATOM     76  O   GLY A 105     104.152  96.737 -44.355  1.00 15.00      A    O  
ANISOU   76  O   GLY A 105     2251   1642   1804    -69    418    181  A    O  
ATOM     77  N   SER A 106     104.176  95.304 -46.095  1.00 15.16      A    N  
ANISOU   77  N   SER A 106     2237   1919   1605    139    495    361  A    N  
ATOM     78  CA  SER A 106     103.635  96.276 -47.038  1.00 16.48      A    C  
ANISOU   78  CA  SER A 106     2545   2121   1594    189    564    517  A    C  
ATOM     79  C   SER A 106     102.236  96.737 -46.676  1.00 16.13      A    C  
ANISOU   79  C   SER A 106     2596   2019   1513     91    332    570  A    C  
ATOM     80  O   SER A 106     101.828  97.828 -47.097  1.00 17.18      A    O  
ANISOU   80  O   SER A 106     2815   2057   1656     52    255    554  A    O  
ATOM     81  CB  SER A 106     103.595  95.672 -48.439  1.00 19.90      A    C  
ANISOU   81  CB  SER A 106     3092   2787   1681    653    891    413  A    C  
ATOM     82  OG  SER A 106     104.892  95.297 -48.853  1.00 25.06      A    O  
ANISOU   82  OG  SER A 106     3840   3511   2171    657    738    363  A    O  
ATOM     83  N   TYR A 107     101.487  95.931 -45.931  1.00 14.35      A    N  
ANISOU   83  N   TYR A 107     2312   1832   1306    -55    146    405  A    N  
ATOM     84  CA  TYR A 107     100.110  96.259 -45.599  1.00 13.54      A    C  
ANISOU   84  CA  TYR A 107     2243   1627   1273    107    107    109  A    C  
ATOM     85  C   TYR A 107      99.957  96.883 -44.225  1.00 13.29      A    C  
ANISOU   85  C   TYR A 107     2328   1502   1221     14     49    294  A    C  
ATOM     86  O   TYR A 107      98.834  97.205 -43.840  1.00 14.11      A    O  
ANISOU   86  O   TYR A 107     2337   1691   1334    125    133     77  A    O  
ATOM     87  CB  TYR A 107      99.210  95.024 -45.764  1.00 13.19      A    C  
ANISOU   87  CB  TYR A 107     2252   1509   1249    -24    172   -141  A    C  
ATOM     88  CG  TYR A 107      99.349  94.483 -47.161  1.00 14.17      A    C  
ANISOU   88  CG  TYR A 107     2256   1825   1304    127    124   -227  A    C  
ATOM     89  CD1 TYR A 107      98.759  95.143 -48.231  1.00 15.67      A    C  
ANISOU   89  CD1 TYR A 107     2397   2220   1337    -21     71      6  A    C  
ATOM     90  CD2 TYR A 107     100.131  93.367 -47.429  1.00 16.27      A    C  
ANISOU   90  CD2 TYR A 107     2361   2312   1507    -62    266   -404  A    C  
ATOM     91  CE1 TYR A 107      98.912  94.694 -49.521  1.00 17.42      A    C  
ANISOU   91  CE1 TYR A 107     2648   2599   1371   -107     71   -223  A    C  
ATOM     92  CE2 TYR A 107     100.288  92.903 -48.732  1.00 16.95      A    C  
ANISOU   92  CE2 TYR A 107     2430   2559   1451   -157    312   -470  A    C  
ATOM     93  CZ  TYR A 107      99.676  93.577 -49.771  1.00 18.24      A    C  
ANISOU   93  CZ  TYR A 107     2695   2885   1349   -107    331   -467  A    C  
ATOM     94  OH  TYR A 107      99.822  93.140 -51.069  1.00 21.38      A    O  
ANISOU   94  OH  TYR A 107     3111   3580   1434   -159    350   -602  A    O  
ATOM     95  N   GLY A 108     101.052  97.093 -43.500  1.00 12.02      A    N  
ANISOU   95  N   GLY A 108     2085   1328   1153    -14    -70    115  A    N  
ATOM     96  CA  GLY A 108     100.973  97.701 -42.179  1.00 11.93      A    C  
ANISOU   96  CA  GLY A 108     1940   1447   1146   -117     85    106  A    C  
ATOM     97  C   GLY A 108     100.264  96.820 -41.171  1.00 10.91      A    C  
ANISOU   97  C   GLY A 108     1777   1210   1159   -143    102    194  A    C  
ATOM     98  O   GLY A 108      99.425  97.313 -40.406  1.00 12.07      A    O  
ANISOU   98  O   GLY A 108     1880   1393   1313    101     98     13  A    O  
ATOM     99  N   PHE A 109     100.589  95.527 -41.151  1.00 10.77      A    N  
ANISOU   99  N   PHE A 109     1774   1052   1264   -143    119    195  A    N  
ATOM    100  CA  PHE A 109      99.874  94.550 -40.342  1.00 10.22      A    C  
ANISOU  100  CA  PHE A 109     1713   1060   1110      6    174    116  A    C  
ATOM    101  C   PHE A 109     100.303  94.623 -38.881  1.00 10.23      A    C  
ANISOU  101  C   PHE A 109     1542   1238   1108   -125    123     17  A    C  
ATOM    102  O   PHE A 109     101.501  94.635 -38.581  1.00 12.27      A    O  
ANISOU  102  O   PHE A 109     1663   1677   1323    -32    192     79  A    O  
ATOM    103  CB  PHE A 109     100.184  93.155 -40.881  1.00 10.00      A    C  
ANISOU  103  CB  PHE A 109     1663    900   1236    293    100     92  A    C  
ATOM    104  CG  PHE A 109      99.603  92.038 -40.061  1.00  9.89      A    C  
ANISOU  104  CG  PHE A 109     1620   1025   1115    199     84     63  A    C  
ATOM    105  CD1 PHE A 109      98.241  91.794 -40.067  1.00 11.08      A    C  
ANISOU  105  CD1 PHE A 109     1803   1238   1169     69    182    -39  A    C  
ATOM    106  CD2 PHE A 109     100.425  91.215 -39.300  1.00 10.82      A    C  
ANISOU  106  CD2 PHE A 109     1813   1121   1179    167    108     -4  A    C  
ATOM    107  CE1 PHE A 109      97.703  90.748 -39.323  1.00 11.99      A    C  
ANISOU  107  CE1 PHE A 109     1952   1335   1270    -12    -14    210  A    C  
ATOM    108  CE2 PHE A 109      99.894  90.166 -38.554  1.00 10.89      A    C  
ANISOU  108  CE2 PHE A 109     1568   1298   1273     53    252     51  A    C  
ATOM    109  CZ  PHE A 109      98.531  89.934 -38.565  1.00 11.38      A    C  
ANISOU  109  CZ  PHE A 109     1773   1228   1323    -32     34    172  A    C  
ATOM    110  N   ARG A 110      99.325  94.635 -37.976  1.00  9.83      A    N  
ANISOU  110  N   ARG A 110     1551   1150   1032    -16    128    138  A    N  
ATOM    111  CA  ARG A 110      99.613  94.542 -36.549  1.00 10.24      A    C  
ANISOU  111  CA  ARG A 110     1500   1341   1052   -195    -54     -8  A    C  
ATOM    112  C   ARG A 110      98.368  94.080 -35.808  1.00  9.86      A    C  
ANISOU  112  C   ARG A 110     1507   1196   1044   -172   -154     71  A    C  
ATOM    113  O   ARG A 110      97.251  94.149 -36.324  1.00 10.28      A    O  
ANISOU  113  O   ARG A 110     1407   1359   1139     -7   -102    123  A    O  
ATOM    114  CB  ARG A 110     100.136  95.864 -35.961  1.00 10.68      A    C  
ANISOU  114  CB  ARG A 110     1432   1374   1253    182   -253     24  A    C  
ATOM    115  CG  ARG A 110      99.101  96.982 -35.828  1.00 11.28      A    C  
ANISOU  115  CG  ARG A 110     1699   1375   1212    180   -315    207  A    C  
ATOM    116  CD  ARG A 110      98.854  97.698 -37.149  1.00 11.55      A    C  
ANISOU  116  CD  ARG A 110     1905   1302   1182    286   -362    178  A    C  
ATOM    117  NE  ARG A 110      97.977  98.849 -36.952  1.00 11.80      A    N  
ANISOU  117  NE  ARG A 110     2004   1107   1372    323   -285    133  A    N  
ATOM    118  CZ  ARG A 110      97.544  99.635 -37.935  1.00 13.35      A    C  
ANISOU  118  CZ  ARG A 110     2542   1178   1351    381     90    160  A    C  
ATOM    119  NH1 ARG A 110      97.912  99.406 -39.190  1.00 14.75      A    N1+
ANISOU  119  NH1 ARG A 110     2909   1487   1207    518    265    152  A    N1+
ATOM    120  NH2 ARG A 110      96.737 100.655 -37.670  1.00 15.31      A    N  
ANISOU  120  NH2 ARG A 110     2724   1457   1635    424    163    -72  A    N  
ATOM    121  N   LEU A 111      98.581  93.621 -34.576  1.00  9.75      A    N  
ANISOU  121  N   LEU A 111     1550   1199    955     -6   -108    120  A    N  
ATOM    122  CA  LEU A 111      97.491  93.131 -33.741  1.00  9.51      A    C  
ANISOU  122  CA  LEU A 111     1572    984   1058   -204    -23    141  A    C  
ATOM    123  C   LEU A 111      96.913  94.249 -32.883  1.00 10.48      A    C  
ANISOU  123  C   LEU A 111     1545   1158   1279   -333     -8    -47  A    C  
ATOM    124  O   LEU A 111      97.526  95.299 -32.681  1.00 13.00      A    O  
ANISOU  124  O   LEU A 111     1838   1380   1722   -269    226   -287  A    O  
ATOM    125  CB  LEU A 111      97.999  92.035 -32.807  1.00 10.36      A    C  
ANISOU  125  CB  LEU A 111     1701   1173   1063     25      4    136  A    C  
ATOM    126  CG  LEU A 111      98.661  90.855 -33.503  1.00 10.47      A    C  
ANISOU  126  CG  LEU A 111     1654   1146   1178    210   -162     15  A    C  
ATOM    127  CD1 LEU A 111      99.164  89.879 -32.461  1.00 11.53      A    C  
ANISOU  127  CD1 LEU A 111     1765   1396   1222    216   -284    217  A    C  
ATOM    128  CD2 LEU A 111      97.693  90.188 -34.477  1.00 10.80      A    C  
ANISOU  128  CD2 LEU A 111     1724   1130   1250    305   -191    -34  A    C  
ATOM    129  N   GLY A 112      95.723  93.987 -32.343  1.00  9.88      A    N  
ANISOU  129  N   GLY A 112     1534   1120   1099   -150    103   -149  A    N  
ATOM    130  CA  GLY A 112      95.145  94.838 -31.325  1.00  9.74      A    C  
ANISOU  130  CA  GLY A 112     1614   1027   1061   -162    149   -151  A    C  
ATOM    131  C   GLY A 112      94.394  93.985 -30.325  1.00  8.84      A    C  
ANISOU  131  C   GLY A 112     1245   1023   1090    245    -50   -252  A    C  
ATOM    132  O   GLY A 112      93.955  92.875 -30.636  1.00  9.87      A    O  
ANISOU  132  O   GLY A 112     1411   1185   1154    -91    -22   -202  A    O  
ATOM    133  N   PHE A 113      94.261  94.512 -29.111  1.00 10.41      A    N  
ANISOU  133  N   PHE A 113     1376   1428   1153    375    -23   -112  A    N  
ATOM    134  CA  PHE A 113      93.578  93.805 -28.040  1.00 10.94      A    C  
ANISOU  134  CA  PHE A 113     1324   1655   1177    404    -44   -165  A    C  
ATOM    135  C   PHE A 113      92.577  94.717 -27.360  1.00 13.39      A    C  
ANISOU  135  C   PHE A 113     1601   2006   1481    409     27   -406  A    C  
ATOM    136  O   PHE A 113      92.794  95.922 -27.248  1.00 14.93      A    O  
ANISOU  136  O   PHE A 113     1908   2012   1751    610    158   -394  A    O  
ATOM    137  CB  PHE A 113      94.567  93.267 -27.000  1.00 11.53      A    C  
ANISOU  137  CB  PHE A 113     1485   1730   1165    387   -298    -61  A    C  
ATOM    138  CG  PHE A 113      95.533  92.285 -27.565  1.00 10.93      A    C  
ANISOU  138  CG  PHE A 113     1553   1403   1199    243   -398   -239  A    C  
ATOM    139  CD1 PHE A 113      96.700  92.723 -28.167  1.00 11.02      A    C  
ANISOU  139  CD1 PHE A 113     1405   1576   1203    197   -229   -220  A    C  
ATOM    140  CD2 PHE A 113      95.272  90.924 -27.524  1.00 12.26      A    C  
ANISOU  140  CD2 PHE A 113     1812   1519   1326    256   -499   -182  A    C  
ATOM    141  CE1 PHE A 113      97.595  91.832 -28.720  1.00 12.70      A    C  
ANISOU  141  CE1 PHE A 113     1749   1802   1273    219   -326   -416  A    C  
ATOM    142  CE2 PHE A 113      96.175  90.020 -28.057  1.00 13.52      A    C  
ANISOU  142  CE2 PHE A 113     1929   1752   1456    263   -445   -346  A    C  
ATOM    143  CZ  PHE A 113      97.335  90.478 -28.665  1.00 13.56      A    C  
ANISOU  143  CZ  PHE A 113     1862   1847   1445    286   -576   -392  A    C  
ATOM    144  N   LEU A 114      91.489  94.118 -26.886  1.00 15.22      A    N  
ANISOU  144  N   LEU A 114     1755   2341   1689    202    263   -516  A    N  
ATOM    145  CA  LEU A 114      90.491  94.844 -26.120  1.00 16.52      A    C  
ANISOU  145  CA  LEU A 114     1758   2583   1938    221    300   -474  A    C  
ATOM    146  C   LEU A 114      91.052  95.230 -24.756  1.00 15.29      A    C  
ANISOU  146  C   LEU A 114     1692   2327   1789    367    231   -473  A    C  
ATOM    147  O   LEU A 114      92.104  94.751 -24.324  1.00 17.26      A    O  
ANISOU  147  O   LEU A 114     2107   2647   1804    528    217   -493  A    O  
ATOM    148  CB  LEU A 114      89.258  93.970 -25.899  1.00 19.32      A    C  
ANISOU  148  CB  LEU A 114     1999   3035   2305    184    133   -613  A    C  
ATOM    149  CG  LEU A 114      88.568  93.460 -27.160  1.00 22.73      A    C  
ANISOU  149  CG  LEU A 114     2535   3468   2633    126    -99   -715  A    C  
ATOM    150  CD1 LEU A 114      87.472  92.470 -26.794  1.00 23.65      A    C  
ANISOU  150  CD1 LEU A 114     2597   3548   2842    179     11   -745  A    C  
ATOM    151  CD2 LEU A 114      88.006  94.631 -27.944  1.00 24.11      A    C  
ANISOU  151  CD2 LEU A 114     2896   3704   2560    317   -399   -679  A    C  
ATOM    152  N   HIS A 115      90.319  96.097 -24.063  1.00 15.91      A    N  
ANISOU  152  N   HIS A 115     2208   2024   1811    301    153   -483  A    N  
ATOM    153  CA  HIS A 115      90.686  96.567 -22.727  1.00 16.20      A    C  
ANISOU  153  CA  HIS A 115     2497   1721   1937    291    105   -426  A    C  
ATOM    154  C   HIS A 115      89.700  95.970 -21.729  1.00 17.88      A    C  
ANISOU  154  C   HIS A 115     2521   1973   2298    283    350   -332  A    C  
ATOM    155  O   HIS A 115      88.673  96.568 -21.406  1.00 20.79      A    O  
ANISOU  155  O   HIS A 115     2912   2270   2720    486    365   -201  A    O  
ATOM    156  CB  HIS A 115      90.705  98.082 -22.697  1.00 18.21      A    C  
ANISOU  156  CB  HIS A 115     2858   1888   2175    128     28   -479  A    C  
ATOM    157  CG  HIS A 115      91.656  98.660 -23.689  1.00 20.43      A    C  
ANISOU  157  CG  HIS A 115     3372   1796   2593   -100    141   -281  A    C  
ATOM    158  CD2 HIS A 115      91.482  99.015 -24.982  1.00 21.49      A    C  
ANISOU  158  CD2 HIS A 115     3608   1883   2675   -251    113    -24  A    C  
ATOM    159  ND1 HIS A 115      92.993  98.848 -23.414  1.00 21.64      A    N  
ANISOU  159  ND1 HIS A 115     3799   1657   2767    -14    192   -277  A    N  
ATOM    160  CE1 HIS A 115      93.595  99.327 -24.487  1.00 20.71      A    C  
ANISOU  160  CE1 HIS A 115     3742   1536   2592    -30    205   -104  A    C  
ATOM    161  NE2 HIS A 115      92.701  99.438 -25.452  1.00 22.92      A    N  
ANISOU  161  NE2 HIS A 115     3919   2042   2749   -126    237    -46  A    N  
ATOM    162  N   SER A 116      90.041  94.793 -21.223  1.00 17.39      A    N  
ANISOU  162  N   SER A 116     2586   1850   2170    132    315   -273  A    N  
ATOM    163  CA  SER A 116      89.125  93.989 -20.431  1.00 18.47      A    C  
ANISOU  163  CA  SER A 116     2964   1871   2184     40    275   -364  A    C  
ATOM    164  C   SER A 116      89.265  94.205 -18.932  1.00 18.43      A    C  
ANISOU  164  C   SER A 116     2873   1963   2168    -80    273   -394  A    C  
ATOM    165  O   SER A 116      88.382  93.777 -18.180  1.00 19.45      A    O  
ANISOU  165  O   SER A 116     2823   2294   2273      9    337   -294  A    O  
ATOM    166  CB  SER A 116      89.332  92.506 -20.761  1.00 20.51      A    C  
ANISOU  166  CB  SER A 116     3660   1953   2179   -202    210   -570  A    C  
ATOM    167  OG  SER A 116      89.166  92.278 -22.152  1.00 24.86      A    O  
ANISOU  167  OG  SER A 116     4270   2619   2556    210    -12   -612  A    O  
ATOM    168  N   GLY A 117      90.335  94.858 -18.476  1.00 17.25      A    N  
ANISOU  168  N   GLY A 117     2765   1799   1990   -112    169   -496  A    N  
ATOM    169  CA  GLY A 117      90.519  95.082 -17.056  1.00 17.27      A    C  
ANISOU  169  CA  GLY A 117     2831   1893   1836   -188    313   -406  A    C  
ATOM    170  C   GLY A 117      91.062  93.858 -16.341  1.00 17.30      A    C  
ANISOU  170  C   GLY A 117     2837   1957   1781    110    541   -385  A    C  
ATOM    171  O   GLY A 117      91.400  92.829 -16.942  1.00 16.33      A    O  
ANISOU  171  O   GLY A 117     2670   1765   1771     21    740   -227  A    O  
ATOM    172  N   THR A 118      91.152  93.979 -15.013  1.00 19.18      A    N  
ANISOU  172  N   THR A 118     3003   2452   1831    205    566   -316  A    N  
ATOM    173  CA  THR A 118      91.769  92.936 -14.200  1.00 22.19      A    C  
ANISOU  173  CA  THR A 118     3540   2912   1979    176    684   -391  A    C  
ATOM    174  C   THR A 118      90.878  92.459 -13.056  1.00 23.41      A    C  
ANISOU  174  C   THR A 118     3881   3135   1877     46    772   -422  A    C  
ATOM    175  O   THR A 118      91.393  91.933 -12.064  1.00 23.93      A    O  
ANISOU  175  O   THR A 118     4037   3242   1814    -63    721   -250  A    O  
ATOM    176  CB  THR A 118      93.132  93.381 -13.658  1.00 24.32      A    C  
ANISOU  176  CB  THR A 118     3693   3324   2225    218    608   -482  A    C  
ATOM    177  CG2 THR A 118      94.085  93.726 -14.795  1.00 25.85      A    C  
ANISOU  177  CG2 THR A 118     3785   3640   2395    388    682   -378  A    C  
ATOM    178  OG1 THR A 118      92.964  94.529 -12.818  1.00 25.19      A    O  
ANISOU  178  OG1 THR A 118     3777   3503   2292    294    479   -567  A    O  
ATOM    179  N   ALA A 119      89.561  92.620 -13.170  1.00 23.12      A    N  
ANISOU  179  N   ALA A 119     3767   3162   1857     -7    953   -424  A    N  
ATOM    180  CA  ALA A 119      88.663  92.099 -12.146  1.00 24.47      A    C  
ANISOU  180  CA  ALA A 119     3900   3388   2010   -157   1029   -245  A    C  
ATOM    181  C   ALA A 119      88.807  90.586 -12.024  1.00 25.85      A    C  
ANISOU  181  C   ALA A 119     4248   3544   2030   -318   1135   -239  A    C  
ATOM    182  O   ALA A 119      89.206  89.897 -12.966  1.00 25.68      A    O  
ANISOU  182  O   ALA A 119     4360   3416   1981   -357    873   -281  A    O  
ATOM    183  CB  ALA A 119      87.214  92.455 -12.477  1.00 25.82      A    C  
ANISOU  183  CB  ALA A 119     4020   3583   2206   -106    947   -212  A    C  
ATOM    184  N   LYS A 120      88.473  90.068 -10.839  1.00 28.47      A    N  
ANISOU  184  N   LYS A 120     4783   3809   2225   -527   1145   -200  A    N  
ATOM    185  CA  LYS A 120      88.605  88.636 -10.587  1.00 30.34      A    C  
ANISOU  185  CA  LYS A 120     5095   4009   2423   -530   1259   -225  A    C  
ATOM    186  C   LYS A 120      87.793  87.807 -11.578  1.00 31.51      A    C  
ANISOU  186  C   LYS A 120     5217   4016   2741   -633   1205   -229  A    C  
ATOM    187  O   LYS A 120      88.159  86.664 -11.877  1.00 32.93      A    O  
ANISOU  187  O   LYS A 120     5608   4029   2875   -603   1173   -317  A    O  
ATOM    188  CB  LYS A 120      88.196  88.318  -9.145  1.00 31.10      A    C  
ANISOU  188  CB  LYS A 120     5168   4235   2412   -483   1342   -249  A    C  
ATOM    189  N   SER A 121      86.713  88.369 -12.117  1.00 30.76      A    N  
ANISOU  189  N   SER A 121     4749   4087   2851   -781   1254   -259  A    N  
ATOM    190  CA  SER A 121      85.820  87.655 -13.022  1.00 29.69      A    C  
ANISOU  190  CA  SER A 121     4405   3892   2985   -961   1235   -301  A    C  
ATOM    191  C   SER A 121      86.273  87.678 -14.480  1.00 27.59      A    C  
ANISOU  191  C   SER A 121     4021   3732   2730   -963   1183   -546  A    C  
ATOM    192  O   SER A 121      85.616  87.053 -15.322  1.00 29.17      A    O  
ANISOU  192  O   SER A 121     4090   4100   2893  -1225   1407   -505  A    O  
ATOM    193  CB  SER A 121      84.412  88.244 -12.923  1.00 31.80      A    C  
ANISOU  193  CB  SER A 121     4636   4078   3367   -766   1017   -197  A    C  
ATOM    194  OG  SER A 121      84.425  89.626 -13.248  1.00 32.82      A    O  
ANISOU  194  OG  SER A 121     4687   4180   3602   -598    929   -287  A    O  
ATOM    195  N   VAL A 122      87.359  88.374 -14.813  1.00 23.45      A    N  
ANISOU  195  N   VAL A 122     3458   3117   2337   -698    974   -520  A    N  
ATOM    196  CA  VAL A 122      87.747  88.496 -16.214  1.00 20.10      A    C  
ANISOU  196  CA  VAL A 122     2932   2709   1998   -658    687   -367  A    C  
ATOM    197  C   VAL A 122      88.283  87.161 -16.724  1.00 18.00      A    C  
ANISOU  197  C   VAL A 122     2434   2581   1826   -438    446   -217  A    C  
ATOM    198  O   VAL A 122      88.986  86.433 -16.012  1.00 19.15      A    O  
ANISOU  198  O   VAL A 122     2701   2750   1824   -334    316   -208  A    O  
ATOM    199  CB  VAL A 122      88.739  89.659 -16.408  1.00 20.67      A    C  
ANISOU  199  CB  VAL A 122     3088   2696   2068   -640    469   -325  A    C  
ATOM    200  CG1 VAL A 122      90.146  89.280 -15.971  1.00 21.59      A    C  
ANISOU  200  CG1 VAL A 122     3198   2713   2293   -847    280   -325  A    C  
ATOM    201  CG2 VAL A 122      88.732  90.144 -17.856  1.00 21.47      A    C  
ANISOU  201  CG2 VAL A 122     3373   2748   2035   -557    376   -286  A    C  
ATOM    202  N   THR A 123      87.928  86.815 -17.963  1.00 15.80      A    N  
ANISOU  202  N   THR A 123     1825   2368   1811   -176    187   -256  A    N  
ATOM    203  CA  THR A 123      88.346  85.540 -18.531  1.00 14.55      A    C  
ANISOU  203  CA  THR A 123     1595   2179   1756   -227    210   -223  A    C  
ATOM    204  C   THR A 123      89.490  85.668 -19.525  1.00 13.44      A    C  
ANISOU  204  C   THR A 123     1661   1787   1659     88    135    -93  A    C  
ATOM    205  O   THR A 123      90.124  84.658 -19.855  1.00 14.03      A    O  
ANISOU  205  O   THR A 123     1697   1800   1834      4    -72    -95  A    O  
ATOM    206  CB  THR A 123      87.159  84.851 -19.218  1.00 17.03      A    C  
ANISOU  206  CB  THR A 123     1759   2774   1938   -315    129   -192  A    C  
ATOM    207  CG2 THR A 123      86.004  84.685 -18.241  1.00 18.57      A    C  
ANISOU  207  CG2 THR A 123     1997   2984   2076   -380    162    -26  A    C  
ATOM    208  OG1 THR A 123      86.726  85.641 -20.333  1.00 17.77      A    O  
ANISOU  208  OG1 THR A 123     1664   3117   1972   -263     14   -166  A    O  
ATOM    209  N   CYS A 124      89.760  86.876 -20.005  1.00 12.35      A    N  
ANISOU  209  N   CYS A 124     1426   1688   1577     70    187   -135  A    N  
ATOM    210  CA  CYS A 124      90.825  87.118 -20.964  1.00 11.73      A    C  
ANISOU  210  CA  CYS A 124     1310   1489   1658    -16     39    -78  A    C  
ATOM    211  C   CYS A 124      91.195  88.581 -20.808  1.00 11.02      A    C  
ANISOU  211  C   CYS A 124     1095   1308   1786      8     29    -98  A    C  
ATOM    212  O   CYS A 124      90.313  89.445 -20.836  1.00 13.20      A    O  
ANISOU  212  O   CYS A 124     1401   1562   2051    219     38   -181  A    O  
ATOM    213  CB  CYS A 124      90.328  86.840 -22.388  1.00 13.86      A    C  
ANISOU  213  CB  CYS A 124     1726   1868   1673   -310    306   -111  A    C  
ATOM    214  SG  CYS A 124      91.558  87.144 -23.670  1.00 17.45      A    S  
ANISOU  214  SG  CYS A 124     2545   2304   1781   -463    128   -242  A    S  
ATOM    215  N   THR A 125      92.479  88.857 -20.612  1.00 10.40      A    N  
ANISOU  215  N   THR A 125     1000   1277   1676    -65    220   -131  A    N  
ATOM    216  CA  THR A 125      92.922  90.230 -20.437  1.00  9.97      A    C  
ANISOU  216  CA  THR A 125     1092   1241   1456   -138    203   -156  A    C  
ATOM    217  C   THR A 125      94.350  90.378 -20.947  1.00  9.03      A    C  
ANISOU  217  C   THR A 125     1073   1088   1272    -16    105      0  A    C  
ATOM    218  O   THR A 125      95.191  89.501 -20.745  1.00 10.49      A    O  
ANISOU  218  O   THR A 125     1211   1215   1558    129    200    197  A    O  
ATOM    219  CB  THR A 125      92.790  90.667 -18.970  1.00 12.09      A    C  
ANISOU  219  CB  THR A 125     1530   1531   1533    -25    154   -272  A    C  
ATOM    220  CG2 THR A 125      93.715  89.866 -18.050  1.00 12.55      A    C  
ANISOU  220  CG2 THR A 125     1723   1596   1450   -161     54    -86  A    C  
ATOM    221  OG1 THR A 125      93.112  92.055 -18.863  1.00 13.24      A    O  
ANISOU  221  OG1 THR A 125     1742   1547   1740   -108    398   -359  A    O  
ATOM    222  N   TYR A 126      94.613  91.484 -21.628  1.00  9.39      A    N  
ANISOU  222  N   TYR A 126     1175   1172   1222    -94     51     53  A    N  
ATOM    223  CA  TYR A 126      95.889  91.720 -22.285  1.00  9.23      A    C  
ANISOU  223  CA  TYR A 126     1286   1135   1084     -5     95   -135  A    C  
ATOM    224  C   TYR A 126      96.660  92.818 -21.557  1.00  9.53      A    C  
ANISOU  224  C   TYR A 126     1320   1044   1257     91     14   -157  A    C  
ATOM    225  O   TYR A 126      96.111  93.893 -21.272  1.00 11.13      A    O  
ANISOU  225  O   TYR A 126     1556   1146   1527    188    -31   -293  A    O  
ATOM    226  CB  TYR A 126      95.675  92.100 -23.752  1.00  9.73      A    C  
ANISOU  226  CB  TYR A 126     1308   1328   1060    127     22     22  A    C  
ATOM    227  CG  TYR A 126      96.963  92.485 -24.422  1.00  9.32      A    C  
ANISOU  227  CG  TYR A 126     1130   1398   1013    102    -69      2  A    C  
ATOM    228  CD1 TYR A 126      97.916  91.525 -24.752  1.00  9.71      A    C  
ANISOU  228  CD1 TYR A 126     1337   1370    982    189   -132    157  A    C  
ATOM    229  CD2 TYR A 126      97.257  93.815 -24.689  1.00  9.22      A    C  
ANISOU  229  CD2 TYR A 126     1240   1347    916     27   -116   -131  A    C  
ATOM    230  CE1 TYR A 126      99.109  91.879 -25.341  1.00  9.43      A    C  
ANISOU  230  CE1 TYR A 126     1439   1275    868    124    -45    307  A    C  
ATOM    231  CE2 TYR A 126      98.445  94.180 -25.279  1.00  9.92      A    C  
ANISOU  231  CE2 TYR A 126     1412   1568    788    101      5   -111  A    C  
ATOM    232  CZ  TYR A 126      99.373  93.209 -25.598  1.00  9.68      A    C  
ANISOU  232  CZ  TYR A 126     1434   1424    818     74     27     65  A    C  
ATOM    233  OH  TYR A 126     100.565  93.564 -26.180  1.00 11.53      A    O  
ANISOU  233  OH  TYR A 126     1661   1733    986     84      8    120  A    O  
ATOM    234  N   SER A 127      97.936  92.555 -21.285  1.00  9.10      A    N  
ANISOU  234  N   SER A 127     1017   1288   1150    -90   -222   -147  A    N  
ATOM    235  CA  SER A 127      98.819  93.536 -20.672  1.00  9.80      A    C  
ANISOU  235  CA  SER A 127     1144   1380   1199   -136   -170   -139  A    C  
ATOM    236  C   SER A 127      99.728  94.152 -21.719  1.00 10.02      A    C  
ANISOU  236  C   SER A 127     1485   1024   1296    165   -148   -107  A    C  
ATOM    237  O   SER A 127     100.665  93.484 -22.178  1.00 10.60      A    O  
ANISOU  237  O   SER A 127     1581   1007   1442     -8      7   -166  A    O  
ATOM    238  CB  SER A 127      99.667  92.870 -19.594  1.00 10.36      A    C  
ANISOU  238  CB  SER A 127     1205   1522   1210   -249   -414     66  A    C  
ATOM    239  OG  SER A 127     100.686  93.756 -19.147  1.00 12.18      A    O  
ANISOU  239  OG  SER A 127     1505   1720   1403   -252   -186    -78  A    O  
ATOM    240  N   PRO A 128      99.531  95.413 -22.099  1.00 10.80      A    N  
ANISOU  240  N   PRO A 128     1622   1027   1454    -83   -185    -23  A    N  
ATOM    241  CA  PRO A 128     100.500  96.048 -23.005  1.00 12.36      A    C  
ANISOU  241  CA  PRO A 128     1789   1259   1648   -166   -265    194  A    C  
ATOM    242  C   PRO A 128     101.891  96.169 -22.413  1.00 12.45      A    C  
ANISOU  242  C   PRO A 128     1811   1325   1595   -273   -250    101  A    C  
ATOM    243  O   PRO A 128     102.877  96.048 -23.147  1.00 14.24      A    O  
ANISOU  243  O   PRO A 128     2008   1561   1839   -299   -111     28  A    O  
ATOM    244  CB  PRO A 128      99.881  97.425 -23.283  1.00 14.09      A    C  
ANISOU  244  CB  PRO A 128     2057   1346   1953    -41   -288    368  A    C  
ATOM    245  CG  PRO A 128      98.438  97.285 -22.944  1.00 15.17      A    C  
ANISOU  245  CG  PRO A 128     2264   1544   1955    217     48    194  A    C  
ATOM    246  CD  PRO A 128      98.333  96.243 -21.877  1.00 12.32      A    C  
ANISOU  246  CD  PRO A 128     1912   1109   1659     88   -199     90  A    C  
ATOM    247  N   ALA A 129     102.006  96.421 -21.103  1.00 13.19      A    N  
ANISOU  247  N   ALA A 129     1984   1411   1618   -251   -508    -40  A    N  
ATOM    248  CA  ALA A 129     103.331  96.606 -20.520  1.00 13.34      A    C  
ANISOU  248  CA  ALA A 129     1919   1404   1746   -271   -403   -347  A    C  
ATOM    249  C   ALA A 129     104.160  95.332 -20.600  1.00 14.45      A    C  
ANISOU  249  C   ALA A 129     1958   1575   1958    -69   -365    -65  A    C  
ATOM    250  O   ALA A 129     105.384  95.398 -20.751  1.00 17.36      A    O  
ANISOU  250  O   ALA A 129     2149   1951   2497   -234   -180    216  A    O  
ATOM    251  CB  ALA A 129     103.215  97.079 -19.070  1.00 14.93      A    C  
ANISOU  251  CB  ALA A 129     2221   1807   1644   -275   -560   -528  A    C  
ATOM    252  N   LEU A 130     103.511  94.172 -20.520  1.00 12.91      A    N  
ANISOU  252  N   LEU A 130     1960   1350   1595   -201   -397    -61  A    N  
ATOM    253  CA  LEU A 130     104.172  92.881 -20.619  1.00 13.26      A    C  
ANISOU  253  CA  LEU A 130     2072   1497   1469    -20   -114     67  A    C  
ATOM    254  C   LEU A 130     104.082  92.261 -22.012  1.00 13.72      A    C  
ANISOU  254  C   LEU A 130     2148   1561   1502   -164   -221    -12  A    C  
ATOM    255  O   LEU A 130     104.724  91.229 -22.249  1.00 15.48      A    O  
ANISOU  255  O   LEU A 130     2453   1783   1648    -44   -100    -53  A    O  
ATOM    256  CB  LEU A 130     103.553  91.909 -19.609  1.00 13.15      A    C  
ANISOU  256  CB  LEU A 130     2073   1565   1358   -159   -161     21  A    C  
ATOM    257  CG  LEU A 130     103.640  92.293 -18.132  1.00 15.22      A    C  
ANISOU  257  CG  LEU A 130     2317   1891   1575   -222   -436    136  A    C  
ATOM    258  CD1 LEU A 130     102.649  91.476 -17.321  1.00 16.96      A    C  
ANISOU  258  CD1 LEU A 130     2757   1939   1748   -268   -354    249  A    C  
ATOM    259  CD2 LEU A 130     105.068  92.106 -17.603  1.00 17.66      A    C  
ANISOU  259  CD2 LEU A 130     2420   2506   1783     22   -605    106  A    C  
ATOM    260  N   ASN A 131     103.322  92.862 -22.934  1.00 12.49      A    N  
ANISOU  260  N   ASN A 131     1923   1441   1380   -417   -322     -5  A    N  
ATOM    261  CA  ASN A 131     102.925  92.232 -24.204  1.00 10.31      A    C  
ANISOU  261  CA  ASN A 131     1538   1197   1181   -522    -19    -37  A    C  
ATOM    262  C   ASN A 131     102.505  90.784 -23.978  1.00  9.36      A    C  
ANISOU  262  C   ASN A 131     1360   1052   1145   -329     -8    126  A    C  
ATOM    263  O   ASN A 131     103.048  89.852 -24.567  1.00 10.10      A    O  
ANISOU  263  O   ASN A 131     1474   1050   1313      9     49    -86  A    O  
ATOM    264  CB  ASN A 131     104.006  92.325 -25.283  1.00 10.10      A    C  
ANISOU  264  CB  ASN A 131     1331   1301   1206   -292     80    -17  A    C  
ATOM    265  CG  ASN A 131     103.525  91.805 -26.643  1.00 11.21      A    C  
ANISOU  265  CG  ASN A 131     1555   1313   1390   -459    208    -10  A    C  
ATOM    266  ND2 ASN A 131     104.438  91.240 -27.411  1.00 11.94      A    N  
ANISOU  266  ND2 ASN A 131     1667   1403   1468   -439    428   -123  A    N  
ATOM    267  OD1 ASN A 131     102.339  91.895 -26.981  1.00 12.18      A    O  
ANISOU  267  OD1 ASN A 131     1889   1347   1392   -395     35     -8  A    O  
ATOM    268  N   LYS A 132     101.527  90.609 -23.093  1.00  9.24      A    N  
ANISOU  268  N   LYS A 132     1292   1037   1181    -69    -87    207  A    N  
ATOM    269  CA  LYS A 132     101.190  89.284 -22.597  1.00  8.65      A    C  
ANISOU  269  CA  LYS A 132     1145    999   1144     12     -8    319  A    C  
ATOM    270  C   LYS A 132      99.687  89.178 -22.415  1.00  8.82      A    C  
ANISOU  270  C   LYS A 132     1149   1081   1120    -37     67     -4  A    C  
ATOM    271  O   LYS A 132      99.075  90.026 -21.760  1.00  9.19      A    O  
ANISOU  271  O   LYS A 132     1276   1043   1171    -78    -95     15  A    O  
ATOM    272  CB  LYS A 132     101.899  89.027 -21.264  1.00 10.04      A    C  
ANISOU  272  CB  LYS A 132     1693   1032   1089     59   -197    386  A    C  
ATOM    273  CG  LYS A 132     101.669  87.642 -20.693  1.00 10.49      A    C  
ANISOU  273  CG  LYS A 132     1584   1140   1263    106   -338    504  A    C  
ATOM    274  CD  LYS A 132     102.701  87.332 -19.608  1.00 11.92      A    C  
ANISOU  274  CD  LYS A 132     1532   1389   1606     95   -340    663  A    C  
ATOM    275  CE  LYS A 132     102.502  85.955 -19.023  1.00 14.36      A    C  
ANISOU  275  CE  LYS A 132     1792   1774   1892    209   -394    759  A    C  
ATOM    276  NZ  LYS A 132     103.616  85.610 -18.094  1.00 16.54      A    N1+
ANISOU  276  NZ  LYS A 132     1819   2334   2130    199   -481    669  A    N1+
ATOM    277  N   LEU A 133      99.108  88.136 -23.001  1.00  8.27      A    N  
ANISOU  277  N   LEU A 133     1028   1104   1009   -234    -52    -28  A    N  
ATOM    278  CA  LEU A 133      97.699  87.827 -22.847  1.00  8.88      A    C  
ANISOU  278  CA  LEU A 133     1090   1185   1098    -97    -69     -6  A    C  
ATOM    279  C   LEU A 133      97.549  86.813 -21.718  1.00  9.13      A    C  
ANISOU  279  C   LEU A 133     1101   1155   1215    -69     28    155  A    C  
ATOM    280  O   LEU A 133      98.278  85.821 -21.672  1.00 10.66      A    O  
ANISOU  280  O   LEU A 133     1401   1193   1455    185    202     86  A    O  
ATOM    281  CB  LEU A 133      97.165  87.222 -24.144  1.00 10.04      A    C  
ANISOU  281  CB  LEU A 133     1078   1462   1276   -260     16   -194  A    C  
ATOM    282  CG  LEU A 133      95.663  86.985 -24.210  1.00 11.52      A    C  
ANISOU  282  CG  LEU A 133     1144   1826   1407   -247   -167   -285  A    C  
ATOM    283  CD1 LEU A 133      94.939  88.334 -24.288  1.00 14.26      A    C  
ANISOU  283  CD1 LEU A 133     1388   2283   1749    242   -196   -319  A    C  
ATOM    284  CD2 LEU A 133      95.337  86.099 -25.401  1.00 14.43      A    C  
ANISOU  284  CD2 LEU A 133     1702   2198   1581   -288   -103   -458  A    C  
ATOM    285  N   PHE A 134      96.605  87.061 -20.818  1.00  8.64      A    N  
ANISOU  285  N   PHE A 134      921   1268   1092   -168    187    138  A    N  
ATOM    286  CA  PHE A 134      96.265  86.145 -19.736  1.00  9.43      A    C  
ANISOU  286  CA  PHE A 134      939   1455   1189    -55    179     83  A    C  
ATOM    287  C   PHE A 134      94.842  85.653 -19.974  1.00 10.18      A    C  
ANISOU  287  C   PHE A 134     1181   1369   1317   -220     48    173  A    C  
ATOM    288  O   PHE A 134      93.923  86.463 -20.141  1.00 11.33      A    O  
ANISOU  288  O   PHE A 134     1369   1487   1449     39    127     58  A    O  
ATOM    289  CB  PHE A 134      96.311  86.867 -18.386  1.00 10.67      A    C  
ANISOU  289  CB  PHE A 134     1041   1726   1287    -12     -4    -16  A    C  
ATOM    290  CG  PHE A 134      97.659  87.401 -18.014  1.00 10.57      A    C  
ANISOU  290  CG  PHE A 134     1225   1497   1292   -135     22     12  A    C  
ATOM    291  CD1 PHE A 134      98.130  88.584 -18.566  1.00 11.10      A    C  
ANISOU  291  CD1 PHE A 134     1487   1419   1313   -177     77   -113  A    C  
ATOM    292  CD2 PHE A 134      98.437  86.748 -17.068  1.00 12.15      A    C  
ANISOU  292  CD2 PHE A 134     1650   1655   1314   -126    120    -65  A    C  
ATOM    293  CE1 PHE A 134      99.365  89.088 -18.217  1.00 11.94      A    C  
ANISOU  293  CE1 PHE A 134     1674   1464   1399    -42     11    -34  A    C  
ATOM    294  CE2 PHE A 134      99.672  87.250 -16.706  1.00 12.86      A    C  
ANISOU  294  CE2 PHE A 134     1815   1632   1439    -99    111     47  A    C  
ATOM    295  CZ  PHE A 134     100.142  88.424 -17.282  1.00 12.46      A    C  
ANISOU  295  CZ  PHE A 134     1796   1534   1406   -120    -61     61  A    C  
ATOM    296  N   CYS A 135      94.647  84.337 -20.001  1.00 10.46      A    N  
ANISOU  296  N   CYS A 135     1425   1281   1270   -334     75    241  A    N  
ATOM    297  CA  CYS A 135      93.310  83.845 -20.307  1.00 11.58      A    C  
ANISOU  297  CA  CYS A 135     1554   1421   1426   -187     -9    105  A    C  
ATOM    298  C   CYS A 135      93.029  82.550 -19.562  1.00 11.91      A    C  
ANISOU  298  C   CYS A 135     1533   1357   1634   -129    -28    175  A    C  
ATOM    299  O   CYS A 135      93.942  81.816 -19.180  1.00 13.02      A    O  
ANISOU  299  O   CYS A 135     1653   1490   1806   -257    -11    434  A    O  
ATOM    300  CB  CYS A 135      93.115  83.619 -21.808  1.00 12.67      A    C  
ANISOU  300  CB  CYS A 135     1848   1556   1411    120    -60   -188  A    C  
ATOM    301  SG  CYS A 135      94.249  82.400 -22.503  1.00 15.94      A    S  
ANISOU  301  SG  CYS A 135     2531   2060   1468    388   -322    -80  A    S  
ATOM    302  N   GLN A 136      91.743  82.285 -19.365  1.00 12.35      A    N  
ANISOU  302  N   GLN A 136     1437   1415   1839   -223    -19    173  A    N  
ATOM    303  CA  GLN A 136      91.296  81.017 -18.817  1.00 13.54      A    C  
ANISOU  303  CA  GLN A 136     1445   1594   2104   -369    280     54  A    C  
ATOM    304  C   GLN A 136      91.282  79.935 -19.892  1.00 13.05      A    C  
ANISOU  304  C   GLN A 136     1448   1359   2151   -361    138    278  A    C  
ATOM    305  O   GLN A 136      91.277  80.204 -21.095  1.00 13.88      A    O  
ANISOU  305  O   GLN A 136     1701   1469   2104    -56    149    343  A    O  
ATOM    306  CB  GLN A 136      89.908  81.167 -18.189  1.00 15.60      A    C  
ANISOU  306  CB  GLN A 136     1659   1930   2340   -429    380   -155  A    C  
ATOM    307  CG  GLN A 136      89.937  81.961 -16.888  1.00 18.66      A    C  
ANISOU  307  CG  GLN A 136     2065   2455   2571   -390    491   -271  A    C  
ATOM    308  CD  GLN A 136      88.560  82.221 -16.313  1.00 21.93      A    C  
ANISOU  308  CD  GLN A 136     2403   3169   2759   -537    542   -355  A    C  
ATOM    309  NE2 GLN A 136      88.520  82.801 -15.122  1.00 24.07      A    N  
ANISOU  309  NE2 GLN A 136     2774   3527   2846   -497    647   -212  A    N  
ATOM    310  OE1 GLN A 136      87.547  81.912 -16.929  1.00 24.48      A    O  
ANISOU  310  OE1 GLN A 136     2671   3719   2910   -380    566   -460  A    O  
ATOM    311  N   LEU A 137      91.262  78.690 -19.429  1.00 12.61      A    N  
ANISOU  311  N   LEU A 137     1370   1206   2216   -341     -3    255  A    N  
ATOM    312  CA  LEU A 137      91.266  77.533 -20.310  1.00 12.53      A    C  
ANISOU  312  CA  LEU A 137     1332   1304   2124   -116   -107    365  A    C  
ATOM    313  C   LEU A 137      90.028  77.511 -21.200  1.00 12.03      A    C  
ANISOU  313  C   LEU A 137     1141   1479   1950   -103    -24    324  A    C  
ATOM    314  O   LEU A 137      88.894  77.569 -20.712  1.00 12.15      A    O  
ANISOU  314  O   LEU A 137     1188   1458   1969   -160    -55    262  A    O  
ATOM    315  CB  LEU A 137      91.272  76.286 -19.434  1.00 13.74      A    C  
ANISOU  315  CB  LEU A 137     1792   1236   2191    -97    182    459  A    C  
ATOM    316  CG  LEU A 137      91.195  74.960 -20.170  1.00 14.99      A    C  
ANISOU  316  CG  LEU A 137     2154   1326   2215    -28    327    368  A    C  
ATOM    317  CD1 LEU A 137      92.475  74.765 -20.917  1.00 16.21      A    C  
ANISOU  317  CD1 LEU A 137     2326   1737   2097      3    613    172  A    C  
ATOM    318  CD2 LEU A 137      90.949  73.821 -19.181  1.00 16.32      A    C  
ANISOU  318  CD2 LEU A 137     2592   1368   2240   -183    336    450  A    C  
ATOM    319  N   ALA A 138      90.253  77.410 -22.514  1.00 12.70      A    N  
ANISOU  319  N   ALA A 138     1323   1507   1995     89     13    296  A    N  
ATOM    320  CA  ALA A 138      89.197  77.204 -23.503  1.00 14.04      A    C  
ANISOU  320  CA  ALA A 138     1610   1534   2190    172   -137    233  A    C  
ATOM    321  C   ALA A 138      88.198  78.355 -23.565  1.00 16.14      A    C  
ANISOU  321  C   ALA A 138     1703   1955   2474    307   -314    181  A    C  
ATOM    322  O   ALA A 138      87.064  78.169 -24.006  1.00 20.97      A    O  
ANISOU  322  O   ALA A 138     2299   2411   3259    517   -657   -214  A    O  
ATOM    323  CB  ALA A 138      88.478  75.857 -23.319  1.00 14.60      A    C  
ANISOU  323  CB  ALA A 138     1776   1575   2197    -58   -263     74  A    C  
ATOM    324  N   LYS A 139      88.588  79.543 -23.135  1.00 14.01      A    N  
ANISOU  324  N   LYS A 139     1616   1749   1958    328      6    376  A    N  
ATOM    325  CA  LYS A 139      87.721  80.706 -23.219  1.00 13.74      A    C  
ANISOU  325  CA  LYS A 139     1709   1757   1755    374    120    452  A    C  
ATOM    326  C   LYS A 139      88.100  81.573 -24.417  1.00 12.18      A    C  
ANISOU  326  C   LYS A 139     1188   1687   1754    125    274    501  A    C  
ATOM    327  O   LYS A 139      89.230  81.553 -24.908  1.00 13.85      A    O  
ANISOU  327  O   LYS A 139     1249   2094   1918    217    211    474  A    O  
ATOM    328  CB  LYS A 139      87.777  81.528 -21.922  1.00 17.62      A    C  
ANISOU  328  CB  LYS A 139     2503   2181   2010    292      0    497  A    C  
ATOM    329  CG  LYS A 139      87.332  80.770 -20.673  1.00 22.23      A    C  
ANISOU  329  CG  LYS A 139     3026   3011   2411    219   -104    658  A    C  
ATOM    330  CD  LYS A 139      85.869  80.381 -20.716  1.00 25.57      A    C  
ANISOU  330  CD  LYS A 139     3517   3608   2589   -129   -132    856  A    C  
ATOM    331  CE  LYS A 139      85.480  79.536 -19.503  1.00 28.40      A    C  
ANISOU  331  CE  LYS A 139     3832   4098   2861   -223   -165    786  A    C  
ATOM    332  NZ  LYS A 139      85.576  80.298 -18.230  1.00 30.27      A    N1+
ANISOU  332  NZ  LYS A 139     4032   4370   3100   -285   -214    743  A    N1+
ATOM    333  N   THR A 140      87.124  82.345 -24.877  1.00 11.42      A    N  
ANISOU  333  N   THR A 140     1142   1489   1708    269     12    535  A    N  
ATOM    334  CA  THR A 140      87.298  83.172 -26.064  1.00 10.77      A    C  
ANISOU  334  CA  THR A 140     1030   1270   1790    -22   -122    441  A    C  
ATOM    335  C   THR A 140      88.371  84.226 -25.839  1.00 11.18      A    C  
ANISOU  335  C   THR A 140     1327   1267   1655    -49     20     86  A    C  
ATOM    336  O   THR A 140      88.326  84.981 -24.862  1.00 12.87      A    O  
ANISOU  336  O   THR A 140     1777   1378   1733     20    168    -81  A    O  
ATOM    337  CB  THR A 140      85.974  83.854 -26.389  1.00 12.53      A    C  
ANISOU  337  CB  THR A 140     1209   1640   1912     25   -146    523  A    C  
ATOM    338  CG2 THR A 140      86.114  84.731 -27.627  1.00 14.90      A    C  
ANISOU  338  CG2 THR A 140     1545   2110   2005    119    -46    704  A    C  
ATOM    339  OG1 THR A 140      84.979  82.857 -26.623  1.00 13.53      A    O  
ANISOU  339  OG1 THR A 140     1303   1927   1910   -159    -93    357  A    O  
ATOM    340  N   CYS A 141      89.333  84.290 -26.758  1.00  9.67      A    N  
ANISOU  340  N   CYS A 141     1011   1240   1425     -6     96    118  A    N  
ATOM    341  CA  CYS A 141      90.370  85.322 -26.737  1.00 10.10      A    C  
ANISOU  341  CA  CYS A 141     1143   1347   1347    -99    -26    -25  A    C  
ATOM    342  C   CYS A 141      90.254  86.132 -28.013  1.00  9.42      A    C  
ANISOU  342  C   CYS A 141     1182   1195   1201   -200    165    -93  A    C  
ATOM    343  O   CYS A 141      90.721  85.686 -29.079  1.00 10.07      A    O  
ANISOU  343  O   CYS A 141     1386   1374   1066   -107    166    -57  A    O  
ATOM    344  CB  CYS A 141      91.760  84.704 -26.655  1.00 11.48      A    C  
ANISOU  344  CB  CYS A 141     1512   1460   1391    136    -50    138  A    C  
ATOM    345  SG  CYS A 141      92.054  83.748 -25.190  1.00 14.14      A    S  
ANISOU  345  SG  CYS A 141     1827   2026   1521    146   -121    111  A    S  
ATOM    346  N   PRO A 142      89.636  87.313 -27.970  1.00 10.89      A    N  
ANISOU  346  N   PRO A 142     1538   1354   1246     59    181   -144  A    N  
ATOM    347  CA  PRO A 142      89.489  88.126 -29.186  1.00 11.72      A    C  
ANISOU  347  CA  PRO A 142     1649   1429   1373    152    235    -28  A    C  
ATOM    348  C   PRO A 142      90.805  88.816 -29.507  1.00 11.01      A    C  
ANISOU  348  C   PRO A 142     1632   1292   1258   -273     -2   -145  A    C  
ATOM    349  O   PRO A 142      91.379  89.514 -28.670  1.00 14.20      A    O  
ANISOU  349  O   PRO A 142     2130   1849   1416   -664     50   -306  A    O  
ATOM    350  CB  PRO A 142      88.405  89.144 -28.808  1.00 14.02      A    C  
ANISOU  350  CB  PRO A 142     1879   1761   1686    468    433    -38  A    C  
ATOM    351  CG  PRO A 142      87.894  88.738 -27.454  1.00 15.23      A    C  
ANISOU  351  CG  PRO A 142     2107   2022   1659    625    506     20  A    C  
ATOM    352  CD  PRO A 142      88.953  87.902 -26.812  1.00 12.89      A    C  
ANISOU  352  CD  PRO A 142     1795   1627   1477    412    446    -49  A    C  
ATOM    353  N   VAL A 143      91.289  88.609 -30.725  1.00 10.05      A    N  
ANISOU  353  N   VAL A 143     1405   1241   1174   -172    -11    -63  A    N  
ATOM    354  CA  VAL A 143      92.503  89.254 -31.206  1.00  9.97      A    C  
ANISOU  354  CA  VAL A 143     1321   1244   1222   -126    -50     65  A    C  
ATOM    355  C   VAL A 143      92.138  90.059 -32.444  1.00 10.43      A    C  
ANISOU  355  C   VAL A 143     1543   1183   1238   -125   -168    -55  A    C  
ATOM    356  O   VAL A 143      91.593  89.509 -33.411  1.00 10.98      A    O  
ANISOU  356  O   VAL A 143     1564   1308   1299   -300   -212   -161  A    O  
ATOM    357  CB  VAL A 143      93.615  88.231 -31.487  1.00 11.29      A    C  
ANISOU  357  CB  VAL A 143     1234   1638   1417     63    -13    175  A    C  
ATOM    358  CG1 VAL A 143      94.865  88.937 -32.000  1.00 12.93      A    C  
ANISOU  358  CG1 VAL A 143     1237   1899   1775     24    286    270  A    C  
ATOM    359  CG2 VAL A 143      93.930  87.418 -30.207  1.00 12.07      A    C  
ANISOU  359  CG2 VAL A 143     1629   1491   1466     46   -252    135  A    C  
ATOM    360  N   GLN A 144      92.400  91.362 -32.405  1.00  9.82      A    N  
ANISOU  360  N   GLN A 144     1463   1124   1145   -100    -95    148  A    N  
ATOM    361  CA  GLN A 144      92.124  92.204 -33.556  1.00 10.28      A    C  
ANISOU  361  CA  GLN A 144     1570   1038   1298     46      1     87  A    C  
ATOM    362  C   GLN A 144      93.281  92.178 -34.540  1.00  9.87      A    C  
ANISOU  362  C   GLN A 144     1417   1163   1169     46   -221    -59  A    C  
ATOM    363  O   GLN A 144      94.451  92.128 -34.150  1.00  9.83      A    O  
ANISOU  363  O   GLN A 144     1304   1351   1081     99   -218    -48  A    O  
ATOM    364  CB  GLN A 144      91.904  93.649 -33.127  1.00 11.89      A    C  
ANISOU  364  CB  GLN A 144     1742   1280   1496    347     70   -120  A    C  
ATOM    365  CG  GLN A 144      90.784  93.835 -32.154  1.00 14.63      A    C  
ANISOU  365  CG  GLN A 144     2066   1900   1592    399    394   -195  A    C  
ATOM    366  CD  GLN A 144      90.686  95.265 -31.696  1.00 17.02      A    C  
ANISOU  366  CD  GLN A 144     2426   2319   1722    531    479   -394  A    C  
ATOM    367  NE2 GLN A 144      89.488  95.675 -31.300  1.00 20.52      A    N  
ANISOU  367  NE2 GLN A 144     2743   2951   2104    698    285   -609  A    N  
ATOM    368  OE1 GLN A 144      91.678  96.001 -31.701  1.00 16.21      A    O  
ANISOU  368  OE1 GLN A 144     2646   1968   1545    541    568    -59  A    O  
ATOM    369  N  ALEU A 145      92.945  92.234 -35.822  0.56 10.41      A    N  
ANISOU  369  N  ALEU A 145     1588   1208   1159     65   -116   -168  A    N  
ATOM    370  N  BLEU A 145      92.937  92.210 -35.826  0.44 10.43      A    N  
ANISOU  370  N  BLEU A 145     1562   1209   1191    129   -137    -73  A    N  
ATOM    371  CA ALEU A 145      93.923  92.381 -36.890  0.56 10.27      A    C  
ANISOU  371  CA ALEU A 145     1572   1160   1170     62    -85   -177  A    C  
ATOM    372  CA BLEU A 145      93.892  92.391 -36.910  0.44 10.50      A    C  
ANISOU  372  CA BLEU A 145     1572   1196   1221    181   -111     14  A    C  
ATOM    373  C  ALEU A 145      93.695  93.739 -37.529  0.56 10.18      A    C  
ANISOU  373  C  ALEU A 145     1513   1134   1219    264      4    -58  A    C  
ATOM    374  C  BLEU A 145      93.680  93.780 -37.484  0.44 10.79      A    C  
ANISOU  374  C  BLEU A 145     1559   1279   1263    294    -22    178  A    C  
ATOM    375  O  ALEU A 145      92.554  94.086 -37.841  0.56 10.03      A    O  
ANISOU  375  O  ALEU A 145     1455   1055   1300    174     -4   -109  A    O  
ATOM    376  O  BLEU A 145      92.538  94.178 -37.728  0.44 11.70      A    O  
ANISOU  376  O  BLEU A 145     1598   1472   1377    239     -1    359  A    O  
ATOM    377  CB ALEU A 145      93.720  91.280 -37.932  0.56 12.23      A    C  
ANISOU  377  CB ALEU A 145     1884   1311   1450     -8   -165   -289  A    C  
ATOM    378  CB BLEU A 145      93.661  91.366 -38.025  0.44 11.77      A    C  
ANISOU  378  CB BLEU A 145     1820   1218   1435    212   -206    -27  A    C  
ATOM    379  CG ALEU A 145      93.606  89.874 -37.340  0.56 14.13      A    C  
ANISOU  379  CG ALEU A 145     2075   1672   1624     24   -282   -108  A    C  
ATOM    380  CG BLEU A 145      93.846  89.881 -37.713  0.44 12.78      A    C  
ANISOU  380  CG BLEU A 145     1977   1319   1560    305   -363    242  A    C  
ATOM    381  CD1ALEU A 145      93.243  88.869 -38.414  0.56 15.18      A    C  
ANISOU  381  CD1ALEU A 145     2278   1791   1697     24   -415   -145  A    C  
ATOM    382  CD1BLEU A 145      95.048  89.670 -36.814  0.44 12.88      A    C  
ANISOU  382  CD1BLEU A 145     1993   1336   1564    483   -508    289  A    C  
ATOM    383  CD2ALEU A 145      94.900  89.483 -36.658  0.56 13.61      A    C  
ANISOU  383  CD2ALEU A 145     1882   1681   1609      8   -264     48  A    C  
ATOM    384  CD2BLEU A 145      92.596  89.302 -37.088  0.44 12.12      A    C  
ANISOU  384  CD2BLEU A 145     1841   1200   1564    224   -306    618  A    C  
ATOM    385  N   TRP A 146      94.772  94.513 -37.688  1.00  9.74      A    N  
ANISOU  385  N   TRP A 146     1527   1014   1160    211    -50    109  A    N  
ATOM    386  CA  TRP A 146      94.729  95.863 -38.233  1.00 10.82      A    C  
ANISOU  386  CA  TRP A 146     1811   1144   1157     75     41    -18  A    C  
ATOM    387  C   TRP A 146      95.686  95.933 -39.407  1.00 11.22      A    C  
ANISOU  387  C   TRP A 146     1948   1209   1106    204     -4    197  A    C  
ATOM    388  O   TRP A 146      96.766  95.336 -39.369  1.00 11.41      A    O  
ANISOU  388  O   TRP A 146     1781   1429   1125    308    -37    154  A    O  
ATOM    389  CB  TRP A 146      95.193  96.886 -37.192  1.00 11.21      A    C  
ANISOU  389  CB  TRP A 146     1826   1249   1186    -75    115   -100  A    C  
ATOM    390  CG  TRP A 146      94.231  97.077 -36.070  1.00 10.38      A    C  
ANISOU  390  CG  TRP A 146     1736   1056   1151    189   -127   -157  A    C  
ATOM    391  CD1 TRP A 146      94.189  96.382 -34.895  1.00 11.48      A    C  
ANISOU  391  CD1 TRP A 146     1939   1265   1157     -7    -22   -215  A    C  
ATOM    392  CD2 TRP A 146      93.150  98.013 -36.024  1.00 10.57      A    C  
ANISOU  392  CD2 TRP A 146     1671    996   1349    229   -201   -382  A    C  
ATOM    393  CE2 TRP A 146      92.502  97.844 -34.783  1.00 11.81      A    C  
ANISOU  393  CE2 TRP A 146     1853   1153   1481    210   -190   -405  A    C  
ATOM    394  CE3 TRP A 146      92.676  98.986 -36.907  1.00 11.57      A    C  
ANISOU  394  CE3 TRP A 146     1799   1024   1574    199   -231   -296  A    C  
ATOM    395  NE1 TRP A 146      93.154  96.846 -34.110  1.00 11.99      A    N  
ANISOU  395  NE1 TRP A 146     1965   1272   1317     61    -24   -285  A    N  
ATOM    396  CZ2 TRP A 146      91.396  98.605 -34.409  1.00 13.08      A    C  
ANISOU  396  CZ2 TRP A 146     2052   1273   1646    325   -142   -381  A    C  
ATOM    397  CZ3 TRP A 146      91.579  99.742 -36.531  1.00 13.81      A    C  
ANISOU  397  CZ3 TRP A 146     2112   1363   1771    307   -174   -339  A    C  
ATOM    398  CH2 TRP A 146      90.954  99.545 -35.298  1.00 13.76      A    C  
ANISOU  398  CH2 TRP A 146     2115   1335   1778    405   -123   -365  A    C  
ATOM    399  N   VAL A 147      95.286  96.653 -40.457  1.00 11.24      A    N  
ANISOU  399  N   VAL A 147     1924   1265   1079     82   -140     75  A    N  
ATOM    400  CA  VAL A 147      96.147  96.903 -41.605  1.00 11.43      A    C  
ANISOU  400  CA  VAL A 147     2064   1155   1125    133    -21    -45  A    C  
ATOM    401  C   VAL A 147      95.972  98.354 -42.028  1.00 11.96      A    C  
ANISOU  401  C   VAL A 147     2158   1184   1201    373    -93    -28  A    C  
ATOM    402  O   VAL A 147      94.950  98.988 -41.755  1.00 14.37      A    O  
ANISOU  402  O   VAL A 147     2489   1486   1485    412     93    170  A    O  
ATOM    403  CB  VAL A 147      95.871  95.976 -42.816  1.00 11.08      A    C  
ANISOU  403  CB  VAL A 147     1822   1189   1198    232   -313   -112  A    C  
ATOM    404  CG1 VAL A 147      96.222  94.516 -42.505  1.00 11.94      A    C  
ANISOU  404  CG1 VAL A 147     2164   1112   1259    281   -366     85  A    C  
ATOM    405  CG2 VAL A 147      94.414  96.097 -43.292  1.00 11.83      A    C  
ANISOU  405  CG2 VAL A 147     1676   1561   1259    521   -387    -82  A    C  
ATOM    406  N   ASP A 148      96.987  98.877 -42.712  1.00 13.31      A    N  
ANISOU  406  N   ASP A 148     2433   1331   1294    137     80     68  A    N  
ATOM    407  CA  ASP A 148      96.883 100.196 -43.327  1.00 14.06      A    C  
ANISOU  407  CA  ASP A 148     2645   1335   1364    170    116    328  A    C  
ATOM    408  C   ASP A 148      96.314 100.148 -44.737  1.00 15.14      A    C  
ANISOU  408  C   ASP A 148     2994   1418   1340    346    -56    185  A    C  
ATOM    409  O   ASP A 148      95.795 101.161 -45.213  1.00 16.68      A    O  
ANISOU  409  O   ASP A 148     3254   1585   1501    539   -292    164  A    O  
ATOM    410  CB  ASP A 148      98.258 100.864 -43.399  1.00 16.20      A    C  
ANISOU  410  CB  ASP A 148     2912   1623   1622   -126    165    394  A    C  
ATOM    411  CG  ASP A 148      98.805 101.219 -42.036  1.00 19.28      A    C  
ANISOU  411  CG  ASP A 148     3359   2022   1946     94    127    488  A    C  
ATOM    412  OD1 ASP A 148      98.003 101.521 -41.122  1.00 19.38      A    O  
ANISOU  412  OD1 ASP A 148     3572   1799   1991    209    232    389  A    O  
ATOM    413  OD2 ASP A 148     100.043 101.200 -41.883  1.00 22.27      A    O1-
ANISOU  413  OD2 ASP A 148     3714   2545   2204     85      4    401  A    O1-
ATOM    414  N   SER A 149      96.426  99.012 -45.421  1.00 16.02      A    N  
ANISOU  414  N   SER A 149     3282   1515   1289    185    -92    -52  A    N  
ATOM    415  CA  SER A 149      95.866  98.860 -46.757  1.00 17.71      A    C  
ANISOU  415  CA  SER A 149     3544   1768   1416    119     31     48  A    C  
ATOM    416  C   SER A 149      95.421  97.416 -46.942  1.00 15.49      A    C  
ANISOU  416  C   SER A 149     3246   1339   1299    365    -53     88  A    C  
ATOM    417  O   SER A 149      95.886  96.508 -46.247  1.00 15.70      A    O  
ANISOU  417  O   SER A 149     3329   1443   1194    452   -293    167  A    O  
ATOM    418  CB  SER A 149      96.847  99.300 -47.851  1.00 21.75      A    C  
ANISOU  418  CB  SER A 149     3917   2483   1862    191    300    146  A    C  
ATOM    419  OG  SER A 149      98.080  98.624 -47.725  1.00 24.05      A    O  
ANISOU  419  OG  SER A 149     4224   2734   2180    143    348    281  A    O  
ATOM    420  N   THR A 150      94.507  97.219 -47.879  1.00 16.22      A    N  
ANISOU  420  N   THR A 150     3292   1487   1385    382    -40    -75  A    N  
ATOM    421  CA  THR A 150      93.831  95.937 -48.056  1.00 16.58      A    C  
ANISOU  421  CA  THR A 150     3228   1517   1556    671   -148   -123  A    C  
ATOM    422  C   THR A 150      94.771  94.914 -48.685  1.00 15.58      A    C  
ANISOU  422  C   THR A 150     2975   1525   1418    731    -75    -15  A    C  
ATOM    423  O   THR A 150      95.287  95.157 -49.784  1.00 17.03      A    O  
ANISOU  423  O   THR A 150     3016   1814   1641    703    195     36  A    O  
ATOM    424  CB  THR A 150      92.638  96.155 -48.982  1.00 18.71      A    C  
ANISOU  424  CB  THR A 150     3293   1805   2012    777   -161   -163  A    C  
ATOM    425  CG2 THR A 150      91.833  94.870 -49.144  1.00 20.15      A    C  
ANISOU  425  CG2 THR A 150     3247   2197   2212    708   -122   -196  A    C  
ATOM    426  OG1 THR A 150      91.800  97.195 -48.455  1.00 20.51      A    O  
ANISOU  426  OG1 THR A 150     3629   1978   2185    818   -210    -27  A    O  
ATOM    427  N   PRO A 151      95.006  93.765 -48.059  1.00 14.70      A    N  
ANISOU  427  N   PRO A 151     2900   1532   1152    552    -24     38  A    N  
ATOM    428  CA  PRO A 151      95.823  92.723 -48.705  1.00 15.23      A    C  
ANISOU  428  CA  PRO A 151     2953   1618   1215    524    -89    -64  A    C  
ATOM    429  C   PRO A 151      95.035  92.009 -49.791  1.00 13.51      A    C  
ANISOU  429  C   PRO A 151     2767   1170   1198    451    -64     -2  A    C  
ATOM    430  O   PRO A 151      93.802  92.132 -49.860  1.00 14.87      A    O  
ANISOU  430  O   PRO A 151     3015   1408   1226    393     77     61  A    O  
ATOM    431  CB  PRO A 151      96.176  91.773 -47.549  1.00 16.72      A    C  
ANISOU  431  CB  PRO A 151     3242   1874   1235    575   -184    -90  A    C  
ATOM    432  CG  PRO A 151      95.157  92.025 -46.510  1.00 18.32      A    C  
ANISOU  432  CG  PRO A 151     3285   2223   1452    799     -1    252  A    C  
ATOM    433  CD  PRO A 151      94.662  93.432 -46.662  1.00 15.64      A    C  
ANISOU  433  CD  PRO A 151     2956   1777   1210    748      9     75  A    C  
ATOM    434  N   PRO A 152      95.712  91.259 -50.663  1.00 13.44      A    N  
ANISOU  434  N   PRO A 152     2723   1177   1206    287    -19    -46  A    N  
ATOM    435  CA  PRO A 152      95.042  90.651 -51.827  1.00 13.81      A    C  
ANISOU  435  CA  PRO A 152     2763   1230   1255    167      6   -106  A    C  
ATOM    436  C   PRO A 152      94.105  89.524 -51.435  1.00 13.30      A    C  
ANISOU  436  C   PRO A 152     2657   1251   1147    329   -142     45  A    C  
ATOM    437  O   PRO A 152      94.275  88.887 -50.383  1.00 13.48      A    O  
ANISOU  437  O   PRO A 152     2659   1372   1091    272     23    114  A    O  
ATOM    438  CB  PRO A 152      96.216  90.094 -52.650  1.00 15.21      A    C  
ANISOU  438  CB  PRO A 152     2825   1594   1362     54    164   -169  A    C  
ATOM    439  CG  PRO A 152      97.400  90.863 -52.216  1.00 15.69      A    C  
ANISOU  439  CG  PRO A 152     2763   1766   1433    141    -27   -106  A    C  
ATOM    440  CD  PRO A 152      97.179  91.171 -50.768  1.00 14.30      A    C  
ANISOU  440  CD  PRO A 152     2634   1489   1309    103    -52    -87  A    C  
ATOM    441  N   PRO A 153      93.140  89.198 -52.297  1.00 13.98      A    N  
ANISOU  441  N   PRO A 153     2592   1509   1212    397   -315    169  A    N  
ATOM    442  CA  PRO A 153      92.342  87.984 -52.089  1.00 13.65      A    C  
ANISOU  442  CA  PRO A 153     2345   1698   1142    354   -286    131  A    C  
ATOM    443  C   PRO A 153      93.251  86.772 -51.954  1.00 12.82      A    C  
ANISOU  443  C   PRO A 153     2201   1549   1122    383   -166     61  A    C  
ATOM    444  O   PRO A 153      94.243  86.632 -52.672  1.00 13.37      A    O  
ANISOU  444  O   PRO A 153     2334   1597   1149    217    -37    -49  A    O  
ATOM    445  CB  PRO A 153      91.495  87.897 -53.367  1.00 15.11      A    C  
ANISOU  445  CB  PRO A 153     2495   2023   1222    406   -281    238  A    C  
ATOM    446  CG  PRO A 153      91.458  89.294 -53.901  1.00 16.02      A    C  
ANISOU  446  CG  PRO A 153     2693   2066   1328    504   -331    122  A    C  
ATOM    447  CD  PRO A 153      92.794  89.875 -53.560  1.00 15.48      A    C  
ANISOU  447  CD  PRO A 153     2604   1978   1300    432   -278    233  A    C  
ATOM    448  N   GLY A 154      92.912  85.889 -51.016  1.00 12.51      A    N  
ANISOU  448  N   GLY A 154     2189   1562   1002    378   -168     83  A    N  
ATOM    449  CA  GLY A 154      93.728  84.723 -50.752  1.00 12.26      A    C  
ANISOU  449  CA  GLY A 154     2292   1486    881    194   -306    -17  A    C  
ATOM    450  C   GLY A 154      94.721  84.888 -49.623  1.00 11.69      A    C  
ANISOU  450  C   GLY A 154     2342   1359    742    220   -147     32  A    C  
ATOM    451  O   GLY A 154      95.349  83.899 -49.222  1.00 12.53      A    O  
ANISOU  451  O   GLY A 154     2459   1415    886    412    -96     78  A    O  
ATOM    452  N   THR A 155      94.882  86.096 -49.095  1.00 11.39      A    N  
ANISOU  452  N   THR A 155     2238   1418    671    109   -158    -54  A    N  
ATOM    453  CA  THR A 155      95.724  86.286 -47.923  1.00 10.18      A    C  
ANISOU  453  CA  THR A 155     2113   1142    615    141   -105     26  A    C  
ATOM    454  C   THR A 155      95.104  85.569 -46.728  1.00 10.14      A    C  
ANISOU  454  C   THR A 155     1928   1237    687    203   -118    -65  A    C  
ATOM    455  O   THR A 155      93.877  85.494 -46.600  1.00 10.59      A    O  
ANISOU  455  O   THR A 155     1818   1396    811    189   -159     73  A    O  
ATOM    456  CB  THR A 155      95.870  87.790 -47.645  1.00 10.85      A    C  
ANISOU  456  CB  THR A 155     2334   1115    674    -82    -17    -75  A    C  
ATOM    457  CG2 THR A 155      96.889  88.041 -46.557  1.00 12.54      A    C  
ANISOU  457  CG2 THR A 155     2305   1415   1045   -183   -167     16  A    C  
ATOM    458  OG1 THR A 155      96.310  88.460 -48.838  1.00 11.87      A    O  
ANISOU  458  OG1 THR A 155     2310   1314    886    118    128    -23  A    O  
ATOM    459  N   ARG A 156      95.958  85.015 -45.861  1.00 10.68      A    N  
ANISOU  459  N   ARG A 156     2103   1149    807    306   -134    145  A    N  
ATOM    460  CA  ARG A 156      95.511  84.250 -44.701  1.00 10.36      A    C  
ANISOU  460  CA  ARG A 156     2131    920    885    126   -223    -17  A    C  
ATOM    461  C   ARG A 156      96.252  84.700 -43.447  1.00  9.53      A    C  
ANISOU  461  C   ARG A 156     1780   1049    793     96   -124     95  A    C  
ATOM    462  O   ARG A 156      97.286  85.368 -43.520  1.00 10.11      A    O  
ANISOU  462  O   ARG A 156     1823   1198    819     -2    -88      0  A    O  
ATOM    463  CB  ARG A 156      95.705  82.742 -44.926  1.00 11.55      A    C  
ANISOU  463  CB  ARG A 156     2309    974   1104    116   -195   -391  A    C  
ATOM    464  CG  ARG A 156      94.959  82.239 -46.142  1.00 12.07      A    C  
ANISOU  464  CG  ARG A 156     2516    934   1135     79   -160   -293  A    C  
ATOM    465  CD  ARG A 156      94.718  80.752 -46.052  1.00 13.59      A    C  
ANISOU  465  CD  ARG A 156     2668   1155   1340     17    -97   -288  A    C  
ATOM    466  NE  ARG A 156      95.948  79.975 -46.099  1.00 14.63      A    N  
ANISOU  466  NE  ARG A 156     3001   1366   1192    219     13   -315  A    N  
ATOM    467  CZ  ARG A 156      95.981  78.655 -45.961  1.00 15.07      A    C  
ANISOU  467  CZ  ARG A 156     2966   1469   1291    181    -87   -205  A    C  
ATOM    468  NH1 ARG A 156      94.858  77.994 -45.711  1.00 16.23      A    N1+
ANISOU  468  NH1 ARG A 156     3267   1472   1428    -24    -95   -239  A    N1+
ATOM    469  NH2 ARG A 156      97.131  78.001 -46.055  1.00 16.26      A    N  
ANISOU  469  NH2 ARG A 156     3077   1685   1414    337    -96   -121  A    N  
ATOM    470  N   VAL A 157      95.699  84.327 -42.290  1.00  9.16      A    N  
ANISOU  470  N   VAL A 157     1644   1071    766    258    -49    111  A    N  
ATOM    471  CA  VAL A 157      96.272  84.652 -40.982  1.00  9.39      A    C  
ANISOU  471  CA  VAL A 157     1793    937    837    222   -163    -18  A    C  
ATOM    472  C   VAL A 157      96.503  83.348 -40.231  1.00  8.46      A    C  
ANISOU  472  C   VAL A 157     1537    848    830    200     -3    214  A    C  
ATOM    473  O   VAL A 157      95.556  82.581 -40.003  1.00  9.19      A    O  
ANISOU  473  O   VAL A 157     1434   1059   1000    108    -24    177  A    O  
ATOM    474  CB  VAL A 157      95.359  85.575 -40.157  1.00 10.93      A    C  
ANISOU  474  CB  VAL A 157     1990   1172    990    540   -223   -127  A    C  
ATOM    475  CG1 VAL A 157      95.969  85.805 -38.781  1.00 11.42      A    C  
ANISOU  475  CG1 VAL A 157     1980   1290   1070    161   -237   -266  A    C  
ATOM    476  CG2 VAL A 157      95.173  86.893 -40.858  1.00 13.33      A    C  
ANISOU  476  CG2 VAL A 157     2401   1349   1315    457    -41    -58  A    C  
ATOM    477  N   ARG A 158      97.755  83.096 -39.849  1.00  8.52      A    N  
ANISOU  477  N   ARG A 158     1436    903    897    434   -204     55  A    N  
ATOM    478  CA  ARG A 158      98.148  81.869 -39.164  1.00  8.60      A    C  
ANISOU  478  CA  ARG A 158     1395    942    931    357   -229     77  A    C  
ATOM    479  C   ARG A 158      98.566  82.179 -37.731  1.00  7.97      A    C  
ANISOU  479  C   ARG A 158     1382    759    885    112   -376    -19  A    C  
ATOM    480  O   ARG A 158      99.218  83.196 -37.474  1.00  9.71      A    O  
ANISOU  480  O   ARG A 158     1818    971    900    -78   -129     42  A    O  
ATOM    481  CB  ARG A 158      99.327  81.200 -39.892  1.00 10.04      A    C  
ANISOU  481  CB  ARG A 158     1834    916   1066    559      6    118  A    C  
ATOM    482  CG  ARG A 158      99.732  79.844 -39.303  1.00 11.23      A    C  
ANISOU  482  CG  ARG A 158     2080    977   1209    642    154     53  A    C  
ATOM    483  CD  ARG A 158     100.860  79.189 -40.082  1.00 12.67      A    C  
ANISOU  483  CD  ARG A 158     2277   1277   1259    622    303    114  A    C  
ATOM    484  NE  ARG A 158     100.503  79.059 -41.487  1.00 13.17      A    N  
ANISOU  484  NE  ARG A 158     2617   1233   1154    663    280    124  A    N  
ATOM    485  CZ  ARG A 158      99.800  78.057 -42.011  1.00 13.07      A    C  
ANISOU  485  CZ  ARG A 158     2706   1238   1023    634    207     82  A    C  
ATOM    486  NH1 ARG A 158      99.370  77.050 -41.259  1.00 13.75      A    N1+
ANISOU  486  NH1 ARG A 158     2775   1404   1044    451     83    119  A    N1+
ATOM    487  NH2 ARG A 158      99.519  78.071 -43.303  1.00 14.34      A    N  
ANISOU  487  NH2 ARG A 158     2687   1793    967    578    113     74  A    N  
ATOM    488  N   ALA A 159      98.212  81.284 -36.801  1.00  8.32      A    N  
ANISOU  488  N   ALA A 159     1455    900    808    252   -142    146  A    N  
ATOM    489  CA  ALA A 159      98.635  81.362 -35.407  1.00  7.44      A    C  
ANISOU  489  CA  ALA A 159     1052    902    873    192     -2    197  A    C  
ATOM    490  C   ALA A 159      99.415  80.104 -35.049  1.00  7.75      A    C  
ANISOU  490  C   ALA A 159     1179    914    852     34   -100    125  A    C  
ATOM    491  O   ALA A 159      99.022  78.993 -35.418  1.00  8.89      A    O  
ANISOU  491  O   ALA A 159     1363    996   1017     71   -180    -25  A    O  
ATOM    492  CB  ALA A 159      97.436  81.479 -34.458  1.00  9.01      A    C  
ANISOU  492  CB  ALA A 159     1156   1222   1047    450     46     77  A    C  
ATOM    493  N   MET A 160     100.510  80.285 -34.315  1.00  8.64      A    N  
ANISOU  493  N   MET A 160     1076   1268    937    290   -168    176  A    N  
ATOM    494  CA  MET A 160     101.370  79.189 -33.885  1.00  9.44      A    C  
ANISOU  494  CA  MET A 160     1323   1219   1046    428   -272     15  A    C  
ATOM    495  C   MET A 160     101.965  79.556 -32.534  1.00  8.89      A    C  
ANISOU  495  C   MET A 160     1311    990   1076    350   -317    -34  A    C  
ATOM    496  O   MET A 160     102.289  80.715 -32.298  1.00 10.63      A    O  
ANISOU  496  O   MET A 160     1978    864   1198    123   -470    -17  A    O  
ATOM    497  CB  MET A 160     102.522  79.002 -34.883  1.00 11.59      A    C  
ANISOU  497  CB  MET A 160     1523   1602   1278    752    -63    -73  A    C  
ATOM    498  CG  MET A 160     103.508  77.890 -34.535  1.00 13.49      A    C  
ANISOU  498  CG  MET A 160     1544   1981   1599    548    215   -120  A    C  
ATOM    499  SD  MET A 160     104.886  77.829 -35.698  1.00 16.48      A    S  
ANISOU  499  SD  MET A 160     1837   2615   1808    321    125   -213  A    S  
ATOM    500  CE  MET A 160     104.056  77.218 -37.166  1.00 17.42      A    C  
ANISOU  500  CE  MET A 160     2024   2732   1864    -78    -51   -319  A    C  
ATOM    501  N   ALA A 161     102.111  78.576 -31.653  1.00  9.09      A    N  
ANISOU  501  N   ALA A 161     1278   1086   1089    236   -288    200  A    N  
ATOM    502  CA  ALA A 161     102.740  78.793 -30.357  1.00  9.68      A    C  
ANISOU  502  CA  ALA A 161     1265   1171   1243    232   -183    282  A    C  
ATOM    503  C   ALA A 161     104.149  78.223 -30.355  1.00  9.36      A    C  
ANISOU  503  C   ALA A 161      994   1237   1325     69   -158    186  A    C  
ATOM    504  O   ALA A 161     104.397  77.164 -30.941  1.00 10.45      A    O  
ANISOU  504  O   ALA A 161     1118   1338   1514    209   -114    -18  A    O  
ATOM    505  CB  ALA A 161     101.936  78.126 -29.242  1.00 10.31      A    C  
ANISOU  505  CB  ALA A 161     1355   1273   1289     47   -122    449  A    C  
ATOM    506  N   ILE A 162     105.076  78.946 -29.720  1.00  8.59      A    N  
ANISOU  506  N   ILE A 162      882   1107   1274    163   -274    285  A    N  
ATOM    507  CA  ILE A 162     106.415  78.443 -29.441  1.00  8.52      A    C  
ANISOU  507  CA  ILE A 162      925   1085   1229     40   -206     98  A    C  
ATOM    508  C   ILE A 162     106.741  78.713 -27.978  1.00  8.20      A    C  
ANISOU  508  C   ILE A 162      913    865   1338    112   -215    173  A    C  
ATOM    509  O   ILE A 162     106.166  79.600 -27.345  1.00  9.47      A    O  
ANISOU  509  O   ILE A 162     1144   1000   1453    381   -129    -36  A    O  
ATOM    510  CB  ILE A 162     107.499  79.064 -30.351  1.00 10.67      A    C  
ANISOU  510  CB  ILE A 162     1537   1189   1327   -133     93    154  A    C  
ATOM    511  CG1 ILE A 162     107.662  80.565 -30.085  1.00 11.59      A    C  
ANISOU  511  CG1 ILE A 162     1461   1421   1523    -81    263    316  A    C  
ATOM    512  CG2 ILE A 162     107.178  78.803 -31.823  1.00 13.42      A    C  
ANISOU  512  CG2 ILE A 162     2083   1725   1291    -34     -8     35  A    C  
ATOM    513  CD1 ILE A 162     108.917  81.146 -30.735  1.00 14.10      A    C  
ANISOU  513  CD1 ILE A 162     1821   1738   1800   -292     88    289  A    C  
ATOM    514  N   TYR A 163     107.665  77.926 -27.428  1.00  9.33      A    N  
ANISOU  514  N   TYR A 163      963   1152   1432    214   -133    404  A    N  
ATOM    515  CA  TYR A 163     108.167  78.249 -26.099  1.00  9.60      A    C  
ANISOU  515  CA  TYR A 163      955   1207   1483    142   -280    371  A    C  
ATOM    516  C   TYR A 163     108.998  79.524 -26.142  1.00 10.34      A    C  
ANISOU  516  C   TYR A 163     1105   1260   1565     93   -211    200  A    C  
ATOM    517  O   TYR A 163     109.766  79.758 -27.077  1.00 11.90      A    O  
ANISOU  517  O   TYR A 163     1305   1582   1633    -53    -90     78  A    O  
ATOM    518  CB  TYR A 163     108.961  77.082 -25.493  1.00  9.75      A    C  
ANISOU  518  CB  TYR A 163      793   1293   1618    157   -244    479  A    C  
ATOM    519  CG  TYR A 163     108.021  75.978 -25.077  1.00  9.91      A    C  
ANISOU  519  CG  TYR A 163      865   1320   1582      8   -131    255  A    C  
ATOM    520  CD1 TYR A 163     107.116  76.174 -24.038  1.00 11.20      A    C  
ANISOU  520  CD1 TYR A 163     1123   1487   1646    -33   -193    382  A    C  
ATOM    521  CD2 TYR A 163     107.996  74.763 -25.754  1.00 10.43      A    C  
ANISOU  521  CD2 TYR A 163     1127   1220   1615     34   -225    188  A    C  
ATOM    522  CE1 TYR A 163     106.220  75.196 -23.681  1.00 11.51      A    C  
ANISOU  522  CE1 TYR A 163     1217   1402   1756    -31   -137    327  A    C  
ATOM    523  CE2 TYR A 163     107.101  73.782 -25.406  1.00 11.30      A    C  
ANISOU  523  CE2 TYR A 163     1476   1259   1557    120   -133    280  A    C  
ATOM    524  CZ  TYR A 163     106.211  74.006 -24.373  1.00 11.51      A    C  
ANISOU  524  CZ  TYR A 163     1376   1304   1694   -132      7    311  A    C  
ATOM    525  OH  TYR A 163     105.311  73.028 -24.032  1.00 13.28      A    O  
ANISOU  525  OH  TYR A 163     1897   1466   1684   -239     90    419  A    O  
ATOM    526  N   LYS A 164     108.832  80.359 -25.114  1.00 10.64      A    N  
ANISOU  526  N   LYS A 164     1332   1006   1704     93   -260     59  A    N  
ATOM    527  CA  LYS A 164     109.515  81.648 -25.074  1.00 11.87      A    C  
ANISOU  527  CA  LYS A 164     1523   1125   1860     44   -183    -75  A    C  
ATOM    528  C   LYS A 164     110.984  81.515 -24.688  1.00 13.19      A    C  
ANISOU  528  C   LYS A 164     1476   1527   2008   -170   -199    156  A    C  
ATOM    529  O   LYS A 164     111.822  82.283 -25.181  1.00 14.64      A    O  
ANISOU  529  O   LYS A 164     1472   1884   2207    -47   -115     78  A    O  
ATOM    530  CB  LYS A 164     108.786  82.580 -24.105  1.00 13.97      A    C  
ANISOU  530  CB  LYS A 164     2070   1152   2086    -14   -137   -269  A    C  
ATOM    531  CG  LYS A 164     109.403  83.955 -23.998  1.00 16.78      A    C  
ANISOU  531  CG  LYS A 164     2427   1434   2516   -262     81   -399  A    C  
ATOM    532  CD  LYS A 164     108.684  84.799 -22.967  1.00 20.11      A    C  
ANISOU  532  CD  LYS A 164     2837   1827   2977   -342    396   -728  A    C  
ATOM    533  CE  LYS A 164     109.230  86.223 -22.962  1.00 23.14      A    C  
ANISOU  533  CE  LYS A 164     3192   2301   3297   -296    594   -937  A    C  
ATOM    534  NZ  LYS A 164     108.811  86.992 -21.763  1.00 26.14      A    N1+
ANISOU  534  NZ  LYS A 164     3519   2872   3540   -352    587   -880  A    N1+
ATOM    535  N   GLN A 165     111.318  80.565 -23.816  1.00 13.30      A    N  
ANISOU  535  N   GLN A 165     1285   1667   2101   -131   -414    146  A    N  
ATOM    536  CA  GLN A 165     112.695  80.399 -23.366  1.00 14.41      A    C  
ANISOU  536  CA  GLN A 165     1297   1932   2247   -296   -478     53  A    C  
ATOM    537  C   GLN A 165     113.516  79.688 -24.433  1.00 15.52      A    C  
ANISOU  537  C   GLN A 165     1512   1816   2567    -59   -304    274  A    C  
ATOM    538  O   GLN A 165     113.094  78.657 -24.965  1.00 15.50      A    O  
ANISOU  538  O   GLN A 165     1536   1726   2626     60   -323    212  A    O  
ATOM    539  CB  GLN A 165     112.728  79.595 -22.072  1.00 16.04      A    C  
ANISOU  539  CB  GLN A 165     1499   2450   2144    -97   -719     50  A    C  
ATOM    540  CG  GLN A 165     112.047  80.284 -20.910  1.00 18.92      A    C  
ANISOU  540  CG  GLN A 165     2184   2879   2127    -43   -879   -140  A    C  
ATOM    541  CD  GLN A 165     111.722  79.326 -19.781  1.00 21.88      A    C  
ANISOU  541  CD  GLN A 165     2643   3544   2126     54   -982     24  A    C  
ATOM    542  NE2 GLN A 165     112.447  79.450 -18.677  1.00 25.42      A    N  
ANISOU  542  NE2 GLN A 165     3090   4239   2331     -9   -990     -5  A    N  
ATOM    543  OE1 GLN A 165     110.837  78.477 -19.902  1.00 21.40      A    O  
ANISOU  543  OE1 GLN A 165     2675   3437   2021    281   -881    195  A    O  
ATOM    544  N   SER A 166     114.712  80.219 -24.702  1.00 17.64      A    N  
ANISOU  544  N   SER A 166     1803   1992   2908    -67    -75    478  A    N  
ATOM    545  CA ASER A 166     115.532  79.704 -25.796  0.49 17.77      A    C  
ANISOU  545  CA ASER A 166     1821   1937   2993   -157    -31    486  A    C  
ATOM    546  CA BSER A 166     115.536  79.705 -25.795  0.51 18.30      A    C  
ANISOU  546  CA BSER A 166     1864   2078   3012   -165    -71    418  A    C  
ATOM    547  C   SER A 166     115.838  78.221 -25.629  1.00 16.59      A    C  
ANISOU  547  C   SER A 166     1504   1898   2902    -20    -69    421  A    C  
ATOM    548  O   SER A 166     115.877  77.479 -26.615  1.00 16.90      A    O  
ANISOU  548  O   SER A 166     1472   2130   2818     77     79    474  A    O  
ATOM    549  CB ASER A 166     116.825  80.510 -25.915  0.49 18.39      A    C  
ANISOU  549  CB ASER A 166     1977   1923   3088   -197     -1    625  A    C  
ATOM    550  CB BSER A 166     116.834  80.504 -25.891  0.51 20.02      A    C  
ANISOU  550  CB BSER A 166     2120   2358   3129   -227   -103    413  A    C  
ATOM    551  OG ASER A 166     116.547  81.842 -26.305  0.49 18.73      A    O  
ANISOU  551  OG ASER A 166     2077   1911   3130     76    -26    622  A    O  
ATOM    552  OG BSER A 166     117.545  80.453 -24.668  0.51 21.24      A    O  
ANISOU  552  OG BSER A 166     2266   2636   3168    -36   -153    290  A    O  
ATOM    553  N   GLN A 167     116.059  77.767 -24.390  1.00 16.06      A    N  
ANISOU  553  N   GLN A 167     1228   1964   2909     37   -213    395  A    N  
ATOM    554  CA  GLN A 167     116.409  76.367 -24.160  1.00 17.29      A    C  
ANISOU  554  CA  GLN A 167     1434   2311   2823    106   -418    335  A    C  
ATOM    555  C   GLN A 167     115.253  75.408 -24.422  1.00 16.11      A    C  
ANISOU  555  C   GLN A 167     1441   1920   2762     63   -300    253  A    C  
ATOM    556  O   GLN A 167     115.470  74.190 -24.434  1.00 17.37      A    O  
ANISOU  556  O   GLN A 167     1538   2088   2972     69   -285    256  A    O  
ATOM    557  CB  GLN A 167     116.988  76.160 -22.751  1.00 19.81      A    C  
ANISOU  557  CB  GLN A 167     1851   2803   2874    172   -451    269  A    C  
ATOM    558  CG  GLN A 167     116.001  76.368 -21.604  1.00 22.62      A    C  
ANISOU  558  CG  GLN A 167     2307   3306   2981     63   -263     63  A    C  
ATOM    559  CD  GLN A 167     115.947  77.806 -21.098  1.00 25.30      A    C  
ANISOU  559  CD  GLN A 167     2757   3772   3083     50   -254    -60  A    C  
ATOM    560  NE2 GLN A 167     115.629  77.966 -19.815  1.00 27.47      A    N  
ANISOU  560  NE2 GLN A 167     3175   4107   3154    -23   -294    -47  A    N  
ATOM    561  OE1 GLN A 167     116.185  78.756 -21.844  1.00 24.97      A    O  
ANISOU  561  OE1 GLN A 167     2693   3671   3123    134   -396   -141  A    O  
ATOM    562  N   HIS A 168     114.044  75.920 -24.639  1.00 13.60      A    N  
ANISOU  562  N   HIS A 168     1098   1607   2461     56   -296    373  A    N  
ATOM    563  CA  HIS A 168     112.892  75.096 -24.976  1.00 14.08      A    C  
ANISOU  563  CA  HIS A 168     1269   1786   2292     51   -111    266  A    C  
ATOM    564  C   HIS A 168     112.338  75.381 -26.361  1.00 13.13      A    C  
ANISOU  564  C   HIS A 168     1067   1739   2185      1   -139    209  A    C  
ATOM    565  O   HIS A 168     111.362  74.740 -26.763  1.00 13.22      A    O  
ANISOU  565  O   HIS A 168     1173   1648   2203    -60   -249   -115  A    O  
ATOM    566  CB  HIS A 168     111.775  75.289 -23.944  1.00 14.17      A    C  
ANISOU  566  CB  HIS A 168     1336   1880   2166    184   -115    378  A    C  
ATOM    567  CG  HIS A 168     112.184  74.912 -22.561  1.00 15.13      A    C  
ANISOU  567  CG  HIS A 168     1473   2100   2177     36   -205    497  A    C  
ATOM    568  CD2 HIS A 168     112.292  75.646 -21.428  1.00 15.48      A    C  
ANISOU  568  CD2 HIS A 168     1604   2148   2128      2   -199    566  A    C  
ATOM    569  ND1 HIS A 168     112.560  73.629 -22.229  1.00 16.32      A    N  
ANISOU  569  ND1 HIS A 168     1785   2196   2221    405   -166    623  A    N  
ATOM    570  CE1 HIS A 168     112.885  73.588 -20.949  1.00 17.31      A    C  
ANISOU  570  CE1 HIS A 168     2009   2344   2225    199   -328    640  A    C  
ATOM    571  NE2 HIS A 168     112.728  74.797 -20.440  1.00 17.40      A    N  
ANISOU  571  NE2 HIS A 168     1983   2344   2285     68   -292    701  A    N  
ATOM    572  N   MET A 169     112.944  76.305 -27.110  1.00 14.43      A    N  
ANISOU  572  N   MET A 169     1495   1761   2225     69    -14    442  A    N  
ATOM    573  CA  MET A 169     112.322  76.796 -28.332  1.00 16.16      A    C  
ANISOU  573  CA  MET A 169     1626   2029   2486    138     65    368  A    C  
ATOM    574  C   MET A 169     112.183  75.731 -29.402  1.00 15.55      A    C  
ANISOU  574  C   MET A 169     1396   2221   2293    203    109    370  A    C  
ATOM    575  O   MET A 169     111.294  75.841 -30.252  1.00 15.42      A    O  
ANISOU  575  O   MET A 169     1444   2395   2019    223    -94    351  A    O  
ATOM    576  CB  MET A 169     113.124  77.951 -28.905  1.00 20.81      A    C  
ANISOU  576  CB  MET A 169     2555   2235   3119    -19    411    477  A    C  
ATOM    577  CG  MET A 169     112.760  79.262 -28.345  1.00 26.68      A    C  
ANISOU  577  CG  MET A 169     3651   2567   3920     26   1078    518  A    C  
ATOM    578  SD  MET A 169     113.124  80.514 -29.571  1.00 30.62      A    S  
ANISOU  578  SD  MET A 169     4553   2536   4546    -46   1774    423  A    S  
ATOM    579  CE  MET A 169     112.644  81.953 -28.634  1.00 31.37      A    C  
ANISOU  579  CE  MET A 169     4612   2719   4587    316   1735    101  A    C  
ATOM    580  N   THR A 170     113.062  74.728 -29.418  1.00 15.83      A    N  
ANISOU  580  N   THR A 170     1351   2278   2387    281      3    265  A    N  
ATOM    581  CA  THR A 170     112.955  73.704 -30.448  1.00 17.06      A    C  
ANISOU  581  CA  THR A 170     1478   2382   2620    313    116     36  A    C  
ATOM    582  C   THR A 170     111.895  72.655 -30.141  1.00 17.08      A    C  
ANISOU  582  C   THR A 170     1525   2323   2643    159    272   -116  A    C  
ATOM    583  O   THR A 170     111.614  71.821 -31.008  1.00 19.18      A    O  
ANISOU  583  O   THR A 170     1700   2742   2845     96    242   -436  A    O  
ATOM    584  CB  THR A 170     114.302  73.021 -30.693  1.00 18.92      A    C  
ANISOU  584  CB  THR A 170     1737   2502   2950    354    234    155  A    C  
ATOM    585  CG2 THR A 170     115.348  74.041 -31.133  1.00 19.72      A    C  
ANISOU  585  CG2 THR A 170     1803   2553   3136    149    283    216  A    C  
ATOM    586  OG1 THR A 170     114.730  72.383 -29.489  1.00 21.11      A    O  
ANISOU  586  OG1 THR A 170     2085   2817   3120    615     53    165  A    O  
ATOM    587  N   GLU A 171     111.298  72.674 -28.948  1.00 15.22      A    N  
ANISOU  587  N   GLU A 171     1094   2149   2542    155    232     43  A    N  
ATOM    588  CA  GLU A 171     110.271  71.704 -28.584  1.00 14.36      A    C  
ANISOU  588  CA  GLU A 171     1295   1748   2412    397     48    151  A    C  
ATOM    589  C   GLU A 171     108.908  72.172 -29.080  1.00 12.44      A    C  
ANISOU  589  C   GLU A 171     1152   1416   2160    383    -75    -14  A    C  
ATOM    590  O   GLU A 171     108.512  73.317 -28.848  1.00 13.28      A    O  
ANISOU  590  O   GLU A 171     1342   1382   2323    317    -11   -108  A    O  
ATOM    591  CB  GLU A 171     110.219  71.525 -27.066  1.00 16.71      A    C  
ANISOU  591  CB  GLU A 171     1703   2187   2459    319     -1    267  A    C  
ATOM    592  CG  GLU A 171     109.147  70.530 -26.612  1.00 19.32      A    C  
ANISOU  592  CG  GLU A 171     2010   2718   2614    245    -69    389  A    C  
ATOM    593  CD  GLU A 171     109.171  70.248 -25.121  1.00 22.36      A    C  
ANISOU  593  CD  GLU A 171     2360   3336   2802    148    -28    354  A    C  
ATOM    594  OE1 GLU A 171     110.226  70.464 -24.480  1.00 24.27      A    O  
ANISOU  594  OE1 GLU A 171     2663   3754   2802     45    -15    314  A    O  
ATOM    595  OE2 GLU A 171     108.129  69.806 -24.595  1.00 23.08      A    O1-
ANISOU  595  OE2 GLU A 171     2437   3450   2882    130    -45    408  A    O1-
ATOM    596  N   VAL A 172     108.183  71.275 -29.748  1.00 11.99      A    N  
ANISOU  596  N   VAL A 172     1327   1351   1877    160     22    -81  A    N  
ATOM    597  CA  VAL A 172     106.847  71.598 -30.236  1.00 10.89      A    C  
ANISOU  597  CA  VAL A 172     1109   1335   1695    -13    101    -13  A    C  
ATOM    598  C   VAL A 172     105.907  71.852 -29.059  1.00 11.01      A    C  
ANISOU  598  C   VAL A 172     1322   1282   1580     77    128     17  A    C  
ATOM    599  O   VAL A 172     105.819  71.041 -28.128  1.00 11.78      A    O  
ANISOU  599  O   VAL A 172     1490   1371   1616    191    102    297  A    O  
ATOM    600  CB  VAL A 172     106.329  70.458 -31.125  1.00 13.47      A    C  
ANISOU  600  CB  VAL A 172     1687   1681   1750    152     76    -92  A    C  
ATOM    601  CG1 VAL A 172     104.865  70.686 -31.490  1.00 14.49      A    C  
ANISOU  601  CG1 VAL A 172     1932   1625   1949    329   -312   -124  A    C  
ATOM    602  CG2 VAL A 172     107.204  70.287 -32.371  1.00 14.92      A    C  
ANISOU  602  CG2 VAL A 172     1962   1975   1730    138    307    -41  A    C  
ATOM    603  N   VAL A 173     105.192  72.975 -29.096  1.00  9.52      A    N  
ANISOU  603  N   VAL A 173      981   1155   1481    141     89    -47  A    N  
ATOM    604  CA  VAL A 173     104.139  73.250 -28.119  1.00  9.24      A    C  
ANISOU  604  CA  VAL A 173     1084    968   1459     72     90     15  A    C  
ATOM    605  C   VAL A 173     102.912  72.424 -28.486  1.00  9.86      A    C  
ANISOU  605  C   VAL A 173     1217   1052   1477    -35    -18    124  A    C  
ATOM    606  O   VAL A 173     102.381  72.549 -29.594  1.00 10.91      A    O  
ANISOU  606  O   VAL A 173     1378   1369   1397     85   -188     93  A    O  
ATOM    607  CB  VAL A 173     103.787  74.743 -28.088  1.00 10.09      A    C  
ANISOU  607  CB  VAL A 173     1151   1078   1606    217     92      4  A    C  
ATOM    608  CG1 VAL A 173     102.665  74.984 -27.097  1.00 10.68      A    C  
ANISOU  608  CG1 VAL A 173     1304   1214   1539    380     87     57  A    C  
ATOM    609  CG2 VAL A 173     105.010  75.573 -27.722  1.00 10.38      A    C  
ANISOU  609  CG2 VAL A 173     1031   1072   1841   -157    -70    -31  A    C  
ATOM    610  N   ARG A 174     102.452  71.589 -27.556  1.00  9.90      A    N  
ANISOU  610  N   ARG A 174     1183    967   1612   -158    -37    161  A    N  
ATOM    611  CA  ARG A 174     101.295  70.738 -27.795  1.00 10.27      A    C  
ANISOU  611  CA  ARG A 174     1290   1042   1568   -106     14     30  A    C  
ATOM    612  C   ARG A 174     100.495  70.615 -26.510  1.00 10.11      A    C  
ANISOU  612  C   ARG A 174     1287   1151   1404   -123     17     40  A    C  
ATOM    613  O   ARG A 174     100.967  70.965 -25.422  1.00 11.67      A    O  
ANISOU  613  O   ARG A 174     1627   1346   1461   -228   -124     39  A    O  
ATOM    614  CB  ARG A 174     101.729  69.344 -28.236  1.00 12.29      A    C  
ANISOU  614  CB  ARG A 174     1729   1192   1749    -48    -27    -41  A    C  
ATOM    615  CG  ARG A 174     102.626  68.654 -27.212  1.00 13.43      A    C  
ANISOU  615  CG  ARG A 174     1938   1182   1983    217    -98     29  A    C  
ATOM    616  CD  ARG A 174     102.927  67.213 -27.607  1.00 15.30      A    C  
ANISOU  616  CD  ARG A 174     2426   1387   2000    296     76      0  A    C  
ATOM    617  NE  ARG A 174     103.614  67.115 -28.897  1.00 17.17      A    N  
ANISOU  617  NE  ARG A 174     2779   1708   2036    514    283     58  A    N  
ATOM    618  CZ  ARG A 174     103.016  66.798 -30.043  1.00 18.27      A    C  
ANISOU  618  CZ  ARG A 174     3106   1854   1981    347    315     89  A    C  
ATOM    619  NH1 ARG A 174     103.721  66.730 -31.167  1.00 19.26      A    N1+
ANISOU  619  NH1 ARG A 174     3412   1926   1979    432    505    -62  A    N1+
ATOM    620  NH2 ARG A 174     101.707  66.549 -30.069  1.00 17.50      A    N  
ANISOU  620  NH2 ARG A 174     2966   1772   1912    294    204    317  A    N  
ATOM    621  N   ARG A 175      99.280  70.087 -26.633  1.00 10.49      A    N  
ANISOU  621  N   ARG A 175     1429   1233   1324    -88     71    243  A    N  
ATOM    622  CA  ARG A 175      98.495  69.799 -25.440  1.00 10.25      A    C  
ANISOU  622  CA  ARG A 175     1356   1253   1285    -23   -150    345  A    C  
ATOM    623  C   ARG A 175      99.113  68.659 -24.643  1.00  9.90      A    C  
ANISOU  623  C   ARG A 175     1636    904   1220     80   -170     57  A    C  
ATOM    624  O   ARG A 175      99.790  67.773 -25.185  1.00 11.06      A    O  
ANISOU  624  O   ARG A 175     1685   1079   1439    -97    -65    117  A    O  
ATOM    625  CB  ARG A 175      97.058  69.460 -25.808  1.00 10.10      A    C  
ANISOU  625  CB  ARG A 175     1268   1251   1319     69   -279    353  A    C  
ATOM    626  CG  ARG A 175      96.325  70.682 -26.346  1.00 10.64      A    C  
ANISOU  626  CG  ARG A 175     1157   1488   1398    294   -240    434  A    C  
ATOM    627  CD  ARG A 175      94.905  70.319 -26.695  1.00 12.64      A    C  
ANISOU  627  CD  ARG A 175     1216   2001   1585    451    -12    340  A    C  
ATOM    628  NE  ARG A 175      93.991  70.434 -25.568  1.00 13.75      A    N  
ANISOU  628  NE  ARG A 175     1748   1834   1641      6    111    619  A    N  
ATOM    629  CZ  ARG A 175      92.767  69.924 -25.568  1.00 12.31      A    C  
ANISOU  629  CZ  ARG A 175     1584   1613   1480   -260    -81    789  A    C  
ATOM    630  NH1 ARG A 175      92.355  69.181 -26.592  1.00 12.42      A    N1+
ANISOU  630  NH1 ARG A 175     1466   1762   1491    -39   -182    456  A    N1+
ATOM    631  NH2 ARG A 175      91.965  70.146 -24.546  1.00 14.38      A    N  
ANISOU  631  NH2 ARG A 175     1862   1923   1679    103    -85    529  A    N  
ATOM    632  N   CYS A 176      98.834  68.675 -23.343  1.00 10.23      A    N  
ANISOU  632  N   CYS A 176     1819    918   1150   -146   -197    170  A    N  
ATOM    633  CA  CYS A 176      99.419  67.740 -22.400  1.00 10.98      A    C  
ANISOU  633  CA  CYS A 176     1938   1037   1198    -62   -180    168  A    C  
ATOM    634  C   CYS A 176      98.783  66.357 -22.553  1.00 12.02      A    C  
ANISOU  634  C   CYS A 176     2048   1219   1299    -75   -170     23  A    C  
ATOM    635  O   CYS A 176      97.779  66.190 -23.260  1.00 10.98      A    O  
ANISOU  635  O   CYS A 176     1829    964   1378   -205   -229    263  A    O  
ATOM    636  CB  CYS A 176      99.233  68.278 -20.978  1.00 10.81      A    C  
ANISOU  636  CB  CYS A 176     1800   1075   1234     41    -18   -121  A    C  
ATOM    637  SG  CYS A 176      97.531  68.127 -20.322  1.00 11.75      A    S  
ANISOU  637  SG  CYS A 176     2017   1170   1279   -119    -13    122  A    S  
ATOM    638  N   PRO A 177      99.362  65.332 -21.910  1.00 12.28      A    N  
ANISOU  638  N   PRO A 177     2278   1103   1286   -106   -213    -47  A    N  
ATOM    639  CA  PRO A 177      98.826  63.973 -22.084  1.00 13.84      A    C  
ANISOU  639  CA  PRO A 177     2583   1234   1441   -209   -207    177  A    C  
ATOM    640  C   PRO A 177      97.395  63.818 -21.619  1.00 13.16      A    C  
ANISOU  640  C   PRO A 177     2334   1288   1376   -511   -199    153  A    C  
ATOM    641  O   PRO A 177      96.689  62.928 -22.107  1.00 16.02      A    O  
ANISOU  641  O   PRO A 177     2804   1687   1595   -777   -129     35  A    O  
ATOM    642  CB  PRO A 177      99.785  63.101 -21.264  1.00 14.64      A    C  
ANISOU  642  CB  PRO A 177     2589   1347   1628     25   -398    168  A    C  
ATOM    643  CG  PRO A 177     101.018  63.891 -21.140  1.00 15.53      A    C  
ANISOU  643  CG  PRO A 177     2687   1427   1788     67   -425     96  A    C  
ATOM    644  CD  PRO A 177     100.609  65.324 -21.123  1.00 13.62      A    C  
ANISOU  644  CD  PRO A 177     2405   1255   1516     73   -353     26  A    C  
ATOM    645  N   HIS A 178      96.941  64.639 -20.672  1.00 12.85      A    N  
ANISOU  645  N   HIS A 178     2318   1330   1233   -268   -106    126  A    N  
ATOM    646  CA  HIS A 178      95.545  64.579 -20.267  1.00 13.43      A    C  
ANISOU  646  CA  HIS A 178     2497   1300   1306   -197   -113    190  A    C  
ATOM    647  C   HIS A 178      94.639  65.241 -21.295  1.00 13.32      A    C  
ANISOU  647  C   HIS A 178     2399   1293   1368    -48   -130    233  A    C  
ATOM    648  O   HIS A 178      93.677  64.631 -21.774  1.00 14.15      A    O  
ANISOU  648  O   HIS A 178     2343   1487   1546   -205   -233    363  A    O  
ATOM    649  CB  HIS A 178      95.346  65.247 -18.908  1.00 14.88      A    C  
ANISOU  649  CB  HIS A 178     2660   1510   1482    113    -10    212  A    C  
ATOM    650  CG  HIS A 178      93.910  65.523 -18.601  1.00 15.86      A    C  
ANISOU  650  CG  HIS A 178     2711   1612   1705    125    336    308  A    C  
ATOM    651  CD2 HIS A 178      93.231  66.689 -18.483  1.00 18.09      A    C  
ANISOU  651  CD2 HIS A 178     2868   2030   1977    230    415    301  A    C  
ATOM    652  ND1 HIS A 178      92.984  64.520 -18.422  1.00 17.76      A    N  
ANISOU  652  ND1 HIS A 178     2914   1818   2016    266    384    268  A    N  
ATOM    653  CE1 HIS A 178      91.799  65.055 -18.184  1.00 18.84      A    C  
ANISOU  653  CE1 HIS A 178     3031   1877   2249    242    528    287  A    C  
ATOM    654  NE2 HIS A 178      91.921  66.370 -18.222  1.00 20.27      A    N  
ANISOU  654  NE2 HIS A 178     3254   2200   2248    115    536    432  A    N  
ATOM    655  N   HIS A 179      94.923  66.495 -21.640  1.00 12.47      A    N  
ANISOU  655  N   HIS A 179     2151   1299   1289    104    -55    272  A    N  
ATOM    656  CA  HIS A 179      93.981  67.228 -22.476  1.00 11.83      A    C  
ANISOU  656  CA  HIS A 179     1901   1214   1379    126   -138    202  A    C  
ATOM    657  C   HIS A 179      93.924  66.692 -23.902  1.00 11.91      A    C  
ANISOU  657  C   HIS A 179     1860   1175   1490     42   -146     70  A    C  
ATOM    658  O   HIS A 179      92.870  66.775 -24.547  1.00 12.72      A    O  
ANISOU  658  O   HIS A 179     1999   1208   1627    105   -343     96  A    O  
ATOM    659  CB  HIS A 179      94.277  68.722 -22.434  1.00 11.83      A    C  
ANISOU  659  CB  HIS A 179     2070   1012   1413    192     43     89  A    C  
ATOM    660  CG  HIS A 179      93.761  69.389 -21.198  1.00 12.66      A    C  
ANISOU  660  CG  HIS A 179     2063   1202   1546    377     90   -122  A    C  
ATOM    661  CD2 HIS A 179      92.497  69.524 -20.726  1.00 14.06      A    C  
ANISOU  661  CD2 HIS A 179     2121   1476   1746    329     59    -74  A    C  
ATOM    662  ND1 HIS A 179      94.582  69.997 -20.271  1.00 12.39      A    N  
ANISOU  662  ND1 HIS A 179     1873   1215   1618    193    219    -82  A    N  
ATOM    663  CE1 HIS A 179      93.847  70.481 -19.284  1.00 12.60      A    C  
ANISOU  663  CE1 HIS A 179     1788   1293   1704    -44    203    -14  A    C  
ATOM    664  NE2 HIS A 179      92.578  70.208 -19.536  1.00 14.54      A    N  
ANISOU  664  NE2 HIS A 179     2254   1435   1833    146     83   -176  A    N  
ATOM    665  N   GLU A 180      95.018  66.130 -24.420  1.00 10.85      A    N  
ANISOU  665  N   GLU A 180     1689   1097   1336    -74   -175    152  A    N  
ATOM    666  CA  GLU A 180      94.921  65.566 -25.761  1.00 11.98      A    C  
ANISOU  666  CA  GLU A 180     1674   1453   1426    -70   -239    127  A    C  
ATOM    667  C   GLU A 180      93.962  64.383 -25.818  1.00 12.40      A    C  
ANISOU  667  C   GLU A 180     1818   1378   1516    -16   -288    123  A    C  
ATOM    668  O   GLU A 180      93.509  64.031 -26.909  1.00 13.67      A    O  
ANISOU  668  O   GLU A 180     2159   1560   1475     20   -354    150  A    O  
ATOM    669  CB  GLU A 180      96.296  65.207 -26.343  1.00 13.64      A    C  
ANISOU  669  CB  GLU A 180     1925   1580   1678     81    -78    224  A    C  
ATOM    670  CG  GLU A 180      96.934  63.968 -25.765  1.00 14.86      A    C  
ANISOU  670  CG  GLU A 180     2404   1545   1697    141   -127    453  A    C  
ATOM    671  CD  GLU A 180      98.122  63.459 -26.578  1.00 16.53      A    C  
ANISOU  671  CD  GLU A 180     2945   1586   1749    179      1    570  A    C  
ATOM    672  OE1 GLU A 180      98.587  64.172 -27.490  1.00 16.12      A    O  
ANISOU  672  OE1 GLU A 180     2715   1583   1829   -149    228    247  A    O  
ATOM    673  OE2 GLU A 180      98.592  62.328 -26.306  1.00 19.46      A    O1-
ANISOU  673  OE2 GLU A 180     3525   1905   1963    586     89    662  A    O1-
ATOM    674  N   ARG A 181      93.620  63.787 -24.669  1.00 11.85      A    N  
ANISOU  674  N   ARG A 181     1582   1184   1738   -207   -108    231  A    N  
ATOM    675  CA  ARG A 181      92.755  62.612 -24.602  1.00 12.57      A    C  
ANISOU  675  CA  ARG A 181     1546   1193   2037     -8   -111    157  A    C  
ATOM    676  C   ARG A 181      91.369  62.897 -24.029  1.00 16.16      A    C  
ANISOU  676  C   ARG A 181     1853   1603   2685     26    -74    -68  A    C  
ATOM    677  O   ARG A 181      90.624  61.952 -23.752  1.00 18.37      A    O  
ANISOU  677  O   ARG A 181     2214   1792   2972   -184    182   -115  A    O  
ATOM    678  CB  ARG A 181      93.426  61.509 -23.774  1.00 12.82      A    C  
ANISOU  678  CB  ARG A 181     1831   1072   1970     85    -89     52  A    C  
ATOM    679  CG  ARG A 181      94.730  61.022 -24.366  1.00 13.00      A    C  
ANISOU  679  CG  ARG A 181     1925   1134   1880    222    -14    207  A    C  
ATOM    680  CD  ARG A 181      95.328  59.881 -23.574  1.00 11.79      A    C  
ANISOU  680  CD  ARG A 181     1777   1127   1576    -45   -189    277  A    C  
ATOM    681  NE  ARG A 181      94.507  58.673 -23.599  1.00 11.06      A    N  
ANISOU  681  NE  ARG A 181     1763   1064   1377   -180     -2    225  A    N  
ATOM    682  CZ  ARG A 181      93.944  58.124 -22.522  1.00 11.09      A    C  
ANISOU  682  CZ  ARG A 181     1809   1100   1305   -157   -194    167  A    C  
ATOM    683  NH1 ARG A 181      94.087  58.697 -21.332  1.00 11.58      A    N1+
ANISOU  683  NH1 ARG A 181     1794   1400   1206   -148   -235    -32  A    N1+
ATOM    684  NH2 ARG A 181      93.243  57.003 -22.635  1.00 12.39      A    N  
ANISOU  684  NH2 ARG A 181     2066   1118   1522   -169   -122    146  A    N  
ATOM    685  N  ACYS A 182      90.992  64.155 -23.837  0.62 16.73      A    N  
ANISOU  685  N  ACYS A 182     1825   1585   2945    127   -297   -109  A    N  
ATOM    686  N  BCYS A 182      91.006  64.170 -23.853  0.38 17.71      A    N  
ANISOU  686  N  BCYS A 182     1926   1753   3048     63   -159   -188  A    N  
ATOM    687  CA ACYS A 182      89.742  64.420 -23.135  0.62 19.40      A    C  
ANISOU  687  CA ACYS A 182     2178   1832   3362    108   -206   -145  A    C  
ATOM    688  CA BCYS A 182      89.765  64.527 -23.175  0.38 20.63      A    C  
ANISOU  688  CA BCYS A 182     2205   2136   3496     50    -88   -317  A    C  
ATOM    689  C  ACYS A 182      88.535  64.561 -24.063  0.62 22.76      A    C  
ANISOU  689  C  ACYS A 182     2628   2146   3872    347   -260     14  A    C  
ATOM    690  C  BCYS A 182      88.530  64.362 -24.044  0.38 23.36      A    C  
ANISOU  690  C  BCYS A 182     2612   2346   3919    265   -243   -259  A    C  
ATOM    691  O  ACYS A 182      87.447  64.902 -23.589  0.62 22.76      A    O  
ANISOU  691  O  ACYS A 182     2604   2039   4005    293    -67    202  A    O  
ATOM    692  O  BCYS A 182      87.417  64.320 -23.508  0.38 23.54      A    O  
ANISOU  692  O  BCYS A 182     2594   2327   4022    287   -153   -385  A    O  
ATOM    693  CB ACYS A 182      89.880  65.619 -22.190  0.62 19.39      A    C  
ANISOU  693  CB ACYS A 182     2309   1815   3245    128    -60   -120  A    C  
ATOM    694  CB BCYS A 182      89.819  65.980 -22.710  0.38 21.13      A    C  
ANISOU  694  CB BCYS A 182     2185   2338   3505     44    149   -395  A    C  
ATOM    695  SG ACYS A 182      89.938  67.211 -22.995  0.62 20.01      A    S  
ANISOU  695  SG ACYS A 182     2537   1968   3098    -11    -51    -66  A    S  
ATOM    696  SG BCYS A 182      90.581  66.199 -21.115  0.38 22.17      A    S  
ANISOU  696  SG BCYS A 182     2218   2705   3502    -44    246   -486  A    S  
ATOM    697  N   SER A 183      88.698  64.292 -25.361  1.00 25.43      A    N  
ANISOU  697  N   SER A 183     2888   2580   4195    441   -484    -35  A    N  
ATOM    698  CA  SER A 183      87.569  64.223 -26.300  1.00 30.07      A    C  
ANISOU  698  CA  SER A 183     3470   3090   4863     -7   -611    144  A    C  
ATOM    699  C   SER A 183      86.718  65.493 -26.275  1.00 30.88      A    C  
ANISOU  699  C   SER A 183     3332   3359   5041   -119   -682    380  A    C  
ATOM    700  O   SER A 183      85.487  65.443 -26.300  1.00 31.44      A    O  
ANISOU  700  O   SER A 183     3265   3412   5269   -291   -631    662  A    O  
ATOM    701  CB  SER A 183      86.716  62.963 -26.105  1.00 33.19      A    C  
ANISOU  701  CB  SER A 183     4126   3236   5249     -3   -510    136  A    C  
ATOM    702  OG  SER A 183      87.472  61.783 -26.329  1.00 34.99      A    O  
ANISOU  702  OG  SER A 183     4525   3293   5478   -100   -399    123  A    O  
ATOM    703  N   ASP A 184      87.380  66.648 -26.210  1.00 29.57      A    N  
ANISOU  703  N   ASP A 184     3135   3178   4921   -204   -690    412  A    N  
ATOM    704  CA  ASP A 184      86.714  67.941 -26.303  1.00 29.09      A    C  
ANISOU  704  CA  ASP A 184     2978   3269   4805    -89   -614    410  A    C  
ATOM    705  C   ASP A 184      86.782  68.516 -27.713  1.00 29.85      A    C  
ANISOU  705  C   ASP A 184     3182   3338   4822    122   -618    486  A    C  
ATOM    706  O   ASP A 184      86.817  69.739 -27.890  1.00 27.80      A    O  
ANISOU  706  O   ASP A 184     2812   2942   4808    -69   -446    597  A    O  
ATOM    707  CB  ASP A 184      87.275  68.925 -25.277  1.00 27.31      A    C  
ANISOU  707  CB  ASP A 184     2619   3113   4646   -168   -537    427  A    C  
ATOM    708  CG  ASP A 184      88.771  69.145 -25.428  1.00 25.30      A    C  
ANISOU  708  CG  ASP A 184     2298   2856   4460   -240   -526    482  A    C  
ATOM    709  OD1 ASP A 184      89.358  68.658 -26.415  1.00 23.71      A    O  
ANISOU  709  OD1 ASP A 184     2189   2510   4309   -228   -618    592  A    O  
ATOM    710  OD2 ASP A 184      89.360  69.809 -24.551  1.00 25.29      A    O1-
ANISOU  710  OD2 ASP A 184     2217   3007   4387   -276   -351    355  A    O1-
ATOM    711  N   SER A 185      86.814  67.645 -28.718  1.00 33.17      A    N  
ANISOU  711  N   SER A 185     3924   3847   4831    417   -670    436  A    N  
ATOM    712  CA  SER A 185      86.943  68.077 -30.100  1.00 35.93      A    C  
ANISOU  712  CA  SER A 185     4473   4349   4829    501   -634    364  A    C  
ATOM    713  C   SER A 185      85.763  68.948 -30.512  1.00 35.65      A    C  
ANISOU  713  C   SER A 185     4300   4477   4768    234   -756    410  A    C  
ATOM    714  O   SER A 185      84.626  68.736 -30.082  1.00 36.26      A    O  
ANISOU  714  O   SER A 185     4371   4578   4829    210   -785    450  A    O  
ATOM    715  CB  SER A 185      87.001  66.847 -31.007  1.00 38.21      A    C  
ANISOU  715  CB  SER A 185     4996   4632   4889    645   -591    314  A    C  
ATOM    716  OG  SER A 185      86.750  67.191 -32.356  1.00 39.82      A    O  
ANISOU  716  OG  SER A 185     5313   4883   4934    726   -515    292  A    O  
ATOM    717  N   ASP A 186      86.046  69.943 -31.348  1.00 34.38      A    N  
ANISOU  717  N   ASP A 186     4036   4394   4633    -35   -983    441  A    N  
ATOM    718  CA  ASP A 186      85.010  70.713 -32.019  1.00 34.34      A    C  
ANISOU  718  CA  ASP A 186     4056   4410   4584   -320   -981    441  A    C  
ATOM    719  C   ASP A 186      84.682  70.159 -33.398  1.00 33.89      A    C  
ANISOU  719  C   ASP A 186     3820   4595   4460   -466  -1228    378  A    C  
ATOM    720  O   ASP A 186      83.908  70.778 -34.135  1.00 34.86      A    O  
ANISOU  720  O   ASP A 186     3918   4785   4544   -286  -1349    497  A    O  
ATOM    721  CB  ASP A 186      85.411  72.190 -32.113  1.00 34.45      A    C  
ANISOU  721  CB  ASP A 186     4256   4260   4575   -468   -868    542  A    C  
ATOM    722  CG  ASP A 186      86.720  72.403 -32.859  1.00 33.62      A    C  
ANISOU  722  CG  ASP A 186     4271   3998   4503   -681   -844    593  A    C  
ATOM    723  OD1 ASP A 186      87.260  71.441 -33.444  1.00 32.53      A    O  
ANISOU  723  OD1 ASP A 186     4208   3695   4457   -724   -930    568  A    O  
ATOM    724  OD2 ASP A 186      87.214  73.549 -32.861  1.00 33.77      A    O1-
ANISOU  724  OD2 ASP A 186     4452   3897   4484   -752   -646    637  A    O1-
ATOM    725  N   GLY A 187      85.258  69.014 -33.761  1.00 32.75      A    N  
ANISOU  725  N   GLY A 187     3625   4574   4246   -753  -1294    219  A    N  
ATOM    726  CA  GLY A 187      85.054  68.425 -35.066  1.00 32.18      A    C  
ANISOU  726  CA  GLY A 187     3717   4522   3988   -868  -1368    109  A    C  
ATOM    727  C   GLY A 187      86.033  68.872 -36.130  1.00 31.16      A    C  
ANISOU  727  C   GLY A 187     3856   4271   3711   -875  -1367     12  A    C  
ATOM    728  O   GLY A 187      85.999  68.333 -37.245  1.00 33.15      A    O  
ANISOU  728  O   GLY A 187     4286   4487   3821   -959  -1249    -31  A    O  
ATOM    729  N   LEU A 188      86.893  69.831 -35.832  1.00 28.33      A    N  
ANISOU  729  N   LEU A 188     3585   3800   3379   -644  -1482    -70  A    N  
ATOM    730  CA  LEU A 188      87.855  70.351 -36.797  1.00 25.88      A    C  
ANISOU  730  CA  LEU A 188     3651   3212   2971   -577  -1387     14  A    C  
ATOM    731  C   LEU A 188      89.277  70.405 -36.254  1.00 21.61      A    C  
ANISOU  731  C   LEU A 188     3285   2464   2463   -679  -1032   -101  A    C  
ATOM    732  O   LEU A 188      90.213  70.005 -36.951  1.00 21.68      A    O  
ANISOU  732  O   LEU A 188     3355   2494   2389   -773   -877   -194  A    O  
ATOM    733  CB  LEU A 188      87.403  71.745 -37.274  1.00 28.91      A    C  
ANISOU  733  CB  LEU A 188     4107   3659   3219   -291  -1417    147  A    C  
ATOM    734  CG  LEU A 188      88.184  72.406 -38.410  1.00 31.18      A    C  
ANISOU  734  CG  LEU A 188     4528   3844   3474   -275  -1220    180  A    C  
ATOM    735  CD1 LEU A 188      88.377  71.432 -39.567  1.00 32.18      A    C  
ANISOU  735  CD1 LEU A 188     4788   3898   3541   -392  -1037    101  A    C  
ATOM    736  CD2 LEU A 188      87.471  73.677 -38.887  1.00 31.19      A    C  
ANISOU  736  CD2 LEU A 188     4528   3809   3516   -187  -1277    295  A    C  
ATOM    737  N   ALA A 189      89.464  70.871 -35.026  1.00 17.45      A    N  
ANISOU  737  N   ALA A 189     2834   1800   1998   -425   -883   -154  A    N  
ATOM    738  CA  ALA A 189      90.806  70.950 -34.463  1.00 14.43      A    C  
ANISOU  738  CA  ALA A 189     2313   1362   1809   -252   -654   -116  A    C  
ATOM    739  C   ALA A 189      91.282  69.560 -34.056  1.00 13.93      A    C  
ANISOU  739  C   ALA A 189     2181   1342   1770   -259   -551    127  A    C  
ATOM    740  O   ALA A 189      90.550  68.839 -33.370  1.00 14.94      A    O  
ANISOU  740  O   ALA A 189     2347   1468   1862   -245   -516    224  A    O  
ATOM    741  CB  ALA A 189      90.805  71.846 -33.228  1.00 14.40      A    C  
ANISOU  741  CB  ALA A 189     2435   1391   1646   -120   -607   -179  A    C  
ATOM    742  N   PRO A 190      92.490  69.154 -34.442  1.00 13.53      A    N  
ANISOU  742  N   PRO A 190     2212   1262   1665   -105   -368    234  A    N  
ATOM    743  CA  PRO A 190      93.038  67.917 -33.903  1.00 12.94      A    C  
ANISOU  743  CA  PRO A 190     2024   1184   1708     65   -428    185  A    C  
ATOM    744  C   PRO A 190      93.176  68.032 -32.401  1.00 12.14      A    C  
ANISOU  744  C   PRO A 190     1785   1162   1667    -84   -363    125  A    C  
ATOM    745  O   PRO A 190      93.434  69.125 -31.864  1.00 11.62      A    O  
ANISOU  745  O   PRO A 190     1705   1086   1622     -8   -338     33  A    O  
ATOM    746  CB  PRO A 190      94.412  67.814 -34.579  1.00 14.46      A    C  
ANISOU  746  CB  PRO A 190     2189   1504   1801    138   -147    163  A    C  
ATOM    747  CG  PRO A 190      94.326  68.709 -35.781  1.00 13.99      A    C  
ANISOU  747  CG  PRO A 190     2112   1465   1739     95    -36    189  A    C  
ATOM    748  CD  PRO A 190      93.439  69.837 -35.336  1.00 13.65      A    C  
ANISOU  748  CD  PRO A 190     2157   1335   1694   -113   -146     85  A    C  
ATOM    749  N   PRO A 191      93.004  66.930 -31.676  1.00 12.00      A    N  
ANISOU  749  N   PRO A 191     1896    992   1669   -319   -431    242  A    N  
ATOM    750  CA  PRO A 191      93.021  67.006 -30.205  1.00 12.81      A    C  
ANISOU  750  CA  PRO A 191     1972   1204   1691   -294   -460    368  A    C  
ATOM    751  C   PRO A 191      94.364  67.407 -29.616  1.00 11.81      A    C  
ANISOU  751  C   PRO A 191     1844   1067   1577   -111   -426    191  A    C  
ATOM    752  O   PRO A 191      94.408  67.821 -28.451  1.00 12.27      A    O  
ANISOU  752  O   PRO A 191     1936   1107   1619   -100   -442    203  A    O  
ATOM    753  CB  PRO A 191      92.602  65.595 -29.772  1.00 15.91      A    C  
ANISOU  753  CB  PRO A 191     2598   1495   1953   -569   -325    422  A    C  
ATOM    754  CG  PRO A 191      92.872  64.733 -30.957  1.00 16.59      A    C  
ANISOU  754  CG  PRO A 191     2738   1474   2092   -504   -441    418  A    C  
ATOM    755  CD  PRO A 191      92.660  65.587 -32.168  1.00 13.94      A    C  
ANISOU  755  CD  PRO A 191     2299   1088   1910   -639   -587    246  A    C  
ATOM    756  N   GLN A 192      95.452  67.317 -30.381  1.00 11.19      A    N  
ANISOU  756  N   GLN A 192     1687    986   1579    -17   -440    273  A    N  
ATOM    757  CA  GLN A 192      96.766  67.699 -29.879  1.00 10.59      A    C  
ANISOU  757  CA  GLN A 192     1644    833   1549    267   -242    157  A    C  
ATOM    758  C   GLN A 192      97.019  69.202 -29.931  1.00  9.62      A    C  
ANISOU  758  C   GLN A 192     1497    819   1339    203   -148    132  A    C  
ATOM    759  O   GLN A 192      97.962  69.674 -29.282  1.00 10.70      A    O  
ANISOU  759  O   GLN A 192     1397   1261   1408    -86   -261    210  A    O  
ATOM    760  CB  GLN A 192      97.854  67.011 -30.704  1.00 11.36      A    C  
ANISOU  760  CB  GLN A 192     1832    832   1652     82   -100     51  A    C  
ATOM    761  CG  GLN A 192      97.762  65.482 -30.733  1.00 13.32      A    C  
ANISOU  761  CG  GLN A 192     2340    920   1802    154    -88   -142  A    C  
ATOM    762  CD  GLN A 192      96.996  64.957 -31.942  1.00 14.97      A    C  
ANISOU  762  CD  GLN A 192     2678   1193   1816    287    -57    -49  A    C  
ATOM    763  NE2 GLN A 192      97.440  63.825 -32.478  1.00 15.64      A    N  
ANISOU  763  NE2 GLN A 192     2884   1229   1829    125     86    -12  A    N  
ATOM    764  OE1 GLN A 192      96.024  65.567 -32.393  1.00 17.76      A    O  
ANISOU  764  OE1 GLN A 192     2913   1887   1947    333   -302   -343  A    O  
ATOM    765  N   HIS A 193      96.240  69.962 -30.709  1.00  9.22      A    N  
ANISOU  765  N   HIS A 193     1674    593   1235    156    -67    157  A    N  
ATOM    766  CA  HIS A 193      96.551  71.372 -30.938  1.00  8.77      A    C  
ANISOU  766  CA  HIS A 193     1559    659   1113     61   -196     29  A    C  
ATOM    767  C   HIS A 193      96.173  72.257 -29.757  1.00  8.38      A    C  
ANISOU  767  C   HIS A 193     1034   1028   1124     37   -117    -46  A    C  
ATOM    768  O   HIS A 193      95.028  72.246 -29.297  1.00 10.06      A    O  
ANISOU  768  O   HIS A 193     1097   1313   1413   -114     58    -79  A    O  
ATOM    769  CB  HIS A 193      95.832  71.869 -32.187  1.00  9.38      A    C  
ANISOU  769  CB  HIS A 193     1712    914    937    191   -125    154  A    C  
ATOM    770  CG  HIS A 193      96.500  71.467 -33.462  1.00  9.67      A    C  
ANISOU  770  CG  HIS A 193     1560   1123    991    105    -38    -22  A    C  
ATOM    771  CD2 HIS A 193      97.058  70.295 -33.844  1.00 11.12      A    C  
ANISOU  771  CD2 HIS A 193     1833   1266   1128    198    -73     17  A    C  
ATOM    772  ND1 HIS A 193      96.657  72.333 -34.524  1.00  9.84      A    N  
ANISOU  772  ND1 HIS A 193     1430   1236   1072     14    -52     82  A    N  
ATOM    773  CE1 HIS A 193      97.279  71.709 -35.508  1.00 10.45      A    C  
ANISOU  773  CE1 HIS A 193     1640   1289   1040    177    -95    -71  A    C  
ATOM    774  NE2 HIS A 193      97.531  70.470 -35.122  1.00 10.98      A    N  
ANISOU  774  NE2 HIS A 193     1836   1336   1000    223   -127    -86  A    N  
ATOM    775  N   LEU A 194      97.129  73.077 -29.313  1.00  8.29      A    N  
ANISOU  775  N   LEU A 194     1150    929   1069    162   -199   -114  A    N  
ATOM    776  CA  LEU A 194      96.869  74.011 -28.224  1.00  8.53      A    C  
ANISOU  776  CA  LEU A 194     1035   1102   1104    194   -103      4  A    C  
ATOM    777  C   LEU A 194      95.918  75.121 -28.652  1.00  8.68      A    C  
ANISOU  777  C   LEU A 194     1123   1067   1107    145    -82     13  A    C  
ATOM    778  O   LEU A 194      94.995  75.479 -27.909  1.00  9.15      A    O  
ANISOU  778  O   LEU A 194     1333   1006   1139    110    -41      6  A    O  
ATOM    779  CB  LEU A 194      98.186  74.617 -27.741  1.00  9.22      A    C  
ANISOU  779  CB  LEU A 194     1165   1195   1142    -59   -114   -157  A    C  
ATOM    780  CG  LEU A 194      98.038  75.688 -26.651  1.00 10.13      A    C  
ANISOU  780  CG  LEU A 194     1239   1473   1138   -183    150   -184  A    C  
ATOM    781  CD1 LEU A 194      97.580  75.087 -25.328  1.00 10.94      A    C  
ANISOU  781  CD1 LEU A 194     1260   1767   1128   -299     66     16  A    C  
ATOM    782  CD2 LEU A 194      99.323  76.470 -26.459  1.00 11.79      A    C  
ANISOU  782  CD2 LEU A 194     1454   1653   1372   -286     89   -242  A    C  
ATOM    783  N   ILE A 195      96.145  75.711 -29.828  1.00  8.28      A    N  
ANISOU  783  N   ILE A 195     1184    883   1077    123   -268      3  A    N  
ATOM    784  CA  ILE A 195      95.397  76.885 -30.272  1.00  8.49      A    C  
ANISOU  784  CA  ILE A 195     1212    864   1149     66   -259     29  A    C  
ATOM    785  C   ILE A 195      94.301  76.448 -31.231  1.00  8.22      A    C  
ANISOU  785  C   ILE A 195     1304    816   1003     96   -258    -42  A    C  
ATOM    786  O   ILE A 195      94.577  75.806 -32.256  1.00  9.87      A    O  
ANISOU  786  O   ILE A 195     1490   1150   1109     75   -115   -205  A    O  
ATOM    787  CB  ILE A 195      96.309  77.915 -30.958  1.00  8.75      A    C  
ANISOU  787  CB  ILE A 195     1167    939   1218    166   -213    145  A    C  
ATOM    788  CG1 ILE A 195      97.452  78.329 -30.032  1.00  9.88      A    C  
ANISOU  788  CG1 ILE A 195     1147   1161   1446    -14   -311    145  A    C  
ATOM    789  CG2 ILE A 195      95.494  79.120 -31.374  1.00 10.09      A    C  
ANISOU  789  CG2 ILE A 195     1364   1080   1392    176   -242     93  A    C  
ATOM    790  CD1 ILE A 195      98.408  79.318 -30.681  1.00 11.49      A    C  
ANISOU  790  CD1 ILE A 195     1388   1271   1705   -132   -310    293  A    C  
ATOM    791  N   ARG A 196      93.063  76.840 -30.927  1.00  8.98      A    N  
ANISOU  791  N   ARG A 196     1233    923   1256    290   -342     72  A    N  
ATOM    792  CA  ARG A 196      91.931  76.681 -31.827  1.00  9.86      A    C  
ANISOU  792  CA  ARG A 196     1389   1020   1339    142   -435    190  A    C  
ATOM    793  C   ARG A 196      91.390  78.042 -32.232  1.00  9.75      A    C  
ANISOU  793  C   ARG A 196     1414   1056   1233    106   -540   -116  A    C  
ATOM    794  O   ARG A 196      91.553  79.035 -31.519  1.00 10.42      A    O  
ANISOU  794  O   ARG A 196     1503   1162   1293    258   -490   -192  A    O  
ATOM    795  CB  ARG A 196      90.791  75.909 -31.167  1.00 10.02      A    C  
ANISOU  795  CB  ARG A 196     1385    909   1514    -94   -250    242  A    C  
ATOM    796  CG  ARG A 196      91.162  74.515 -30.776  1.00 11.15      A    C  
ANISOU  796  CG  ARG A 196     1514   1060   1662   -187   -311    321  A    C  
ATOM    797  CD  ARG A 196      89.977  73.786 -30.185  1.00 12.95      A    C  
ANISOU  797  CD  ARG A 196     1758   1242   1920   -197   -360    426  A    C  
ATOM    798  NE  ARG A 196      90.385  72.478 -29.698  1.00 13.28      A    N  
ANISOU  798  NE  ARG A 196     1752   1232   2064   -176   -480    489  A    N  
ATOM    799  CZ  ARG A 196      89.583  71.636 -29.063  1.00 15.32      A    C  
ANISOU  799  CZ  ARG A 196     1813   1749   2259   -308   -416    444  A    C  
ATOM    800  NH1 ARG A 196      88.316  71.961 -28.834  1.00 17.18      A    N1+
ANISOU  800  NH1 ARG A 196     2039   2143   2347   -147   -428    375  A    N1+
ATOM    801  NH2 ARG A 196      90.052  70.468 -28.656  1.00 15.89      A    N  
ANISOU  801  NH2 ARG A 196     1747   1822   2468   -303   -343    444  A    N  
ATOM    802  N   VAL A 197      90.736  78.073 -33.391  1.00 10.43      A    N  
ANISOU  802  N   VAL A 197     1513   1171   1278    154   -539     25  A    N  
ATOM    803  CA  VAL A 197      89.918  79.206 -33.798  1.00 10.39      A    C  
ANISOU  803  CA  VAL A 197     1490   1113   1343    225   -390     55  A    C  
ATOM    804  C   VAL A 197      88.466  78.837 -33.557  1.00 12.43      A    C  
ANISOU  804  C   VAL A 197     1719   1280   1725    -31   -339    -19  A    C  
ATOM    805  O   VAL A 197      88.008  77.769 -33.977  1.00 15.05      A    O  
ANISOU  805  O   VAL A 197     2040   1446   2233   -249   -292   -315  A    O  
ATOM    806  CB  VAL A 197      90.157  79.575 -35.273  1.00 10.90      A    C  
ANISOU  806  CB  VAL A 197     1450   1461   1231    281   -431    129  A    C  
ATOM    807  CG1 VAL A 197      89.105  80.572 -35.768  1.00 12.39      A    C  
ANISOU  807  CG1 VAL A 197     1682   1687   1340    612   -334    252  A    C  
ATOM    808  CG2 VAL A 197      91.538  80.165 -35.444  1.00 12.06      A    C  
ANISOU  808  CG2 VAL A 197     1414   1749   1419    110   -263    -73  A    C  
ATOM    809  N   GLU A 198      87.745  79.721 -32.892  1.00 12.36      A    N  
ANISOU  809  N   GLU A 198     1466   1447   1782     14   -221    -51  A    N  
ATOM    810  CA  GLU A 198      86.348  79.515 -32.563  1.00 14.84      A    C  
ANISOU  810  CA  GLU A 198     1738   1867   2033    -23    -97    -33  A    C  
ATOM    811  C   GLU A 198      85.468  80.136 -33.642  1.00 14.69      A    C  
ANISOU  811  C   GLU A 198     1571   1905   2107   -109    -74     87  A    C  
ATOM    812  O   GLU A 198      85.744  81.235 -34.129  1.00 15.61      A    O  
ANISOU  812  O   GLU A 198     1710   1959   2264    184    -99    483  A    O  
ATOM    813  CB  GLU A 198      86.082  80.211 -31.229  1.00 18.69      A    C  
ANISOU  813  CB  GLU A 198     2362   2440   2301    -48    289    -66  A    C  
ATOM    814  CG  GLU A 198      84.881  79.742 -30.501  1.00 21.05      A    C  
ANISOU  814  CG  GLU A 198     2729   2830   2438    255    184     24  A    C  
ATOM    815  CD  GLU A 198      84.780  80.362 -29.124  1.00 20.78      A    C  
ANISOU  815  CD  GLU A 198     2584   2766   2545    577    117     88  A    C  
ATOM    816  OE1 GLU A 198      85.655  81.182 -28.750  1.00 20.50      A    O  
ANISOU  816  OE1 GLU A 198     2200   3143   2447    793    182    225  A    O  
ATOM    817  OE2 GLU A 198      83.825  80.020 -28.417  1.00 22.62      A    O1-
ANISOU  817  OE2 GLU A 198     2768   2853   2973    479     85     44  A    O1-
ATOM    818  N   GLY A 199      84.414  79.419 -34.022  1.00 16.62      A    N  
ANISOU  818  N   GLY A 199     1778   2313   2226    -94    -86    -24  A    N  
ATOM    819  CA  GLY A 199      83.373  79.994 -34.854  1.00 18.40      A    C  
ANISOU  819  CA  GLY A 199     2238   2451   2302    -52   -124    143  A    C  
ATOM    820  C   GLY A 199      83.777  80.344 -36.269  1.00 19.41      A    C  
ANISOU  820  C   GLY A 199     2459   2575   2340    212   -375     62  A    C  
ATOM    821  O   GLY A 199      83.273  81.327 -36.822  1.00 22.20      A    O  
ANISOU  821  O   GLY A 199     2782   2978   2675    618   -507   -101  A    O  
ATOM    822  N   ASN A 200      84.666  79.566 -36.881  1.00 18.24      A    N  
ANISOU  822  N   ASN A 200     2391   2373   2167   -153   -415   -215  A    N  
ATOM    823  CA  ASN A 200      85.065  79.809 -38.267  1.00 17.22      A    C  
ANISOU  823  CA  ASN A 200     2199   2207   2136   -341   -557   -260  A    C  
ATOM    824  C   ASN A 200      85.242  78.455 -38.944  1.00 16.98      A    C  
ANISOU  824  C   ASN A 200     1906   2276   2272   -139   -628   -370  A    C  
ATOM    825  O   ASN A 200      86.262  77.785 -38.750  1.00 17.25      A    O  
ANISOU  825  O   ASN A 200     1859   2449   2247    -69   -696   -100  A    O  
ATOM    826  CB  ASN A 200      86.339  80.636 -38.350  1.00 17.53      A    C  
ANISOU  826  CB  ASN A 200     2487   2187   1985   -454   -418   -197  A    C  
ATOM    827  CG  ASN A 200      86.635  81.092 -39.765  1.00 18.37      A    C  
ANISOU  827  CG  ASN A 200     2788   2267   1925   -226   -447   -172  A    C  
ATOM    828  ND2 ASN A 200      87.359  82.190 -39.893  1.00 18.24      A    N  
ANISOU  828  ND2 ASN A 200     2617   2391   1923   -159   -293   -178  A    N  
ATOM    829  OD1 ASN A 200      86.197  80.467 -40.732  1.00 19.11      A    O  
ANISOU  829  OD1 ASN A 200     3067   2183   2012   -301   -620   -219  A    O  
ATOM    830  N   LEU A 201      84.259  78.075 -39.761  1.00 18.24      A    N  
ANISOU  830  N   LEU A 201     2116   2398   2418   -209   -664   -714  A    N  
ATOM    831  CA  LEU A 201      84.297  76.786 -40.432  1.00 19.50      A    C  
ANISOU  831  CA  LEU A 201     2151   2600   2658   -290   -772   -950  A    C  
ATOM    832  C   LEU A 201      85.383  76.704 -41.497  1.00 19.61      A    C  
ANISOU  832  C   LEU A 201     2210   2515   2724   -192   -858   -779  A    C  
ATOM    833  O   LEU A 201      85.665  75.605 -41.983  1.00 21.32      A    O  
ANISOU  833  O   LEU A 201     2667   2585   2847    -66   -818   -929  A    O  
ATOM    834  CB  LEU A 201      82.927  76.475 -41.046  1.00 23.16      A    C  
ANISOU  834  CB  LEU A 201     2569   3232   2999   -329   -604  -1099  A    C  
ATOM    835  CG  LEU A 201      81.751  76.416 -40.065  1.00 27.34      A    C  
ANISOU  835  CG  LEU A 201     3178   3890   3319   -238   -517   -896  A    C  
ATOM    836  CD1 LEU A 201      80.439  76.129 -40.781  1.00 27.91      A    C  
ANISOU  836  CD1 LEU A 201     3236   3988   3381   -209   -500   -999  A    C  
ATOM    837  CD2 LEU A 201      82.010  75.390 -38.965  1.00 29.20      A    C  
ANISOU  837  CD2 LEU A 201     3487   4183   3423   -194   -406   -793  A    C  
ATOM    838  N   ARG A 202      86.001  77.824 -41.868  1.00 18.06      A    N  
ANISOU  838  N   ARG A 202     1883   2391   2590   -100   -827   -430  A    N  
ATOM    839  CA  ARG A 202      87.085  77.813 -42.839  1.00 18.35      A    C  
ANISOU  839  CA  ARG A 202     2117   2371   2485    -15   -712    -40  A    C  
ATOM    840  C   ARG A 202      88.462  77.720 -42.197  1.00 16.47      A    C  
ANISOU  840  C   ARG A 202     2151   2040   2068   -136   -588   -157  A    C  
ATOM    841  O   ARG A 202      89.473  77.779 -42.907  1.00 17.28      A    O  
ANISOU  841  O   ARG A 202     2397   2103   2066    138   -573    -87  A    O  
ATOM    842  CB  ARG A 202      86.991  79.032 -43.762  1.00 21.15      A    C  
ANISOU  842  CB  ARG A 202     2289   2907   2838     82  -1079    378  A    C  
ATOM    843  CG  ARG A 202      85.760  78.982 -44.664  1.00 24.88      A    C  
ANISOU  843  CG  ARG A 202     2768   3399   3287     78  -1326    517  A    C  
ATOM    844  CD  ARG A 202      85.942  79.844 -45.895  1.00 28.97      A    C  
ANISOU  844  CD  ARG A 202     3507   3752   3747   -106  -1400    399  A    C  
ATOM    845  NE  ARG A 202      86.036  81.257 -45.549  1.00 32.00      A    N  
ANISOU  845  NE  ARG A 202     4007   4030   4122   -344  -1568    346  A    N  
ATOM    846  CZ  ARG A 202      86.457  82.204 -46.381  1.00 34.16      A    C  
ANISOU  846  CZ  ARG A 202     4398   4306   4277   -306  -1712    341  A    C  
ATOM    847  NH1 ARG A 202      86.840  81.889 -47.610  1.00 35.01      A    N1+
ANISOU  847  NH1 ARG A 202     4609   4416   4277   -346  -1853    303  A    N1+
ATOM    848  NH2 ARG A 202      86.507  83.467 -45.976  1.00 34.76      A    N  
ANISOU  848  NH2 ARG A 202     4477   4312   4417   -132  -1692    267  A    N  
ATOM    849  N   ALA A 203      88.534  77.568 -40.878  1.00 15.35      A    N  
ANISOU  849  N   ALA A 203     1974   1966   1894     -5   -615    -72  A    N  
ATOM    850  CA  ALA A 203      89.820  77.367 -40.235  1.00 14.20      A    C  
ANISOU  850  CA  ALA A 203     1793   1845   1757    243   -500   -140  A    C  
ATOM    851  C   ALA A 203      90.431  76.049 -40.693  1.00 14.58      A    C  
ANISOU  851  C   ALA A 203     1930   1659   1950    -32   -412   -222  A    C  
ATOM    852  O   ALA A 203      89.735  75.043 -40.854  1.00 16.64      A    O  
ANISOU  852  O   ALA A 203     2059   1886   2377   -221   -311   -342  A    O  
ATOM    853  CB  ALA A 203      89.632  77.334 -38.719  1.00 14.97      A    C  
ANISOU  853  CB  ALA A 203     1899   2158   1630    354   -266   -103  A    C  
ATOM    854  N   GLU A 204      91.742  76.064 -40.909  1.00 12.13      A    N  
ANISOU  854  N   GLU A 204     1706   1396   1508     69   -420    -92  A    N  
ATOM    855  CA AGLU A 204      92.490  74.877 -41.283  0.62 11.82      A    C  
ANISOU  855  CA AGLU A 204     1843   1283   1366     30   -441     55  A    C  
ATOM    856  CA BGLU A 204      92.511  74.893 -41.305  0.38 12.17      A    C  
ANISOU  856  CA BGLU A 204     1860   1352   1413     58   -328    -87  A    C  
ATOM    857  C   GLU A 204      93.603  74.656 -40.272  1.00 11.02      A    C  
ANISOU  857  C   GLU A 204     1771   1061   1356     38   -414   -165  A    C  
ATOM    858  O   GLU A 204      94.259  75.605 -39.826  1.00 11.92      A    O  
ANISOU  858  O   GLU A 204     2013   1073   1443     10   -419    -49  A    O  
ATOM    859  CB AGLU A 204      93.052  74.994 -42.708  0.62 13.89      A    C  
ANISOU  859  CB AGLU A 204     2156   1741   1381     27   -516    -40  A    C  
ATOM    860  CB BGLU A 204      93.158  75.109 -42.684  0.38 14.28      A    C  
ANISOU  860  CB BGLU A 204     2189   1780   1455     84   -173   -253  A    C  
ATOM    861  CG AGLU A 204      91.966  75.153 -43.768  0.62 15.79      A    C  
ANISOU  861  CG AGLU A 204     2451   2066   1483     30   -563    -18  A    C  
ATOM    862  CG BGLU A 204      94.155  74.030 -43.097  0.38 16.15      A    C  
ANISOU  862  CG BGLU A 204     2503   2083   1551     40    -12   -344  A    C  
ATOM    863  CD AGLU A 204      92.511  75.273 -45.179  0.62 18.27      A    C  
ANISOU  863  CD AGLU A 204     2903   2318   1721     70   -469   -111  A    C  
ATOM    864  CD BGLU A 204      95.061  74.461 -44.245  0.38 17.76      A    C  
ANISOU  864  CD BGLU A 204     2714   2376   1657    153     35   -586  A    C  
ATOM    865  OE1AGLU A 204      93.740  75.181 -45.361  0.62 19.26      A    O  
ANISOU  865  OE1AGLU A 204     3075   2386   1856   -123   -380   -193  A    O  
ATOM    866  OE1BGLU A 204      94.602  75.211 -45.127  0.38 18.42      A    O  
ANISOU  866  OE1BGLU A 204     2971   2301   1727     48     67   -604  A    O  
ATOM    867  OE2AGLU A 204      91.704  75.472 -46.108  0.62 20.08      A    O1-
ANISOU  867  OE2AGLU A 204     3217   2621   1791     46   -414   -119  A    O1-
ATOM    868  OE2BGLU A 204      96.240  74.057 -44.258  0.38 18.13      A    O1-
ANISOU  868  OE2BGLU A 204     2615   2585   1688    154    142   -594  A    O1-
ATOM    869  N   TYR A 205      93.793  73.401 -39.890  1.00 11.36      A    N  
ANISOU  869  N   TYR A 205     1922   1164   1231    129   -385     81  A    N  
ATOM    870  CA  TYR A 205      94.780  73.030 -38.892  1.00 11.42      A    C  
ANISOU  870  CA  TYR A 205     1841   1094   1402    108   -412      9  A    C  
ATOM    871  C   TYR A 205      95.901  72.276 -39.579  1.00 13.45      A    C  
ANISOU  871  C   TYR A 205     2007   1446   1659    147   -188   -335  A    C  
ATOM    872  O   TYR A 205      95.644  71.342 -40.345  1.00 16.19      A    O  
ANISOU  872  O   TYR A 205     2314   1792   2046     73   -202   -760  A    O  
ATOM    873  CB  TYR A 205      94.140  72.171 -37.806  1.00 10.83      A    C  
ANISOU  873  CB  TYR A 205     1738    996   1380    108   -317     85  A    C  
ATOM    874  CG  TYR A 205      93.196  72.978 -36.960  1.00 10.20      A    C  
ANISOU  874  CG  TYR A 205     1570   1006   1300    261   -313    -43  A    C  
ATOM    875  CD1 TYR A 205      91.886  73.197 -37.357  1.00 10.61      A    C  
ANISOU  875  CD1 TYR A 205     1562   1128   1342    188   -372   -124  A    C  
ATOM    876  CD2 TYR A 205      93.636  73.568 -35.776  1.00 10.70      A    C  
ANISOU  876  CD2 TYR A 205     1746    938   1383     52   -412    -26  A    C  
ATOM    877  CE1 TYR A 205      91.021  73.974 -36.588  1.00 10.63      A    C  
ANISOU  877  CE1 TYR A 205     1600   1154   1286    115   -281   -239  A    C  
ATOM    878  CE2 TYR A 205      92.789  74.327 -35.002  1.00 10.17      A    C  
ANISOU  878  CE2 TYR A 205     1553    878   1432     34   -376    -58  A    C  
ATOM    879  CZ  TYR A 205      91.482  74.538 -35.411  1.00 10.53      A    C  
ANISOU  879  CZ  TYR A 205     1673    978   1352    -21   -250   -245  A    C  
ATOM    880  OH  TYR A 205      90.655  75.306 -34.615  1.00 12.03      A    O  
ANISOU  880  OH  TYR A 205     1880   1227   1466    198   -306   -364  A    O  
ATOM    881  N   LEU A 206      97.135  72.691 -39.321  1.00 12.51      A    N  
ANISOU  881  N   LEU A 206     1867   1444   1443    286     -4   -226  A    N  
ATOM    882  CA  LEU A 206      98.298  72.114 -39.977  1.00 12.75      A    C  
ANISOU  882  CA  LEU A 206     2118   1345   1383    410    -24    -44  A    C  
ATOM    883  C   LEU A 206      99.198  71.441 -38.956  1.00 12.48      A    C  
ANISOU  883  C   LEU A 206     2152   1235   1354    315    -44   -195  A    C  
ATOM    884  O   LEU A 206      99.503  72.028 -37.911  1.00 11.57      A    O  
ANISOU  884  O   LEU A 206     1996   1104   1295    302    -71   -121  A    O  
ATOM    885  CB  LEU A 206      99.106  73.205 -40.691  1.00 14.25      A    C  
ANISOU  885  CB  LEU A 206     2460   1476   1478    231    173    -75  A    C  
ATOM    886  CG  LEU A 206     100.436  72.739 -41.304  1.00 16.97      A    C  
ANISOU  886  CG  LEU A 206     2894   1951   1602    226    229   -235  A    C  
ATOM    887  CD1 LEU A 206     100.211  71.724 -42.428  1.00 18.14      A    C  
ANISOU  887  CD1 LEU A 206     3124   2204   1562    195    293   -399  A    C  
ATOM    888  CD2 LEU A 206     101.264  73.927 -41.810  1.00 18.05      A    C  
ANISOU  888  CD2 LEU A 206     2963   2197   1698    125    325     52  A    C  
ATOM    889  N   ASP A 207      99.577  70.197 -39.256  1.00 14.91      A    N  
ANISOU  889  N   ASP A 207     2592   1380   1691    466    118   -160  A    N  
ATOM    890  CA AASP A 207     100.715  69.541 -38.628  0.47 16.20      A    C  
ANISOU  890  CA AASP A 207     2760   1552   1843    515    273   -164  A    C  
ATOM    891  CA BASP A 207     100.711  69.523 -38.630  0.53 15.83      A    C  
ANISOU  891  CA BASP A 207     2706   1501   1807    508    240   -216  A    C  
ATOM    892  C   ASP A 207     101.840  69.575 -39.653  1.00 16.57      A    C  
ANISOU  892  C   ASP A 207     2680   1745   1873    518    329   -160  A    C  
ATOM    893  O   ASP A 207     101.775  68.896 -40.682  1.00 17.77      A    O  
ANISOU  893  O   ASP A 207     2848   2002   1900    518    312   -299  A    O  
ATOM    894  CB AASP A 207     100.371  68.105 -38.245  0.47 18.04      A    C  
ANISOU  894  CB AASP A 207     3165   1657   2033    277    340    -70  A    C  
ATOM    895  CB BASP A 207     100.388  68.058 -38.338  0.53 17.00      A    C  
ANISOU  895  CB BASP A 207     3015   1502   1943    244    251   -199  A    C  
ATOM    896  CG AASP A 207      99.541  68.024 -36.985  0.47 20.84      A    C  
ANISOU  896  CG AASP A 207     3685   1981   2250    -41    383    -49  A    C  
ATOM    897  CG BASP A 207      99.304  67.873 -37.292  0.53 19.13      A    C  
ANISOU  897  CG BASP A 207     3415   1750   2102    -87    247   -226  A    C  
ATOM    898  OD1AASP A 207      98.342  68.368 -37.040  0.47 21.23      A    O  
ANISOU  898  OD1AASP A 207     3767   1920   2378    -25    527   -160  A    O  
ATOM    899  OD1BASP A 207      99.211  68.687 -36.352  0.53 18.58      A    O  
ANISOU  899  OD1BASP A 207     3344   1630   2085    124    272   -248  A    O  
ATOM    900  OD2AASP A 207     100.089  67.604 -35.944  0.47 22.92      A    O1-
ANISOU  900  OD2AASP A 207     3995   2439   2273   -378    383      3  A    O1-
ATOM    901  OD2BASP A 207      98.555  66.875 -37.405  0.53 21.31      A    O1-
ANISOU  901  OD2BASP A 207     3747   2160   2189   -547    241   -343  A    O1-
ATOM    902  N   ASP A 208     102.860  70.380 -39.384  1.00 16.30      A    N  
ANISOU  902  N   ASP A 208     2526   1731   1936    395    397   -163  A    N  
ATOM    903  CA  ASP A 208     103.913  70.577 -40.371  1.00 18.30      A    C  
ANISOU  903  CA  ASP A 208     2808   2030   2114    453    482   -254  A    C  
ATOM    904  C   ASP A 208     104.673  69.278 -40.592  1.00 19.44      A    C  
ANISOU  904  C   ASP A 208     3032   2141   2214    619    463   -433  A    C  
ATOM    905  O   ASP A 208     105.135  68.646 -39.639  1.00 19.37      A    O  
ANISOU  905  O   ASP A 208     2896   2157   2306    868    346   -429  A    O  
ATOM    906  CB  ASP A 208     104.859  71.685 -39.911  1.00 20.06      A    C  
ANISOU  906  CB  ASP A 208     3096   2219   2307    398    526   -159  A    C  
ATOM    907  CG  ASP A 208     105.776  72.163 -41.020  1.00 22.28      A    C  
ANISOU  907  CG  ASP A 208     3346   2577   2541    461    637   -136  A    C  
ATOM    908  OD1 ASP A 208     106.728  71.435 -41.355  1.00 23.69      A    O  
ANISOU  908  OD1 ASP A 208     3584   2700   2717    665    604   -272  A    O  
ATOM    909  OD2 ASP A 208     105.548  73.268 -41.553  1.00 23.28      A    O1-
ANISOU  909  OD2 ASP A 208     3451   2769   2624    229    716   -105  A    O1-
ATOM    910  N   ARG A 209     104.795  68.869 -41.858  1.00 21.81      A    N  
ANISOU  910  N   ARG A 209     3354   2568   2364    767    524   -657  A    N  
ATOM    911  CA  ARG A 209     105.396  67.574 -42.158  1.00 25.33      A    C  
ANISOU  911  CA  ARG A 209     3923   2959   2742    933    446   -971  A    C  
ATOM    912  C   ARG A 209     106.890  67.531 -41.866  1.00 26.74      A    C  
ANISOU  912  C   ARG A 209     4013   3135   3012   1232    686  -1099  A    C  
ATOM    913  O   ARG A 209     107.447  66.438 -41.719  1.00 27.90      A    O  
ANISOU  913  O   ARG A 209     4075   3345   3182   1375    789  -1113  A    O  
ATOM    914  CB  ARG A 209     105.123  67.178 -43.612  1.00 27.07      A    C  
ANISOU  914  CB  ARG A 209     4268   3173   2842    920    397   -992  A    C  
ATOM    915  N   ASN A 210     107.550  68.685 -41.772  1.00 27.80      A    N  
ANISOU  915  N   ASN A 210     4063   3358   3143   1200    776   -973  A    N  
ATOM    916  CA  ASN A 210     108.981  68.739 -41.499  1.00 29.17      A    C  
ANISOU  916  CA  ASN A 210     4098   3588   3399   1097    649   -810  A    C  
ATOM    917  C   ASN A 210     109.313  69.137 -40.069  1.00 27.37      A    C  
ANISOU  917  C   ASN A 210     3551   3352   3496   1074    544   -758  A    C  
ATOM    918  O   ASN A 210     110.200  68.535 -39.458  1.00 27.82      A    O  
ANISOU  918  O   ASN A 210     3385   3484   3699   1225    508   -714  A    O  
ATOM    919  CB  ASN A 210     109.675  69.695 -42.472  1.00 32.33      A    C  
ANISOU  919  CB  ASN A 210     4694   4054   3534   1076    609   -721  A    C  
ATOM    920  CG  ASN A 210     109.556  69.237 -43.907  1.00 35.29      A    C  
ANISOU  920  CG  ASN A 210     5184   4518   3705   1146    560   -573  A    C  
ATOM    921  ND2 ASN A 210     109.918  67.984 -44.158  1.00 36.24      A    N  
ANISOU  921  ND2 ASN A 210     5364   4643   3762   1217    522   -545  A    N  
ATOM    922  OD1 ASN A 210     109.129  69.993 -44.780  1.00 36.89      A    O  
ANISOU  922  OD1 ASN A 210     5406   4799   3811   1053    499   -421  A    O  
ATOM    923  N   THR A 211     108.629  70.135 -39.514  1.00 23.93      A    N  
ANISOU  923  N   THR A 211     2910   2869   3314    972    686   -863  A    N  
ATOM    924  CA  THR A 211     108.925  70.593 -38.162  1.00 22.49      A    C  
ANISOU  924  CA  THR A 211     2584   2742   3219    777    455   -755  A    C  
ATOM    925  C   THR A 211     108.020  69.980 -37.108  1.00 21.24      A    C  
ANISOU  925  C   THR A 211     2437   2607   3026   1006    213   -779  A    C  
ATOM    926  O   THR A 211     108.327  70.090 -35.916  1.00 22.00      A    O  
ANISOU  926  O   THR A 211     2399   2930   3030   1183     -5   -552  A    O  
ATOM    927  CB  THR A 211     108.776  72.115 -38.063  1.00 22.90      A    C  
ANISOU  927  CB  THR A 211     2455   2876   3369    488    581   -475  A    C  
ATOM    928  CG2 THR A 211     109.512  72.806 -39.197  1.00 23.72      A    C  
ANISOU  928  CG2 THR A 211     2474   3069   3468    247    708   -384  A    C  
ATOM    929  OG1 THR A 211     107.387  72.457 -38.121  1.00 21.57      A    O  
ANISOU  929  OG1 THR A 211     2084   2765   3345    331    446   -390  A    O  
ATOM    930  N   PHE A 212     106.905  69.375 -37.512  1.00 19.44      A    N  
ANISOU  930  N   PHE A 212     2257   2274   2856    995    115   -768  A    N  
ATOM    931  CA  PHE A 212     105.901  68.801 -36.622  1.00 18.47      A    C  
ANISOU  931  CA  PHE A 212     2255   1992   2770   1087    133   -642  A    C  
ATOM    932  C   PHE A 212     105.177  69.843 -35.784  1.00 15.69      A    C  
ANISOU  932  C   PHE A 212     1927   1685   2349    817    -24   -538  A    C  
ATOM    933  O   PHE A 212     104.393  69.487 -34.897  1.00 15.62      A    O  
ANISOU  933  O   PHE A 212     2057   1645   2235    623     90   -337  A    O  
ATOM    934  CB  PHE A 212     106.465  67.674 -35.749  1.00 21.64      A    C  
ANISOU  934  CB  PHE A 212     2661   2288   3272   1350    245   -535  A    C  
ATOM    935  CG  PHE A 212     107.235  66.656 -36.528  1.00 25.86      A    C  
ANISOU  935  CG  PHE A 212     3223   2835   3768   1505    398   -730  A    C  
ATOM    936  CD1 PHE A 212     106.574  65.758 -37.344  1.00 28.11      A    C  
ANISOU  936  CD1 PHE A 212     3620   3104   3957   1382    476   -912  A    C  
ATOM    937  CD2 PHE A 212     108.618  66.619 -36.475  1.00 28.29      A    C  
ANISOU  937  CD2 PHE A 212     3508   3157   4083   1638    559   -801  A    C  
ATOM    938  CE1 PHE A 212     107.272  64.826 -38.076  1.00 29.15      A    C  
ANISOU  938  CE1 PHE A 212     3672   3251   4152   1675    579   -994  A    C  
ATOM    939  CE2 PHE A 212     109.328  65.683 -37.206  1.00 29.84      A    C  
ANISOU  939  CE2 PHE A 212     3724   3365   4250   1666    560   -946  A    C  
ATOM    940  CZ  PHE A 212     108.653  64.790 -38.010  1.00 29.44      A    C  
ANISOU  940  CZ  PHE A 212     3619   3332   4237   1667    654  -1031  A    C  
ATOM    941  N   ARG A 213     105.386  71.122 -36.056  1.00 14.11      A    N  
ANISOU  941  N   ARG A 213     1644   1539   2179    587   -229   -488  A    N  
ATOM    942  CA  ARG A 213     104.690  72.147 -35.298  1.00 12.69      A    C  
ANISOU  942  CA  ARG A 213     1367   1412   2042    456    126   -304  A    C  
ATOM    943  C   ARG A 213     103.245  72.268 -35.749  1.00 11.69      A    C  
ANISOU  943  C   ARG A 213     1505   1224   1712    412     97   -129  A    C  
ATOM    944  O   ARG A 213     102.896  71.960 -36.893  1.00 12.80      A    O  
ANISOU  944  O   ARG A 213     1681   1578   1604    493    -16   -288  A    O  
ATOM    945  CB  ARG A 213     105.398  73.485 -35.450  1.00 14.12      A    C  
ANISOU  945  CB  ARG A 213     1358   1679   2329    394     83   -435  A    C  
ATOM    946  CG  ARG A 213     106.753  73.472 -34.800  1.00 15.60      A    C  
ANISOU  946  CG  ARG A 213     1428   2103   2396    245     92   -372  A    C  
ATOM    947  CD  ARG A 213     107.300  74.849 -34.723  1.00 15.73      A    C  
ANISOU  947  CD  ARG A 213     1578   2031   2369    159     51   -358  A    C  
ATOM    948  NE  ARG A 213     108.688  74.861 -34.301  1.00 15.57      A    N  
ANISOU  948  NE  ARG A 213     1791   1884   2240    320     64   -319  A    N  
ATOM    949  CZ  ARG A 213     109.077  74.998 -33.040  1.00 14.97      A    C  
ANISOU  949  CZ  ARG A 213     1630   1965   2093    541    181    -60  A    C  
ATOM    950  NH1 ARG A 213     108.169  75.106 -32.073  1.00 14.84      A    N1+
ANISOU  950  NH1 ARG A 213     1689   1830   2119    140    325    109  A    N1+
ATOM    951  NH2 ARG A 213     110.368  75.029 -32.751  1.00 16.11      A    N  
ANISOU  951  NH2 ARG A 213     1657   2316   2147    499    220    192  A    N  
ATOM    952  N   HIS A 214     102.403  72.714 -34.828  1.00  9.86      A    N  
ANISOU  952  N   HIS A 214     1292    955   1497    508     99     58  A    N  
ATOM    953  CA  HIS A 214     100.982  72.887 -35.078  1.00  9.80      A    C  
ANISOU  953  CA  HIS A 214     1420    974   1330    374     63    113  A    C  
ATOM    954  C   HIS A 214     100.694  74.344 -35.370  1.00  8.93      A    C  
ANISOU  954  C   HIS A 214     1341    908   1142    332    -31     48  A    C  
ATOM    955  O   HIS A 214     101.321  75.241 -34.803  1.00 10.01      A    O  
ANISOU  955  O   HIS A 214     1642    937   1226    136   -254    -86  A    O  
ATOM    956  CB  HIS A 214     100.177  72.509 -33.838  1.00 10.46      A    C  
ANISOU  956  CB  HIS A 214     1723    867   1387    264     53    176  A    C  
ATOM    957  CG  HIS A 214     100.452  71.133 -33.342  1.00 10.47      A    C  
ANISOU  957  CG  HIS A 214     1718    805   1455    270     -2    106  A    C  
ATOM    958  CD2 HIS A 214     101.006  70.056 -33.948  1.00 12.16      A    C  
ANISOU  958  CD2 HIS A 214     1957    978   1684    286     71    221  A    C  
ATOM    959  ND1 HIS A 214     100.118  70.732 -32.069  1.00 11.96      A    N  
ANISOU  959  ND1 HIS A 214     1897   1155   1492    126   -122    319  A    N  
ATOM    960  CE1 HIS A 214     100.464  69.468 -31.906  1.00 13.33      A    C  
ANISOU  960  CE1 HIS A 214     2243   1108   1713    107      7    327  A    C  
ATOM    961  NE2 HIS A 214     101.000  69.034 -33.032  1.00 13.34      A    N  
ANISOU  961  NE2 HIS A 214     2265   1061   1742    341    150    322  A    N  
ATOM    962  N   SER A 215      99.716  74.575 -36.238  1.00  8.57      A    N  
ANISOU  962  N   SER A 215     1387    836   1032    232   -141    154  A    N  
ATOM    963  CA  SER A 215      99.227  75.927 -36.432  1.00  8.43      A    C  
ANISOU  963  CA  SER A 215     1353    791   1060    415   -165    138  A    C  
ATOM    964  C   SER A 215      97.793  75.874 -36.931  1.00  8.75      A    C  
ANISOU  964  C   SER A 215     1351    877   1096    283    -70    -50  A    C  
ATOM    965  O   SER A 215      97.308  74.833 -37.390  1.00  9.40      A    O  
ANISOU  965  O   SER A 215     1512    920   1139    197   -155   -111  A    O  
ATOM    966  CB  SER A 215     100.124  76.709 -37.399  1.00 10.13      A    C  
ANISOU  966  CB  SER A 215     1733   1040   1076    120    254    -52  A    C  
ATOM    967  OG  SER A 215     100.196  76.062 -38.664  1.00 11.54      A    O  
ANISOU  967  OG  SER A 215     2132   1219   1032    284     32      8  A    O  
ATOM    968  N   VAL A 216      97.115  77.012 -36.834  1.00  8.78      A    N  
ANISOU  968  N   VAL A 216     1275    899   1161     53   -106     11  A    N  
ATOM    969  CA  VAL A 216      95.751  77.157 -37.327  1.00  8.98      A    C  
ANISOU  969  CA  VAL A 216     1364    959   1088    125   -123    144  A    C  
ATOM    970  C   VAL A 216      95.706  78.413 -38.180  1.00  8.27      A    C  
ANISOU  970  C   VAL A 216     1281    869    991     45   -142      6  A    C  
ATOM    971  O   VAL A 216      96.234  79.459 -37.783  1.00  8.82      A    O  
ANISOU  971  O   VAL A 216     1341    994   1015    -98   -187     32  A    O  
ATOM    972  CB  VAL A 216      94.705  77.165 -36.185  1.00  9.76      A    C  
ANISOU  972  CB  VAL A 216     1515   1095   1098    243   -268   -109  A    C  
ATOM    973  CG1 VAL A 216      94.998  78.244 -35.144  1.00 10.21      A    C  
ANISOU  973  CG1 VAL A 216     1584   1145   1149    147    -55   -239  A    C  
ATOM    974  CG2 VAL A 216      93.291  77.293 -36.745  1.00 10.05      A    C  
ANISOU  974  CG2 VAL A 216     1548   1186   1084    133   -306     60  A    C  
ATOM    975  N   VAL A 217      95.103  78.303 -39.360  1.00  8.36      A    N  
ANISOU  975  N   VAL A 217     1343    823   1010     -7   -251     48  A    N  
ATOM    976  CA  VAL A 217      95.138  79.372 -40.346  1.00  9.40      A    C  
ANISOU  976  CA  VAL A 217     1529   1065    977    169   -241    100  A    C  
ATOM    977  C   VAL A 217      93.722  79.615 -40.853  1.00  9.18      A    C  
ANISOU  977  C   VAL A 217     1360   1070   1056    117   -320    -67  A    C  
ATOM    978  O   VAL A 217      92.956  78.665 -41.062  1.00 10.99      A    O  
ANISOU  978  O   VAL A 217     1692   1213   1270    -43   -403     14  A    O  
ATOM    979  CB  VAL A 217      96.129  79.058 -41.495  1.00 11.21      A    C  
ANISOU  979  CB  VAL A 217     2204    930   1126    103    -40     -6  A    C  
ATOM    980  CG1 VAL A 217      95.757  77.764 -42.214  1.00 13.51      A    C  
ANISOU  980  CG1 VAL A 217     2569   1207   1356    187    139   -181  A    C  
ATOM    981  CG2 VAL A 217      96.208  80.225 -42.477  1.00 11.67      A    C  
ANISOU  981  CG2 VAL A 217     2250   1120   1062    108   -221    128  A    C  
ATOM    982  N   VAL A 218      93.366  80.887 -41.019  1.00  9.91      A    N  
ANISOU  982  N   VAL A 218     1456   1263   1045    500   -250    164  A    N  
ATOM    983  CA  VAL A 218      92.044  81.269 -41.519  1.00 11.43      A    C  
ANISOU  983  CA  VAL A 218     1749   1423   1170    380   -178    208  A    C  
ATOM    984  C   VAL A 218      92.190  82.237 -42.686  1.00 10.67      A    C  
ANISOU  984  C   VAL A 218     1648   1233   1174    279   -312    156  A    C  
ATOM    985  O   VAL A 218      93.163  83.001 -42.744  1.00 11.36      A    O  
ANISOU  985  O   VAL A 218     1700   1440   1175    125   -363    130  A    O  
ATOM    986  CB  VAL A 218      91.169  81.911 -40.431  1.00 13.97      A    C  
ANISOU  986  CB  VAL A 218     2246   1687   1373    213    146    165  A    C  
ATOM    987  CG1 VAL A 218      90.901  80.945 -39.298  1.00 15.86      A    C  
ANISOU  987  CG1 VAL A 218     2744   1844   1438    120    414    474  A    C  
ATOM    988  CG2 VAL A 218      91.804  83.190 -39.927  1.00 15.31      A    C  
ANISOU  988  CG2 VAL A 218     2407   1886   1522    224    124   -191  A    C  
ATOM    989  N   PRO A 219      91.238  82.261 -43.613  1.00 10.83      A    N  
ANISOU  989  N   PRO A 219     1593   1399   1121    129   -412      5  A    N  
ATOM    990  CA  PRO A 219      91.262  83.289 -44.659  1.00 12.04      A    C  
ANISOU  990  CA  PRO A 219     1964   1385   1225    186   -471     57  A    C  
ATOM    991  C   PRO A 219      91.012  84.663 -44.066  1.00 13.01      A    C  
ANISOU  991  C   PRO A 219     2160   1422   1360    400   -392    112  A    C  
ATOM    992  O   PRO A 219      90.222  84.822 -43.134  1.00 13.68      A    O  
ANISOU  992  O   PRO A 219     2158   1544   1497    358    -48    132  A    O  
ATOM    993  CB  PRO A 219      90.097  82.889 -45.574  1.00 14.03      A    C  
ANISOU  993  CB  PRO A 219     2244   1747   1341     16   -615     44  A    C  
ATOM    994  CG  PRO A 219      89.834  81.457 -45.260  1.00 15.01      A    C  
ANISOU  994  CG  PRO A 219     2463   1787   1453    163   -555    163  A    C  
ATOM    995  CD  PRO A 219      90.139  81.303 -43.804  1.00 12.94      A    C  
ANISOU  995  CD  PRO A 219     1958   1625   1333     57   -462      8  A    C  
ATOM    996  N   CYS A 220      91.685  85.664 -44.620  1.00 12.79      A    N  
ANISOU  996  N   CYS A 220     2217   1316   1325    238   -358     82  A    N  
ATOM    997  CA  CYS A 220      91.390  87.041 -44.251  1.00 14.54      A    C  
ANISOU  997  CA  CYS A 220     2442   1402   1682    372   -331    -59  A    C  
ATOM    998  C   CYS A 220      89.999  87.414 -44.728  1.00 16.62      A    C  
ANISOU  998  C   CYS A 220     2692   1526   2098    629   -559   -149  A    C  
ATOM    999  O   CYS A 220      89.614  87.119 -45.862  1.00 18.65      A    O  
ANISOU  999  O   CYS A 220     3165   1814   2108    528   -759    -71  A    O  
ATOM   1000  CB  CYS A 220      92.371  87.986 -44.926  1.00 14.01      A    C  
ANISOU 1000  CB  CYS A 220     2355   1403   1566    513   -289    -58  A    C  
ATOM   1001  SG  CYS A 220      94.049  87.812 -44.364  1.00 15.27      A    S  
ANISOU 1001  SG  CYS A 220     2710   1645   1448    397   -284   -271  A    S  
ATOM   1002  N   GLU A 221      89.250  88.090 -43.864  1.00 18.39      A    N  
ANISOU 1002  N   GLU A 221     2581   1738   2667    835   -631   -304  A    N  
ATOM   1003  CA  GLU A 221      87.965  88.626 -44.262  1.00 21.40      A    C  
ANISOU 1003  CA  GLU A 221     3005   1998   3128   1046   -575   -442  A    C  
ATOM   1004  C   GLU A 221      87.936  90.106 -43.913  1.00 20.23      A    C  
ANISOU 1004  C   GLU A 221     2734   2078   2875   1005   -576   -494  A    C  
ATOM   1005  O   GLU A 221      88.496  90.512 -42.887  1.00 18.83      A    O  
ANISOU 1005  O   GLU A 221     2442   1943   2768    684   -584   -496  A    O  
ATOM   1006  CB  GLU A 221      86.828  87.887 -43.550  1.00 26.03      A    C  
ANISOU 1006  CB  GLU A 221     3813   2377   3701    887   -365   -529  A    C  
ATOM   1007  CG  GLU A 221      86.727  86.425 -43.972  1.00 31.48      A    C  
ANISOU 1007  CG  GLU A 221     4684   3041   4235    813    -51   -490  A    C  
ATOM   1008  CD  GLU A 221      85.587  85.688 -43.297  1.00 36.81      A    C  
ANISOU 1008  CD  GLU A 221     5497   3817   4670    803    152   -412  A    C  
ATOM   1009  OE1 GLU A 221      85.539  84.444 -43.406  1.00 38.41      A    O  
ANISOU 1009  OE1 GLU A 221     5758   4030   4806    781     75   -299  A    O  
ATOM   1010  OE2 GLU A 221      84.740  86.351 -42.660  1.00 39.29      A    O1-
ANISOU 1010  OE2 GLU A 221     5830   4251   4848    647    301   -413  A    O1-
ATOM   1011  N   PRO A 222      87.334  90.936 -44.758  1.00 20.96      A    N  
ANISOU 1011  N   PRO A 222     2735   2440   2789    983   -556   -363  A    N  
ATOM   1012  CA APRO A 222      87.291  92.370 -44.480  0.63 20.98      A    C  
ANISOU 1012  CA APRO A 222     2712   2501   2758   1123   -456   -325  A    C  
ATOM   1013  CA BPRO A 222      87.286  92.371 -44.484  0.37 20.94      A    C  
ANISOU 1013  CA BPRO A 222     2698   2484   2775   1071   -453   -325  A    C  
ATOM   1014  C   PRO A 222      86.462  92.651 -43.241  1.00 20.16      A    C  
ANISOU 1014  C   PRO A 222     2523   2426   2713   1002   -402   -326  A    C  
ATOM   1015  O   PRO A 222      85.613  91.835 -42.852  1.00 19.88      A    O  
ANISOU 1015  O   PRO A 222     2486   2376   2692    976   -453   -284  A    O  
ATOM   1016  CB APRO A 222      86.618  92.948 -45.736  0.63 22.44      A    C  
ANISOU 1016  CB APRO A 222     2959   2706   2861   1122   -437   -275  A    C  
ATOM   1017  CB BPRO A 222      86.601  92.943 -45.736  0.37 22.03      A    C  
ANISOU 1017  CB BPRO A 222     2884   2615   2871   1064   -410   -289  A    C  
ATOM   1018  CG APRO A 222      85.803  91.830 -46.270  0.63 22.34      A    C  
ANISOU 1018  CG APRO A 222     2824   2796   2868   1072   -574   -323  A    C  
ATOM   1019  CG BPRO A 222      86.839  91.921 -46.800  0.37 22.15      A    C  
ANISOU 1019  CG BPRO A 222     2850   2668   2899    981   -454   -320  A    C  
ATOM   1020  CD APRO A 222      86.601  90.586 -45.987  0.63 21.95      A    C  
ANISOU 1020  CD APRO A 222     2797   2707   2836   1035   -615   -380  A    C  
ATOM   1021  CD BPRO A 222      86.793  90.605 -46.087  0.37 21.70      A    C  
ANISOU 1021  CD BPRO A 222     2784   2607   2854   1000   -540   -358  A    C  
ATOM   1022  N   PRO A 223      86.692  93.782 -42.582  1.00 18.99      A    N  
ANISOU 1022  N   PRO A 223     2289   2337   2589    835   -305   -274  A    N  
ATOM   1023  CA  PRO A 223      85.852  94.147 -41.436  1.00 19.22      A    C  
ANISOU 1023  CA  PRO A 223     2089   2470   2742    726   -215   -426  A    C  
ATOM   1024  C   PRO A 223      84.384  94.223 -41.831  1.00 20.48      A    C  
ANISOU 1024  C   PRO A 223     2149   2628   3003    720   -291   -363  A    C  
ATOM   1025  O   PRO A 223      84.037  94.524 -42.975  1.00 21.33      A    O  
ANISOU 1025  O   PRO A 223     2257   2765   3082    926   -317   -234  A    O  
ATOM   1026  CB  PRO A 223      86.386  95.527 -41.037  1.00 19.09      A    C  
ANISOU 1026  CB  PRO A 223     2167   2407   2681    713   -224   -198  A    C  
ATOM   1027  CG  PRO A 223      87.815  95.515 -41.491  1.00 19.33      A    C  
ANISOU 1027  CG  PRO A 223     2264   2449   2630    649   -266    -52  A    C  
ATOM   1028  CD  PRO A 223      87.827  94.700 -42.761  1.00 18.70      A    C  
ANISOU 1028  CD  PRO A 223     2175   2359   2572    682   -352    -75  A    C  
ATOM   1029  N   GLU A 224      83.518  93.929 -40.865  1.00 21.45      A    N  
ANISOU 1029  N   GLU A 224     2195   2698   3257    599   -158   -485  A    N  
ATOM   1030  CA  GLU A 224      82.095  94.131 -41.072  1.00 23.47      A    C  
ANISOU 1030  CA  GLU A 224     2352   3032   3532    633    -49   -403  A    C  
ATOM   1031  C   GLU A 224      81.823  95.610 -41.320  1.00 22.71      A    C  
ANISOU 1031  C   GLU A 224     2122   3139   3367    800    100   -332  A    C  
ATOM   1032  O   GLU A 224      82.583  96.489 -40.899  1.00 22.31      A    O  
ANISOU 1032  O   GLU A 224     2141   2987   3348    664    206   -269  A    O  
ATOM   1033  CB  GLU A 224      81.308  93.690 -39.837  1.00 28.40      A    C  
ANISOU 1033  CB  GLU A 224     3086   3576   4127    608    -63   -345  A    C  
ATOM   1034  CG  GLU A 224      81.645  92.293 -39.328  1.00 32.97      A    C  
ANISOU 1034  CG  GLU A 224     3718   4237   4572    543    -94   -369  A    C  
ATOM   1035  CD  GLU A 224      81.180  91.201 -40.267  1.00 36.91      A    C  
ANISOU 1035  CD  GLU A 224     4283   4810   4931    512   -239   -295  A    C  
ATOM   1036  OE1 GLU A 224      82.034  90.428 -40.759  1.00 38.24      A    O  
ANISOU 1036  OE1 GLU A 224     4552   4937   5043    505   -300   -296  A    O  
ATOM   1037  OE2 GLU A 224      79.959  91.121 -40.521  1.00 38.14      A    O1-
ANISOU 1037  OE2 GLU A 224     4413   5030   5048    485   -344   -214  A    O1-
ATOM   1038  N   VAL A 225      80.721  95.883 -42.020  1.00 23.01      A    N  
ANISOU 1038  N   VAL A 225     2113   3339   3290    972    147   -320  A    N  
ATOM   1039  CA  VAL A 225      80.339  97.263 -42.289  1.00 23.78      A    C  
ANISOU 1039  CA  VAL A 225     2323   3376   3335    912    190    -52  A    C  
ATOM   1040  C   VAL A 225      80.183  98.012 -40.974  1.00 22.75      A    C  
ANISOU 1040  C   VAL A 225     2323   2872   3449    769    299    151  A    C  
ATOM   1041  O   VAL A 225      79.456  97.577 -40.073  1.00 22.01      A    O  
ANISOU 1041  O   VAL A 225     2367   2624   3371    497    600    324  A    O  
ATOM   1042  CB  VAL A 225      79.055  97.302 -43.126  1.00 26.57      A    C  
ANISOU 1042  CB  VAL A 225     2821   3872   3403    998     61   -191  A    C  
ATOM   1043  CG1 VAL A 225      78.647  98.737 -43.385  1.00 26.97      A    C  
ANISOU 1043  CG1 VAL A 225     2952   3846   3449    983   -102   -131  A    C  
ATOM   1044  CG2 VAL A 225      79.250  96.537 -44.435  1.00 28.39      A    C  
ANISOU 1044  CG2 VAL A 225     3116   4202   3469    990      2   -232  A    C  
ATOM   1045  N   GLY A 226      80.876  99.144 -40.856  1.00 23.36      A    N  
ANISOU 1045  N   GLY A 226     2528   2719   3631    781    251    170  A    N  
ATOM   1046  CA  GLY A 226      80.887  99.926 -39.639  1.00 23.80      A    C  
ANISOU 1046  CA  GLY A 226     2737   2510   3795    633    173     87  A    C  
ATOM   1047  C   GLY A 226      82.065  99.657 -38.727  1.00 23.71      A    C  
ANISOU 1047  C   GLY A 226     2691   2473   3846    457    196   -215  A    C  
ATOM   1048  O   GLY A 226      82.232 100.371 -37.731  1.00 26.80      A    O  
ANISOU 1048  O   GLY A 226     3105   2888   4189    483     99   -590  A    O  
ATOM   1049  N   SER A 227      82.879  98.654 -39.029  1.00 20.31      A    N  
ANISOU 1049  N   SER A 227     2225   1922   3571    294    391     84  A    N  
ATOM   1050  CA  SER A 227      84.046  98.325 -38.228  1.00 20.63      A    C  
ANISOU 1050  CA  SER A 227     2376   2068   3396     42    426    150  A    C  
ATOM   1051  C   SER A 227      85.314  98.654 -39.001  1.00 19.19      A    C  
ANISOU 1051  C   SER A 227     2298   1773   3221    130    198    251  A    C  
ATOM   1052  O   SER A 227      85.325  98.710 -40.234  1.00 19.22      A    O  
ANISOU 1052  O   SER A 227     2245   1878   3181    126    114    125  A    O  
ATOM   1053  CB  SER A 227      84.045  96.846 -37.832  1.00 22.82      A    C  
ANISOU 1053  CB  SER A 227     2618   2620   3433   -185    689    264  A    C  
ATOM   1054  OG  SER A 227      82.922  96.546 -37.018  1.00 25.69      A    O  
ANISOU 1054  OG  SER A 227     2949   3231   3582   -422    644    341  A    O  
ATOM   1055  N   ASP A 228      86.391  98.883 -38.251  1.00 18.08      A    N  
ANISOU 1055  N   ASP A 228     2238   1502   3130    207    113    336  A    N  
ATOM   1056  CA  ASP A 228      87.664  99.264 -38.837  1.00 18.48      A    C  
ANISOU 1056  CA  ASP A 228     2426   1485   3111    286   -257    278  A    C  
ATOM   1057  C   ASP A 228      88.711  98.167 -38.765  1.00 16.98      A    C  
ANISOU 1057  C   ASP A 228     2345   1470   2637    158   -250    103  A    C  
ATOM   1058  O   ASP A 228      89.802  98.337 -39.319  1.00 18.02      A    O  
ANISOU 1058  O   ASP A 228     2529   1580   2739    179   -232     14  A    O  
ATOM   1059  CB  ASP A 228      88.199 100.535 -38.167  1.00 21.84      A    C  
ANISOU 1059  CB  ASP A 228     2945   1751   3602    607   -457    164  A    C  
ATOM   1060  CG  ASP A 228      87.359 101.754 -38.491  1.00 27.00      A    C  
ANISOU 1060  CG  ASP A 228     3782   2459   4017    630   -357     76  A    C  
ATOM   1061  OD1 ASP A 228      86.868 101.854 -39.638  1.00 28.35      A    O  
ANISOU 1061  OD1 ASP A 228     4011   2598   4163    580   -426    206  A    O  
ATOM   1062  OD2 ASP A 228      87.191 102.607 -37.599  1.00 30.37      A    O1-
ANISOU 1062  OD2 ASP A 228     4204   3072   4263    603   -201   -125  A    O1-
ATOM   1063  N   CYS A 229      88.411  97.054 -38.105  1.00 14.40      A    N  
ANISOU 1063  N   CYS A 229     2173   1161   2138    175   -277    164  A    N  
ATOM   1064  CA  CYS A 229      89.349  95.952 -38.006  1.00 13.34      A    C  
ANISOU 1064  CA  CYS A 229     2148   1094   1828     38   -242     96  A    C  
ATOM   1065  C   CYS A 229      88.561  94.655 -38.025  1.00 12.46      A    C  
ANISOU 1065  C   CYS A 229     1825   1129   1781    -85   -228    169  A    C  
ATOM   1066  O   CYS A 229      87.331  94.644 -37.950  1.00 14.87      A    O  
ANISOU 1066  O   CYS A 229     2049   1494   2106   -222   -303    167  A    O  
ATOM   1067  CB  CYS A 229      90.187  96.050 -36.724  1.00 13.86      A    C  
ANISOU 1067  CB  CYS A 229     2175   1485   1607     90   -324    116  A    C  
ATOM   1068  SG  CYS A 229      89.276  95.743 -35.189  1.00 16.57      A    S  
ANISOU 1068  SG  CYS A 229     2710   1889   1697     76   -185    -98  A    S  
ATOM   1069  N   THR A 230      89.285  93.556 -38.151  1.00 12.06      A    N  
ANISOU 1069  N   THR A 230     1854   1076   1654     40   -407    209  A    N  
ATOM   1070  CA ATHR A 230      88.678  92.240 -38.075  0.13 12.12      A    C  
ANISOU 1070  CA ATHR A 230     1925   1100   1580      8   -461    260  A    C  
ATOM   1071  CA BTHR A 230      88.720  92.216 -38.108  0.87 11.91      A    C  
ANISOU 1071  CA BTHR A 230     1993   1042   1491     48   -494    104  A    C  
ATOM   1072  C   THR A 230      89.199  91.526 -36.837  1.00 11.80      A    C  
ANISOU 1072  C   THR A 230     1796   1160   1526     57   -467    248  A    C  
ATOM   1073  O   THR A 230      90.330  91.746 -36.399  1.00 14.60      A    O  
ANISOU 1073  O   THR A 230     1934   1982   1632    -67   -391    399  A    O  
ATOM   1074  CB ATHR A 230      88.970  91.414 -39.331  0.13 12.82      A    C  
ANISOU 1074  CB ATHR A 230     2140   1146   1584    -23   -476    354  A    C  
ATOM   1075  CB BTHR A 230      89.152  91.442 -39.369  0.87 13.83      A    C  
ANISOU 1075  CB BTHR A 230     2505   1232   1519    353   -425     61  A    C  
ATOM   1076  CG2ATHR A 230      90.406  90.977 -39.339  0.13 12.71      A    C  
ANISOU 1076  CG2ATHR A 230     2161   1063   1604      2   -436    403  A    C  
ATOM   1077  CG2BTHR A 230      88.821  89.942 -39.286  0.87 14.26      A    C  
ANISOU 1077  CG2BTHR A 230     2492   1346   1582    520   -235    -94  A    C  
ATOM   1078  OG1ATHR A 230      88.125  90.256 -39.351  0.13 13.54      A    O  
ANISOU 1078  OG1ATHR A 230     2229   1325   1592    -53   -550    370  A    O  
ATOM   1079  OG1BTHR A 230      88.500  92.024 -40.508  0.87 15.87      A    O  
ANISOU 1079  OG1BTHR A 230     2749   1639   1644    644   -522    187  A    O  
ATOM   1080  N   THR A 231      88.339  90.706 -36.243  1.00 11.37      A    N  
ANISOU 1080  N   THR A 231     1705   1002   1612     76   -258    147  A    N  
ATOM   1081  CA  THR A 231      88.681  89.991 -35.021  1.00 12.21      A    C  
ANISOU 1081  CA  THR A 231     1747   1197   1695     72   -105    310  A    C  
ATOM   1082  C   THR A 231      88.655  88.491 -35.282  1.00 12.27      A    C  
ANISOU 1082  C   THR A 231     1670   1186   1807   -123   -328    211  A    C  
ATOM   1083  O   THR A 231      87.745  87.981 -35.950  1.00 15.18      A    O  
ANISOU 1083  O   THR A 231     2055   1496   2218   -240   -698    208  A    O  
ATOM   1084  CB  THR A 231      87.720  90.360 -33.881  1.00 15.17      A    C  
ANISOU 1084  CB  THR A 231     2098   1834   1832    250   -132    298  A    C  
ATOM   1085  CG2 THR A 231      88.078  89.617 -32.599  1.00 16.81      A    C  
ANISOU 1085  CG2 THR A 231     2198   2318   1872    349   -281    526  A    C  
ATOM   1086  OG1 THR A 231      87.804  91.767 -33.633  1.00 16.10      A    O  
ANISOU 1086  OG1 THR A 231     2093   2095   1928     79      8    -86  A    O  
ATOM   1087  N   ILE A 232      89.676  87.797 -34.789  1.00 10.92      A    N  
ANISOU 1087  N   ILE A 232     1477   1143   1531   -114   -163     94  A    N  
ATOM   1088  CA  ILE A 232      89.697  86.338 -34.748  1.00 10.78      A    C  
ANISOU 1088  CA  ILE A 232     1461   1128   1507   -101    -55    112  A    C  
ATOM   1089  C   ILE A 232      89.543  85.931 -33.291  1.00 10.38      A    C  
ANISOU 1089  C   ILE A 232     1393   1235   1316   -138   -271     84  A    C  
ATOM   1090  O   ILE A 232      90.152  86.538 -32.405  1.00 11.93      A    O  
ANISOU 1090  O   ILE A 232     1708   1462   1364   -580   -445    -60  A    O  
ATOM   1091  CB  ILE A 232      90.996  85.738 -35.333  1.00 11.86      A    C  
ANISOU 1091  CB  ILE A 232     1473   1434   1601    156     28    196  A    C  
ATOM   1092  CG1 ILE A 232      91.145  86.092 -36.812  1.00 15.21      A    C  
ANISOU 1092  CG1 ILE A 232     1924   2108   1747    115    251     57  A    C  
ATOM   1093  CG2 ILE A 232      91.014  84.210 -35.162  1.00 11.92      A    C  
ANISOU 1093  CG2 ILE A 232     1320   1402   1806    103    -55    -23  A    C  
ATOM   1094  CD1 ILE A 232      92.445  85.600 -37.416  1.00 16.91      A    C  
ANISOU 1094  CD1 ILE A 232     2163   2407   1854     69    276    -20  A    C  
ATOM   1095  N   HIS A 233      88.726  84.919 -33.037  1.00  9.37      A    N  
ANISOU 1095  N   HIS A 233     1202   1035   1324     19   -220     76  A    N  
ATOM   1096  CA  HIS A 233      88.509  84.428 -31.680  1.00  9.78      A    C  
ANISOU 1096  CA  HIS A 233     1035   1200   1481    128   -251    184  A    C  
ATOM   1097  C   HIS A 233      89.308  83.145 -31.491  1.00 10.22      A    C  
ANISOU 1097  C   HIS A 233     1244   1167   1472    139   -398    -11  A    C  
ATOM   1098  O   HIS A 233      89.006  82.123 -32.107  1.00 12.60      A    O  
ANISOU 1098  O   HIS A 233     1672   1293   1824    -17   -508   -216  A    O  
ATOM   1099  CB  HIS A 233      87.017  84.204 -31.444  1.00 12.19      A    C  
ANISOU 1099  CB  HIS A 233     1021   1709   1902    259   -205    283  A    C  
ATOM   1100  CG  HIS A 233      86.213  85.453 -31.591  1.00 15.65      A    C  
ANISOU 1100  CG  HIS A 233     1410   2182   2353    334   -360    338  A    C  
ATOM   1101  CD2 HIS A 233      86.054  86.515 -30.766  1.00 17.91      A    C  
ANISOU 1101  CD2 HIS A 233     1748   2370   2688    409   -422    315  A    C  
ATOM   1102  ND1 HIS A 233      85.497  85.743 -32.731  1.00 20.51      A    N  
ANISOU 1102  ND1 HIS A 233     2137   2855   2799    615   -579    287  A    N  
ATOM   1103  CE1 HIS A 233      84.910  86.918 -32.593  1.00 20.29      A    C  
ANISOU 1103  CE1 HIS A 233     1988   2787   2936    786   -435    352  A    C  
ATOM   1104  NE2 HIS A 233      85.234  87.409 -31.411  1.00 18.42      A    N  
ANISOU 1104  NE2 HIS A 233     1567   2611   2820    599   -383    287  A    N  
ATOM   1105  N   TYR A 234      90.321  83.197 -30.638  1.00  8.65      A    N  
ANISOU 1105  N   TYR A 234     1169    938   1182    156   -260     90  A    N  
ATOM   1106  CA  TYR A 234      91.155  82.041 -30.354  1.00  8.91      A    C  
ANISOU 1106  CA  TYR A 234     1217    944   1223    116    -83    115  A    C  
ATOM   1107  C   TYR A 234      90.768  81.408 -29.022  1.00  9.70      A    C  
ANISOU 1107  C   TYR A 234     1438   1040   1206    228   -180     41  A    C  
ATOM   1108  O   TYR A 234      90.217  82.059 -28.131  1.00 11.45      A    O  
ANISOU 1108  O   TYR A 234     1895   1143   1314    254    194    -22  A    O  
ATOM   1109  CB  TYR A 234      92.630  82.437 -30.319  1.00 10.09      A    C  
ANISOU 1109  CB  TYR A 234     1160   1443   1231     16    106     53  A    C  
ATOM   1110  CG  TYR A 234      93.212  82.827 -31.661  1.00  9.96      A    C  
ANISOU 1110  CG  TYR A 234     1326   1434   1025     74     36    -62  A    C  
ATOM   1111  CD1 TYR A 234      93.479  81.871 -32.640  1.00  9.96      A    C  
ANISOU 1111  CD1 TYR A 234     1346   1496    941    324     56   -129  A    C  
ATOM   1112  CD2 TYR A 234      93.517  84.151 -31.949  1.00 10.59      A    C  
ANISOU 1112  CD2 TYR A 234     1497   1378   1148    164     34   -287  A    C  
ATOM   1113  CE1 TYR A 234      94.023  82.230 -33.862  1.00 10.08      A    C  
ANISOU 1113  CE1 TYR A 234     1440   1406    982    444   -114   -161  A    C  
ATOM   1114  CE2 TYR A 234      94.059  84.515 -33.161  1.00 11.37      A    C  
ANISOU 1114  CE2 TYR A 234     1587   1580   1152    188    -13   -366  A    C  
ATOM   1115  CZ  TYR A 234      94.314  83.549 -34.118  1.00 10.25      A    C  
ANISOU 1115  CZ  TYR A 234     1465   1442    987    315    -84   -149  A    C  
ATOM   1116  OH  TYR A 234      94.858  83.896 -35.339  1.00 11.24      A    O  
ANISOU 1116  OH  TYR A 234     1759   1366   1145    217    -97     44  A    O  
ATOM   1117  N   ASN A 235      91.072  80.119 -28.896  1.00  9.84      A    N  
ANISOU 1117  N   ASN A 235     1423   1133   1184    351   -259     88  A    N  
ATOM   1118  CA  ASN A 235      90.956  79.395 -27.636  1.00 10.49      A    C  
ANISOU 1118  CA  ASN A 235     1390   1258   1336    196   -266    227  A    C  
ATOM   1119  C   ASN A 235      92.279  78.704 -27.378  1.00  9.37      A    C  
ANISOU 1119  C   ASN A 235     1260   1201   1097    321   -167     37  A    C  
ATOM   1120  O   ASN A 235      92.868  78.135 -28.303  1.00 11.57      A    O  
ANISOU 1120  O   ASN A 235     1614   1727   1056    493   -285   -246  A    O  
ATOM   1121  CB  ASN A 235      89.880  78.293 -27.699  1.00 13.34      A    C  
ANISOU 1121  CB  ASN A 235     1693   1447   1930    -15   -356     67  A    C  
ATOM   1122  CG  ASN A 235      88.479  78.838 -27.893  1.00 17.91      A    C  
ANISOU 1122  CG  ASN A 235     2268   1898   2640   -282   -300   -135  A    C  
ATOM   1123  ND2 ASN A 235      87.601  78.004 -28.426  1.00 20.78      A    N  
ANISOU 1123  ND2 ASN A 235     2579   2433   2882   -239   -377   -233  A    N  
ATOM   1124  OD1 ASN A 235      88.181  79.986 -27.548  1.00 19.79      A    O  
ANISOU 1124  OD1 ASN A 235     2475   2016   3028    -49   -312   -250  A    O  
ATOM   1125  N   TYR A 236      92.726  78.712 -26.118  1.00  8.59      A    N  
ANISOU 1125  N   TYR A 236     1028   1136   1100    122    -69    233  A    N  
ATOM   1126  CA  TYR A 236      93.910  77.966 -25.693  1.00  8.57      A    C  
ANISOU 1126  CA  TYR A 236     1225    927   1103     47   -197    241  A    C  
ATOM   1127  C   TYR A 236      93.454  76.783 -24.849  1.00  9.23      A    C  
ANISOU 1127  C   TYR A 236     1290   1078   1141    -37    -65    151  A    C  
ATOM   1128  O   TYR A 236      92.727  76.963 -23.866  1.00  9.36      A    O  
ANISOU 1128  O   TYR A 236     1236   1197   1124     67     33    169  A    O  
ATOM   1129  CB  TYR A 236      94.867  78.865 -24.901  1.00  9.06      A    C  
ANISOU 1129  CB  TYR A 236     1028   1173   1241   -336    -53     92  A    C  
ATOM   1130  CG  TYR A 236      95.494  79.934 -25.767  1.00  9.15      A    C  
ANISOU 1130  CG  TYR A 236      992   1186   1301    -40      2     41  A    C  
ATOM   1131  CD1 TYR A 236      94.816  81.124 -26.037  1.00  9.58      A    C  
ANISOU 1131  CD1 TYR A 236     1153   1135   1352    -16   -159    134  A    C  
ATOM   1132  CD2 TYR A 236      96.743  79.738 -26.355  1.00  9.79      A    C  
ANISOU 1132  CD2 TYR A 236     1110   1265   1345    -62     40    -94  A    C  
ATOM   1133  CE1 TYR A 236      95.376  82.096 -26.859  1.00 10.10      A    C  
ANISOU 1133  CE1 TYR A 236     1165   1319   1352   -331   -186    164  A    C  
ATOM   1134  CE2 TYR A 236      97.305  80.698 -27.176  1.00 10.35      A    C  
ANISOU 1134  CE2 TYR A 236     1367   1176   1390     47     19    -40  A    C  
ATOM   1135  CZ  TYR A 236      96.621  81.879 -27.418  1.00 10.56      A    C  
ANISOU 1135  CZ  TYR A 236     1320   1295   1397   -271    -50    174  A    C  
ATOM   1136  OH  TYR A 236      97.181  82.829 -28.236  1.00 11.94      A    O  
ANISOU 1136  OH  TYR A 236     1577   1552   1407   -400    -21    181  A    O  
ATOM   1137  N   MET A 237      93.892  75.578 -25.223  1.00  9.89      A    N  
ANISOU 1137  N   MET A 237     1387   1049   1323    109   -133     93  A    N  
ATOM   1138  CA  MET A 237      93.232  74.355 -24.772  1.00 10.12      A    C  
ANISOU 1138  CA  MET A 237     1467   1023   1356     60   -162    290  A    C  
ATOM   1139  C   MET A 237      93.996  73.575 -23.703  1.00 10.20      A    C  
ANISOU 1139  C   MET A 237     1424   1070   1380    132    -87    212  A    C  
ATOM   1140  O   MET A 237      93.640  72.423 -23.426  1.00 10.68      A    O  
ANISOU 1140  O   MET A 237     1367   1191   1500    -14   -226    220  A    O  
ATOM   1141  CB  MET A 237      92.904  73.467 -25.975  1.00 10.44      A    C  
ANISOU 1141  CB  MET A 237     1327   1084   1557    150   -385    199  A    C  
ATOM   1142  CG  MET A 237      92.065  74.169 -27.029  1.00 12.56      A    C  
ANISOU 1142  CG  MET A 237     1457   1523   1794     32   -407    266  A    C  
ATOM   1143  SD  MET A 237      90.475  74.722 -26.396  1.00 14.20      A    S  
ANISOU 1143  SD  MET A 237     1669   1512   2216    -76   -534    108  A    S  
ATOM   1144  CE  MET A 237      89.763  73.176 -25.797  1.00 14.84      A    C  
ANISOU 1144  CE  MET A 237     1552   1751   2335   -312   -216    134  A    C  
ATOM   1145  N   CYS A 238      95.021  74.175 -23.100  1.00  9.98      A    N  
ANISOU 1145  N   CYS A 238     1315   1261   1217     -5   -102      4  A    N  
ATOM   1146  CA  CYS A 238      95.717  73.645 -21.933  1.00 10.86      A    C  
ANISOU 1146  CA  CYS A 238     1534   1214   1377    243     -8     87  A    C  
ATOM   1147  C   CYS A 238      96.125  74.817 -21.062  1.00 11.54      A    C  
ANISOU 1147  C   CYS A 238     1711   1410   1262   -231   -240    176  A    C  
ATOM   1148  O   CYS A 238      96.312  75.933 -21.552  1.00 12.71      A    O  
ANISOU 1148  O   CYS A 238     2051   1447   1331   -330   -235    337  A    O  
ATOM   1149  CB  CYS A 238      97.032  72.971 -22.306  1.00 13.36      A    C  
ANISOU 1149  CB  CYS A 238     2095   1187   1796    721    188    381  A    C  
ATOM   1150  SG  CYS A 238      96.976  71.224 -22.471  1.00 16.40      A    S  
ANISOU 1150  SG  CYS A 238     2796   1392   2045    249    716    241  A    S  
ATOM   1151  N   TYR A 239      96.284  74.550 -19.767  1.00 10.70      A    N  
ANISOU 1151  N   TYR A 239     1380   1577   1111   -341   -295    181  A    N  
ATOM   1152  CA  TYR A 239      96.868  75.534 -18.866  1.00 10.84      A    C  
ANISOU 1152  CA  TYR A 239     1305   1637   1176   -301   -184    301  A    C  
ATOM   1153  C   TYR A 239      98.380  75.595 -19.041  1.00 10.83      A    C  
ANISOU 1153  C   TYR A 239     1447   1439   1231   -377   -211    188  A    C  
ATOM   1154  O   TYR A 239      99.033  74.593 -19.355  1.00 11.53      A    O  
ANISOU 1154  O   TYR A 239     1665   1428   1286   -208   -139     50  A    O  
ATOM   1155  CB  TYR A 239      96.601  75.152 -17.414  1.00 12.08      A    C  
ANISOU 1155  CB  TYR A 239     1359   1941   1289   -159   -126    543  A    C  
ATOM   1156  CG  TYR A 239      95.178  75.334 -16.964  1.00 13.50      A    C  
ANISOU 1156  CG  TYR A 239     1323   2209   1596   -258    -32    627  A    C  
ATOM   1157  CD1 TYR A 239      94.642  76.603 -16.804  1.00 15.19      A    C  
ANISOU 1157  CD1 TYR A 239     1418   2537   1818   -169   -177    546  A    C  
ATOM   1158  CD2 TYR A 239      94.377  74.237 -16.666  1.00 15.55      A    C  
ANISOU 1158  CD2 TYR A 239     1643   2486   1781   -204    -85    775  A    C  
ATOM   1159  CE1 TYR A 239      93.342  76.778 -16.374  1.00 16.48      A    C  
ANISOU 1159  CE1 TYR A 239     1541   2709   2012    -83     36    696  A    C  
ATOM   1160  CE2 TYR A 239      93.075  74.399 -16.233  1.00 17.42      A    C  
ANISOU 1160  CE2 TYR A 239     1835   2748   2036   -153     -4    802  A    C  
ATOM   1161  CZ  TYR A 239      92.561  75.673 -16.096  1.00 17.48      A    C  
ANISOU 1161  CZ  TYR A 239     1671   2831   2141    -54    182    830  A    C  
ATOM   1162  OH  TYR A 239      91.265  75.838 -15.665  1.00 20.78      A    O  
ANISOU 1162  OH  TYR A 239     2058   3398   2442   -226    239    850  A    O  
ATOM   1163  N   SER A 240      98.945  76.782 -18.790  1.00 10.41      A    N  
ANISOU 1163  N   SER A 240     1357   1343   1255   -352   -212    327  A    N  
ATOM   1164  CA  SER A 240     100.399  76.907 -18.777  1.00 10.05      A    C  
ANISOU 1164  CA  SER A 240     1512    978   1328   -191   -252    351  A    C  
ATOM   1165  C   SER A 240     101.039  75.907 -17.829  1.00 11.01      A    C  
ANISOU 1165  C   SER A 240     1640   1185   1360    -70   -162    358  A    C  
ATOM   1166  O   SER A 240     102.148  75.431 -18.091  1.00 12.89      A    O  
ANISOU 1166  O   SER A 240     1755   1621   1522    275   -213    175  A    O  
ATOM   1167  CB  SER A 240     100.797  78.331 -18.395  1.00 11.07      A    C  
ANISOU 1167  CB  SER A 240     1608   1111   1485   -242   -303    274  A    C  
ATOM   1168  OG  SER A 240     100.445  79.228 -19.435  1.00 11.53      A    O  
ANISOU 1168  OG  SER A 240     1471   1313   1598    -48   -270    307  A    O  
ATOM   1169  N   SER A 241     100.344  75.554 -16.745  1.00 11.52      A    N  
ANISOU 1169  N   SER A 241     1893   1196   1287   -148   -365    272  A    N  
ATOM   1170  CA  SER A 241     100.868  74.661 -15.722  1.00 12.36      A    C  
ANISOU 1170  CA  SER A 241     2112   1327   1256    -76   -178    173  A    C  
ATOM   1171  C   SER A 241     100.717  73.178 -16.047  1.00 13.77      A    C  
ANISOU 1171  C   SER A 241     2437   1300   1495    -29   -206    188  A    C  
ATOM   1172  O   SER A 241     101.184  72.355 -15.253  1.00 15.46      A    O  
ANISOU 1172  O   SER A 241     2842   1371   1660    119   -383    335  A    O  
ATOM   1173  CB  SER A 241     100.151  74.932 -14.399  1.00 14.40      A    C  
ANISOU 1173  CB  SER A 241     2173   1852   1444     64    101    213  A    C  
ATOM   1174  OG  SER A 241      98.768  74.610 -14.522  1.00 16.91      A    O  
ANISOU 1174  OG  SER A 241     2344   2329   1751    -49    267    107  A    O  
ATOM   1175  N   CYS A 242     100.087  72.801 -17.161  1.00 11.88      A    N  
ANISOU 1175  N   CYS A 242     1961   1078   1476   -160   -166     86  A    N  
ATOM   1176  CA  CYS A 242      99.758  71.386 -17.371  1.00 13.33      A    C  
ANISOU 1176  CA  CYS A 242     2341   1161   1562    -89    -41    192  A    C  
ATOM   1177  C   CYS A 242     101.005  70.503 -17.366  1.00 14.57      A    C  
ANISOU 1177  C   CYS A 242     2479   1358   1698   -132    -62    296  A    C  
ATOM   1178  O   CYS A 242     101.936  70.708 -18.153  1.00 14.60      A    O  
ANISOU 1178  O   CYS A 242     2248   1371   1927     48    -13    304  A    O  
ATOM   1179  CB  CYS A 242      98.981  71.188 -18.675  1.00 14.51      A    C  
ANISOU 1179  CB  CYS A 242     2295   1529   1689     20     35   -168  A    C  
ATOM   1180  SG  CYS A 242      97.179  71.493 -18.539  1.00 14.18      A    S  
ANISOU 1180  SG  CYS A 242     2150   1440   1797   -189    320   -198  A    S  
ATOM   1181  N   MET A 243     101.005  69.500 -16.493  1.00 16.54      A    N  
ANISOU 1181  N   MET A 243     2974   1397   1912    -95   -334    275  A    N  
ATOM   1182  CA  MET A 243     102.132  68.585 -16.404  1.00 18.61      A    C  
ANISOU 1182  CA  MET A 243     3279   1592   2202    231   -358    445  A    C  
ATOM   1183  C   MET A 243     102.238  67.738 -17.666  1.00 16.95      A    C  
ANISOU 1183  C   MET A 243     2828   1508   2107    239   -274    519  A    C  
ATOM   1184  O   MET A 243     101.232  67.291 -18.228  1.00 16.04      A    O  
ANISOU 1184  O   MET A 243     2621   1464   2009    171   -179    363  A    O  
ATOM   1185  CB  MET A 243     101.955  67.674 -15.191  1.00 24.43      A    C  
ANISOU 1185  CB  MET A 243     4173   2408   2699    442   -397    325  A    C  
ATOM   1186  CG  MET A 243     101.992  68.410 -13.870  1.00 31.45      A    C  
ANISOU 1186  CG  MET A 243     4923   3599   3428    475   -410     46  A    C  
ATOM   1187  SD  MET A 243     103.641  69.043 -13.508  1.00 38.97      A    S  
ANISOU 1187  SD  MET A 243     5818   4821   4169    290   -270   -273  A    S  
ATOM   1188  CE  MET A 243     104.473  67.525 -13.045  1.00 39.71      A    C  
ANISOU 1188  CE  MET A 243     5844   4976   4268    464   -299   -273  A    C  
ATOM   1189  N   GLY A 244     103.471  67.518 -18.115  1.00 17.26      A    N  
ANISOU 1189  N   GLY A 244     2654   1713   2192    220   -219    381  A    N  
ATOM   1190  CA  GLY A 244     103.705  66.800 -19.348  1.00 17.75      A    C  
ANISOU 1190  CA  GLY A 244     2679   1908   2158      0     17    354  A    C  
ATOM   1191  C   GLY A 244     103.386  67.574 -20.603  1.00 18.20      A    C  
ANISOU 1191  C   GLY A 244     2692   2030   2195   -153     95    219  A    C  
ATOM   1192  O   GLY A 244     103.566  67.036 -21.700  1.00 19.33      A    O  
ANISOU 1192  O   GLY A 244     2922   2180   2243   -376    208    -22  A    O  
ATOM   1193  N   GLY A 245     102.893  68.806 -20.475  1.00 16.55      A    N  
ANISOU 1193  N   GLY A 245     2452   1711   2124   -370     93    445  A    N  
ATOM   1194  CA  GLY A 245     102.682  69.691 -21.602  1.00 15.51      A    C  
ANISOU 1194  CA  GLY A 245     2226   1567   2099   -455     86    286  A    C  
ATOM   1195  C   GLY A 245     103.521  70.933 -21.409  1.00 14.54      A    C  
ANISOU 1195  C   GLY A 245     1997   1481   2047   -372    114    127  A    C  
ATOM   1196  O   GLY A 245     104.744  70.837 -21.266  1.00 15.10      A    O  
ANISOU 1196  O   GLY A 245     1856   1600   2281   -235    108    106  A    O  
ATOM   1197  N   MET A 246     102.888  72.104 -21.360  1.00 13.41      A    N  
ANISOU 1197  N   MET A 246     2055   1344   1698   -242    102    153  A    N  
ATOM   1198  CA  MET A 246     103.669  73.323 -21.174  1.00 12.91      A    C  
ANISOU 1198  CA  MET A 246     1894   1408   1605    -92    -74    253  A    C  
ATOM   1199  C   MET A 246     104.454  73.316 -19.866  1.00 13.37      A    C  
ANISOU 1199  C   MET A 246     1931   1456   1694     -1    -72    436  A    C  
ATOM   1200  O   MET A 246     105.556  73.867 -19.811  1.00 13.90      A    O  
ANISOU 1200  O   MET A 246     1770   1659   1850     29    -75    269  A    O  
ATOM   1201  CB  MET A 246     102.789  74.564 -21.318  1.00 12.65      A    C  
ANISOU 1201  CB  MET A 246     1810   1491   1507    114    -18    292  A    C  
ATOM   1202  CG  MET A 246     102.369  74.798 -22.762  1.00 13.08      A    C  
ANISOU 1202  CG  MET A 246     1828   1700   1440    -19     93    337  A    C  
ATOM   1203  SD  MET A 246     101.325  76.243 -23.025  1.00 13.43      A    S  
ANISOU 1203  SD  MET A 246     1684   1945   1474   -176   -192    300  A    S  
ATOM   1204  CE  MET A 246      99.739  75.649 -22.424  1.00 14.97      A    C  
ANISOU 1204  CE  MET A 246     1726   2453   1507   -393   -110    215  A    C  
ATOM   1205  N   ASN A 247     103.916  72.696 -18.811  1.00 13.66      A    N  
ANISOU 1205  N   ASN A 247     1941   1494   1756     37   -130    517  A    N  
ATOM   1206  CA  ASN A 247     104.684  72.423 -17.591  1.00 16.02      A    C  
ANISOU 1206  CA  ASN A 247     2060   1898   2131    204   -330    517  A    C  
ATOM   1207  C   ASN A 247     105.306  73.691 -17.004  1.00 15.05      A    C  
ANISOU 1207  C   ASN A 247     1968   1818   1934     25   -459    618  A    C  
ATOM   1208  O   ASN A 247     106.479  73.707 -16.621  1.00 16.21      A    O  
ANISOU 1208  O   ASN A 247     2193   1862   2104     32   -503    588  A    O  
ATOM   1209  CB  ASN A 247     105.739  71.332 -17.824  1.00 20.70      A    C  
ANISOU 1209  CB  ASN A 247     2693   2526   2646    418   -216    541  A    C  
ATOM   1210  CG  ASN A 247     106.311  70.780 -16.529  1.00 25.51      A    C  
ANISOU 1210  CG  ASN A 247     3472   3129   3093    536    -19    727  A    C  
ATOM   1211  ND2 ASN A 247     107.534  70.274 -16.595  1.00 27.48      A    N  
ANISOU 1211  ND2 ASN A 247     3630   3498   3314    554   -149    655  A    N  
ATOM   1212  OD1 ASN A 247     105.665  70.819 -15.483  1.00 27.95      A    O  
ANISOU 1212  OD1 ASN A 247     4044   3388   3187    406   -152   1015  A    O  
ATOM   1213  N   ARG A 248     104.515  74.764 -16.943  1.00 14.09      A    N  
ANISOU 1213  N   ARG A 248     1930   1759   1664   -109   -394    554  A    N  
ATOM   1214  CA  ARG A 248     104.848  76.070 -16.366  1.00 16.05      A    C  
ANISOU 1214  CA  ARG A 248     2278   2082   1740   -181   -655    359  A    C  
ATOM   1215  C   ARG A 248     105.759  76.910 -17.252  1.00 16.02      A    C  
ANISOU 1215  C   ARG A 248     2239   1883   1965   -342   -458    218  A    C  
ATOM   1216  O   ARG A 248     106.139  78.023 -16.847  1.00 18.84      A    O  
ANISOU 1216  O   ARG A 248     2898   2156   2106   -398   -310    -16  A    O  
ATOM   1217  CB  ARG A 248     105.425  76.005 -14.940  1.00 20.19      A    C  
ANISOU 1217  CB  ARG A 248     2830   2931   1910   -303   -732    417  A    C  
ATOM   1218  CG  ARG A 248     104.582  75.141 -14.031  1.00 23.94      A    C  
ANISOU 1218  CG  ARG A 248     3443   3633   2021   -193   -658    448  A    C  
ATOM   1219  CD  ARG A 248     104.839  75.423 -12.563  1.00 29.48      A    C  
ANISOU 1219  CD  ARG A 248     4190   4495   2515   -334   -340    469  A    C  
ATOM   1220  NE  ARG A 248     103.770  74.892 -11.741  1.00 35.41      A    N  
ANISOU 1220  NE  ARG A 248     5073   5246   3134    -95   -306    442  A    N  
ATOM   1221  CZ  ARG A 248     102.633  75.537 -11.507  1.00 39.38      A    C  
ANISOU 1221  CZ  ARG A 248     5597   5831   3533   -149   -105    434  A    C  
ATOM   1222  NH1 ARG A 248     102.390  76.738 -12.026  1.00 40.39      A    N1+
ANISOU 1222  NH1 ARG A 248     5772   5915   3660   -153    -84    350  A    N1+
ATOM   1223  NH2 ARG A 248     101.704  74.971 -10.741  1.00 40.75      A    N  
ANISOU 1223  NH2 ARG A 248     5767   6016   3699   -234      4    486  A    N  
ATOM   1224  N   ARG A 249     106.116  76.437 -18.430  1.00 14.05      A    N  
ANISOU 1224  N   ARG A 249     1819   1641   1878   -149   -464    335  A    N  
ATOM   1225  CA  ARG A 249     106.990  77.194 -19.321  1.00 13.95      A    C  
ANISOU 1225  CA  ARG A 249     1843   1457   2001   -103   -299    382  A    C  
ATOM   1226  C   ARG A 249     106.184  78.232 -20.093  1.00 14.03      A    C  
ANISOU 1226  C   ARG A 249     1959   1519   1852   -290   -416    244  A    C  
ATOM   1227  O   ARG A 249     105.155  77.893 -20.686  1.00 14.58      A    O  
ANISOU 1227  O   ARG A 249     1780   1717   2042    -97   -437    215  A    O  
ATOM   1228  CB  ARG A 249     107.671  76.259 -20.307  1.00 14.65      A    C  
ANISOU 1228  CB  ARG A 249     1837   1615   2114   -128   -389    340  A    C  
ATOM   1229  CG  ARG A 249     108.591  75.252 -19.647  1.00 15.76      A    C  
ANISOU 1229  CG  ARG A 249     1899   1737   2351   -210   -327    269  A    C  
ATOM   1230  CD  ARG A 249     109.133  74.270 -20.658  1.00 16.49      A    C  
ANISOU 1230  CD  ARG A 249     1887   1927   2453   -263   -278    166  A    C  
ATOM   1231  NE  ARG A 249     108.115  73.315 -21.081  1.00 16.34      A    N  
ANISOU 1231  NE  ARG A 249     1867   1867   2474   -160   -106    201  A    N  
ATOM   1232  CZ  ARG A 249     108.337  72.336 -21.948  1.00 15.22      A    C  
ANISOU 1232  CZ  ARG A 249     1650   1672   2460    159     54    330  A    C  
ATOM   1233  NH1 ARG A 249     109.546  72.179 -22.470  1.00 16.19      A    N1+
ANISOU 1233  NH1 ARG A 249     1645   1995   2510    371    343    279  A    N1+
ATOM   1234  NH2 ARG A 249     107.357  71.508 -22.283  1.00 15.19      A    N  
ANISOU 1234  NH2 ARG A 249     1675   1603   2492     90   -163    560  A    N  
ATOM   1235  N   PRO A 250     106.621  79.488 -20.121  1.00 13.19      A    N  
ANISOU 1235  N   PRO A 250     1887   1481   1645   -320   -399    124  A    N  
ATOM   1236  CA APRO A 250     105.892  80.494 -20.900  0.44 12.43      A    C  
ANISOU 1236  CA APRO A 250     1802   1385   1534    -42   -305    100  A    C  
ATOM   1237  CA BPRO A 250     105.905  80.504 -20.900  0.56 12.35      A    C  
ANISOU 1237  CA BPRO A 250     1806   1365   1522    -38   -289     77  A    C  
ATOM   1238  C   PRO A 250     105.962  80.211 -22.391  1.00 11.50      A    C  
ANISOU 1238  C   PRO A 250     1739   1215   1414    151   -214     13  A    C  
ATOM   1239  O   PRO A 250     106.945  79.669 -22.905  1.00 11.88      A    O  
ANISOU 1239  O   PRO A 250     1663   1443   1408    184   -300    101  A    O  
ATOM   1240  CB APRO A 250     106.616  81.800 -20.557  0.44 13.30      A    C  
ANISOU 1240  CB APRO A 250     1885   1535   1633    -65   -318     67  A    C  
ATOM   1241  CB BPRO A 250     106.672  81.791 -20.579  0.56 13.17      A    C  
ANISOU 1241  CB BPRO A 250     1886   1492   1626   -106   -253     -8  A    C  
ATOM   1242  CG APRO A 250     107.189  81.553 -19.205  0.44 13.42      A    C  
ANISOU 1242  CG APRO A 250     1938   1534   1627   -147   -388    123  A    C  
ATOM   1243  CG BPRO A 250     108.058  81.314 -20.243  0.56 13.17      A    C  
ANISOU 1243  CG BPRO A 250     1937   1451   1617   -288   -267     39  A    C  
ATOM   1244  CD APRO A 250     107.609  80.106 -19.219  0.44 13.66      A    C  
ANISOU 1244  CD APRO A 250     2010   1518   1664   -256   -437     82  A    C  
ATOM   1245  CD BPRO A 250     107.862  80.015 -19.522  0.56 13.72      A    C  
ANISOU 1245  CD BPRO A 250     1994   1555   1664   -361   -361     84  A    C  
ATOM   1246  N   ILE A 251     104.893  80.600 -23.086  1.00 10.72      A    N  
ANISOU 1246  N   ILE A 251     1698   1170   1205     44   -137     43  A    N  
ATOM   1247  CA  ILE A 251     104.808  80.479 -24.531  1.00  9.80      A    C  
ANISOU 1247  CA  ILE A 251     1484   1067   1174     42   -136    186  A    C  
ATOM   1248  C   ILE A 251     104.551  81.843 -25.150  1.00  9.14      A    C  
ANISOU 1248  C   ILE A 251     1169   1077   1228    136    -78      3  A    C  
ATOM   1249  O   ILE A 251     104.093  82.787 -24.495  1.00  9.78      A    O  
ANISOU 1249  O   ILE A 251     1274   1189   1253    159    -22    -49  A    O  
ATOM   1250  CB  ILE A 251     103.725  79.490 -25.012  1.00  9.98      A    C  
ANISOU 1250  CB  ILE A 251     1216   1148   1429     43     54      3  A    C  
ATOM   1251  CG1 ILE A 251     102.328  79.942 -24.556  1.00 11.47      A    C  
ANISOU 1251  CG1 ILE A 251     1378   1375   1605    -68    -63   -264  A    C  
ATOM   1252  CG2 ILE A 251     104.063  78.054 -24.594  1.00 11.05      A    C  
ANISOU 1252  CG2 ILE A 251     1584   1033   1581     50     -3    216  A    C  
ATOM   1253  CD1 ILE A 251     101.204  79.340 -25.384  1.00 12.46      A    C  
ANISOU 1253  CD1 ILE A 251     1599   1552   1584   -305   -138   -242  A    C  
ATOM   1254  N  ALEU A 252     104.908  81.947 -26.426  0.76  8.64      A    N  
ANISOU 1254  N  ALEU A 252      969   1201   1112    180   -287    180  A    N  
ATOM   1255  N  BLEU A 252     104.788  81.913 -26.458  0.24  9.13      A    N  
ANISOU 1255  N  BLEU A 252     1127   1147   1195    179   -125    101  A    N  
ATOM   1256  CA ALEU A 252     104.505  83.048 -27.287  0.76  9.98      A    C  
ANISOU 1256  CA ALEU A 252     1304   1261   1227   -257   -278    233  A    C  
ATOM   1257  CA BLEU A 252     104.517  83.095 -27.264  0.24  9.55      A    C  
ANISOU 1257  CA BLEU A 252     1173   1212   1243     97    -92    159  A    C  
ATOM   1258  C  ALEU A 252     103.538  82.507 -28.328  0.76  8.08      A    C  
ANISOU 1258  C  ALEU A 252     1081    863   1125    131   -192    149  A    C  
ATOM   1259  C  BLEU A 252     103.711  82.668 -28.482  0.24  8.71      A    C  
ANISOU 1259  C  BLEU A 252     1125   1035   1148    197    -36    162  A    C  
ATOM   1260  O  ALEU A 252     103.660  81.361 -28.765  0.76  9.19      A    O  
ANISOU 1260  O  ALEU A 252     1287    944   1259    107   -282     -9  A    O  
ATOM   1261  O  BLEU A 252     104.104  81.732 -29.186  0.24  8.60      A    O  
ANISOU 1261  O  BLEU A 252     1129    897   1240     64    127    199  A    O  
ATOM   1262  CB ALEU A 252     105.710  83.633 -28.043  0.76 13.91      A    C  
ANISOU 1262  CB ALEU A 252     1917   1744   1625   -573   -348    364  A    C  
ATOM   1263  CB BLEU A 252     105.840  83.725 -27.718  0.24 10.92      A    C  
ANISOU 1263  CB BLEU A 252     1285   1409   1455     91   -103    218  A    C  
ATOM   1264  CG ALEU A 252     106.941  84.029 -27.228  0.76 16.96      A    C  
ANISOU 1264  CG ALEU A 252     2205   2230   2009   -715   -176    127  A    C  
ATOM   1265  CG BLEU A 252     105.837  84.800 -28.803  0.24 11.20      A    C  
ANISOU 1265  CG BLEU A 252     1208   1486   1561    206     55    233  A    C  
ATOM   1266  CD1ALEU A 252     108.075  84.508 -28.126  0.76 19.35      A    C  
ANISOU 1266  CD1ALEU A 252     2435   2643   2275   -526     40    -54  A    C  
ATOM   1267  CD1BLEU A 252     106.006  86.169 -28.172  0.24 11.42      A    C  
ANISOU 1267  CD1BLEU A 252      994   1632   1712    172     50    142  A    C  
ATOM   1268  CD2ALEU A 252     106.577  85.098 -26.210  0.76 17.25      A    C  
ANISOU 1268  CD2ALEU A 252     2299   2155   2102   -635   -216      8  A    C  
ATOM   1269  CD2BLEU A 252     106.946  84.533 -29.805  0.24 10.52      A    C  
ANISOU 1269  CD2BLEU A 252     1168   1297   1532    411    238    471  A    C  
ATOM   1270  N   THR A 253     102.584  83.339 -28.727  1.00  8.35      A    N  
ANISOU 1270  N   THR A 253     1115   1082    976    269   -112    160  A    N  
ATOM   1271  CA  THR A 253     101.812  83.115 -29.941  1.00  8.84      A    C  
ANISOU 1271  CA  THR A 253     1203   1095   1061    226      4    257  A    C  
ATOM   1272  C   THR A 253     102.352  84.043 -31.015  1.00  8.92      A    C  
ANISOU 1272  C   THR A 253     1248    991   1150    275    -34    286  A    C  
ATOM   1273  O   THR A 253     102.514  85.245 -30.779  1.00  9.49      A    O  
ANISOU 1273  O   THR A 253     1452   1060   1093     89     11    -18  A    O  
ATOM   1274  CB  THR A 253     100.320  83.379 -29.731  1.00  9.34      A    C  
ANISOU 1274  CB  THR A 253     1266   1217   1065    119    -34    216  A    C  
ATOM   1275  CG2 THR A 253      99.544  83.175 -31.028  1.00 10.14      A    C  
ANISOU 1275  CG2 THR A 253     1456   1251   1145     -6   -149    253  A    C  
ATOM   1276  OG1 THR A 253      99.819  82.470 -28.754  1.00 10.47      A    O  
ANISOU 1276  OG1 THR A 253     1505   1504    969   -180    -62    352  A    O  
ATOM   1277  N   ILE A 254     102.663  83.473 -32.173  1.00  8.69      A    N  
ANISOU 1277  N   ILE A 254     1222   1045   1034    108     -4    186  A    N  
ATOM   1278  CA  ILE A 254     103.110  84.216 -33.347  1.00  8.85      A    C  
ANISOU 1278  CA  ILE A 254     1262   1091   1010    -29     98    140  A    C  
ATOM   1279  C   ILE A 254     101.962  84.234 -34.347  1.00  8.48      A    C  
ANISOU 1279  C   ILE A 254     1364    913    945   -118    -21    -16  A    C  
ATOM   1280  O   ILE A 254     101.444  83.176 -34.731  1.00  8.81      A    O  
ANISOU 1280  O   ILE A 254     1453    824   1072    -36    -35     16  A    O  
ATOM   1281  CB  ILE A 254     104.356  83.575 -33.970  1.00 10.59      A    C  
ANISOU 1281  CB  ILE A 254     1327   1442   1255     62    207     96  A    C  
ATOM   1282  CG1 ILE A 254     105.483  83.482 -32.941  1.00 12.39      A    C  
ANISOU 1282  CG1 ILE A 254     1329   1753   1625    485    146    214  A    C  
ATOM   1283  CG2 ILE A 254     104.809  84.363 -35.199  1.00 11.05      A    C  
ANISOU 1283  CG2 ILE A 254     1582   1388   1228   -168    315    307  A    C  
ATOM   1284  CD1 ILE A 254     106.594  82.541 -33.357  1.00 14.43      A    C  
ANISOU 1284  CD1 ILE A 254     1633   1955   1894    478    136    205  A    C  
ATOM   1285  N   ILE A 255     101.544  85.434 -34.748  1.00  8.12      A    N  
ANISOU 1285  N   ILE A 255     1288    970    828     55      4     60  A    N  
ATOM   1286  CA  ILE A 255     100.490  85.621 -35.740  1.00  8.75      A    C  
ANISOU 1286  CA  ILE A 255     1293   1110    921    138   -172     87  A    C  
ATOM   1287  C   ILE A 255     101.150  86.109 -37.016  1.00  9.33      A    C  
ANISOU 1287  C   ILE A 255     1459   1081   1004      4   -210    -57  A    C  
ATOM   1288  O   ILE A 255     101.819  87.153 -37.019  1.00 10.21      A    O  
ANISOU 1288  O   ILE A 255     1696   1145   1038    -37    -74   -100  A    O  
ATOM   1289  CB  ILE A 255      99.433  86.634 -35.275  1.00  9.97      A    C  
ANISOU 1289  CB  ILE A 255     1489   1337    962    130   -245    133  A    C  
ATOM   1290  CG1 ILE A 255      98.875  86.256 -33.900  1.00 10.97      A    C  
ANISOU 1290  CG1 ILE A 255     1663   1405   1098    -66   -100    222  A    C  
ATOM   1291  CG2 ILE A 255      98.336  86.769 -36.331  1.00 11.01      A    C  
ANISOU 1291  CG2 ILE A 255     1562   1492   1129     59   -424    233  A    C  
ATOM   1292  CD1 ILE A 255      98.149  84.966 -33.873  1.00 12.02      A    C  
ANISOU 1292  CD1 ILE A 255     1708   1570   1290    -66   -140     77  A    C  
ATOM   1293  N   THR A 256     100.961  85.372 -38.102  1.00  9.40      A    N  
ANISOU 1293  N   THR A 256     1425   1251    897     40    -12     23  A    N  
ATOM   1294  CA ATHR A 256     101.550  85.746 -39.377  0.69  9.69      A    C  
ANISOU 1294  CA ATHR A 256     1539   1168    975     11     45     89  A    C  
ATOM   1295  CA BTHR A 256     101.556  85.699 -39.388  0.31  9.47      A    C  
ANISOU 1295  CA BTHR A 256     1483   1152    963     39     21    130  A    C  
ATOM   1296  C   THR A 256     100.468  85.996 -40.414  1.00  9.69      A    C  
ANISOU 1296  C   THR A 256     1593   1106    982   -116    -37     80  A    C  
ATOM   1297  O   THR A 256      99.485  85.257 -40.513  1.00 11.62      A    O  
ANISOU 1297  O   THR A 256     1947   1160   1307   -263   -402    395  A    O  
ATOM   1298  CB ATHR A 256     102.556  84.721 -39.908  0.69 11.25      A    C  
ANISOU 1298  CB ATHR A 256     1742   1392   1139    -43     46     31  A    C  
ATOM   1299  CB BTHR A 256     102.395  84.522 -39.882  0.31 10.17      A    C  
ANISOU 1299  CB BTHR A 256     1540   1290   1036    164     48    217  A    C  
ATOM   1300  CG2ATHR A 256     103.865  84.789 -39.126  0.69 12.59      A    C  
ANISOU 1300  CG2ATHR A 256     1862   1713   1209   -220     42     89  A    C  
ATOM   1301  CG2BTHR A 256     103.146  84.908 -41.134  0.31  9.54      A    C  
ANISOU 1301  CG2BTHR A 256     1384   1270    972    237     72    347  A    C  
ATOM   1302  OG1ATHR A 256     101.995  83.409 -39.824  0.69 11.55      A    O  
ANISOU 1302  OG1ATHR A 256     1807   1288   1294   -108     39     71  A    O  
ATOM   1303  OG1BTHR A 256     103.329  84.136 -38.863  0.31 11.62      A    O  
ANISOU 1303  OG1BTHR A 256     1799   1413   1204    116      1    217  A    O  
ATOM   1304  N   LEU A 257     100.658  87.065 -41.170  1.00  9.37      A    N  
ANISOU 1304  N   LEU A 257     1706   1036    820    -17      4    136  A    N  
ATOM   1305  CA  LEU A 257      99.868  87.333 -42.358  1.00  9.75      A    C  
ANISOU 1305  CA  LEU A 257     1902   1095    707     39    -48    139  A    C  
ATOM   1306  C   LEU A 257     100.643  86.714 -43.514  1.00 10.58      A    C  
ANISOU 1306  C   LEU A 257     1930   1261    830     12     -4     40  A    C  
ATOM   1307  O   LEU A 257     101.840  86.966 -43.662  1.00 11.80      A    O  
ANISOU 1307  O   LEU A 257     2028   1565    889   -185    166     31  A    O  
ATOM   1308  CB  LEU A 257      99.741  88.845 -42.543  1.00 11.09      A    C  
ANISOU 1308  CB  LEU A 257     1963   1289    962     98     71    263  A    C  
ATOM   1309  CG  LEU A 257      98.770  89.326 -43.615  1.00 10.80      A    C  
ANISOU 1309  CG  LEU A 257     1845   1189   1070     20     84    168  A    C  
ATOM   1310  CD1 LEU A 257      97.333  89.079 -43.185  1.00 11.49      A    C  
ANISOU 1310  CD1 LEU A 257     1784   1461   1122     17    174     66  A    C  
ATOM   1311  CD2 LEU A 257      99.000  90.805 -43.930  1.00 11.91      A    C  
ANISOU 1311  CD2 LEU A 257     2158   1126   1241    -20     44    156  A    C  
ATOM   1312  N  AGLU A 258      99.978  85.879 -44.311  0.39 11.28      A    N  
ANISOU 1312  N  AGLU A 258     2072   1315    898    -32    -30    -30  A    N  
ATOM   1313  N  BGLU A 258      99.965  85.877 -44.305  0.61 10.97      A    N  
ANISOU 1313  N  BGLU A 258     2046   1263    860     -9   -140    -69  A    N  
ATOM   1314  CA AGLU A 258     100.679  85.134 -45.349  0.39 11.99      A    C  
ANISOU 1314  CA AGLU A 258     2205   1336   1017    158     71     -5  A    C  
ATOM   1315  CA BGLU A 258     100.607  85.082 -45.344  0.61 11.52      A    C  
ANISOU 1315  CA BGLU A 258     2175   1214    989    357    -91     -6  A    C  
ATOM   1316  C  AGLU A 258      99.895  85.163 -46.651  0.39 11.25      A    C  
ANISOU 1316  C  AGLU A 258     2032   1328    916     74    198      0  A    C  
ATOM   1317  C  BGLU A 258      99.881  85.260 -46.667  0.61 10.58      A    C  
ANISOU 1317  C  BGLU A 258     1927   1182    911    156    130   -116  A    C  
ATOM   1318  O  AGLU A 258      98.662  85.208 -46.651  0.39 11.36      A    O  
ANISOU 1318  O  AGLU A 258     1949   1437    931    -30    241    144  A    O  
ATOM   1319  O  BGLU A 258      98.669  85.481 -46.702  0.61 10.76      A    O  
ANISOU 1319  O  BGLU A 258     1912   1184    994    160    129    -84  A    O  
ATOM   1320  CB AGLU A 258     100.948  83.677 -44.935  0.39 13.81      A    C  
ANISOU 1320  CB AGLU A 258     2471   1533   1242    141    100     52  A    C  
ATOM   1321  CB BGLU A 258     100.545  83.578 -45.024  0.61 13.67      A    C  
ANISOU 1321  CB BGLU A 258     2495   1472   1227    442   -149    246  A    C  
ATOM   1322  CG AGLU A 258      99.707  82.902 -44.518  0.39 15.00      A    C  
ANISOU 1322  CG AGLU A 258     2540   1792   1367    161    154     76  A    C  
ATOM   1323  CG BGLU A 258     101.342  83.104 -43.818  0.61 15.11      A    C  
ANISOU 1323  CG BGLU A 258     2534   1772   1435    564   -230    381  A    C  
ATOM   1324  CD AGLU A 258     100.009  81.460 -44.147  0.39 16.14      A    C  
ANISOU 1324  CD AGLU A 258     2716   1973   1444    140     -2    156  A    C  
ATOM   1325  CD BGLU A 258     101.227  81.594 -43.627  0.61 16.66      A    C  
ANISOU 1325  CD BGLU A 258     2590   2126   1613    462   -272    481  A    C  
ATOM   1326  OE1AGLU A 258      99.395  80.549 -44.743  0.39 16.48      A    O  
ANISOU 1326  OE1AGLU A 258     2888   1871   1501    220     42    202  A    O  
ATOM   1327  OE1BGLU A 258     100.372  80.973 -44.293  0.61 16.81      A    O  
ANISOU 1327  OE1BGLU A 258     2657   2087   1644    556   -344    385  A    O  
ATOM   1328  OE2AGLU A 258     100.866  81.236 -43.267  0.39 16.00      A    O1-
ANISOU 1328  OE2AGLU A 258     2625   2021   1434     78   -113    264  A    O1-
ATOM   1329  OE2BGLU A 258     101.987  81.022 -42.821  0.61 18.39      A    O1-
ANISOU 1329  OE2BGLU A 258     2723   2522   1743    225   -158    674  A    O1-
ATOM   1330  N   ASP A 259     100.625  85.127 -47.764  1.00 11.79      A    N  
ANISOU 1330  N   ASP A 259     2242   1352    887    137    145    -75  A    N  
ATOM   1331  CA  ASP A 259      99.986  85.081 -49.072  1.00 11.65      A    C  
ANISOU 1331  CA  ASP A 259     2198   1401    826    -34    166    -53  A    C  
ATOM   1332  C   ASP A 259      99.428  83.683 -49.331  1.00 12.08      A    C  
ANISOU 1332  C   ASP A 259     2336   1356    897    193    -70    -43  A    C  
ATOM   1333  O   ASP A 259      99.535  82.774 -48.500  1.00 12.81      A    O  
ANISOU 1333  O   ASP A 259     2562   1406    897    175    -62     18  A    O  
ATOM   1334  CB  ASP A 259     100.887  85.636 -50.185  1.00 12.88      A    C  
ANISOU 1334  CB  ASP A 259     2196   1596   1100    206    356    208  A    C  
ATOM   1335  CG  ASP A 259     102.063  84.736 -50.526  1.00 15.40      A    C  
ANISOU 1335  CG  ASP A 259     2570   1868   1414    164    492    298  A    C  
ATOM   1336  OD1 ASP A 259     102.066  83.542 -50.170  1.00 15.96      A    O  
ANISOU 1336  OD1 ASP A 259     2748   1903   1415    262    440    114  A    O  
ATOM   1337  OD2 ASP A 259     102.992  85.238 -51.202  1.00 17.27      A    O1-
ANISOU 1337  OD2 ASP A 259     2562   2189   1812    215    607    322  A    O1-
ATOM   1338  N   SER A 260      98.826  83.503 -50.505  1.00 12.56      A    N  
ANISOU 1338  N   SER A 260     2387   1402    984     50    -92   -175  A    N  
ATOM   1339  CA  SER A 260      98.150  82.248 -50.810  1.00 13.21      A    C  
ANISOU 1339  CA  SER A 260     2638   1242   1138     97    -60   -150  A    C  
ATOM   1340  C   SER A 260      99.102  81.056 -50.855  1.00 14.39      A    C  
ANISOU 1340  C   SER A 260     2974   1290   1204    135    -17    -87  A    C  
ATOM   1341  O   SER A 260      98.653  79.916 -50.677  1.00 15.27      A    O  
ANISOU 1341  O   SER A 260     3151   1164   1487   -157     42    -74  A    O  
ATOM   1342  CB  SER A 260      97.385  82.378 -52.126  1.00 13.71      A    C  
ANISOU 1342  CB  SER A 260     2633   1474   1102    -15    -16    -29  A    C  
ATOM   1343  OG  SER A 260      98.260  82.690 -53.193  1.00 13.56      A    O  
ANISOU 1343  OG  SER A 260     2573   1532   1047   -115     56     85  A    O  
ATOM   1344  N   SER A 261     100.395  81.288 -51.082  1.00 15.37      A    N  
ANISOU 1344  N   SER A 261     3098   1555   1187    433    199    -15  A    N  
ATOM   1345  CA  SER A 261     101.406  80.237 -51.067  1.00 17.24      A    C  
ANISOU 1345  CA  SER A 261     3411   1679   1461    487    369    104  A    C  
ATOM   1346  C   SER A 261     102.036  80.036 -49.699  1.00 16.34      A    C  
ANISOU 1346  C   SER A 261     3048   1637   1524    502    259    -32  A    C  
ATOM   1347  O   SER A 261     102.883  79.147 -49.553  1.00 18.26      A    O  
ANISOU 1347  O   SER A 261     3138   1946   1854    653    240   -287  A    O  
ATOM   1348  CB  SER A 261     102.530  80.570 -52.048  1.00 21.86      A    C  
ANISOU 1348  CB  SER A 261     4112   2436   1758    960    696    272  A    C  
ATOM   1349  OG  SER A 261     102.117  80.383 -53.380  1.00 25.25      A    O  
ANISOU 1349  OG  SER A 261     4682   3018   1894   1553    806    457  A    O  
ATOM   1350  N   GLY A 262     101.674  80.849 -48.713  1.00 14.88      A    N  
ANISOU 1350  N   GLY A 262     2802   1585   1265    178    280    -62  A    N  
ATOM   1351  CA  GLY A 262     102.267  80.761 -47.394  1.00 15.56      A    C  
ANISOU 1351  CA  GLY A 262     2774   1692   1448    163     35     42  A    C  
ATOM   1352  C   GLY A 262     103.469  81.651 -47.174  1.00 16.36      A    C  
ANISOU 1352  C   GLY A 262     2783   1875   1557    378    144    -41  A    C  
ATOM   1353  O   GLY A 262     104.095  81.558 -46.116  1.00 18.01      A    O  
ANISOU 1353  O   GLY A 262     3095   2223   1524    446    -23     42  A    O  
ATOM   1354  N   ASN A 263     103.812  82.509 -48.135  1.00 14.92      A    N  
ANISOU 1354  N   ASN A 263     2440   1616   1615    343    494    -59  A    N  
ATOM   1355  CA  ASN A 263     104.930  83.426 -47.956  1.00 16.04      A    C  
ANISOU 1355  CA  ASN A 263     2471   1969   1657    219    429   -300  A    C  
ATOM   1356  C   ASN A 263     104.572  84.529 -46.967  1.00 14.49      A    C  
ANISOU 1356  C   ASN A 263     2162   1835   1511    213    294   -144  A    C  
ATOM   1357  O   ASN A 263     103.429  84.978 -46.883  1.00 14.29      A    O  
ANISOU 1357  O   ASN A 263     1901   1982   1546    104    231    -68  A    O  
ATOM   1358  CB  ASN A 263     105.308  84.072 -49.289  1.00 18.26      A    C  
ANISOU 1358  CB  ASN A 263     2771   2320   1850    307    556   -432  A    C  
ATOM   1359  CG  ASN A 263     105.707  83.063 -50.339  1.00 21.75      A    C  
ANISOU 1359  CG  ASN A 263     3269   2821   2173    626    493   -363  A    C  
ATOM   1360  ND2 ASN A 263     105.079  83.150 -51.503  1.00 22.15      A    N  
ANISOU 1360  ND2 ASN A 263     3443   2933   2041    631    568   -370  A    N  
ATOM   1361  OD1 ASN A 263     106.562  82.209 -50.108  1.00 23.80      A    O  
ANISOU 1361  OD1 ASN A 263     3551   2992   2501    947    475   -378  A    O  
ATOM   1362  N   LEU A 264     105.579  84.990 -46.238  1.00 14.58      A    N  
ANISOU 1362  N   LEU A 264     2225   1765   1551    253    260   -162  A    N  
ATOM   1363  CA  LEU A 264     105.366  85.954 -45.169  1.00 14.66      A    C  
ANISOU 1363  CA  LEU A 264     2159   1889   1521    293    147   -147  A    C  
ATOM   1364  C   LEU A 264     105.007  87.333 -45.718  1.00 13.80      A    C  
ANISOU 1364  C   LEU A 264     2118   1756   1370    189    286    -43  A    C  
ATOM   1365  O   LEU A 264     105.710  87.877 -46.571  1.00 16.08      A    O  
ANISOU 1365  O   LEU A 264     2470   2022   1620    164    491     29  A    O  
ATOM   1366  CB  LEU A 264     106.653  86.063 -44.360  1.00 17.37      A    C  
ANISOU 1366  CB  LEU A 264     2333   2566   1699    269    -98   -318  A    C  
ATOM   1367  CG  LEU A 264     106.690  87.178 -43.324  1.00 20.72      A    C  
ANISOU 1367  CG  LEU A 264     2707   3186   1980    390   -218   -425  A    C  
ATOM   1368  CD1 LEU A 264     105.880  86.769 -42.131  1.00 22.32      A    C  
ANISOU 1368  CD1 LEU A 264     2988   3446   2048    558   -123   -353  A    C  
ATOM   1369  CD2 LEU A 264     108.122  87.472 -42.920  1.00 22.07      A    C  
ANISOU 1369  CD2 LEU A 264     2745   3382   2259    268   -256   -436  A    C  
ATOM   1370  N   LEU A 265     103.925  87.912 -45.194  1.00 11.41      A    N  
ANISOU 1370  N   LEU A 265     1921   1374   1040    109    204   -131  A    N  
ATOM   1371  CA  LEU A 265     103.565  89.300 -45.465  1.00 11.18      A    C  
ANISOU 1371  CA  LEU A 265     1939   1303   1006    -28    119    -13  A    C  
ATOM   1372  C   LEU A 265     103.642  90.202 -44.245  1.00 11.75      A    C  
ANISOU 1372  C   LEU A 265     2162   1284   1019   -198    124     15  A    C  
ATOM   1373  O   LEU A 265     103.813  91.413 -44.396  1.00 13.99      A    O  
ANISOU 1373  O   LEU A 265     2611   1500   1206   -259    110     59  A    O  
ATOM   1374  CB  LEU A 265     102.144  89.389 -46.029  1.00 12.31      A    C  
ANISOU 1374  CB  LEU A 265     1960   1679   1037   -118     53   -126  A    C  
ATOM   1375  CG  LEU A 265     101.893  88.612 -47.317  1.00 14.02      A    C  
ANISOU 1375  CG  LEU A 265     2254   1977   1096    -75     90    -81  A    C  
ATOM   1376  CD1 LEU A 265     100.435  88.719 -47.712  1.00 14.80      A    C  
ANISOU 1376  CD1 LEU A 265     2316   2033   1276     96     45    -84  A    C  
ATOM   1377  CD2 LEU A 265     102.811  89.125 -48.423  1.00 15.76      A    C  
ANISOU 1377  CD2 LEU A 265     2477   2365   1145   -165    253     82  A    C  
ATOM   1378  N   GLY A 266     103.499  89.642 -43.050  1.00 10.96      A    N  
ANISOU 1378  N   GLY A 266     1884   1370    912     23    276     27  A    N  
ATOM   1379  CA  GLY A 266     103.533  90.412 -41.823  1.00 10.85      A    C  
ANISOU 1379  CA  GLY A 266     1954   1306    864     18    283     60  A    C  
ATOM   1380  C   GLY A 266     103.571  89.462 -40.649  1.00 10.25      A    C  
ANISOU 1380  C   GLY A 266     1649   1258    988     86    238    120  A    C  
ATOM   1381  O   GLY A 266     103.192  88.295 -40.768  1.00 10.36      A    O  
ANISOU 1381  O   GLY A 266     1576   1196   1165      1    159     43  A    O  
ATOM   1382  N   ARG A 267     104.043  89.969 -39.512  1.00  9.32      A    N  
ANISOU 1382  N   ARG A 267     1496   1160    885    130    137     74  A    N  
ATOM   1383  CA  ARG A 267     104.166  89.138 -38.319  1.00  9.12      A    C  
ANISOU 1383  CA  ARG A 267     1306   1151   1009    173    160    117  A    C  
ATOM   1384  C   ARG A 267     104.023  89.997 -37.071  1.00  9.17      A    C  
ANISOU 1384  C   ARG A 267     1258   1092   1133      9    158     17  A    C  
ATOM   1385  O   ARG A 267     104.516  91.126 -37.023  1.00  9.59      A    O  
ANISOU 1385  O   ARG A 267     1292   1079   1274   -179    -15     64  A    O  
ATOM   1386  CB  ARG A 267     105.533  88.442 -38.267  1.00 11.46      A    C  
ANISOU 1386  CB  ARG A 267     1573   1463   1319    348     76    249  A    C  
ATOM   1387  CG  ARG A 267     105.643  87.396 -37.168  1.00 13.17      A    C  
ANISOU 1387  CG  ARG A 267     1634   1813   1555    706     15    378  A    C  
ATOM   1388  CD  ARG A 267     107.063  86.853 -37.026  1.00 16.28      A    C  
ANISOU 1388  CD  ARG A 267     2164   2176   1846    926     18    210  A    C  
ATOM   1389  NE  ARG A 267     107.548  86.150 -38.209  1.00 19.41      A    N  
ANISOU 1389  NE  ARG A 267     2602   2715   2059    943   -210    143  A    N  
ATOM   1390  CZ  ARG A 267     108.458  86.624 -39.056  1.00 20.82      A    C  
ANISOU 1390  CZ  ARG A 267     2595   3238   2079    968   -189   -106  A    C  
ATOM   1391  NH1 ARG A 267     108.987  87.826 -38.874  1.00 21.33      A    N1+
ANISOU 1391  NH1 ARG A 267     2498   3528   2078    588   -196    147  A    N1+
ATOM   1392  NH2 ARG A 267     108.842  85.887 -40.094  1.00 22.10      A    N  
ANISOU 1392  NH2 ARG A 267     2689   3464   2245   1352   -230   -459  A    N  
ATOM   1393  N   ASP A 268     103.368  89.439 -36.059  1.00  8.43      A    N  
ANISOU 1393  N   ASP A 268     1067   1149    987    -27    130   -141  A    N  
ATOM   1394  CA  ASP A 268     103.281  90.044 -34.736  1.00  8.26      A    C  
ANISOU 1394  CA  ASP A 268     1117    973   1048    131    132    -48  A    C  
ATOM   1395  C   ASP A 268     103.247  88.892 -33.737  1.00  7.96      A    C  
ANISOU 1395  C   ASP A 268     1064    932   1030   -107    -63    -39  A    C  
ATOM   1396  O   ASP A 268     103.091  87.730 -34.113  1.00  9.74      A    O  
ANISOU 1396  O   ASP A 268     1466   1076   1157   -240    -61   -101  A    O  
ATOM   1397  CB  ASP A 268     102.052  90.965 -34.651  1.00 10.26      A    C  
ANISOU 1397  CB  ASP A 268     1555   1126   1217    310     58   -126  A    C  
ATOM   1398  CG  ASP A 268     102.169  92.051 -33.578  1.00 11.14      A    C  
ANISOU 1398  CG  ASP A 268     1721   1266   1247     32      5    145  A    C  
ATOM   1399  OD1 ASP A 268     103.005  91.953 -32.651  1.00 11.47      A    O  
ANISOU 1399  OD1 ASP A 268     1923   1162   1272    152     90    106  A    O  
ATOM   1400  OD2 ASP A 268     101.369  93.004 -33.649  1.00 11.99      A    O1-
ANISOU 1400  OD2 ASP A 268     1732   1493   1330     25   -218    -41  A    O1-
ATOM   1401  N   SER A 269     103.391  89.210 -32.458  1.00  8.45      A    N  
ANISOU 1401  N   SER A 269     1084   1118   1008     -3    -95     68  A    N  
ATOM   1402  CA  SER A 269     103.425  88.152 -31.457  1.00  9.23      A    C  
ANISOU 1402  CA  SER A 269     1283   1186   1036    155     35     96  A    C  
ATOM   1403  C   SER A 269     103.105  88.714 -30.084  1.00  9.27      A    C  
ANISOU 1403  C   SER A 269     1476    974   1073     30     71     -8  A    C  
ATOM   1404  O   SER A 269     103.174  89.922 -29.848  1.00 10.22      A    O  
ANISOU 1404  O   SER A 269     1627   1056   1200   -127      2     34  A    O  
ATOM   1405  CB  SER A 269     104.783  87.448 -31.415  1.00 10.94      A    C  
ANISOU 1405  CB  SER A 269     1351   1379   1427    -77    -70     96  A    C  
ATOM   1406  OG  SER A 269     105.807  88.357 -31.059  1.00 12.95      A    O  
ANISOU 1406  OG  SER A 269     1410   1706   1804    -66     -7    150  A    O  
ATOM   1407  N   PHE A 270     102.785  87.798 -29.171  1.00  8.94      A    N  
ANISOU 1407  N   PHE A 270     1422   1062    911     81     63    110  A    N  
ATOM   1408  CA  PHE A 270     102.512  88.144 -27.786  1.00  9.04      A    C  
ANISOU 1408  CA  PHE A 270     1465   1082    890    151     24    187  A    C  
ATOM   1409  C   PHE A 270     102.733  86.913 -26.922  1.00  7.70      A    C  
ANISOU 1409  C   PHE A 270     1136    950    839     92    -37     48  A    C  
ATOM   1410  O   PHE A 270     102.535  85.782 -27.371  1.00  9.08      A    O  
ANISOU 1410  O   PHE A 270     1531    954    966    182    -10   -151  A    O  
ATOM   1411  CB  PHE A 270     101.080  88.676 -27.604  1.00  9.11      A    C  
ANISOU 1411  CB  PHE A 270     1410   1021   1031    120     23    -35  A    C  
ATOM   1412  CG  PHE A 270      99.997  87.783 -28.184  1.00  8.23      A    C  
ANISOU 1412  CG  PHE A 270     1173   1002    951     39     24    159  A    C  
ATOM   1413  CD1 PHE A 270      99.677  87.836 -29.536  1.00  8.99      A    C  
ANISOU 1413  CD1 PHE A 270     1368   1061    988    134    -36     30  A    C  
ATOM   1414  CD2 PHE A 270      99.292  86.900 -27.371  1.00  9.41      A    C  
ANISOU 1414  CD2 PHE A 270     1300   1118   1157    -92    113     45  A    C  
ATOM   1415  CE1 PHE A 270      98.678  87.027 -30.061  1.00  9.68      A    C  
ANISOU 1415  CE1 PHE A 270     1452   1176   1052    199    -42    114  A    C  
ATOM   1416  CE2 PHE A 270      98.293  86.090 -27.899  1.00  9.84      A    C  
ANISOU 1416  CE2 PHE A 270     1366   1309   1065    -76     96    111  A    C  
ATOM   1417  CZ  PHE A 270      97.990  86.155 -29.249  1.00  9.76      A    C  
ANISOU 1417  CZ  PHE A 270     1476   1204   1028    342     16    119  A    C  
ATOM   1418  N   GLU A 271     103.143  87.139 -25.679  1.00  7.84      A    N  
ANISOU 1418  N   GLU A 271     1067   1077    836    -64    -15    121  A    N  
ATOM   1419  CA  GLU A 271     103.238  86.054 -24.712  1.00  8.04      A    C  
ANISOU 1419  CA  GLU A 271     1135   1101    819   -145    -22     46  A    C  
ATOM   1420  C   GLU A 271     101.834  85.676 -24.243  1.00  8.29      A    C  
ANISOU 1420  C   GLU A 271     1251   1001    897   -115     83    117  A    C  
ATOM   1421  O   GLU A 271     100.909  86.495 -24.278  1.00  8.45      A    O  
ANISOU 1421  O   GLU A 271     1151   1046   1013     32    -29    167  A    O  
ATOM   1422  CB  GLU A 271     104.105  86.495 -23.528  1.00 10.26      A    C  
ANISOU 1422  CB  GLU A 271     1573   1236   1088    -17   -171     50  A    C  
ATOM   1423  CG  GLU A 271     104.347  85.400 -22.486  1.00 13.92      A    C  
ANISOU 1423  CG  GLU A 271     2066   1868   1356    277   -486    142  A    C  
ATOM   1424  CD  GLU A 271     105.329  85.799 -21.398  1.00 17.25      A    C  
ANISOU 1424  CD  GLU A 271     2541   2191   1822    198   -389    202  A    C  
ATOM   1425  OE1 GLU A 271     106.035  86.819 -21.573  1.00 18.84      A    O  
ANISOU 1425  OE1 GLU A 271     2363   2568   2229    -71   -416     30  A    O  
ATOM   1426  OE2 GLU A 271     105.399  85.075 -20.377  1.00 19.18      A    O1-
ANISOU 1426  OE2 GLU A 271     3008   2423   1855    319   -184    342  A    O1-
ATOM   1427  N   VAL A 272     101.663  84.419 -23.826  1.00  9.15      A    N  
ANISOU 1427  N   VAL A 272     1265   1075   1136    -34     11    179  A    N  
ATOM   1428  CA  VAL A 272     100.384  83.937 -23.315  1.00  9.19      A    C  
ANISOU 1428  CA  VAL A 272     1178   1267   1045   -265     21    213  A    C  
ATOM   1429  C   VAL A 272     100.613  83.180 -22.021  1.00  9.58      A    C  
ANISOU 1429  C   VAL A 272     1272   1180   1186    -52      8    239  A    C  
ATOM   1430  O   VAL A 272     101.533  82.361 -21.926  1.00 11.97      A    O  
ANISOU 1430  O   VAL A 272     1640   1380   1529    267     44    265  A    O  
ATOM   1431  CB  VAL A 272      99.671  83.003 -24.315  1.00 10.65      A    C  
ANISOU 1431  CB  VAL A 272     1360   1560   1127   -482   -163     79  A    C  
ATOM   1432  CG1 VAL A 272      98.342  82.539 -23.748  1.00 12.02      A    C  
ANISOU 1432  CG1 VAL A 272     1536   1962   1067   -419    -75    127  A    C  
ATOM   1433  CG2 VAL A 272      99.448  83.707 -25.634  1.00 12.51      A    C  
ANISOU 1433  CG2 VAL A 272     1793   1697   1262   -454   -158    158  A    C  
ATOM   1434  N   ARG A 273      99.756  83.437 -21.035  1.00  9.12      A    N  
ANISOU 1434  N   ARG A 273     1310   1149   1008    -56     48    282  A    N  
ATOM   1435  CA  ARG A 273      99.629  82.600 -19.848  1.00  9.53      A    C  
ANISOU 1435  CA  ARG A 273     1237   1332   1053   -221    -63    181  A    C  
ATOM   1436  C   ARG A 273      98.183  82.135 -19.773  1.00  9.28      A    C  
ANISOU 1436  C   ARG A 273     1030   1275   1220    -43     41    265  A    C  
ATOM   1437  O   ARG A 273      97.258  82.958 -19.761  1.00 10.40      A    O  
ANISOU 1437  O   ARG A 273     1042   1435   1474      8     67    151  A    O  
ATOM   1438  CB  ARG A 273      99.990  83.380 -18.584  1.00 10.40      A    C  
ANISOU 1438  CB  ARG A 273     1517   1432   1003    -80    -76     32  A    C  
ATOM   1439  CG  ARG A 273      99.727  82.581 -17.315  1.00 12.78      A    C  
ANISOU 1439  CG  ARG A 273     1900   1825   1130   -295   -131     47  A    C  
ATOM   1440  CD  ARG A 273     100.174  83.374 -16.100  1.00 15.76      A    C  
ANISOU 1440  CD  ARG A 273     2308   2369   1311   -395    -87     78  A    C  
ATOM   1441  NE  ARG A 273      99.799  82.744 -14.838  1.00 19.50      A    N  
ANISOU 1441  NE  ARG A 273     2692   2999   1719   -244    -35    320  A    N  
ATOM   1442  CZ  ARG A 273     100.466  81.744 -14.282  1.00 24.00      A    C  
ANISOU 1442  CZ  ARG A 273     3124   3881   2114     98    156    636  A    C  
ATOM   1443  NH1 ARG A 273     101.534  81.247 -14.888  1.00 26.97      A    N1+
ANISOU 1443  NH1 ARG A 273     3350   4340   2558    279    139    597  A    N1+
ATOM   1444  NH2 ARG A 273     100.060  81.239 -13.123  1.00 25.25      A    N  
ANISOU 1444  NH2 ARG A 273     3394   4135   2064    155    165   1024  A    N  
ATOM   1445  N   VAL A 274      97.983  80.826 -19.763  1.00  9.50      A    N  
ANISOU 1445  N   VAL A 274     1240   1172   1197   -174    -14    215  A    N  
ATOM   1446  CA  VAL A 274      96.657  80.247 -19.592  1.00 10.37      A    C  
ANISOU 1446  CA  VAL A 274     1260   1319   1360   -169      6     97  A    C  
ATOM   1447  C   VAL A 274      96.553  79.823 -18.137  1.00 11.17      A    C  
ANISOU 1447  C   VAL A 274     1552   1319   1373   -158     91    143  A    C  
ATOM   1448  O   VAL A 274      97.338  78.991 -17.671  1.00 12.78      A    O  
ANISOU 1448  O   VAL A 274     1794   1577   1483     40     76    372  A    O  
ATOM   1449  CB  VAL A 274      96.431  79.054 -20.532  1.00 11.07      A    C  
ANISOU 1449  CB  VAL A 274     1218   1478   1508   -318   -196    233  A    C  
ATOM   1450  CG1 VAL A 274      94.975  78.619 -20.480  1.00 12.00      A    C  
ANISOU 1450  CG1 VAL A 274     1062   1674   1822     73   -382    373  A    C  
ATOM   1451  CG2 VAL A 274      96.837  79.401 -21.954  1.00 12.29      A    C  
ANISOU 1451  CG2 VAL A 274     1595   1567   1508   -151   -160    352  A    C  
ATOM   1452  N   CYS A 275      95.597  80.397 -17.412  1.00 11.57      A    N  
ANISOU 1452  N   CYS A 275     1576   1502   1318   -116    200     81  A    N  
ATOM   1453  CA  CYS A 275      95.597  80.272 -15.963  1.00 13.50      A    C  
ANISOU 1453  CA  CYS A 275     1811   1855   1463   -186    163     44  A    C  
ATOM   1454  C   CYS A 275      94.178  80.434 -15.442  1.00 14.76      A    C  
ANISOU 1454  C   CYS A 275     1959   2028   1622   -394    261    194  A    C  
ATOM   1455  O   CYS A 275      93.279  80.889 -16.153  1.00 15.82      A    O  
ANISOU 1455  O   CYS A 275     1943   2386   1682   -122    178    -18  A    O  
ATOM   1456  CB  CYS A 275      96.533  81.309 -15.337  1.00 15.35      A    C  
ANISOU 1456  CB  CYS A 275     2192   2013   1626   -161   -137     94  A    C  
ATOM   1457  SG  CYS A 275      96.138  83.021 -15.792  1.00 17.65      A    S  
ANISOU 1457  SG  CYS A 275     2545   2206   1957   -174   -100   -201  A    S  
ATOM   1458  N   ALA A 276      93.990  80.069 -14.172  1.00 15.71      A    N  
ANISOU 1458  N   ALA A 276     2202   2018   1748   -430    454    320  A    N  
ATOM   1459  CA  ALA A 276      92.653  80.082 -13.590  1.00 17.93      A    C  
ANISOU 1459  CA  ALA A 276     2585   2358   1869   -387    734    491  A    C  
ATOM   1460  C   ALA A 276      92.149  81.493 -13.319  1.00 17.97      A    C  
ANISOU 1460  C   ALA A 276     2613   2439   1777   -382    639    364  A    C  
ATOM   1461  O   ALA A 276      90.940  81.740 -13.405  1.00 18.33      A    O  
ANISOU 1461  O   ALA A 276     2535   2478   1952   -383    582    208  A    O  
ATOM   1462  CB  ALA A 276      92.636  79.261 -12.297  1.00 20.52      A    C  
ANISOU 1462  CB  ALA A 276     2997   2615   2184   -459    721    718  A    C  
ATOM   1463  N   CYS A 277      93.037  82.427 -12.989  1.00 17.35      A    N  
ANISOU 1463  N   CYS A 277     2739   2285   1569   -516    497    293  A    N  
ATOM   1464  CA ACYS A 277      92.647  83.780 -12.591  0.39 17.30      A    C  
ANISOU 1464  CA ACYS A 277     2704   2397   1473   -397    384    191  A    C  
ATOM   1465  CA BCYS A 277      92.656  83.781 -12.581  0.61 17.93      A    C  
ANISOU 1465  CA BCYS A 277     2888   2430   1495   -484    464    198  A    C  
ATOM   1466  C   CYS A 277      93.487  84.798 -13.348  1.00 16.43      A    C  
ANISOU 1466  C   CYS A 277     2431   2371   1442   -482    286    113  A    C  
ATOM   1467  O   CYS A 277      94.431  85.385 -12.797  1.00 16.53      A    O  
ANISOU 1467  O   CYS A 277     2355   2508   1419   -358    154     94  A    O  
ATOM   1468  CB ACYS A 277      92.756  83.973 -11.079  0.39 18.74      A    C  
ANISOU 1468  CB ACYS A 277     2985   2672   1463   -327    343    168  A    C  
ATOM   1469  CB BCYS A 277      92.858  83.978 -11.079  0.61 20.89      A    C  
ANISOU 1469  CB BCYS A 277     3514   2848   1574   -651    566    205  A    C  
ATOM   1470  SG ACYS A 277      91.899  85.447 -10.495  0.39 20.06      A    S  
ANISOU 1470  SG ACYS A 277     3208   2910   1504   -300    383     89  A    S  
ATOM   1471  SG BCYS A 277      92.038  82.763 -10.042  0.61 23.75      A    S  
ANISOU 1471  SG BCYS A 277     4039   3213   1773   -929    795    168  A    S  
ATOM   1472  N   PRO A 278      93.152  85.049 -14.614  1.00 14.37      A    N  
ANISOU 1472  N   PRO A 278     2033   2108   1320   -523    238    -40  A    N  
ATOM   1473  CA  PRO A 278      93.965  85.979 -15.419  1.00 14.04      A    C  
ANISOU 1473  CA  PRO A 278     1978   2035   1322   -486    133     27  A    C  
ATOM   1474  C   PRO A 278      94.029  87.401 -14.884  1.00 14.67      A    C  
ANISOU 1474  C   PRO A 278     2168   1946   1459   -273     27     27  A    C  
ATOM   1475  O   PRO A 278      95.072  88.047 -15.021  1.00 14.93      A    O  
ANISOU 1475  O   PRO A 278     2137   2026   1509   -317     17      0  A    O  
ATOM   1476  CB  PRO A 278      93.327  85.902 -16.814  1.00 15.95      A    C  
ANISOU 1476  CB  PRO A 278     2243   2458   1361   -687    -12     75  A    C  
ATOM   1477  CG  PRO A 278      92.053  85.158 -16.659  1.00 16.58      A    C  
ANISOU 1477  CG  PRO A 278     2337   2460   1501   -676     57    224  A    C  
ATOM   1478  CD  PRO A 278      92.144  84.337 -15.416  1.00 15.25      A    C  
ANISOU 1478  CD  PRO A 278     2113   2276   1405   -628     71     25  A    C  
ATOM   1479  N   GLY A 279      92.954  87.913 -14.284  1.00 14.73      A    N  
ANISOU 1479  N   GLY A 279     2192   1880   1525   -294     58    -18  A    N  
ATOM   1480  CA  GLY A 279      92.998  89.266 -13.747  1.00 16.29      A    C  
ANISOU 1480  CA  GLY A 279     2425   2063   1702   -269     24    -77  A    C  
ATOM   1481  C   GLY A 279      93.996  89.407 -12.616  1.00 16.63      A    C  
ANISOU 1481  C   GLY A 279     2539   2094   1684   -320     58   -232  A    C  
ATOM   1482  O   GLY A 279      94.788  90.355 -12.574  1.00 16.50      A    O  
ANISOU 1482  O   GLY A 279     2474   2145   1651   -572    -70   -356  A    O  
ATOM   1483  N   ARG A 280      93.986  88.452 -11.685  1.00 17.11      A    N  
ANISOU 1483  N   ARG A 280     2665   2301   1535   -290   -134   -161  A    N  
ATOM   1484  CA  ARG A 280      94.940  88.513 -10.586  1.00 19.12      A    C  
ANISOU 1484  CA  ARG A 280     2990   2557   1718   -552   -126    -94  A    C  
ATOM   1485  C   ARG A 280      96.364  88.301 -11.083  1.00 17.51      A    C  
ANISOU 1485  C   ARG A 280     2674   2502   1475   -447   -132    -42  A    C  
ATOM   1486  O   ARG A 280      97.292  88.988 -10.642  1.00 17.29      A    O  
ANISOU 1486  O   ARG A 280     2457   2694   1420   -409     -7   -113  A    O  
ATOM   1487  CB  ARG A 280      94.592  87.478  -9.525  1.00 25.14      A    C  
ANISOU 1487  CB  ARG A 280     3861   3315   2375   -705    -70     16  A    C  
ATOM   1488  CG  ARG A 280      95.627  87.373  -8.424  1.00 31.19      A    C  
ANISOU 1488  CG  ARG A 280     4832   4018   3002   -645    -28    109  A    C  
ATOM   1489  CD  ARG A 280      95.343  86.152  -7.561  1.00 36.66      A    C  
ANISOU 1489  CD  ARG A 280     5709   4595   3625   -513     28     35  A    C  
ATOM   1490  NE  ARG A 280      95.680  84.918  -8.267  1.00 41.35      A    N  
ANISOU 1490  NE  ARG A 280     6397   5167   4147   -451     29     50  A    N  
ATOM   1491  CZ  ARG A 280      95.114  83.740  -8.037  1.00 44.95      A    C  
ANISOU 1491  CZ  ARG A 280     6876   5717   4486   -451    163    -56  A    C  
ATOM   1492  NH1 ARG A 280      94.169  83.605  -7.113  1.00 45.99      A    N1+
ANISOU 1492  NH1 ARG A 280     7025   5926   4524   -446    253    -41  A    N1+
ATOM   1493  NH2 ARG A 280      95.484  82.670  -8.743  1.00 46.12      A    N  
ANISOU 1493  NH2 ARG A 280     7015   5891   4616   -302    190   -139  A    N  
ATOM   1494  N   ASP A 281      96.559  87.366 -12.011  1.00 16.81      A    N  
ANISOU 1494  N   ASP A 281     2718   2357   1310   -427   -204    112  A    N  
ATOM   1495  CA  ASP A 281      97.911  87.120 -12.498  1.00 17.20      A    C  
ANISOU 1495  CA  ASP A 281     2777   2407   1350   -468   -266    164  A    C  
ATOM   1496  C   ASP A 281      98.451  88.315 -13.275  1.00 16.20      A    C  
ANISOU 1496  C   ASP A 281     2520   2323   1314   -302   -363    219  A    C  
ATOM   1497  O   ASP A 281      99.632  88.664 -13.141  1.00 16.83      A    O  
ANISOU 1497  O   ASP A 281     2535   2378   1482   -300   -430    234  A    O  
ATOM   1498  CB  ASP A 281      97.975  85.824 -13.307  1.00 18.71      A    C  
ANISOU 1498  CB  ASP A 281     3327   2378   1404   -500   -187    253  A    C  
ATOM   1499  CG  ASP A 281      97.886  84.580 -12.425  1.00 22.16      A    C  
ANISOU 1499  CG  ASP A 281     4191   2711   1520   -372   -280    233  A    C  
ATOM   1500  OD1 ASP A 281      97.908  84.707 -11.176  1.00 23.68      A    O  
ANISOU 1500  OD1 ASP A 281     4507   2859   1632   -293   -360    371  A    O  
ATOM   1501  OD2 ASP A 281      97.798  83.472 -12.987  1.00 23.91      A    O1-
ANISOU 1501  OD2 ASP A 281     4468   2914   1703   -407   -208    158  A    O1-
ATOM   1502  N   ARG A 282      97.608  88.973 -14.076  1.00 14.92      A    N  
ANISOU 1502  N   ARG A 282     2470   2029   1171   -115   -125     90  A    N  
ATOM   1503  CA  ARG A 282      98.062  90.182 -14.757  1.00 14.59      A    C  
ANISOU 1503  CA  ARG A 282     2289   2028   1227   -352   -322     50  A    C  
ATOM   1504  C   ARG A 282      98.477  91.254 -13.755  1.00 16.28      A    C  
ANISOU 1504  C   ARG A 282     2562   2318   1306   -552   -264   -116  A    C  
ATOM   1505  O   ARG A 282      99.530  91.882 -13.907  1.00 16.44      A    O  
ANISOU 1505  O   ARG A 282     2525   2332   1389   -674   -206   -102  A    O  
ATOM   1506  CB  ARG A 282      96.993  90.720 -15.708  1.00 13.82      A    C  
ANISOU 1506  CB  ARG A 282     2069   1902   1282    -54   -346    207  A    C  
ATOM   1507  CG  ARG A 282      97.417  92.034 -16.350  1.00 13.48      A    C  
ANISOU 1507  CG  ARG A 282     1968   1864   1290   -142   -194    117  A    C  
ATOM   1508  CD  ARG A 282      96.402  92.542 -17.368  1.00 12.85      A    C  
ANISOU 1508  CD  ARG A 282     1851   1756   1273   -151   -183     71  A    C  
ATOM   1509  NE  ARG A 282      96.698  93.928 -17.714  1.00 13.37      A    N  
ANISOU 1509  NE  ARG A 282     2033   1696   1352    -62     66   -121  A    N  
ATOM   1510  CZ  ARG A 282      95.845  94.780 -18.277  1.00 13.51      A    C  
ANISOU 1510  CZ  ARG A 282     2010   1724   1399   -137    125   -128  A    C  
ATOM   1511  NH1 ARG A 282      94.616  94.396 -18.609  1.00 13.16      A    N1+
ANISOU 1511  NH1 ARG A 282     2041   1632   1326    -98     71   -310  A    N1+
ATOM   1512  NH2 ARG A 282      96.232  96.027 -18.513  1.00 15.18      A    N  
ANISOU 1512  NH2 ARG A 282     2227   1890   1651   -257    144   -145  A    N  
ATOM   1513  N   ARG A 283      97.664  91.467 -12.712  1.00 16.78      A    N  
ANISOU 1513  N   ARG A 283     2611   2453   1312   -664   -141   -301  A    N  
ATOM   1514  CA  ARG A 283      98.011  92.466 -11.702  1.00 20.17      A    C  
ANISOU 1514  CA  ARG A 283     2922   3162   1578   -747    -61   -415  A    C  
ATOM   1515  C   ARG A 283      99.327  92.122 -11.017  1.00 20.54      A    C  
ANISOU 1515  C   ARG A 283     2786   3511   1508   -958   -246   -306  A    C  
ATOM   1516  O   ARG A 283     100.178  92.996 -10.817  1.00 21.81      A    O  
ANISOU 1516  O   ARG A 283     2917   3780   1591  -1122   -278   -436  A    O  
ATOM   1517  CB  ARG A 283      96.886  92.599 -10.671  1.00 23.53      A    C  
ANISOU 1517  CB  ARG A 283     3364   3686   1890   -542    298   -574  A    C  
ATOM   1518  CG  ARG A 283      95.636  93.283 -11.195  1.00 28.28      A    C  
ANISOU 1518  CG  ARG A 283     3986   4358   2400   -228    600   -568  A    C  
ATOM   1519  CD  ARG A 283      94.618  93.614 -10.099  1.00 32.72      A    C  
ANISOU 1519  CD  ARG A 283     4548   4948   2936    222    841   -512  A    C  
ATOM   1520  NE  ARG A 283      93.915  92.440  -9.582  1.00 36.90      A    N  
ANISOU 1520  NE  ARG A 283     5048   5587   3385    500    903   -584  A    N  
ATOM   1521  CZ  ARG A 283      94.166  91.878  -8.401  1.00 39.88      A    C  
ANISOU 1521  CZ  ARG A 283     5466   5984   3702    501    880   -647  A    C  
ATOM   1522  NH1 ARG A 283      95.108  92.380  -7.612  1.00 41.38      A    N1+
ANISOU 1522  NH1 ARG A 283     5715   6149   3858    522    862   -680  A    N1+
ATOM   1523  NH2 ARG A 283      93.475  90.817  -8.002  1.00 40.50      A    N  
ANISOU 1523  NH2 ARG A 283     5493   6072   3824    479    904   -679  A    N  
ATOM   1524  N   THR A 284      99.517  90.849 -10.664  1.00 20.94      A    N  
ANISOU 1524  N   THR A 284     2743   3783   1432   -957   -368     23  A    N  
ATOM   1525  CA  THR A 284     100.747  90.433  -9.997  1.00 22.44      A    C  
ANISOU 1525  CA  THR A 284     2837   4069   1618   -963   -570    393  A    C  
ATOM   1526  C   THR A 284     101.962  90.660 -10.886  1.00 21.96      A    C  
ANISOU 1526  C   THR A 284     2671   4010   1660  -1018   -781    412  A    C  
ATOM   1527  O   THR A 284     102.975  91.214 -10.446  1.00 23.51      A    O  
ANISOU 1527  O   THR A 284     2762   4369   1799  -1043   -735    339  A    O  
ATOM   1528  CB  THR A 284     100.640  88.962  -9.598  1.00 24.66      A    C  
ANISOU 1528  CB  THR A 284     3128   4342   1900   -795   -479    742  A    C  
ATOM   1529  CG2 THR A 284     101.925  88.493  -8.919  1.00 26.71      A    C  
ANISOU 1529  CG2 THR A 284     3364   4575   2209   -752   -490    887  A    C  
ATOM   1530  OG1 THR A 284      99.540  88.797  -8.694  1.00 26.34      A    O  
ANISOU 1530  OG1 THR A 284     3436   4570   2002   -690   -214    752  A    O  
ATOM   1531  N   GLU A 285     101.880  90.245 -12.151  1.00 21.35      A    N  
ANISOU 1531  N   GLU A 285     2678   3745   1688   -810   -775    465  A    N  
ATOM   1532  CA  GLU A 285     103.041  90.366 -13.026  1.00 20.96      A    C  
ANISOU 1532  CA  GLU A 285     2559   3517   1887   -810   -709    398  A    C  
ATOM   1533  C   GLU A 285     103.340  91.818 -13.382  1.00 20.33      A    C  
ANISOU 1533  C   GLU A 285     2501   3308   1915   -925   -547    233  A    C  
ATOM   1534  O   GLU A 285     104.513  92.185 -13.520  1.00 20.94      A    O  
ANISOU 1534  O   GLU A 285     2556   3385   2013   -953   -419    231  A    O  
ATOM   1535  CB  GLU A 285     102.873  89.486 -14.268  1.00 21.59      A    C  
ANISOU 1535  CB  GLU A 285     2747   3499   1959   -732   -678    438  A    C  
ATOM   1536  CG  GLU A 285     102.735  88.007 -13.923  1.00 23.59      A    C  
ANISOU 1536  CG  GLU A 285     3036   3782   2146   -599   -621    421  A    C  
ATOM   1537  CD  GLU A 285     102.906  87.095 -15.120  1.00 25.21      A    C  
ANISOU 1537  CD  GLU A 285     3257   3980   2344   -506   -602    463  A    C  
ATOM   1538  OE1 GLU A 285     103.473  87.542 -16.139  1.00 25.90      A    O  
ANISOU 1538  OE1 GLU A 285     3356   4145   2339   -191   -679    639  A    O  
ATOM   1539  OE2 GLU A 285     102.475  85.924 -15.034  1.00 26.07      A    O1-
ANISOU 1539  OE2 GLU A 285     3352   4074   2481   -492   -654    317  A    O1-
ATOM   1540  N   GLU A 286     102.309  92.658 -13.520  1.00 20.03      A    N  
ANISOU 1540  N   GLU A 286     2667   3096   1846   -940   -425    -60  A    N  
ATOM   1541  CA  GLU A 286     102.551  94.079 -13.757  1.00 20.36      A    C  
ANISOU 1541  CA  GLU A 286     2725   3078   1934  -1090   -413   -257  A    C  
ATOM   1542  C   GLU A 286     103.173  94.745 -12.539  1.00 23.05      A    C  
ANISOU 1542  C   GLU A 286     3079   3473   2207  -1409   -617   -354  A    C  
ATOM   1543  O   GLU A 286     104.013  95.640 -12.679  1.00 23.75      A    O  
ANISOU 1543  O   GLU A 286     3115   3579   2329  -1523   -663   -460  A    O  
ATOM   1544  CB  GLU A 286     101.263  94.788 -14.183  1.00 19.13      A    C  
ANISOU 1544  CB  GLU A 286     2623   2816   1828   -736   -236   -451  A    C  
ATOM   1545  CG  GLU A 286     100.814  94.403 -15.588  1.00 18.31      A    C  
ANISOU 1545  CG  GLU A 286     2533   2631   1795   -478   -262   -719  A    C  
ATOM   1546  CD  GLU A 286      99.661  95.237 -16.122  1.00 19.56      A    C  
ANISOU 1546  CD  GLU A 286     2743   2727   1961   -146    -95   -864  A    C  
ATOM   1547  OE1 GLU A 286      99.094  96.063 -15.373  1.00 23.37      A    O  
ANISOU 1547  OE1 GLU A 286     3260   3435   2183    367    -68  -1060  A    O  
ATOM   1548  OE2 GLU A 286      99.313  95.059 -17.307  1.00 16.78      A    O1-
ANISOU 1548  OE2 GLU A 286     2167   2362   1846   -289   -149   -715  A    O1-
ATOM   1549  N   GLU A 287     102.774  94.319 -11.340  1.00 24.78      A    N  
ANISOU 1549  N   GLU A 287     3318   3812   2285  -1516   -849   -317  A    N  
ATOM   1550  CA  GLU A 287     103.403  94.830 -10.126  1.00 27.41      A    C  
ANISOU 1550  CA  GLU A 287     3519   4338   2559  -1633  -1004   -156  A    C  
ATOM   1551  C   GLU A 287     104.862  94.405 -10.047  1.00 29.71      A    C  
ANISOU 1551  C   GLU A 287     3731   4694   2862  -1754  -1076     66  A    C  
ATOM   1552  O   GLU A 287     105.734  95.212  -9.700  1.00 31.54      A    O  
ANISOU 1552  O   GLU A 287     3967   5024   2993  -1796  -1113    -38  A    O  
ATOM   1553  CB  GLU A 287     102.630  94.346  -8.899  1.00 28.20      A    C  
ANISOU 1553  CB  GLU A 287     3667   4491   2556  -1504   -999   -219  A    C  
ATOM   1554  N   ASN A 288     105.150  93.140 -10.373  1.00 30.64      A    N  
ANISOU 1554  N   ASN A 288     3719   4865   3058  -1749  -1116    263  A    N  
ATOM   1555  CA  ASN A 288     106.536  92.680 -10.393  1.00 32.42      A    C  
ANISOU 1555  CA  ASN A 288     3764   5183   3369  -1604  -1155    369  A    C  
ATOM   1556  C   ASN A 288     107.370  93.511 -11.358  1.00 32.50      A    C  
ANISOU 1556  C   ASN A 288     3702   5169   3477  -1798  -1132    352  A    C  
ATOM   1557  O   ASN A 288     108.524  93.844 -11.067  1.00 32.92      A    O  
ANISOU 1557  O   ASN A 288     3648   5293   3568  -1899  -1114    244  A    O  
ATOM   1558  CB  ASN A 288     106.605  91.202 -10.780  1.00 34.42      A    C  
ANISOU 1558  CB  ASN A 288     4008   5452   3617  -1192  -1082    502  A    C  
ATOM   1559  CG  ASN A 288     106.010  90.289  -9.727  1.00 37.28      A    C  
ANISOU 1559  CG  ASN A 288     4402   5831   3930   -829   -980    461  A    C  
ATOM   1560  ND2 ASN A 288     105.688  89.063 -10.124  1.00 38.09      A    N  
ANISOU 1560  ND2 ASN A 288     4532   5839   4101   -643   -843    523  A    N  
ATOM   1561  OD1 ASN A 288     105.847  90.676  -8.571  1.00 38.70      A    O  
ANISOU 1561  OD1 ASN A 288     4634   6071   3997   -664   -906    544  A    O  
ATOM   1562  N   LEU A 289     106.799  93.855 -12.515  1.00 31.97      A    N  
ANISOU 1562  N   LEU A 289     3676   4954   3518  -1788  -1157    347  A    N  
ATOM   1563  CA  LEU A 289     107.516  94.674 -13.485  1.00 32.53      A    C  
ANISOU 1563  CA  LEU A 289     3785   4903   3672  -1752  -1068    265  A    C  
ATOM   1564  C   LEU A 289     107.757  96.081 -12.950  1.00 35.01      A    C  
ANISOU 1564  C   LEU A 289     4185   5124   3993  -1775   -905    117  A    C  
ATOM   1565  O   LEU A 289     108.846  96.642 -13.127  1.00 35.42      A    O  
ANISOU 1565  O   LEU A 289     4308   5123   4025  -1820   -753     93  A    O  
ATOM   1566  CB  LEU A 289     106.730  94.716 -14.796  1.00 31.18      A    C  
ANISOU 1566  CB  LEU A 289     3621   4675   3552  -1724   -967    337  A    C  
ATOM   1567  CG  LEU A 289     107.361  95.510 -15.939  1.00 31.67      A    C  
ANISOU 1567  CG  LEU A 289     3757   4672   3605  -1478   -734    390  A    C  
ATOM   1568  CD1 LEU A 289     108.674  94.873 -16.363  1.00 32.30      A    C  
ANISOU 1568  CD1 LEU A 289     3798   4813   3664  -1429   -564    389  A    C  
ATOM   1569  CD2 LEU A 289     106.397  95.609 -17.112  1.00 31.44      A    C  
ANISOU 1569  CD2 LEU A 289     3761   4587   3597  -1468   -746    397  A    C  
ATOM   1570  N   ARG A 290     106.759  96.663 -12.282  1.00 37.28      A    N  
ANISOU 1570  N   ARG A 290     4558   5338   4270  -1785   -873    -15  A    N  
ATOM   1571  CA  ARG A 290     106.927  98.001 -11.724  1.00 39.70      A    C  
ANISOU 1571  CA  ARG A 290     4987   5568   4529  -1657   -817   -125  A    C  
ATOM   1572  C   ARG A 290     108.007  98.021 -10.648  1.00 41.82      A    C  
ANISOU 1572  C   ARG A 290     5328   5812   4749  -1617   -889   -264  A    C  
ATOM   1573  O   ARG A 290     108.773  98.987 -10.544  1.00 42.48      A    O  
ANISOU 1573  O   ARG A 290     5495   5875   4770  -1703   -817   -347  A    O  
ATOM   1574  CB  ARG A 290     105.595  98.505 -11.169  1.00 39.83      A    C  
ANISOU 1574  CB  ARG A 290     4958   5619   4554  -1590   -703    -81  A    C  
ATOM   1575  N   LYS A 291     108.093  96.963  -9.848  1.00 43.11      A    N  
ANISOU 1575  N   LYS A 291     5381   6065   4933  -1437  -1125   -386  A    N  
ATOM   1576  CA  LYS A 291     109.094  96.890  -8.787  1.00 44.47      A    C  
ANISOU 1576  CA  LYS A 291     5456   6292   5147  -1266  -1335   -460  A    C  
ATOM   1577  C   LYS A 291     110.487  96.667  -9.364  1.00 45.86      A    C  
ANISOU 1577  C   LYS A 291     5541   6540   5344  -1045  -1300   -499  A    C  
ATOM   1578  O   LYS A 291     111.476  97.184  -8.840  1.00 46.74      A    O  
ANISOU 1578  O   LYS A 291     5629   6682   5448   -869  -1271   -541  A    O  
ATOM   1579  CB  LYS A 291     108.748  95.775  -7.796  1.00 44.05      A    C  
ANISOU 1579  CB  LYS A 291     5436   6203   5098  -1315  -1521   -490  A    C  
TER   
HETATM 1580  C01 9GQ A 402      90.928  93.752 -45.487  1.00 21.36      D    C  
ANISOU 1580  C01 9GQ A 402     3625   2606   1883    477   -132     73  D    C  
HETATM 1581  N01 9GQ A 402      92.279  91.557 -42.811  1.00 17.57      D    N  
ANISOU 1581  N01 9GQ A 402     3060   1663   1954    409    -35   -607  D    N  
HETATM 1582  O01 9GQ A 402      90.925  96.166 -42.714  1.00 17.36      D    O  
ANISOU 1582  O01 9GQ A 402     2954   1954   1689    308   -316    437  D    O  
HETATM 1583  C02 9GQ A 402      91.424  92.591 -44.881  1.00 21.06      D    C  
ANISOU 1583  C02 9GQ A 402     3794   2420   1789    406   -189   -126  D    C  
HETATM 1584  O02 9GQ A 402      90.171  97.235 -44.828  1.00 24.25      D    O  
ANISOU 1584  O02 9GQ A 402     3752   3544   1919    761   -244    356  D    O  
HETATM 1585  C03 9GQ A 402      91.752  92.655 -43.517  1.00 18.01      D    C  
ANISOU 1585  C03 9GQ A 402     3220   1840   1782    315    -26   -345  D    C  
HETATM 1586  O03 9GQ A 402      89.890  95.981 -46.708  1.00 24.02      D    O  
ANISOU 1586  O03 9GQ A 402     3686   3565   1876    622    -95    113  D    O  
HETATM 1587  C04 9GQ A 402      91.588  93.849 -42.791  1.00 16.67      D    C  
ANISOU 1587  C04 9GQ A 402     2865   1805   1663    276    -29   -121  D    C  
HETATM 1588  O04 9GQ A 402      91.611  91.390 -45.513  1.00 25.14      D    O  
ANISOU 1588  O04 9GQ A 402     4651   3042   1858    459   -439    -28  D    O  
HETATM 1589  C05 9GQ A 402      91.090  94.998 -43.419  1.00 17.86      D    C  
ANISOU 1589  C05 9GQ A 402     2994   2087   1703    273   -145    187  D    C  
HETATM 1590  C06 9GQ A 402      90.754  94.952 -44.772  1.00 20.37      D    C  
ANISOU 1590  C06 9GQ A 402     3361   2601   1777    499   -224    168  D    C  
HETATM 1591  C07 9GQ A 402      90.223  96.156 -45.493  1.00 22.94      D    C  
ANISOU 1591  C07 9GQ A 402     3631   3222   1863    615   -219    259  D    C  
HETATM 1592  C08 9GQ A 402      90.941  91.099 -46.748  1.00 27.78      D    C  
ANISOU 1592  C08 9GQ A 402     4966   3583   2008    353   -588    164  D    C  
HETATM 1593  C09 9GQ A 402      91.851  90.259 -47.642  1.00 30.35      D    C  
ANISOU 1593  C09 9GQ A 402     5154   4120   2259    -74   -627    157  D    C  
HETATM 1594  C10 9GQ A 402      91.098  89.120 -48.316  1.00 31.63      D    C  
ANISOU 1594  C10 9GQ A 402     5127   4538   2351   -281   -650     81  D    C  
HETATM 1595  C11 9GQ A 402      93.612  91.423 -42.465  1.00 17.33      D    C  
ANISOU 1595  C11 9GQ A 402     3060   1536   1988    361     45   -809  D    C  
HETATM 1596  C12 9GQ A 402      93.768  90.262 -41.742  1.00 17.80      D    C  
ANISOU 1596  C12 9GQ A 402     2916   1820   2026    295   -111   -512  D    C  
HETATM 1597  C13 9GQ A 402      92.489  89.673 -41.638  1.00 17.34      D    C  
ANISOU 1597  C13 9GQ A 402     2666   1835   2087    344     11   -465  D    C  
HETATM 1598  C14 9GQ A 402      91.590  90.486 -42.294  1.00 17.39      D    C  
ANISOU 1598  C14 9GQ A 402     2882   1657   2070    116     21   -367  D    C  
HETATM 1599  C15 9GQ A 402      89.985  89.674 -49.188  1.00 31.86      D    C  
ANISOU 1599  C15 9GQ A 402     5148   4616   2341   -259   -761    134  D    C  
HETATM 1600  I01 9GQ A 402      92.059  93.965 -40.725  1.00 15.89      D    I  
ANISOU 1600  I01 9GQ A 402     2663   1843   1533    113   -207      1  D    I  
CONECT 1580 1583 1590
CONECT 1581 1585 1595 1598
CONECT 1582 1589
CONECT 1583 1580 1585 1588
CONECT 1584 1591
CONECT 1585 1583 1581 1587
CONECT 1586 1591
CONECT 1587 1585 1589 1600
CONECT 1588 1583 1592
CONECT 1589 1587 1582 1590
CONECT 1590 1580 1589 1591
CONECT 1591 1590 1584 1586
CONECT 1592 1588 1593
CONECT 1593 1592 1594
CONECT 1594 1593 1599
CONECT 1595 1581 1596
CONECT 1596 1595 1597
CONECT 1597 1596 1598
CONECT 1598 1597 1581
CONECT 1599 1594
CONECT 1600 1587
END



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