CNRS Nantes University US2B US2B
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
**Some cleaning from time to time**
Sorry for the inconvenience.


***  fg  ***

elNémo ID: 2606040549382699479

Job options:

ID        	=	 2606040549382699479
JOBID     	=	 fg
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER fg

ATOM      1  N   ALA B   5     -38.830 -20.826  20.120  1.00 63.86      B    N  
ANISOU    1  N   ALA B   5     5147   6057  13063   2454      6    229  B    N  
ATOM      2  CA  ALA B   5     -38.111 -20.929  18.852  1.00 98.22      B    C  
ANISOU    2  CA  ALA B   5     9459  10610  17250   2651   -128   -109  B    C  
ATOM      3  C   ALA B   5     -38.280 -22.340  18.276  1.00111.21      B    C  
ANISOU    3  C   ALA B   5    10935  11886  19434   2826   -203   -414  B    C  
ATOM      4  O   ALA B   5     -38.980 -22.538  17.277  1.00106.84      B    O  
ANISOU    4  O   ALA B   5    10299  11248  19047   2885   -313   -833  B    O  
ATOM      5  CB  ALA B   5     -36.631 -20.592  19.047  1.00101.08      B    C  
ANISOU    5  CB  ALA B   5     9879  11341  17183   2724   -100    125  B    C  
ATOM      6  N   ALA B   6     -37.628 -23.309  18.917  1.00 97.12      B    N  
ANISOU    6  N   ALA B   6     9081   9891  17929   2907   -138   -201  B    N  
ATOM      7  CA  ALA B   6     -37.863 -24.730  18.662  1.00 91.63      B    C  
ANISOU    7  CA  ALA B   6     8212   8738  17864   3045   -193   -413  B    C  
ATOM      8  C   ALA B   6     -38.970 -25.259  19.569  1.00104.22      B    C  
ANISOU    8  C   ALA B   6     9751   9881  19968   2887   -117   -204  B    C  
ATOM      9  O   ALA B   6     -39.453 -26.371  19.378  1.00 99.07      B    O  
ANISOU    9  O   ALA B   6     8948   8789  19904   2956   -174   -380  B    O  
ATOM     10  CB  ALA B   6     -36.582 -25.540  18.873  1.00 64.00      B    C  
ANISOU   10  CB  ALA B   6     4642   5227  14449   3225   -169   -271  B    C  
ATOM     11  N   ALA B   7     -39.348 -24.468  20.571  1.00109.18      B    N  
ANISOU   11  N   ALA B   7    10479  10634  20370   2676      1    178  B    N  
ATOM     12  CA  ALA B   7     -40.492 -24.784  21.425  1.00 95.77      B    C  
ANISOU   12  CA  ALA B   7     8718   8609  19059   2510     58    393  B    C  
ATOM     13  C   ALA B   7     -41.559 -23.699  21.271  1.00 86.71      B    C  
ANISOU   13  C   ALA B   7     7695   7616  17636   2344     41    282  B    C  
ATOM     14  O   ALA B   7     -41.824 -22.935  22.191  1.00 97.22      B    O  
ANISOU   14  O   ALA B   7     9098   9119  18722   2176    135    602  B    O  
ATOM     15  CB  ALA B   7     -40.055 -24.922  22.881  1.00 69.99      B    C  
ANISOU   15  CB  ALA B   7     5403   5375  15816   2415    214    971  B    C  
ATOM     16  N   PRO B   8     -42.177 -23.633  20.090  1.00 71.35      B    N  
ANISOU   16  N   PRO B   8     5753   5627  15729   2397    -77   -186  B    N  
ATOM     17  CA  PRO B   8     -43.138 -22.589  19.734  1.00 59.54      B    C  
ANISOU   17  CA  PRO B   8     4364   4302  13954   2265    -97   -336  B    C  
ATOM     18  C   PRO B   8     -44.456 -22.845  20.415  1.00 59.82      B    C  
ANISOU   18  C   PRO B   8     4369   4036  14323   2105    -65   -199  B    C  
ATOM     19  O   PRO B   8     -44.895 -23.994  20.454  1.00 76.15      B    O  
ANISOU   19  O   PRO B   8     6298   5699  16936   2141   -101   -250  B    O  
ATOM     20  CB  PRO B   8     -43.322 -22.783  18.221  1.00 57.45      B    C  
ANISOU   20  CB  PRO B   8     4036   4059  13734   2406   -230   -883  B    C  
ATOM     21  CG  PRO B   8     -42.423 -23.912  17.824  1.00 68.14      B    C  
ANISOU   21  CG  PRO B   8     5252   5256  15381   2619   -290  -1037  B    C  
ATOM     22  CD  PRO B   8     -42.130 -24.679  19.065  1.00 84.00      B    C  
ANISOU   22  CD  PRO B   8     7215   6974  17726   2584   -196   -609  B    C  
ATOM     23  N   LEU B   9     -45.066 -21.803  20.954  1.00 51.20      B    N  
ANISOU   23  N   LEU B   9     3391   3142  12920   1934     -9    -25  B    N  
ATOM     24  CA  LEU B   9     -46.451 -21.869  21.420  1.00 59.09      B    C  
ANISOU   24  CA  LEU B   9     4374   3934  14145   1785     -2     46  B    C  
ATOM     25  C   LEU B   9     -47.367 -21.935  20.207  1.00 66.86      B    C  
ANISOU   25  C   LEU B   9     5354   4809  15241   1811    -95   -417  B    C  
ATOM     26  O   LEU B   9     -47.131 -21.237  19.221  1.00 71.24      B    O  
ANISOU   26  O   LEU B   9     5971   5631  15465   1869   -135   -705  B    O  
ATOM     27  CB  LEU B   9     -46.790 -20.641  22.244  1.00 55.44      B    C  
ANISOU   27  CB  LEU B   9     4030   3765  13269   1618     73    306  B    C  
ATOM     28  CG  LEU B   9     -46.277 -20.578  23.685  1.00 59.29      B    C  
ANISOU   28  CG  LEU B   9     4473   4370  13684   1542    180    793  B    C  
ATOM     29  CD1 LEU B   9     -44.801 -20.921  23.761  1.00 83.96      B    C  
ANISOU   29  CD1 LEU B   9     7565   7595  16740   1667    220    915  B    C  
ATOM     30  CD2 LEU B   9     -46.547 -19.207  24.271  1.00 52.36      B    C  
ANISOU   30  CD2 LEU B   9     3713   3835  12344   1402    231    925  B    C  
ATOM     31  N   ARG B  10     -48.389 -22.788  20.267  1.00 69.56      B    N  
ANISOU   31  N   ARG B  10     5599   4783  16048   1767   -131   -473  B    N  
ATOM     32  CA  ARG B  10     -49.391 -22.852  19.199  1.00 66.51      B    C  
ANISOU   32  CA  ARG B  10     5199   4306  15766   1768   -202   -898  B    C  
ATOM     33  C   ARG B  10     -50.719 -22.330  19.714  1.00 61.61      B    C  
ANISOU   33  C   ARG B  10     4650   3680  15081   1581   -171   -754  B    C  
ATOM     34  O   ARG B  10     -51.161 -22.697  20.797  1.00 69.79      B    O  
ANISOU   34  O   ARG B  10     5640   4544  16332   1479   -144   -402  B    O  
ATOM     35  CB  ARG B  10     -49.551 -24.282  18.647  1.00 57.32      B    C  
ANISOU   35  CB  ARG B  10     3858   2719  15204   1880   -288  -1168  B    C  
ATOM     36  CG  ARG B  10     -48.284 -24.815  18.059  1.00 61.22      B    C  
ANISOU   36  CG  ARG B  10     4268   3231  15762   2086   -334  -1363  B    C  
ATOM     37  CD  ARG B  10     -48.338 -26.305  17.816  1.00 83.06      B    C  
ANISOU   37  CD  ARG B  10     6840   5518  19201   2195   -416  -1553  B    C  
ATOM     38  NE  ARG B  10     -46.977 -26.825  17.705  1.00103.75      B    N  
ANISOU   38  NE  ARG B  10     9388   8145  21887   2383   -436  -1568  B    N  
ATOM     39  CZ  ARG B  10     -46.297 -26.900  16.567  1.00104.71      B    C  
ANISOU   39  CZ  ARG B  10     9452   8446  21888   2571   -514  -2006  B    C  
ATOM     40  NH1 ARG B  10     -46.867 -26.514  15.431  1.00 89.15      B    N  
ANISOU   40  NH1 ARG B  10     7460   6669  19745   2595   -575  -2462  B    N  
ATOM     41  NH2 ARG B  10     -45.054 -27.372  16.566  1.00107.26      B    N  
ANISOU   41  NH2 ARG B  10     9717   8787  22252   2742   -532  -1979  B    N  
ATOM     42  N   THR B  11     -51.354 -21.458  18.945  1.00 63.56      B    N  
ANISOU   42  N   THR B  11     4984   4147  15018   1539   -176  -1010  B    N  
ATOM     43  CA  THR B  11     -52.633 -20.911  19.345  1.00 49.18      B    C  
ANISOU   43  CA  THR B  11     3239   2346  13102   1374   -148   -905  B    C  
ATOM     44  C   THR B  11     -53.497 -20.668  18.122  1.00 57.73      B    C  
ANISOU   44  C   THR B  11     4325   3489  14119   1375   -178  -1322  B    C  
ATOM     45  O   THR B  11     -52.985 -20.470  17.018  1.00 64.75      B    O  
ANISOU   45  O   THR B  11     5178   4563  14860   1489   -206  -1649  B    O  
ATOM     46  CB  THR B  11     -52.445 -19.608  20.137  1.00 62.17      B    C  
ANISOU   46  CB  THR B  11     5025   4328  14269   1276    -79   -611  B    C  
ATOM     47  CG2 THR B  11     -51.506 -18.673  19.403  1.00 55.68      B    C  
ANISOU   47  CG2 THR B  11     4276   3847  13032   1354    -75   -769  B    C  
ATOM     48  OG1 THR B  11     -53.712 -18.957  20.319  1.00 53.23      B    O  
ANISOU   48  OG1 THR B  11     3970   3261  12996   1138    -61   -588  B    O  
ATOM     49  N   ARG B  12     -54.813 -20.716  18.319  1.00 48.79      B    N  
ANISOU   49  N   ARG B  12     3210   2235  13092   1250   -173  -1298  B    N  
ATOM     50  CA  ARG B  12     -55.762 -20.341  17.272  1.00 61.42      B    C  
ANISOU   50  CA  ARG B  12     4822   3946  14570   1222   -174  -1642  B    C  
ATOM     51  C   ARG B  12     -55.698 -18.849  16.935  1.00 57.62      B    C  
ANISOU   51  C   ARG B  12     4460   3891  13540   1189   -121  -1657  B    C  
ATOM     52  O   ARG B  12     -55.919 -18.457  15.791  1.00 69.26      B    O  
ANISOU   52  O   ARG B  12     5897   5569  14851   1226   -120  -1975  B    O  
ATOM     53  CB  ARG B  12     -57.203 -20.706  17.675  1.00 57.96      B    C  
ANISOU   53  CB  ARG B  12     4389   3294  14341   1084   -177  -1559  B    C  
ATOM     54  CG  ARG B  12     -57.369 -22.139  18.183  1.00 62.31      B    C  
ANISOU   54  CG  ARG B  12     4806   3398  15472   1087   -242  -1453  B    C  
ATOM     55  CD  ARG B  12     -56.847 -23.107  17.157  1.00 67.14      B    C  
ANISOU   55  CD  ARG B  12     5266   3814  16429   1237   -304  -1858  B    C  
ATOM     56  NE  ARG B  12     -57.863 -23.578  16.218  1.00 82.45      B    N  
ANISOU   56  NE  ARG B  12     7126   5633  18569   1220   -337  -2243  B    N  
ATOM     57  CZ  ARG B  12     -59.121 -23.874  16.538  1.00101.22      B    C  
ANISOU   57  CZ  ARG B  12     9508   7828  21122   1083   -348  -2150  B    C  
ATOM     58  NH1 ARG B  12     -59.549 -23.768  17.794  1.00 88.47      B    N  
ANISOU   58  NH1 ARG B  12     7958   6145  19513    956   -342  -1675  B    N  
ATOM     59  NH2 ARG B  12     -59.957 -24.292  15.592  1.00115.29      B    N  
ANISOU   59  NH2 ARG B  12    11209   9531  23064   1074   -370  -2537  B    N  
ATOM     60  N   VAL B  13     -55.410 -18.017  17.934  1.00 48.40      B    N  
ANISOU   60  N   VAL B  13     3413   2871  12108   1117    -80  -1310  B    N  
ATOM     61  CA  VAL B  13     -55.464 -16.562  17.778  1.00 40.60      B    C  
ANISOU   61  CA  VAL B  13     2538   2232  10656   1064    -40  -1283  B    C  
ATOM     62  C   VAL B  13     -54.284 -15.930  18.543  1.00 53.50      B    C  
ANISOU   62  C   VAL B  13     4236   4032  12058   1078    -25  -1014  B    C  
ATOM     63  O   VAL B  13     -54.174 -16.101  19.758  1.00 51.39      B    O  
ANISOU   63  O   VAL B  13     3991   3679  11857   1023     -4   -704  B    O  
ATOM     64  CB  VAL B  13     -56.789 -16.018  18.359  1.00 39.36      B    C  
ANISOU   64  CB  VAL B  13     2473   2080  10400    914     -4  -1145  B    C  
ATOM     65  CG1 VAL B  13     -56.905 -14.495  18.218  1.00 37.31      B    C  
ANISOU   65  CG1 VAL B  13     2322   2147   9708    861     33  -1123  B    C  
ATOM     66  CG2 VAL B  13     -57.949 -16.664  17.708  1.00 46.87      B    C  
ANISOU   66  CG2 VAL B  13     3367   2874  11567    886    -12  -1372  B    C  
ATOM     67  N   CYS B  14     -53.390 -15.229  17.840  1.00 53.55      B    N  
ANISOU   67  N   CYS B  14     4248   4304  11794   1151    -38  -1122  B    N  
ATOM     68  CA  CYS B  14     -52.313 -14.463  18.492  1.00 37.31      B    C  
ANISOU   68  CA  CYS B  14     2262   2444   9470   1149    -25   -879  B    C  
ATOM     69  C   CYS B  14     -52.587 -12.963  18.365  1.00 53.03      B    C  
ANISOU   69  C   CYS B  14     4344   4706  11099   1067    -12   -851  B    C  
ATOM     70  O   CYS B  14     -52.781 -12.443  17.257  1.00 46.64      B    O  
ANISOU   70  O   CYS B  14     3496   4071  10155   1092    -35  -1063  B    O  
ATOM     71  CB  CYS B  14     -50.960 -14.774  17.877  1.00 39.93      B    C  
ANISOU   71  CB  CYS B  14     2524   2883   9765   1295    -69   -969  B    C  
ATOM     72  SG  CYS B  14     -49.619 -13.881  18.648  1.00 45.79      B    S  
ANISOU   72  SG  CYS B  14     3352   3873  10171   1284    -52   -668  B    S  
ATOM     73  N   ILE B  15     -52.623 -12.277  19.504  1.00 45.46      B    N  
ANISOU   73  N   ILE B  15     3478   3797   9999    970     21   -591  B    N  
ATOM     74  CA  ILE B  15     -52.946 -10.866  19.527  1.00 36.49      B    C  
ANISOU   74  CA  ILE B  15     2423   2866   8575    887     26   -562  B    C  
ATOM     75  C   ILE B  15     -51.699 -10.032  19.829  1.00 47.14      B    C  
ANISOU   75  C   ILE B  15     3807   4423   9679    897     10   -417  B    C  
ATOM     76  O   ILE B  15     -50.998 -10.265  20.825  1.00 41.39      B    O  
ANISOU   76  O   ILE B  15     3091   3686   8951    892     35   -211  B    O  
ATOM     77  CB  ILE B  15     -54.013 -10.528  20.568  1.00 33.10      B    C  
ANISOU   77  CB  ILE B  15     2059   2376   8141    769     62   -422  B    C  
ATOM     78  CG1 ILE B  15     -55.316 -11.236  20.250  1.00 32.22      B    C  
ANISOU   78  CG1 ILE B  15     1922   2085   8235    744     70   -546  B    C  
ATOM     79  CG2 ILE B  15     -54.230  -9.048  20.589  1.00 29.82      B    C  
ANISOU   79  CG2 ILE B  15     1718   2157   7456    701     58   -411  B    C  
ATOM     80  CD1 ILE B  15     -56.239 -11.314  21.439  1.00 36.55      B    C  
ANISOU   80  CD1 ILE B  15     2497   2560   8830    648     87   -357  B    C  
ATOM     81  N   ILE B  16     -51.430  -9.055  18.969  1.00 37.07      B    N  
ANISOU   81  N   ILE B  16     2529   3358   8199    906    -30   -505  B    N  
ATOM     82  CA  ILE B  16     -50.259  -8.210  19.134  1.00 45.34      B    C  
ANISOU   82  CA  ILE B  16     3601   4610   9018    909    -64   -370  B    C  
ATOM     83  C   ILE B  16     -50.687  -6.815  19.550  1.00 38.30      B    C  
ANISOU   83  C   ILE B  16     2779   3811   7962    796    -68   -294  B    C  
ATOM     84  O   ILE B  16     -51.332  -6.111  18.772  1.00 28.90      B    O  
ANISOU   84  O   ILE B  16     1565   2690   6725    771    -90   -401  B    O  
ATOM     85  CB  ILE B  16     -49.469  -8.102  17.840  1.00 39.04      B    C  
ANISOU   85  CB  ILE B  16     2706   4014   8114   1008   -136   -487  B    C  
ATOM     86  CG1 ILE B  16     -49.194  -9.505  17.277  1.00 36.83      B    C  
ANISOU   86  CG1 ILE B  16     2332   3637   8024   1137   -144   -642  B    C  
ATOM     87  CG2 ILE B  16     -48.225  -7.345  18.111  1.00 31.38      B    C  
ANISOU   87  CG2 ILE B  16     1763   3241   6919   1004   -179   -311  B    C  
ATOM     88  CD1 ILE B  16     -48.410  -9.535  15.967  1.00 33.54      B    C  
ANISOU   88  CD1 ILE B  16     1777   3475   7494   1261   -228   -793  B    C  
ATOM     89  N   GLY B  17     -50.339  -6.430  20.780  1.00 28.64      B    N  
ANISOU   89  N   GLY B  17     1617   2602   6664    734    -43   -117  B    N  
ATOM     90  CA  GLY B  17     -50.730  -5.139  21.308  1.00 29.25      B    C  
ANISOU   90  CA  GLY B  17     1748   2749   6618    634    -56    -74  B    C  
ATOM     91  C   GLY B  17     -51.463  -5.261  22.623  1.00 40.65      B    C  
ANISOU   91  C   GLY B  17     3221   4116   8110    566     -3      3  B    C  
ATOM     92  O   GLY B  17     -51.838  -6.365  23.008  1.00 41.26      B    O  
ANISOU   92  O   GLY B  17     3267   4071   8338    587     40     37  B    O  
ATOM     93  N   SER B  18     -51.661  -4.137  23.318  1.00 32.85      B    N  
ANISOU   93  N   SER B  18     2264   3212   7006    489    -19     31  B    N  
ATOM     94  CA  SER B  18     -52.226  -4.195  24.661  1.00 28.04      B    C  
ANISOU   94  CA  SER B  18     1639   2615   6398    435     19    106  B    C  
ATOM     95  C   SER B  18     -53.110  -3.003  25.033  1.00 39.85      B    C  
ANISOU   95  C   SER B  18     3164   4156   7822    366    -13     21  B    C  
ATOM     96  O   SER B  18     -53.236  -2.677  26.205  1.00 38.10      B    O  
ANISOU   96  O   SER B  18     2903   4037   7533    325     -6     68  B    O  
ATOM     97  CB  SER B  18     -51.123  -4.397  25.703  1.00 33.81      B    C  
ANISOU   97  CB  SER B  18     2319   3477   7050    433     52    276  B    C  
ATOM     98  OG  SER B  18     -50.213  -3.319  25.645  1.00 43.54      B    O  
ANISOU   98  OG  SER B  18     3578   4840   8127    407     10    275  B    O  
ATOM     99  N   GLY B  19     -53.728  -2.359  24.037  1.00 39.77      B    N  
ANISOU   99  N   GLY B  19     3194   4091   7826    360    -47   -108  B    N  
ATOM    100  CA  GLY B  19     -54.718  -1.332  24.310  1.00 35.20      B    C  
ANISOU  100  CA  GLY B  19     2641   3521   7213    306    -72   -196  B    C  
ATOM    101  C   GLY B  19     -56.136  -1.901  24.425  1.00 40.98      B    C  
ANISOU  101  C   GLY B  19     3387   4181   8004    300    -38   -242  B    C  
ATOM    102  O   GLY B  19     -56.332  -3.115  24.530  1.00 45.21      B    O  
ANISOU  102  O   GLY B  19     3900   4654   8625    326      1   -186  B    O  
ATOM    103  N   PRO B  20     -57.138  -1.023  24.391  1.00 24.73      B    N  
ANISOU  103  N   PRO B  20     1359   2127   5911    267    -58   -338  B    N  
ATOM    104  CA  PRO B  20     -58.549  -1.431  24.401  1.00 30.43      B    C  
ANISOU  104  CA  PRO B  20     2103   2805   6653    258    -30   -381  B    C  
ATOM    105  C   PRO B  20     -58.879  -2.438  23.316  1.00 35.37      B    C  
ANISOU  105  C   PRO B  20     2736   3322   7381    287     16   -409  B    C  
ATOM    106  O   PRO B  20     -59.621  -3.383  23.583  1.00 46.21      B    O  
ANISOU  106  O   PRO B  20     4103   4642   8813    285     42   -379  B    O  
ATOM    107  CB  PRO B  20     -59.317  -0.116  24.141  1.00 29.69      B    C  
ANISOU  107  CB  PRO B  20     2045   2730   6506    230    -58   -491  B    C  
ATOM    108  CG  PRO B  20     -58.359   0.981  24.532  1.00 24.22      B    C  
ANISOU  108  CG  PRO B  20     1329   2091   5781    215   -119   -497  B    C  
ATOM    109  CD  PRO B  20     -56.977   0.440  24.278  1.00 33.43      B    C  
ANISOU  109  CD  PRO B  20     2470   3264   6968    237   -114   -405  B    C  
ATOM    110  N   ALA B  21     -58.356  -2.235  22.112  1.00 25.87      B    N  
ANISOU  110  N   ALA B  21     1520   2108   6203    312     18   -466  B    N  
ATOM    111  CA  ALA B  21     -58.647  -3.125  20.983  1.00 25.76      B    C  
ANISOU  111  CA  ALA B  21     1475   2035   6277    347     60   -543  B    C  
ATOM    112  C   ALA B  21     -58.134  -4.544  21.245  1.00 38.49      B    C  
ANISOU  112  C   ALA B  21     3056   3554   8014    391     72   -493  B    C  
ATOM    113  O   ALA B  21     -58.905  -5.517  21.194  1.00 42.42      B    O  
ANISOU  113  O   ALA B  21     3546   3948   8623    391    100   -522  B    O  
ATOM    114  CB  ALA B  21     -58.062  -2.559  19.684  1.00 31.08      B    C  
ANISOU  114  CB  ALA B  21     2084   2797   6927    376     45   -601  B    C  
ATOM    115  N   ALA B  22     -56.840  -4.659  21.546  1.00 29.64      B    N  
ANISOU  115  N   ALA B  22     1911   2465   6886    424     47   -409  B    N  
ATOM    116  CA  ALA B  22     -56.210  -5.969  21.853  1.00 33.01      B    C  
ANISOU  116  CA  ALA B  22     2295   2800   7448    473     60   -336  B    C  
ATOM    117  C   ALA B  22     -56.948  -6.685  22.978  1.00 45.28      B    C  
ANISOU  117  C   ALA B  22     3837   4278   9090    437     79   -222  B    C  
ATOM    118  O   ALA B  22     -57.334  -7.848  22.840  1.00 45.60      B    O  
ANISOU  118  O   ALA B  22     3838   4173   9317    456     93   -222  B    O  
ATOM    119  CB  ALA B  22     -54.707  -5.806  22.206  1.00 28.31      B    C  
ANISOU  119  CB  ALA B  22     1682   2292   6781    505     40   -226  B    C  
ATOM    120  N   HIS B  23     -57.176  -5.976  24.083  1.00 36.77      B    N  
ANISOU  120  N   HIS B  23     2769   3314   7888    384     67   -128  B    N  
ATOM    121  CA  HIS B  23     -57.841  -6.588  25.217  1.00 38.74      B    C  
ANISOU  121  CA  HIS B  23     2959   3571   8187    352     70     14  B    C  
ATOM    122  C   HIS B  23     -59.292  -6.988  24.973  1.00 35.41      B    C  
ANISOU  122  C   HIS B  23     2555   3065   7831    323     69    -37  B    C  
ATOM    123  O   HIS B  23     -59.733  -8.026  25.439  1.00 45.56      B    O  
ANISOU  123  O   HIS B  23     3771   4275   9263    314     65     85  B    O  
ATOM    124  CB  HIS B  23     -57.667  -5.774  26.493  1.00 27.69      B    C  
ANISOU  124  CB  HIS B  23     1519   2382   6620    316     52    110  B    C  
ATOM    125  CG  HIS B  23     -56.313  -5.927  27.104  1.00 39.95      B    C  
ANISOU  125  CG  HIS B  23     3001   4026   8151    335     70    243  B    C  
ATOM    126  CD2 HIS B  23     -55.290  -5.043  27.265  1.00 29.08      B    C  
ANISOU  126  CD2 HIS B  23     1641   2774   6635    333     65    227  B    C  
ATOM    127  ND1 HIS B  23     -55.852  -7.133  27.596  1.00 39.56      B    N  
ANISOU  127  ND1 HIS B  23     2847   3940   8243    358    102    430  B    N  
ATOM    128  CE1 HIS B  23     -54.628  -6.974  28.068  1.00 46.85      B    C  
ANISOU  128  CE1 HIS B  23     3725   4988   9088    370    128    528  B    C  
ATOM    129  NE2 HIS B  23     -54.259  -5.721  27.869  1.00 42.95      B    N  
ANISOU  129  NE2 HIS B  23     3309   4596   8415    354    104    401  B    N  
ATOM    130  N   THR B  24     -60.039  -6.201  24.225  1.00 31.27      B    N  
ANISOU  130  N   THR B  24     2114   2556   7212    306     72   -194  B    N  
ATOM    131  CA  THR B  24     -61.391  -6.638  23.901  1.00 31.05      B    C  
ANISOU  131  CA  THR B  24     2107   2459   7230    277     83   -244  B    C  
ATOM    132  C   THR B  24     -61.330  -7.850  22.987  1.00 41.22      B    C  
ANISOU  132  C   THR B  24     3362   3560   8739    309    107   -312  B    C  
ATOM    133  O   THR B  24     -62.108  -8.774  23.136  1.00 55.48      B    O  
ANISOU  133  O   THR B  24     5136   5260  10682    286    101   -266  B    O  
ATOM    134  CB  THR B  24     -62.206  -5.560  23.223  1.00 25.78      B    C  
ANISOU  134  CB  THR B  24     1520   1862   6412    253    100   -390  B    C  
ATOM    135  CG2 THR B  24     -63.631  -6.057  22.964  1.00 25.79      B    C  
ANISOU  135  CG2 THR B  24     1544   1821   6431    218    121   -422  B    C  
ATOM    136  OG1 THR B  24     -62.264  -4.446  24.098  1.00 34.66      B    O  
ANISOU  136  OG1 THR B  24     2663   3137   7371    232     66   -356  B    O  
ATOM    137  N   ALA B  25     -60.396  -7.854  22.043  1.00 38.87      B    N  
ANISOU  137  N   ALA B  25     3053   3234   8482    365    120   -427  B    N  
ATOM    138  CA  ALA B  25     -60.207  -9.027  21.201  1.00 28.91      B    C  
ANISOU  138  CA  ALA B  25     1731   1813   7442    415    130   -532  B    C  
ATOM    139  C   ALA B  25     -59.866 -10.241  22.060  1.00 43.67      B    C  
ANISOU  139  C   ALA B  25     3528   3527   9536    428    107   -361  B    C  
ATOM    140  O   ALA B  25     -60.401 -11.324  21.826  1.00 38.49      B    O  
ANISOU  140  O   ALA B  25     2820   2691   9114    429     99   -393  B    O  
ATOM    141  CB  ALA B  25     -59.139  -8.777  20.216  1.00 33.85      B    C  
ANISOU  141  CB  ALA B  25     2326   2501   8036    486    130   -659  B    C  
ATOM    142  N   ALA B  26     -59.004 -10.057  23.066  1.00 38.32      B    N  
ANISOU  142  N   ALA B  26     2826   2928   8805    432     95   -169  B    N  
ATOM    143  CA  ALA B  26     -58.623 -11.165  23.967  1.00 42.23      B    C  
ANISOU  143  CA  ALA B  26     3214   3316   9515    442     83     48  B    C  
ATOM    144  C   ALA B  26     -59.796 -11.687  24.770  1.00 41.27      B    C  
ANISOU  144  C   ALA B  26     3035   3158   9488    374     57    207  B    C  
ATOM    145  O   ALA B  26     -59.951 -12.893  24.936  1.00 47.45      B    O  
ANISOU  145  O   ALA B  26     3717   3751  10561    378     36    314  B    O  
ATOM    146  CB  ALA B  26     -57.496 -10.758  24.923  1.00 36.84      B    C  
ANISOU  146  CB  ALA B  26     2495   2795   8707    452     94    234  B    C  
ATOM    147  N   ILE B  27     -60.602 -10.769  25.290  1.00 34.38      B    N  
ANISOU  147  N   ILE B  27     2210   2474   8380    317     47    235  B    N  
ATOM    148  CA  ILE B  27     -61.763 -11.129  26.092  1.00 33.06      B    C  
ANISOU  148  CA  ILE B  27     1978   2348   8236    255      8    400  B    C  
ATOM    149  C   ILE B  27     -62.706 -12.001  25.286  1.00 39.74      B    C  
ANISOU  149  C   ILE B  27     2838   2971   9292    236     -4    303  B    C  
ATOM    150  O   ILE B  27     -63.078 -13.063  25.766  1.00 43.25      B    O  
ANISOU  150  O   ILE B  27     3166   3294   9974    211    -46    487  B    O  
ATOM    151  CB  ILE B  27     -62.445  -9.884  26.654  1.00 39.24      B    C  
ANISOU  151  CB  ILE B  27     2817   3395   8699    215     -7    387  B    C  
ATOM    152  CG1 ILE B  27     -61.489  -9.196  27.627  1.00 36.21      B    C  
ANISOU  152  CG1 ILE B  27     2369   3232   8156    230     -6    492  B    C  
ATOM    153  CG2 ILE B  27     -63.737 -10.229  27.296  1.00 31.23      B    C  
ANISOU  153  CG2 ILE B  27     1740   2455   7670    161    -59    529  B    C  
ATOM    154  CD1 ILE B  27     -62.006  -7.920  28.174  1.00 29.55      B    C  
ANISOU  154  CD1 ILE B  27     1562   2641   7026    206    -31    430  B    C  
ATOM    155  N   TYR B  28     -63.041 -11.595  24.052  1.00 38.57      B    N  
ANISOU  155  N   TYR B  28     2803   2775   9075    247     35     26  B    N  
ATOM    156  CA  TYR B  28     -63.871 -12.438  23.173  1.00 42.87      B    C  
ANISOU  156  CA  TYR B  28     3345   3126   9817    231     37   -113  B    C  
ATOM    157  C   TYR B  28     -63.196 -13.746  22.714  1.00 43.44      B    C  
ANISOU  157  C   TYR B  28     3316   2924  10267    286     21   -162  B    C  
ATOM    158  O   TYR B  28     -63.812 -14.806  22.738  1.00 51.67      B    O  
ANISOU  158  O   TYR B  28     4282   3766  11583    256    -18   -115  B    O  
ATOM    159  CB  TYR B  28     -64.442 -11.674  21.980  1.00 31.33      B    C  
ANISOU  159  CB  TYR B  28     1987   1745   8172    228     95   -388  B    C  
ATOM    160  CG  TYR B  28     -65.620 -10.838  22.368  1.00 34.03      B    C  
ANISOU  160  CG  TYR B  28     2410   2269   8252    162    100   -336  B    C  
ATOM    161  CD1 TYR B  28     -65.450  -9.613  23.007  1.00 30.75      B    C  
ANISOU  161  CD1 TYR B  28     2048   2066   7569    159     96   -271  B    C  
ATOM    162  CD2 TYR B  28     -66.917 -11.260  22.097  1.00 30.24      B    C  
ANISOU  162  CD2 TYR B  28     1947   1752   7791    104    103   -364  B    C  
ATOM    163  CE1 TYR B  28     -66.546  -8.834  23.370  1.00 33.03      B    C  
ANISOU  163  CE1 TYR B  28     2402   2526   7621    113     92   -244  B    C  
ATOM    164  CE2 TYR B  28     -68.011 -10.484  22.462  1.00 35.14      B    C  
ANISOU  164  CE2 TYR B  28     2643   2562   8145     52    105   -309  B    C  
ATOM    165  CZ  TYR B  28     -67.811  -9.268  23.098  1.00 44.61      B    C  
ANISOU  165  CZ  TYR B  28     3893   3970   9086     63     98   -256  B    C  
ATOM    166  OH  TYR B  28     -68.882  -8.499  23.483  1.00 48.93      B    O  
ANISOU  166  OH  TYR B  28     4505   4706   9378     27     90   -221  B    O  
ATOM    167  N   ALA B  29     -61.939 -13.684  22.293  1.00 41.41      B    N  
ANISOU  167  N   ALA B  29     3048   2652  10034    367     42   -257  B    N  
ATOM    168  CA  ALA B  29     -61.262 -14.895  21.813  1.00 39.30      B    C  
ANISOU  168  CA  ALA B  29     2679   2131  10121    438     22   -337  B    C  
ATOM    169  C   ALA B  29     -61.173 -15.914  22.929  1.00 56.47      B    C  
ANISOU  169  C   ALA B  29     4728   4142  12587    416    -28    -25  B    C  
ATOM    170  O   ALA B  29     -61.496 -17.091  22.734  1.00 61.72      B    O  
ANISOU  170  O   ALA B  29     5294   4534  13623    418    -71    -37  B    O  
ATOM    171  CB  ALA B  29     -59.877 -14.582  21.292  1.00 38.43      B    C  
ANISOU  171  CB  ALA B  29     2573   2092   9937    536     42   -455  B    C  
ATOM    172  N   ALA B  30     -60.730 -15.460  24.096  1.00 48.81      B    N  
ANISOU  172  N   ALA B  30     3732   3353  11462    396    -25    257  B    N  
ATOM    173  CA  ALA B  30     -60.650 -16.326  25.263  1.00 39.63      B    C  
ANISOU  173  CA  ALA B  30     2401   2119  10539    369    -64    614  B    C  
ATOM    174  C   ALA B  30     -62.022 -16.882  25.678  1.00 59.02      B    C  
ANISOU  174  C   ALA B  30     4784   4503  13136    279   -129    767  B    C  
ATOM    175  O   ALA B  30     -62.161 -18.069  25.932  1.00 60.94      B    O  
ANISOU  175  O   ALA B  30     4876   4508  13771    268   -183    935  B    O  
ATOM    176  CB  ALA B  30     -60.005 -15.606  26.416  1.00 38.80      B    C  
ANISOU  176  CB  ALA B  30     2255   2308  10178    358    -39    863  B    C  
ATOM    177  N   ARG B  31     -63.048 -16.049  25.743  1.00 45.21      B    N  
ANISOU  177  N   ARG B  31     3133   2954  11088    217   -131    723  B    N  
ATOM    178  CA  ARG B  31     -64.347 -16.585  26.121  1.00 44.93      B    C  
ANISOU  178  CA  ARG B  31     3031   2883  11159    134   -201    883  B    C  
ATOM    179  C   ARG B  31     -64.891 -17.582  25.102  1.00 54.34      B    C  
ANISOU  179  C   ARG B  31     4221   3731  12695    125   -225    686  B    C  
ATOM    180  O   ARG B  31     -65.679 -18.462  25.459  1.00 55.67      B    O  
ANISOU  180  O   ARG B  31     4274   3758  13120     62   -304    876  B    O  
ATOM    181  CB  ARG B  31     -65.355 -15.473  26.420  1.00 39.83      B    C  
ANISOU  181  CB  ARG B  31     2490   2546  10097     77   -201    875  B    C  
ATOM    182  CG  ARG B  31     -64.930 -14.689  27.634  1.00 55.97      B    C  
ANISOU  182  CG  ARG B  31     4468   4929  11871     80   -206   1093  B    C  
ATOM    183  CD  ARG B  31     -65.974 -13.725  28.087  1.00 68.97      B    C  
ANISOU  183  CD  ARG B  31     6174   6880  13151     36   -232   1104  B    C  
ATOM    184  NE  ARG B  31     -67.084 -14.399  28.760  1.00 58.54      B    N  
ANISOU  184  NE  ARG B  31     4717   5620  11904    -31   -327   1371  B    N  
ATOM    185  CZ  ARG B  31     -68.317 -14.360  28.296  1.00 62.48      B    C  
ANISOU  185  CZ  ARG B  31     5313   6108  12321    -79   -351   1284  B    C  
ATOM    186  NH1 ARG B  31     -68.560 -13.686  27.170  1.00 76.42      B    N  
ANISOU  186  NH1 ARG B  31     7293   7808  13934    -67   -271    941  B    N  
ATOM    187  NH2 ARG B  31     -69.293 -14.982  28.945  1.00 53.25      B    N  
ANISOU  187  NH2 ARG B  31     4008   5016  11209   -143   -453   1559  B    N  
ATOM    188  N   ALA B  32     -64.470 -17.453  23.845  1.00 48.56      B    N  
ANISOU  188  N   ALA B  32     3592   2888  11972    189   -166    311  B    N  
ATOM    189  CA  ALA B  32     -64.914 -18.369  22.807  1.00 42.28      B    C  
ANISOU  189  CA  ALA B  32     2769   1801  11494    194   -184     58  B    C  
ATOM    190  C   ALA B  32     -64.009 -19.604  22.863  1.00 51.84      B    C  
ANISOU  190  C   ALA B  32     3820   2688  13189    259   -231    112  B    C  
ATOM    191  O   ALA B  32     -64.021 -20.466  21.975  1.00 55.87      B    O  
ANISOU  191  O   ALA B  32     4274   2918  14036    297   -253   -145  B    O  
ATOM    192  CB  ALA B  32     -64.878 -17.731  21.457  1.00 40.93      B    C  
ANISOU  192  CB  ALA B  32     2718   1715  11119    240   -106   -361  B    C  
ATOM    193  N   GLU B  33     -63.237 -19.683  23.938  1.00 50.88      B    N  
ANISOU  193  N   GLU B  33     3605   2622  13106    275   -245    446  B    N  
ATOM    194  CA  GLU B  33     -62.398 -20.844  24.190  1.00 65.53      B    C  
ANISOU  194  CA  GLU B  33     5286   4186  15426    331   -286    583  B    C  
ATOM    195  C   GLU B  33     -61.359 -21.070  23.098  1.00 68.94      B    C  
ANISOU  195  C   GLU B  33     5748   4467  15977    459   -251    219  B    C  
ATOM    196  O   GLU B  33     -61.085 -22.200  22.710  1.00 66.27      B    O  
ANISOU  196  O   GLU B  33     5287   3787  16103    513   -301    125  B    O  
ATOM    197  CB  GLU B  33     -63.268 -22.079  24.390  1.00 60.27      B    C  
ANISOU  197  CB  GLU B  33     4459   3202  15237    263   -388    738  B    C  
ATOM    198  CG  GLU B  33     -63.825 -22.153  25.797  1.00 76.52      B    C  
ANISOU  198  CG  GLU B  33     6378   5420  17278    165   -447   1251  B    C  
ATOM    199  CD  GLU B  33     -64.944 -23.145  25.931  1.00 97.10      B    C  
ANISOU  199  CD  GLU B  33     8848   7781  20266     71   -562   1412  B    C  
ATOM    200  OE1 GLU B  33     -65.718 -23.308  24.968  1.00101.86      B    O  
ANISOU  200  OE1 GLU B  33     9549   8226  20929     46   -574   1090  B    O  
ATOM    201  OE2 GLU B  33     -65.052 -23.761  27.008  1.00115.22      B    O  
ANISOU  201  OE2 GLU B  33    10917  10067  22797     20   -641   1876  B    O  
ATOM    202  N   LEU B  34     -60.781 -19.985  22.602  1.00 64.34      B    N  
ANISOU  202  N   LEU B  34     5312   4152  14984    511   -178     16  B    N  
ATOM    203  CA  LEU B  34     -59.780 -20.112  21.567  1.00 57.22      B    C  
ANISOU  203  CA  LEU B  34     4419   3191  14133    638   -158   -312  B    C  
ATOM    204  C   LEU B  34     -58.384 -20.000  22.165  1.00 62.53      B    C  
ANISOU  204  C   LEU B  34     5063   3951  14748    712   -131   -114  B    C  
ATOM    205  O   LEU B  34     -57.395 -20.097  21.434  1.00 62.43      B    O  
ANISOU  205  O   LEU B  34     5047   3927  14747    829   -121   -334  B    O  
ATOM    206  CB  LEU B  34     -59.970 -19.052  20.493  1.00 46.38      B    C  
ANISOU  206  CB  LEU B  34     3183   2073  12368    655   -105   -656  B    C  
ATOM    207  CG  LEU B  34     -61.231 -19.208  19.665  1.00 55.68      B    C  
ANISOU  207  CG  LEU B  34     4372   3191  13595    601   -110   -914  B    C  
ATOM    208  CD1 LEU B  34     -61.486 -17.948  18.866  1.00 47.94      B    C  
ANISOU  208  CD1 LEU B  34     3510   2541  12163    595    -41  -1133  B    C  
ATOM    209  CD2 LEU B  34     -61.089 -20.419  18.778  1.00 47.19      B    C  
ANISOU  209  CD2 LEU B  34     3160   1816  12955    681   -159  -1218  B    C  
ATOM    210  N   LYS B  35     -58.301 -19.805  23.485  1.00 46.63      B    N  
ANISOU  210  N   LYS B  35     3005   2060  12652    647   -119    300  B    N  
ATOM    211  CA  LYS B  35     -57.004 -19.739  24.172  1.00 46.17      B    C  
ANISOU  211  CA  LYS B  35     2897   2112  12534    703    -78    528  B    C  
ATOM    212  C   LYS B  35     -56.025 -18.785  23.489  1.00 54.72      B    C  
ANISOU  212  C   LYS B  35     4118   3425  13246    783    -28    297  B    C  
ATOM    213  O   LYS B  35     -55.014 -19.208  22.962  1.00 61.67      B    O  
ANISOU  213  O   LYS B  35     4969   4222  14238    895    -28    173  B    O  
ATOM    214  CB  LYS B  35     -56.358 -21.128  24.230  1.00 56.03      B    C  
ANISOU  214  CB  LYS B  35     3970   3025  14295    781   -112    620  B    C  
ATOM    215  CG  LYS B  35     -56.883 -22.032  25.329  1.00 65.48      B    C  
ANISOU  215  CG  LYS B  35     4965   4057  15858    703   -155   1036  B    C  
ATOM    216  CD  LYS B  35     -55.886 -23.129  25.631  1.00 85.54      B    C  
ANISOU  216  CD  LYS B  35     7322   6355  18822    787   -159   1224  B    C  
ATOM    217  CE  LYS B  35     -56.146 -23.732  26.999  1.00112.94      B    C  
ANISOU  217  CE  LYS B  35    10553   9819  22541    702   -177   1769  B    C  
ATOM    218  NZ  LYS B  35     -57.451 -24.451  27.060  1.00125.51      B    N  
ANISOU  218  NZ  LYS B  35    12034  11159  24495    611   -282   1849  B    N  
ATOM    219  N   PRO B  36     -56.330 -17.489  23.472  1.00 45.82      B    N  
ANISOU  219  N   PRO B  36     3129   2592  11688    729      4    241  B    N  
ATOM    220  CA  PRO B  36     -55.457 -16.574  22.736  1.00 43.88      B    C  
ANISOU  220  CA  PRO B  36     2993   2555  11123    795     32     35  B    C  
ATOM    221  C   PRO B  36     -54.157 -16.325  23.462  1.00 51.67      B    C  
ANISOU  221  C   PRO B  36     3963   3701  11968    832     70    260  B    C  
ATOM    222  O   PRO B  36     -54.112 -16.320  24.684  1.00 54.16      B    O  
ANISOU  222  O   PRO B  36     4214   4101  12264    772     97    581  B    O  
ATOM    223  CB  PRO B  36     -56.244 -15.274  22.750  1.00 38.00      B    C  
ANISOU  223  CB  PRO B  36     2373   2051  10013    708     49    -13  B    C  
ATOM    224  CG  PRO B  36     -57.072 -15.383  24.022  1.00 48.99      B    C  
ANISOU  224  CG  PRO B  36     3712   3459  11444    606     45    287  B    C  
ATOM    225  CD  PRO B  36     -57.537 -16.806  23.954  1.00 42.07      B    C  
ANISOU  225  CD  PRO B  36     2710   2257  11016    613      1    323  B    C  
ATOM    226  N   VAL B  37     -53.109 -16.084  22.691  1.00 55.71      B    N  
ANISOU  226  N   VAL B  37     4517   4299  12353    928     72     92  B    N  
ATOM    227  CA  VAL B  37     -51.862 -15.597  23.236  1.00 41.64      B    C  
ANISOU  227  CA  VAL B  37     2752   2728  10341    955    111    273  B    C  
ATOM    228  C   VAL B  37     -51.716 -14.135  22.862  1.00 55.39      B    C  
ANISOU  228  C   VAL B  37     4623   4756  11666    923    111    161  B    C  
ATOM    229  O   VAL B  37     -51.768 -13.777  21.677  1.00 55.81      B    O  
ANISOU  229  O   VAL B  37     4720   4855  11632    969     74   -111  B    O  
ATOM    230  CB  VAL B  37     -50.648 -16.352  22.650  1.00 42.70      B    C  
ANISOU  230  CB  VAL B  37     2830   2784  10608   1096     97    194  B    C  
ATOM    231  CG1 VAL B  37     -49.368 -15.686  23.110  1.00 39.07      B    C  
ANISOU  231  CG1 VAL B  37     2413   2594   9836   1115    140    368  B    C  
ATOM    232  CG2 VAL B  37     -50.732 -17.811  22.993  1.00 42.71      B    C  
ANISOU  232  CG2 VAL B  37     2687   2463  11078   1136     89    303  B    C  
ATOM    233  N   LEU B  38     -51.520 -13.300  23.877  1.00 39.88      B    N  
ANISOU  233  N   LEU B  38     2691   3000   9463    846    149    375  B    N  
ATOM    234  CA  LEU B  38     -51.434 -11.875  23.666  1.00 39.07      B    C  
ANISOU  234  CA  LEU B  38     2695   3135   9013    802    141    294  B    C  
ATOM    235  C   LEU B  38     -50.045 -11.372  24.029  1.00 36.43      B    C  
ANISOU  235  C   LEU B  38     2376   3009   8456    827    162    426  B    C  
ATOM    236  O   LEU B  38     -49.544 -11.689  25.107  1.00 46.88      B    O  
ANISOU  236  O   LEU B  38     3631   4392   9790    808    216    672  B    O  
ATOM    237  CB  LEU B  38     -52.521 -11.155  24.484  1.00 32.69      B    C  
ANISOU  237  CB  LEU B  38     1912   2406   8102    688    149    368  B    C  
ATOM    238  CG  LEU B  38     -52.648  -9.632  24.325  1.00 39.20      B    C  
ANISOU  238  CG  LEU B  38     2839   3430   8626    634    131    270  B    C  
ATOM    239  CD1 LEU B  38     -54.049  -9.187  24.576  1.00 30.42      B    C  
ANISOU  239  CD1 LEU B  38     1754   2310   7493    557    121    222  B    C  
ATOM    240  CD2 LEU B  38     -51.674  -8.904  25.222  1.00 30.80      B    C  
ANISOU  240  CD2 LEU B  38     1770   2585   7347    606    153    431  B    C  
ATOM    241  N   PHE B  39     -49.440 -10.585  23.131  1.00 39.04      B    N  
ANISOU  241  N   PHE B  39     2774   3480   8579    862    120    284  B    N  
ATOM    242  CA  PHE B  39     -48.168  -9.904  23.414  1.00 42.57      B    C  
ANISOU  242  CA  PHE B  39     3250   4153   8772    867    125    407  B    C  
ATOM    243  C   PHE B  39     -48.493  -8.484  23.823  1.00 48.67      B    C  
ANISOU  243  C   PHE B  39     4088   5087   9318    762    113    415  B    C  
ATOM    244  O   PHE B  39     -48.820  -7.669  22.963  1.00 44.08      B    O  
ANISOU  244  O   PHE B  39     3552   4547   8650    750     54    258  B    O  
ATOM    245  CB  PHE B  39     -47.281  -9.788  22.168  1.00 43.28      B    C  
ANISOU  245  CB  PHE B  39     3349   4340   8755    966     60    270  B    C  
ATOM    246  CG  PHE B  39     -46.595 -11.049  21.765  1.00 34.65      B    C  
ANISOU  246  CG  PHE B  39     2186   3147   7831   1095     59    247  B    C  
ATOM    247  CD1 PHE B  39     -45.328 -11.347  22.237  1.00 53.27      B    C  
ANISOU  247  CD1 PHE B  39     4531   5611  10100   1145     91    431  B    C  
ATOM    248  CD2 PHE B  39     -47.200 -11.936  20.893  1.00 39.30      B    C  
ANISOU  248  CD2 PHE B  39     2714   3545   8673   1171     26     28  B    C  
ATOM    249  CE1 PHE B  39     -44.683 -12.502  21.862  1.00 34.99      B    C  
ANISOU  249  CE1 PHE B  39     2145   3198   7950   1277     86    404  B    C  
ATOM    250  CE2 PHE B  39     -46.564 -13.096  20.517  1.00 40.35      B    C  
ANISOU  250  CE2 PHE B  39     2766   3570   8994   1301     13    -28  B    C  
ATOM    251  CZ  PHE B  39     -45.303 -13.371  20.990  1.00 35.67      B    C  
ANISOU  251  CZ  PHE B  39     2166   3073   8316   1359     40    161  B    C  
ATOM    252  N   GLU B  40     -48.370  -8.170  25.111  1.00 34.42      B    N  
ANISOU  252  N   GLU B  40     2258   3394   7426    690    164    594  B    N  
ATOM    253  CA  GLU B  40     -48.724  -6.844  25.594  1.00 50.30      B    C  
ANISOU  253  CA  GLU B  40     4311   5545   9255    595    144    567  B    C  
ATOM    254  C   GLU B  40     -47.599  -5.801  25.409  1.00 43.17      B    C  
ANISOU  254  C   GLU B  40     3455   4831   8118    582    107    582  B    C  
ATOM    255  O   GLU B  40     -47.779  -4.616  25.713  1.00 36.04      B    O  
ANISOU  255  O   GLU B  40     2579   4021   7091    507     73    538  B    O  
ATOM    256  CB  GLU B  40     -49.187  -6.914  27.057  1.00 46.84      B    C  
ANISOU  256  CB  GLU B  40     3785   5194   8817    528    201    713  B    C  
ATOM    257  CG  GLU B  40     -48.065  -7.005  28.097  1.00 48.94      B    C  
ANISOU  257  CG  GLU B  40     3967   5672   8957    517    270    926  B    C  
ATOM    258  CD  GLU B  40     -48.619  -7.141  29.500  1.00 55.41      B    C  
ANISOU  258  CD  GLU B  40     4639   6636   9777    458    323   1070  B    C  
ATOM    259  OE1 GLU B  40     -49.812  -6.865  29.648  1.00 49.21      B    O  
ANISOU  259  OE1 GLU B  40     3849   5811   9037    420    286    977  B    O  
ATOM    260  OE2 GLU B  40     -47.893  -7.518  30.447  1.00 52.32      B    O  
ANISOU  260  OE2 GLU B  40     4116   6433   9330    452    403   1283  B    O  
ATOM    261  N   GLY B  41     -46.459  -6.238  24.887  1.00 39.97      B    N  
ANISOU  261  N   GLY B  41     3050   4476   7663    657    101    639  B    N  
ATOM    262  CA  GLY B  41     -45.274  -5.395  24.810  1.00 43.29      B    C  
ANISOU  262  CA  GLY B  41     3501   5097   7851    644     64    707  B    C  
ATOM    263  C   GLY B  41     -44.511  -5.265  26.127  1.00 39.90      B    C  
ANISOU  263  C   GLY B  41     3034   4846   7281    591    143    894  B    C  
ATOM    264  O   GLY B  41     -45.037  -5.515  27.201  1.00 41.99      B    O  
ANISOU  264  O   GLY B  41     3230   5123   7602    545    216    962  B    O  
ATOM    265  N   TRP B  42     -43.242  -4.893  26.038  1.00 48.37      B    N  
ANISOU  265  N   TRP B  42     4128   6098   8153    599    127    991  B    N  
ATOM    266  CA  TRP B  42     -42.502  -4.442  27.213  1.00 45.05      B    C  
ANISOU  266  CA  TRP B  42     3668   5898   7550    528    194   1139  B    C  
ATOM    267  C   TRP B  42     -42.101  -3.023  26.920  1.00 43.02      B    C  
ANISOU  267  C   TRP B  42     3468   5747   7130    458     93   1075  B    C  
ATOM    268  O   TRP B  42     -41.056  -2.775  26.319  1.00 49.65      B    O  
ANISOU  268  O   TRP B  42     4346   6701   7819    483     37   1144  B    O  
ATOM    269  CB  TRP B  42     -41.255  -5.305  27.484  1.00 43.25      B    C  
ANISOU  269  CB  TRP B  42     3407   5807   7218    591    279   1348  B    C  
ATOM    270  CG  TRP B  42     -40.369  -4.747  28.568  1.00 56.25      B    C  
ANISOU  270  CG  TRP B  42     5006   7735   8629    512    352   1498  B    C  
ATOM    271  CD1 TRP B  42     -39.156  -4.141  28.407  1.00 70.51      B    C  
ANISOU  271  CD1 TRP B  42     6861   9741  10188    496    322   1578  B    C  
ATOM    272  CD2 TRP B  42     -40.643  -4.723  29.972  1.00 59.64      B    C  
ANISOU  272  CD2 TRP B  42     5308   8316   9038    438    463   1580  B    C  
ATOM    273  CE2 TRP B  42     -39.556  -4.087  30.602  1.00 61.99      B    C  
ANISOU  273  CE2 TRP B  42     5579   8903   9071    377    507   1683  B    C  
ATOM    274  CE3 TRP B  42     -41.712  -5.166  30.760  1.00 85.99      B    C  
ANISOU  274  CE3 TRP B  42     8525  11608  12540    416    522   1581  B    C  
ATOM    275  NE1 TRP B  42     -38.659  -3.745  29.624  1.00 69.41      B    N  
ANISOU  275  NE1 TRP B  42     6643   9850   9879    410    418   1687  B    N  
ATOM    276  CZ2 TRP B  42     -39.501  -3.891  31.980  1.00 82.63      B    C  
ANISOU  276  CZ2 TRP B  42     8037  11780  11581    300    619   1762  B    C  
ATOM    277  CZ3 TRP B  42     -41.655  -4.972  32.136  1.00 98.53      B    C  
ANISOU  277  CZ3 TRP B  42     9944  13474  14018    344    621   1683  B    C  
ATOM    278  CH2 TRP B  42     -40.554  -4.343  32.729  1.00 97.59      B    C  
ANISOU  278  CH2 TRP B  42     9788  13659  13635    289    674   1761  B    C  
ATOM    279  N   MET B  43     -42.949  -2.089  27.327  1.00 47.29      B    N  
ANISOU  279  N   MET B  43     4002   6251   7716    372     59    947  B    N  
ATOM    280  CA  MET B  43     -42.843  -0.705  26.891  1.00 44.87      B    C  
ANISOU  280  CA  MET B  43     3734   5959   7354    306    -62    858  B    C  
ATOM    281  C   MET B  43     -42.657  -0.626  25.383  1.00 47.68      B    C  
ANISOU  281  C   MET B  43     4135   6247   7733    365   -173    839  B    C  
ATOM    282  O   MET B  43     -41.954   0.240  24.879  1.00 55.40      B    O  
ANISOU  282  O   MET B  43     5122   7316   8611    335   -276    883  B    O  
ATOM    283  CB  MET B  43     -41.701   0.023  27.598  1.00 39.94      B    C  
ANISOU  283  CB  MET B  43     3091   5556   6529    235    -61    953  B    C  
ATOM    284  CG  MET B  43     -41.811   0.048  29.124  1.00 54.29      B    C  
ANISOU  284  CG  MET B  43     4812   7527   8289    174     50    959  B    C  
ATOM    285  SD  MET B  43     -40.238   0.430  29.940  1.00 62.83      B    S  
ANISOU  285  SD  MET B  43     5848   8932   9092    113    105   1115  B    S  
ATOM    286  CE  MET B  43     -40.729   0.032  31.610  1.00 55.98      B    C  
ANISOU  286  CE  MET B  43     4800   8268   8203     78    262   1115  B    C  
ATOM    287  N   ALA B  44     -43.310  -1.512  24.651  1.00 42.72      B    N  
ANISOU  287  N   ALA B  44     3507   5481   7242    449   -160    774  B    N  
ATOM    288  CA  ALA B  44     -43.193  -1.480  23.203  1.00 38.76      B    C  
ANISOU  288  CA  ALA B  44     2998   4976   6751    515   -262    733  B    C  
ATOM    289  C   ALA B  44     -43.523  -0.102  22.700  1.00 43.71      B    C  
ANISOU  289  C   ALA B  44     3614   5602   7395    440   -377    681  B    C  
ATOM    290  O   ALA B  44     -44.550   0.489  23.086  1.00 43.26      B    O  
ANISOU  290  O   ALA B  44     3565   5415   7455    372   -371    572  B    O  
ATOM    291  CB  ALA B  44     -44.110  -2.477  22.584  1.00 38.08      B    C  
ANISOU  291  CB  ALA B  44     2895   4732   6840    594   -228    610  B    C  
ATOM    292  N   ASN B  45     -42.645   0.422  21.855  1.00 26.69      B    N  
ANISOU  292  N   ASN B  45     1419   3598   5124    452   -491    774  B    N  
ATOM    293  CA  ASN B  45     -42.899   1.696  21.206  1.00 31.73      B    C  
ANISOU  293  CA  ASN B  45     2002   4238   5815    387   -618    770  B    C  
ATOM    294  C   ASN B  45     -42.876   2.855  22.210  1.00 45.25      B    C  
ANISOU  294  C   ASN B  45     3744   5901   7549    261   -640    773  B    C  
ATOM    295  O   ASN B  45     -43.448   3.915  21.963  1.00 45.56      B    O  
ANISOU  295  O   ASN B  45     3744   5848   7719    195   -722    725  B    O  
ATOM    296  CB  ASN B  45     -44.257   1.644  20.489  1.00 44.01      B    C  
ANISOU  296  CB  ASN B  45     3520   5651   7552    408   -612    619  B    C  
ATOM    297  CG  ASN B  45     -44.288   2.537  19.263  1.00 44.08      B    C  
ANISOU  297  CG  ASN B  45     3404   5755   7591    397   -746    670  B    C  
ATOM    298  ND2 ASN B  45     -45.484   2.960  18.819  1.00 40.73      B    N  
ANISOU  298  ND2 ASN B  45     2935   5214   7326    372   -744    567  B    N  
ATOM    299  OD1 ASN B  45     -43.237   2.840  18.723  1.00 47.36      B    O  
ANISOU  299  OD1 ASN B  45     3746   6370   7877    411   -852    823  B    O  
ATOM    300  N   ASP B  46     -42.256   2.630  23.362  1.00 30.81      B    N  
ANISOU  300  N   ASP B  46     1962   4139   5607    232   -561    818  B    N  
ATOM    301  CA  ASP B  46     -42.182   3.662  24.387  1.00 41.09      B    C  
ANISOU  301  CA  ASP B  46     3264   5432   6918    119   -577    779  B    C  
ATOM    302  C   ASP B  46     -43.531   4.108  24.942  1.00 49.50      B    C  
ANISOU  302  C   ASP B  46     4324   6317   8166     76   -551    582  B    C  
ATOM    303  O   ASP B  46     -43.702   5.247  25.365  1.00 56.35      B    O  
ANISOU  303  O   ASP B  46     5164   7132   9116     -7   -621    499  B    O  
ATOM    304  CB  ASP B  46     -41.394   4.845  23.891  1.00 46.21      B    C  
ANISOU  304  CB  ASP B  46     3870   6147   7542     52   -735    882  B    C  
ATOM    305  CG  ASP B  46     -39.924   4.509  23.703  1.00 62.52      B    C  
ANISOU  305  CG  ASP B  46     5943   8448   9365     77   -757   1089  B    C  
ATOM    306  OD1 ASP B  46     -39.537   3.374  24.041  1.00 48.71      B    O  
ANISOU  306  OD1 ASP B  46     4234   6794   7479    149   -636   1135  B    O  
ATOM    307  OD2 ASP B  46     -39.160   5.371  23.225  1.00 53.55      B    O  
ANISOU  307  OD2 ASP B  46     4762   7403   8182     25   -899   1220  B    O  
ATOM    308  N   ILE B  47     -44.466   3.170  24.960  1.00 40.63      B    N  
ANISOU  308  N   ILE B  47     3221   5106   7110    137   -457    506  B    N  
ATOM    309  CA  ILE B  47     -45.737   3.318  25.620  1.00 40.10      B    C  
ANISOU  309  CA  ILE B  47     3151   4921   7165    113   -414    341  B    C  
ATOM    310  C   ILE B  47     -45.887   2.066  26.474  1.00 43.67      B    C  
ANISOU  310  C   ILE B  47     3597   5432   7562    157   -275    371  B    C  
ATOM    311  O   ILE B  47     -45.586   0.966  26.022  1.00 35.47      B    O  
ANISOU  311  O   ILE B  47     2575   4399   6501    230   -224    465  B    O  
ATOM    312  CB  ILE B  47     -46.863   3.353  24.601  1.00 37.19      B    C  
ANISOU  312  CB  ILE B  47     2792   4391   6949    144   -446    255  B    C  
ATOM    313  CG1 ILE B  47     -46.812   4.660  23.865  1.00 52.57      B    C  
ANISOU  313  CG1 ILE B  47     4702   6289   8985     92   -579    255  B    C  
ATOM    314  CG2 ILE B  47     -48.189   3.329  25.293  1.00 41.37      B    C  
ANISOU  314  CG2 ILE B  47     3328   4823   7569    131   -393    104  B    C  
ATOM    315  CD1 ILE B  47     -47.199   5.783  24.766  1.00 49.65      B    C  
ANISOU  315  CD1 ILE B  47     4314   5851   8700     13   -622    128  B    C  
ATOM    316  N   ALA B  48     -46.328   2.240  27.711  1.00 30.78      B    N  
ANISOU  316  N   ALA B  48     1914   3862   5918    115   -226    297  B    N  
ATOM    317  CA  ALA B  48     -46.571   1.112  28.597  1.00 42.92      B    C  
ANISOU  317  CA  ALA B  48     3398   5488   7424    147   -103    362  B    C  
ATOM    318  C   ALA B  48     -47.615   0.152  28.025  1.00 47.32      B    C  
ANISOU  318  C   ALA B  48     3985   5875   8118    209    -73    345  B    C  
ATOM    319  O   ALA B  48     -48.492   0.555  27.261  1.00 37.67      B    O  
ANISOU  319  O   ALA B  48     2813   4498   7002    211   -131    226  B    O  
ATOM    320  CB  ALA B  48     -47.025   1.614  29.945  1.00 32.46      B    C  
ANISOU  320  CB  ALA B  48     1966   4309   6057     94    -80    265  B    C  
ATOM    321  N   ALA B  49     -47.516  -1.117  28.392  1.00 40.02      B    N  
ANISOU  321  N   ALA B  49     3016   4981   7206    256     20    474  B    N  
ATOM    322  CA  ALA B  49     -48.611  -2.031  28.125  1.00 37.94      B    C  
ANISOU  322  CA  ALA B  49     2755   4563   7098    297     48    452  B    C  
ATOM    323  C   ALA B  49     -49.849  -1.392  28.712  1.00 36.36      B    C  
ANISOU  323  C   ALA B  49     2526   4367   6922    250     21    320  B    C  
ATOM    324  O   ALA B  49     -49.798  -0.832  29.792  1.00 46.15      B    O  
ANISOU  324  O   ALA B  49     3680   5790   8067    206     27    304  B    O  
ATOM    325  CB  ALA B  49     -48.355  -3.414  28.763  1.00 29.54      B    C  
ANISOU  325  CB  ALA B  49     1601   3542   6079    337    147    638  B    C  
ATOM    326  N   GLY B  50     -50.960  -1.470  27.992  1.00 40.83      B    N  
ANISOU  326  N   GLY B  50     3151   4760   7602    265     -8    216  B    N  
ATOM    327  CA  GLY B  50     -52.163  -0.775  28.393  1.00 39.90      B    C  
ANISOU  327  CA  GLY B  50     3025   4644   7491    230    -45     81  B    C  
ATOM    328  C   GLY B  50     -52.522   0.272  27.357  1.00 45.60      B    C  
ANISOU  328  C   GLY B  50     3836   5236   8255    216   -119    -65  B    C  
ATOM    329  O   GLY B  50     -53.703   0.593  27.112  1.00 39.83      B    O  
ANISOU  329  O   GLY B  50     3135   4425   7575    209   -140   -176  B    O  
ATOM    330  N   GLY B  51     -51.487   0.818  26.738  1.00 29.31      B    N  
ANISOU  330  N   GLY B  51     1799   3172   6164    210   -161    -43  B    N  
ATOM    331  CA  GLY B  51     -51.693   1.679  25.588  1.00 45.42      B    C  
ANISOU  331  CA  GLY B  51     3882   5106   8267    201   -233   -117  B    C  
ATOM    332  C   GLY B  51     -51.763   3.153  25.931  1.00 39.37      B    C  
ANISOU  332  C   GLY B  51     3099   4345   7515    142   -314   -215  B    C  
ATOM    333  O   GLY B  51     -51.465   3.562  27.047  1.00 43.47      B    O  
ANISOU  333  O   GLY B  51     3573   4971   7974    109   -322   -251  B    O  
ATOM    334  N   GLN B  52     -52.177   3.959  24.964  1.00 32.01      B    N  
ANISOU  334  N   GLN B  52     2177   3307   6677    129   -377   -263  B    N  
ATOM    335  CA  GLN B  52     -52.167   5.410  25.133  1.00 34.03      B    C  
ANISOU  335  CA  GLN B  52     2400   3521   7009     74   -472   -343  B    C  
ATOM    336  C   GLN B  52     -52.921   5.913  26.349  1.00 34.10      B    C  
ANISOU  336  C   GLN B  52     2387   3547   7019     55   -480   -508  B    C  
ATOM    337  O   GLN B  52     -52.510   6.884  26.988  1.00 36.72      B    O  
ANISOU  337  O   GLN B  52     2670   3900   7381     13   -551   -593  B    O  
ATOM    338  CB  GLN B  52     -52.693   6.101  23.901  1.00 34.64      B    C  
ANISOU  338  CB  GLN B  52     2460   3485   7217     68   -524   -338  B    C  
ATOM    339  CG  GLN B  52     -51.819   5.925  22.686  1.00 34.65      B    C  
ANISOU  339  CG  GLN B  52     2421   3535   7210     84   -557   -180  B    C  
ATOM    340  CD  GLN B  52     -52.489   6.466  21.442  1.00 48.12      B    C  
ANISOU  340  CD  GLN B  52     4061   5192   9033     84   -587   -155  B    C  
ATOM    341  NE2 GLN B  52     -52.922   5.572  20.546  1.00 39.37      B    N  
ANISOU  341  NE2 GLN B  52     2938   4132   7888    137   -517   -140  B    N  
ATOM    342  OE1 GLN B  52     -52.649   7.668  21.302  1.00 58.63      B    O  
ANISOU  342  OE1 GLN B  52     5331   6446  10499     35   -669   -154  B    O  
ATOM    343  N   LEU B  53     -54.020   5.255  26.672  1.00 30.18      B    N  
ANISOU  343  N   LEU B  53     1912   3064   6493     86   -416   -561  B    N  
ATOM    344  CA  LEU B  53     -54.773   5.590  27.865  1.00 33.27      B    C  
ANISOU  344  CA  LEU B  53     2254   3542   6844     86   -427   -711  B    C  
ATOM    345  C   LEU B  53     -53.913   5.683  29.148  1.00 33.29      B    C  
ANISOU  345  C   LEU B  53     2161   3744   6745     65   -433   -736  B    C  
ATOM    346  O   LEU B  53     -54.250   6.406  30.072  1.00 51.13      B    O  
ANISOU  346  O   LEU B  53     4338   6100   8991     58   -482   -907  B    O  
ATOM    347  CB  LEU B  53     -55.927   4.613  28.033  1.00 35.71      B    C  
ANISOU  347  CB  LEU B  53     2584   3884   7100    123   -358   -699  B    C  
ATOM    348  CG  LEU B  53     -57.337   5.103  27.696  1.00 40.31      B    C  
ANISOU  348  CG  LEU B  53     3205   4379   7731    134   -379   -816  B    C  
ATOM    349  CD1 LEU B  53     -57.369   6.096  26.581  1.00 44.16      B    C  
ANISOU  349  CD1 LEU B  53     3727   4693   8358    115   -425   -845  B    C  
ATOM    350  CD2 LEU B  53     -58.225   3.924  27.377  1.00 34.09      B    C  
ANISOU  350  CD2 LEU B  53     2464   3584   6904    160   -301   -738  B    C  
ATOM    351  N   THR B  54     -52.806   4.963  29.210  1.00 28.72      B    N  
ANISOU  351  N   THR B  54     1574   3252   6085     63   -380   -577  B    N  
ATOM    352  CA  THR B  54     -51.936   5.040  30.387  1.00 46.26      B    C  
ANISOU  352  CA  THR B  54     3687   5701   8190     39   -365   -579  B    C  
ATOM    353  C   THR B  54     -51.211   6.389  30.461  1.00 41.65      B    C  
ANISOU  353  C   THR B  54     3074   5089   7661    -15   -463   -697  B    C  
ATOM    354  O   THR B  54     -50.654   6.726  31.496  1.00 62.22      B    O  
ANISOU  354  O   THR B  54     5568   7892  10181    -42   -465   -773  B    O  
ATOM    355  CB  THR B  54     -50.902   3.907  30.415  1.00 38.52      B    C  
ANISOU  355  CB  THR B  54     2702   4826   7107     52   -273   -355  B    C  
ATOM    356  CG2 THR B  54     -51.565   2.558  30.206  1.00 30.23      B    C  
ANISOU  356  CG2 THR B  54     1675   3741   6071    103   -193   -232  B    C  
ATOM    357  OG1 THR B  54     -49.968   4.112  29.366  1.00 38.14      B    O  
ANISOU  357  OG1 THR B  54     2740   4657   7093     42   -307   -261  B    O  
ATOM    358  N   THR B  55     -51.245   7.156  29.367  1.00 34.77      B    N  
ANISOU  358  N   THR B  55     2278   3990   6944    -33   -546   -705  B    N  
ATOM    359  CA  THR B  55     -50.653   8.504  29.326  1.00 37.38      B    C  
ANISOU  359  CA  THR B  55     2569   4238   7395    -92   -665   -797  B    C  
ATOM    360  C   THR B  55     -51.616   9.654  29.662  1.00 58.04      B    C  
ANISOU  360  C   THR B  55     5133   6744  10175    -98   -757  -1052  B    C  
ATOM    361  O   THR B  55     -51.258  10.823  29.555  1.00 56.50      B    O  
ANISOU  361  O   THR B  55     4894   6424  10148   -146   -872  -1140  B    O  
ATOM    362  CB  THR B  55     -49.912   8.802  27.987  1.00 35.93      B    C  
ANISOU  362  CB  THR B  55     2441   3906   7306   -117   -728   -615  B    C  
ATOM    363  CG2 THR B  55     -49.046   7.600  27.566  1.00 33.70      B    C  
ANISOU  363  CG2 THR B  55     2209   3741   6855    -88   -644   -387  B    C  
ATOM    364  OG1 THR B  55     -50.844   9.103  26.955  1.00 44.38      B    O  
ANISOU  364  OG1 THR B  55     3544   4788   8532    -99   -763   -615  B    O  
ATOM    365  N   THR B  56     -52.823   9.301  30.088  1.00 55.54      B    N  
ANISOU  365  N   THR B  56     4810   6476   9816    -47   -715  -1163  B    N  
ATOM    366  CA  THR B  56     -53.811  10.258  30.549  1.00 37.05      B    C  
ANISOU  366  CA  THR B  56     2409   4081   7588    -32   -795  -1423  B    C  
ATOM    367  C   THR B  56     -54.395   9.871  31.932  1.00 55.81      B    C  
ANISOU  367  C   THR B  56     4668   6751   9785     12   -760  -1584  B    C  
ATOM    368  O   THR B  56     -54.202   8.757  32.409  1.00 80.03      B    O  
ANISOU  368  O   THR B  56     7708  10038  12663     29   -662  -1448  B    O  
ATOM    369  CB  THR B  56     -54.934  10.435  29.498  1.00 54.69      B    C  
ANISOU  369  CB  THR B  56     4732   6092   9954     -5   -804  -1399  B    C  
ATOM    370  CG2 THR B  56     -55.894   9.248  29.491  1.00 43.33      B    C  
ANISOU  370  CG2 THR B  56     3351   4755   8357     48   -697  -1325  B    C  
ATOM    371  OG1 THR B  56     -55.674  11.610  29.795  1.00 53.57      B    O  
ANISOU  371  OG1 THR B  56     4533   5847   9975      5   -904  -1641  B    O  
ATOM    372  N   THR B  57     -55.117  10.785  32.566  1.00 53.80      B    N  
ANISOU  372  N   THR B  57     4321   6519   9601     38   -848  -1866  B    N  
ATOM    373  CA  THR B  57     -55.405  10.688  34.003  1.00 72.60      B    C  
ANISOU  373  CA  THR B  57     6518   9256  11809     77   -851  -2060  B    C  
ATOM    374  C   THR B  57     -56.876  10.491  34.292  1.00 78.38      B    C  
ANISOU  374  C   THR B  57     7229  10085  12466    152   -859  -2160  B    C  
ATOM    375  O   THR B  57     -57.285  10.067  35.385  1.00 87.06      B    O  
ANISOU  375  O   THR B  57     8166  11545  13368    197   -848  -2236  B    O  
ATOM    376  CB  THR B  57     -55.070  12.009  34.704  1.00 70.26      B    C  
ANISOU  376  CB  THR B  57     6075   8980  11637     64   -974  -2388  B    C  
ATOM    377  CG2 THR B  57     -53.571  12.136  34.957  1.00 56.92      B    C  
ANISOU  377  CG2 THR B  57     4330   7365   9933     -9   -963  -2335  B    C  
ATOM    378  OG1 THR B  57     -55.521  13.088  33.873  1.00 59.50      B    O  
ANISOU  378  OG1 THR B  57     4797   7245  10564     58  -1080  -2495  B    O  
ATOM    379  N   ASP B  58     -57.676  10.861  33.315  1.00 61.51      B    N  
ANISOU  379  N   ASP B  58     5234   7656  10480    164   -887  -2153  B    N  
ATOM    380  CA  ASP B  58     -59.092  11.018  33.556  1.00 64.71      B    C  
ANISOU  380  CA  ASP B  58     5623   8123  10840    233   -921  -2299  B    C  
ATOM    381  C   ASP B  58     -59.812  10.790  32.247  1.00 45.80      B    C  
ANISOU  381  C   ASP B  58     3419   5451   8532    230   -872  -2124  B    C  
ATOM    382  O   ASP B  58     -59.745  11.602  31.343  1.00 47.81      B    O  
ANISOU  382  O   ASP B  58     3746   5410   9011    203   -912  -2130  B    O  
ATOM    383  CB  ASP B  58     -59.376  12.409  34.118  1.00 74.86      B    C  
ANISOU  383  CB  ASP B  58     6790   9385  12270    267  -1060  -2662  B    C  
ATOM    384  CG  ASP B  58     -60.849  12.658  34.320  1.00 91.52      B    C  
ANISOU  384  CG  ASP B  58     8887  11560  14327    351  -1106  -2824  B    C  
ATOM    385  OD1 ASP B  58     -61.544  11.748  34.825  1.00 94.12      B    O  
ANISOU  385  OD1 ASP B  58     9179  12182  14401    396  -1059  -2745  B    O  
ATOM    386  OD2 ASP B  58     -61.311  13.766  33.974  1.00 99.99      B    O  
ANISOU  386  OD2 ASP B  58     9977  12393  15620    373  -1196  -3012  B    O  
ATOM    387  N   VAL B  59     -60.431   9.624  32.132  1.00 42.32      B    N  
ANISOU  387  N   VAL B  59     3037   5124   7920    249   -783  -1945  B    N  
ATOM    388  CA  VAL B  59     -61.196   9.256  30.957  1.00 46.07      B    C  
ANISOU  388  CA  VAL B  59     3670   5399   8437    247   -718  -1794  B    C  
ATOM    389  C   VAL B  59     -62.675   9.353  31.332  1.00 46.57      B    C  
ANISOU  389  C   VAL B  59     3723   5583   8389    309   -744  -1912  B    C  
ATOM    390  O   VAL B  59     -63.120   8.735  32.300  1.00 48.98      B    O  
ANISOU  390  O   VAL B  59     3934   6186   8489    347   -750  -1924  B    O  
ATOM    391  CB  VAL B  59     -60.871   7.841  30.573  1.00 46.47      B    C  
ANISOU  391  CB  VAL B  59     3783   5484   8389    225   -609  -1529  B    C  
ATOM    392  CG1 VAL B  59     -61.718   7.398  29.374  1.00 27.67      B    C  
ANISOU  392  CG1 VAL B  59     1541   2935   6038    224   -539  -1405  B    C  
ATOM    393  CG2 VAL B  59     -59.379   7.715  30.326  1.00 33.26      B    C  
ANISOU  393  CG2 VAL B  59     2107   3746   6784    178   -590  -1418  B    C  
ATOM    394  N   GLU B  60     -63.426  10.149  30.588  1.00 45.18      B    N  
ANISOU  394  N   GLU B  60     3623   5203   8340    322   -765  -1983  B    N  
ATOM    395  CA  GLU B  60     -64.743  10.548  31.036  1.00 40.11      B    C  
ANISOU  395  CA  GLU B  60     2959   4679   7603    390   -814  -2147  B    C  
ATOM    396  C   GLU B  60     -65.821  10.113  30.063  1.00 52.92      B    C  
ANISOU  396  C   GLU B  60     4722   6210   9175    390   -726  -1997  B    C  
ATOM    397  O   GLU B  60     -67.024  10.179  30.367  1.00 40.24      B    O  
ANISOU  397  O   GLU B  60     3123   4739   7427    445   -745  -2073  B    O  
ATOM    398  CB  GLU B  60     -64.786  12.057  31.193  1.00 40.66      B    C  
ANISOU  398  CB  GLU B  60     2961   4609   7878    419   -929  -2415  B    C  
ATOM    399  CG  GLU B  60     -63.864  12.630  32.268  1.00 49.63      B    C  
ANISOU  399  CG  GLU B  60     3929   5863   9064    426  -1033  -2638  B    C  
ATOM    400  CD  GLU B  60     -64.415  12.515  33.686  1.00 71.82      B    C  
ANISOU  400  CD  GLU B  60     6569   9082  11636    508  -1103  -2854  B    C  
ATOM    401  OE1 GLU B  60     -65.407  11.791  33.912  1.00 75.38      B    O  
ANISOU  401  OE1 GLU B  60     7034   9754  11851    552  -1072  -2774  B    O  
ATOM    402  OE2 GLU B  60     -63.842  13.157  34.586  1.00 81.91      B    O  
ANISOU  402  OE2 GLU B  60     7674  10489  12957    528  -1197  -3105  B    O  
ATOM    403  N   ASN B  61     -65.388   9.661  28.891  1.00 46.30      B    N  
ANISOU  403  N   ASN B  61     3447   4969   9176     10   -302  -1279  B    N  
ATOM    404  CA  ASN B  61     -66.317   9.318  27.813  1.00 44.06      B    C  
ANISOU  404  CA  ASN B  61     3269   4504   8966     66   -357  -1048  B    C  
ATOM    405  C   ASN B  61     -66.229   7.840  27.393  1.00 39.46      B    C  
ANISOU  405  C   ASN B  61     2770   4063   8160     44   -354   -786  B    C  
ATOM    406  O   ASN B  61     -66.544   7.497  26.274  1.00 35.22      B    O  
ANISOU  406  O   ASN B  61     2348   3376   7658     45   -396   -584  B    O  
ATOM    407  CB  ASN B  61     -66.006  10.172  26.598  1.00 30.51      B    C  
ANISOU  407  CB  ASN B  61     1676   2432   7484     39   -412   -938  B    C  
ATOM    408  CG  ASN B  61     -64.541  10.039  26.197  1.00 51.13      B    C  
ANISOU  408  CG  ASN B  61     4374   5035  10019    -74   -395   -851  B    C  
ATOM    409  ND2 ASN B  61     -64.076  10.851  25.266  1.00 40.44      B    N  
ANISOU  409  ND2 ASN B  61     3104   3413   8846   -131   -434   -764  B    N  
ATOM    410  OD1 ASN B  61     -63.840   9.203  26.745  1.00 33.55      B    O  
ANISOU  410  OD1 ASN B  61     2123   3054   7572   -112   -349   -850  B    O  
ATOM    411  N   PHE B  62     -65.773   6.965  28.272  1.00 43.08      B    N  
ANISOU  411  N   PHE B  62     3160   4809   8398     18   -306   -787  B    N  
ATOM    412  CA  PHE B  62     -65.818   5.550  27.966  1.00 43.01      B    C  
ANISOU  412  CA  PHE B  62     3292   4855   8195     12   -294   -552  B    C  
ATOM    413  C   PHE B  62     -67.076   5.065  28.695  1.00 39.90      B    C  
ANISOU  413  C   PHE B  62     2828   4629   7704     59   -283   -567  B    C  
ATOM    414  O   PHE B  62     -67.147   5.115  29.926  1.00 49.04      B    O  
ANISOU  414  O   PHE B  62     3847   6047   8741     60   -247   -705  B    O  
ATOM    415  CB  PHE B  62     -64.535   4.840  28.446  1.00 37.67      B    C  
ANISOU  415  CB  PHE B  62     2640   4336   7336    -35   -252   -493  B    C  
ATOM    416  CG  PHE B  62     -64.398   3.427  27.928  1.00 41.03      B    C  
ANISOU  416  CG  PHE B  62     3193   4744   7654    -37   -243   -251  B    C  
ATOM    417  CD1 PHE B  62     -63.586   3.143  26.832  1.00 39.87      B    C  
ANISOU  417  CD1 PHE B  62     3160   4435   7554    -66   -246   -139  B    C  
ATOM    418  CD2 PHE B  62     -65.096   2.386  28.529  1.00 33.31      B    C  
ANISOU  418  CD2 PHE B  62     2191   3916   6551    -19   -230   -142  B    C  
ATOM    419  CE1 PHE B  62     -63.489   1.836  26.322  1.00 29.41      B    C  
ANISOU  419  CE1 PHE B  62     1919   3081   6176    -63   -232     37  B    C  
ATOM    420  CE2 PHE B  62     -64.989   1.078  28.043  1.00 33.93      B    C  
ANISOU  420  CE2 PHE B  62     2355   3940   6597    -25   -222     66  B    C  
ATOM    421  CZ  PHE B  62     -64.194   0.799  26.939  1.00 33.72      B    C  
ANISOU  421  CZ  PHE B  62     2435   3734   6641    -42   -222    137  B    C  
ATOM    422  N   PRO B  63     -68.093   4.642  27.940  1.00 33.10      B    N  
ANISOU  422  N   PRO B  63     2039   3652   6886     84   -315   -437  B    N  
ATOM    423  CA  PRO B  63     -69.430   4.381  28.519  1.00 39.60      B    C  
ANISOU  423  CA  PRO B  63     2774   4616   7655    124   -311   -467  B    C  
ATOM    424  C   PRO B  63     -69.362   3.352  29.633  1.00 40.07      B    C  
ANISOU  424  C   PRO B  63     2778   4972   7474     92   -261   -407  B    C  
ATOM    425  O   PRO B  63     -68.710   2.320  29.472  1.00 39.84      B    O  
ANISOU  425  O   PRO B  63     2840   4949   7350     51   -248   -219  B    O  
ATOM    426  CB  PRO B  63     -70.217   3.811  27.332  1.00 29.10      B    C  
ANISOU  426  CB  PRO B  63     1561   3117   6379    124   -353   -281  B    C  
ATOM    427  CG  PRO B  63     -69.140   3.232  26.432  1.00 28.15      B    C  
ANISOU  427  CG  PRO B  63     1589   2866   6240     68   -354   -128  B    C  
ATOM    428  CD  PRO B  63     -68.050   4.292  26.518  1.00 36.88      B    C  
ANISOU  428  CD  PRO B  63     2666   3913   7436     63   -353   -254  B    C  
ATOM    429  N   GLY B  64     -69.986   3.639  30.762  1.00 38.07      B    N  
ANISOU  429  N   GLY B  64     2349   4978   7137    110   -234   -563  B    N  
ATOM    430  CA  GLY B  64     -70.065   2.663  31.838  1.00 39.92      B    C  
ANISOU  430  CA  GLY B  64     2490   5545   7131     69   -195   -464  B    C  
ATOM    431  C   GLY B  64     -69.496   3.180  33.122  1.00 46.88      B    C  
ANISOU  431  C   GLY B  64     3186   6752   7873     47   -157   -661  B    C  
ATOM    432  O   GLY B  64     -69.633   2.551  34.169  1.00 49.60      B    O  
ANISOU  432  O   GLY B  64     3394   7454   7997      5   -128   -597  B    O  
ATOM    433  N   PHE B  65     -68.854   4.335  33.023  1.00 51.11      B    N  
ANISOU  433  N   PHE B  65     3695   7181   8545     60   -159   -894  B    N  
ATOM    434  CA  PHE B  65     -68.175   4.954  34.153  1.00 49.14      B    C  
ANISOU  434  CA  PHE B  65     3254   7231   8188     23   -122  -1135  B    C  
ATOM    435  C   PHE B  65     -68.691   6.391  34.424  1.00 55.96      B    C  
ANISOU  435  C   PHE B  65     3940   8072   9251     67   -106  -1527  B    C  
ATOM    436  O   PHE B  65     -68.100   7.378  33.997  1.00 55.64      B    O  
ANISOU  436  O   PHE B  65     3902   7801   9438     74   -118  -1691  B    O  
ATOM    437  CB  PHE B  65     -66.663   4.894  33.922  1.00 50.13      B    C  
ANISOU  437  CB  PHE B  65     3467   7284   8294    -25   -129  -1062  B    C  
ATOM    438  CG  PHE B  65     -66.135   3.474  33.778  1.00 63.26      B    C  
ANISOU  438  CG  PHE B  65     5250   8988   9800    -50   -138   -704  B    C  
ATOM    439  CD1 PHE B  65     -66.097   2.854  32.542  1.00 56.05      B    C  
ANISOU  439  CD1 PHE B  65     4551   7734   9011    -27   -165   -479  B    C  
ATOM    440  CD2 PHE B  65     -65.716   2.754  34.883  1.00 53.25      B    C  
ANISOU  440  CD2 PHE B  65     3846   8112   8277    -96   -121   -597  B    C  
ATOM    441  CE1 PHE B  65     -65.638   1.562  32.403  1.00 46.49      B    C  
ANISOU  441  CE1 PHE B  65     3414   6533   7717    -41   -167   -190  B    C  
ATOM    442  CE2 PHE B  65     -65.267   1.472  34.750  1.00 52.68      B    C  
ANISOU  442  CE2 PHE B  65     3846   8041   8129   -105   -135   -259  B    C  
ATOM    443  CZ  PHE B  65     -65.224   0.873  33.496  1.00 53.03      B    C  
ANISOU  443  CZ  PHE B  65     4105   7701   8345    -73   -155    -70  B    C  
ATOM    444  N   PRO B  66     -69.823   6.496  35.129  1.00 40.17      B    N  
ANISOU  444  N   PRO B  66     1761   6309   7191     98    -75  -1677  B    N  
ATOM    445  CA  PRO B  66     -70.542   7.748  35.352  1.00 44.07      B    C  
ANISOU  445  CA  PRO B  66     2065   6764   7915    171    -53  -2053  B    C  
ATOM    446  C   PRO B  66     -69.671   8.829  36.034  1.00 57.49      B    C  
ANISOU  446  C   PRO B  66     3660   8529   9653    129    -13  -2424  B    C  
ATOM    447  O   PRO B  66     -69.999  10.006  36.005  1.00 52.09      B    O  
ANISOU  447  O   PRO B  66     2922   7645   9226    189     -0  -2747  B    O  
ATOM    448  CB  PRO B  66     -71.662   7.331  36.308  1.00 46.16      B    C  
ANISOU  448  CB  PRO B  66     2132   7439   7967    174     -6  -2126  B    C  
ATOM    449  CG  PRO B  66     -71.733   5.821  36.196  1.00 49.85      B    C  
ANISOU  449  CG  PRO B  66     2756   8011   8172    114    -27  -1699  B    C  
ATOM    450  CD  PRO B  66     -70.372   5.383  35.928  1.00 45.60      B    C  
ANISOU  450  CD  PRO B  66     2376   7380   7569     54    -50  -1504  B    C  
ATOM    451  N   THR B  67     -68.557   8.437  36.626  1.00 59.08      B    N  
ANISOU  451  N   THR B  67     3825   9001   9624     25      3  -2382  B    N  
ATOM    452  CA  THR B  67     -67.758   9.358  37.413  1.00 47.46      B    C  
ANISOU  452  CA  THR B  67     2218   7684   8133    -41     46  -2753  B    C  
ATOM    453  C   THR B  67     -66.402   9.534  36.755  1.00 65.69      B    C  
ANISOU  453  C   THR B  67     4691   9729  10539    -95     10  -2645  B    C  
ATOM    454  O   THR B  67     -65.512  10.221  37.259  1.00 58.18      B    O  
ANISOU  454  O   THR B  67     3658   8869   9579   -173     35  -2904  B    O  
ATOM    455  CB  THR B  67     -67.612   8.773  38.797  1.00 50.49      B    C  
ANISOU  455  CB  THR B  67     2362   8710   8110   -134     94  -2808  B    C  
ATOM    456  CG2 THR B  67     -66.413   9.346  39.528  1.00 67.39      B    C  
ANISOU  456  CG2 THR B  67     4387  11081  10139   -243    121  -3070  B    C  
ATOM    457  OG1 THR B  67     -68.824   9.048  39.509  1.00 58.14      B    O  
ANISOU  457  OG1 THR B  67     3130   9934   9026    -97    147  -3064  B    O  
ATOM    458  N   GLY B  68     -66.251   8.893  35.604  1.00 63.31      B    N  
ANISOU  458  N   GLY B  68     4614   9115  10325    -63    -46  -2271  B    N  
ATOM    459  CA  GLY B  68     -64.983   8.890  34.912  1.00 45.64      B    C  
ANISOU  459  CA  GLY B  68     2529   6664   8148   -118    -75  -2125  B    C  
ATOM    460  C   GLY B  68     -64.116   7.804  35.496  1.00 56.66      B    C  
ANISOU  460  C   GLY B  68     3870   8431   9228   -187    -70  -1913  B    C  
ATOM    461  O   GLY B  68     -64.504   7.127  36.454  1.00 60.34      B    O  
ANISOU  461  O   GLY B  68     4212   9296   9422   -200    -46  -1871  B    O  
ATOM    462  N   ILE B  69     -62.938   7.624  34.910  1.00 45.35      B    N  
ANISOU  462  N   ILE B  69     2568   6850   7814   -228    -91  -1759  B    N  
ATOM    463  CA  ILE B  69     -62.024   6.611  35.382  1.00 37.57      B    C  
ANISOU  463  CA  ILE B  69     1594   6141   6540   -269    -90  -1538  B    C  
ATOM    464  C   ILE B  69     -60.652   6.928  34.852  1.00 45.63      B    C  
ANISOU  464  C   ILE B  69     2687   7011   7640   -325   -100  -1527  B    C  
ATOM    465  O   ILE B  69     -60.528   7.413  33.729  1.00 62.07      B    O  
ANISOU  465  O   ILE B  69     4912   8697   9972   -314   -120  -1507  B    O  
ATOM    466  CB  ILE B  69     -62.443   5.199  34.931  1.00 44.39      B    C  
ANISOU  466  CB  ILE B  69     2627   6938   7303   -207   -110  -1139  B    C  
ATOM    467  CG1 ILE B  69     -61.450   4.171  35.450  1.00 45.22      B    C  
ANISOU  467  CG1 ILE B  69     2700   7309   7173   -238   -115   -897  B    C  
ATOM    468  CG2 ILE B  69     -62.519   5.126  33.435  1.00 33.19      B    C  
ANISOU  468  CG2 ILE B  69     1450   5043   6118   -161   -136   -985  B    C  
ATOM    469  CD1 ILE B  69     -61.971   2.786  35.462  1.00 41.02      B    C  
ANISOU  469  CD1 ILE B  69     2224   6823   6539   -198   -127   -549  B    C  
ATOM    470  N   MET B  70     -59.617   6.687  35.655  1.00 41.45      B    N  
ANISOU  470  N   MET B  70     2034   6824   6891   -392    -92  -1533  B    N  
ATOM    471  CA  MET B  70     -58.280   6.967  35.176  1.00 45.94      B    C  
ANISOU  471  CA  MET B  70     2654   7280   7521   -450   -100  -1525  B    C  
ATOM    472  C   MET B  70     -57.867   5.934  34.124  1.00 40.31      B    C  
ANISOU  472  C   MET B  70     2167   6319   6828   -386   -119  -1156  B    C  
ATOM    473  O   MET B  70     -58.165   4.761  34.257  1.00 47.11      B    O  
ANISOU  473  O   MET B  70     3071   7273   7555   -325   -128   -892  B    O  
ATOM    474  CB  MET B  70     -57.318   6.997  36.347  1.00 47.12      B    C  
ANISOU  474  CB  MET B  70     2583   7901   7422   -541    -91  -1641  B    C  
ATOM    475  CG  MET B  70     -57.728   8.005  37.393  1.00 53.28      B    C  
ANISOU  475  CG  MET B  70     3105   8964   8175   -622    -63  -2059  B    C  
ATOM    476  SD  MET B  70     -56.266   8.740  38.121  1.00102.21      B    S  
ANISOU  476  SD  MET B  70     9115  15465  14254   -778    -53  -2333  B    S  
ATOM    477  CE  MET B  70     -55.575   7.335  39.014  1.00 59.31      B    C  
ANISOU  477  CE  MET B  70     3546  10592   8396   -775    -82  -1984  B    C  
ATOM    478  N   GLY B  71     -57.201   6.387  33.069  1.00 35.18      B    N  
ANISOU  478  N   GLY B  71     1641   5358   6365   -412   -124  -1152  B    N  
ATOM    479  CA  GLY B  71     -56.730   5.496  32.022  1.00 28.83      B    C  
ANISOU  479  CA  GLY B  71     1020   4346   5587   -364   -132   -863  B    C  
ATOM    480  C   GLY B  71     -56.020   4.255  32.570  1.00 41.62      B    C  
ANISOU  480  C   GLY B  71     2589   6231   6993   -331   -133   -636  B    C  
ATOM    481  O   GLY B  71     -56.326   3.132  32.187  1.00 50.73      B    O  
ANISOU  481  O   GLY B  71     3838   7298   8141   -258   -139   -385  B    O  
ATOM    482  N   ILE B  72     -55.068   4.447  33.473  1.00 45.81      B    N  
ANISOU  482  N   ILE B  72     2946   7090   7371   -392   -132   -721  B    N  
ATOM    483  CA  ILE B  72     -54.362   3.304  34.031  1.00 47.94      B    C  
ANISOU  483  CA  ILE B  72     3129   7629   7459   -356   -147   -474  B    C  
ATOM    484  C   ILE B  72     -55.306   2.273  34.664  1.00 52.93      B    C  
ANISOU  484  C   ILE B  72     3719   8417   7977   -291   -161   -259  B    C  
ATOM    485  O   ILE B  72     -55.134   1.072  34.462  1.00 52.59      B    O  
ANISOU  485  O   ILE B  72     3706   8333   7942   -222   -174     42  B    O  
ATOM    486  CB  ILE B  72     -53.269   3.716  35.037  1.00 52.92      B    C  
ANISOU  486  CB  ILE B  72     3534   8666   7907   -442   -153   -600  B    C  
ATOM    487  CG1 ILE B  72     -52.017   4.177  34.295  1.00 75.89      B    C  
ANISOU  487  CG1 ILE B  72     6485  11432  10917   -492   -142   -663  B    C  
ATOM    488  CG2 ILE B  72     -52.845   2.516  35.848  1.00 63.95      B    C  
ANISOU  488  CG2 ILE B  72     4784  10409   9103   -395   -182   -307  B    C  
ATOM    489  CD1 ILE B  72     -51.869   5.662  34.153  1.00 89.45      B    C  
ANISOU  489  CD1 ILE B  72     8180  13052  12756   -613   -123  -1010  B    C  
ATOM    490  N   ASP B  73     -56.300   2.740  35.418  1.00 45.91      B    N  
ANISOU  490  N   ASP B  73     2736   7701   7005   -319   -156   -416  B    N  
ATOM    491  CA  ASP B  73     -57.229   1.833  36.090  1.00 54.72      B    C  
ANISOU  491  CA  ASP B  73     3781   9014   7994   -282   -167   -214  B    C  
ATOM    492  C   ASP B  73     -58.120   1.100  35.116  1.00 49.74      B    C  
ANISOU  492  C   ASP B  73     3355   8004   7539   -204   -167    -22  B    C  
ATOM    493  O   ASP B  73     -58.351  -0.102  35.253  1.00 52.18      B    O  
ANISOU  493  O   ASP B  73     3650   8352   7824   -163   -181    280  B    O  
ATOM    494  CB  ASP B  73     -58.068   2.574  37.141  1.00 42.94      B    C  
ANISOU  494  CB  ASP B  73     2110   7849   6357   -341   -151   -472  B    C  
ATOM    495  CG  ASP B  73     -57.214   3.131  38.242  1.00 57.26      B    C  
ANISOU  495  CG  ASP B  73     3672  10131   7956   -437   -151   -659  B    C  
ATOM    496  OD1 ASP B  73     -57.632   4.095  38.888  1.00 67.50      B    O  
ANISOU  496  OD1 ASP B  73     4818  11631   9195   -506   -126  -1005  B    O  
ATOM    497  OD2 ASP B  73     -56.092   2.610  38.444  1.00 69.69      B    O  
ANISOU  497  OD2 ASP B  73     5177  11873   9428   -446   -177   -477  B    O  
ATOM    498  N   LEU B  74     -58.616   1.824  34.125  1.00 41.48      B    N  
ANISOU  498  N   LEU B  74     2477   6596   6686   -195   -155   -190  B    N  
ATOM    499  CA  LEU B  74     -59.433   1.202  33.087  1.00 49.50      B    C  
ANISOU  499  CA  LEU B  74     3679   7266   7862   -138   -156    -36  B    C  
ATOM    500  C   LEU B  74     -58.643   0.081  32.400  1.00 57.53      B    C  
ANISOU  500  C   LEU B  74     4778   8129   8950    -98   -161    223  B    C  
ATOM    501  O   LEU B  74     -59.149  -1.029  32.235  1.00 54.19      B    O  
ANISOU  501  O   LEU B  74     4385   7631   8574    -59   -164    447  B    O  
ATOM    502  CB  LEU B  74     -59.910   2.232  32.065  1.00 34.29      B    C  
ANISOU  502  CB  LEU B  74     1890   5009   6130   -141   -154   -233  B    C  
ATOM    503  CG  LEU B  74     -60.728   1.651  30.913  1.00 38.68      B    C  
ANISOU  503  CG  LEU B  74     2620   5247   6829    -98   -162    -89  B    C  
ATOM    504  CD1 LEU B  74     -61.872   0.760  31.400  1.00 28.37      B    C  
ANISOU  504  CD1 LEU B  74     1280   4043   5457    -71   -166     57  B    C  
ATOM    505  CD2 LEU B  74     -61.235   2.767  30.040  1.00 28.96      B    C  
ANISOU  505  CD2 LEU B  74     1473   3759   5773   -106   -173   -258  B    C  
ATOM    506  N   MET B  75     -57.395   0.363  32.025  1.00 32.84      B    N  
ANISOU  506  N   MET B  75     1661   4963   5853   -113   -154    177  B    N  
ATOM    507  CA  MET B  75     -56.591  -0.644  31.349  1.00 34.53      B    C  
ANISOU  507  CA  MET B  75     1924   5038   6157    -68   -148    376  B    C  
ATOM    508  C   MET B  75     -56.112  -1.774  32.269  1.00 41.90      B    C  
ANISOU  508  C   MET B  75     2690   6224   7006    -27   -164    634  B    C  
ATOM    509  O   MET B  75     -55.949  -2.901  31.815  1.00 54.88      B    O  
ANISOU  509  O   MET B  75     4351   7717   8783     33   -161    843  B    O  
ATOM    510  CB  MET B  75     -55.433  -0.011  30.599  1.00 30.41      B    C  
ANISOU  510  CB  MET B  75     1450   4410   5695    -98   -132    253  B    C  
ATOM    511  CG  MET B  75     -55.859   0.998  29.547  1.00 30.43      B    C  
ANISOU  511  CG  MET B  75     1597   4144   5821   -140   -123     74  B    C  
ATOM    512  SD  MET B  75     -57.126   0.348  28.440  1.00 41.09      B    S  
ANISOU  512  SD  MET B  75     3113   5188   7311    -98   -123    177  B    S  
ATOM    513  CE  MET B  75     -56.476  -1.179  27.788  1.00 18.99      B    C  
ANISOU  513  CE  MET B  75      330   2291   4594    -41    -99    379  B    C  
ATOM    514  N   ASP B  76     -55.899  -1.477  33.550  1.00 42.24      B    N  
ANISOU  514  N   ASP B  76     2545   6660   6844    -64   -184    619  B    N  
ATOM    515  CA  ASP B  76     -55.705  -2.527  34.545  1.00 32.69      B    C  
ANISOU  515  CA  ASP B  76     1140   5745   5536    -34   -214    914  B    C  
ATOM    516  C   ASP B  76     -56.905  -3.468  34.543  1.00 50.98      B    C  
ANISOU  516  C   ASP B  76     3481   7957   7934     -3   -219   1125  B    C  
ATOM    517  O   ASP B  76     -56.738  -4.683  34.659  1.00 64.21      B    O  
ANISOU  517  O   ASP B  76     5070   9617   9710     51   -237   1435  B    O  
ATOM    518  CB  ASP B  76     -55.538  -1.959  35.951  1.00 36.45      B    C  
ANISOU  518  CB  ASP B  76     1386   6731   5733   -105   -236    840  B    C  
ATOM    519  CG  ASP B  76     -54.157  -1.385  36.194  1.00 50.98      B    C  
ANISOU  519  CG  ASP B  76     3121   8767   7479   -140   -243    722  B    C  
ATOM    520  OD1 ASP B  76     -53.327  -1.454  35.277  1.00 36.81      B    O  
ANISOU  520  OD1 ASP B  76     1435   6712   5840   -103   -229    717  B    O  
ATOM    521  OD2 ASP B  76     -53.899  -0.859  37.301  1.00 56.50      B    O  
ANISOU  521  OD2 ASP B  76     3614   9912   7942   -215   -260    618  B    O  
ATOM    522  N   ASN B  77     -58.109  -2.914  34.418  1.00 35.84      B    N  
ANISOU  522  N   ASN B  77     1657   5962   6000    -37   -205    963  B    N  
ATOM    523  CA  ASN B  77     -59.299  -3.756  34.436  1.00 43.58      B    C  
ANISOU  523  CA  ASN B  77     2644   6868   7046    -25   -210   1148  B    C  
ATOM    524  C   ASN B  77     -59.380  -4.614  33.199  1.00 46.30      B    C  
ANISOU  524  C   ASN B  77     3144   6785   7663     28   -197   1261  B    C  
ATOM    525  O   ASN B  77     -59.657  -5.793  33.307  1.00 51.08      B    O  
ANISOU  525  O   ASN B  77     3677   7347   8383     54   -209   1530  B    O  
ATOM    526  CB  ASN B  77     -60.562  -2.939  34.592  1.00 40.28      B    C  
ANISOU  526  CB  ASN B  77     2266   6492   6548    -66   -197    933  B    C  
ATOM    527  CG  ASN B  77     -60.636  -2.262  35.920  1.00 49.02      B    C  
ANISOU  527  CG  ASN B  77     3166   8068   7391   -125   -200    810  B    C  
ATOM    528  ND2 ASN B  77     -61.612  -1.375  36.095  1.00 56.08      B    N  
ANISOU  528  ND2 ASN B  77     4063   9014   8232   -153   -180    553  B    N  
ATOM    529  OD1 ASN B  77     -59.822  -2.531  36.788  1.00 47.64      B    O  
ANISOU  529  OD1 ASN B  77     2807   8230   7066   -144   -220    937  B    O  
ATOM    530  N   CYS B  78     -59.113  -4.027  32.029  1.00 40.87      B    N  
ANISOU  530  N   CYS B  78     2641   5802   7085     34   -174   1054  B    N  
ATOM    531  CA  CYS B  78     -59.164  -4.766  30.767  1.00 42.21      B    C  
ANISOU  531  CA  CYS B  78     2940   5607   7489     67   -155   1105  B    C  
ATOM    532  C   CYS B  78     -58.250  -5.996  30.800  1.00 47.87      B    C  
ANISOU  532  C   CYS B  78     3546   6290   8353    130   -154   1340  B    C  
ATOM    533  O   CYS B  78     -58.648  -7.105  30.433  1.00 52.15      B    O  
ANISOU  533  O   CYS B  78     4072   6645   9096    162   -148   1497  B    O  
ATOM    534  CB  CYS B  78     -58.805  -3.859  29.590  1.00 41.54      B    C  
ANISOU  534  CB  CYS B  78     3021   5308   7455     49   -134    864  B    C  
ATOM    535  SG  CYS B  78     -60.101  -2.631  29.180  1.00 38.83      B    S  
ANISOU  535  SG  CYS B  78     2805   4874   7073      2   -144    640  B    S  
ATOM    536  N   ARG B  79     -57.032  -5.793  31.283  1.00 34.09      B    N  
ANISOU  536  N   ARG B  79     1698   4730   6525    151   -160   1359  B    N  
ATOM    537  CA  ARG B  79     -56.062  -6.869  31.395  1.00 38.64      B    C  
ANISOU  537  CA  ARG B  79     2135   5298   7249    231   -166   1584  B    C  
ATOM    538  C   ARG B  79     -56.513  -7.967  32.373  1.00 50.02      B    C  
ANISOU  538  C   ARG B  79     3384   6881   8742    263   -206   1931  B    C  
ATOM    539  O   ARG B  79     -56.396  -9.159  32.079  1.00 56.30      B    O  
ANISOU  539  O   ARG B  79     4111   7473   9808    339   -208   2135  B    O  
ATOM    540  CB  ARG B  79     -54.715  -6.300  31.819  1.00 33.01      B    C  
ANISOU  540  CB  ARG B  79     1326   4816   6399    237   -174   1533  B    C  
ATOM    541  CG  ARG B  79     -53.546  -7.261  31.712  1.00 42.84      B    C  
ANISOU  541  CG  ARG B  79     2436   6020   7820    338   -175   1718  B    C  
ATOM    542  CD  ARG B  79     -52.319  -6.686  32.423  1.00 38.33      B    C  
ANISOU  542  CD  ARG B  79     1721   5782   7062    332   -198   1703  B    C  
ATOM    543  NE  ARG B  79     -51.101  -7.380  32.051  1.00 38.17      B    N  
ANISOU  543  NE  ARG B  79     1600   5686   7219    433   -188   1801  B    N  
ATOM    544  CZ  ARG B  79     -50.763  -8.574  32.502  1.00 45.75      B    C  
ANISOU  544  CZ  ARG B  79     2369   6663   8354    545   -221   2120  B    C  
ATOM    545  NH1 ARG B  79     -51.565  -9.206  33.343  1.00 52.07      B    N  
ANISOU  545  NH1 ARG B  79     3058   7566   9159    554   -271   2396  B    N  
ATOM    546  NH2 ARG B  79     -49.647  -9.138  32.086  1.00 38.87      B    N  
ANISOU  546  NH2 ARG B  79     1402   5695   7670    654   -207   2171  B    N  
ATOM    547  N   ALA B  80     -57.025  -7.566  33.530  1.00 36.84      B    N  
ANISOU  547  N   ALA B  80     1604   5565   6828    204   -239   1994  B    N  
ATOM    548  CA  ALA B  80     -57.414  -8.521  34.554  1.00 49.88      B    C  
ANISOU  548  CA  ALA B  80     3034   7431   8486    211   -287   2356  B    C  
ATOM    549  C   ALA B  80     -58.546  -9.346  33.990  1.00 52.05      B    C  
ANISOU  549  C   ALA B  80     3378   7403   8997    212   -276   2452  B    C  
ATOM    550  O   ALA B  80     -58.774 -10.485  34.383  1.00 51.42      B    O  
ANISOU  550  O   ALA B  80     3142   7306   9089    244   -311   2787  B    O  
ATOM    551  CB  ALA B  80     -57.865  -7.799  35.825  1.00 31.74      B    C  
ANISOU  551  CB  ALA B  80      602   5621   5835    121   -313   2340  B    C  
ATOM    552  N   GLN B  81     -59.241  -8.755  33.038  1.00 35.49      B    N  
ANISOU  552  N   GLN B  81     1506   5061   6919    174   -234   2164  B    N  
ATOM    553  CA  GLN B  81     -60.422  -9.368  32.492  1.00 47.18      B    C  
ANISOU  553  CA  GLN B  81     3052   6299   8577    152   -223   2200  B    C  
ATOM    554  C   GLN B  81     -59.952 -10.388  31.479  1.00 50.29      B    C  
ANISOU  554  C   GLN B  81     3470   6310   9329    231   -203   2252  B    C  
ATOM    555  O   GLN B  81     -60.413 -11.524  31.492  1.00 52.84      B    O  
ANISOU  555  O   GLN B  81     3766   6451   9862    236   -207   2472  B    O  
ATOM    556  CB  GLN B  81     -61.262  -8.280  31.841  1.00 46.03      B    C  
ANISOU  556  CB  GLN B  81     3117   6067   8305     92   -196   1873  B    C  
ATOM    557  CG  GLN B  81     -62.620  -8.672  31.450  1.00 51.52      B    C  
ANISOU  557  CG  GLN B  81     3862   6615   9098     47   -192   1885  B    C  
ATOM    558  CD  GLN B  81     -63.473  -7.459  31.189  1.00 52.37      B    C  
ANISOU  558  CD  GLN B  81     4116   6754   9030      2   -184   1609  B    C  
ATOM    559  NE2 GLN B  81     -64.720  -7.689  30.837  1.00 37.04      B    N  
ANISOU  559  NE2 GLN B  81     2215   4711   7146    -38   -184   1598  B    N  
ATOM    560  OE1 GLN B  81     -63.007  -6.321  31.298  1.00 49.60      B    O  
ANISOU  560  OE1 GLN B  81     3821   6510   8515      5   -180   1407  B    O  
ATOM    561  N   SER B  82     -59.029  -9.971  30.609  1.00 43.27      B    N  
ANISOU  561  N   SER B  82     2698   5268   8474    269   -168   2035  B    N  
ATOM    562  CA  SER B  82     -58.379 -10.876  29.651  1.00 46.28      B    C  
ANISOU  562  CA  SER B  82     3091   5323   9173    355   -134   2030  B    C  
ATOM    563  C   SER B  82     -57.731 -12.090  30.308  1.00 52.21      B    C  
ANISOU  563  C   SER B  82     3674   6035  10127    445   -158   2366  B    C  
ATOM    564  O   SER B  82     -57.797 -13.198  29.789  1.00 57.34      B    O  
ANISOU  564  O   SER B  82     4339   6355  11094    491   -135   2446  B    O  
ATOM    565  CB  SER B  82     -57.278 -10.156  28.900  1.00 37.18      B    C  
ANISOU  565  CB  SER B  82     2028   4139   7961    372    -96   1783  B    C  
ATOM    566  OG  SER B  82     -57.808  -9.170  28.084  1.00 45.84      B    O  
ANISOU  566  OG  SER B  82     3319   5177   8922    286    -71   1505  B    O  
ATOM    567  N   VAL B  83     -57.077 -11.867  31.436  1.00 42.53      B    N  
ANISOU  567  N   VAL B  83     2278   5150   8732    469   -208   2556  B    N  
ATOM    568  CA  VAL B  83     -56.430 -12.950  32.150  1.00 43.30      B    C  
ANISOU  568  CA  VAL B  83     2188   5257   9006    560   -249   2929  B    C  
ATOM    569  C   VAL B  83     -57.465 -13.890  32.736  1.00 56.64      B    C  
ANISOU  569  C   VAL B  83     3820   6886  10812    517   -281   3250  B    C  
ATOM    570  O   VAL B  83     -57.338 -15.114  32.672  1.00 63.24      B    O  
ANISOU  570  O   VAL B  83     4595   7440  11993    586   -287   3500  B    O  
ATOM    571  CB  VAL B  83     -55.526 -12.422  33.261  1.00 46.96      B    C  
ANISOU  571  CB  VAL B  83     2460   6175   9208    576   -304   3067  B    C  
ATOM    572  CG1 VAL B  83     -55.059 -13.562  34.106  1.00 47.50      B    C  
ANISOU  572  CG1 VAL B  83     2314   6293   9441    659   -365   3527  B    C  
ATOM    573  CG2 VAL B  83     -54.310 -11.690  32.652  1.00 36.23      B    C  
ANISOU  573  CG2 VAL B  83     1131   4835   7801    626   -271   2791  B    C  
ATOM    574  N   ARG B  84     -58.519 -13.311  33.283  1.00 64.98      B    N  
ANISOU  574  N   ARG B  84     4892   8193  11605    398   -297   3234  B    N  
ATOM    575  CA  ARG B  84     -59.556 -14.094  33.936  1.00 55.22      B    C  
ANISOU  575  CA  ARG B  84     3582   6975  10422    328   -327   3546  B    C  
ATOM    576  C   ARG B  84     -60.152 -15.141  33.001  1.00 57.24      B    C  
ANISOU  576  C   ARG B  84     3954   6720  11074    332   -289   3553  B    C  
ATOM    577  O   ARG B  84     -60.485 -16.228  33.437  1.00 59.01      B    O  
ANISOU  577  O   ARG B  84     4082   6820  11518    323   -317   3902  B    O  
ATOM    578  CB  ARG B  84     -60.620 -13.163  34.482  1.00 51.48      B    C  
ANISOU  578  CB  ARG B  84     3118   6849   9594    201   -330   3425  B    C  
ATOM    579  CG  ARG B  84     -61.772 -13.837  35.160  1.00 56.83      B    C  
ANISOU  579  CG  ARG B  84     3713   7611  10271    105   -354   3717  B    C  
ATOM    580  CD  ARG B  84     -63.003 -12.941  35.101  1.00 59.49      B    C  
ANISOU  580  CD  ARG B  84     4132   8104  10365     -2   -327   3449  B    C  
ATOM    581  NE  ARG B  84     -64.126 -13.560  35.778  1.00 63.59      B    N  
ANISOU  581  NE  ARG B  84     4554   8749  10858   -109   -344   3722  B    N  
ATOM    582  CZ  ARG B  84     -65.379 -13.139  35.687  1.00 72.64      B    C  
ANISOU  582  CZ  ARG B  84     5752   9967  11880   -203   -320   3560  B    C  
ATOM    583  NH1 ARG B  84     -65.675 -12.070  34.945  1.00 63.97      B    N  
ANISOU  583  NH1 ARG B  84     4807   8813  10687   -192   -286   3137  B    N  
ATOM    584  NH2 ARG B  84     -66.334 -13.795  36.341  1.00 83.09      B    N  
ANISOU  584  NH2 ARG B  84     6963  11423  13185   -309   -334   3843  B    N  
ATOM    585  N   PHE B  85     -60.245 -14.833  31.714  1.00 57.96      B    N  
ANISOU  585  N   PHE B  85     4237   6522  11262    339   -228   3174  B    N  
ATOM    586  CA  PHE B  85     -60.838 -15.763  30.762  1.00 49.79      B    C  
ANISOU  586  CA  PHE B  85     3308   5034  10575    323   -186   3111  B    C  
ATOM    587  C   PHE B  85     -59.850 -16.693  30.042  1.00 59.34      B    C  
ANISOU  587  C   PHE B  85     4505   5856  12185    446   -150   3092  B    C  
ATOM    588  O   PHE B  85     -60.215 -17.392  29.091  1.00 55.85      B    O  
ANISOU  588  O   PHE B  85     4154   5028  12039    433   -100   2943  B    O  
ATOM    589  CB  PHE B  85     -61.715 -14.998  29.778  1.00 44.22      B    C  
ANISOU  589  CB  PHE B  85     2794   4268   9741    235   -144   2728  B    C  
ATOM    590  CG  PHE B  85     -62.919 -14.382  30.427  1.00 64.97      B    C  
ANISOU  590  CG  PHE B  85     5415   7183  12087    120   -173   2764  B    C  
ATOM    591  CD1 PHE B  85     -63.887 -15.185  31.018  1.00 54.63      B    C  
ANISOU  591  CD1 PHE B  85     4030   5861  10864     40   -196   3037  B    C  
ATOM    592  CD2 PHE B  85     -63.078 -13.015  30.475  1.00 56.04      B    C  
ANISOU  592  CD2 PHE B  85     4337   6332  10625     92   -176   2529  B    C  
ATOM    593  CE1 PHE B  85     -64.981 -14.638  31.629  1.00 54.27      B    C  
ANISOU  593  CE1 PHE B  85     3955   6109  10555    -64   -215   3059  B    C  
ATOM    594  CE2 PHE B  85     -64.189 -12.466  31.092  1.00 56.66      B    C  
ANISOU  594  CE2 PHE B  85     4387   6672  10470      1   -196   2537  B    C  
ATOM    595  CZ  PHE B  85     -65.134 -13.279  31.668  1.00 63.54      B    C  
ANISOU  595  CZ  PHE B  85     5175   7562  11406    -75   -213   2795  B    C  
ATOM    596  N   GLY B  86     -58.613 -16.725  30.517  1.00 46.60      B    N  
ANISOU  596  N   GLY B  86     2760   4360  10585    564   -174   3236  B    N  
ATOM    597  CA  GLY B  86     -57.622 -17.629  29.962  1.00 51.21      B    C  
ANISOU  597  CA  GLY B  86     3293   4600  11566    704   -141   3239  B    C  
ATOM    598  C   GLY B  86     -56.557 -17.064  29.025  1.00 53.96      B    C  
ANISOU  598  C   GLY B  86     3701   4916  11885    784    -82   2877  B    C  
ATOM    599  O   GLY B  86     -55.703 -17.798  28.535  1.00 47.74      B    O  
ANISOU  599  O   GLY B  86     2853   3860  11427    908    -44   2842  B    O  
ATOM    600  N   THR B  87     -56.593 -15.769  28.741  1.00 43.79      B    N  
ANISOU  600  N   THR B  87     2523   3888  10226    712    -69   2600  B    N  
ATOM    601  CA  THR B  87     -55.589 -15.220  27.849  1.00 39.86      B    C  
ANISOU  601  CA  THR B  87     2075   3380   9691    765    -12   2284  B    C  
ATOM    602  C   THR B  87     -54.210 -15.492  28.455  1.00 50.04      B    C  
ANISOU  602  C   THR B  87     3171   4780  11061    907    -38   2477  B    C  
ATOM    603  O   THR B  87     -54.024 -15.397  29.663  1.00 50.46      B    O  
ANISOU  603  O   THR B  87     3081   5119  10973    921   -114   2786  B    O  
ATOM    604  CB  THR B  87     -55.807 -13.712  27.586  1.00 43.02      B    C  
ANISOU  604  CB  THR B  87     2602   4054   9688    657     -8   2019  B    C  
ATOM    605  CG2 THR B  87     -54.758 -13.141  26.643  1.00 40.18      B    C  
ANISOU  605  CG2 THR B  87     2286   3695   9286    688     50   1722  B    C  
ATOM    606  OG1 THR B  87     -57.086 -13.519  27.006  1.00 48.14      B    O  
ANISOU  606  OG1 THR B  87     3408   4595  10288    542      7   1867  B    O  
ATOM    607  N   ASN B  88     -53.272 -15.909  27.613  1.00 46.66      B    N  
ANISOU  607  N   ASN B  88     2720   4138  10873   1012     25   2301  B    N  
ATOM    608  CA  ASN B  88     -51.871 -16.070  28.018  1.00 46.06      B    C  
ANISOU  608  CA  ASN B  88     2456   4175  10870   1156      9   2426  B    C  
ATOM    609  C   ASN B  88     -51.122 -14.842  27.556  1.00 52.97      B    C  
ANISOU  609  C   ASN B  88     3382   5311  11432   1114     42   2128  B    C  
ATOM    610  O   ASN B  88     -51.002 -14.596  26.348  1.00 52.35      B    O  
ANISOU  610  O   ASN B  88     3421   5094  11375   1083    126   1777  B    O  
ATOM    611  CB  ASN B  88     -51.272 -17.310  27.387  1.00 38.77      B    C  
ANISOU  611  CB  ASN B  88     1445   2851  10435   1310     65   2400  B    C  
ATOM    612  CG  ASN B  88     -49.773 -17.454  27.657  1.00 58.54      B    C  
ANISOU  612  CG  ASN B  88     3745   5464  13037   1476     57   2488  B    C  
ATOM    613  ND2 ASN B  88     -49.186 -18.510  27.113  1.00 60.93      B    N  
ANISOU  613  ND2 ASN B  88     3947   5412  13792   1630    112   2442  B    N  
ATOM    614  OD1 ASN B  88     -49.160 -16.648  28.348  1.00 62.11      B    O  
ANISOU  614  OD1 ASN B  88     4114   6310  13175   1466      3   2585  B    O  
ATOM    615  N   ILE B  89     -50.668 -14.041  28.511  1.00 41.78      B    N  
ANISOU  615  N   ILE B  89     1872   4291   9713   1092    -23   2263  B    N  
ATOM    616  CA  ILE B  89     -50.134 -12.733  28.153  1.00 42.14      B    C  
ANISOU  616  CA  ILE B  89     1996   4580   9434   1001      5   1982  B    C  
ATOM    617  C   ILE B  89     -48.639 -12.712  28.306  1.00 45.65      B    C  
ANISOU  617  C   ILE B  89     2278   5177   9892   1096      9   2003  B    C  
ATOM    618  O   ILE B  89     -48.114 -12.880  29.396  1.00 56.96      B    O  
ANISOU  618  O   ILE B  89     3524   6846  11274   1156    -65   2288  B    O  
ATOM    619  CB  ILE B  89     -50.736 -11.604  28.992  1.00 42.18      B    C  
ANISOU  619  CB  ILE B  89     2073   4913   9040    849    -50   2008  B    C  
ATOM    620  CG1 ILE B  89     -52.240 -11.488  28.713  1.00 38.85      B    C  
ANISOU  620  CG1 ILE B  89     1818   4352   8590    748    -46   1938  B    C  
ATOM    621  CG2 ILE B  89     -50.037 -10.294  28.687  1.00 45.88      B    C  
ANISOU  621  CG2 ILE B  89     2629   5585   9220    753    -24   1741  B    C  
ATOM    622  CD1 ILE B  89     -52.956 -10.359  29.481  1.00 35.38      B    C  
ANISOU  622  CD1 ILE B  89     1456   4205   7783    609    -89   1915  B    C  
ATOM    623  N   LEU B  90     -47.949 -12.510  27.197  1.00 45.01      B    N  
ANISOU  623  N   LEU B  90     2247   4995   9862   1106     92   1705  B    N  
ATOM    624  CA  LEU B  90     -46.510 -12.364  27.242  1.00 39.59      B    C  
ANISOU  624  CA  LEU B  90     1405   4480   9156   1181    105   1679  B    C  
ATOM    625  C   LEU B  90     -46.168 -10.888  27.365  1.00 44.93      B    C  
ANISOU  625  C   LEU B  90     2170   5481   9420   1019     95   1516  B    C  
ATOM    626  O   LEU B  90     -46.660 -10.068  26.594  1.00 47.33      B    O  
ANISOU  626  O   LEU B  90     2670   5741   9571    883    137   1262  B    O  
ATOM    627  CB  LEU B  90     -45.882 -12.964  25.981  1.00 39.53      B    C  
ANISOU  627  CB  LEU B  90     1368   4218   9434   1282    210   1430  B    C  
ATOM    628  CG  LEU B  90     -46.342 -14.376  25.636  1.00 51.40      B    C  
ANISOU  628  CG  LEU B  90     2830   5315  11385   1422    240   1492  B    C  
ATOM    629  CD1 LEU B  90     -45.794 -14.818  24.282  1.00 60.69      B    C  
ANISOU  629  CD1 LEU B  90     4008   6269  12783   1478    365   1144  B    C  
ATOM    630  CD2 LEU B  90     -45.907 -15.339  26.722  1.00 44.28      B    C  
ANISOU  630  CD2 LEU B  90     1700   4390  10736   1596    162   1895  B    C  
ATOM    631  N   SER B  91     -45.348 -10.552  28.356  1.00 47.04      B    N  
ANISOU  631  N   SER B  91     2276   6074   9521   1033     35   1673  B    N  
ATOM    632  CA  SER B  91     -44.899  -9.176  28.558  1.00 50.40      B    C  
ANISOU  632  CA  SER B  91     2754   6806   9590    885     24   1510  B    C  
ATOM    633  C   SER B  91     -43.720  -8.889  27.681  1.00 54.06      B    C  
ANISOU  633  C   SER B  91     3174   7291  10075    894     93   1289  B    C  
ATOM    634  O   SER B  91     -42.690  -8.426  28.150  1.00 47.67      B    O  
ANISOU  634  O   SER B  91     2224   6767   9120    884     70   1300  B    O  
ATOM    635  CB  SER B  91     -44.514  -8.916  30.011  1.00 33.70      B    C  
ANISOU  635  CB  SER B  91      459   5082   7264    878    -68   1742  B    C  
ATOM    636  OG  SER B  91     -45.631  -9.165  30.851  1.00 47.97      B    O  
ANISOU  636  OG  SER B  91     2282   6921   9023    855   -128   1950  B    O  
ATOM    637  N   GLU B  92     -43.882  -9.164  26.395  1.00 59.01      B    N  
ANISOU  637  N   GLU B  92     3904   7645  10870    903    181   1077  B    N  
ATOM    638  CA  GLU B  92     -42.788  -9.047  25.447  1.00 47.92      B    C  
ANISOU  638  CA  GLU B  92     2430   6266   9511    920    264    858  B    C  
ATOM    639  C   GLU B  92     -43.249  -8.293  24.216  1.00 37.08      B    C  
ANISOU  639  C   GLU B  92     1260   4800   8031    766    335    572  B    C  
ATOM    640  O   GLU B  92     -44.415  -8.315  23.851  1.00 40.35      B    O  
ANISOU  640  O   GLU B  92     1841   5026   8462    711    337    535  B    O  
ATOM    641  CB  GLU B  92     -42.273 -10.443  25.064  1.00 36.78      B    C  
ANISOU  641  CB  GLU B  92      842   4649   8484   1135    315    898  B    C  
ATOM    642  CG  GLU B  92     -42.080 -11.360  26.280  1.00 54.06      B    C  
ANISOU  642  CG  GLU B  92     2830   6862  10847   1305    229   1262  B    C  
ATOM    643  CD  GLU B  92     -41.697 -12.782  25.940  1.00 60.87      B    C  
ANISOU  643  CD  GLU B  92     3520   7443  12164   1536    270   1322  B    C  
ATOM    644  OE1 GLU B  92     -41.684 -13.156  24.752  1.00 61.81      B    O  
ANISOU  644  OE1 GLU B  92     3680   7331  12476   1570    378   1045  B    O  
ATOM    645  OE2 GLU B  92     -41.407 -13.529  26.886  1.00 73.87      B    O  
ANISOU  645  OE2 GLU B  92     4973   9109  13986   1688    194   1652  B    O  
ATOM    646  N   THR B  93     -42.309  -7.638  23.574  1.00 50.53      B    N  
ANISOU  646  N   THR B  93     2922   6655   9621    692    391    387  B    N  
ATOM    647  CA  THR B  93     -42.548  -6.877  22.370  1.00 39.98      B    C  
ANISOU  647  CA  THR B  93     1730   5291   8170    535    458    149  B    C  
ATOM    648  C   THR B  93     -42.329  -7.747  21.135  1.00 46.86      B    C  
ANISOU  648  C   THR B  93     2532   6019   9253    614    574    -37  B    C  
ATOM    649  O   THR B  93     -41.339  -8.482  21.032  1.00 52.79      B    O  
ANISOU  649  O   THR B  93     3081   6802  10173    755    625    -72  B    O  
ATOM    650  CB  THR B  93     -41.560  -5.697  22.342  1.00 41.70      B    C  
ANISOU  650  CB  THR B  93     1905   5781   8156    396    463     61  B    C  
ATOM    651  CG2 THR B  93     -41.669  -4.911  21.058  1.00 36.65      B    C  
ANISOU  651  CG2 THR B  93     1377   5141   7406    223    534   -142  B    C  
ATOM    652  OG1 THR B  93     -41.828  -4.849  23.461  1.00 49.18      B    O  
ANISOU  652  OG1 THR B  93     2911   6857   8917    315    366    176  B    O  
ATOM    653  N   VAL B  94     -43.239  -7.654  20.178  1.00 42.51      B    N  
ANISOU  653  N   VAL B  94     2129   5333   8691    523    617   -175  B    N  
ATOM    654  CA  VAL B  94     -43.090  -8.412  18.947  1.00 46.55      B    C  
ANISOU  654  CA  VAL B  94     2622   5727   9336    555    729   -401  B    C  
ATOM    655  C   VAL B  94     -42.125  -7.674  18.034  1.00 56.87      B    C  
ANISOU  655  C   VAL B  94     3878   7275  10457    425    809   -592  B    C  
ATOM    656  O   VAL B  94     -42.241  -6.467  17.845  1.00 53.57      B    O  
ANISOU  656  O   VAL B  94     3565   7001   9788    236    782   -586  B    O  
ATOM    657  CB  VAL B  94     -44.428  -8.595  18.234  1.00 49.79      B    C  
ANISOU  657  CB  VAL B  94     3229   5935   9754    476    737   -482  B    C  
ATOM    658  CG1 VAL B  94     -44.196  -9.177  16.867  1.00 35.01      B    C  
ANISOU  658  CG1 VAL B  94     1324   4027   7950    460    861   -770  B    C  
ATOM    659  CG2 VAL B  94     -45.356  -9.472  19.071  1.00 45.58      B    C  
ANISOU  659  CG2 VAL B  94     2726   5156   9436    601    671   -299  B    C  
ATOM    660  N   THR B  95     -41.170  -8.400  17.469  1.00 42.47      B    N  
ANISOU  660  N   THR B  95     1877   5489   8769    525    909   -759  B    N  
ATOM    661  CA  THR B  95     -40.139  -7.765  16.666  1.00 41.21      B    C  
ANISOU  661  CA  THR B  95     1627   5603   8427    405    993   -931  B    C  
ATOM    662  C   THR B  95     -40.255  -8.126  15.192  1.00 49.48      B    C  
ANISOU  662  C   THR B  95     2692   6654   9456    330   1118  -1221  B    C  
ATOM    663  O   THR B  95     -39.702  -7.461  14.329  1.00 50.70      B    O  
ANISOU  663  O   THR B  95     2817   7056   9392    167   1186  -1357  B    O  
ATOM    664  CB  THR B  95     -38.782  -8.205  17.139  1.00 52.42      B    C  
ANISOU  664  CB  THR B  95     2783   7156   9977    562   1023   -926  B    C  
ATOM    665  CG2 THR B  95     -38.513  -7.650  18.518  1.00 44.48      B    C  
ANISOU  665  CG2 THR B  95     1733   6262   8904    583    902   -660  B    C  
ATOM    666  OG1 THR B  95     -38.767  -9.634  17.202  1.00 51.92      B    O  
ANISOU  666  OG1 THR B  95     2602   6857  10270    802   1062   -970  B    O  
ATOM    667  N   GLU B  96     -41.005  -9.169  14.902  1.00 44.81      B    N  
ANISOU  667  N   GLU B  96     2139   5806   9083    434   1146  -1316  B    N  
ATOM    668  CA  GLU B  96     -41.016  -9.685  13.562  1.00 41.96      B    C  
ANISOU  668  CA  GLU B  96     1743   5469   8728    384   1275  -1639  B    C  
ATOM    669  C   GLU B  96     -42.175 -10.640  13.434  1.00 48.73      B    C  
ANISOU  669  C   GLU B  96     2702   6007   9806    454   1270  -1696  B    C  
ATOM    670  O   GLU B  96     -42.529 -11.317  14.388  1.00 58.31      B    O  
ANISOU  670  O   GLU B  96     3912   6957  11286    622   1203  -1520  B    O  
ATOM    671  CB  GLU B  96     -39.689 -10.409  13.307  1.00 39.93      B    C  
ANISOU  671  CB  GLU B  96     1215   5307   8649    535   1392  -1843  B    C  
ATOM    672  CG  GLU B  96     -39.651 -11.191  12.024  1.00 83.72      B    C  
ANISOU  672  CG  GLU B  96     6677  10859  14273    528   1541  -2234  B    C  
ATOM    673  CD  GLU B  96     -38.352 -11.942  11.859  1.00 94.33      B    C  
ANISOU  673  CD  GLU B  96     7731  12273  15837    706   1658  -2450  B    C  
ATOM    674  OE1 GLU B  96     -37.548 -11.946  12.828  1.00 76.13      B    O  
ANISOU  674  OE1 GLU B  96     5295   9977  13656    859   1606  -2251  B    O  
ATOM    675  OE2 GLU B  96     -38.139 -12.521  10.768  1.00 96.99      B    O  
ANISOU  675  OE2 GLU B  96     7957  12676  16219    694   1802  -2827  B    O  
ATOM    676  N   VAL B  97     -42.782 -10.678  12.256  1.00 50.83      B    N  
ANISOU  676  N   VAL B  97     3046   6318   9949    308   1336  -1929  B    N  
ATOM    677  CA  VAL B  97     -43.795 -11.679  11.994  1.00 43.14      B    C  
ANISOU  677  CA  VAL B  97     2136   5058   9199    361   1352  -2051  B    C  
ATOM    678  C   VAL B  97     -43.499 -12.325  10.668  1.00 53.22      B    C  
ANISOU  678  C   VAL B  97     3292   6431  10497    319   1508  -2477  B    C  
ATOM    679  O   VAL B  97     -42.650 -11.836   9.912  1.00 50.95      B    O  
ANISOU  679  O   VAL B  97     2901   6477   9982    215   1593  -2643  B    O  
ATOM    680  CB  VAL B  97     -45.198 -11.076  11.940  1.00 45.27      B    C  
ANISOU  680  CB  VAL B  97     2643   5282   9274    199   1254  -1906  B    C  
ATOM    681  CG1 VAL B  97     -45.456 -10.248  13.163  1.00 33.14      B    C  
ANISOU  681  CG1 VAL B  97     1213   3719   7659    209   1114  -1533  B    C  
ATOM    682  CG2 VAL B  97     -45.375 -10.267  10.666  1.00 44.32      B    C  
ANISOU  682  CG2 VAL B  97     2584   5469   8785    -50   1298  -2062  B    C  
ATOM    683  N   ASP B  98     -44.183 -13.430  10.392  1.00 42.07      B    N  
ANISOU  683  N   ASP B  98     1879   4744   9361    388   1550  -2667  B    N  
ATOM    684  CA  ASP B  98     -44.101 -14.035   9.071  1.00 53.34      B    C  
ANISOU  684  CA  ASP B  98     3202   6277  10788    317   1699  -3126  B    C  
ATOM    685  C   ASP B  98     -45.497 -14.394   8.632  1.00 55.80      B    C  
ANISOU  685  C   ASP B  98     3662   6434  11104    206   1674  -3216  B    C  
ATOM    686  O   ASP B  98     -46.118 -15.272   9.207  1.00 58.09      B    O  
ANISOU  686  O   ASP B  98     3984   6339  11750    334   1638  -3164  B    O  
ATOM    687  CB  ASP B  98     -43.219 -15.271   9.063  1.00 48.16      B    C  
ANISOU  687  CB  ASP B  98     2303   5428  10565    548   1820  -3400  B    C  
ATOM    688  CG  ASP B  98     -43.245 -15.980   7.725  1.00 62.36      B    C  
ANISOU  688  CG  ASP B  98     3983   7314  12394    472   1983  -3932  B    C  
ATOM    689  OD1 ASP B  98     -44.173 -15.721   6.936  1.00 53.56      B    O  
ANISOU  689  OD1 ASP B  98     2994   6337  11019    256   1983  -4053  B    O  
ATOM    690  OD2 ASP B  98     -42.327 -16.791   7.448  1.00 65.82      B    O  
ANISOU  690  OD2 ASP B  98     4188   7709  13114    627   2115  -4245  B    O  
ATOM    691  N   PHE B  99     -45.997 -13.697   7.620  1.00 58.14      B    N  
ANISOU  691  N   PHE B  99     4042   7047  11002    -43   1686  -3324  B    N  
ATOM    692  CA  PHE B  99     -47.386 -13.869   7.208  1.00 56.21      B    C  
ANISOU  692  CA  PHE B  99     3943   6716  10698   -174   1641  -3368  B    C  
ATOM    693  C   PHE B  99     -47.436 -14.587   5.864  1.00 64.21      B    C  
ANISOU  693  C   PHE B  99     4829   7885  11683   -282   1788  -3877  B    C  
ATOM    694  O   PHE B  99     -48.501 -14.738   5.253  1.00 63.42      B    O  
ANISOU  694  O   PHE B  99     4810   7812  11475   -431   1773  -3999  B    O  
ATOM    695  CB  PHE B  99     -48.096 -12.513   7.098  1.00 56.39      B    C  
ANISOU  695  CB  PHE B  99     4152   6982  10290   -382   1518  -3071  B    C  
ATOM    696  CG  PHE B  99     -48.381 -11.847   8.423  1.00 54.17      B    C  
ANISOU  696  CG  PHE B  99     4014   6520  10048   -298   1367  -2616  B    C  
ATOM    697  CD1 PHE B  99     -48.409 -12.575   9.598  1.00 53.62      B    C  
ANISOU  697  CD1 PHE B  99     3936   6084  10356    -82   1325  -2467  B    C  
ATOM    698  CD2 PHE B  99     -48.661 -10.488   8.480  1.00 54.99      B    C  
ANISOU  698  CD2 PHE B  99     4248   6828   9816   -446   1266  -2339  B    C  
ATOM    699  CE1 PHE B  99     -48.696 -11.959  10.819  1.00 54.86      B    C  
ANISOU  699  CE1 PHE B  99     4202   6131  10510    -23   1192  -2072  B    C  
ATOM    700  CE2 PHE B  99     -48.948  -9.873   9.688  1.00 44.15      B    C  
ANISOU  700  CE2 PHE B  99     2990   5304   8483   -376   1137  -1977  B    C  
ATOM    701  CZ  PHE B  99     -48.961 -10.617  10.859  1.00 51.36      B    C  
ANISOU  701  CZ  PHE B  99     3884   5900   9730   -168   1103  -1857  B    C  
ATOM    702  N   SER B 100     -46.271 -15.027   5.405  1.00 56.34      B    N  
ANISOU  702  N   SER B 100     3615   7016  10775   -209   1933  -4193  B    N  
ATOM    703  CA  SER B 100     -46.194 -15.715   4.122  1.00 74.06      B    C  
ANISOU  703  CA  SER B 100     5702   9452  12986   -310   2094  -4737  B    C  
ATOM    704  C   SER B 100     -46.696 -17.148   4.219  1.00 76.12      B    C  
ANISOU  704  C   SER B 100     5908   9264  13753   -171   2151  -5027  B    C  
ATOM    705  O   SER B 100     -47.043 -17.742   3.205  1.00 75.54      B    O  
ANISOU  705  O   SER B 100     5747   9296  13661   -291   2259  -5479  B    O  
ATOM    706  CB  SER B 100     -44.759 -15.725   3.602  1.00 55.35      B    C  
ANISOU  706  CB  SER B 100     3091   7384  10556   -272   2244  -5011  B    C  
ATOM    707  OG  SER B 100     -44.033 -16.777   4.205  1.00 87.88      B    O  
ANISOU  707  OG  SER B 100     7050  11132  15210     16   2315  -5153  B    O  
ATOM    708  N   ALA B 101     -46.722 -17.699   5.433  1.00 76.12      B    N  
ANISOU  708  N   ALA B 101     5943   8775  14205     67   2078  -4767  B    N  
ATOM    709  CA  ALA B 101     -47.052 -19.115   5.623  1.00 78.65      B    C  
ANISOU  709  CA  ALA B 101     6186   8604  15092    222   2134  -5002  B    C  
ATOM    710  C   ALA B 101     -48.058 -19.295   6.737  1.00 77.01      B    C  
ANISOU  710  C   ALA B 101     6163   7981  15116    291   1978  -4580  B    C  
ATOM    711  O   ALA B 101     -48.225 -18.425   7.586  1.00 69.18      B    O  
ANISOU  711  O   ALA B 101     5318   7040  13929    295   1837  -4101  B    O  
ATOM    712  CB  ALA B 101     -45.792 -19.933   5.944  1.00 68.82      B    C  
ANISOU  712  CB  ALA B 101     4703   7140  14305    495   2238  -5167  B    C  
ATOM    713  N   ARG B 102     -48.702 -20.452   6.755  1.00 83.83      B    N  
ANISOU  713  N   ARG B 102     7003   8433  16417    344   2009  -4771  B    N  
ATOM    714  CA  ARG B 102     -49.589 -20.797   7.852  1.00 82.33      B    C  
ANISOU  714  CA  ARG B 102     6950   7822  16511    423   1876  -4375  B    C  
ATOM    715  C   ARG B 102     -49.253 -22.139   8.478  1.00 81.01      B    C  
ANISOU  715  C   ARG B 102     6640   7099  17040    671   1916  -4409  B    C  
ATOM    716  O   ARG B 102     -49.033 -23.110   7.771  1.00 90.16      B    O  
ANISOU  716  O   ARG B 102     7640   8081  18534    707   2056  -4887  B    O  
ATOM    717  CB  ARG B 102     -51.003 -20.796   7.348  1.00 88.56      B    C  
ANISOU  717  CB  ARG B 102     7885   8633  17133    197   1836  -4465  B    C  
ATOM    718  CG  ARG B 102     -51.286 -19.546   6.598  1.00 93.39      B    C  
ANISOU  718  CG  ARG B 102     8600   9788  17096    -41   1803  -4455  B    C  
ATOM    719  CD  ARG B 102     -52.734 -19.431   6.237  1.00103.36      B    C  
ANISOU  719  CD  ARG B 102    10008  11094  18169   -252   1731  -4452  B    C  
ATOM    720  NE  ARG B 102     -52.970 -18.128   5.648  1.00114.07      B    N  
ANISOU  720  NE  ARG B 102    11463  12959  18921   -455   1673  -4339  B    N  
ATOM    721  CZ  ARG B 102     -53.979 -17.851   4.840  1.00133.97      B    C  
ANISOU  721  CZ  ARG B 102    14049  15721  21132   -685   1645  -4454  B    C  
ATOM    722  NH1 ARG B 102     -54.851 -18.803   4.523  1.00142.98      B    N  
ANISOU  722  NH1 ARG B 102    15172  16653  22501   -753   1676  -4722  B    N  
ATOM    723  NH2 ARG B 102     -54.109 -16.624   4.350  1.00136.96      B    N  
ANISOU  723  NH2 ARG B 102    14502  16548  20990   -852   1581  -4291  B    N  
ATOM    724  N   PRO B 103     -49.241 -22.199   9.816  1.00 74.76      B    N  
ANISOU  724  N   PRO B 103     5894   6035  16477    840   1792  -3895  B    N  
ATOM    725  CA  PRO B 103     -49.696 -21.104  10.669  1.00 52.57      B    C  
ANISOU  725  CA  PRO B 103     3273   3417  13284    776   1630  -3374  B    C  
ATOM    726  C   PRO B 103     -48.728 -19.944  10.628  1.00 54.35      B    C  
ANISOU  726  C   PRO B 103     3482   4089  13081    766   1623  -3278  B    C  
ATOM    727  O   PRO B 103     -47.550 -20.139  10.344  1.00 61.57      B    O  
ANISOU  727  O   PRO B 103     4213   5079  14099    884   1721  -3480  B    O  
ATOM    728  CB  PRO B 103     -49.669 -21.720  12.073  1.00 75.63      B    C  
ANISOU  728  CB  PRO B 103     6164   5933  16640    988   1532  -2926  B    C  
ATOM    729  CG  PRO B 103     -49.437 -23.207  11.863  1.00 72.54      B    C  
ANISOU  729  CG  PRO B 103     5595   5067  16901   1139   1635  -3206  B    C  
ATOM    730  CD  PRO B 103     -48.675 -23.302  10.605  1.00 61.98      B    C  
ANISOU  730  CD  PRO B 103     4116   3932  15501   1112   1803  -3780  B    C  
ATOM    731  N   PHE B 104     -49.239 -18.749  10.919  1.00 57.25      B    N  
ANISOU  731  N   PHE B 104     4029   4733  12992    625   1508  -2975  B    N  
ATOM    732  CA  PHE B 104     -48.430 -17.551  11.012  1.00 59.58      B    C  
ANISOU  732  CA  PHE B 104     4329   5417  12890    593   1481  -2824  B    C  
ATOM    733  C   PHE B 104     -47.449 -17.639  12.162  1.00 63.92      B    C  
ANISOU  733  C   PHE B 104     4767   5864  13655    819   1435  -2522  B    C  
ATOM    734  O   PHE B 104     -47.733 -18.210  13.208  1.00 62.12      B    O  
ANISOU  734  O   PHE B 104     4539   5327  13738    958   1356  -2228  B    O  
ATOM    735  CB  PHE B 104     -49.305 -16.316  11.210  1.00 47.02      B    C  
ANISOU  735  CB  PHE B 104     2953   4055  10857    411   1356  -2542  B    C  
ATOM    736  CG  PHE B 104     -50.319 -16.132  10.153  1.00 49.56      B    C  
ANISOU  736  CG  PHE B 104     3380   4515  10936    189   1373  -2766  B    C  
ATOM    737  CD1 PHE B 104     -49.928 -15.948   8.829  1.00 63.12      B    C  
ANISOU  737  CD1 PHE B 104     5023   6546  12412     49   1486  -3143  B    C  
ATOM    738  CD2 PHE B 104     -51.670 -16.121  10.471  1.00 49.08      B    C  
ANISOU  738  CD2 PHE B 104     3475   4312  10862    108   1275  -2594  B    C  
ATOM    739  CE1 PHE B 104     -50.878 -15.769   7.832  1.00 70.02      B    C  
ANISOU  739  CE1 PHE B 104     5975   7599  13031   -170   1493  -3335  B    C  
ATOM    740  CE2 PHE B 104     -52.638 -15.948   9.476  1.00 53.93      B    C  
ANISOU  740  CE2 PHE B 104     4169   5082  11239   -101   1282  -2792  B    C  
ATOM    741  CZ  PHE B 104     -52.242 -15.763   8.160  1.00 62.18      B    C  
ANISOU  741  CZ  PHE B 104     5138   6451  12037   -242   1386  -3153  B    C  
ATOM    742  N   ARG B 105     -46.299 -17.022  11.965  1.00 65.10      B    N  
ANISOU  742  N   ARG B 105     4814   6315  13605    836   1480  -2574  B    N  
ATOM    743  CA  ARG B 105     -45.261 -17.027  12.956  1.00 55.39      B    C  
ANISOU  743  CA  ARG B 105     3451   5067  12529   1034   1441  -2319  B    C  
ATOM    744  C   ARG B 105     -45.160 -15.616  13.527  1.00 56.39      B    C  
ANISOU  744  C   ARG B 105     3690   5516  12218    925   1333  -2002  B    C  
ATOM    745  O   ARG B 105     -45.035 -14.642  12.775  1.00 52.24      B    O  
ANISOU  745  O   ARG B 105     3228   5326  11297    739   1361  -2125  B    O  
ATOM    746  CB  ARG B 105     -43.962 -17.475  12.283  1.00 56.95      B    C  
ANISOU  746  CB  ARG B 105     3407   5359  12873   1144   1587  -2662  B    C  
ATOM    747  CG  ARG B 105     -42.897 -17.953  13.238  1.00 90.23      B    C  
ANISOU  747  CG  ARG B 105     7421   9447  17417   1408   1565  -2455  B    C  
ATOM    748  CD  ARG B 105     -41.775 -18.742  12.511  1.00121.34      B    C  
ANISOU  748  CD  ARG B 105    11091  13368  21646   1559   1727  -2860  B    C  
ATOM    749  NE  ARG B 105     -41.166 -17.997  11.406  1.00127.59      B    N  
ANISOU  749  NE  ARG B 105    11837  14607  22034   1392   1839  -3194  B    N  
ATOM    750  CZ  ARG B 105     -40.502 -16.838  11.530  1.00122.90      B    C  
ANISOU  750  CZ  ARG B 105    11248  14417  21031   1293   1806  -3041  B    C  
ATOM    751  NH1 ARG B 105     -40.342 -16.230  12.717  1.00 77.30      B    N  
ANISOU  751  NH1 ARG B 105     5524   8679  15169   1340   1664  -2590  B    N  
ATOM    752  NH2 ARG B 105     -39.993 -16.267  10.443  1.00136.49      B    N  
ANISOU  752  NH2 ARG B 105    12914  16531  22415   1126   1918  -3348  B    N  
ATOM    753  N   VAL B 106     -45.264 -15.515  14.856  1.00 62.35      B    N  
ANISOU  753  N   VAL B 106     4468   6169  13052   1026   1207  -1595  B    N  
ATOM    754  CA  VAL B 106     -45.091 -14.256  15.586  1.00 38.29      B    C  
ANISOU  754  CA  VAL B 106     1496   3399   9654    948   1104  -1306  B    C  
ATOM    755  C   VAL B 106     -44.021 -14.400  16.672  1.00 46.22      B    C  
ANISOU  755  C   VAL B 106     2319   4437  10805   1137   1058  -1063  B    C  
ATOM    756  O   VAL B 106     -44.105 -15.291  17.505  1.00 70.33      B    O  
ANISOU  756  O   VAL B 106     5291   7238  14193   1310   1010   -855  B    O  
ATOM    757  CB  VAL B 106     -46.396 -13.833  16.263  1.00 45.38      B    C  
ANISOU  757  CB  VAL B 106     2596   4220  10428    855    981  -1038  B    C  
ATOM    758  CG1 VAL B 106     -46.214 -12.497  17.002  1.00 48.39      B    C  
ANISOU  758  CG1 VAL B 106     3041   4880  10467    770    884   -795  B    C  
ATOM    759  CG2 VAL B 106     -47.511 -13.736  15.243  1.00 47.66      B    C  
ANISOU  759  CG2 VAL B 106     3046   4477  10584    679   1011  -1248  B    C  
ATOM    760  N   THR B 107     -43.019 -13.535  16.674  1.00 46.21      B    N  
ANISOU  760  N   THR B 107     2243   4758  10557   1095   1067  -1067  B    N  
ATOM    761  CA  THR B 107     -41.884 -13.724  17.591  1.00 55.30      B    C  
ANISOU  761  CA  THR B 107     3182   5986  11844   1274   1034   -876  B    C  
ATOM    762  C   THR B 107     -41.453 -12.452  18.274  1.00 50.48      B    C  
ANISOU  762  C   THR B 107     2591   5708  10880   1168    951   -679  B    C  
ATOM    763  O   THR B 107     -41.492 -11.359  17.698  1.00 52.66      B    O  
ANISOU  763  O   THR B 107     2981   6211  10817    964    968   -792  B    O  
ATOM    764  CB  THR B 107     -40.595 -14.302  16.915  1.00 55.29      B    C  
ANISOU  764  CB  THR B 107     2938   6039  12032   1405   1163  -1147  B    C  
ATOM    765  CG2 THR B 107     -40.903 -15.421  15.953  1.00 63.97      B    C  
ANISOU  765  CG2 THR B 107     4003   6855  13448   1472   1281  -1475  B    C  
ATOM    766  OG1 THR B 107     -39.953 -13.259  16.192  1.00 70.94      B    O  
ANISOU  766  OG1 THR B 107     4920   8387  13647   1232   1223  -1331  B    O  
ATOM    767  N   SER B 108     -41.015 -12.624  19.511  1.00 55.43      B    N  
ANISOU  767  N   SER B 108     3090   6368  11604   1306    859   -379  B    N  
ATOM    768  CA  SER B 108     -40.437 -11.557  20.301  1.00 49.81      B    C  
ANISOU  768  CA  SER B 108     2339   5985  10603   1230    780   -209  B    C  
ATOM    769  C   SER B 108     -38.993 -11.952  20.547  1.00 56.18      B    C  
ANISOU  769  C   SER B 108     2860   6935  11551   1396    809   -196  B    C  
ATOM    770  O   SER B 108     -38.520 -12.959  20.023  1.00 62.12      B    O  
ANISOU  770  O   SER B 108     3466   7520  12615   1561    895   -341  B    O  
ATOM    771  CB  SER B 108     -41.125 -11.514  21.642  1.00 39.11      B    C  
ANISOU  771  CB  SER B 108     1026   4606   9228   1256    643    140  B    C  
ATOM    772  OG  SER B 108     -40.846 -12.717  22.348  1.00 60.84      B    O  
ANISOU  772  OG  SER B 108     3594   7193  12330   1489    607    357  B    O  
ATOM    773  N   ASP B 109     -38.293 -11.184  21.371  1.00 67.63      B    N  
ANISOU  773  N   ASP B 109     4225   8688  12783   1353    734    -33  B    N  
ATOM    774  CA  ASP B 109     -36.950 -11.582  21.771  1.00 70.59      B    C  
ANISOU  774  CA  ASP B 109     4318   9220  13283   1517    737     31  B    C  
ATOM    775  C   ASP B 109     -36.929 -12.997  22.305  1.00 64.85      B    C  
ANISOU  775  C   ASP B 109     3421   8224  12997   1794    707    229  B    C  
ATOM    776  O   ASP B 109     -36.032 -13.751  22.006  1.00 67.24      B    O  
ANISOU  776  O   ASP B 109     3489   8481  13578   1985    772    145  B    O  
ATOM    777  CB  ASP B 109     -36.429 -10.665  22.870  1.00 76.47      B    C  
ANISOU  777  CB  ASP B 109     5023  10302  13728   1423    625    246  B    C  
ATOM    778  CG  ASP B 109     -35.592  -9.535  22.331  1.00 84.54      B    C  
ANISOU  778  CG  ASP B 109     6030  11639  14451   1238    679     36  B    C  
ATOM    779  OD1 ASP B 109     -35.363  -9.488  21.094  1.00 69.52      B    O  
ANISOU  779  OD1 ASP B 109     4128   9722  12561   1186    806   -253  B    O  
ATOM    780  OD2 ASP B 109     -35.167  -8.692  23.152  1.00 86.47      B    O  
ANISOU  780  OD2 ASP B 109     6249  12164  14445   1134    598    158  B    O  
ATOM    781  N   SER B 110     -37.920 -13.349  23.112  1.00 72.45      B    N  
ANISOU  781  N   SER B 110     4486   9008  14032   1818    607    507  B    N  
ATOM    782  CA  SER B 110     -37.845 -14.581  23.890  1.00 67.22      B    C  
ANISOU  782  CA  SER B 110     3640   8135  13766   2065    544    809  B    C  
ATOM    783  C   SER B 110     -38.763 -15.685  23.403  1.00 67.74      B    C  
ANISOU  783  C   SER B 110     3781   7729  14227   2165    590    759  B    C  
ATOM    784  O   SER B 110     -38.512 -16.856  23.645  1.00 80.64      B    O  
ANISOU  784  O   SER B 110     5241   9100  16301   2391    583    906  B    O  
ATOM    785  CB  SER B 110     -38.155 -14.284  25.352  1.00 73.10      B    C  
ANISOU  785  CB  SER B 110     4381   9073  14320   2026    385   1228  B    C  
ATOM    786  OG  SER B 110     -37.339 -13.225  25.818  1.00 79.68      B    O  
ANISOU  786  OG  SER B 110     5153  10344  14776   1910    344   1239  B    O  
ATOM    787  N   THR B 111     -39.829 -15.319  22.714  1.00 58.96      B    N  
ANISOU  787  N   THR B 111     2936   6499  12968   1984    635    556  B    N  
ATOM    788  CA  THR B 111     -40.839 -16.298  22.388  1.00 46.07      B    C  
ANISOU  788  CA  THR B 111     1406   4439  11660   2031    660    532  B    C  
ATOM    789  C   THR B 111     -41.222 -16.361  20.912  1.00 68.89      B    C  
ANISOU  789  C   THR B 111     4434   7171  14569   1930    802     74  B    C  
ATOM    790  O   THR B 111     -41.141 -15.368  20.176  1.00 60.72      B    O  
ANISOU  790  O   THR B 111     3512   6383  13176   1747    856   -175  B    O  
ATOM    791  CB  THR B 111     -42.084 -16.040  23.208  1.00 56.42      B    C  
ANISOU  791  CB  THR B 111     2893   5729  12817   1917    549    815  B    C  
ATOM    792  CG2 THR B 111     -43.107 -17.131  22.978  1.00 47.90      B    C  
ANISOU  792  CG2 THR B 111     1893   4204  12103   1964    566    833  B    C  
ATOM    793  OG1 THR B 111     -41.723 -16.005  24.593  1.00 69.05      B    O  
ANISOU  793  OG1 THR B 111     4338   7531  14367   1997    419   1237  B    O  
ATOM    794  N   THR B 112     -41.624 -17.551  20.487  1.00 64.33      B    N  
ANISOU  794  N   THR B 112     3833   6188  14423   2044    859    -29  B    N  
ATOM    795  CA  THR B 112     -42.115 -17.745  19.145  1.00 47.76      B    C  
ANISOU  795  CA  THR B 112     1851   3938  12356   1940    987   -466  B    C  
ATOM    796  C   THR B 112     -43.457 -18.431  19.177  1.00 64.45      B    C  
ANISOU  796  C   THR B 112     4114   5691  14682   1902    961   -407  B    C  
ATOM    797  O   THR B 112     -43.615 -19.477  19.807  1.00 77.44      B    O  
ANISOU  797  O   THR B 112     5661   7007  16755   2064    918   -178  B    O  
ATOM    798  CB  THR B 112     -41.168 -18.591  18.352  1.00 51.20      B    C  
ANISOU  798  CB  THR B 112     2072   4236  13145   2107   1122   -793  B    C  
ATOM    799  CG2 THR B 112     -41.747 -18.859  16.985  1.00 58.81      B    C  
ANISOU  799  CG2 THR B 112     3141   5070  14133   1984   1256  -1265  B    C  
ATOM    800  OG1 THR B 112     -39.931 -17.883  18.212  1.00 57.86      B    O  
ANISOU  800  OG1 THR B 112     2775   5457  13750   2114   1158   -882  B    O  
ATOM    801  N   VAL B 113     -44.420 -17.855  18.475  1.00 51.47      B    N  
ANISOU  801  N   VAL B 113     2695   4109  12753   1682    985   -601  B    N  
ATOM    802  CA  VAL B 113     -45.774 -18.372  18.490  1.00 52.91      B    C  
ANISOU  802  CA  VAL B 113     3028   4002  13073   1610    955   -553  B    C  
ATOM    803  C   VAL B 113     -46.207 -18.756  17.094  1.00 59.03      B    C  
ANISOU  803  C   VAL B 113     3865   4644  13919   1512   1084  -1024  B    C  
ATOM    804  O   VAL B 113     -45.995 -18.006  16.140  1.00 58.47      B    O  
ANISOU  804  O   VAL B 113     3850   4851  13515   1370   1155  -1321  B    O  
ATOM    805  CB  VAL B 113     -46.767 -17.321  18.963  1.00 51.59      B    C  
ANISOU  805  CB  VAL B 113     3075   4043  12484   1421    850   -344  B    C  
ATOM    806  CG1 VAL B 113     -48.165 -17.900  18.898  1.00 53.65      B    C  
ANISOU  806  CG1 VAL B 113     3473   4019  12892   1342    829   -320  B    C  
ATOM    807  CG2 VAL B 113     -46.439 -16.828  20.367  1.00 49.21      B    C  
ANISOU  807  CG2 VAL B 113     2715   3938  12045   1480    723     88  B    C  
ATOM    808  N   LEU B 114     -46.811 -19.931  16.968  1.00 55.36      B    N  
ANISOU  808  N   LEU B 114     3381   3767  13887   1572   1113  -1092  B    N  
ATOM    809  CA  LEU B 114     -47.390 -20.339  15.698  1.00 52.76      B    C  
ANISOU  809  CA  LEU B 114     3111   3315  13619   1452   1228  -1551  B    C  
ATOM    810  C   LEU B 114     -48.919 -20.164  15.802  1.00 58.84      B    C  
ANISOU  810  C   LEU B 114     4098   4016  14241   1268   1152  -1433  B    C  
ATOM    811  O   LEU B 114     -49.577 -20.821  16.598  1.00 67.56      B    O  
ANISOU  811  O   LEU B 114     5216   4827  15627   1320   1080  -1151  B    O  
ATOM    812  CB  LEU B 114     -46.950 -21.762  15.310  1.00 53.48      B    C  
ANISOU  812  CB  LEU B 114     3008   2996  14317   1629   1337  -1813  B    C  
ATOM    813  CG  LEU B 114     -45.418 -21.838  15.122  1.00 68.11      B    C  
ANISOU  813  CG  LEU B 114     4629   4969  16281   1810   1419  -1967  B    C  
ATOM    814  CD1 LEU B 114     -44.891 -23.231  14.795  1.00 60.36      B    C  
ANISOU  814  CD1 LEU B 114     3423   3562  15950   2021   1528  -2231  B    C  
ATOM    815  CD2 LEU B 114     -44.936 -20.856  14.065  1.00 61.51      B    C  
ANISOU  815  CD2 LEU B 114     3819   4599  14954   1651   1511  -2324  B    C  
ATOM    816  N   ALA B 115     -49.459 -19.241  15.016  1.00 50.71      B    N  
ANISOU  816  N   ALA B 115     3223   3282  12760   1052   1166  -1624  B    N  
ATOM    817  CA  ALA B 115     -50.836 -18.824  15.168  1.00 42.27      B    C  
ANISOU  817  CA  ALA B 115     2352   2234  11475    881   1080  -1479  B    C  
ATOM    818  C   ALA B 115     -51.656 -19.032  13.903  1.00 57.52      B    C  
ANISOU  818  C   ALA B 115     4361   4158  13337    701   1157  -1880  B    C  
ATOM    819  O   ALA B 115     -51.207 -18.723  12.800  1.00 59.44      B    O  
ANISOU  819  O   ALA B 115     4571   4632  13380    617   1252  -2237  B    O  
ATOM    820  CB  ALA B 115     -50.886 -17.379  15.574  1.00 46.60      B    C  
ANISOU  820  CB  ALA B 115     3020   3158  11527    783    988  -1247  B    C  
ATOM    821  N   ASP B 116     -52.865 -19.550  14.083  1.00 43.49      B    N  
ANISOU  821  N   ASP B 116     2670   2148  11708    630   1113  -1810  B    N  
ATOM    822  CA  ASP B 116     -53.811 -19.744  12.994  1.00 45.93      B    C  
ANISOU  822  CA  ASP B 116     3051   2466  11934    439   1165  -2153  B    C  
ATOM    823  C   ASP B 116     -54.368 -18.420  12.485  1.00 57.80      B    C  
ANISOU  823  C   ASP B 116     4706   4388  12868    241   1112  -2146  B    C  
ATOM    824  O   ASP B 116     -54.642 -18.275  11.299  1.00 72.07      B    O  
ANISOU  824  O   ASP B 116     6528   6383  14472     83   1175  -2486  B    O  
ATOM    825  CB  ASP B 116     -54.939 -20.654  13.467  1.00 47.26      B    C  
ANISOU  825  CB  ASP B 116     3257   2265  12435    418   1120  -2029  B    C  
ATOM    826  CG  ASP B 116     -54.446 -22.061  13.753  1.00 64.55      B    C  
ANISOU  826  CG  ASP B 116     5285   3989  15251    594   1183  -2085  B    C  
ATOM    827  OD1 ASP B 116     -53.509 -22.492  13.053  1.00 60.70      B    O  
ANISOU  827  OD1 ASP B 116     4660   3462  14941    675   1303  -2439  B    O  
ATOM    828  OD2 ASP B 116     -54.980 -22.728  14.663  1.00 76.03      B    O  
ANISOU  828  OD2 ASP B 116     6737   5122  17030    650   1115  -1773  B    O  
ATOM    829  N   THR B 117     -54.543 -17.471  13.402  1.00 56.74      B    N  
ANISOU  829  N   THR B 117     4667   4400  12491    250    994  -1752  B    N  
ATOM    830  CA  THR B 117     -54.885 -16.091  13.064  1.00 41.33      B    C  
ANISOU  830  CA  THR B 117     2842   2820  10043     99    935  -1691  B    C  
ATOM    831  C   THR B 117     -54.113 -15.152  13.945  1.00 41.60      B    C  
ANISOU  831  C   THR B 117     2878   3021   9908    184    872  -1397  B    C  
ATOM    832  O   THR B 117     -53.694 -15.507  15.045  1.00 55.22      B    O  
ANISOU  832  O   THR B 117     4538   4595  11850    339    835  -1150  B    O  
ATOM    833  CB  THR B 117     -56.367 -15.751  13.271  1.00 40.66      B    C  
ANISOU  833  CB  THR B 117     2899   2738   9813    -28    837  -1531  B    C  
ATOM    834  CG2 THR B 117     -57.226 -16.546  12.320  1.00 41.89      B    C  
ANISOU  834  CG2 THR B 117     3056   2789  10073   -153    890  -1836  B    C  
ATOM    835  OG1 THR B 117     -56.718 -16.051  14.624  1.00 46.61      B    O  
ANISOU  835  OG1 THR B 117     3660   3285  10764     80    755  -1179  B    O  
ATOM    836  N   VAL B 118     -53.934 -13.942  13.438  1.00 43.28      B    N  
ANISOU  836  N   VAL B 118     3155   3559   9732     68    855  -1418  B    N  
ATOM    837  CA  VAL B 118     -53.260 -12.898  14.161  1.00 41.46      B    C  
ANISOU  837  CA  VAL B 118     2934   3510   9310    108    797  -1180  B    C  
ATOM    838  C   VAL B 118     -54.122 -11.640  14.130  1.00 44.44      B    C  
ANISOU  838  C   VAL B 118     3460   4076   9347    -38    702  -1038  B    C  
ATOM    839  O   VAL B 118     -54.674 -11.264  13.095  1.00 45.32      B    O  
ANISOU  839  O   VAL B 118     3635   4324   9259   -190    712  -1185  B    O  
ATOM    840  CB  VAL B 118     -51.883 -12.601  13.524  1.00 35.61      B    C  
ANISOU  840  CB  VAL B 118     2086   2975   8471    116    885  -1363  B    C  
ATOM    841  CG1 VAL B 118     -51.264 -11.371  14.149  1.00 42.48      B    C  
ANISOU  841  CG1 VAL B 118     2976   4060   9104    109    821  -1141  B    C  
ATOM    842  CG2 VAL B 118     -50.979 -13.759  13.709  1.00 46.22      B    C  
ANISOU  842  CG2 VAL B 118     3260   4125  10174    293    968  -1475  B    C  
ATOM    843  N   VAL B 119     -54.233 -10.994  15.279  1.00 45.35      B    N  
ANISOU  843  N   VAL B 119     3614   4211   9408     12    611   -751  B    N  
ATOM    844  CA  VAL B 119     -54.833  -9.688  15.342  1.00 35.16      B    C  
ANISOU  844  CA  VAL B 119     2440   3086   7833    -99    527   -624  B    C  
ATOM    845  C   VAL B 119     -53.759  -8.667  15.634  1.00 45.57      B    C  
ANISOU  845  C   VAL B 119     3727   4593   8994    -95    518   -552  B    C  
ATOM    846  O   VAL B 119     -53.206  -8.641  16.724  1.00 49.84      B    O  
ANISOU  846  O   VAL B 119     4204   5124   9607     11    490   -399  B    O  
ATOM    847  CB  VAL B 119     -55.914  -9.621  16.427  1.00 40.16      B    C  
ANISOU  847  CB  VAL B 119     3133   3620   8508    -68    431   -393  B    C  
ATOM    848  CG1 VAL B 119     -56.469  -8.205  16.544  1.00 20.40      B    C  
ANISOU  848  CG1 VAL B 119      730   1273   5750   -159    349   -284  B    C  
ATOM    849  CG2 VAL B 119     -57.051 -10.622  16.119  1.00 30.42      B    C  
ANISOU  849  CG2 VAL B 119     1927   2201   7430    -95    437   -459  B    C  
ATOM    850  N   VAL B 120     -53.456  -7.834  14.649  1.00 39.36      B    N  
ANISOU  850  N   VAL B 120     2972   3998   7987   -226    540   -655  B    N  
ATOM    851  CA  VAL B 120     -52.605  -6.668  14.862  1.00 29.40      B    C  
ANISOU  851  CA  VAL B 120     1698   2912   6560   -268    521   -572  B    C  
ATOM    852  C   VAL B 120     -53.423  -5.506  15.462  1.00 51.46      B    C  
ANISOU  852  C   VAL B 120     4602   5717   9233   -324    411   -383  B    C  
ATOM    853  O   VAL B 120     -54.364  -4.978  14.818  1.00 40.60      B    O  
ANISOU  853  O   VAL B 120     3323   4362   7742   -433    368   -371  B    O  
ATOM    854  CB  VAL B 120     -52.001  -6.182  13.525  1.00 28.74      B    C  
ANISOU  854  CB  VAL B 120     1598   3037   6285   -411    585   -726  B    C  
ATOM    855  CG1 VAL B 120     -51.086  -5.005  13.753  1.00 22.64      B    C  
ANISOU  855  CG1 VAL B 120      805   2426   5370   -470    567   -630  B    C  
ATOM    856  CG2 VAL B 120     -51.330  -7.312  12.778  1.00 25.52      B    C  
ANISOU  856  CG2 VAL B 120     1073   2641   5982   -371    705   -977  B    C  
ATOM    857  N   ALA B 121     -53.043  -5.099  16.677  1.00 37.98      B    N  
ANISOU  857  N   ALA B 121     2860   4014   7555   -250    367   -247  B    N  
ATOM    858  CA  ALA B 121     -53.740  -4.055  17.431  1.00 28.59      B    C  
ANISOU  858  CA  ALA B 121     1743   2830   6290   -281    274   -109  B    C  
ATOM    859  C   ALA B 121     -52.690  -3.275  18.201  1.00 46.07      B    C  
ANISOU  859  C   ALA B 121     3887   5161   8456   -274    264    -63  B    C  
ATOM    860  O   ALA B 121     -52.779  -3.113  19.416  1.00 37.94      B    O  
ANISOU  860  O   ALA B 121     2846   4132   7440   -204    216     29  B    O  
ATOM    861  CB  ALA B 121     -54.772  -4.688  18.412  1.00 27.81      B    C  
ANISOU  861  CB  ALA B 121     1655   2609   6305   -187    226     -5  B    C  
ATOM    862  N   THR B 122     -51.688  -2.793  17.481  1.00 33.66      B    N  
ANISOU  862  N   THR B 122     2285   3707   6799   -355    311   -136  B    N  
ATOM    863  CA  THR B 122     -50.538  -2.190  18.112  1.00 30.38      B    C  
ANISOU  863  CA  THR B 122     1778   3417   6347   -361    314   -119  B    C  
ATOM    864  C   THR B 122     -50.712  -0.678  18.195  1.00 43.63      B    C  
ANISOU  864  C   THR B 122     3556   5112   7911   -477    253    -75  B    C  
ATOM    865  O   THR B 122     -49.874   0.015  18.738  1.00 35.00      B    O  
ANISOU  865  O   THR B 122     2418   4107   6775   -504    246    -75  B    O  
ATOM    866  CB  THR B 122     -49.259  -2.492  17.342  1.00 43.79      B    C  
ANISOU  866  CB  THR B 122     3378   5240   8018   -385    405   -228  B    C  
ATOM    867  CG2 THR B 122     -48.845  -3.950  17.495  1.00 33.93      B    C  
ANISOU  867  CG2 THR B 122     2019   3946   6929   -226    464   -281  B    C  
ATOM    868  OG1 THR B 122     -49.488  -2.220  15.963  1.00 39.27      B    O  
ANISOU  868  OG1 THR B 122     2873   4706   7342   -518    438   -299  B    O  
ATOM    869  N   GLY B 123     -51.812  -0.169  17.653  1.00 45.53      B    N  
ANISOU  869  N   GLY B 123     3915   5260   8124   -543    208    -40  B    N  
ATOM    870  CA  GLY B 123     -52.194   1.205  17.926  1.00 29.96      B    C  
ANISOU  870  CA  GLY B 123     2024   3241   6118   -611    138     16  B    C  
ATOM    871  C   GLY B 123     -51.324   2.242  17.268  1.00 36.86      B    C  
ANISOU  871  C   GLY B 123     2885   4191   6928   -763    151     22  B    C  
ATOM    872  O   GLY B 123     -50.816   2.042  16.161  1.00 49.10      B    O  
ANISOU  872  O   GLY B 123     4405   5840   8411   -859    205      4  B    O  
ATOM    873  N   ALA B 124     -51.125   3.353  17.964  1.00 30.07      B    N  
ANISOU  873  N   ALA B 124     2031   3301   6094   -801    108     35  B    N  
ATOM    874  CA  ALA B 124     -50.379   4.470  17.395  1.00 39.05      B    C  
ANISOU  874  CA  ALA B 124     3158   4473   7206   -967    111     62  B    C  
ATOM    875  C   ALA B 124     -49.875   5.369  18.518  1.00 33.56      B    C  
ANISOU  875  C   ALA B 124     2415   3765   6569   -984     85      8  B    C  
ATOM    876  O   ALA B 124     -50.146   5.139  19.692  1.00 52.86      B    O  
ANISOU  876  O   ALA B 124     4830   6208   9047   -873     66    -52  B    O  
ATOM    877  CB  ALA B 124     -51.282   5.267  16.384  1.00 29.43      B    C  
ANISOU  877  CB  ALA B 124     2039   3139   6003  -1075     55    187  B    C  
ATOM    878  N   VAL B 125     -49.136   6.392  18.154  1.00 24.95      B    N  
ANISOU  878  N   VAL B 125     1304   2688   5490  -1143     88     26  B    N  
ATOM    879  CA  VAL B 125     -48.547   7.290  19.141  1.00 48.23      B    C  
ANISOU  879  CA  VAL B 125     4185   5635   8504  -1195     73    -60  B    C  
ATOM    880  C   VAL B 125     -48.535   8.718  18.618  1.00 40.18      B    C  
ANISOU  880  C   VAL B 125     3205   4464   7596  -1376     35      7  B    C  
ATOM    881  O   VAL B 125     -48.133   8.943  17.496  1.00 38.86      B    O  
ANISOU  881  O   VAL B 125     3053   4331   7383  -1509     54    122  B    O  
ATOM    882  CB  VAL B 125     -47.093   6.906  19.484  1.00 42.82      B    C  
ANISOU  882  CB  VAL B 125     3364   5178   7726  -1218    135   -139  B    C  
ATOM    883  CG1 VAL B 125     -46.481   8.001  20.308  1.00 43.08      B    C  
ANISOU  883  CG1 VAL B 125     3325   5219   7823  -1326    116   -234  B    C  
ATOM    884  CG2 VAL B 125     -47.075   5.642  20.284  1.00 42.41      B    C  
ANISOU  884  CG2 VAL B 125     3251   5243   7619  -1032    153   -186  B    C  
ATOM    885  N   ALA B 126     -48.981   9.671  19.419  1.00 35.27      B    N  
ANISOU  885  N   ALA B 126     2585   3681   7134  -1388    -15    -63  B    N  
ATOM    886  CA  ALA B 126     -49.080  11.047  18.938  1.00 43.31      B    C  
ANISOU  886  CA  ALA B 126     3639   4487   8331  -1551    -59     16  B    C  
ATOM    887  C   ALA B 126     -47.679  11.517  18.631  1.00 43.94      B    C  
ANISOU  887  C   ALA B 126     3643   4679   8374  -1735    -15     18  B    C  
ATOM    888  O   ALA B 126     -46.762  11.263  19.399  1.00 54.94      B    O  
ANISOU  888  O   ALA B 126     4931   6252   9691  -1732     29   -131  B    O  
ATOM    889  CB  ALA B 126     -49.742  11.958  19.980  1.00 27.66      B    C  
ANISOU  889  CB  ALA B 126     1642   2299   6570  -1528   -110   -126  B    C  
ATOM    890  N   ARG B 127     -47.521  12.182  17.492  1.00 43.00      B    N  
ANISOU  890  N   ARG B 127     3563   4481   8296  -1905    -29    208  B    N  
ATOM    891  CA  ARG B 127     -46.237  12.747  17.080  1.00 37.59      B    C  
ANISOU  891  CA  ARG B 127     2800   3895   7586  -2118     12    245  B    C  
ATOM    892  C   ARG B 127     -45.923  14.031  17.816  1.00 42.59      B    C  
ANISOU  892  C   ARG B 127     3389   4333   8459  -2243    -17    145  B    C  
ATOM    893  O   ARG B 127     -46.839  14.795  18.151  1.00 45.46      B    O  
ANISOU  893  O   ARG B 127     3806   4404   9064  -2217    -82    135  B    O  
ATOM    894  CB  ARG B 127     -46.237  13.051  15.584  1.00 40.15      B    C  
ANISOU  894  CB  ARG B 127     3166   4222   7866  -2285      3    517  B    C  
ATOM    895  CG  ARG B 127     -46.002  11.862  14.715  1.00 59.96      B    C  
ANISOU  895  CG  ARG B 127     5656   7020  10105  -2252     67    563  B    C  
ATOM    896  CD  ARG B 127     -46.843  11.908  13.469  1.00 67.54      B    C  
ANISOU  896  CD  ARG B 127     6690   7948  11024  -2318     27    804  B    C  
ATOM    897  NE  ARG B 127     -45.990  11.884  12.296  1.00 73.68      B    N  
ANISOU  897  NE  ARG B 127     7393   8981  11621  -2531     86    941  B    N  
ATOM    898  CZ  ARG B 127     -45.339  12.955  11.844  1.00 92.99      B    C  
ANISOU  898  CZ  ARG B 127     9796  11401  14133  -2773     76   1109  B    C  
ATOM    899  NH1 ARG B 127     -45.464  14.110  12.479  1.00 76.95      B    N  
ANISOU  899  NH1 ARG B 127     7796   9059  12381  -2824      9   1140  B    N  
ATOM    900  NH2 ARG B 127     -44.567  12.881  10.761  1.00104.39      B    N  
ANISOU  900  NH2 ARG B 127    11165  13134  15365  -2958    135   1236  B    N  
ATOM    901  N   ARG B 128     -44.634  14.272  18.052  1.00 50.30      B    N  
ANISOU  901  N   ARG B 128     3839   3083  12191    202     18    778  B    N  
ATOM    902  CA  ARG B 128     -44.174  15.565  18.588  1.00 48.19      B    C  
ANISOU  902  CA  ARG B 128     3374   2778  12156    263   -160    710  B    C  
ATOM    903  C   ARG B 128     -42.865  16.012  17.939  1.00 46.66      B    C  
ANISOU  903  C   ARG B 128     3093   2405  12232    338   -156    896  B    C  
ATOM    904  O   ARG B 128     -42.214  15.272  17.196  1.00 38.59      B    O  
ANISOU  904  O   ARG B 128     2155   1293  11213    362      1   1076  B    O  
ATOM    905  CB  ARG B 128     -44.000  15.508  20.114  1.00 49.19      B    C  
ANISOU  905  CB  ARG B 128     3469   2990  12230    264   -284    597  B    C  
ATOM    906  CG  ARG B 128     -43.018  14.420  20.558  1.00 52.14      B    C  
ANISOU  906  CG  ARG B 128     3930   3321  12560    269   -225    730  B    C  
ATOM    907  CD  ARG B 128     -42.687  14.511  22.038  1.00 64.91      B    C  
ANISOU  907  CD  ARG B 128     5520   4982  14160    273   -383    634  B    C  
ATOM    908  NE  ARG B 128     -41.341  15.025  22.310  1.00 63.86      B    N  
ANISOU  908  NE  ARG B 128     5267   4702  14295    341   -512    745  B    N  
ATOM    909  CZ  ARG B 128     -41.079  16.209  22.844  1.00 54.64      B    C  
ANISOU  909  CZ  ARG B 128     3969   3486  13306    376   -719    671  B    C  
ATOM    910  NH1 ARG B 128     -42.072  17.018  23.156  1.00 85.34      B    N  
ANISOU  910  NH1 ARG B 128     7836   7462  17127    369   -805    472  B    N  
ATOM    911  NH2 ARG B 128     -39.834  16.594  23.056  1.00 62.00      B    N  
ANISOU  911  NH2 ARG B 128     4791   4275  14490    421   -847    799  B    N  
ATOM    912  N   LEU B 129     -42.479  17.244  18.225  1.00 41.50      B    N  
ANISOU  912  N   LEU B 129     2268   1695  11806    379   -331    857  B    N  
ATOM    913  CA  LEU B 129     -41.207  17.757  17.747  1.00 56.40      B    C  
ANISOU  913  CA  LEU B 129     4037   3418  13973    437   -353   1042  B    C  
ATOM    914  C   LEU B 129     -40.256  17.876  18.926  1.00 64.29      B    C  
ANISOU  914  C   LEU B 129     4939   4389  15098    465   -510   1059  B    C  
ATOM    915  O   LEU B 129     -40.699  17.907  20.084  1.00 55.96      B    O  
ANISOU  915  O   LEU B 129     3906   3429  13928    443   -639    890  B    O  
ATOM    916  CB  LEU B 129     -41.376  19.109  17.051  1.00 41.87      B    C  
ANISOU  916  CB  LEU B 129     2081   1500  12327    450   -457   1023  B    C  
ATOM    917  CG  LEU B 129     -42.246  18.991  15.802  1.00 56.49      B    C  
ANISOU  917  CG  LEU B 129     4043   3353  14068    420   -314   1028  B    C  
ATOM    918  CD1 LEU B 129     -42.585  20.342  15.229  1.00 44.96      B    C  
ANISOU  918  CD1 LEU B 129     2484   1826  12772    424   -446    975  B    C  
ATOM    919  CD2 LEU B 129     -41.555  18.092  14.764  1.00 46.37      B    C  
ANISOU  919  CD2 LEU B 129     2871   1977  12770    441    -78   1255  B    C  
ATOM    920  N   TYR B 130     -38.959  17.945  18.625  1.00 52.11      B    N  
ANISOU  920  N   TYR B 130     3290   2713  13794    510   -499   1270  B    N  
ATOM    921  CA  TYR B 130     -37.937  18.020  19.651  1.00 42.34      B    C  
ANISOU  921  CA  TYR B 130     1954   1423  12712    531   -663   1325  B    C  
ATOM    922  C   TYR B 130     -37.030  19.247  19.512  1.00 52.49      B    C  
ANISOU  922  C   TYR B 130     3031   2567  14347    553   -840   1436  B    C  
ATOM    923  O   TYR B 130     -35.822  19.161  19.688  1.00 69.17      B    O  
ANISOU  923  O   TYR B 130     5026   4582  16675    580   -881   1620  B    O  
ATOM    924  CB  TYR B 130     -37.108  16.748  19.622  1.00 42.57      B    C  
ANISOU  924  CB  TYR B 130     2038   1425  12712    562   -500   1500  B    C  
ATOM    925  CG  TYR B 130     -37.968  15.494  19.685  1.00 56.39      B    C  
ANISOU  925  CG  TYR B 130     4013   3297  14116    529   -333   1411  B    C  
ATOM    926  CD1 TYR B 130     -38.268  14.901  20.892  1.00 51.72      B    C  
ANISOU  926  CD1 TYR B 130     3518   2799  13337    490   -418   1285  B    C  
ATOM    927  CD2 TYR B 130     -38.486  14.930  18.541  1.00 61.65      B    C  
ANISOU  927  CD2 TYR B 130     4809   3974  14640    528   -106   1460  B    C  
ATOM    928  CE1 TYR B 130     -39.037  13.786  20.962  1.00 50.40      B    C  
ANISOU  928  CE1 TYR B 130     3548   2738  12863    443   -281   1218  B    C  
ATOM    929  CE2 TYR B 130     -39.267  13.806  18.600  1.00 73.76      B    C  
ANISOU  929  CE2 TYR B 130     6553   5605  15867    484     17   1392  B    C  
ATOM    930  CZ  TYR B 130     -39.543  13.234  19.813  1.00 62.07      B    C  
ANISOU  930  CZ  TYR B 130     5144   4224  14215    437    -69   1274  B    C  
ATOM    931  OH  TYR B 130     -40.342  12.119  19.871  1.00 62.85      B    O  
ANISOU  931  OH  TYR B 130     5451   4420  14008    376     45   1218  B    O  
ATOM    932  N   PHE B 131     -37.617  20.393  19.210  1.00 52.45      B    N  
ANISOU  932  N   PHE B 131     2976   2548  14404    538   -957   1330  B    N  
ATOM    933  CA  PHE B 131     -36.888  21.644  19.244  1.00 56.26      B    C  
ANISOU  933  CA  PHE B 131     3281   2898  15195    542  -1180   1403  B    C  
ATOM    934  C   PHE B 131     -36.492  22.005  20.680  1.00 52.98      B    C  
ANISOU  934  C   PHE B 131     2831   2459  14840    537  -1466   1317  B    C  
ATOM    935  O   PHE B 131     -37.149  21.592  21.636  1.00 59.51      B    O  
ANISOU  935  O   PHE B 131     3785   3391  15433    530  -1509   1128  B    O  
ATOM    936  CB  PHE B 131     -37.727  22.774  18.607  1.00 44.11      B    C  
ANISOU  936  CB  PHE B 131     1732   1348  13681    530  -1255   1285  B    C  
ATOM    937  CG  PHE B 131     -39.107  22.933  19.202  1.00 58.85      B    C  
ANISOU  937  CG  PHE B 131     3716   3346  15296    524  -1322    994  B    C  
ATOM    938  CD1 PHE B 131     -39.264  23.496  20.454  1.00 55.19      B    C  
ANISOU  938  CD1 PHE B 131     3253   2900  14815    536  -1570    821  B    C  
ATOM    939  CD2 PHE B 131     -40.260  22.564  18.485  1.00 42.29      B    C  
ANISOU  939  CD2 PHE B 131     1729   1350  12987    511  -1144    898  B    C  
ATOM    940  CE1 PHE B 131     -40.539  23.672  21.001  1.00 58.20      B    C  
ANISOU  940  CE1 PHE B 131     3733   3411  14970    548  -1608    558  B    C  
ATOM    941  CE2 PHE B 131     -41.522  22.731  19.025  1.00 51.99      B    C  
ANISOU  941  CE2 PHE B 131     3031   2708  14013    509  -1198    648  B    C  
ATOM    942  CZ  PHE B 131     -41.663  23.287  20.283  1.00 53.08      B    C  
ANISOU  942  CZ  PHE B 131     3157   2877  14134    535  -1416    477  B    C  
ATOM    943  N   SER B 132     -35.439  22.803  20.817  1.00 56.43      B    N  
ANISOU  943  N   SER B 132     3101   2748  15588    533  -1668   1463  B    N  
ATOM    944  CA  SER B 132     -34.998  23.307  22.117  1.00 61.24      B    C  
ANISOU  944  CA  SER B 132     3690   3294  16285    520  -1989   1398  B    C  
ATOM    945  C   SER B 132     -36.115  23.832  23.004  1.00 67.71      B    C  
ANISOU  945  C   SER B 132     4654   4190  16883    526  -2155   1089  B    C  
ATOM    946  O   SER B 132     -36.880  24.718  22.608  1.00 74.23      B    O  
ANISOU  946  O   SER B 132     5486   5024  17693    536  -2206    959  B    O  
ATOM    947  CB  SER B 132     -33.995  24.439  21.931  1.00 65.14      B    C  
ANISOU  947  CB  SER B 132     3990   3609  17151    498  -2222   1571  B    C  
ATOM    948  OG  SER B 132     -33.160  24.209  20.819  1.00 82.93      B    O  
ANISOU  948  OG  SER B 132     6089   5802  19617    501  -2028   1852  B    O  
ATOM    949  N   GLY B 133     -36.179  23.328  24.229  1.00 62.65      B    N  
ANISOU  949  N   GLY B 133     4128   3597  16078    526  -2248    974  B    N  
ATOM    950  CA  GLY B 133     -37.208  23.774  25.154  1.00 48.25      B    C  
ANISOU  950  CA  GLY B 133     2453   1852  14026    545  -2383    684  B    C  
ATOM    951  C   GLY B 133     -38.379  22.821  25.258  1.00 75.66      B    C  
ANISOU  951  C   GLY B 133     6074   5529  17142    547  -2136    518  B    C  
ATOM    952  O   GLY B 133     -39.204  22.982  26.158  1.00 75.44      B    O  
ANISOU  952  O   GLY B 133     6173   5592  16899    567  -2210    289  B    O  
ATOM    953  N   SER B 134     -38.441  21.817  24.376  1.00 55.68      B    N  
ANISOU  953  N   SER B 134     3541   3069  14548    528  -1849    641  B    N  
ATOM    954  CA  SER B 134     -39.653  21.022  24.270  1.00 49.89      B    C  
ANISOU  954  CA  SER B 134     2938   2521  13497    514  -1625    499  B    C  
ATOM    955  C   SER B 134     -39.807  20.031  25.418  1.00 50.13      B    C  
ANISOU  955  C   SER B 134     3116   2651  13279    490  -1605    416  B    C  
ATOM    956  O   SER B 134     -40.890  19.865  25.950  1.00 67.56      B    O  
ANISOU  956  O   SER B 134     5435   5008  15228    482  -1558    217  B    O  
ATOM    957  CB  SER B 134     -39.756  20.340  22.903  1.00 61.24      B    C  
ANISOU  957  CB  SER B 134     4360   3981  14927    497  -1349    647  B    C  
ATOM    958  OG  SER B 134     -38.672  19.462  22.663  1.00 61.47      B    O  
ANISOU  958  OG  SER B 134     4369   3939  15048    496  -1246    873  B    O  
ATOM    959  N   ASP B 135     -38.726  19.361  25.793  1.00 63.46      B    N  
ANISOU  959  N   ASP B 135     4804   4258  15048    478  -1637    574  B    N  
ATOM    960  CA  ASP B 135     -38.716  18.522  26.994  1.00 56.41      B    C  
ANISOU  960  CA  ASP B 135     4062   3425  13945    450  -1673    504  B    C  
ATOM    961  C   ASP B 135     -38.908  19.412  28.211  1.00 64.99      B    C  
ANISOU  961  C   ASP B 135     5211   4489  14992    468  -1941    316  B    C  
ATOM    962  O   ASP B 135     -39.672  19.109  29.123  1.00 68.51      B    O  
ANISOU  962  O   ASP B 135     5814   5056  15163    456  -1934    135  B    O  
ATOM    963  CB  ASP B 135     -37.362  17.813  27.146  1.00 48.79      B    C  
ANISOU  963  CB  ASP B 135     3059   2339  13141    445  -1709    728  B    C  
ATOM    964  CG  ASP B 135     -37.155  16.695  26.139  1.00 74.57      B    C  
ANISOU  964  CG  ASP B 135     6322   5628  16382    445  -1427    901  B    C  
ATOM    965  OD1 ASP B 135     -35.996  16.191  26.041  1.00 68.57      B    O  
ANISOU  965  OD1 ASP B 135     5495   4759  15798    466  -1428   1110  B    O  
ATOM    966  OD2 ASP B 135     -38.151  16.309  25.466  1.00 59.20      B    O  
ANISOU  966  OD2 ASP B 135     4450   3806  14239    427  -1213    832  B    O  
ATOM    967  N   THR B 136     -38.180  20.518  28.213  1.00 59.39      B    N  
ANISOU  967  N   THR B 136     4387   3615  14562    497  -2181    373  B    N  
ATOM    968  CA  THR B 136     -38.124  21.417  29.351  1.00 70.71      B    C  
ANISOU  968  CA  THR B 136     5897   4973  15998    521  -2483    227  B    C  
ATOM    969  C   THR B 136     -39.489  21.880  29.823  1.00 72.15      B    C  
ANISOU  969  C   THR B 136     6204   5296  15914    561  -2460    -57  B    C  
ATOM    970  O   THR B 136     -39.798  21.803  31.016  1.00 72.87      B    O  
ANISOU  970  O   THR B 136     6467   5427  15794    572  -2556   -217  B    O  
ATOM    971  CB  THR B 136     -37.264  22.650  29.031  1.00 75.61      B    C  
ANISOU  971  CB  THR B 136     6364   5391  16974    538  -2740    339  B    C  
ATOM    972  CG2 THR B 136     -37.174  23.540  30.241  1.00 69.48      B    C  
ANISOU  972  CG2 THR B 136     5706   4509  16183    562  -3078    191  B    C  
ATOM    973  OG1 THR B 136     -35.948  22.230  28.628  1.00 76.43      B    O  
ANISOU  973  OG1 THR B 136     6323   5368  17349    505  -2755    623  B    O  
ATOM    974  N   TYR B 137     -40.296  22.367  28.887  1.00 57.69      B    N  
ANISOU  974  N   TYR B 137     4288   3537  14096    588  -2332   -116  B    N  
ATOM    975  CA  TYR B 137     -41.628  22.861  29.207  1.00 50.42      B    C  
ANISOU  975  CA  TYR B 137     3444   2756  12958    642  -2294   -375  B    C  
ATOM    976  C   TYR B 137     -42.781  21.854  28.977  1.00 54.36      B    C  
ANISOU  976  C   TYR B 137     3995   3488  13171    609  -1984   -452  B    C  
ATOM    977  O   TYR B 137     -43.938  22.237  28.875  1.00 56.53      B    O  
ANISOU  977  O   TYR B 137     4269   3891  13319    649  -1903   -621  B    O  
ATOM    978  CB  TYR B 137     -41.842  24.185  28.485  1.00 54.88      B    C  
ANISOU  978  CB  TYR B 137     3893   3237  13724    698  -2411   -414  B    C  
ATOM    979  CG  TYR B 137     -40.776  25.156  28.935  1.00 76.57      B    C  
ANISOU  979  CG  TYR B 137     6622   5757  16716    718  -2750   -355  B    C  
ATOM    980  CD1 TYR B 137     -40.859  25.767  30.179  1.00 75.18      B    C  
ANISOU  980  CD1 TYR B 137     6599   5528  16437    773  -2989   -530  B    C  
ATOM    981  CD2 TYR B 137     -39.646  25.395  28.167  1.00 88.38      B    C  
ANISOU  981  CD2 TYR B 137     7960   7086  18534    675  -2834   -108  B    C  
ATOM    982  CE1 TYR B 137     -39.881  26.615  30.622  1.00 76.73      B    C  
ANISOU  982  CE1 TYR B 137     6802   5500  16850    778  -3328   -467  B    C  
ATOM    983  CE2 TYR B 137     -38.652  26.249  28.609  1.00 80.30      B    C  
ANISOU  983  CE2 TYR B 137     6911   5853  17747    673  -3164    -32  B    C  
ATOM    984  CZ  TYR B 137     -38.776  26.853  29.839  1.00 85.80      B    C  
ANISOU  984  CZ  TYR B 137     7773   6489  18338    720  -3425   -212  B    C  
ATOM    985  OH  TYR B 137     -37.794  27.711  30.294  1.00100.47      B    O  
ANISOU  985  OH  TYR B 137     9626   8117  20430    708  -3786   -131  B    O  
ATOM    986  N   TRP B 138     -42.453  20.565  28.898  1.00 57.06      B    N  
ANISOU  986  N   TRP B 138     4380   3879  13423    535  -1823   -318  B    N  
ATOM    987  CA  TRP B 138     -43.466  19.512  28.769  1.00 55.83      B    C  
ANISOU  987  CA  TRP B 138     4296   3928  12988    483  -1557   -370  B    C  
ATOM    988  C   TRP B 138     -44.251  19.427  30.074  1.00 60.32      B    C  
ANISOU  988  C   TRP B 138     5012   4635  13272    494  -1573   -583  B    C  
ATOM    989  O   TRP B 138     -43.674  19.354  31.144  1.00 67.75      B    O  
ANISOU  989  O   TRP B 138     6070   5511  14160    496  -1723   -607  B    O  
ATOM    990  CB  TRP B 138     -42.831  18.157  28.429  1.00 45.22      B    C  
ANISOU  990  CB  TRP B 138     2992   2575  11615    406  -1411   -171  B    C  
ATOM    991  CG  TRP B 138     -43.845  17.171  27.993  1.00 59.25      B    C  
ANISOU  991  CG  TRP B 138     4830   4531  13152    341  -1154   -190  B    C  
ATOM    992  CD1 TRP B 138     -44.559  16.344  28.786  1.00 49.22      B    C  
ANISOU  992  CD1 TRP B 138     3696   3422  11582    284  -1057   -288  B    C  
ATOM    993  CD2 TRP B 138     -44.302  16.940  26.653  1.00 72.27      B    C  
ANISOU  993  CD2 TRP B 138     6413   6210  14836    317   -975   -107  B    C  
ATOM    994  CE2 TRP B 138     -45.291  15.952  26.721  1.00 63.82      B    C  
ANISOU  994  CE2 TRP B 138     5445   5317  13487    240   -793   -156  B    C  
ATOM    995  CE3 TRP B 138     -43.965  17.474  25.407  1.00 75.74      B    C  
ANISOU  995  CE3 TRP B 138     6732   6535  15510    348   -960     10  B    C  
ATOM    996  NE1 TRP B 138     -45.432  15.605  28.033  1.00 57.76      B    N  
ANISOU  996  NE1 TRP B 138     4791   4635  12523    219   -840   -263  B    N  
ATOM    997  CZ2 TRP B 138     -45.952  15.484  25.591  1.00 62.76      B    C  
ANISOU  997  CZ2 TRP B 138     5303   5238  13306    191   -616    -92  B    C  
ATOM    998  CZ3 TRP B 138     -44.616  16.993  24.280  1.00 64.34      B    C  
ANISOU  998  CZ3 TRP B 138     5296   5146  14003    305   -769     68  B    C  
ATOM    999  CH2 TRP B 138     -45.595  16.010  24.382  1.00 66.27      B    C  
ANISOU  999  CH2 TRP B 138     5650   5556  13972    229   -610     16  B    C  
ATOM   1000  N   ASN B 139     -45.574  19.464  29.982  1.00 69.12      B    N  
ANISOU 1000  N   ASN B 139     6124   5936  14204    503  -1420   -733  B    N  
ATOM   1001  CA  ASN B 139     -46.441  19.567  31.162  1.00 59.01      B    C  
ANISOU 1001  CA  ASN B 139     4960   4802  12661    537  -1411   -948  B    C  
ATOM   1002  C   ASN B 139     -46.305  20.899  31.892  1.00 67.16      B    C  
ANISOU 1002  C   ASN B 139     6022   5729  13765    658  -1651  -1104  B    C  
ATOM   1003  O   ASN B 139     -47.016  21.168  32.856  1.00 79.84      B    O  
ANISOU 1003  O   ASN B 139     7734   7439  15162    719  -1650  -1297  B    O  
ATOM   1004  CB  ASN B 139     -46.231  18.402  32.130  1.00 48.61      B    C  
ANISOU 1004  CB  ASN B 139     3817   3548  11102    456  -1355   -924  B    C  
ATOM   1005  CG  ASN B 139     -46.506  17.059  31.480  1.00 61.46      B    C  
ANISOU 1005  CG  ASN B 139     5448   5287  12618    337  -1121   -788  B    C  
ATOM   1006  ND2 ASN B 139     -45.682  16.066  31.805  1.00 51.50      B    N  
ANISOU 1006  ND2 ASN B 139     4296   3963  11309    265  -1131   -657  B    N  
ATOM   1007  OD1 ASN B 139     -47.445  16.914  30.688  1.00 61.76      B    O  
ANISOU 1007  OD1 ASN B 139     5398   5453  12615    311   -948   -799  B    O  
ATOM   1008  N   ARG B 140     -45.386  21.740  31.450  1.00 61.19      B    N  
ANISOU 1008  N   ARG B 140     5185   4763  13301    697  -1859  -1018  B    N  
ATOM   1009  CA  ARG B 140     -45.323  23.072  32.019  1.00 56.36      B    C  
ANISOU 1009  CA  ARG B 140     4610   4037  12767    811  -2107  -1165  B    C  
ATOM   1010  C   ARG B 140     -45.595  24.069  30.907  1.00 62.72      B    C  
ANISOU 1010  C   ARG B 140     5246   4787  13799    865  -2142  -1165  B    C  
ATOM   1011  O   ARG B 140     -44.892  25.085  30.770  1.00 73.12      B    O  
ANISOU 1011  O   ARG B 140     6524   5906  15351    910  -2389  -1134  B    O  
ATOM   1012  CB  ARG B 140     -43.974  23.327  32.698  1.00 71.21      B    C  
ANISOU 1012  CB  ARG B 140     6578   5690  14788    802  -2394  -1076  B    C  
ATOM   1013  CG  ARG B 140     -43.609  22.272  33.765  1.00 77.96      B    C  
ANISOU 1013  CG  ARG B 140     7614   6576  15430    736  -2380  -1056  B    C  
ATOM   1014  CD  ARG B 140     -42.269  22.581  34.433  1.00 78.49      B    C  
ANISOU 1014  CD  ARG B 140     7760   6400  15661    726  -2701   -960  B    C  
ATOM   1015  NE  ARG B 140     -42.296  23.896  35.070  1.00 82.60      B    N  
ANISOU 1015  NE  ARG B 140     8376   6793  16216    829  -2972  -1118  B    N  
ATOM   1016  CZ  ARG B 140     -41.262  24.729  35.115  1.00101.30      B    C  
ANISOU 1016  CZ  ARG B 140    10721   8915  18853    837  -3294  -1027  B    C  
ATOM   1017  NH1 ARG B 140     -40.104  24.390  34.560  1.00104.02      B    N  
ANISOU 1017  NH1 ARG B 140    10925   9126  19472    752  -3368   -770  B    N  
ATOM   1018  NH2 ARG B 140     -41.389  25.910  35.710  1.00114.18      B    N  
ANISOU 1018  NH2 ARG B 140    12472  10429  20482    935  -3545  -1187  B    N  
ATOM   1019  N   GLY B 141     -46.612  23.746  30.103  1.00 59.80      B    N  
ANISOU 1019  N   GLY B 141     4778   4585  13360    849  -1906  -1187  B    N  
ATOM   1020  CA  GLY B 141     -47.046  24.594  29.005  1.00 58.86      B    C  
ANISOU 1020  CA  GLY B 141     4509   4432  13422    893  -1915  -1196  B    C  
ATOM   1021  C   GLY B 141     -47.252  23.824  27.718  1.00 57.11      B    C  
ANISOU 1021  C   GLY B 141     4180   4272  13248    797  -1698  -1035  B    C  
ATOM   1022  O   GLY B 141     -48.280  23.946  27.062  1.00 70.96      B    O  
ANISOU 1022  O   GLY B 141     5856   6136  14969    809  -1576  -1098  B    O  
ATOM   1023  N   ILE B 142     -46.261  23.032  27.357  1.00 53.64      B    N  
ANISOU 1023  N   ILE B 142     3744   3748  12889    708  -1660   -822  B    N  
ATOM   1024  CA  ILE B 142     -46.298  22.234  26.143  1.00 58.44      B    C  
ANISOU 1024  CA  ILE B 142     4293   4381  13530    624  -1460   -651  B    C  
ATOM   1025  C   ILE B 142     -47.000  20.907  26.376  1.00 55.91      B    C  
ANISOU 1025  C   ILE B 142     4058   4253  12931    546  -1231   -660  B    C  
ATOM   1026  O   ILE B 142     -46.900  20.342  27.447  1.00 77.79      B    O  
ANISOU 1026  O   ILE B 142     6939   7088  15528    528  -1229   -708  B    O  
ATOM   1027  CB  ILE B 142     -44.889  21.931  25.649  1.00 52.88      B    C  
ANISOU 1027  CB  ILE B 142     3561   3501  13031    583  -1502   -411  B    C  
ATOM   1028  CG1 ILE B 142     -44.174  23.249  25.304  1.00 51.07      B    C  
ANISOU 1028  CG1 ILE B 142     3228   3076  13099    638  -1731   -369  B    C  
ATOM   1029  CG2 ILE B 142     -44.941  20.958  24.454  1.00 43.02      B    C  
ANISOU 1029  CG2 ILE B 142     2300   2279  11765    509  -1267   -240  B    C  
ATOM   1030  CD1 ILE B 142     -42.692  23.089  25.092  1.00 45.10      B    C  
ANISOU 1030  CD1 ILE B 142     2422   2145  12569    607  -1809   -136  B    C  
ATOM   1031  N   SER B 143     -47.702  20.420  25.359  1.00 68.26      B    N  
ANISOU 1031  N   SER B 143     5585   5897  14454    489  -1052   -604  B    N  
ATOM   1032  CA  SER B 143     -48.456  19.175  25.438  1.00 73.72      B    C  
ANISOU 1032  CA  SER B 143     6354   6765  14891    397   -845   -595  B    C  
ATOM   1033  C   SER B 143     -48.872  18.705  24.054  1.00 63.80      B    C  
ANISOU 1033  C   SER B 143     5072   5509  13661    329   -700   -472  B    C  
ATOM   1034  O   SER B 143     -48.821  19.456  23.081  1.00 67.63      B    O  
ANISOU 1034  O   SER B 143     5471   5889  14335    364   -749   -434  B    O  
ATOM   1035  CB  SER B 143     -49.702  19.364  26.288  1.00 78.26      B    C  
ANISOU 1035  CB  SER B 143     6927   7540  15267    423   -806   -807  B    C  
ATOM   1036  OG  SER B 143     -50.748  18.561  25.796  1.00 75.04      B    O  
ANISOU 1036  OG  SER B 143     6513   7292  14705    334   -618   -788  B    O  
ATOM   1037  N   ALA B 144     -49.288  17.453  23.969  1.00 57.09      B    N  
ANISOU 1037  N   ALA B 144     4315   4768  12607    226   -534   -408  B    N  
ATOM   1038  CA  ALA B 144     -49.691  16.882  22.691  1.00 51.47      B    C  
ANISOU 1038  CA  ALA B 144     3627   4044  11886    152   -406   -284  B    C  
ATOM   1039  C   ALA B 144     -51.177  16.571  22.682  1.00 53.51      B    C  
ANISOU 1039  C   ALA B 144     3867   4497  11966     85   -310   -380  B    C  
ATOM   1040  O   ALA B 144     -51.656  15.831  21.815  1.00 57.61      B    O  
ANISOU 1040  O   ALA B 144     4446   5032  12411     -8   -206   -279  B    O  
ATOM   1041  CB  ALA B 144     -48.887  15.618  22.401  1.00 41.61      B    C  
ANISOU 1041  CB  ALA B 144     2522   2724  10563     84   -303    -95  B    C  
ATOM   1042  N   CYS B 145     -51.900  17.125  23.657  1.00 47.07      B    N  
ANISOU 1042  N   CYS B 145     2975   3827  11081    134   -349   -566  B    N  
ATOM   1043  CA  CYS B 145     -53.323  16.901  23.771  1.00 55.04      B    C  
ANISOU 1043  CA  CYS B 145     3929   5041  11941     81   -253   -657  B    C  
ATOM   1044  C   CYS B 145     -54.084  18.166  24.119  1.00 71.31      B    C  
ANISOU 1044  C   CYS B 145     5834   7175  14085    201   -331   -851  B    C  
ATOM   1045  O   CYS B 145     -54.531  18.344  25.258  1.00 66.72      B    O  
ANISOU 1045  O   CYS B 145     5235   6738  13378    251   -315   -999  B    O  
ATOM   1046  CB  CYS B 145     -53.633  15.812  24.799  1.00 42.93      B    C  
ANISOU 1046  CB  CYS B 145     2495   3679  10140    -10   -142   -669  B    C  
ATOM   1047  SG  CYS B 145     -55.393  15.225  24.694  1.00 63.93      B    S  
ANISOU 1047  SG  CYS B 145     5078   6594  12618   -129      7   -702  B    S  
ATOM   1048  N   ALA B 146     -54.240  19.033  23.120  1.00 76.61      B    N  
ANISOU 1048  N   ALA B 146     6409   7741  14958    252   -411   -849  B    N  
ATOM   1049  CA  ALA B 146     -55.005  20.282  23.264  1.00 66.64      B    C  
ANISOU 1049  CA  ALA B 146     4997   6524  13799    378   -499  -1028  B    C  
ATOM   1050  C   ALA B 146     -56.317  20.087  24.020  1.00 53.35      B    C  
ANISOU 1050  C   ALA B 146     3232   5097  11943    379   -387  -1162  B    C  
ATOM   1051  O   ALA B 146     -56.683  20.886  24.870  1.00 58.94      B    O  
ANISOU 1051  O   ALA B 146     3876   5881  12639    510   -427  -1341  B    O  
ATOM   1052  CB  ALA B 146     -55.290  20.887  21.893  1.00 65.83      B    C  
ANISOU 1052  CB  ALA B 146     4815   6306  13892    381   -564   -975  B    C  
ATOM   1053  N   VAL B 147     -57.022  19.007  23.712  1.00 68.83      B    N  
ANISOU 1053  N   VAL B 147     5202   7186  13764    233   -244  -1066  B    N  
ATOM   1054  CA  VAL B 147     -58.329  18.772  24.309  1.00 64.94      B    C  
ANISOU 1054  CA  VAL B 147     4601   6946  13126    213   -124  -1160  B    C  
ATOM   1055  C   VAL B 147     -58.232  18.291  25.747  1.00 63.99      B    C  
ANISOU 1055  C   VAL B 147     4560   6971  12781    217    -33  -1235  B    C  
ATOM   1056  O   VAL B 147     -59.084  18.606  26.566  1.00 66.81      B    O  
ANISOU 1056  O   VAL B 147     4821   7514  13048    289     39  -1378  B    O  
ATOM   1057  CB  VAL B 147     -59.132  17.774  23.498  1.00 61.20      B    C  
ANISOU 1057  CB  VAL B 147     4113   6553  12586     36    -26  -1015  B    C  
ATOM   1058  CG1 VAL B 147     -60.438  17.489  24.196  1.00 52.01      B    C  
ANISOU 1058  CG1 VAL B 147     2816   5664  11282      2    107  -1090  B    C  
ATOM   1059  CG2 VAL B 147     -59.392  18.344  22.111  1.00 56.96      B    C  
ANISOU 1059  CG2 VAL B 147     3503   5878  12261     39   -124   -961  B    C  
ATOM   1060  N   CYS B 148     -57.183  17.531  26.043  1.00 65.49      B    N  
ANISOU 1060  N   CYS B 148     4931   7071  12882    148    -36  -1136  B    N  
ATOM   1061  CA  CYS B 148     -56.876  17.150  27.412  1.00 57.61      B    C  
ANISOU 1061  CA  CYS B 148     4045   6160  11682    156     10  -1203  B    C  
ATOM   1062  C   CYS B 148     -56.664  18.347  28.323  1.00 67.37      B    C  
ANISOU 1062  C   CYS B 148     5265   7370  12962    348    -93  -1398  B    C  
ATOM   1063  O   CYS B 148     -57.279  18.431  29.389  1.00 69.21      B    O  
ANISOU 1063  O   CYS B 148     5497   7775  13026    402    -10  -1534  B    O  
ATOM   1064  CB  CYS B 148     -55.612  16.305  27.451  1.00 49.13      B    C  
ANISOU 1064  CB  CYS B 148     3163   4938  10566     73    -25  -1059  B    C  
ATOM   1065  SG  CYS B 148     -55.773  14.712  26.620  1.00 69.44      B    S  
ANISOU 1065  SG  CYS B 148     5833   7533  13018   -146     99   -836  B    S  
ATOM   1066  N   ASP B 149     -55.799  19.271  27.894  1.00 61.50      B    N  
ANISOU 1066  N   ASP B 149     4520   6409  12439    449   -273  -1407  B    N  
ATOM   1067  CA  ASP B 149     -55.285  20.316  28.786  1.00 65.71      B    C  
ANISOU 1067  CA  ASP B 149     5100   6856  13011    615   -421  -1563  B    C  
ATOM   1068  C   ASP B 149     -55.798  21.760  28.576  1.00 74.77      B    C  
ANISOU 1068  C   ASP B 149     6117   7969  14325    790   -531  -1723  B    C  
ATOM   1069  O   ASP B 149     -55.536  22.635  29.394  1.00 73.89      B    O  
ANISOU 1069  O   ASP B 149     6062   7800  14214    936   -651  -1872  B    O  
ATOM   1070  CB  ASP B 149     -53.757  20.312  28.756  1.00 51.56      B    C  
ANISOU 1070  CB  ASP B 149     3432   4825  11333    601   -582  -1455  B    C  
ATOM   1071  CG  ASP B 149     -53.184  18.937  28.954  1.00 71.77      B    C  
ANISOU 1071  CG  ASP B 149     6126   7396  13746    451   -493  -1300  B    C  
ATOM   1072  OD1 ASP B 149     -53.932  18.073  29.461  1.00 94.90      B    O  
ANISOU 1072  OD1 ASP B 149     9093  10523  16443    369   -328  -1315  B    O  
ATOM   1073  OD2 ASP B 149     -51.996  18.714  28.602  1.00 60.44      B    O  
ANISOU 1073  OD2 ASP B 149     4756   5775  12432    417   -586  -1159  B    O  
ATOM   1074  N   GLY B 150     -56.522  22.007  27.494  1.00 77.91      B    N  
ANISOU 1074  N   GLY B 150     6357   8387  14857    776   -504  -1692  B    N  
ATOM   1075  CA  GLY B 150     -56.918  23.362  27.163  1.00 64.70      B    C  
ANISOU 1075  CA  GLY B 150     4566   6649  13366    936   -633  -1825  B    C  
ATOM   1076  C   GLY B 150     -57.638  24.129  28.257  1.00 69.91      B    C  
ANISOU 1076  C   GLY B 150     5201   7437  13924   1118   -620  -2058  B    C  
ATOM   1077  O   GLY B 150     -57.357  25.294  28.484  1.00 85.21      B    O  
ANISOU 1077  O   GLY B 150     7159   9244  15971   1279   -794  -2186  B    O  
ATOM   1078  N   ALA B 151     -58.584  23.484  28.926  1.00 82.65      B    N  
ANISOU 1078  N   ALA B 151     6778   9302  15325   1095   -411  -2109  B    N  
ATOM   1079  CA  ALA B 151     -59.410  24.170  29.914  1.00 87.05      B    C  
ANISOU 1079  CA  ALA B 151     7297  10007  15772   1281   -351  -2328  B    C  
ATOM   1080  C   ALA B 151     -58.547  24.732  31.034  1.00 94.10      B    C  
ANISOU 1080  C   ALA B 151     8401  10776  16578   1408   -485  -2452  B    C  
ATOM   1081  O   ALA B 151     -58.778  25.845  31.518  1.00100.94      B    O  
ANISOU 1081  O   ALA B 151     9279  11605  17468   1617   -576  -2641  B    O  
ATOM   1082  CB  ALA B 151     -60.451  23.228  30.475  1.00 74.45      B    C  
ANISOU 1082  CB  ALA B 151     5634   8706  13946   1205    -81  -2324  B    C  
ATOM   1083  N   ALA B 152     -57.542  23.951  31.419  1.00 72.85      B    N  
ANISOU 1083  N   ALA B 152     5885   8004  13790   1283   -512  -2341  B    N  
ATOM   1084  CA  ALA B 152     -56.648  24.285  32.524  1.00 75.49      B    C  
ANISOU 1084  CA  ALA B 152     6444   8212  14026   1364   -652  -2426  B    C  
ATOM   1085  C   ALA B 152     -56.312  25.784  32.717  1.00 96.65      B    C  
ANISOU 1085  C   ALA B 152     9174  10700  16848   1573   -899  -2585  B    C  
ATOM   1086  O   ALA B 152     -56.134  26.545  31.755  1.00 85.30      B    O  
ANISOU 1086  O   ALA B 152     7629   9114  15666   1607  -1051  -2557  B    O  
ATOM   1087  CB  ALA B 152     -55.372  23.457  32.421  1.00 67.62      B    C  
ANISOU 1087  CB  ALA B 152     5581   7065  13047   1197   -735  -2238  B    C  
ATOM   1088  N   PRO B 153     -56.187  26.191  33.987  1.00107.63      B    N  
ANISOU 1088  N   PRO B 153    10758  12078  18060   1706   -951  -2748  B    N  
ATOM   1089  CA  PRO B 153     -55.984  27.578  34.399  1.00103.98      B    C  
ANISOU 1089  CA  PRO B 153    10394  11445  17669   1921  -1180  -2926  B    C  
ATOM   1090  C   PRO B 153     -54.848  28.250  33.641  1.00 87.68      B    C  
ANISOU 1090  C   PRO B 153     8336   9082  15898   1891  -1487  -2823  B    C  
ATOM   1091  O   PRO B 153     -55.045  29.308  33.054  1.00 86.69      B    O  
ANISOU 1091  O   PRO B 153     8122   8853  15962   2006  -1627  -2891  B    O  
ATOM   1092  CB  PRO B 153     -55.602  27.440  35.875  1.00111.83      B    C  
ANISOU 1092  CB  PRO B 153    11671  12425  18395   1976  -1206  -3030  B    C  
ATOM   1093  CG  PRO B 153     -56.178  26.140  36.305  1.00109.14      B    C  
ANISOU 1093  CG  PRO B 153    11321  12345  17803   1849   -903  -2974  B    C  
ATOM   1094  CD  PRO B 153     -56.076  25.256  35.121  1.00108.03      B    C  
ANISOU 1094  CD  PRO B 153    10989  12241  17815   1636   -819  -2749  B    C  
ATOM   1095  N   ILE B 154     -53.669  27.641  33.664  1.00 79.02      B    N  
ANISOU 1095  N   ILE B 154     7339   7848  14839   1738  -1589  -2654  B    N  
ATOM   1096  CA  ILE B 154     -52.481  28.248  33.069  1.00 83.49      B    C  
ANISOU 1096  CA  ILE B 154     7914   8130  15681   1703  -1878  -2536  B    C  
ATOM   1097  C   ILE B 154     -52.762  28.911  31.720  1.00 90.40      B    C  
ANISOU 1097  C   ILE B 154     8581   8945  16823   1716  -1926  -2490  B    C  
ATOM   1098  O   ILE B 154     -52.112  29.892  31.362  1.00 94.66      B    O  
ANISOU 1098  O   ILE B 154     9129   9258  17578   1764  -2187  -2477  B    O  
ATOM   1099  CB  ILE B 154     -51.358  27.209  32.867  1.00 94.51      B    C  
ANISOU 1099  CB  ILE B 154     9341   9445  17124   1504  -1887  -2299  B    C  
ATOM   1100  CG1 ILE B 154     -51.483  26.072  33.887  1.00114.60      B    C  
ANISOU 1100  CG1 ILE B 154    12028  12148  19367   1433  -1712  -2307  B    C  
ATOM   1101  CG2 ILE B 154     -49.977  27.878  32.916  1.00 81.91      B    C  
ANISOU 1101  CG2 ILE B 154     7834   7549  15739   1499  -2220  -2214  B    C  
ATOM   1102  CD1 ILE B 154     -50.516  24.910  33.648  1.00115.91      B    C  
ANISOU 1102  CD1 ILE B 154    12215  12262  19563   1242  -1687  -2075  B    C  
ATOM   1103  N   PHE B 155     -53.723  28.370  30.976  1.00 84.34      B    N  
ANISOU 1103  N   PHE B 155     7634   8372  16040   1662  -1687  -2455  B    N  
ATOM   1104  CA  PHE B 155     -53.956  28.783  29.594  1.00 69.82      B    C  
ANISOU 1104  CA  PHE B 155     5611   6474  14442   1636  -1719  -2374  B    C  
ATOM   1105  C   PHE B 155     -55.101  29.779  29.481  1.00 87.62      B    C  
ANISOU 1105  C   PHE B 155     7766   8797  16728   1817  -1726  -2571  B    C  
ATOM   1106  O   PHE B 155     -55.211  30.527  28.505  1.00 82.47      B    O  
ANISOU 1106  O   PHE B 155     7006   8035  16296   1845  -1844  -2553  B    O  
ATOM   1107  CB  PHE B 155     -54.267  27.565  28.732  1.00 68.23      B    C  
ANISOU 1107  CB  PHE B 155     5293   6409  14223   1454  -1487  -2196  B    C  
ATOM   1108  CG  PHE B 155     -53.246  26.461  28.846  1.00 74.25      B    C  
ANISOU 1108  CG  PHE B 155     6151   7127  14931   1289  -1446  -2007  B    C  
ATOM   1109  CD1 PHE B 155     -51.913  26.691  28.544  1.00 51.45      B    C  
ANISOU 1109  CD1 PHE B 155     3316   4003  12230   1242  -1639  -1867  B    C  
ATOM   1110  CD2 PHE B 155     -53.627  25.197  29.246  1.00 69.05      B    C  
ANISOU 1110  CD2 PHE B 155     5526   6663  14048   1182  -1217  -1961  B    C  
ATOM   1111  CE1 PHE B 155     -50.989  25.696  28.645  1.00 67.53      B    C  
ANISOU 1111  CE1 PHE B 155     5426   5997  14233   1110  -1600  -1694  B    C  
ATOM   1112  CE2 PHE B 155     -52.699  24.181  29.345  1.00 66.74      B    C  
ANISOU 1112  CE2 PHE B 155     5331   6320  13707   1042  -1189  -1792  B    C  
ATOM   1113  CZ  PHE B 155     -51.374  24.433  29.045  1.00 65.18      B    C  
ANISOU 1113  CZ  PHE B 155     5177   5886  13704   1014  -1378  -1661  B    C  
ATOM   1114  N   ARG B 156     -55.966  29.778  30.484  1.00100.03      B    N  
ANISOU 1114  N   ARG B 156     9377  10552  18078   1943  -1591  -2755  B    N  
ATOM   1115  CA  ARG B 156     -57.141  30.625  30.454  1.00 98.97      B    C  
ANISOU 1115  CA  ARG B 156     9132  10514  17957   2134  -1558  -2944  B    C  
ATOM   1116  C   ARG B 156     -56.762  32.057  30.094  1.00 96.29      B    C  
ANISOU 1116  C   ARG B 156     8825   9926  17837   2273  -1865  -3025  B    C  
ATOM   1117  O   ARG B 156     -55.893  32.660  30.731  1.00 92.21      B    O  
ANISOU 1117  O   ARG B 156     8500   9214  17321   2337  -2091  -3077  B    O  
ATOM   1118  CB  ARG B 156     -57.861  30.581  31.804  1.00 97.41      B    C  
ANISOU 1118  CB  ARG B 156     9028  10505  17478   2286  -1401  -3141  B    C  
ATOM   1119  CG  ARG B 156     -59.298  31.044  31.746  1.00 85.36      B    C  
ANISOU 1119  CG  ARG B 156     7327   9171  15937   2456  -1249  -3300  B    C  
ATOM   1120  CD  ARG B 156     -60.073  30.208  30.765  1.00 91.47      B    C  
ANISOU 1120  CD  ARG B 156     7850  10126  16779   2298  -1045  -3153  B    C  
ATOM   1121  NE  ARG B 156     -60.164  28.821  31.204  1.00103.95      B    N  
ANISOU 1121  NE  ARG B 156     9448  11904  18145   2124   -800  -3042  B    N  
ATOM   1122  CZ  ARG B 156     -61.241  28.291  31.777  1.00 99.68      B    C  
ANISOU 1122  CZ  ARG B 156     8814  11645  17416   2151   -530  -3101  B    C  
ATOM   1123  NH1 ARG B 156     -62.323  29.030  31.978  1.00 89.32      B    N  
ANISOU 1123  NH1 ARG B 156     7368  10458  16112   2359   -452  -3271  B    N  
ATOM   1124  NH2 ARG B 156     -61.240  27.017  32.143  1.00 97.46      B    N  
ANISOU 1124  NH2 ARG B 156     8567  11520  16942   1970   -334  -2981  B    N  
ATOM   1125  N   ASN B 157     -57.400  32.576  29.050  1.00 94.25      B    N  
ANISOU 1125  N   ASN B 157     8386   9658  17766   2303  -1890  -3026  B    N  
ATOM   1126  CA  ASN B 157     -57.278  33.978  28.670  1.00100.87      B    C  
ANISOU 1126  CA  ASN B 157     9239  10283  18805   2449  -2169  -3123  B    C  
ATOM   1127  C   ASN B 157     -55.896  34.403  28.178  1.00 96.13      B    C  
ANISOU 1127  C   ASN B 157     8736   9387  18404   2346  -2452  -2976  B    C  
ATOM   1128  O   ASN B 157     -55.691  35.560  27.823  1.00 96.45      B    O  
ANISOU 1128  O   ASN B 157     8800   9227  18620   2439  -2709  -3032  B    O  
ATOM   1129  CB  ASN B 157     -57.731  34.881  29.824  1.00112.13      B    C  
ANISOU 1129  CB  ASN B 157    10798  11717  20092   2717  -2236  -3390  B    C  
ATOM   1130  CG  ASN B 157     -58.520  36.077  29.345  1.00118.83      B    C  
ANISOU 1130  CG  ASN B 157    11550  12510  21091   2913  -2359  -3543  B    C  
ATOM   1131  ND2 ASN B 157     -59.243  36.709  30.256  1.00135.36      B    N  
ANISOU 1131  ND2 ASN B 157    13713  14676  23041   3169  -2331  -3785  B    N  
ATOM   1132  OD1 ASN B 157     -58.488  36.426  28.165  1.00108.98      B    O  
ANISOU 1132  OD1 ASN B 157    10179  11153  20078   2842  -2475  -3445  B    O  
ATOM   1133  N   LYS B 158     -54.948  33.474  28.170  1.00 99.83      B    N  
ANISOU 1133  N   LYS B 158     9255   9826  18851   2155  -2406  -2783  B    N  
ATOM   1134  CA  LYS B 158     -53.599  33.747  27.685  1.00 90.64      B    C  
ANISOU 1134  CA  LYS B 158     8148   8403  17888   2041  -2639  -2609  B    C  
ATOM   1135  C   LYS B 158     -53.495  33.295  26.230  1.00 85.81      B    C  
ANISOU 1135  C   LYS B 158     7380   7774  17453   1873  -2558  -2394  B    C  
ATOM   1136  O   LYS B 158     -54.392  32.624  25.734  1.00 90.29      B    O  
ANISOU 1136  O   LYS B 158     7824   8527  17957   1825  -2330  -2375  B    O  
ATOM   1137  CB  LYS B 158     -52.583  32.995  28.538  1.00 94.76      B    C  
ANISOU 1137  CB  LYS B 158     8816   8896  18295   1945  -2640  -2516  B    C  
ATOM   1138  CG  LYS B 158     -52.611  33.339  30.017  1.00107.17      B    C  
ANISOU 1138  CG  LYS B 158    10589  10469  19661   2095  -2722  -2713  B    C  
ATOM   1139  CD  LYS B 158     -51.535  34.357  30.357  1.00116.93      B    C  
ANISOU 1139  CD  LYS B 158    11981  11409  21038   2140  -3094  -2715  B    C  
ATOM   1140  CE  LYS B 158     -51.091  34.221  31.807  1.00118.08      B    C  
ANISOU 1140  CE  LYS B 158    12372  11522  20973   2193  -3175  -2808  B    C  
ATOM   1141  NZ  LYS B 158     -49.766  34.872  32.081  1.00106.46      B    N  
ANISOU 1141  NZ  LYS B 158    11043   9747  19659   2157  -3543  -2722  B    N  
ATOM   1142  N   PRO B 159     -52.408  33.668  25.535  1.00 81.93      B    N  
ANISOU 1142  N   PRO B 159     6895   7052  17182   1779  -2749  -2224  B    N  
ATOM   1143  CA  PRO B 159     -52.223  33.181  24.159  1.00 70.74      B    C  
ANISOU 1143  CA  PRO B 159     5362   5607  15908   1619  -2653  -2008  B    C  
ATOM   1144  C   PRO B 159     -51.716  31.724  24.092  1.00 86.52      B    C  
ANISOU 1144  C   PRO B 159     7365   7701  17806   1451  -2428  -1816  B    C  
ATOM   1145  O   PRO B 159     -50.870  31.310  24.904  1.00 79.61      B    O  
ANISOU 1145  O   PRO B 159     6586   6794  16866   1418  -2454  -1768  B    O  
ATOM   1146  CB  PRO B 159     -51.167  34.134  23.576  1.00 68.64      B    C  
ANISOU 1146  CB  PRO B 159     5116   5061  15903   1590  -2933  -1892  B    C  
ATOM   1147  CG  PRO B 159     -51.031  35.261  24.573  1.00 67.77      B    C  
ANISOU 1147  CG  PRO B 159     5122   4834  15795   1750  -3203  -2078  B    C  
ATOM   1148  CD  PRO B 159     -51.399  34.678  25.902  1.00 79.53      B    C  
ANISOU 1148  CD  PRO B 159     6705   6495  17017   1826  -3074  -2228  B    C  
ATOM   1149  N   ILE B 160     -52.242  30.971  23.124  1.00 71.09      B    N  
ANISOU 1149  N   ILE B 160     5323   5847  15840   1349  -2226  -1710  B    N  
ATOM   1150  CA  ILE B 160     -51.862  29.590  22.887  1.00 58.15      B    C  
ANISOU 1150  CA  ILE B 160     3701   4287  14106   1195  -2012  -1527  B    C  
ATOM   1151  C   ILE B 160     -51.294  29.449  21.468  1.00 60.95      B    C  
ANISOU 1151  C   ILE B 160     4019   4502  14639   1077  -1999  -1302  B    C  
ATOM   1152  O   ILE B 160     -51.711  30.172  20.563  1.00 73.17      B    O  
ANISOU 1152  O   ILE B 160     5507   5971  16322   1097  -2077  -1311  B    O  
ATOM   1153  CB  ILE B 160     -53.096  28.658  22.979  1.00 67.70      B    C  
ANISOU 1153  CB  ILE B 160     4868   5752  15104   1167  -1760  -1590  B    C  
ATOM   1154  CG1 ILE B 160     -54.010  29.029  24.155  1.00 60.65      B    C  
ANISOU 1154  CG1 ILE B 160     3973   5018  14053   1313  -1749  -1836  B    C  
ATOM   1155  CG2 ILE B 160     -52.679  27.194  23.059  1.00 73.70      B    C  
ANISOU 1155  CG2 ILE B 160     5688   6595  15718   1021  -1560  -1429  B    C  
ATOM   1156  CD1 ILE B 160     -53.492  28.649  25.507  1.00 55.31      B    C  
ANISOU 1156  CD1 ILE B 160     3425   4387  13206   1337  -1740  -1891  B    C  
ATOM   1157  N   ALA B 161     -50.354  28.520  21.274  1.00 58.82      B    N  
ANISOU 1157  N   ALA B 161     3794   4193  14362    963  -1897  -1101  B    N  
ATOM   1158  CA  ALA B 161     -49.920  28.104  19.930  1.00 55.32      B    C  
ANISOU 1158  CA  ALA B 161     3340   3654  14027    852  -1806   -879  B    C  
ATOM   1159  C   ALA B 161     -50.249  26.648  19.659  1.00 60.87      B    C  
ANISOU 1159  C   ALA B 161     4088   4497  14545    748  -1545   -781  B    C  
ATOM   1160  O   ALA B 161     -50.243  25.823  20.566  1.00 63.01      B    O  
ANISOU 1160  O   ALA B 161     4409   4894  14640    732  -1446   -812  B    O  
ATOM   1161  CB  ALA B 161     -48.455  28.331  19.725  1.00 55.33      B    C  
ANISOU 1161  CB  ALA B 161     3349   3459  14215    817  -1909   -695  B    C  
ATOM   1162  N   VAL B 162     -50.567  26.361  18.400  1.00 59.46      B    N  
ANISOU 1162  N   VAL B 162     3912   4284  14396    676  -1449   -668  B    N  
ATOM   1163  CA  VAL B 162     -50.787  25.016  17.929  1.00 47.01      B    C  
ANISOU 1163  CA  VAL B 162     2411   2793  12660    569  -1226   -546  B    C  
ATOM   1164  C   VAL B 162     -49.883  24.826  16.726  1.00 63.72      B    C  
ANISOU 1164  C   VAL B 162     4583   4730  14899    508  -1179   -316  B    C  
ATOM   1165  O   VAL B 162     -49.806  25.705  15.870  1.00 77.34      B    O  
ANISOU 1165  O   VAL B 162     6276   6316  16793    522  -1281   -281  B    O  
ATOM   1166  CB  VAL B 162     -52.238  24.805  17.470  1.00 47.23      B    C  
ANISOU 1166  CB  VAL B 162     2413   2949  12581    539  -1154   -629  B    C  
ATOM   1167  CG1 VAL B 162     -52.387  23.463  16.832  1.00 40.43      B    C  
ANISOU 1167  CG1 VAL B 162     1659   2132  11572    414   -958   -478  B    C  
ATOM   1168  CG2 VAL B 162     -53.177  24.907  18.637  1.00 58.63      B    C  
ANISOU 1168  CG2 VAL B 162     3788   4593  13896    605  -1156   -841  B    C  
ATOM   1169  N   ILE B 163     -49.185  23.694  16.663  1.00 55.88      B    N  
ANISOU 1169  N   ILE B 163     3678   3735  13819    444  -1020   -157  B    N  
ATOM   1170  CA  ILE B 163     -48.374  23.381  15.494  1.00 46.85      B    C  
ANISOU 1170  CA  ILE B 163     2604   2434  12761    399   -927     68  B    C  
ATOM   1171  C   ILE B 163     -49.021  22.270  14.671  1.00 59.33      B    C  
ANISOU 1171  C   ILE B 163     4320   4062  14160    315   -740    148  B    C  
ATOM   1172  O   ILE B 163     -49.423  21.236  15.216  1.00 63.83      B    O  
ANISOU 1172  O   ILE B 163     4955   4769  14527    270   -631    121  B    O  
ATOM   1173  CB  ILE B 163     -46.970  22.918  15.901  1.00 43.90      B    C  
ANISOU 1173  CB  ILE B 163     2241   1992  12448    409   -884    220  B    C  
ATOM   1174  CG1 ILE B 163     -46.246  23.988  16.707  1.00 44.33      B    C  
ANISOU 1174  CG1 ILE B 163     2176   1974  12693    476  -1098    165  B    C  
ATOM   1175  CG2 ILE B 163     -46.140  22.507  14.668  1.00 42.30      B    C  
ANISOU 1175  CG2 ILE B 163     2111   1640  12320    379   -743    463  B    C  
ATOM   1176  CD1 ILE B 163     -44.852  23.480  17.192  1.00 53.43      B    C  
ANISOU 1176  CD1 ILE B 163     3321   3061  13921    478  -1075    326  B    C  
ATOM   1177  N   GLY B 164     -49.093  22.459  13.359  1.00 57.64      B    N  
ANISOU 1177  N   GLY B 164     4172   3722  14008    284   -711    255  B    N  
ATOM   1178  CA  GLY B 164     -49.632  21.434  12.478  1.00 52.23      B    C  
ANISOU 1178  CA  GLY B 164     3654   3039  13150    202   -557    347  B    C  
ATOM   1179  C   GLY B 164     -50.469  22.029  11.357  1.00 63.21      B    C  
ANISOU 1179  C   GLY B 164     5078   4351  14588    171   -625    334  B    C  
ATOM   1180  O   GLY B 164     -50.764  23.235  11.336  1.00 52.18      B    O  
ANISOU 1180  O   GLY B 164     3559   2919  13349    217   -794    230  B    O  
ATOM   1181  N   GLY B 165     -50.846  21.198  10.394  1.00 67.64      B    N  
ANISOU 1181  N   GLY B 165     5823   4865  15012     93   -511    442  B    N  
ATOM   1182  CA  GLY B 165     -51.607  21.709   9.268  1.00 62.49      B    C  
ANISOU 1182  CA  GLY B 165     5233   4113  14399     53   -588    446  B    C  
ATOM   1183  C   GLY B 165     -52.706  20.762   8.855  1.00 70.39      B    C  
ANISOU 1183  C   GLY B 165     6373   5175  15198    -49   -537    452  B    C  
ATOM   1184  O   GLY B 165     -53.201  20.825   7.734  1.00 76.04      B    O  
ANISOU 1184  O   GLY B 165     7221   5772  15900   -105   -570    513  B    O  
ATOM   1185  N   GLY B 166     -53.088  19.874   9.764  1.00 63.25      B    N  
ANISOU 1185  N   GLY B 166     5450   4448  14135    -84   -471    397  B    N  
ATOM   1186  CA  GLY B 166     -54.090  18.890   9.436  1.00 49.00      B    C  
ANISOU 1186  CA  GLY B 166     3775   2704  12138   -199   -429    422  B    C  
ATOM   1187  C   GLY B 166     -55.463  19.309   9.889  1.00 60.60      B    C  
ANISOU 1187  C   GLY B 166     5065   4334  13623   -228   -552    259  B    C  
ATOM   1188  O   GLY B 166     -55.667  20.428  10.366  1.00 61.33      B    O  
ANISOU 1188  O   GLY B 166     4951   4476  13876   -142   -670    115  B    O  
ATOM   1189  N   ASP B 167     -56.417  18.397   9.741  1.00 52.08      B    N  
ANISOU 1189  N   ASP B 167     4068   3336  12382   -346   -527    286  B    N  
ATOM   1190  CA  ASP B 167     -57.766  18.625  10.229  1.00 61.97      B    C  
ANISOU 1190  CA  ASP B 167     5133   4771  13645   -383   -616    153  B    C  
ATOM   1191  C   ASP B 167     -57.696  18.776  11.733  1.00 59.07      B    C  
ANISOU 1191  C   ASP B 167     4562   4615  13267   -307   -576      8  B    C  
ATOM   1192  O   ASP B 167     -58.397  19.594  12.309  1.00 69.02      B    O  
ANISOU 1192  O   ASP B 167     5602   5999  14626   -241   -659   -150  B    O  
ATOM   1193  CB  ASP B 167     -58.690  17.479   9.831  1.00 47.15      B    C  
ANISOU 1193  CB  ASP B 167     3390   2938  11589   -545   -592    244  B    C  
ATOM   1194  CG  ASP B 167     -59.090  17.523   8.345  1.00 65.31      B    C  
ANISOU 1194  CG  ASP B 167     5874   5030  13909   -624   -688    357  B    C  
ATOM   1195  OD1 ASP B 167     -58.897  18.570   7.680  1.00 59.80      B    O  
ANISOU 1195  OD1 ASP B 167     5153   4187  13381   -553   -787    335  B    O  
ATOM   1196  OD2 ASP B 167     -59.617  16.508   7.844  1.00 73.81      B    O  
ANISOU 1196  OD2 ASP B 167     7137   6079  14828   -764   -679    469  B    O  
ATOM   1197  N   SER B 168     -56.815  18.011  12.362  1.00 53.02      B    N  
ANISOU 1197  N   SER B 168     3886   3877  12383   -305   -452     61  B    N  
ATOM   1198  CA  SER B 168     -56.681  18.050  13.815  1.00 60.72      B    C  
ANISOU 1198  CA  SER B 168     4714   5036  13320   -243   -414    -66  B    C  
ATOM   1199  C   SER B 168     -56.238  19.430  14.280  1.00 63.10      B    C  
ANISOU 1199  C   SER B 168     4847   5308  13818    -89   -522   -201  B    C  
ATOM   1200  O   SER B 168     -56.757  19.983  15.264  1.00 60.50      B    O  
ANISOU 1200  O   SER B 168     4344   5135  13510    -18   -563   -370  B    O  
ATOM   1201  CB  SER B 168     -55.676  17.002  14.303  1.00 45.57      B    C  
ANISOU 1201  CB  SER B 168     2948   3111  11254   -267   -285     33  B    C  
ATOM   1202  OG  SER B 168     -56.230  15.702  14.206  1.00 58.96      B    O  
ANISOU 1202  OG  SER B 168     4786   4878  12738   -409   -199    122  B    O  
ATOM   1203  N   ALA B 169     -55.268  19.984  13.574  1.00 45.38      B    N  
ANISOU 1203  N   ALA B 169     2521   4298  10426    220  -1725    433  B    N  
ATOM   1204  CA  ALA B 169     -54.793  21.302  13.906  1.00 43.89      B    C  
ANISOU 1204  CA  ALA B 169     2350   3928  10400    318  -1808    507  B    C  
ATOM   1205  C   ALA B 169     -55.942  22.332  13.800  1.00 59.39      B    C  
ANISOU 1205  C   ALA B 169     4198   5860  12508    455  -1950    541  B    C  
ATOM   1206  O   ALA B 169     -56.183  23.103  14.722  1.00 56.37      B    O  
ANISOU 1206  O   ALA B 169     3791   5341  12287    583  -1966    467  B    O  
ATOM   1207  CB  ALA B 169     -53.618  21.674  13.017  1.00 48.74      B    C  
ANISOU 1207  CB  ALA B 169     3061   4494  10965    245  -1843    687  B    C  
ATOM   1208  N   MET B 170     -56.668  22.328  12.691  1.00 60.78      B    N  
ANISOU 1208  N   MET B 170     4303   6168  12622    438  -2053    645  B    N  
ATOM   1209  CA  MET B 170     -57.815  23.216  12.556  1.00 57.40      B    C  
ANISOU 1209  CA  MET B 170     3742   5736  12333    586  -2191    692  B    C  
ATOM   1210  C   MET B 170     -58.782  23.040  13.717  1.00 66.35      B    C  
ANISOU 1210  C   MET B 170     4748   6897  13563    692  -2120    501  B    C  
ATOM   1211  O   MET B 170     -59.232  24.031  14.290  1.00 70.63      B    O  
ANISOU 1211  O   MET B 170     5234   7312  14289    870  -2168    477  B    O  
ATOM   1212  CB  MET B 170     -58.568  22.998  11.233  1.00 56.14      B    C  
ANISOU 1212  CB  MET B 170     3499   5777  12055    533  -2313    820  B    C  
ATOM   1213  CG  MET B 170     -57.700  22.939   9.977  1.00 57.94      B    C  
ANISOU 1213  CG  MET B 170     3852   6042  12121    403  -2359    999  B    C  
ATOM   1214  SD  MET B 170     -56.665  24.393   9.735  1.00 78.29      B    S  
ANISOU 1214  SD  MET B 170     6545   8368  14833    468  -2446   1208  B    S  
ATOM   1215  CE  MET B 170     -55.086  23.793  10.271  1.00 68.28      B    C  
ANISOU 1215  CE  MET B 170     5430   7020  13495    341  -2263   1136  B    C  
ATOM   1216  N   GLU B 171     -59.124  21.800  14.073  1.00 49.89      B    N  
ANISOU 1216  N   GLU B 171     2625   4972  11360    589  -1997    363  B    N  
ATOM   1217  CA  GLU B 171     -60.182  21.642  15.088  1.00 56.02      B    C  
ANISOU 1217  CA  GLU B 171     3251   5812  12220    682  -1928    205  B    C  
ATOM   1218  C   GLU B 171     -59.711  21.922  16.498  1.00 54.28      B    C  
ANISOU 1218  C   GLU B 171     3102   5434  12088    767  -1812     64  B    C  
ATOM   1219  O   GLU B 171     -60.445  22.493  17.301  1.00 73.74      B    O  
ANISOU 1219  O   GLU B 171     5467   7869  14682    926  -1796    -29  B    O  
ATOM   1220  CB  GLU B 171     -60.974  20.318  15.005  1.00 46.22      B    C  
ANISOU 1220  CB  GLU B 171     1910   4805  10846    541  -1853    118  B    C  
ATOM   1221  CG  GLU B 171     -60.249  19.134  14.468  1.00 73.59      B    C  
ANISOU 1221  CG  GLU B 171     5516   8329  14114    332  -1783    119  B    C  
ATOM   1222  CD  GLU B 171     -61.174  18.214  13.698  1.00 91.32      B    C  
ANISOU 1222  CD  GLU B 171     7663  10798  16235    186  -1816    109  B    C  
ATOM   1223  OE1 GLU B 171     -61.829  18.708  12.747  1.00 93.17      B    O  
ANISOU 1223  OE1 GLU B 171     7787  11138  16475    208  -1981    222  B    O  
ATOM   1224  OE2 GLU B 171     -61.244  17.008  14.039  1.00 81.60      B    O  
ANISOU 1224  OE2 GLU B 171     6468   9634  14903     42  -1688     -4  B    O  
ATOM   1225  N   GLU B 172     -58.472  21.562  16.788  1.00 58.21      B    N  
ANISOU 1225  N   GLU B 172     3768   5839  12509    670  -1736     52  B    N  
ATOM   1226  CA  GLU B 172     -57.911  21.831  18.095  1.00 51.34      B    C  
ANISOU 1226  CA  GLU B 172     2979   4830  11698    729  -1648    -70  B    C  
ATOM   1227  C   GLU B 172     -57.652  23.304  18.283  1.00 52.58      B    C  
ANISOU 1227  C   GLU B 172     3180   4770  12026    872  -1753    -35  B    C  
ATOM   1228  O   GLU B 172     -57.720  23.807  19.407  1.00 70.48      B    O  
ANISOU 1228  O   GLU B 172     5468   6931  14379    979  -1708   -171  B    O  
ATOM   1229  CB  GLU B 172     -56.624  21.028  18.286  1.00 55.57      B    C  
ANISOU 1229  CB  GLU B 172     3662   5344  12107    587  -1555    -69  B    C  
ATOM   1230  CG  GLU B 172     -56.891  19.543  18.337  1.00 45.88      B    C  
ANISOU 1230  CG  GLU B 172     2421   4284  10727    463  -1428   -132  B    C  
ATOM   1231  CD  GLU B 172     -55.620  18.739  18.526  1.00 57.14      B    C  
ANISOU 1231  CD  GLU B 172     3991   5678  12042    357  -1332   -120  B    C  
ATOM   1232  OE1 GLU B 172     -54.584  19.338  18.903  1.00 56.78      B    O  
ANISOU 1232  OE1 GLU B 172     4030   5502  12043    382  -1354    -89  B    O  
ATOM   1233  OE2 GLU B 172     -55.649  17.503  18.289  1.00 55.22      B    O  
ANISOU 1233  OE2 GLU B 172     3775   5536  11671    245  -1237   -140  B    O  
ATOM   1234  N   GLY B 173     -57.362  23.994  17.185  1.00 50.09      B    N  
ANISOU 1234  N   GLY B 173     2894   4384  11756    869  -1892    145  B    N  
ATOM   1235  CA  GLY B 173     -57.268  25.443  17.210  1.00 48.63      B    C  
ANISOU 1235  CA  GLY B 173     2751   3970  11754   1004  -2010    204  B    C  
ATOM   1236  C   GLY B 173     -58.594  26.075  17.621  1.00 64.81      B    C  
ANISOU 1236  C   GLY B 173     4663   6010  13950   1218  -2037    122  B    C  
ATOM   1237  O   GLY B 173     -58.650  26.897  18.553  1.00 65.16      B    O  
ANISOU 1237  O   GLY B 173     4751   5875  14131   1359  -2023      4  B    O  
ATOM   1238  N   ASN B 174     -59.663  25.687  16.929  1.00 47.19      B    N  
ANISOU 1238  N   ASN B 174     2262   3980  11689   1243  -2074    178  B    N  
ATOM   1239  CA  ASN B 174     -60.968  26.218  17.247  1.00 64.48      B    C  
ANISOU 1239  CA  ASN B 174     4277   6203  14019   1455  -2094    118  B    C  
ATOM   1240  C   ASN B 174     -61.274  25.924  18.704  1.00 74.21      B    C  
ANISOU 1240  C   ASN B 174     5484   7453  15260   1522  -1924   -124  B    C  
ATOM   1241  O   ASN B 174     -61.558  26.839  19.492  1.00 75.04      B    O  
ANISOU 1241  O   ASN B 174     5598   7399  15515   1718  -1908   -229  B    O  
ATOM   1242  CB  ASN B 174     -62.036  25.651  16.312  1.00 75.57      B    C  
ANISOU 1242  CB  ASN B 174     5479   7876  15360   1429  -2159    212  B    C  
ATOM   1243  CG  ASN B 174     -62.007  26.310  14.945  1.00 84.65      B    C  
ANISOU 1243  CG  ASN B 174     6630   8996  16536   1442  -2356    459  B    C  
ATOM   1244  ND2 ASN B 174     -62.007  25.502  13.892  1.00 72.35      B    N  
ANISOU 1244  ND2 ASN B 174     5047   7642  14802   1264  -2406    569  B    N  
ATOM   1245  OD1 ASN B 174     -61.974  27.535  14.842  1.00101.39      B    O  
ANISOU 1245  OD1 ASN B 174     8792  10903  18830   1610  -2459    550  B    O  
ATOM   1246  N   PHE B 175     -61.166  24.652  19.070  1.00 62.66      B    N  
ANISOU 1246  N   PHE B 175     4011   6167  13628   1357  -1792   -211  B    N  
ATOM   1247  CA  PHE B 175     -61.375  24.253  20.456  1.00 73.09      B    C  
ANISOU 1247  CA  PHE B 175     5323   7528  14920   1390  -1620   -420  B    C  
ATOM   1248  C   PHE B 175     -60.620  25.104  21.483  1.00 74.84      B    C  
ANISOU 1248  C   PHE B 175     5717   7505  15214   1482  -1592   -536  B    C  
ATOM   1249  O   PHE B 175     -61.128  25.375  22.568  1.00 83.12      B    O  
ANISOU 1249  O   PHE B 175     6733   8543  16306   1617  -1492   -709  B    O  
ATOM   1250  CB  PHE B 175     -61.019  22.785  20.674  1.00 63.33      B    C  
ANISOU 1250  CB  PHE B 175     4121   6456  13486   1173  -1493   -462  B    C  
ATOM   1251  CG  PHE B 175     -61.112  22.364  22.114  1.00 67.32      B    C  
ANISOU 1251  CG  PHE B 175     4642   6997  13939   1191  -1318   -650  B    C  
ATOM   1252  CD1 PHE B 175     -62.328  21.950  22.658  1.00 70.29      B    C  
ANISOU 1252  CD1 PHE B 175     4833   7563  14312   1244  -1208   -748  B    C  
ATOM   1253  CD2 PHE B 175     -60.004  22.412  22.932  1.00 51.14      B    C  
ANISOU 1253  CD2 PHE B 175     2783   4810  11837   1152  -1269   -717  B    C  
ATOM   1254  CE1 PHE B 175     -62.423  21.573  23.993  1.00 55.38      B    C  
ANISOU 1254  CE1 PHE B 175     2965   5723  12356   1258  -1036   -908  B    C  
ATOM   1255  CE2 PHE B 175     -60.092  22.038  24.259  1.00 68.53      B    C  
ANISOU 1255  CE2 PHE B 175     5011   7061  13967   1167  -1117   -879  B    C  
ATOM   1256  CZ  PHE B 175     -61.305  21.619  24.793  1.00 67.94      B    C  
ANISOU 1256  CZ  PHE B 175     4765   7173  13876   1222   -994   -975  B    C  
ATOM   1257  N   LEU B 176     -59.408  25.522  21.154  1.00 76.56      B    N  
ANISOU 1257  N   LEU B 176     6114   7538  15437   1398  -1678   -447  B    N  
ATOM   1258  CA  LEU B 176     -58.643  26.326  22.098  1.00 75.24      B    C  
ANISOU 1258  CA  LEU B 176     6115   7140  15334   1450  -1675   -559  B    C  
ATOM   1259  C   LEU B 176     -59.107  27.778  22.177  1.00 72.89      B    C  
ANISOU 1259  C   LEU B 176     5832   6615  15249   1671  -1764   -585  B    C  
ATOM   1260  O   LEU B 176     -58.906  28.424  23.204  1.00 76.58      B    O  
ANISOU 1260  O   LEU B 176     6409   6916  15771   1760  -1728   -751  B    O  
ATOM   1261  CB  LEU B 176     -57.147  26.256  21.803  1.00 70.19      B    C  
ANISOU 1261  CB  LEU B 176     5644   6392  14631   1266  -1730   -456  B    C  
ATOM   1262  CG  LEU B 176     -56.519  24.869  21.983  1.00 59.47      B    C  
ANISOU 1262  CG  LEU B 176     4308   5214  13073   1079  -1621   -461  B    C  
ATOM   1263  CD1 LEU B 176     -55.182  24.809  21.264  1.00 56.14      B    C  
ANISOU 1263  CD1 LEU B 176     3996   4727  12610    920  -1690   -299  B    C  
ATOM   1264  CD2 LEU B 176     -56.351  24.521  23.459  1.00 53.19      B    C  
ANISOU 1264  CD2 LEU B 176     3570   4440  12200   1085  -1495   -657  B    C  
ATOM   1265  N   THR B 177     -59.742  28.294  21.126  1.00 58.41      B    N  
ANISOU 1265  N   THR B 177     3896   4768  13530   1768  -1883   -426  B    N  
ATOM   1266  CA  THR B 177     -60.176  29.700  21.164  1.00 63.87      B    C  
ANISOU 1266  CA  THR B 177     4614   5211  14445   2001  -1973   -432  B    C  
ATOM   1267  C   THR B 177     -61.306  29.898  22.162  1.00 68.46      B    C  
ANISOU 1267  C   THR B 177     5076   5841  15095   2233  -1851   -644  B    C  
ATOM   1268  O   THR B 177     -61.678  31.023  22.479  1.00 79.54      B    O  
ANISOU 1268  O   THR B 177     6520   7024  16681   2459  -1882   -711  B    O  
ATOM   1269  CB  THR B 177     -60.575  30.263  19.784  1.00 62.00      B    C  
ANISOU 1269  CB  THR B 177     4298   4941  14318   2066  -2143   -180  B    C  
ATOM   1270  CG2 THR B 177     -59.447  30.093  18.806  1.00 78.88      B    C  
ANISOU 1270  CG2 THR B 177     6556   7045  16371   1839  -2243     29  B    C  
ATOM   1271  OG1 THR B 177     -61.703  29.554  19.285  1.00 58.49      B    O  
ANISOU 1271  OG1 THR B 177     3609   4794  13820   2104  -2126   -132  B    O  
ATOM   1272  N   LYS B 178     -61.836  28.786  22.661  1.00 73.10      B    N  
ANISOU 1272  N   LYS B 178     5526   6713  15534   2176  -1701   -747  B    N  
ATOM   1273  CA  LYS B 178     -62.826  28.810  23.733  1.00 86.23      B    C  
ANISOU 1273  CA  LYS B 178     7071   8472  17222   2363  -1545   -959  B    C  
ATOM   1274  C   LYS B 178     -62.194  29.092  25.102  1.00 87.92      B    C  
ANISOU 1274  C   LYS B 178     7485   8534  17386   2375  -1438  -1191  B    C  
ATOM   1275  O   LYS B 178     -62.882  29.504  26.030  1.00 90.61      B    O  
ANISOU 1275  O   LYS B 178     7789   8865  17772   2575  -1322  -1385  B    O  
ATOM   1276  CB  LYS B 178     -63.585  27.481  23.783  1.00 92.40      B    C  
ANISOU 1276  CB  LYS B 178     7637   9617  17853   2260  -1420   -969  B    C  
ATOM   1277  CG  LYS B 178     -64.379  27.175  22.525  1.00 99.75      B    C  
ANISOU 1277  CG  LYS B 178     8346  10734  18819   2246  -1525   -772  B    C  
ATOM   1278  CD  LYS B 178     -64.531  25.672  22.325  1.00114.39      B    C  
ANISOU 1278  CD  LYS B 178    10098  12886  20478   2003  -1446   -744  B    C  
ATOM   1279  CE  LYS B 178     -65.499  25.053  23.319  1.00124.63      B    C  
ANISOU 1279  CE  LYS B 178    11217  14411  21725   2047  -1251   -906  B    C  
ATOM   1280  NZ  LYS B 178     -65.812  23.639  22.968  1.00125.44      B    N  
ANISOU 1280  NZ  LYS B 178    11202  14789  21671   1807  -1198   -852  B    N  
ATOM   1281  N   TYR B 179     -60.890  28.873  25.233  1.00 79.48      B    N  
ANISOU 1281  N   TYR B 179     6621   7365  16214   2165  -1477  -1175  B    N  
ATOM   1282  CA  TYR B 179     -60.236  29.079  26.524  1.00 78.49      B    C  
ANISOU 1282  CA  TYR B 179     6684   7126  16013   2147  -1399  -1387  B    C  
ATOM   1283  C   TYR B 179     -59.168  30.171  26.526  1.00 83.99      B    C  
ANISOU 1283  C   TYR B 179     7621   7478  16812   2118  -1541  -1386  B    C  
ATOM   1284  O   TYR B 179     -58.977  30.850  27.532  1.00 82.42      B    O  
ANISOU 1284  O   TYR B 179     7575   7108  16632   2197  -1509  -1592  B    O  
ATOM   1285  CB  TYR B 179     -59.634  27.778  27.042  1.00 74.96      B    C  
ANISOU 1285  CB  TYR B 179     6262   6891  15328   1922  -1295  -1411  B    C  
ATOM   1286  CG  TYR B 179     -60.652  26.682  27.264  1.00102.88      B    C  
ANISOU 1286  CG  TYR B 179     9592  10746  18753   1925  -1135  -1440  B    C  
ATOM   1287  CD1 TYR B 179     -61.391  26.624  28.432  1.00109.66      B    C  
ANISOU 1287  CD1 TYR B 179    10401  11711  19555   2051   -963  -1646  B    C  
ATOM   1288  CD2 TYR B 179     -60.871  25.698  26.300  1.00109.41      B    C  
ANISOU 1288  CD2 TYR B 179    10280  11766  19524   1787  -1150  -1265  B    C  
ATOM   1289  CE1 TYR B 179     -62.321  25.622  28.638  1.00116.77      B    C  
ANISOU 1289  CE1 TYR B 179    11102  12907  20359   2030   -811  -1657  B    C  
ATOM   1290  CE2 TYR B 179     -61.803  24.692  26.498  1.00108.64      B    C  
ANISOU 1290  CE2 TYR B 179     9999  11946  19333   1759  -1011  -1289  B    C  
ATOM   1291  CZ  TYR B 179     -62.522  24.660  27.671  1.00113.83      B    C  
ANISOU 1291  CZ  TYR B 179    10594  12708  19948   1875   -842  -1476  B    C  
ATOM   1292  OH  TYR B 179     -63.450  23.669  27.886  1.00113.18      B    O  
ANISOU 1292  OH  TYR B 179    10320  12906  19778   1827   -697  -1489  B    O  
ATOM   1293  N   GLY B 180     -58.470  30.329  25.405  1.00 79.74      B    N  
ANISOU 1293  N   GLY B 180     7123   6844  16331   1988  -1695  -1157  B    N  
ATOM   1294  CA  GLY B 180     -57.400  31.308  25.301  1.00 60.39      B    C  
ANISOU 1294  CA  GLY B 180     4884   4079  13981   1915  -1836  -1117  B    C  
ATOM   1295  C   GLY B 180     -57.877  32.675  24.828  1.00 72.73      B    C  
ANISOU 1295  C   GLY B 180     6490   5348  15795   2118  -1950  -1072  B    C  
ATOM   1296  O   GLY B 180     -59.021  32.834  24.389  1.00 70.02      B    O  
ANISOU 1296  O   GLY B 180     5987   5069  15552   2322  -1938  -1028  B    O  
ATOM   1297  N   SER B 181     -56.980  33.658  24.905  1.00 79.54      B    N  
ANISOU 1297  N   SER B 181     7569   5887  16765   2054  -2069  -1070  B    N  
ATOM   1298  CA  SER B 181     -57.232  35.010  24.420  1.00 83.04      B    C  
ANISOU 1298  CA  SER B 181     8103   5988  17461   2216  -2194  -1001  B    C  
ATOM   1299  C   SER B 181     -56.969  35.141  22.922  1.00 79.19      B    C  
ANISOU 1299  C   SER B 181     7567   5477  17046   2125  -2341   -659  B    C  
ATOM   1300  O   SER B 181     -57.553  36.001  22.235  1.00 73.93      B    O  
ANISOU 1300  O   SER B 181     6888   4628  16574   2302  -2437   -529  B    O  
ATOM   1301  CB  SER B 181     -56.336  35.987  25.166  1.00 85.91      B    C  
ANISOU 1301  CB  SER B 181     8741   5999  17903   2147  -2263  -1149  B    C  
ATOM   1302  OG  SER B 181     -54.971  35.727  24.896  1.00 80.55      B    O  
ANISOU 1302  OG  SER B 181     8150   5318  17138   1834  -2349  -1016  B    O  
ATOM   1303  N   GLN B 182     -56.088  34.279  22.431  1.00 62.15      B    N  
ANISOU 1303  N   GLN B 182     5381   3508  14723   1862  -2354   -512  B    N  
ATOM   1304  CA  GLN B 182     -55.671  34.277  21.041  1.00 79.78      B    C  
ANISOU 1304  CA  GLN B 182     7582   5760  16971   1735  -2471   -195  B    C  
ATOM   1305  C   GLN B 182     -55.005  32.924  20.742  1.00 85.12      B    C  
ANISOU 1305  C   GLN B 182     8176   6757  17410   1499  -2404   -118  B    C  
ATOM   1306  O   GLN B 182     -54.331  32.358  21.601  1.00 82.50      B    O  
ANISOU 1306  O   GLN B 182     7896   6500  16953   1373  -2324   -262  B    O  
ATOM   1307  CB  GLN B 182     -54.708  35.449  20.793  1.00 79.29      B    C  
ANISOU 1307  CB  GLN B 182     7728   5332  17066   1634  -2617    -84  B    C  
ATOM   1308  CG  GLN B 182     -54.059  35.476  19.414  1.00 95.01      B    C  
ANISOU 1308  CG  GLN B 182     9710   7344  19048   1462  -2728    255  B    C  
ATOM   1309  CD  GLN B 182     -55.033  35.845  18.305  1.00109.67      B    C  
ANISOU 1309  CD  GLN B 182    11465   9203  21002   1637  -2810    469  B    C  
ATOM   1310  NE2 GLN B 182     -54.992  35.094  17.203  1.00116.54      B    N  
ANISOU 1310  NE2 GLN B 182    12212  10342  21727   1528  -2824    689  B    N  
ATOM   1311  OE1 GLN B 182     -55.807  36.795  18.435  1.00101.06      B    O  
ANISOU 1311  OE1 GLN B 182    10409   7878  20110   1873  -2864    435  B    O  
ATOM   1312  N   VAL B 183     -55.211  32.396  19.539  1.00 75.48      B    N  
ANISOU 1312  N   VAL B 183     6834   5725  16120   1449  -2436    106  B    N  
ATOM   1313  CA  VAL B 183     -54.620  31.115  19.162  1.00 58.06      B    C  
ANISOU 1313  CA  VAL B 183     4563   3801  13695   1246  -2363    176  B    C  
ATOM   1314  C   VAL B 183     -53.820  31.252  17.875  1.00 69.28      B    C  
ANISOU 1314  C   VAL B 183     6018   5212  15094   1087  -2462    462  B    C  
ATOM   1315  O   VAL B 183     -54.294  31.849  16.910  1.00 85.72      B    O  
ANISOU 1315  O   VAL B 183     8073   7234  17262   1162  -2569    647  B    O  
ATOM   1316  CB  VAL B 183     -55.693  30.019  18.974  1.00 60.65      B    C  
ANISOU 1316  CB  VAL B 183     4704   4443  13896   1311  -2268    134  B    C  
ATOM   1317  CG1 VAL B 183     -55.051  28.722  18.451  1.00 50.49      B    C  
ANISOU 1317  CG1 VAL B 183     3383   3408  12394   1100  -2199    217  B    C  
ATOM   1318  CG2 VAL B 183     -56.426  29.761  20.278  1.00 60.26      B    C  
ANISOU 1318  CG2 VAL B 183     4608   4446  13841   1442  -2142   -137  B    C  
ATOM   1319  N   TYR B 184     -52.604  30.712  17.859  1.00 67.77      B    N  
ANISOU 1319  N   TYR B 184     5877   5088  14783    875  -2423    510  B    N  
ATOM   1320  CA  TYR B 184     -51.784  30.759  16.656  1.00 68.22      B    C  
ANISOU 1320  CA  TYR B 184     5954   5171  14794    715  -2485    777  B    C  
ATOM   1321  C   TYR B 184     -51.544  29.362  16.107  1.00 64.59      B    C  
ANISOU 1321  C   TYR B 184     5407   5030  14105    601  -2377    824  B    C  
ATOM   1322  O   TYR B 184     -50.905  28.566  16.768  1.00 63.05      B    O  
ANISOU 1322  O   TYR B 184     5216   4934  13804    512  -2273    713  B    O  
ATOM   1323  CB  TYR B 184     -50.419  31.372  16.953  1.00 69.49      B    C  
ANISOU 1323  CB  TYR B 184     6239   5145  15019    549  -2531    828  B    C  
ATOM   1324  CG  TYR B 184     -50.449  32.739  17.565  1.00 76.37      B    C  
ANISOU 1324  CG  TYR B 184     7240   5665  16114    619  -2637    763  B    C  
ATOM   1325  CD1 TYR B 184     -50.679  33.865  16.785  1.00 83.85      B    C  
ANISOU 1325  CD1 TYR B 184     8249   6383  17227    670  -2769    952  B    C  
ATOM   1326  CD2 TYR B 184     -50.219  32.911  18.921  1.00 69.56      B    C  
ANISOU 1326  CD2 TYR B 184     6454   4688  15288    627  -2608    513  B    C  
ATOM   1327  CE1 TYR B 184     -50.703  35.124  17.339  1.00 82.41      B    C  
ANISOU 1327  CE1 TYR B 184     8211   5839  17262    736  -2864    883  B    C  
ATOM   1328  CE2 TYR B 184     -50.232  34.171  19.493  1.00 74.39      B    C  
ANISOU 1328  CE2 TYR B 184     7212   4957  16098    684  -2703    425  B    C  
ATOM   1329  CZ  TYR B 184     -50.477  35.279  18.697  1.00 86.48      B    C  
ANISOU 1329  CZ  TYR B 184     8813   6234  17812    741  -2829    607  B    C  
ATOM   1330  OH  TYR B 184     -50.496  36.546  19.255  1.00 96.87      B    O  
ANISOU 1330  OH  TYR B 184    10299   7167  19340    802  -2922    514  B    O  
ATOM   1331  N   ILE B 185     -52.048  29.071  14.905  1.00 57.73      B    N  
ANISOU 1331  N   ILE B 185     4470   4310  13155    606  -2406    986  B    N  
ATOM   1332  CA  ILE B 185     -51.661  27.872  14.168  1.00 54.64      B    C  
ANISOU 1332  CA  ILE B 185     4035   4182  12544    474  -2317   1056  B    C  
ATOM   1333  C   ILE B 185     -50.317  28.158  13.472  1.00 58.73      B    C  
ANISOU 1333  C   ILE B 185     4624   4661  13029    308  -2335   1264  B    C  
ATOM   1334  O   ILE B 185     -50.198  29.148  12.753  1.00 78.80      B    O  
ANISOU 1334  O   ILE B 185     7209   7070  15662    297  -2452   1461  B    O  
ATOM   1335  CB  ILE B 185     -52.710  27.466  13.101  1.00 62.00      B    C  
ANISOU 1335  CB  ILE B 185     4878   5304  13377    523  -2353   1143  B    C  
ATOM   1336  CG1 ILE B 185     -54.001  26.975  13.737  1.00 63.69      B    C  
ANISOU 1336  CG1 ILE B 185     4983   5616  13599    655  -2314    946  B    C  
ATOM   1337  CG2 ILE B 185     -52.192  26.306  12.271  1.00 58.81      B    C  
ANISOU 1337  CG2 ILE B 185     4470   5137  12739    374  -2262   1208  B    C  
ATOM   1338  CD1 ILE B 185     -54.564  27.891  14.755  1.00 80.95      B    C  
ANISOU 1338  CD1 ILE B 185     7166   7601  15991    825  -2351    817  B    C  
ATOM   1339  N   ILE B 186     -49.306  27.315  13.706  1.00 61.70      B    N  
ANISOU 1339  N   ILE B 186     5006   5152  13285    184  -2217   1232  B    N  
ATOM   1340  CA  ILE B 186     -47.979  27.457  13.078  1.00 54.50      B    C  
ANISOU 1340  CA  ILE B 186     4127   4251  12329     25  -2205   1426  B    C  
ATOM   1341  C   ILE B 186     -47.670  26.261  12.177  1.00 61.87      B    C  
ANISOU 1341  C   ILE B 186     5025   5452  13033    -47  -2082   1491  B    C  
ATOM   1342  O   ILE B 186     -47.685  25.124  12.625  1.00 65.15      B    O  
ANISOU 1342  O   ILE B 186     5413   6003  13336    -37  -1957   1339  B    O  
ATOM   1343  CB  ILE B 186     -46.870  27.574  14.133  1.00 52.30      B    C  
ANISOU 1343  CB  ILE B 186     3872   3879  12120    -57  -2173   1348  B    C  
ATOM   1344  CG1 ILE B 186     -47.199  28.684  15.132  1.00 59.63      B    C  
ANISOU 1344  CG1 ILE B 186     4864   4537  13255     11  -2285   1232  B    C  
ATOM   1345  CG2 ILE B 186     -45.503  27.803  13.480  1.00 48.79      B    C  
ANISOU 1345  CG2 ILE B 186     3429   3458  11653   -227  -2164   1567  B    C  
ATOM   1346  CD1 ILE B 186     -46.191  28.828  16.251  1.00 50.69      B    C  
ANISOU 1346  CD1 ILE B 186     3762   3321  12176    -80  -2279   1132  B    C  
ATOM   1347  N   HIS B 187     -47.393  26.518  10.906  1.00 65.49      B    N  
ANISOU 1347  N   HIS B 187     5496   5974  13415   -118  -2111   1716  B    N  
ATOM   1348  CA  HIS B 187     -47.245  25.448   9.926  1.00 54.31      B    C  
ANISOU 1348  CA  HIS B 187     4067   4807  11760   -173  -1998   1766  B    C  
ATOM   1349  C   HIS B 187     -46.059  25.735   9.003  1.00 58.94      B    C  
ANISOU 1349  C   HIS B 187     4671   5447  12276   -305  -1964   2006  B    C  
ATOM   1350  O   HIS B 187     -45.760  26.874   8.699  1.00 75.52      B    O  
ANISOU 1350  O   HIS B 187     6793   7407  14494   -354  -2072   2190  B    O  
ATOM   1351  CB  HIS B 187     -48.549  25.301   9.143  1.00 51.75      B    C  
ANISOU 1351  CB  HIS B 187     3730   4583  11349   -105  -2070   1773  B    C  
ATOM   1352  CG  HIS B 187     -48.522  24.243   8.082  1.00 62.33      B    C  
ANISOU 1352  CG  HIS B 187     5084   6173  12429   -170  -1973   1803  B    C  
ATOM   1353  CD2 HIS B 187     -48.793  24.308   6.753  1.00 71.65      B    C  
ANISOU 1353  CD2 HIS B 187     6286   7487  13450   -213  -2024   1966  B    C  
ATOM   1354  ND1 HIS B 187     -48.236  22.924   8.349  1.00 66.18      B    N  
ANISOU 1354  ND1 HIS B 187     5577   6790  12779   -194  -1807   1642  B    N  
ATOM   1355  CE1 HIS B 187     -48.312  22.222   7.228  1.00 70.55      B    C  
ANISOU 1355  CE1 HIS B 187     6166   7534  13105   -250  -1751   1687  B    C  
ATOM   1356  NE2 HIS B 187     -48.648  23.038   6.248  1.00 71.60      B    N  
ANISOU 1356  NE2 HIS B 187     6308   7688  13210   -268  -1882   1880  B    N  
ATOM   1357  N   ARG B 188     -45.370  24.691   8.573  1.00 80.36      B    N  
ANISOU 1357  N   ARG B 188     7372   8358  14802   -361  -1803   2004  B    N  
ATOM   1358  CA  ARG B 188     -44.122  24.853   7.833  1.00 77.81      B    C  
ANISOU 1358  CA  ARG B 188     7041   8115  14409   -480  -1729   2213  B    C  
ATOM   1359  C   ARG B 188     -44.337  25.454   6.446  1.00 79.73      B    C  
ANISOU 1359  C   ARG B 188     7322   8419  14551   -533  -1799   2452  B    C  
ATOM   1360  O   ARG B 188     -43.472  26.156   5.928  1.00 87.15      B    O  
ANISOU 1360  O   ARG B 188     8258   9344  15512   -640  -1804   2679  B    O  
ATOM   1361  CB  ARG B 188     -43.423  23.501   7.720  1.00 71.34      B    C  
ANISOU 1361  CB  ARG B 188     6200   7498  13407   -488  -1519   2130  B    C  
ATOM   1362  CG  ARG B 188     -41.923  23.579   7.593  1.00 98.63      B    C  
ANISOU 1362  CG  ARG B 188     9595  11016  16863   -582  -1413   2280  B    C  
ATOM   1363  CD  ARG B 188     -41.298  22.197   7.655  1.00114.50      B    C  
ANISOU 1363  CD  ARG B 188    11580  13200  18725   -541  -1200   2170  B    C  
ATOM   1364  NE  ARG B 188     -42.030  21.257   6.816  1.00136.88      B    N  
ANISOU 1364  NE  ARG B 188    14495  16176  21336   -493  -1119   2083  B    N  
ATOM   1365  CZ  ARG B 188     -41.620  20.024   6.540  1.00152.37      B    C  
ANISOU 1365  CZ  ARG B 188    16478  18285  23131   -456   -924   1995  B    C  
ATOM   1366  NH1 ARG B 188     -40.472  19.579   7.038  1.00158.95      B    N  
ANISOU 1366  NH1 ARG B 188    17237  19158  24000   -436   -787   2001  B    N  
ATOM   1367  NH2 ARG B 188     -42.357  19.237   5.764  1.00147.43      B    N  
ANISOU 1367  NH2 ARG B 188    15949  17766  22302   -435   -872   1901  B    N  
ATOM   1368  N   ARG B 189     -45.492  25.175   5.848  1.00 79.93      B    N  
ANISOU 1368  N   ARG B 189     7381   8528  14461   -471  -1857   2412  B    N  
ATOM   1369  CA  ARG B 189     -45.783  25.633   4.489  1.00 85.40      B    C  
ANISOU 1369  CA  ARG B 189     8116   9317  15014   -515  -1933   2638  B    C  
ATOM   1370  C   ARG B 189     -46.724  26.827   4.467  1.00 85.38      B    C  
ANISOU 1370  C   ARG B 189     8126   9133  15182   -451  -2154   2743  B    C  
ATOM   1371  O   ARG B 189     -47.058  27.392   5.507  1.00 81.39      B    O  
ANISOU 1371  O   ARG B 189     7602   8408  14915   -373  -2238   2642  B    O  
ATOM   1372  CB  ARG B 189     -46.328  24.485   3.628  1.00 80.63      B    C  
ANISOU 1372  CB  ARG B 189     7545   8968  14123   -511  -1853   2552  B    C  
ATOM   1373  CG  ARG B 189     -45.329  23.342   3.510  1.00 87.55      B    C  
ANISOU 1373  CG  ARG B 189     8432  10006  14827   -559  -1620   2468  B    C  
ATOM   1374  CD  ARG B 189     -45.845  22.201   2.661  1.00105.62      B    C  
ANISOU 1374  CD  ARG B 189    10787  12518  16827   -565  -1536   2357  B    C  
ATOM   1375  NE  ARG B 189     -45.378  20.921   3.197  1.00129.93      B    N  
ANISOU 1375  NE  ARG B 189    13876  15648  19844   -538  -1338   2139  B    N  
ATOM   1376  CZ  ARG B 189     -44.139  20.456   3.057  1.00143.79      B    C  
ANISOU 1376  CZ  ARG B 189    15629  17481  21524   -562  -1144   2173  B    C  
ATOM   1377  NH1 ARG B 189     -43.233  21.161   2.388  1.00148.10      B    N  
ANISOU 1377  NH1 ARG B 189    16152  18082  22039   -633  -1115   2417  B    N  
ATOM   1378  NH2 ARG B 189     -43.806  19.282   3.585  1.00137.27      B    N  
ANISOU 1378  NH2 ARG B 189    14816  16680  20659   -511   -974   1977  B    N  
ATOM   1379  N   ASN B 190     -47.133  27.221   3.272  1.00 86.46      B    N  
ANISOU 1379  N   ASN B 190     8298   9362  15191   -473  -2246   2954  B    N  
ATOM   1380  CA  ASN B 190     -48.022  28.361   3.133  1.00105.68      B    C  
ANISOU 1380  CA  ASN B 190    10742  11628  17782   -392  -2461   3092  B    C  
ATOM   1381  C   ASN B 190     -49.384  27.843   2.732  1.00109.61      B    C  
ANISOU 1381  C   ASN B 190    11208  12284  18156   -297  -2546   3000  B    C  
ATOM   1382  O   ASN B 190     -50.258  28.589   2.315  1.00111.22      B    O  
ANISOU 1382  O   ASN B 190    11402  12436  18419   -218  -2726   3137  B    O  
ATOM   1383  CB  ASN B 190     -47.488  29.343   2.091  1.00110.27      B    C  
ANISOU 1383  CB  ASN B 190    11384  12182  18332   -490  -2534   3447  B    C  
ATOM   1384  CG  ASN B 190     -47.221  28.682   0.762  1.00122.53      B    C  
ANISOU 1384  CG  ASN B 190    12969  14048  19538   -590  -2447   3576  B    C  
ATOM   1385  ND2 ASN B 190     -46.772  29.470  -0.205  1.00125.79      B    N  
ANISOU 1385  ND2 ASN B 190    13436  14474  19885   -684  -2497   3900  B    N  
ATOM   1386  OD1 ASN B 190     -47.415  27.472   0.602  1.00126.67      B    O  
ANISOU 1386  OD1 ASN B 190    13483  14795  19850   -588  -2333   3384  B    O  
ATOM   1387  N   THR B 191     -49.558  26.543   2.872  1.00107.70      B    N  
ANISOU 1387  N   THR B 191    10943  12230  17747   -308  -2419   2769  B    N  
ATOM   1388  CA  THR B 191     -50.802  25.921   2.489  1.00 95.14      B    C  
ANISOU 1388  CA  THR B 191     9314  10814  16021   -257  -2491   2665  B    C  
ATOM   1389  C   THR B 191     -51.096  24.757   3.435  1.00 94.62      B    C  
ANISOU 1389  C   THR B 191     9207  10788  15957   -230  -2365   2341  B    C  
ATOM   1390  O   THR B 191     -50.177  24.039   3.853  1.00 86.60      B    O  
ANISOU 1390  O   THR B 191     8225   9783  14894   -287  -2184   2227  B    O  
ATOM   1391  CB  THR B 191     -50.729  25.451   1.025  1.00 92.56      B    C  
ANISOU 1391  CB  THR B 191     9050  10758  15359   -367  -2480   2801  B    C  
ATOM   1392  CG2 THR B 191     -49.455  24.620   0.785  1.00 78.64      B    C  
ANISOU 1392  CG2 THR B 191     7359   9107  13413   -483  -2246   2758  B    C  
ATOM   1393  OG1 THR B 191     -51.897  24.682   0.701  1.00109.74      B    O  
ANISOU 1393  OG1 THR B 191    11189  13123  17384   -352  -2545   2662  B    O  
ATOM   1394  N   PHE B 192     -52.374  24.592   3.780  1.00 92.41      B    N  
ANISOU 1394  N   PHE B 192     8843  10533  15735   -141  -2462   2210  B    N  
ATOM   1395  CA  PHE B 192     -52.809  23.550   4.719  1.00 75.73      B    C  
ANISOU 1395  CA  PHE B 192     6684   8452  13638   -119  -2356   1919  B    C  
ATOM   1396  C   PHE B 192     -53.227  22.237   4.055  1.00 78.37      B    C  
ANISOU 1396  C   PHE B 192     7041   9036  13700   -218  -2293   1797  B    C  
ATOM   1397  O   PHE B 192     -53.963  22.231   3.056  1.00 79.17      B    O  
ANISOU 1397  O   PHE B 192     7128   9305  13647   -253  -2418   1883  B    O  
ATOM   1398  CB  PHE B 192     -53.961  24.051   5.598  1.00 64.77      B    C  
ANISOU 1398  CB  PHE B 192     5177   6956  12476     27  -2469   1825  B    C  
ATOM   1399  CG  PHE B 192     -53.532  24.970   6.698  1.00 73.64      B    C  
ANISOU 1399  CG  PHE B 192     6302   7809  13871    125  -2469   1811  B    C  
ATOM   1400  CD1 PHE B 192     -52.407  24.695   7.442  1.00 80.49      B    C  
ANISOU 1400  CD1 PHE B 192     7231   8580  14772     72  -2320   1726  B    C  
ATOM   1401  CD2 PHE B 192     -54.260  26.095   7.001  1.00 78.25      B    C  
ANISOU 1401  CD2 PHE B 192     6824   8234  14672    272  -2618   1874  B    C  
ATOM   1402  CE1 PHE B 192     -52.009  25.532   8.457  1.00 67.36      B    C  
ANISOU 1402  CE1 PHE B 192     5578   6677  13339    138  -2334   1699  B    C  
ATOM   1403  CE2 PHE B 192     -53.862  26.939   8.017  1.00 83.59      B    C  
ANISOU 1403  CE2 PHE B 192     7530   8645  15588    353  -2616   1836  B    C  
ATOM   1404  CZ  PHE B 192     -52.737  26.659   8.740  1.00 72.38      B    C  
ANISOU 1404  CZ  PHE B 192     6180   7141  14182    272  -2480   1744  B    C  
ATOM   1405  N   ARG B 193     -52.772  21.134   4.645  1.00 77.91      B    N  
ANISOU 1405  N   ARG B 193     7024   8989  13587   -263  -2107   1594  B    N  
ATOM   1406  CA  ARG B 193     -53.135  19.780   4.226  1.00 70.52      B    C  
ANISOU 1406  CA  ARG B 193     6135   8234  12424   -360  -2022   1429  B    C  
ATOM   1407  C   ARG B 193     -54.606  19.449   4.525  1.00 73.43      B    C  
ANISOU 1407  C   ARG B 193     6393   8677  12830   -344  -2127   1294  B    C  
ATOM   1408  O   ARG B 193     -55.171  18.521   3.954  1.00 83.19      B    O  
ANISOU 1408  O   ARG B 193     7654  10080  13874   -448  -2125   1194  B    O  
ATOM   1409  CB  ARG B 193     -52.216  18.782   4.942  1.00 63.79      B    C  
ANISOU 1409  CB  ARG B 193     5359   7323  11557   -384  -1795   1265  B    C  
ATOM   1410  CG  ARG B 193     -52.484  17.325   4.639  1.00 97.08      B    C  
ANISOU 1410  CG  ARG B 193     9656  11667  15565   -478  -1681   1076  B    C  
ATOM   1411  CD  ARG B 193     -51.481  16.425   5.366  1.00114.30      B    C  
ANISOU 1411  CD  ARG B 193    11915  13759  17755   -470  -1456    949  B    C  
ATOM   1412  NE  ARG B 193     -51.885  16.112   6.740  1.00112.37      B    N  
ANISOU 1412  NE  ARG B 193    11607  13398  17691   -414  -1420    793  B    N  
ATOM   1413  CZ  ARG B 193     -51.492  16.786   7.821  1.00 95.82      B    C  
ANISOU 1413  CZ  ARG B 193     9443  11154  15809   -321  -1422    818  B    C  
ATOM   1414  NH1 ARG B 193     -50.673  17.831   7.700  1.00 96.81      B    N  
ANISOU 1414  NH1 ARG B 193     9553  11211  16018   -283  -1465    991  B    N  
ATOM   1415  NH2 ARG B 193     -51.919  16.415   9.027  1.00 72.92      B    N  
ANISOU 1415  NH2 ARG B 193     6498   8177  13031   -279  -1380    669  B    N  
ATOM   1416  N   ALA B 194     -55.214  20.221   5.422  1.00 73.03      B    N  
ANISOU 1416  N   ALA B 194     6217   8503  13029   -218  -2215   1289  B    N  
ATOM   1417  CA  ALA B 194     -56.566  19.965   5.906  1.00 61.37      B    C  
ANISOU 1417  CA  ALA B 194     4599   7092  11627   -182  -2288   1160  B    C  
ATOM   1418  C   ALA B 194     -57.604  20.206   4.830  1.00 72.14      B    C  
ANISOU 1418  C   ALA B 194     5878   8649  12884   -209  -2486   1272  B    C  
ATOM   1419  O   ALA B 194     -57.332  20.843   3.808  1.00 77.85      B    O  
ANISOU 1419  O   ALA B 194     6648   9418  13513   -219  -2593   1480  B    O  
ATOM   1420  CB  ALA B 194     -56.859  20.846   7.103  1.00 58.97      B    C  
ANISOU 1420  CB  ALA B 194     4189   6606  11610    -16  -2315   1134  B    C  
ATOM   1421  N   SER B 195     -58.810  19.715   5.082  1.00 65.07      B    N  
ANISOU 1421  N   SER B 195     4843   7876  12003   -224  -2541   1149  B    N  
ATOM   1422  CA  SER B 195     -59.913  19.859   4.136  1.00 68.90      B    C  
ANISOU 1422  CA  SER B 195     5211   8578  12390   -257  -2747   1243  B    C  
ATOM   1423  C   SER B 195     -60.231  21.333   3.925  1.00 82.48      B    C  
ANISOU 1423  C   SER B 195     6830  10229  14280    -77  -2932   1476  B    C  
ATOM   1424  O   SER B 195     -59.978  22.154   4.813  1.00 88.85      B    O  
ANISOU 1424  O   SER B 195     7612  10815  15332     83  -2900   1492  B    O  
ATOM   1425  CB  SER B 195     -61.144  19.141   4.667  1.00 67.05      B    C  
ANISOU 1425  CB  SER B 195     4806   8474  12196   -297  -2761   1068  B    C  
ATOM   1426  OG  SER B 195     -61.796  19.939   5.641  1.00 89.23      B    O  
ANISOU 1426  OG  SER B 195     7432  11188  15284   -103  -2799   1068  B    O  
ATOM   1427  N   LYS B 196     -60.781  21.666   2.759  1.00 80.41      B    N  
ANISOU 1427  N   LYS B 196     6521  10149  13884   -105  -3131   1654  B    N  
ATOM   1428  CA  LYS B 196     -61.061  23.061   2.436  1.00 86.51      B    C  
ANISOU 1428  CA  LYS B 196     7216  10847  14806     70  -3319   1910  B    C  
ATOM   1429  C   LYS B 196     -62.091  23.637   3.395  1.00 83.35      B    C  
ANISOU 1429  C   LYS B 196     6596  10373  14700    274  -3381   1861  B    C  
ATOM   1430  O   LYS B 196     -62.058  24.832   3.714  1.00 75.02      B    O  
ANISOU 1430  O   LYS B 196     5513   9116  13874    472  -3446   1996  B    O  
ATOM   1431  CB  LYS B 196     -61.519  23.223   0.985  1.00 94.82      B    C  
ANISOU 1431  CB  LYS B 196     8254  12142  15631     -3  -3531   2121  B    C  
ATOM   1432  CG  LYS B 196     -60.401  23.622   0.025  1.00 99.75      B    C  
ANISOU 1432  CG  LYS B 196     9088  12733  16079    -73  -3525   2330  B    C  
ATOM   1433  CD  LYS B 196     -60.977  23.985  -1.333  1.00115.52      B    C  
ANISOU 1433  CD  LYS B 196    11054  14965  17871   -110  -3766   2574  B    C  
ATOM   1434  CE  LYS B 196     -59.940  24.646  -2.235  1.00122.45      B    C  
ANISOU 1434  CE  LYS B 196    12120  15793  18613   -146  -3773   2837  B    C  
ATOM   1435  NZ  LYS B 196     -60.544  25.141  -3.516  1.00119.33      B    N  
ANISOU 1435  NZ  LYS B 196    11692  15621  18027   -158  -4027   3114  B    N  
ATOM   1436  N   ILE B 197     -62.986  22.776   3.870  1.00 74.33      B    N  
ANISOU 1436  N   ILE B 197     5303   9388  13552    223  -3347   1663  B    N  
ATOM   1437  CA  ILE B 197     -63.959  23.180   4.875  1.00 77.48      B    C  
ANISOU 1437  CA  ILE B 197     5477   9745  14216    411  -3360   1585  B    C  
ATOM   1438  C   ILE B 197     -63.305  23.560   6.198  1.00 81.49      B    C  
ANISOU 1438  C   ILE B 197     6060   9959  14945    541  -3179   1462  B    C  
ATOM   1439  O   ILE B 197     -63.533  24.647   6.728  1.00 82.06      B    O  
ANISOU 1439  O   ILE B 197     6064   9855  15261    767  -3224   1523  B    O  
ATOM   1440  CB  ILE B 197     -64.950  22.068   5.172  1.00 87.41      B    C  
ANISOU 1440  CB  ILE B 197     6564  11238  15409    289  -3327   1391  B    C  
ATOM   1441  CG1 ILE B 197     -65.643  21.608   3.887  1.00 91.18      B    C  
ANISOU 1441  CG1 ILE B 197     6966  12030  15649    127  -3521   1486  B    C  
ATOM   1442  CG2 ILE B 197     -65.965  22.562   6.174  1.00 86.23      B    C  
ANISOU 1442  CG2 ILE B 197     6161  11071  15530    501  -3330   1332  B    C  
ATOM   1443  CD1 ILE B 197     -66.534  22.662   3.268  1.00 88.79      B    C  
ANISOU 1443  CD1 ILE B 197     6461  11836  15441    302  -3779   1728  B    C  
ATOM   1444  N   MET B 198     -62.494  22.649   6.728  1.00 75.09      B    N  
ANISOU 1444  N   MET B 198     5396   9091  14043    398  -2977   1283  B    N  
ATOM   1445  CA  MET B 198     -61.805  22.863   7.994  1.00 71.66      B    C  
ANISOU 1445  CA  MET B 198     5042   8410  13774    486  -2806   1154  B    C  
ATOM   1446  C   MET B 198     -60.906  24.095   7.964  1.00 87.61      B    C  
ANISOU 1446  C   MET B 198     7191  10171  15925    604  -2848   1313  B    C  
ATOM   1447  O   MET B 198     -60.828  24.833   8.945  1.00 84.89      B    O  
ANISOU 1447  O   MET B 198     6840   9615  15799    764  -2808   1258  B    O  
ATOM   1448  CB  MET B 198     -60.974  21.637   8.368  1.00 75.25      B    C  
ANISOU 1448  CB  MET B 198     5648   8866  14077    303  -2605    983  B    C  
ATOM   1449  CG  MET B 198     -61.784  20.386   8.668  1.00 83.04      B    C  
ANISOU 1449  CG  MET B 198     6536  10044  14972    177  -2529    798  B    C  
ATOM   1450  SD  MET B 198     -62.977  20.679   9.987  1.00102.93      B    S  
ANISOU 1450  SD  MET B 198     8812  12567  17729    350  -2496    666  B    S  
ATOM   1451  CE  MET B 198     -61.887  21.293  11.262  1.00 87.26      B    C  
ANISOU 1451  CE  MET B 198     6976  10271  15907    485  -2345    593  B    C  
ATOM   1452  N   GLN B 199     -60.213  24.301   6.848  1.00 90.89      B    N  
ANISOU 1452  N   GLN B 199     7734  10602  16197    512  -2921   1504  B    N  
ATOM   1453  CA  GLN B 199     -59.339  25.462   6.703  1.00 80.88      B    C  
ANISOU 1453  CA  GLN B 199     6591   9096  15044    585  -2968   1686  B    C  
ATOM   1454  C   GLN B 199     -60.154  26.727   6.847  1.00 83.30      B    C  
ANISOU 1454  C   GLN B 199     6783   9273  15593    817  -3126   1804  B    C  
ATOM   1455  O   GLN B 199     -59.689  27.729   7.402  1.00 77.52      B    O  
ANISOU 1455  O   GLN B 199     6127   8261  15068    937  -3126   1844  B    O  
ATOM   1456  CB  GLN B 199     -58.665  25.471   5.334  1.00 72.15      B    C  
ANISOU 1456  CB  GLN B 199     5609   8086  13721    446  -3032   1903  B    C  
ATOM   1457  CG  GLN B 199     -57.657  24.368   5.135  1.00 70.65      B    C  
ANISOU 1457  CG  GLN B 199     5559   7981  13304    245  -2858   1806  B    C  
ATOM   1458  CD  GLN B 199     -56.798  24.593   3.906  1.00 83.32      B    C  
ANISOU 1458  CD  GLN B 199     7299   9637  14719    134  -2890   2031  B    C  
ATOM   1459  NE2 GLN B 199     -56.619  23.540   3.117  1.00 78.25      B    N  
ANISOU 1459  NE2 GLN B 199     6724   9218  13791    -29  -2827   1986  B    N  
ATOM   1460  OE1 GLN B 199     -56.286  25.697   3.673  1.00 81.57      B    O  
ANISOU 1460  OE1 GLN B 199     7133   9254  14606    188  -2962   2242  B    O  
ATOM   1461  N   ALA B 200     -61.381  26.678   6.336  1.00 83.99      B    N  
ANISOU 1461  N   ALA B 200     6688   9566  15658    881  -3267   1860  B    N  
ATOM   1462  CA  ALA B 200     -62.231  27.862   6.309  1.00 72.88      B    C  
ANISOU 1462  CA  ALA B 200     5153   8062  14475   1126  -3434   2005  B    C  
ATOM   1463  C   ALA B 200     -62.818  28.173   7.689  1.00 81.01      B    C  
ANISOU 1463  C   ALA B 200     6068   8950  15762   1330  -3345   1803  B    C  
ATOM   1464  O   ALA B 200     -62.900  29.338   8.084  1.00 94.18      B    O  
ANISOU 1464  O   ALA B 200     7748  10364  17672   1546  -3397   1867  B    O  
ATOM   1465  CB  ALA B 200     -63.313  27.702   5.274  1.00 68.47      B    C  
ANISOU 1465  CB  ALA B 200     4418   7798  13799   1126  -3625   2151  B    C  
ATOM   1466  N   ARG B 201     -63.212  27.134   8.428  1.00101.88      B    N  
ANISOU 1466  N   ARG B 201     8614  11748  18349   1260  -3202   1557  B    N  
ATOM   1467  CA  ARG B 201     -63.807  27.326   9.753  1.00111.23      B    C  
ANISOU 1467  CA  ARG B 201     9681  12843  19739   1441  -3094   1355  B    C  
ATOM   1468  C   ARG B 201     -62.803  27.862  10.782  1.00107.09      B    C  
ANISOU 1468  C   ARG B 201     9350  11991  19346   1494  -2965   1244  B    C  
ATOM   1469  O   ARG B 201     -63.197  28.468  11.779  1.00110.29      B    O  
ANISOU 1469  O   ARG B 201     9707  12245  19954   1695  -2912   1122  B    O  
ATOM   1470  CB  ARG B 201     -64.477  26.039  10.245  1.00 57.62      B    C  
ANISOU 1470  CB  ARG B 201     2740   6315  12836   1324  -2972   1144  B    C  
ATOM   1471  N   ALA B 202     -61.511  27.652  10.517  1.00 86.98      B    N  
ANISOU 1471  N   ALA B 202     7019   9349  16678   1312  -2916   1286  B    N  
ATOM   1472  CA  ALA B 202     -60.425  28.158  11.363  1.00 74.45      B    C  
ANISOU 1472  CA  ALA B 202     5619   7473  15196   1319  -2822   1209  B    C  
ATOM   1473  C   ALA B 202     -59.943  29.509  10.894  1.00 84.39      B    C  
ANISOU 1473  C   ALA B 202     6997   8464  16604   1407  -2958   1422  B    C  
ATOM   1474  O   ALA B 202     -59.754  30.414  11.690  1.00 96.56      B    O  
ANISOU 1474  O   ALA B 202     8613   9726  18349   1543  -2948   1360  B    O  
ATOM   1475  CB  ALA B 202     -59.250  27.190  11.371  1.00 70.85      B    C  
ANISOU 1475  CB  ALA B 202     5307   7070  14544   1078  -2691   1150  B    C  
ATOM   1476  N   LEU B 203     -59.705  29.627   9.594  1.00 92.81      B    N  
ANISOU 1476  N   LEU B 203     8101   9608  17554   1313  -3082   1673  B    N  
ATOM   1477  CA  LEU B 203     -59.345  30.903   8.989  1.00 94.18      B    C  
ANISOU 1477  CA  LEU B 203     8380   9544  17858   1386  -3228   1926  B    C  
ATOM   1478  C   LEU B 203     -60.458  31.956   9.173  1.00 90.08      B    C  
ANISOU 1478  C   LEU B 203     7750   8887  17589   1680  -3354   1978  B    C  
ATOM   1479  O   LEU B 203     -60.234  33.169   9.056  1.00 96.26      B    O  
ANISOU 1479  O   LEU B 203     8639   9375  18562   1796  -3454   2134  B    O  
ATOM   1480  CB  LEU B 203     -59.033  30.705   7.504  1.00 84.36      B    C  
ANISOU 1480  CB  LEU B 203     7174   8478  16399   1228  -3331   2192  B    C  
ATOM   1481  CG  LEU B 203     -57.685  30.044   7.212  1.00 85.14      B    C  
ANISOU 1481  CG  LEU B 203     7427   8626  16296    972  -3211   2201  B    C  
ATOM   1482  CD1 LEU B 203     -57.634  29.539   5.769  1.00 86.41      B    C  
ANISOU 1482  CD1 LEU B 203     7594   9056  16183    822  -3280   2399  B    C  
ATOM   1483  CD2 LEU B 203     -56.551  31.036   7.509  1.00 70.05      B    C  
ANISOU 1483  CD2 LEU B 203     5689   6388  14541    947  -3204   2296  B    C  
ATOM   1484  N   SER B 204     -61.665  31.505   9.468  1.00 71.58      B    N  
ANISOU 1484  N   SER B 204     5189   6748  15261   1805  -3345   1854  B    N  
ATOM   1485  CA  SER B 204     -62.729  32.475   9.641  1.00 83.55      B    C  
ANISOU 1485  CA  SER B 204     6575   8152  17020   2111  -3450   1906  B    C  
ATOM   1486  C   SER B 204     -62.790  32.869  11.107  1.00 86.92      B    C  
ANISOU 1486  C   SER B 204     7031   8344  17652   2277  -3310   1639  B    C  
ATOM   1487  O   SER B 204     -63.363  33.886  11.465  1.00100.90      B    O  
ANISOU 1487  O   SER B 204     8772   9900  19665   2549  -3361   1647  B    O  
ATOM   1488  CB  SER B 204     -64.071  31.914   9.166  1.00 79.49      B    C  
ANISOU 1488  CB  SER B 204     5776   7992  16434   2182  -3529   1935  B    C  
ATOM   1489  OG  SER B 204     -64.660  31.112  10.168  1.00 92.19      B    O  
ANISOU 1489  OG  SER B 204     7232   9757  18037   2199  -3369   1651  B    O  
ATOM   1490  N   ASN B 205     -62.175  32.068  11.960  1.00 91.58      B    N  
ANISOU 1490  N   ASN B 205     7690   8968  18136   2118  -3130   1402  B    N  
ATOM   1491  CA  ASN B 205     -62.203  32.338  13.388  1.00 93.35      B    C  
ANISOU 1491  CA  ASN B 205     7953   9008  18506   2250  -2989   1132  B    C  
ATOM   1492  C   ASN B 205     -61.490  33.633  13.776  1.00 91.75      B    C  
ANISOU 1492  C   ASN B 205     7975   8375  18512   2345  -3030   1154  B    C  
ATOM   1493  O   ASN B 205     -60.340  33.858  13.371  1.00 79.89      B    O  
ANISOU 1493  O   ASN B 205     6666   6726  16965   2161  -3072   1279  B    O  
ATOM   1494  CB  ASN B 205     -61.611  31.157  14.157  1.00 88.32      B    C  
ANISOU 1494  CB  ASN B 205     7358   8516  17685   2039  -2803    907  B    C  
ATOM   1495  CG  ASN B 205     -61.770  31.307  15.651  1.00 90.76      B    C  
ANISOU 1495  CG  ASN B 205     7684   8702  18098   2168  -2652    622  B    C  
ATOM   1496  ND2 ASN B 205     -62.140  30.223  16.310  1.00 61.95      B    N  
ANISOU 1496  ND2 ASN B 205     3923   5295  14320   2102  -2500    434  B    N  
ATOM   1497  OD1 ASN B 205     -61.569  32.392  16.209  1.00100.60      B    O  
ANISOU 1497  OD1 ASN B 205     9057   9634  19534   2322  -2670    570  B    O  
ATOM   1498  N   PRO B 206     -62.182  34.488  14.561  1.00 96.69      B    N  
ANISOU 1498  N   PRO B 206     8575   8796  19367   2630  -3013   1027  B    N  
ATOM   1499  CA  PRO B 206     -61.693  35.818  14.988  1.00 81.74      B    C  
ANISOU 1499  CA  PRO B 206     6901   6452  17704   2757  -3059   1019  B    C  
ATOM   1500  C   PRO B 206     -60.451  35.704  15.871  1.00 92.56      B    C  
ANISOU 1500  C   PRO B 206     8496   7657  19018   2554  -2953    834  B    C  
ATOM   1501  O   PRO B 206     -59.504  36.476  15.736  1.00 89.04      B    O  
ANISOU 1501  O   PRO B 206     8267   6909  18657   2460  -3028    929  B    O  
ATOM   1502  CB  PRO B 206     -62.862  36.383  15.813  1.00 71.25      B    C  
ANISOU 1502  CB  PRO B 206     5455   5039  16580   3110  -3003    840  B    C  
ATOM   1503  CG  PRO B 206     -64.079  35.569  15.421  1.00 76.86      B    C  
ANISOU 1503  CG  PRO B 206     5838   6163  17202   3192  -2994    873  B    C  
ATOM   1504  CD  PRO B 206     -63.542  34.202  15.067  1.00 81.79      B    C  
ANISOU 1504  CD  PRO B 206     6432   7114  17532   2853  -2942    881  B    C  
ATOM   1505  N   LYS B 207     -60.457  34.713  16.757  1.00 96.08      B    N  
ANISOU 1505  N   LYS B 207     8877   8314  19315   2473  -2787    587  B    N  
ATOM   1506  CA  LYS B 207     -59.384  34.537  17.723  1.00 88.27      B    C  
ANISOU 1506  CA  LYS B 207     8070   7209  18259   2304  -2686    395  B    C  
ATOM   1507  C   LYS B 207     -58.255  33.634  17.232  1.00 83.46      B    C  
ANISOU 1507  C   LYS B 207     7513   6763  17433   1980  -2673    500  B    C  
ATOM   1508  O   LYS B 207     -57.353  33.310  17.999  1.00 88.34      B    O  
ANISOU 1508  O   LYS B 207     8246   7347  17970   1826  -2591    358  B    O  
ATOM   1509  CB  LYS B 207     -59.944  33.995  19.037  1.00 80.41      B    C  
ANISOU 1509  CB  LYS B 207     6997   6340  17213   2402  -2506     76  B    C  
ATOM   1510  CG  LYS B 207     -60.694  35.043  19.844  1.00 76.46      B    C  
ANISOU 1510  CG  LYS B 207     6525   5594  16931   2711  -2481    -97  B    C  
ATOM   1511  CD  LYS B 207     -61.577  34.394  20.912  1.00 85.09      B    C  
ANISOU 1511  CD  LYS B 207     7463   6914  17952   2839  -2292   -365  B    C  
ATOM   1512  CE  LYS B 207     -60.759  33.863  22.086  1.00 83.41      B    C  
ANISOU 1512  CE  LYS B 207     7394   6717  17584   2670  -2158   -605  B    C  
ATOM   1513  NZ  LYS B 207     -61.626  33.689  23.294  1.00 79.56      B    N  
ANISOU 1513  NZ  LYS B 207     6816   6335  17077   2857  -1977   -886  B    N  
ATOM   1514  N   ILE B 208     -58.293  33.235  15.964  1.00 77.74      B    N  
ANISOU 1514  N   ILE B 208     6706   6223  16607   1882  -2754    746  B    N  
ATOM   1515  CA  ILE B 208     -57.193  32.447  15.400  1.00 70.10      B    C  
ANISOU 1515  CA  ILE B 208     5798   5397  15441   1597  -2733    856  B    C  
ATOM   1516  C   ILE B 208     -56.391  33.208  14.347  1.00 70.03      B    C  
ANISOU 1516  C   ILE B 208     5911   5221  15475   1490  -2872   1144  B    C  
ATOM   1517  O   ILE B 208     -56.954  33.822  13.443  1.00 77.16      B    O  
ANISOU 1517  O   ILE B 208     6778   6083  16456   1595  -3003   1354  B    O  
ATOM   1518  CB  ILE B 208     -57.669  31.123  14.791  1.00 70.31      B    C  
ANISOU 1518  CB  ILE B 208     5659   5810  15246   1506  -2678    883  B    C  
ATOM   1519  CG1 ILE B 208     -58.220  30.206  15.882  1.00 83.07      B    C  
ANISOU 1519  CG1 ILE B 208     7174   7599  16789   1541  -2517    609  B    C  
ATOM   1520  CG2 ILE B 208     -56.514  30.420  14.077  1.00 54.65      B    C  
ANISOU 1520  CG2 ILE B 208     3754   3943  13068   1242  -2656   1014  B    C  
ATOM   1521  CD1 ILE B 208     -58.760  28.878  15.386  1.00 74.17      B    C  
ANISOU 1521  CD1 ILE B 208     5895   6824  15462   1439  -2458    611  B    C  
ATOM   1522  N   GLN B 209     -55.072  33.156  14.473  1.00 72.40      B    N  
ANISOU 1522  N   GLN B 209     6347   5440  15720   1277  -2842   1167  B    N  
ATOM   1523  CA  GLN B 209     -54.187  33.770  13.500  1.00 79.77      B    C  
ANISOU 1523  CA  GLN B 209     7388   6250  16672   1132  -2946   1447  B    C  
ATOM   1524  C   GLN B 209     -53.226  32.713  13.026  1.00 69.92      B    C  
ANISOU 1524  C   GLN B 209     6126   5253  15186    889  -2860   1512  B    C  
ATOM   1525  O   GLN B 209     -52.566  32.090  13.839  1.00 83.11      B    O  
ANISOU 1525  O   GLN B 209     7816   6976  16785    787  -2746   1342  B    O  
ATOM   1526  CB  GLN B 209     -53.413  34.936  14.128  1.00 75.19      B    C  
ANISOU 1526  CB  GLN B 209     6990   5281  16294   1103  -3002   1427  B    C  
ATOM   1527  CG  GLN B 209     -52.369  35.544  13.206  1.00 97.71      B    C  
ANISOU 1527  CG  GLN B 209     9953   8006  19165    909  -3094   1721  B    C  
ATOM   1528  CD  GLN B 209     -51.753  36.811  13.772  1.00115.13      B    C  
ANISOU 1528  CD  GLN B 209    12344   9794  21604    877  -3175   1713  B    C  
ATOM   1529  NE2 GLN B 209     -50.581  37.187  13.261  1.00115.69      B    N  
ANISOU 1529  NE2 GLN B 209    12507   9772  21677    641  -3220   1921  B    N  
ATOM   1530  OE1 GLN B 209     -52.324  37.443  14.662  1.00115.45      B    O  
ANISOU 1530  OE1 GLN B 209    12450   9598  21819   1057  -3192   1515  B    O  
ATOM   1531  N   VAL B 210     -53.149  32.511  11.716  1.00 61.24      B    N  
ANISOU 1531  N   VAL B 210     4998   4312  13961    805  -2910   1761  B    N  
ATOM   1532  CA  VAL B 210     -52.207  31.554  11.153  1.00 52.67      B    C  
ANISOU 1532  CA  VAL B 210     3909   3456  12647    589  -2816   1834  B    C  
ATOM   1533  C   VAL B 210     -50.832  32.150  10.973  1.00 64.49      B    C  
ANISOU 1533  C   VAL B 210     5521   4795  14186    411  -2830   1993  B    C  
ATOM   1534  O   VAL B 210     -50.689  33.323  10.611  1.00 65.88      B    O  
ANISOU 1534  O   VAL B 210     5783   4730  14520    416  -2955   2179  B    O  
ATOM   1535  CB  VAL B 210     -52.676  30.967   9.819  1.00 66.98      B    C  
ANISOU 1535  CB  VAL B 210     5648   5542  14259    559  -2843   2007  B    C  
ATOM   1536  CG1 VAL B 210     -51.583  30.074   9.223  1.00 64.83      B    C  
ANISOU 1536  CG1 VAL B 210     5401   5475  13757    346  -2730   2080  B    C  
ATOM   1537  CG2 VAL B 210     -53.989  30.181  10.016  1.00 52.22      B    C  
ANISOU 1537  CG2 VAL B 210     3638   3877  12324    690  -2819   1835  B    C  
ATOM   1538  N   VAL B 211     -49.817  31.333  11.239  1.00 61.00      B    N  
ANISOU 1538  N   VAL B 211     5076   4489  13613    251  -2703   1928  B    N  
ATOM   1539  CA  VAL B 211     -48.433  31.744  11.063  1.00 55.58      B    C  
ANISOU 1539  CA  VAL B 211     4457   3715  12947     57  -2699   2082  B    C  
ATOM   1540  C   VAL B 211     -47.744  30.868  10.021  1.00 77.06      B    C  
ANISOU 1540  C   VAL B 211     7131   6721  15427    -87  -2599   2239  B    C  
ATOM   1541  O   VAL B 211     -47.030  29.929  10.366  1.00 90.66      B    O  
ANISOU 1541  O   VAL B 211     8815   8604  17028   -169  -2463   2137  B    O  
ATOM   1542  CB  VAL B 211     -47.678  31.718  12.408  1.00 62.10      B    C  
ANISOU 1542  CB  VAL B 211     5311   4427  13857     -1  -2645   1877  B    C  
ATOM   1543  CG1 VAL B 211     -46.276  32.236  12.247  1.00 52.64      B    C  
ANISOU 1543  CG1 VAL B 211     4158   3137  12705   -213  -2662   2046  B    C  
ATOM   1544  CG2 VAL B 211     -48.415  32.559  13.450  1.00 56.62      B    C  
ANISOU 1544  CG2 VAL B 211     4682   3458  13376    154  -2728   1690  B    C  
ATOM   1545  N   TRP B 212     -47.965  31.182   8.747  1.00 80.68      B    N  
ANISOU 1545  N   TRP B 212     7601   7243  15809   -107  -2665   2489  B    N  
ATOM   1546  CA  TRP B 212     -47.451  30.369   7.640  1.00 84.36      B    C  
ANISOU 1546  CA  TRP B 212     8039   7997  16017   -226  -2567   2632  B    C  
ATOM   1547  C   TRP B 212     -45.935  30.320   7.545  1.00 83.25      B    C  
ANISOU 1547  C   TRP B 212     7904   7890  15837   -415  -2468   2746  B    C  
ATOM   1548  O   TRP B 212     -45.234  31.079   8.208  1.00 82.90      B    O  
ANISOU 1548  O   TRP B 212     7890   7631  15977   -488  -2508   2763  B    O  
ATOM   1549  CB  TRP B 212     -47.967  30.893   6.304  1.00 84.88      B    C  
ANISOU 1549  CB  TRP B 212     8133   8112  16007   -216  -2679   2901  B    C  
ATOM   1550  CG  TRP B 212     -49.425  31.045   6.225  1.00 82.66      B    C  
ANISOU 1550  CG  TRP B 212     7819   7820  15767    -34  -2800   2849  B    C  
ATOM   1551  CD1 TRP B 212     -50.131  32.190   6.408  1.00 80.21      B    C  
ANISOU 1551  CD1 TRP B 212     7539   7254  15683    101  -2962   2919  B    C  
ATOM   1552  CD2 TRP B 212     -50.378  30.026   5.918  1.00 83.70      B    C  
ANISOU 1552  CD2 TRP B 212     7874   8212  15717     38  -2771   2722  B    C  
ATOM   1553  CE2 TRP B 212     -51.653  30.630   5.935  1.00 82.45      B    C  
ANISOU 1553  CE2 TRP B 212     7673   7966  15687    214  -2927   2732  B    C  
ATOM   1554  CE3 TRP B 212     -50.280  28.665   5.624  1.00 87.72      B    C  
ANISOU 1554  CE3 TRP B 212     8349   9009  15972    -34  -2632   2601  B    C  
ATOM   1555  NE1 TRP B 212     -51.473  31.949   6.245  1.00 78.49      B    N  
ANISOU 1555  NE1 TRP B 212     7240   7143  15437    268  -3035   2851  B    N  
ATOM   1556  CZ2 TRP B 212     -52.822  29.920   5.674  1.00 86.19      B    C  
ANISOU 1556  CZ2 TRP B 212     8047   8659  16042    302  -2955   2633  B    C  
ATOM   1557  CZ3 TRP B 212     -51.444  27.954   5.368  1.00 89.93      B    C  
ANISOU 1557  CZ3 TRP B 212     8560   9478  16133     41  -2661   2489  B    C  
ATOM   1558  CH2 TRP B 212     -52.694  28.583   5.397  1.00101.88      B    C  
ANISOU 1558  CH2 TRP B 212    10008  10926  17777    197  -2825   2510  B    C  
ATOM   1559  N   ASP B 213     -45.447  29.424   6.688  1.00 75.86      B    N  
ANISOU 1559  N   ASP B 213     6937   7232  14656   -497  -2337   2821  B    N  
ATOM   1560  CA  ASP B 213     -44.038  29.375   6.305  1.00 66.75      B    C  
ANISOU 1560  CA  ASP B 213     5763   6166  13435   -668  -2228   2983  B    C  
ATOM   1561  C   ASP B 213     -43.088  29.436   7.517  1.00 72.27      B    C  
ANISOU 1561  C   ASP B 213     6421   6748  14290   -732  -2185   2864  B    C  
ATOM   1562  O   ASP B 213     -41.969  29.943   7.407  1.00 87.16      B    O  
ANISOU 1562  O   ASP B 213     8284   8598  16235   -887  -2170   3034  B    O  
ATOM   1563  CB  ASP B 213     -43.730  30.525   5.323  1.00 63.68      B    C  
ANISOU 1563  CB  ASP B 213     5425   5686  13083   -775  -2328   3322  B    C  
ATOM   1564  CG  ASP B 213     -44.377  30.337   3.938  1.00 87.66      B    C  
ANISOU 1564  CG  ASP B 213     8496   8920  15893   -750  -2348   3489  B    C  
ATOM   1565  OD1 ASP B 213     -44.448  29.197   3.434  1.00 92.47      B    O  
ANISOU 1565  OD1 ASP B 213     9079   9807  16249   -738  -2218   3403  B    O  
ATOM   1566  OD2 ASP B 213     -44.795  31.348   3.335  1.00 98.80      B    O  
ANISOU 1566  OD2 ASP B 213     9967  10201  17372   -748  -2499   3714  B    O  
ATOM   1567  N   SER B 214     -43.527  28.930   8.668  1.00 59.44      B    N  
ANISOU 1567  N   SER B 214     4780   5078  12727   -626  -2170   2584  B    N  
ATOM   1568  CA  SER B 214     -42.753  29.080   9.913  1.00 72.02      B    C  
ANISOU 1568  CA  SER B 214     6347   6551  14466   -678  -2165   2460  B    C  
ATOM   1569  C   SER B 214     -42.477  27.770  10.638  1.00 71.73      B    C  
ANISOU 1569  C   SER B 214     6245   6691  14318   -632  -2015   2248  B    C  
ATOM   1570  O   SER B 214     -43.181  26.780  10.442  1.00 66.30      B    O  
ANISOU 1570  O   SER B 214     5553   6156  13481   -529  -1932   2127  B    O  
ATOM   1571  CB  SER B 214     -43.473  30.005  10.895  1.00 79.08      B    C  
ANISOU 1571  CB  SER B 214     7312   7149  15585   -596  -2318   2322  B    C  
ATOM   1572  OG  SER B 214     -43.671  31.289  10.347  1.00 89.45      B    O  
ANISOU 1572  OG  SER B 214     8704   8243  17041   -629  -2464   2518  B    O  
ATOM   1573  N   GLU B 215     -41.451  27.791  11.487  1.00 70.08      B    N  
ANISOU 1573  N   GLU B 215     5985   6455  14186   -716  -1993   2211  B    N  
ATOM   1574  CA  GLU B 215     -41.133  26.678  12.379  1.00 60.95      B    C  
ANISOU 1574  CA  GLU B 215     4771   5428  12960   -666  -1877   2020  B    C  
ATOM   1575  C   GLU B 215     -40.837  27.233  13.742  1.00 65.68      B    C  
ANISOU 1575  C   GLU B 215     5379   5853  13722   -697  -1975   1891  B    C  
ATOM   1576  O   GLU B 215     -40.290  28.330  13.864  1.00 75.31      B    O  
ANISOU 1576  O   GLU B 215     6615   6907  15092   -822  -2093   1996  B    O  
ATOM   1577  CB  GLU B 215     -39.888  25.927  11.914  1.00 71.70      B    C  
ANISOU 1577  CB  GLU B 215     6030   7015  14198   -744  -1722   2145  B    C  
ATOM   1578  CG  GLU B 215     -40.079  25.176  10.623  1.00 99.74      B    C  
ANISOU 1578  CG  GLU B 215     9585  10768  17544   -709  -1590   2234  B    C  
ATOM   1579  CD  GLU B 215     -38.911  24.277  10.297  1.00110.80      B    C  
ANISOU 1579  CD  GLU B 215    10889  12393  18818   -739  -1404   2307  B    C  
ATOM   1580  OE1 GLU B 215     -37.767  24.616  10.698  1.00101.11      B    O  
ANISOU 1580  OE1 GLU B 215     9557  11175  17684   -839  -1404   2405  B    O  
ATOM   1581  OE2 GLU B 215     -39.148  23.237   9.634  1.00114.67      B    O  
ANISOU 1581  OE2 GLU B 215    11401  13050  19118   -660  -1257   2263  B    O  
ATOM   1582  N   VAL B 216     -41.179  26.479  14.772  1.00 51.61      B    N  
ANISOU 1582  N   VAL B 216     3596   4109  11905   -597  -1930   1664  B    N  
ATOM   1583  CA  VAL B 216     -40.774  26.864  16.108  1.00 57.46      B    C  
ANISOU 1583  CA  VAL B 216     4344   4733  12756   -636  -2009   1533  B    C  
ATOM   1584  C   VAL B 216     -39.368  26.325  16.317  1.00 66.83      B    C  
ANISOU 1584  C   VAL B 216     5412   6086  13894   -739  -1938   1619  B    C  
ATOM   1585  O   VAL B 216     -39.115  25.144  16.089  1.00 73.00      B    O  
ANISOU 1585  O   VAL B 216     6127   7076  14533   -678  -1786   1622  B    O  
ATOM   1586  CB  VAL B 216     -41.713  26.279  17.151  1.00 60.73      B    C  
ANISOU 1586  CB  VAL B 216     4803   5138  13133   -488  -1984   1270  B    C  
ATOM   1587  CG1 VAL B 216     -41.158  26.511  18.543  1.00 57.24      B    C  
ANISOU 1587  CG1 VAL B 216     4368   4628  12753   -536  -2049   1136  B    C  
ATOM   1588  CG2 VAL B 216     -43.107  26.891  17.006  1.00 54.21      B    C  
ANISOU 1588  CG2 VAL B 216     4063   4157  12377   -373  -2057   1187  B    C  
ATOM   1589  N   VAL B 217     -38.442  27.179  16.733  1.00 65.30      B    N  
ANISOU 1589  N   VAL B 217     5187   5800  13825   -898  -2047   1693  B    N  
ATOM   1590  CA  VAL B 217     -37.058  26.736  16.930  1.00 53.96      B    C  
ANISOU 1590  CA  VAL B 217     3600   4544  12359  -1005  -1995   1798  B    C  
ATOM   1591  C   VAL B 217     -36.628  26.748  18.395  1.00 64.45      B    C  
ANISOU 1591  C   VAL B 217     4913   5846  13729  -1040  -2083   1643  B    C  
ATOM   1592  O   VAL B 217     -35.560  26.252  18.739  1.00 64.96      B    O  
ANISOU 1592  O   VAL B 217     4839   6083  13760  -1099  -2049   1706  B    O  
ATOM   1593  CB  VAL B 217     -36.078  27.550  16.083  1.00 57.28      B    C  
ANISOU 1593  CB  VAL B 217     3942   4964  12860  -1200  -2034   2064  B    C  
ATOM   1594  CG1 VAL B 217     -36.404  27.364  14.619  1.00 64.04      B    C  
ANISOU 1594  CG1 VAL B 217     4806   5904  13621  -1160  -1924   2229  B    C  
ATOM   1595  CG2 VAL B 217     -36.134  29.026  16.459  1.00 49.66      B    C  
ANISOU 1595  CG2 VAL B 217     3076   3707  12087  -1346  -2239   2066  B    C  
ATOM   1596  N   GLU B 218     -37.478  27.285  19.264  1.00 65.38      B    N  
ANISOU 1596  N   GLU B 218     5168   5765  13908   -992  -2192   1437  B    N  
ATOM   1597  CA  GLU B 218     -37.174  27.299  20.687  1.00 55.93      B    C  
ANISOU 1597  CA  GLU B 218     3983   4549  12717  -1022  -2278   1265  B    C  
ATOM   1598  C   GLU B 218     -38.421  27.607  21.478  1.00 64.68      B    C  
ANISOU 1598  C   GLU B 218     5256   5479  13841   -898  -2327   1013  B    C  
ATOM   1599  O   GLU B 218     -39.244  28.409  21.058  1.00 75.90      B    O  
ANISOU 1599  O   GLU B 218     6783   6700  15357   -861  -2379    992  B    O  
ATOM   1600  CB  GLU B 218     -36.112  28.362  20.976  1.00 71.52      B    C  
ANISOU 1600  CB  GLU B 218     5922   6426  14826  -1259  -2442   1355  B    C  
ATOM   1601  CG  GLU B 218     -35.762  28.559  22.445  1.00 85.11      B    C  
ANISOU 1601  CG  GLU B 218     7674   8115  16549  -1328  -2569   1173  B    C  
ATOM   1602  CD  GLU B 218     -34.701  29.648  22.662  1.00 96.90      B    C  
ANISOU 1602  CD  GLU B 218     9133   9504  18179  -1600  -2750   1262  B    C  
ATOM   1603  OE1 GLU B 218     -33.786  29.817  21.803  1.00 78.03      B    O  
ANISOU 1603  OE1 GLU B 218     6599   7201  15845  -1749  -2737   1516  B    O  
ATOM   1604  OE2 GLU B 218     -34.781  30.328  23.709  1.00103.04      B    O  
ANISOU 1604  OE2 GLU B 218    10031  10118  19001  -1675  -2901   1074  B    O  
ATOM   1605  N   ALA B 219     -38.567  26.970  22.630  1.00 69.77      B    N  
ANISOU 1605  N   ALA B 219     5915   6205  14389   -823  -2306    830  B    N  
ATOM   1606  CA  ALA B 219     -39.563  27.404  23.605  1.00 66.39      B    C  
ANISOU 1606  CA  ALA B 219     5636   5615  13975   -734  -2363    577  B    C  
ATOM   1607  C   ALA B 219     -38.827  27.825  24.871  1.00 74.44      B    C  
ANISOU 1607  C   ALA B 219     6683   6606  14995   -858  -2496    462  B    C  
ATOM   1608  O   ALA B 219     -37.889  27.156  25.293  1.00 81.62      B    O  
ANISOU 1608  O   ALA B 219     7482   7713  15817   -922  -2488    522  B    O  
ATOM   1609  CB  ALA B 219     -40.546  26.296  23.905  1.00 42.44      B    C  
ANISOU 1609  CB  ALA B 219     2615   2708  10802   -541  -2215    445  B    C  
ATOM   1610  N   TYR B 220     -39.240  28.943  25.459  1.00 69.02      B    N  
ANISOU 1610  N   TYR B 220     6149   5671  14404   -891  -2623    297  B    N  
ATOM   1611  CA  TYR B 220     -38.603  29.471  26.672  1.00 70.63      B    C  
ANISOU 1611  CA  TYR B 220     6414   5821  14599  -1029  -2771    156  B    C  
ATOM   1612  C   TYR B 220     -39.638  29.805  27.753  1.00 85.75      B    C  
ANISOU 1612  C   TYR B 220     8509   7599  16472   -902  -2783   -151  B    C  
ATOM   1613  O   TYR B 220     -40.829  30.006  27.456  1.00 80.61      B    O  
ANISOU 1613  O   TYR B 220     7940   6822  15867   -730  -2711   -238  B    O  
ATOM   1614  CB  TYR B 220     -37.758  30.716  26.351  1.00 62.13      B    C  
ANISOU 1614  CB  TYR B 220     5361   4546  13698  -1266  -2945    261  B    C  
ATOM   1615  CG  TYR B 220     -38.525  31.838  25.656  1.00 71.34      B    C  
ANISOU 1615  CG  TYR B 220     6670   5391  15045  -1235  -2988    260  B    C  
ATOM   1616  CD1 TYR B 220     -39.332  32.718  26.382  1.00 82.70      B    C  
ANISOU 1616  CD1 TYR B 220     8317   6555  16550  -1166  -3061      8  B    C  
ATOM   1617  CD2 TYR B 220     -38.445  32.014  24.274  1.00 73.43      B    C  
ANISOU 1617  CD2 TYR B 220     6865   5629  15407  -1260  -2950    516  B    C  
ATOM   1618  CE1 TYR B 220     -40.049  33.745  25.748  1.00 76.83      B    C  
ANISOU 1618  CE1 TYR B 220     7703   5501  15988  -1107  -3100     20  B    C  
ATOM   1619  CE2 TYR B 220     -39.162  33.019  23.633  1.00 87.62      B    C  
ANISOU 1619  CE2 TYR B 220     8792   7135  17365  -1217  -2998    542  B    C  
ATOM   1620  CZ  TYR B 220     -39.959  33.887  24.375  1.00 86.25      B    C  
ANISOU 1620  CZ  TYR B 220     8819   6675  17278  -1134  -3076    297  B    C  
ATOM   1621  OH  TYR B 220     -40.650  34.898  23.737  1.00 75.31      B    O  
ANISOU 1621  OH  TYR B 220     7561   4985  16069  -1070  -3126    338  B    O  
ATOM   1622  N   GLY B 221     -39.182  29.868  29.002  1.00 81.64      B    N  
ANISOU 1622  N   GLY B 221     8041   7120  15855   -985  -2873   -311  B    N  
ATOM   1623  CA  GLY B 221     -40.069  30.135  30.122  1.00 86.99      B    C  
ANISOU 1623  CA  GLY B 221     8894   7704  16456   -871  -2870   -614  B    C  
ATOM   1624  C   GLY B 221     -39.799  31.487  30.741  1.00107.95      B    C  
ANISOU 1624  C   GLY B 221    11723  10086  19206  -1017  -3056   -782  B    C  
ATOM   1625  O   GLY B 221     -39.061  32.291  30.175  1.00122.39      B    O  
ANISOU 1625  O   GLY B 221    13546  11760  21196  -1205  -3186   -650  B    O  
ATOM   1626  N   GLY B 222     -40.391  31.743  31.904  1.00110.88      B    N  
ANISOU 1626  N   GLY B 222    12259  10393  19477   -940  -3064  -1076  B    N  
ATOM   1627  CA  GLY B 222     -40.195  33.011  32.588  1.00109.43      B    C  
ANISOU 1627  CA  GLY B 222    12281   9932  19365  -1070  -3233  -1285  B    C  
ATOM   1628  C   GLY B 222     -39.491  32.843  33.920  1.00117.17      B    C  
ANISOU 1628  C   GLY B 222    13310  11065  20143  -1212  -3342  -1445  B    C  
ATOM   1629  O   GLY B 222     -38.974  31.764  34.225  1.00117.76      B    O  
ANISOU 1629  O   GLY B 222    13232  11466  20045  -1231  -3306  -1338  B    O  
ATOM   1630  N   ALA B 223     -39.472  33.915  34.709  1.00116.75      B    N  
ANISOU 1630  N   ALA B 223    13480  10770  20109  -1309  -3480  -1701  B    N  
ATOM   1631  CA  ALA B 223     -38.878  33.900  36.049  1.00105.33      B    C  
ANISOU 1631  CA  ALA B 223    12121   9449  18450  -1456  -3606  -1895  B    C  
ATOM   1632  C   ALA B 223     -37.370  33.539  35.989  1.00113.71      B    C  
ANISOU 1632  C   ALA B 223    12987  10738  19477  -1735  -3767  -1660  B    C  
ATOM   1633  O   ALA B 223     -36.694  34.019  35.074  1.00121.36      B    O  
ANISOU 1633  O   ALA B 223    13866  11593  20653  -1903  -3857  -1449  B    O  
ATOM   1634  CB  ALA B 223     -39.700  33.008  36.983  1.00 90.96      B    C  
ANISOU 1634  CB  ALA B 223    10333   7861  16365  -1235  -3442  -2071  B    C  
ATOM   1635  N   GLY B 224     -36.806  32.749  36.911  1.00108.29      B    N  
ANISOU 1635  N   GLY B 224    12226  10373  18546  -1793  -3811  -1673  B    N  
ATOM   1636  CA  GLY B 224     -37.472  32.126  38.037  1.00105.84      B    C  
ANISOU 1636  CA  GLY B 224    12014  10236  17963  -1627  -3714  -1889  B    C  
ATOM   1637  C   GLY B 224     -37.875  30.715  37.670  1.00118.07      B    C  
ANISOU 1637  C   GLY B 224    13375  12066  19420  -1410  -3497  -1698  B    C  
ATOM   1638  O   GLY B 224     -38.661  30.082  38.372  1.00118.76      B    O  
ANISOU 1638  O   GLY B 224    13525  12285  19312  -1230  -3356  -1833  B    O  
ATOM   1639  N   GLY B 225     -37.341  30.227  36.553  1.00120.04      B    N  
ANISOU 1639  N   GLY B 225    13401  12398  19809  -1433  -3461  -1383  B    N  
ATOM   1640  CA  GLY B 225     -37.650  28.889  36.088  1.00115.98      B    C  
ANISOU 1640  CA  GLY B 225    12720  12118  19228  -1244  -3259  -1193  B    C  
ATOM   1641  C   GLY B 225     -39.143  28.632  36.057  1.00114.61      B    C  
ANISOU 1641  C   GLY B 225    12649  11872  19025   -982  -3047  -1340  B    C  
ATOM   1642  O   GLY B 225     -39.620  27.617  36.560  1.00115.93      B    O  
ANISOU 1642  O   GLY B 225    12793  12245  19008   -839  -2906  -1358  B    O  
ATOM   1643  N   GLY B 226     -39.884  29.561  35.468  1.00107.01      B    N  
ANISOU 1643  N   GLY B 226    11791  10616  18249   -922  -3024  -1435  B    N  
ATOM   1644  CA  GLY B 226     -41.323  29.413  35.356  1.00104.83      B    C  
ANISOU 1644  CA  GLY B 226    11582  10272  17975   -673  -2832  -1562  B    C  
ATOM   1645  C   GLY B 226     -41.736  28.533  34.193  1.00 98.38      B    C  
ANISOU 1645  C   GLY B 226    10594   9553  17233   -544  -2668  -1331  B    C  
ATOM   1646  O   GLY B 226     -40.893  27.951  33.514  1.00100.27      B    O  
ANISOU 1646  O   GLY B 226    10672   9925  17501   -630  -2683  -1079  B    O  
ATOM   1647  N   PRO B 227     -43.049  28.432  33.955  1.00 90.51      B    N  
ANISOU 1647  N   PRO B 227     9628   8498  16262   -335  -2509  -1422  B    N  
ATOM   1648  CA  PRO B 227     -43.640  27.658  32.862  1.00 84.77      B    C  
ANISOU 1648  CA  PRO B 227     8761   7850  15597   -211  -2356  -1243  B    C  
ATOM   1649  C   PRO B 227     -43.464  28.347  31.512  1.00 91.43      B    C  
ANISOU 1649  C   PRO B 227     9559   8506  16674   -257  -2421  -1072  B    C  
ATOM   1650  O   PRO B 227     -42.949  29.462  31.460  1.00 98.84      B    O  
ANISOU 1650  O   PRO B 227    10582   9230  17743   -379  -2576  -1094  B    O  
ATOM   1651  CB  PRO B 227     -45.129  27.628  33.223  1.00 76.20      B    C  
ANISOU 1651  CB  PRO B 227     7739   6740  14474      2  -2204  -1440  B    C  
ATOM   1652  CG  PRO B 227     -45.219  28.107  34.632  1.00 80.42      B    C  
ANISOU 1652  CG  PRO B 227     8435   7249  14873      0  -2243  -1712  B    C  
ATOM   1653  CD  PRO B 227     -44.084  29.035  34.806  1.00 86.43      B    C  
ANISOU 1653  CD  PRO B 227     9279   7860  15699   -201  -2459  -1722  B    C  
ATOM   1654  N   LEU B 228     -43.896  27.684  30.441  1.00 79.26      B    N  
ANISOU 1654  N   LEU B 228     7897   7041  15176   -171  -2304   -901  B    N  
ATOM   1655  CA  LEU B 228     -43.786  28.230  29.095  1.00 77.29      B    C  
ANISOU 1655  CA  LEU B 228     7600   6652  15114   -205  -2350   -715  B    C  
ATOM   1656  C   LEU B 228     -44.200  29.705  29.047  1.00 83.43      B    C  
ANISOU 1656  C   LEU B 228     8519   7108  16074   -190  -2461   -829  B    C  
ATOM   1657  O   LEU B 228     -45.263  30.067  29.545  1.00 75.02      B    O  
ANISOU 1657  O   LEU B 228     7544   5942  15018    -29  -2411  -1033  B    O  
ATOM   1658  CB  LEU B 228     -44.661  27.427  28.138  1.00 68.45      B    C  
ANISOU 1658  CB  LEU B 228     6379   5639  13989    -65  -2199   -609  B    C  
ATOM   1659  CG  LEU B 228     -44.576  27.854  26.674  1.00 57.05      B    C  
ANISOU 1659  CG  LEU B 228     4881   4098  12699    -95  -2236   -395  B    C  
ATOM   1660  CD1 LEU B 228     -43.156  27.614  26.166  1.00 48.04      B    C  
ANISOU 1660  CD1 LEU B 228     3653   3049  11553   -278  -2288   -176  B    C  
ATOM   1661  CD2 LEU B 228     -45.606  27.104  25.818  1.00 52.43      B    C  
ANISOU 1661  CD2 LEU B 228     4214   3622  12085     45  -2102   -332  B    C  
ATOM   1662  N   ALA B 229     -43.360  30.543  28.439  1.00 72.28      B    N  
ANISOU 1662  N   ALA B 229     7122   5530  14809   -353  -2602   -688  B    N  
ATOM   1663  CA  ALA B 229     -43.647  31.963  28.331  1.00 77.70      B    C  
ANISOU 1663  CA  ALA B 229     7961   5872  15690   -355  -2717   -767  B    C  
ATOM   1664  C   ALA B 229     -43.662  32.445  26.881  1.00 85.84      B    C  
ANISOU 1664  C   ALA B 229     8944   6771  16898   -375  -2749   -517  B    C  
ATOM   1665  O   ALA B 229     -44.358  33.406  26.545  1.00 89.30      B    O  
ANISOU 1665  O   ALA B 229     9488   6943  17501   -279  -2792   -552  B    O  
ATOM   1666  CB  ALA B 229     -42.641  32.767  29.158  1.00 69.06      B    C  
ANISOU 1666  CB  ALA B 229     6985   4637  14617   -570  -2889   -869  B    C  
ATOM   1667  N   GLY B 230     -42.894  31.785  26.022  1.00 80.13      B    N  
ANISOU 1667  N   GLY B 230     8068   6238  16139   -487  -2723   -261  B    N  
ATOM   1668  CA  GLY B 230     -42.828  32.178  24.628  1.00 85.16      B    C  
ANISOU 1668  CA  GLY B 230     8660   6791  16906   -522  -2747     -5  B    C  
ATOM   1669  C   GLY B 230     -42.158  31.161  23.734  1.00 78.80      B    C  
ANISOU 1669  C   GLY B 230     7676   6264  16002   -593  -2659    241  B    C  
ATOM   1670  O   GLY B 230     -41.642  30.160  24.209  1.00 84.14      B    O  
ANISOU 1670  O   GLY B 230     8259   7182  16527   -620  -2589    224  B    O  
ATOM   1671  N   VAL B 231     -42.183  31.417  22.431  1.00 69.16      B    N  
ANISOU 1671  N   VAL B 231     6414   5006  14859   -612  -2659    470  B    N  
ATOM   1672  CA  VAL B 231     -41.508  30.575  21.457  1.00 58.74      B    C  
ANISOU 1672  CA  VAL B 231     4941   3932  13446   -683  -2570    708  B    C  
ATOM   1673  C   VAL B 231     -40.789  31.457  20.449  1.00 73.48      B    C  
ANISOU 1673  C   VAL B 231     6801   5676  15441   -853  -2658    964  B    C  
ATOM   1674  O   VAL B 231     -41.300  32.503  20.061  1.00 74.23      B    O  
ANISOU 1674  O   VAL B 231     7006   5512  15685   -836  -2748    999  B    O  
ATOM   1675  CB  VAL B 231     -42.495  29.632  20.688  1.00 59.67      B    C  
ANISOU 1675  CB  VAL B 231     4999   4218  13454   -502  -2426    737  B    C  
ATOM   1676  CG1 VAL B 231     -43.174  28.604  21.628  1.00 47.11      B    C  
ANISOU 1676  CG1 VAL B 231     3398   2779  11724   -355  -2316    513  B    C  
ATOM   1677  CG2 VAL B 231     -43.526  30.427  19.934  1.00 46.77      B    C  
ANISOU 1677  CG2 VAL B 231     3437   2399  11935   -396  -2476    782  B    C  
ATOM   1678  N   LYS B 232     -39.597  31.048  20.035  1.00 79.50      B    N  
ANISOU 1678  N   LYS B 232     7430   6622  16152  -1015  -2627   1154  B    N  
ATOM   1679  CA  LYS B 232     -38.943  31.683  18.894  1.00 69.13      B    C  
ANISOU 1679  CA  LYS B 232     6080   5261  14925  -1173  -2665   1437  B    C  
ATOM   1680  C   LYS B 232     -39.386  30.977  17.615  1.00 68.80      B    C  
ANISOU 1680  C   LYS B 232     5971   5399  14770  -1065  -2528   1598  B    C  
ATOM   1681  O   LYS B 232     -39.234  29.770  17.470  1.00 83.60      B    O  
ANISOU 1681  O   LYS B 232     7739   7543  16481   -998  -2385   1597  B    O  
ATOM   1682  CB  LYS B 232     -37.421  31.646  19.028  1.00 75.82      B    C  
ANISOU 1682  CB  LYS B 232     6794   6238  15775  -1406  -2690   1576  B    C  
ATOM   1683  CG  LYS B 232     -36.844  32.697  19.953  1.00 78.18      B    C  
ANISOU 1683  CG  LYS B 232     7173   6312  16220  -1597  -2874   1493  B    C  
ATOM   1684  CD  LYS B 232     -35.429  32.363  20.331  1.00 89.38      B    C  
ANISOU 1684  CD  LYS B 232     8417   7938  17603  -1797  -2892   1583  B    C  
ATOM   1685  CE  LYS B 232     -34.686  33.540  20.956  1.00107.81      B    C  
ANISOU 1685  CE  LYS B 232    10812  10053  20097  -2062  -3095   1567  B    C  
ATOM   1686  NZ  LYS B 232     -33.332  33.135  21.472  1.00105.12      B    N  
ANISOU 1686  NZ  LYS B 232    10272   9958  19710  -2252  -3129   1636  B    N  
ATOM   1687  N   VAL B 233     -39.966  31.743  16.704  1.00 69.39      B    N  
ANISOU 1687  N   VAL B 233     6124   5314  14928  -1044  -2580   1731  B    N  
ATOM   1688  CA  VAL B 233     -40.444  31.223  15.435  1.00 61.77      B    C  
ANISOU 1688  CA  VAL B 233     5117   4508  13846   -958  -2481   1888  B    C  
ATOM   1689  C   VAL B 233     -39.539  31.683  14.314  1.00 75.66      B    C  
ANISOU 1689  C   VAL B 233     6824   6301  15620  -1141  -2484   2203  B    C  
ATOM   1690  O   VAL B 233     -39.186  32.859  14.233  1.00 94.35      B    O  
ANISOU 1690  O   VAL B 233     9259   8435  18154  -1283  -2613   2325  B    O  
ATOM   1691  CB  VAL B 233     -41.842  31.745  15.118  1.00 56.90      B    C  
ANISOU 1691  CB  VAL B 233     4610   3716  13293   -787  -2545   1841  B    C  
ATOM   1692  CG1 VAL B 233     -42.374  31.065  13.869  1.00 60.01      B    C  
ANISOU 1692  CG1 VAL B 233     4953   4319  13530   -705  -2451   1978  B    C  
ATOM   1693  CG2 VAL B 233     -42.761  31.530  16.300  1.00 59.20      B    C  
ANISOU 1693  CG2 VAL B 233     4954   3937  13603   -616  -2549   1531  B    C  
ATOM   1694  N   LYS B 234     -39.158  30.757  13.448  1.00 75.40      B    N  
ANISOU 1694  N   LYS B 234     6682   6556  15410  -1142  -2334   2335  B    N  
ATOM   1695  CA  LYS B 234     -38.333  31.111  12.307  1.00 76.91      B    C  
ANISOU 1695  CA  LYS B 234     6815   6826  15581  -1305  -2305   2643  B    C  
ATOM   1696  C   LYS B 234     -39.144  31.054  11.019  1.00 81.90      B    C  
ANISOU 1696  C   LYS B 234     7499   7520  16102  -1214  -2270   2783  B    C  
ATOM   1697  O   LYS B 234     -39.748  30.020  10.689  1.00 79.76      B    O  
ANISOU 1697  O   LYS B 234     7208   7443  15653  -1069  -2158   2690  B    O  
ATOM   1698  CB  LYS B 234     -37.119  30.191  12.195  1.00 68.61      B    C  
ANISOU 1698  CB  LYS B 234     5591   6075  14403  -1388  -2150   2718  B    C  
ATOM   1699  CG  LYS B 234     -36.275  30.479  10.972  1.00 81.69      B    C  
ANISOU 1699  CG  LYS B 234     7169   7858  16013  -1546  -2085   3038  B    C  
ATOM   1700  CD  LYS B 234     -35.338  29.327  10.671  1.00 94.24      B    C  
ANISOU 1700  CD  LYS B 234     8585   9788  17433  -1543  -1880   3089  B    C  
ATOM   1701  CE  LYS B 234     -34.298  29.713   9.634  1.00 94.70      B    C  
ANISOU 1701  CE  LYS B 234     8535   9983  17463  -1729  -1808   3410  B    C  
ATOM   1702  NZ  LYS B 234     -33.705  28.506   9.031  1.00 93.10      B    N  
ANISOU 1702  NZ  LYS B 234     8198  10123  17051  -1655  -1572   3453  B    N  
ATOM   1703  N   ASN B 235     -39.161  32.169  10.296  1.00 89.61      B    N  
ANISOU 1703  N   ASN B 235     8546   8323  17179  -1312  -2376   3011  B    N  
ATOM   1704  CA  ASN B 235     -39.743  32.176   8.971  1.00 82.43      B    C  
ANISOU 1704  CA  ASN B 235     7674   7503  16142  -1261  -2353   3200  B    C  
ATOM   1705  C   ASN B 235     -38.822  31.422   8.020  1.00 86.56      B    C  
ANISOU 1705  C   ASN B 235     8081   8353  16453  -1358  -2175   3381  B    C  
ATOM   1706  O   ASN B 235     -37.615  31.610   8.043  1.00 91.21      B    O  
ANISOU 1706  O   ASN B 235     8577   8998  17080  -1536  -2130   3516  B    O  
ATOM   1707  CB  ASN B 235     -39.976  33.593   8.503  1.00 82.05      B    C  
ANISOU 1707  CB  ASN B 235     7743   7169  16264  -1335  -2519   3416  B    C  
ATOM   1708  CG  ASN B 235     -40.767  33.647   7.236  1.00 92.71      B    C  
ANISOU 1708  CG  ASN B 235     9145   8597  17483  -1252  -2530   3600  B    C  
ATOM   1709  ND2 ASN B 235     -42.045  33.997   7.354  1.00 90.57      B    N  
ANISOU 1709  ND2 ASN B 235     8964   8160  17288  -1068  -2649   3507  B    N  
ATOM   1710  OD1 ASN B 235     -40.246  33.373   6.155  1.00101.61      B    O  
ANISOU 1710  OD1 ASN B 235    10224   9950  18433  -1347  -2432   3825  B    O  
ATOM   1711  N   LEU B 236     -39.382  30.540   7.207  1.00 87.65      B    N  
ANISOU 1711  N   LEU B 236     8220   8720  16364  -1242  -2067   3369  B    N  
ATOM   1712  CA  LEU B 236     -38.547  29.694   6.377  1.00 92.01      B    C  
ANISOU 1712  CA  LEU B 236     8675   9589  16694  -1300  -1871   3487  B    C  
ATOM   1713  C   LEU B 236     -38.307  30.300   5.008  1.00107.40      B    C  
ANISOU 1713  C   LEU B 236    10652  11608  18546  -1417  -1865   3816  B    C  
ATOM   1714  O   LEU B 236     -37.513  29.773   4.228  1.00109.42      B    O  
ANISOU 1714  O   LEU B 236    10830  12126  18618  -1486  -1693   3952  B    O  
ATOM   1715  CB  LEU B 236     -39.139  28.297   6.259  1.00 84.53      B    C  
ANISOU 1715  CB  LEU B 236     7727   8860  15532  -1132  -1734   3276  B    C  
ATOM   1716  CG  LEU B 236     -38.448  27.264   7.152  1.00 99.92      B    C  
ANISOU 1716  CG  LEU B 236     9573  10928  17462  -1093  -1595   3084  B    C  
ATOM   1717  CD1 LEU B 236     -38.137  27.825   8.537  1.00 97.84      B    C  
ANISOU 1717  CD1 LEU B 236     9281  10454  17440  -1133  -1713   2975  B    C  
ATOM   1718  CD2 LEU B 236     -39.280  25.986   7.246  1.00100.36      B    C  
ANISOU 1718  CD2 LEU B 236     9669  11107  17355   -920  -1499   2842  B    C  
ATOM   1719  N   VAL B 237     -38.989  31.409   4.729  1.00104.76      B    N  
ANISOU 1719  N   VAL B 237    10431  11038  18334  -1430  -2047   3949  B    N  
ATOM   1720  CA  VAL B 237     -38.776  32.158   3.499  1.00103.24      B    C  
ANISOU 1720  CA  VAL B 237    10281  10870  18075  -1555  -2072   4298  B    C  
ATOM   1721  C   VAL B 237     -37.725  33.228   3.739  1.00103.11      B    C  
ANISOU 1721  C   VAL B 237    10235  10673  18270  -1780  -2129   4508  B    C  
ATOM   1722  O   VAL B 237     -36.687  33.251   3.086  1.00108.60      B    O  
ANISOU 1722  O   VAL B 237    10843  11545  18876  -1950  -2009   4738  B    O  
ATOM   1723  CB  VAL B 237     -40.062  32.854   3.018  1.00104.16      B    C  
ANISOU 1723  CB  VAL B 237    10540  10815  18223  -1446  -2253   4375  B    C  
ATOM   1724  CG1 VAL B 237     -39.897  33.317   1.592  1.00104.03      B    C  
ANISOU 1724  CG1 VAL B 237    10567  10913  18046  -1552  -2248   4735  B    C  
ATOM   1725  CG2 VAL B 237     -41.255  31.920   3.132  1.00101.87      B    C  
ANISOU 1725  CG2 VAL B 237    10268  10638  17802  -1227  -2248   4110  B    C  
ATOM   1726  N   THR B 238     -37.994  34.104   4.697  1.00 98.02      B    N  
ANISOU 1726  N   THR B 238     9662   9676  17906  -1787  -2306   4418  B    N  
ATOM   1727  CA  THR B 238     -37.112  35.223   4.993  1.00 91.22      B    C  
ANISOU 1727  CA  THR B 238     8803   8584  17274  -2019  -2398   4596  B    C  
ATOM   1728  C   THR B 238     -35.910  34.798   5.835  1.00 99.29      B    C  
ANISOU 1728  C   THR B 238     9664   9717  18346  -2152  -2308   4491  B    C  
ATOM   1729  O   THR B 238     -34.818  35.347   5.701  1.00105.78      B    O  
ANISOU 1729  O   THR B 238    10405  10536  19250  -2396  -2298   4705  B    O  
ATOM   1730  CB  THR B 238     -37.873  36.292   5.758  1.00 94.07      B    C  
ANISOU 1730  CB  THR B 238     9326   8505  17913  -1965  -2621   4499  B    C  
ATOM   1731  CG2 THR B 238     -39.321  36.360   5.254  1.00 80.44      B    C  
ANISOU 1731  CG2 THR B 238     7720   6712  16131  -1729  -2703   4480  B    C  
ATOM   1732  OG1 THR B 238     -37.865  35.969   7.155  1.00105.62      B    O  
ANISOU 1732  OG1 THR B 238    10761   9880  19491  -1902  -2643   4160  B    O  
ATOM   1733  N   GLY B 239     -36.115  33.824   6.711  1.00 94.77      B    N  
ANISOU 1733  N   GLY B 239     9034   9249  17726  -1997  -2247   4175  B    N  
ATOM   1734  CA  GLY B 239     -35.060  33.363   7.598  1.00 91.42      B    C  
ANISOU 1734  CA  GLY B 239     8452   8937  17346  -2090  -2180   4064  B    C  
ATOM   1735  C   GLY B 239     -35.140  34.028   8.961  1.00 88.82      B    C  
ANISOU 1735  C   GLY B 239     8188   8296  17262  -2128  -2359   3863  B    C  
ATOM   1736  O   GLY B 239     -34.509  33.589   9.933  1.00 82.49      B    O  
ANISOU 1736  O   GLY B 239     7280   7568  16493  -2162  -2340   3703  B    O  
ATOM   1737  N   GLU B 240     -35.925  35.093   9.029  1.00 95.86      B    N  
ANISOU 1737  N   GLU B 240     9264   8839  18320  -2113  -2534   3873  B    N  
ATOM   1738  CA  GLU B 240     -36.085  35.855  10.257  1.00101.80      B    C  
ANISOU 1738  CA  GLU B 240    10121   9253  19305  -2144  -2708   3675  B    C  
ATOM   1739  C   GLU B 240     -36.621  35.029  11.417  1.00100.92      B    C  
ANISOU 1739  C   GLU B 240    10004   9191  19152  -1946  -2687   3303  B    C  
ATOM   1740  O   GLU B 240     -37.469  34.148  11.237  1.00 99.21      B    O  
ANISOU 1740  O   GLU B 240     9786   9130  18779  -1720  -2595   3176  B    O  
ATOM   1741  CB  GLU B 240     -37.009  37.044  10.023  1.00103.30      B    C  
ANISOU 1741  CB  GLU B 240    10526   9059  19667  -2095  -2874   3737  B    C  
ATOM   1742  CG  GLU B 240     -36.305  38.246   9.459  1.00127.95      B    C  
ANISOU 1742  CG  GLU B 240    13701  11970  22945  -2363  -2968   4054  B    C  
ATOM   1743  CD  GLU B 240     -37.251  39.400   9.262  1.00142.52      B    C  
ANISOU 1743  CD  GLU B 240    15774  13403  24972  -2283  -3134   4117  B    C  
ATOM   1744  OE1 GLU B 240     -38.465  39.222   9.523  1.00142.34      B    O  
ANISOU 1744  OE1 GLU B 240    15840  13300  24944  -2004  -3164   3915  B    O  
ATOM   1745  OE2 GLU B 240     -36.782  40.477   8.846  1.00142.80      B    O  
ANISOU 1745  OE2 GLU B 240    15893  13199  25164  -2496  -3229   4375  B    O  
ATOM   1746  N   VAL B 241     -36.135  35.348  12.612  1.00 84.70      B    N  
ANISOU 1746  N   VAL B 241     7953   6998  17232  -2047  -2781   3135  B    N  
ATOM   1747  CA  VAL B 241     -36.601  34.710  13.831  1.00 80.45      B    C  
ANISOU 1747  CA  VAL B 241     7428   6477  16660  -1884  -2780   2790  B    C  
ATOM   1748  C   VAL B 241     -37.266  35.715  14.757  1.00 81.37      B    C  
ANISOU 1748  C   VAL B 241     7742   6202  16973  -1850  -2954   2587  B    C  
ATOM   1749  O   VAL B 241     -36.704  36.764  15.034  1.00 93.89      B    O  
ANISOU 1749  O   VAL B 241     9401   7536  18737  -2056  -3091   2648  B    O  
ATOM   1750  CB  VAL B 241     -35.442  34.073  14.560  1.00 79.69      B    C  
ANISOU 1750  CB  VAL B 241     7161   6603  16514  -2011  -2731   2735  B    C  
ATOM   1751  CG1 VAL B 241     -35.926  33.368  15.824  1.00 84.52      B    C  
ANISOU 1751  CG1 VAL B 241     7794   7251  17067  -1841  -2726   2398  B    C  
ATOM   1752  CG2 VAL B 241     -34.749  33.104  13.628  1.00 85.19      B    C  
ANISOU 1752  CG2 VAL B 241     7662   7675  17030  -2022  -2541   2935  B    C  
ATOM   1753  N   SER B 242     -38.460  35.391  15.241  1.00 76.32      B    N  
ANISOU 1753  N   SER B 242     7189   5510  16298  -1593  -2943   2342  B    N  
ATOM   1754  CA  SER B 242     -39.226  36.322  16.067  1.00 80.81      B    C  
ANISOU 1754  CA  SER B 242     7951   5712  17042  -1509  -3081   2134  B    C  
ATOM   1755  C   SER B 242     -39.694  35.707  17.382  1.00 88.67      B    C  
ANISOU 1755  C   SER B 242     8960   6760  17970  -1358  -3053   1779  B    C  
ATOM   1756  O   SER B 242     -40.045  34.528  17.420  1.00 85.33      B    O  
ANISOU 1756  O   SER B 242     8434   6621  17368  -1210  -2918   1693  B    O  
ATOM   1757  CB  SER B 242     -40.441  36.815  15.284  1.00 73.63      B    C  
ANISOU 1757  CB  SER B 242     7151   4632  16192  -1316  -3108   2211  B    C  
ATOM   1758  OG  SER B 242     -40.976  35.769  14.478  1.00 76.20      B    O  
ANISOU 1758  OG  SER B 242     7365   5269  16319  -1162  -2972   2277  B    O  
ATOM   1759  N   ASP B 243     -39.700  36.501  18.456  1.00 85.03      B    N  
ANISOU 1759  N   ASP B 243     8641   6022  17645  -1401  -3177   1572  B    N  
ATOM   1760  CA  ASP B 243     -40.307  36.058  19.714  1.00 79.85      B    C  
ANISOU 1760  CA  ASP B 243     8031   5388  16920  -1237  -3151   1227  B    C  
ATOM   1761  C   ASP B 243     -41.823  36.143  19.593  1.00 86.48      B    C  
ANISOU 1761  C   ASP B 243     8959   6116  17785   -940  -3115   1108  B    C  
ATOM   1762  O   ASP B 243     -42.344  37.042  18.958  1.00101.26      B    O  
ANISOU 1762  O   ASP B 243    10933   7733  19807   -885  -3185   1220  B    O  
ATOM   1763  CB  ASP B 243     -39.815  36.870  20.916  1.00 67.77      B    C  
ANISOU 1763  CB  ASP B 243     6636   3614  15498  -1384  -3293   1024  B    C  
ATOM   1764  CG  ASP B 243     -38.377  36.522  21.319  1.00109.32      B    C  
ANISOU 1764  CG  ASP B 243    11767   9075  20693  -1656  -3326   1085  B    C  
ATOM   1765  OD1 ASP B 243     -38.065  35.314  21.393  1.00116.78      B    O  
ANISOU 1765  OD1 ASP B 243    12537  10378  21456  -1614  -3206   1098  B    O  
ATOM   1766  OD2 ASP B 243     -37.559  37.451  21.572  1.00110.96      B    O  
ANISOU 1766  OD2 ASP B 243    12044   9080  21037  -1910  -3474   1122  B    O  
ATOM   1767  N   LEU B 244     -42.525  35.185  20.185  1.00 85.01      B    N  
ANISOU 1767  N   LEU B 244     8718   6130  17452   -750  -3003    899  B    N  
ATOM   1768  CA  LEU B 244     -43.982  35.142  20.130  1.00 72.00      B    C  
ANISOU 1768  CA  LEU B 244     7109   4434  15814   -468  -2955    779  B    C  
ATOM   1769  C   LEU B 244     -44.532  34.694  21.478  1.00 69.59      B    C  
ANISOU 1769  C   LEU B 244     6832   4179  15426   -331  -2895    444  B    C  
ATOM   1770  O   LEU B 244     -44.459  33.526  21.822  1.00 77.34      B    O  
ANISOU 1770  O   LEU B 244     7703   5456  16226   -311  -2782    376  B    O  
ATOM   1771  CB  LEU B 244     -44.430  34.167  19.053  1.00 64.50      B    C  
ANISOU 1771  CB  LEU B 244     6011   3771  14726   -376  -2839    946  B    C  
ATOM   1772  CG  LEU B 244     -45.932  33.928  19.035  1.00 71.19      B    C  
ANISOU 1772  CG  LEU B 244     6850   4641  15559   -103  -2784    821  B    C  
ATOM   1773  CD1 LEU B 244     -46.645  35.223  18.635  1.00 65.35      B    C  
ANISOU 1773  CD1 LEU B 244     6228   3569  15033     10  -2902    883  B    C  
ATOM   1774  CD2 LEU B 244     -46.296  32.770  18.107  1.00 59.76      B    C  
ANISOU 1774  CD2 LEU B 244     5253   3517  13935    -50  -2669    945  B    C  
ATOM   1775  N   GLN B 245     -45.059  35.630  22.257  1.00 86.72      B    N  
ANISOU 1775  N   GLN B 245     9165   6056  17727   -239  -2966    236  B    N  
ATOM   1776  CA  GLN B 245     -45.428  35.323  23.633  1.00 97.01      B    C  
ANISOU 1776  CA  GLN B 245    10518   7402  18939   -141  -2913    -90  B    C  
ATOM   1777  C   GLN B 245     -46.579  34.340  23.678  1.00 97.69      B    C  
ANISOU 1777  C   GLN B 245    10492   7732  18896     96  -2758   -183  B    C  
ATOM   1778  O   GLN B 245     -47.507  34.414  22.878  1.00101.81      B    O  
ANISOU 1778  O   GLN B 245    10966   8238  19480    258  -2731    -89  B    O  
ATOM   1779  CB  GLN B 245     -45.759  36.595  24.411  1.00103.27      B    C  
ANISOU 1779  CB  GLN B 245    11529   7811  19896    -83  -3011   -309  B    C  
ATOM   1780  CG  GLN B 245     -46.315  36.330  25.793  1.00118.63      B    C  
ANISOU 1780  CG  GLN B 245    13537   9805  21731     54  -2937   -658  B    C  
ATOM   1781  CD  GLN B 245     -46.973  37.558  26.381  1.00129.98      B    C  
ANISOU 1781  CD  GLN B 245    15191  10861  23336    198  -2994   -884  B    C  
ATOM   1782  NE2 GLN B 245     -48.264  37.456  26.704  1.00126.81      B    N  
ANISOU 1782  NE2 GLN B 245    14778  10478  22926    494  -2878  -1057  B    N  
ATOM   1783  OE1 GLN B 245     -46.330  38.592  26.536  1.00132.75      B    O  
ANISOU 1783  OE1 GLN B 245    15713  10899  23826     44  -3135   -904  B    O  
ATOM   1784  N   VAL B 246     -46.525  33.407  24.614  1.00 91.41      B    N  
ANISOU 1784  N   VAL B 246     9648   7165  17918    105  -2662   -354  B    N  
ATOM   1785  CA  VAL B 246     -47.507  32.341  24.602  1.00 77.10      B    C  
ANISOU 1785  CA  VAL B 246     7713   5608  15973    281  -2508   -409  B    C  
ATOM   1786  C   VAL B 246     -47.412  31.529  25.892  1.00 61.77      B    C  
ANISOU 1786  C   VAL B 246     5770   3855  13846    281  -2419   -626  B    C  
ATOM   1787  O   VAL B 246     -46.323  31.320  26.412  1.00 74.58      B    O  
ANISOU 1787  O   VAL B 246     7410   5539  15388    105  -2462   -626  B    O  
ATOM   1788  CB  VAL B 246     -47.293  31.460  23.350  1.00 63.66      B    C  
ANISOU 1788  CB  VAL B 246     5858   4134  14198    223  -2455   -143  B    C  
ATOM   1789  CG1 VAL B 246     -46.214  30.412  23.616  1.00 56.54      B    C  
ANISOU 1789  CG1 VAL B 246     4880   3477  13126     61  -2399    -93  B    C  
ATOM   1790  CG2 VAL B 246     -48.603  30.834  22.884  1.00 68.25      B    C  
ANISOU 1790  CG2 VAL B 246     6336   4863  14732    418  -2349   -152  B    C  
ATOM   1791  N   SER B 247     -48.557  31.109  26.419  1.00 67.93      B    N  
ANISOU 1791  N   SER B 247     6522   4730  14559    475  -2298   -799  B    N  
ATOM   1792  CA  SER B 247     -48.613  30.371  27.676  1.00 63.94      B    C  
ANISOU 1792  CA  SER B 247     6026   4402  13868    491  -2200  -1002  B    C  
ATOM   1793  C   SER B 247     -48.803  28.877  27.440  1.00 74.69      B    C  
ANISOU 1793  C   SER B 247     7233   6084  15060    496  -2059   -912  B    C  
ATOM   1794  O   SER B 247     -48.693  28.077  28.369  1.00 76.16      B    O  
ANISOU 1794  O   SER B 247     7417   6445  15075    481  -1976  -1018  B    O  
ATOM   1795  CB  SER B 247     -49.765  30.879  28.544  1.00 61.01      B    C  
ANISOU 1795  CB  SER B 247     5728   3934  13518    700  -2137  -1268  B    C  
ATOM   1796  OG  SER B 247     -49.469  32.136  29.116  1.00 85.05      B    O  
ANISOU 1796  OG  SER B 247     8958   6682  16674    684  -2253  -1419  B    O  
ATOM   1797  N   GLY B 248     -49.117  28.512  26.200  1.00 73.98      B    N  
ANISOU 1797  N   GLY B 248     7034   6061  15012    517  -2035   -718  B    N  
ATOM   1798  CA  GLY B 248     -49.390  27.130  25.851  1.00 62.24      B    C  
ANISOU 1798  CA  GLY B 248     5424   4844  13382    520  -1904   -640  B    C  
ATOM   1799  C   GLY B 248     -48.991  26.882  24.416  1.00 65.40      B    C  
ANISOU 1799  C   GLY B 248     5750   5286  13813    440  -1933   -388  B    C  
ATOM   1800  O   GLY B 248     -49.107  27.765  23.577  1.00 72.99      B    O  
ANISOU 1800  O   GLY B 248     6725   6093  14917    453  -2029   -279  B    O  
ATOM   1801  N   LEU B 249     -48.478  25.693  24.151  1.00 59.88      B    N  
ANISOU 1801  N   LEU B 249     4985   4791  12976    359  -1848   -291  B    N  
ATOM   1802  CA  LEU B 249     -48.109  25.283  22.805  1.00 57.43      B    C  
ANISOU 1802  CA  LEU B 249     4610   4559  12653    289  -1843    -73  B    C  
ATOM   1803  C   LEU B 249     -48.520  23.819  22.675  1.00 56.52      B    C  
ANISOU 1803  C   LEU B 249     4426   4667  12383    309  -1694    -79  B    C  
ATOM   1804  O   LEU B 249     -48.155  23.003  23.519  1.00 53.15      B    O  
ANISOU 1804  O   LEU B 249     4008   4344  11845    286  -1613   -149  B    O  
ATOM   1805  CB  LEU B 249     -46.602  25.451  22.555  1.00 40.53      B    C  
ANISOU 1805  CB  LEU B 249     2479   2401  10521    130  -1905     79  B    C  
ATOM   1806  CG  LEU B 249     -46.150  25.079  21.129  1.00 60.61      B    C  
ANISOU 1806  CG  LEU B 249     4959   5033  13037     61  -1883    308  B    C  
ATOM   1807  CD1 LEU B 249     -44.892  25.773  20.739  1.00 53.36      B    C  
ANISOU 1807  CD1 LEU B 249     4043   4038  12193    -82  -1974    472  B    C  
ATOM   1808  CD2 LEU B 249     -45.957  23.579  20.938  1.00 75.02      B    C  
ANISOU 1808  CD2 LEU B 249     6727   7081  14696     55  -1734    336  B    C  
ATOM   1809  N   PHE B 250     -49.306  23.496  21.648  1.00 45.35      B    N  
ANISOU 1809  N   PHE B 250     2952   3320  10957    347  -1665     -9  B    N  
ATOM   1810  CA  PHE B 250     -49.839  22.149  21.532  1.00 52.05      B    C  
ANISOU 1810  CA  PHE B 250     3752   4355  11670    353  -1531    -38  B    C  
ATOM   1811  C   PHE B 250     -49.470  21.551  20.189  1.00 51.20      B    C  
ANISOU 1811  C   PHE B 250     3621   4338  11494    278  -1506    130  B    C  
ATOM   1812  O   PHE B 250     -49.444  22.259  19.178  1.00 63.88      B    O  
ANISOU 1812  O   PHE B 250     5218   5890  13163    263  -1596    259  B    O  
ATOM   1813  CB  PHE B 250     -51.354  22.138  21.737  1.00 46.65      B    C  
ANISOU 1813  CB  PHE B 250     3010   3708  11007    463  -1499   -161  B    C  
ATOM   1814  CG  PHE B 250     -51.787  22.500  23.135  1.00 55.56      B    C  
ANISOU 1814  CG  PHE B 250     4162   4787  12161    549  -1474   -352  B    C  
ATOM   1815  CD1 PHE B 250     -52.205  23.778  23.439  1.00 58.12      B    C  
ANISOU 1815  CD1 PHE B 250     4508   4949  12625    651  -1564   -426  B    C  
ATOM   1816  CD2 PHE B 250     -51.788  21.559  24.138  1.00 74.06      B    C  
ANISOU 1816  CD2 PHE B 250     6518   7244  14380    534  -1353   -456  B    C  
ATOM   1817  CE1 PHE B 250     -52.611  24.112  24.721  1.00 57.93      B    C  
ANISOU 1817  CE1 PHE B 250     4519   4887  12607    738  -1525   -622  B    C  
ATOM   1818  CE2 PHE B 250     -52.190  21.889  25.418  1.00 74.30      B    C  
ANISOU 1818  CE2 PHE B 250     6577   7250  14402    609  -1320   -631  B    C  
ATOM   1819  CZ  PHE B 250     -52.607  23.174  25.707  1.00 60.37      B    C  
ANISOU 1819  CZ  PHE B 250     4834   5335  12768    714  -1402   -725  B    C  
ATOM   1820  N   PHE B 251     -49.151  20.260  20.201  1.00 48.56      B    N  
ANISOU 1820  N   PHE B 251     3289   4135  11025    233  -1382    131  B    N  
ATOM   1821  CA  PHE B 251     -48.786  19.525  18.987  1.00 51.19      B    C  
ANISOU 1821  CA  PHE B 251     3621   4564  11267    171  -1327    257  B    C  
ATOM   1822  C   PHE B 251     -50.015  18.900  18.371  1.00 49.22      B    C  
ANISOU 1822  C   PHE B 251     3343   4407  10953    182  -1289    212  B    C  
ATOM   1823  O   PHE B 251     -50.679  18.091  19.011  1.00 60.28      B    O  
ANISOU 1823  O   PHE B 251     4735   5867  12301    196  -1201     91  B    O  
ATOM   1824  CB  PHE B 251     -47.739  18.423  19.280  1.00 38.86      B    C  
ANISOU 1824  CB  PHE B 251     2090   3074   9600    130  -1206    282  B    C  
ATOM   1825  CG  PHE B 251     -46.371  18.958  19.629  1.00 56.93      B    C  
ANISOU 1825  CG  PHE B 251     4375   5315  11939     94  -1254    370  B    C  
ATOM   1826  CD1 PHE B 251     -45.529  19.448  18.650  1.00 55.43      B    C  
ANISOU 1826  CD1 PHE B 251     4164   5121  11774     35  -1295    537  B    C  
ATOM   1827  CD2 PHE B 251     -45.932  18.969  20.941  1.00 54.80      B    C  
ANISOU 1827  CD2 PHE B 251     4115   5023  11681    107  -1260    295  B    C  
ATOM   1828  CE1 PHE B 251     -44.276  19.940  18.967  1.00 54.06      B    C  
ANISOU 1828  CE1 PHE B 251     3963   4922  11655    -19  -1342    627  B    C  
ATOM   1829  CE2 PHE B 251     -44.682  19.460  21.269  1.00 49.26      B    C  
ANISOU 1829  CE2 PHE B 251     3395   4297  11026     54  -1323    377  B    C  
ATOM   1830  CZ  PHE B 251     -43.851  19.949  20.280  1.00 55.35      B    C  
ANISOU 1830  CZ  PHE B 251     4127   5064  11839    -14  -1364    545  B    C  
ATOM   1831  N   ALA B 252     -50.310  19.293  17.133  1.00 48.51      B    N  
ANISOU 1831  N   ALA B 252     3232   4336  10862    162  -1360    317  B    N  
ATOM   1832  CA  ALA B 252     -51.396  18.697  16.346  1.00 44.17      B    C  
ANISOU 1832  CA  ALA B 252     2649   3902  10233    144  -1348    295  B    C  
ATOM   1833  C   ALA B 252     -50.850  18.246  14.996  1.00 43.08      B    C  
ANISOU 1833  C   ALA B 252     2556   3843   9969     62  -1326    420  B    C  
ATOM   1834  O   ALA B 252     -51.384  18.600  13.950  1.00 48.93      B    O  
ANISOU 1834  O   ALA B 252     3275   4636  10682     45  -1413    499  B    O  
ATOM   1835  CB  ALA B 252     -52.546  19.691  16.156  1.00 55.79      B    C  
ANISOU 1835  CB  ALA B 252     4039   5346  11815    220  -1480    294  B    C  
ATOM   1836  N   ILE B 253     -49.790  17.440  15.037  1.00 49.06      B    N  
ANISOU 1836  N   ILE B 253     3377   4622  10641     22  -1206    436  B    N  
ATOM   1837  CA  ILE B 253     -49.107  17.014  13.826  1.00 44.84      B    C  
ANISOU 1837  CA  ILE B 253     2895   4163   9981    -41  -1154    545  B    C  
ATOM   1838  C   ILE B 253     -49.270  15.515  13.540  1.00 52.94      B    C  
ANISOU 1838  C   ILE B 253     3992   5273  10849    -84  -1010    453  B    C  
ATOM   1839  O   ILE B 253     -48.400  14.902  12.918  1.00 44.30      B    O  
ANISOU 1839  O   ILE B 253     2962   4220   9649   -107   -906    504  B    O  
ATOM   1840  CB  ILE B 253     -47.610  17.433  13.839  1.00 48.27      B    C  
ANISOU 1840  CB  ILE B 253     3335   4557  10447    -46  -1131    675  B    C  
ATOM   1841  CG1 ILE B 253     -46.774  16.517  14.719  1.00 47.43      B    C  
ANISOU 1841  CG1 ILE B 253     3252   4449  10320    -23   -995    618  B    C  
ATOM   1842  CG2 ILE B 253     -47.455  18.870  14.349  1.00 47.19      B    C  
ANISOU 1842  CG2 ILE B 253     3149   4298  10483    -24  -1275    737  B    C  
ATOM   1843  CD1 ILE B 253     -46.442  17.091  16.061  1.00 67.76      B    C  
ANISOU 1843  CD1 ILE B 253     5789   6933  13024     14  -1048    581  B    C  
ATOM   1844  N   GLY B 254     -50.392  14.943  13.980  1.00 57.81      B    N  
ANISOU 1844  N   GLY B 254     4597   5910  11457    -95   -998    317  B    N  
ATOM   1845  CA  GLY B 254     -50.724  13.567  13.657  1.00 40.97      B    C  
ANISOU 1845  CA  GLY B 254     2544   3834   9187   -161   -881    222  B    C  
ATOM   1846  C   GLY B 254     -50.249  12.497  14.628  1.00 45.26      B    C  
ANISOU 1846  C   GLY B 254     3156   4320   9720   -142   -727    143  B    C  
ATOM   1847  O   GLY B 254     -49.720  12.809  15.698  1.00 53.38      B    O  
ANISOU 1847  O   GLY B 254     4154   5286  10841    -75   -718    153  B    O  
ATOM   1848  N   HIS B 255     -50.424  11.236  14.214  1.00 36.20      B    N  
ANISOU 1848  N   HIS B 255     2113   3190   8451   -207   -614     68  B    N  
ATOM   1849  CA  HIS B 255     -50.202  10.046  15.041  1.00 41.82      B    C  
ANISOU 1849  CA  HIS B 255     2912   3833   9146   -199   -465     -8  B    C  
ATOM   1850  C   HIS B 255     -49.382   9.072  14.222  1.00 49.49      B    C  
ANISOU 1850  C   HIS B 255     4024   4785   9995   -205   -329     -2  B    C  
ATOM   1851  O   HIS B 255     -49.494   9.035  13.006  1.00 49.79      B    O  
ANISOU 1851  O   HIS B 255     4108   4885   9926   -262   -344      0  B    O  
ATOM   1852  CB  HIS B 255     -51.557   9.434  15.519  1.00 33.43      B    C  
ANISOU 1852  CB  HIS B 255     1840   2781   8081   -286   -459   -134  B    C  
ATOM   1853  CG  HIS B 255     -52.287  10.322  16.489  1.00 47.32      B    C  
ANISOU 1853  CG  HIS B 255     3457   4561   9961   -248   -554   -150  B    C  
ATOM   1854  CD2 HIS B 255     -52.388  10.279  17.843  1.00 43.42      B    C  
ANISOU 1854  CD2 HIS B 255     2933   4032   9534   -202   -511   -188  B    C  
ATOM   1855  ND1 HIS B 255     -52.922  11.489  16.097  1.00 49.21      B    N  
ANISOU 1855  ND1 HIS B 255     3573   4862  10263   -233   -707   -121  B    N  
ATOM   1856  CE1 HIS B 255     -53.416  12.102  17.162  1.00 47.82      B    C  
ANISOU 1856  CE1 HIS B 255     3298   4679  10194   -171   -744   -157  B    C  
ATOM   1857  NE2 HIS B 255     -53.099  11.394  18.235  1.00 55.29      B    N  
ANISOU 1857  NE2 HIS B 255     4301   5575  11133   -158   -627   -202  B    N  
ATOM   1858  N   GLU B 256     -48.526   8.300  14.876  1.00 50.57      B    N  
ANISOU 1858  N   GLU B 256     3734   4351  11129   -148    228   1018  B    N  
ATOM   1859  CA  GLU B 256     -47.686   7.362  14.155  1.00 42.83      B    C  
ANISOU 1859  CA  GLU B 256     2603   3562  10109   -132    299   1107  B    C  
ATOM   1860  C   GLU B 256     -48.173   5.933  14.413  1.00 39.54      B    C  
ANISOU 1860  C   GLU B 256     2282   3306   9437    -87    321    903  B    C  
ATOM   1861  O   GLU B 256     -48.041   5.414  15.514  1.00 58.28      B    O  
ANISOU 1861  O   GLU B 256     4761   5585  11799   -143    202    742  B    O  
ATOM   1862  CB  GLU B 256     -46.233   7.543  14.598  1.00 49.68      B    C  
ANISOU 1862  CB  GLU B 256     3373   4270  11232   -248    175   1195  B    C  
ATOM   1863  CG  GLU B 256     -45.223   6.727  13.832  1.00 69.64      B    C  
ANISOU 1863  CG  GLU B 256     5724   6973  13764   -225    259   1336  B    C  
ATOM   1864  CD  GLU B 256     -44.783   7.398  12.547  1.00 90.96      B    C  
ANISOU 1864  CD  GLU B 256     8205   9775  16582   -165    386   1639  B    C  
ATOM   1865  OE1 GLU B 256     -45.353   8.458  12.179  1.00 94.62      B    O  
ANISOU 1865  OE1 GLU B 256     8644  10188  17120   -138    424   1748  B    O  
ATOM   1866  OE2 GLU B 256     -43.862   6.849  11.905  1.00 92.49      B    O  
ANISOU 1866  OE2 GLU B 256     8240  10111  16793   -131    459   1785  B    O  
ATOM   1867  N   PRO B 257     -48.787   5.317  13.403  1.00 47.87      B    N  
ANISOU 1867  N   PRO B 257     3291   4607  10291     19    469    914  B    N  
ATOM   1868  CA  PRO B 257     -49.387   3.987  13.594  1.00 44.76      B    C  
ANISOU 1868  CA  PRO B 257     2978   4342   9685     64    486    716  B    C  
ATOM   1869  C   PRO B 257     -48.247   3.026  13.759  1.00 46.79      B    C  
ANISOU 1869  C   PRO B 257     3153   4615  10010     24    460    696  B    C  
ATOM   1870  O   PRO B 257     -47.226   3.214  13.111  1.00 44.58      B    O  
ANISOU 1870  O   PRO B 257     2722   4373   9844     19    506    863  B    O  
ATOM   1871  CB  PRO B 257     -50.120   3.726  12.276  1.00 32.41      B    C  
ANISOU 1871  CB  PRO B 257     1346   3039   7931    177    642    757  B    C  
ATOM   1872  CG  PRO B 257     -49.360   4.603  11.273  1.00 36.36      B    C  
ANISOU 1872  CG  PRO B 257     1663   3601   8550    199    726   1014  B    C  
ATOM   1873  CD  PRO B 257     -49.032   5.853  12.060  1.00 34.86      B    C  
ANISOU 1873  CD  PRO B 257     1506   3133   8605    105    619   1106  B    C  
ATOM   1874  N   ALA B 258     -48.396   2.040  14.631  1.00 47.56      B    N  
ANISOU 1874  N   ALA B 258     3335   4682  10054      2    392    524  B    N  
ATOM   1875  CA  ALA B 258     -47.268   1.197  14.959  1.00 36.40      B    C  
ANISOU 1875  CA  ALA B 258     1840   3252   8739    -47    360    524  B    C  
ATOM   1876  C   ALA B 258     -47.212   0.022  13.987  1.00 51.52      B    C  
ANISOU 1876  C   ALA B 258     3662   5366  10548     41    493    484  B    C  
ATOM   1877  O   ALA B 258     -47.545  -1.109  14.348  1.00 35.45      B    O  
ANISOU 1877  O   ALA B 258     1657   3360   8453     59    490    334  B    O  
ATOM   1878  CB  ALA B 258     -47.346   0.718  16.436  1.00 35.21      B    C  
ANISOU 1878  CB  ALA B 258     1792   2978   8608   -112    223    386  B    C  
ATOM   1879  N   THR B 259     -46.748   0.289  12.766  1.00 38.56      B    N  
ANISOU 1879  N   THR B 259     1892   3862   8899    103    610    625  B    N  
ATOM   1880  CA  THR B 259     -46.697  -0.774  11.759  1.00 32.95      B    C  
ANISOU 1880  CA  THR B 259     1096   3360   8064    208    739    562  B    C  
ATOM   1881  C   THR B 259     -45.318  -1.118  11.185  1.00 42.89      B    C  
ANISOU 1881  C   THR B 259     2192   4685   9421    235    815    699  B    C  
ATOM   1882  O   THR B 259     -45.190  -2.027  10.348  1.00 49.98      B    O  
ANISOU 1882  O   THR B 259     3019   5755  10214    339    927    629  B    O  
ATOM   1883  CB  THR B 259     -47.712  -0.496  10.652  1.00 42.88      B    C  
ANISOU 1883  CB  THR B 259     2353   4820   9120    315    839    547  B    C  
ATOM   1884  CG2 THR B 259     -49.103  -0.532  11.246  1.00 31.50      B    C  
ANISOU 1884  CG2 THR B 259     1070   3327   7573    300    773    391  B    C  
ATOM   1885  OG1 THR B 259     -47.510   0.825  10.163  1.00 43.46      B    O  
ANISOU 1885  OG1 THR B 259     2357   4906   9248    320    870    772  B    O  
ATOM   1886  N   LYS B 260     -44.275  -0.425  11.634  1.00 49.24      B    N  
ANISOU 1886  N   LYS B 260     2930   5349  10428    148    751    889  B    N  
ATOM   1887  CA  LYS B 260     -42.968  -0.745  11.094  1.00 51.73      B    C  
ANISOU 1887  CA  LYS B 260     3080   5732  10844    181    830   1055  B    C  
ATOM   1888  C   LYS B 260     -42.554  -2.207  11.338  1.00 48.27      B    C  
ANISOU 1888  C   LYS B 260     2625   5310  10403    200    864    918  B    C  
ATOM   1889  O   LYS B 260     -41.903  -2.814  10.496  1.00 47.28      B    O  
ANISOU 1889  O   LYS B 260     2381   5329  10252    301    993    969  B    O  
ATOM   1890  CB  LYS B 260     -41.917   0.282  11.535  1.00 52.48      B    C  
ANISOU 1890  CB  LYS B 260     3090   5662  11187     72    739   1307  B    C  
ATOM   1891  CG  LYS B 260     -42.221   1.663  10.958  1.00 61.53      B    C  
ANISOU 1891  CG  LYS B 260     4194   6817  12368     89    750   1482  B    C  
ATOM   1892  CD  LYS B 260     -41.272   2.728  11.474  1.00 88.12      B    C  
ANISOU 1892  CD  LYS B 260     7479   9974  16027    -35    630   1711  B    C  
ATOM   1893  CE  LYS B 260     -41.894   4.119  11.320  1.00 89.87      B    C  
ANISOU 1893  CE  LYS B 260     7715  10112  16319    -53    596   1804  B    C  
ATOM   1894  NZ  LYS B 260     -41.252   5.121  12.217  1.00 92.07      B    N  
ANISOU 1894  NZ  LYS B 260     7984  10103  16895   -209    414   1910  B    N  
ATOM   1895  N   PHE B 261     -42.971  -2.783  12.460  1.00 40.80      B    N  
ANISOU 1895  N   PHE B 261     1788   4231   9483    119    760    750  B    N  
ATOM   1896  CA  PHE B 261     -42.518  -4.125  12.799  1.00 43.30      B    C  
ANISOU 1896  CA  PHE B 261     2062   4535   9854    125    790    656  B    C  
ATOM   1897  C   PHE B 261     -42.995  -5.143  11.785  1.00 45.07      B    C  
ANISOU 1897  C   PHE B 261     2266   4930   9930    268    929    487  B    C  
ATOM   1898  O   PHE B 261     -42.397  -6.207  11.633  1.00 50.92      B    O  
ANISOU 1898  O   PHE B 261     2926   5691  10730    314   1006    444  B    O  
ATOM   1899  CB  PHE B 261     -42.948  -4.516  14.225  1.00 39.86      B    C  
ANISOU 1899  CB  PHE B 261     1724   3946   9476     23    653    536  B    C  
ATOM   1900  CG  PHE B 261     -44.373  -4.986  14.342  1.00 35.30      B    C  
ANISOU 1900  CG  PHE B 261     1263   3397   8753     70    642    314  B    C  
ATOM   1901  CD1 PHE B 261     -45.401  -4.088  14.399  1.00 42.70      B    C  
ANISOU 1901  CD1 PHE B 261     2318   4329   9575     67    587    278  B    C  
ATOM   1902  CD2 PHE B 261     -44.675  -6.332  14.418  1.00 38.39      B    C  
ANISOU 1902  CD2 PHE B 261     1631   3805   9150    115    685    160  B    C  
ATOM   1903  CE1 PHE B 261     -46.712  -4.503  14.525  1.00 38.80      B    C  
ANISOU 1903  CE1 PHE B 261     1923   3864   8957    109    574    107  B    C  
ATOM   1904  CE2 PHE B 261     -45.979  -6.747  14.554  1.00 44.48      B    C  
ANISOU 1904  CE2 PHE B 261     2491   4589   9819    150    659    -16  B    C  
ATOM   1905  CZ  PHE B 261     -46.994  -5.844  14.603  1.00 39.78      B    C  
ANISOU 1905  CZ  PHE B 261     2016   4006   9094    148    604    -36  B    C  
ATOM   1906  N   LEU B 262     -44.095  -4.826  11.109  1.00 42.67      B    N  
ANISOU 1906  N   LEU B 262     2031   4745   9438    338    957    383  B    N  
ATOM   1907  CA  LEU B 262     -44.698  -5.764  10.163  1.00 48.55      B    C  
ANISOU 1907  CA  LEU B 262     2769   5657  10022    466   1059    180  B    C  
ATOM   1908  C   LEU B 262     -43.831  -5.866   8.920  1.00 48.69      B    C  
ANISOU 1908  C   LEU B 262     2651   5869   9982    598   1210    274  B    C  
ATOM   1909  O   LEU B 262     -44.051  -6.717   8.055  1.00 48.94      B    O  
ANISOU 1909  O   LEU B 262     2655   6055   9883    723   1305     99  B    O  
ATOM   1910  CB  LEU B 262     -46.075  -5.290   9.732  1.00 33.77      B    C  
ANISOU 1910  CB  LEU B 262      992   3885   7953    502   1041     77  B    C  
ATOM   1911  CG  LEU B 262     -47.187  -5.243  10.742  1.00 41.32      B    C  
ANISOU 1911  CG  LEU B 262     2087   4703   8911    418    917    -31  B    C  
ATOM   1912  CD1 LEU B 262     -48.340  -4.562  10.094  1.00 40.20      B    C  
ANISOU 1912  CD1 LEU B 262     2006   4693   8578    466    930    -55  B    C  
ATOM   1913  CD2 LEU B 262     -47.551  -6.657  11.172  1.00 43.00      B    C  
ANISOU 1913  CD2 LEU B 262     2311   4852   9175    422    895   -243  B    C  
ATOM   1914  N   ASN B 263     -42.877  -4.949   8.836  1.00 58.08      B    N  
ANISOU 1914  N   ASN B 263     3751   7053  11265    575   1224    552  B    N  
ATOM   1915  CA  ASN B 263     -41.941  -4.872   7.728  1.00 53.55      B    C  
ANISOU 1915  CA  ASN B 263     3023   6670  10654    708   1370    720  B    C  
ATOM   1916  C   ASN B 263     -42.585  -5.138   6.371  1.00 56.53      B    C  
ANISOU 1916  C   ASN B 263     3380   7341  10759    889   1493    584  B    C  
ATOM   1917  O   ASN B 263     -42.106  -5.956   5.597  1.00 67.37      B    O  
ANISOU 1917  O   ASN B 263     4675   8867  12053   1029   1616    511  B    O  
ATOM   1918  CB  ASN B 263     -40.767  -5.825   7.949  1.00 40.29      B    C  
ANISOU 1918  CB  ASN B 263     1254   4929   9127    721   1428    755  B    C  
ATOM   1919  CG  ASN B 263     -39.600  -5.537   7.003  1.00 56.33      B    C  
ANISOU 1919  CG  ASN B 263     3110   7127  11165    846   1568   1020  B    C  
ATOM   1920  ND2 ASN B 263     -38.986  -6.494   6.489  1.00 54.05      B    N  
ANISOU 1920  ND2 ASN B 263     2745   6934  10857    969   1695    968  B    N  
ATOM   1921  OD1 ASN B 263     -39.290  -4.352   6.779  1.00 59.12      B    O  
ANISOU 1921  OD1 ASN B 263     3390   7514  11560    829   1555   1290  B    O  
ATOM   1922  N   GLY B 264     -43.677  -4.443   6.087  1.00 51.31      B    N  
ANISOU 1922  N   GLY B 264     2784   6765   9946    890   1460    547  B    N  
ATOM   1923  CA  GLY B 264     -44.243  -4.445   4.749  1.00 46.97      B    C  
ANISOU 1923  CA  GLY B 264     2188   6536   9122   1057   1569    478  B    C  
ATOM   1924  C   GLY B 264     -45.249  -5.543   4.430  1.00 56.55      B    C  
ANISOU 1924  C   GLY B 264     3494   7835  10157   1114   1563    111  B    C  
ATOM   1925  O   GLY B 264     -45.922  -5.488   3.396  1.00 59.70      B    O  
ANISOU 1925  O   GLY B 264     3872   8506  10305   1233   1621     25  B    O  
ATOM   1926  N   GLN B 265     -45.365  -6.530   5.314  1.00 48.14      B    N  
ANISOU 1926  N   GLN B 265     2512   6547   9231   1029   1486    -93  B    N  
ATOM   1927  CA  GLN B 265     -46.220  -7.692   5.060  1.00 44.37      B    C  
ANISOU 1927  CA  GLN B 265     2098   6107   8653   1075   1470   -440  B    C  
ATOM   1928  C   GLN B 265     -47.741  -7.468   5.050  1.00 44.31      B    C  
ANISOU 1928  C   GLN B 265     2197   6139   8500   1036   1380   -580  B    C  
ATOM   1929  O   GLN B 265     -48.511  -8.366   4.725  1.00 63.00      B    O  
ANISOU 1929  O   GLN B 265     4602   8556  10779   1076   1353   -858  B    O  
ATOM   1930  CB  GLN B 265     -45.867  -8.775   6.054  1.00 38.60      B    C  
ANISOU 1930  CB  GLN B 265     1392   5112   8163    994   1419   -565  B    C  
ATOM   1931  CG  GLN B 265     -44.408  -9.159   5.939  1.00 44.72      B    C  
ANISOU 1931  CG  GLN B 265     2052   5871   9067   1051   1525   -444  B    C  
ATOM   1932  CD  GLN B 265     -44.065 -10.223   6.925  1.00 60.81      B    C  
ANISOU 1932  CD  GLN B 265     4092   7658  11356    971   1486   -539  B    C  
ATOM   1933  NE2 GLN B 265     -43.269  -9.846   7.932  1.00 55.40      B    N  
ANISOU 1933  NE2 GLN B 265     3379   6795  10876    851   1442   -305  B    N  
ATOM   1934  OE1 GLN B 265     -44.538 -11.377   6.819  1.00 54.26      B    O  
ANISOU 1934  OE1 GLN B 265     3279   6787  10551   1011   1487   -816  B    O  
ATOM   1935  N   LEU B 266     -48.186  -6.291   5.447  1.00 41.25      B    N  
ANISOU 1935  N   LEU B 266     1854   5711   8109    955   1325   -386  B    N  
ATOM   1936  CA  LEU B 266     -49.592  -5.947   5.299  1.00 41.05      B    C  
ANISOU 1936  CA  LEU B 266     1910   5760   7927    938   1268   -466  B    C  
ATOM   1937  C   LEU B 266     -49.633  -4.700   4.450  1.00 50.73      B    C  
ANISOU 1937  C   LEU B 266     3063   7216   8996   1004   1345   -233  B    C  
ATOM   1938  O   LEU B 266     -48.743  -3.840   4.509  1.00 54.51      B    O  
ANISOU 1938  O   LEU B 266     3466   7667   9579    996   1390     33  B    O  
ATOM   1939  CB  LEU B 266     -50.254  -5.639   6.645  1.00 41.26      B    C  
ANISOU 1939  CB  LEU B 266     2060   5517   8099    790   1137   -438  B    C  
ATOM   1940  CG  LEU B 266     -50.428  -6.769   7.642  1.00 55.38      B    C  
ANISOU 1940  CG  LEU B 266     3907   7081  10054    719   1047   -622  B    C  
ATOM   1941  CD1 LEU B 266     -51.331  -6.278   8.775  1.00 41.38      B    C  
ANISOU 1941  CD1 LEU B 266     2250   5132   8342    614    932   -572  B    C  
ATOM   1942  CD2 LEU B 266     -51.028  -7.956   6.944  1.00 50.26      B    C  
ANISOU 1942  CD2 LEU B 266     3245   6540   9313    794   1054   -903  B    C  
ATOM   1943  N   GLU B 267     -50.684  -4.582   3.670  1.00 47.10      B    N  
ANISOU 1943  N   GLU B 267     2610   6981   8306   1065   1357   -313  B    N  
ATOM   1944  CA  GLU B 267     -50.844  -3.393   2.860  1.00 48.29      B    C  
ANISOU 1944  CA  GLU B 267     2670   7367   8309   1132   1438    -69  B    C  
ATOM   1945  C   GLU B 267     -51.264  -2.184   3.699  1.00 50.66      B    C  
ANISOU 1945  C   GLU B 267     3033   7467   8746   1012   1379    151  B    C  
ATOM   1946  O   GLU B 267     -52.284  -2.219   4.396  1.00 59.35      B    O  
ANISOU 1946  O   GLU B 267     4263   8426   9864    926   1285     54  B    O  
ATOM   1947  CB  GLU B 267     -51.849  -3.671   1.755  1.00 50.78      B    C  
ANISOU 1947  CB  GLU B 267     2961   8015   8320   1236   1467   -221  B    C  
ATOM   1948  CG  GLU B 267     -52.185  -2.473   0.929  1.00 63.23      B    C  
ANISOU 1948  CG  GLU B 267     4429   9861   9734   1305   1552     44  B    C  
ATOM   1949  CD  GLU B 267     -53.281  -2.801  -0.058  1.00 76.34      B    C  
ANISOU 1949  CD  GLU B 267     6071  11852  11083   1389   1558   -119  B    C  
ATOM   1950  OE1 GLU B 267     -53.269  -3.951  -0.569  1.00 77.00      B    O  
ANISOU 1950  OE1 GLU B 267     6160  12063  11034   1465   1545   -420  B    O  
ATOM   1951  OE2 GLU B 267     -54.145  -1.924  -0.314  1.00 69.80      B    O  
ANISOU 1951  OE2 GLU B 267     5217  11151  10151   1381   1571     49  B    O  
ATOM   1952  N   LEU B 268     -50.476  -1.117   3.596  1.00 48.77      B    N  
ANISOU 1952  N   LEU B 268     2692   7224   8615   1018   1438    452  B    N  
ATOM   1953  CA  LEU B 268     -50.653   0.091   4.386  1.00 48.04      B    C  
ANISOU 1953  CA  LEU B 268     2644   6907   8701    909   1385    661  B    C  
ATOM   1954  C   LEU B 268     -51.114   1.213   3.505  1.00 49.50      B    C  
ANISOU 1954  C   LEU B 268     2715   7314   8780    980   1478    904  B    C  
ATOM   1955  O   LEU B 268     -50.884   1.198   2.312  1.00 52.97      B    O  
ANISOU 1955  O   LEU B 268     3000   8082   9045   1118   1593    988  B    O  
ATOM   1956  CB  LEU B 268     -49.310   0.491   4.993  1.00 38.40      B    C  
ANISOU 1956  CB  LEU B 268     1369   5469   7749    845   1365    838  B    C  
ATOM   1957  CG  LEU B 268     -48.649  -0.591   5.862  1.00 40.95      B    C  
ANISOU 1957  CG  LEU B 268     1767   5590   8201    777   1289    652  B    C  
ATOM   1958  CD1 LEU B 268     -47.408  -0.042   6.462  1.00 36.91      B    C  
ANISOU 1958  CD1 LEU B 268     1194   4879   7949    700   1256    859  B    C  
ATOM   1959  CD2 LEU B 268     -49.611  -1.097   6.982  1.00 34.74      B    C  
ANISOU 1959  CD2 LEU B 268     1170   4595   7436    675   1161    424  B    C  
ATOM   1960  N   HIS B 269     -51.781   2.194   4.090  1.00 51.92      B    N  
ANISOU 1960  N   HIS B 269     3088   7454   9186    900   1433   1023  B    N  
ATOM   1961  CA  HIS B 269     -52.007   3.450   3.398  1.00 46.26      B    C  
ANISOU 1961  CA  HIS B 269     2234   6880   8464    952   1528   1324  B    C  
ATOM   1962  C   HIS B 269     -50.703   4.247   3.505  1.00 56.97      B    C  
ANISOU 1962  C   HIS B 269     3455   8102  10090    933   1549   1598  B    C  
ATOM   1963  O   HIS B 269     -49.776   3.815   4.202  1.00 52.36      B    O  
ANISOU 1963  O   HIS B 269     2915   7309   9671    864   1477   1527  B    O  
ATOM   1964  CB  HIS B 269     -53.142   4.208   4.057  1.00 37.63      B    C  
ANISOU 1964  CB  HIS B 269     1264   5615   7419    874   1476   1352  B    C  
ATOM   1965  CG  HIS B 269     -54.464   3.502   4.006  1.00 59.74      B    C  
ANISOU 1965  CG  HIS B 269     4185   8529   9985    885   1446   1130  B    C  
ATOM   1966  CD2 HIS B 269     -55.262   3.032   4.998  1.00 68.11      B    C  
ANISOU 1966  CD2 HIS B 269     5439   9383  11057    804   1336    927  B    C  
ATOM   1967  ND1 HIS B 269     -55.154   3.282   2.830  1.00 62.66      B    N  
ANISOU 1967  ND1 HIS B 269     4458   9273  10078    990   1529   1131  B    N  
ATOM   1968  CE1 HIS B 269     -56.306   2.682   3.101  1.00 52.24      B    C  
ANISOU 1968  CE1 HIS B 269     3271   7953   8625    960   1461    930  B    C  
ATOM   1969  NE2 HIS B 269     -56.402   2.532   4.408  1.00 50.63      B    N  
ANISOU 1969  NE2 HIS B 269     3240   7399   8600    853   1350    818  B    N  
ATOM   1970  N   ALA B 270     -50.622   5.401   2.840  1.00 66.50      B    N  
ANISOU 1970  N   ALA B 270     4482   9423  11363    988   1645   1926  B    N  
ATOM   1971  CA  ALA B 270     -49.327   6.098   2.750  1.00 59.60      B    C  
ANISOU 1971  CA  ALA B 270     3429   8462  10752    989   1673   2220  B    C  
ATOM   1972  C   ALA B 270     -48.919   6.658   4.103  1.00 59.46      B    C  
ANISOU 1972  C   ALA B 270     3531   7984  11078    815   1526   2219  B    C  
ATOM   1973  O   ALA B 270     -47.728   6.785   4.396  1.00 64.77      B    O  
ANISOU 1973  O   ALA B 270     4124   8505  11980    770   1485   2338  B    O  
ATOM   1974  CB  ALA B 270     -49.351   7.210   1.691  1.00 44.57      B    C  
ANISOU 1974  CB  ALA B 270     1269   6796   8871   1097   1815   2609  B    C  
ATOM   1975  N   ASP B 271     -49.914   6.989   4.926  1.00 59.06      B    N  
ANISOU 1975  N   ASP B 271     3665   7723  11051    726   1443   2084  B    N  
ATOM   1976  CA  ASP B 271     -49.642   7.513   6.256  1.00 54.31      B    C  
ANISOU 1976  CA  ASP B 271     3197   6704  10733    576   1293   2035  B    C  
ATOM   1977  C   ASP B 271     -49.259   6.395   7.235  1.00 54.97      B    C  
ANISOU 1977  C   ASP B 271     3450   6637  10799    496   1168   1743  B    C  
ATOM   1978  O   ASP B 271     -49.029   6.673   8.414  1.00 60.08      B    O  
ANISOU 1978  O   ASP B 271     4219   6970  11636    375   1030   1664  B    O  
ATOM   1979  CB  ASP B 271     -50.868   8.237   6.763  1.00 49.63      B    C  
ANISOU 1979  CB  ASP B 271     2741   5970  10146    539   1266   1992  B    C  
ATOM   1980  CG  ASP B 271     -52.079   7.376   6.692  1.00 61.19      B    C  
ANISOU 1980  CG  ASP B 271     4349   7605  11297    585   1283   1760  B    C  
ATOM   1981  OD1 ASP B 271     -51.897   6.177   6.410  1.00 68.56      B    O  
ANISOU 1981  OD1 ASP B 271     5294   8709  12046    623   1289   1589  B    O  
ATOM   1982  OD2 ASP B 271     -53.200   7.881   6.905  1.00 75.92      B    O  
ANISOU 1982  OD2 ASP B 271     6304   9427  13115    584   1293   1754  B    O  
ATOM   1983  N   GLY B 272     -49.210   5.145   6.748  1.00 44.21      B    N  
ANISOU 1983  N   GLY B 272     2086   5500   9212    567   1218   1584  B    N  
ATOM   1984  CA  GLY B 272     -48.698   4.008   7.519  1.00 36.80      B    C  
ANISOU 1984  CA  GLY B 272     1252   4446   8284    508   1128   1356  B    C  
ATOM   1985  C   GLY B 272     -49.722   3.126   8.213  1.00 43.92      B    C  
ANISOU 1985  C   GLY B 272     2352   5299   9035    480   1057   1055  B    C  
ATOM   1986  O   GLY B 272     -49.389   2.026   8.648  1.00 43.85      B    O  
ANISOU 1986  O   GLY B 272     2394   5254   9011    459   1012    875  B    O  
ATOM   1987  N   TYR B 273     -50.953   3.615   8.337  1.00 34.42      B    N  
ANISOU 1987  N   TYR B 273     1245   4089   7743    484   1052   1027  B    N  
ATOM   1988  CA  TYR B 273     -52.086   2.829   8.847  1.00 41.50      B    C  
ANISOU 1988  CA  TYR B 273     2304   4980   8486    478    999    786  B    C  
ATOM   1989  C   TYR B 273     -52.351   1.592   8.004  1.00 40.85      B    C  
ANISOU 1989  C   TYR B 273     2179   5153   8189    563   1059    629  B    C  
ATOM   1990  O   TYR B 273     -52.171   1.601   6.790  1.00 50.82      B    O  
ANISOU 1990  O   TYR B 273     3303   6680   9327    657   1169    712  B    O  
ATOM   1991  CB  TYR B 273     -53.386   3.676   8.966  1.00 32.55      B    C  
ANISOU 1991  CB  TYR B 273     1256   3825   7287    488   1007    837  B    C  
ATOM   1992  CG  TYR B 273     -53.247   4.766   9.994  1.00 41.83      B    C  
ANISOU 1992  CG  TYR B 273     2513   4703   8676    407    926    916  B    C  
ATOM   1993  CD1 TYR B 273     -52.565   5.950   9.697  1.00 46.11      B    C  
ANISOU 1993  CD1 TYR B 273     2940   5170   9412    390    958   1149  B    C  
ATOM   1994  CD2 TYR B 273     -53.739   4.602  11.274  1.00 48.00      B    C  
ANISOU 1994  CD2 TYR B 273     3477   5279   9482    353    812    758  B    C  
ATOM   1995  CE1 TYR B 273     -52.404   6.951  10.646  1.00 48.93      B    C  
ANISOU 1995  CE1 TYR B 273     3373   5228   9991    311    867   1188  B    C  
ATOM   1996  CE2 TYR B 273     -53.599   5.612  12.235  1.00 52.33      B    C  
ANISOU 1996  CE2 TYR B 273     4111   5562  10210    291    729    793  B    C  
ATOM   1997  CZ  TYR B 273     -52.931   6.779  11.913  1.00 52.01      B    C  
ANISOU 1997  CZ  TYR B 273     3966   5426  10371    265    750    990  B    C  
ATOM   1998  OH  TYR B 273     -52.787   7.764  12.859  1.00 44.97      B    O  
ANISOU 1998  OH  TYR B 273     3160   4251   9677    200    653    992  B    O  
ATOM   1999  N   VAL B 274     -52.763   0.520   8.673  1.00 44.42      B    N  
ANISOU 1999  N   VAL B 274     2741   5529   8609    533    981    400  B    N  
ATOM   2000  CA  VAL B 274     -53.086  -0.739   8.028  1.00 39.86      B    C  
ANISOU 2000  CA  VAL B 274     2139   5134   7872    597   1009    203  B    C  
ATOM   2001  C   VAL B 274     -54.381  -0.620   7.228  1.00 48.51      B    C  
ANISOU 2001  C   VAL B 274     3238   6448   8747    661   1051    182  B    C  
ATOM   2002  O   VAL B 274     -55.406  -0.204   7.762  1.00 55.34      B    O  
ANISOU 2002  O   VAL B 274     4203   7229   9595    628   1006    199  B    O  
ATOM   2003  CB  VAL B 274     -53.208  -1.855   9.065  1.00 46.76      B    C  
ANISOU 2003  CB  VAL B 274     3108   5830   8831    540    907     -2  B    C  
ATOM   2004  CG1 VAL B 274     -53.620  -3.179   8.399  1.00 31.08      B    C  
ANISOU 2004  CG1 VAL B 274     1090   3997   6722    602    923   -223  B    C  
ATOM   2005  CG2 VAL B 274     -51.878  -2.001   9.829  1.00 35.18      B    C  
ANISOU 2005  CG2 VAL B 274     1616   4178   7572    477    869     38  B    C  
ATOM   2006  N   ALA B 275     -54.336  -0.968   5.943  1.00 42.41      B    N  
ANISOU 2006  N   ALA B 275     2350   5969   7793    760   1139    151  B    N  
ATOM   2007  CA  ALA B 275     -55.539  -0.836   5.125  1.00 48.11      B    C  
ANISOU 2007  CA  ALA B 275     3057   6934   8289    817   1172    141  B    C  
ATOM   2008  C   ALA B 275     -56.436  -2.001   5.419  1.00 46.20      B    C  
ANISOU 2008  C   ALA B 275     2906   6659   7990    795   1079   -122  B    C  
ATOM   2009  O   ALA B 275     -56.073  -3.139   5.158  1.00 55.13      B    O  
ANISOU 2009  O   ALA B 275     4011   7829   9107    822   1061   -334  B    O  
ATOM   2010  CB  ALA B 275     -55.217  -0.796   3.638  1.00 35.90      B    C  
ANISOU 2010  CB  ALA B 275     1346   5756   6540    944   1291    193  B    C  
ATOM   2011  N   THR B 276     -57.613  -1.717   5.957  1.00 36.80      B    N  
ANISOU 2011  N   THR B 276     1812   5389   6784    750   1023    -97  B    N  
ATOM   2012  CA  THR B 276     -58.596  -2.757   6.236  1.00 48.18      B    C  
ANISOU 2012  CA  THR B 276     3317   6798   8190    729    927   -301  B    C  
ATOM   2013  C   THR B 276     -59.773  -2.635   5.273  1.00 51.29      B    C  
ANISOU 2013  C   THR B 276     3672   7464   8353    774    945   -293  B    C  
ATOM   2014  O   THR B 276     -60.034  -1.567   4.721  1.00 54.11      B    O  
ANISOU 2014  O   THR B 276     3980   7979   8601    808   1029    -85  B    O  
ATOM   2015  CB  THR B 276     -59.116  -2.684   7.706  1.00 41.92      B    C  
ANISOU 2015  CB  THR B 276     2657   5708   7559    653    835   -272  B    C  
ATOM   2016  CG2 THR B 276     -58.063  -3.184   8.680  1.00 40.13      B    C  
ANISOU 2016  CG2 THR B 276     2458   5246   7544    605    787   -338  B    C  
ATOM   2017  OG1 THR B 276     -59.425  -1.328   8.038  1.00 43.86      B    O  
ANISOU 2017  OG1 THR B 276     2953   5899   7812    643    874    -43  B    O  
ATOM   2018  N   LYS B 277     -60.464  -3.745   5.055  1.00 44.60      B    N  
ANISOU 2018  N   LYS B 277     2830   6671   7446    773    863   -515  B    N  
ATOM   2019  CA  LYS B 277     -61.722  -3.742   4.319  1.00 52.78      B    C  
ANISOU 2019  CA  LYS B 277     3838   7935   8282    793    842   -521  B    C  
ATOM   2020  C   LYS B 277     -62.765  -2.958   5.133  1.00 55.72      B    C  
ANISOU 2020  C   LYS B 277     4299   8174   8699    747    823   -314  B    C  
ATOM   2021  O   LYS B 277     -63.193  -3.409   6.190  1.00 60.34      B    O  
ANISOU 2021  O   LYS B 277     4974   8520   9435    696    734   -355  B    O  
ATOM   2022  CB  LYS B 277     -62.160  -5.189   4.112  1.00 61.40      B    C  
ANISOU 2022  CB  LYS B 277     4920   9035   9375    782    727   -825  B    C  
ATOM   2023  CG  LYS B 277     -63.522  -5.408   3.441  1.00 85.95      B    C  
ANISOU 2023  CG  LYS B 277     8000  12353  12306    781    661   -872  B    C  
ATOM   2024  CD  LYS B 277     -63.842  -6.911   3.373  1.00 89.31      B    C  
ANISOU 2024  CD  LYS B 277     8411  12714  12810    757    521  -1195  B    C  
ATOM   2025  CE  LYS B 277     -65.114  -7.209   2.598  1.00 84.40      B    C  
ANISOU 2025  CE  LYS B 277     7742  12313  12013    749    432  -1273  B    C  
ATOM   2026  NZ  LYS B 277     -66.308  -6.742   3.339  1.00 81.64      B    N  
ANISOU 2026  NZ  LYS B 277     7448  11853  11721    690    386  -1047  B    N  
ATOM   2027  N   PRO B 278     -63.195  -1.795   4.635  1.00 46.14      B    N  
ANISOU 2027  N   PRO B 278     3049   7125   7356    777    915    -77  B    N  
ATOM   2028  CA  PRO B 278     -64.023  -0.880   5.447  1.00 44.27      B    C  
ANISOU 2028  CA  PRO B 278     2902   6738   7183    750    926    145  B    C  
ATOM   2029  C   PRO B 278     -65.179  -1.578   6.083  1.00 53.35      B    C  
ANISOU 2029  C   PRO B 278     4127   7784   8362    715    815     75  B    C  
ATOM   2030  O   PRO B 278     -65.900  -2.277   5.380  1.00 52.56      B    O  
ANISOU 2030  O   PRO B 278     3969   7869   8134    716    758    -33  B    O  
ATOM   2031  CB  PRO B 278     -64.552   0.127   4.434  1.00 32.27      B    C  
ANISOU 2031  CB  PRO B 278     1281   5501   5477    799   1038    369  B    C  
ATOM   2032  CG  PRO B 278     -63.509   0.111   3.289  1.00 49.47      B    C  
ANISOU 2032  CG  PRO B 278     3317   7935   7546    861   1117    333  B    C  
ATOM   2033  CD  PRO B 278     -62.997  -1.321   3.252  1.00 44.42      B    C  
ANISOU 2033  CD  PRO B 278     2690   7267   6922    853   1019      3  B    C  
ATOM   2034  N   GLY B 279     -65.366  -1.392   7.386  1.00 57.43      B    N  
ANISOU 2034  N   GLY B 279     4760   8020   9040    689    778    141  B    N  
ATOM   2035  CA  GLY B 279     -66.483  -2.034   8.062  1.00 32.38      B    C  
ANISOU 2035  CA  GLY B 279     1643   4751   5909    673    678    122  B    C  
ATOM   2036  C   GLY B 279     -66.114  -3.415   8.591  1.00 49.94      B    C  
ANISOU 2036  C   GLY B 279     3864   6826   8285    640    561   -108  B    C  
ATOM   2037  O   GLY B 279     -66.979  -4.167   9.030  1.00 45.37      B    O  
ANISOU 2037  O   GLY B 279     3291   6181   7767    628    466   -139  B    O  
ATOM   2038  N   SER B 280     -64.830  -3.762   8.536  1.00 37.23      B    N  
ANISOU 2038  N   SER B 280     2229   5163   6753    631    573   -250  B    N  
ATOM   2039  CA  SER B 280     -64.362  -5.008   9.140  1.00 47.21      B    C  
ANISOU 2039  CA  SER B 280     3480   6259   8198    603    482   -441  B    C  
ATOM   2040  C   SER B 280     -62.903  -4.832   9.516  1.00 45.08      B    C  
ANISOU 2040  C   SER B 280     3220   5871   8036    594    528   -468  B    C  
ATOM   2041  O   SER B 280     -62.324  -3.757   9.335  1.00 57.79      B    O  
ANISOU 2041  O   SER B 280     4848   7517   9595    605    615   -339  B    O  
ATOM   2042  CB  SER B 280     -64.510  -6.198   8.187  1.00 45.08      B    C  
ANISOU 2042  CB  SER B 280     3111   6119   7897    599    419   -679  B    C  
ATOM   2043  OG  SER B 280     -63.407  -6.269   7.282  1.00 52.70      B    O  
ANISOU 2043  OG  SER B 280     4017   7217   8791    625    487   -805  B    O  
ATOM   2044  N   THR B 281     -62.306  -5.897  10.021  1.00 39.14      B    N  
ANISOU 2044  N   THR B 281     2439   4976   7456    571    469   -618  B    N  
ATOM   2045  CA  THR B 281     -60.934  -5.822  10.466  1.00 43.23      B    C  
ANISOU 2045  CA  THR B 281     2957   5377   8093    556    502   -628  B    C  
ATOM   2046  C   THR B 281     -60.034  -6.596   9.510  1.00 47.49      B    C  
ANISOU 2046  C   THR B 281     3398   6015   8630    572    535   -813  B    C  
ATOM   2047  O   THR B 281     -58.847  -6.789   9.757  1.00 55.99      B    O  
ANISOU 2047  O   THR B 281     4447   7006   9821    562    564   -839  B    O  
ATOM   2048  CB  THR B 281     -60.840  -6.363  11.876  1.00 46.85      B    C  
ANISOU 2048  CB  THR B 281     3446   5606   8751    528    427   -619  B    C  
ATOM   2049  CG2 THR B 281     -61.784  -5.576  12.775  1.00 32.07      B    C  
ANISOU 2049  CG2 THR B 281     1675   3667   6843    542    404   -443  B    C  
ATOM   2050  OG1 THR B 281     -61.255  -7.732  11.864  1.00 39.22      B    O  
ANISOU 2050  OG1 THR B 281     2403   4601   7899    523    353   -769  B    O  
ATOM   2051  N   HIS B 282     -60.610  -7.018   8.397  1.00 44.73      B    N  
ANISOU 2051  N   HIS B 282     2993   5862   8140    604    532   -939  B    N  
ATOM   2052  CA  HIS B 282     -59.866  -7.758   7.389  1.00 44.03      B    C  
ANISOU 2052  CA  HIS B 282     2817   5901   8012    646    566  -1143  B    C  
ATOM   2053  C   HIS B 282     -58.761  -6.937   6.775  1.00 49.13      B    C  
ANISOU 2053  C   HIS B 282     3429   6679   8557    691    688  -1044  B    C  
ATOM   2054  O   HIS B 282     -58.961  -5.765   6.442  1.00 48.06      B    O  
ANISOU 2054  O   HIS B 282     3303   6674   8283    709    751   -851  B    O  
ATOM   2055  CB  HIS B 282     -60.804  -8.250   6.281  1.00 50.11      B    C  
ANISOU 2055  CB  HIS B 282     3539   6891   8610    679    525  -1307  B    C  
ATOM   2056  CG  HIS B 282     -61.742  -9.325   6.735  1.00 52.44      B    C  
ANISOU 2056  CG  HIS B 282     3828   7043   9053    634    390  -1445  B    C  
ATOM   2057  CD2 HIS B 282     -62.430  -9.477   7.892  1.00 61.15      B    C  
ANISOU 2057  CD2 HIS B 282     4971   7934  10329    583    311  -1336  B    C  
ATOM   2058  ND1 HIS B 282     -62.030 -10.435   5.973  1.00 58.23      B    N  
ANISOU 2058  ND1 HIS B 282     4492   7845   9789    649    318  -1722  B    N  
ATOM   2059  CE1 HIS B 282     -62.877 -11.209   6.629  1.00 54.49      B    C  
ANISOU 2059  CE1 HIS B 282     4006   7189   9510    595    194  -1762  B    C  
ATOM   2060  NE2 HIS B 282     -63.131 -10.655   7.799  1.00 65.84      B    N  
ANISOU 2060  NE2 HIS B 282     5505   8466  11046    562    195  -1515  B    N  
ATOM   2061  N   THR B 283     -57.600  -7.572   6.625  1.00 43.11      B    N  
ANISOU 2061  N   THR B 283     2611   5882   7887    716    726  -1156  B    N  
ATOM   2062  CA  THR B 283     -56.449  -6.937   6.036  1.00 35.83      B    C  
ANISOU 2062  CA  THR B 283     1632   5083   6900    770    842  -1049  B    C  
ATOM   2063  C   THR B 283     -56.099  -7.640   4.734  1.00 52.78      B    C  
ANISOU 2063  C   THR B 283     3688   7473   8895    874    899  -1251  B    C  
ATOM   2064  O   THR B 283     -56.767  -8.571   4.315  1.00 58.27      B    O  
ANISOU 2064  O   THR B 283     4373   8224   9543    892    834  -1493  B    O  
ATOM   2065  CB  THR B 283     -55.227  -7.084   6.927  1.00 47.23      B    C  
ANISOU 2065  CB  THR B 283     3074   6300   8572    728    853   -988  B    C  
ATOM   2066  CG2 THR B 283     -55.542  -6.712   8.389  1.00 33.41      B    C  
ANISOU 2066  CG2 THR B 283     1416   4290   6986    631    771   -862  B    C  
ATOM   2067  OG1 THR B 283     -54.768  -8.439   6.843  1.00 42.98      B    O  
ANISOU 2067  OG1 THR B 283     2484   5699   8145    750    841  -1216  B    O  
ATOM   2068  N   SER B 284     -55.010  -7.201   4.121  1.00 44.16      B    N  
ANISOU 2068  N   SER B 284     2520   6520   7738    949   1013  -1151  B    N  
ATOM   2069  CA  SER B 284     -54.577  -7.734   2.849  1.00 49.12      B    C  
ANISOU 2069  CA  SER B 284     3056   7419   8187   1080   1090  -1316  B    C  
ATOM   2070  C   SER B 284     -54.206  -9.226   2.932  1.00 59.76      B    C  
ANISOU 2070  C   SER B 284     4397   8637   9673   1099   1053  -1624  B    C  
ATOM   2071  O   SER B 284     -53.977  -9.865   1.904  1.00 55.14      B    O  
ANISOU 2071  O   SER B 284     3753   8258   8941   1216   1098  -1837  B    O  
ATOM   2072  CB  SER B 284     -53.413  -6.873   2.250  1.00 42.67      B    C  
ANISOU 2072  CB  SER B 284     2140   6778   7294   1172   1234  -1078  B    C  
ATOM   2073  OG  SER B 284     -52.161  -7.054   2.914  1.00 60.55      B    O  
ANISOU 2073  OG  SER B 284     4389   8828   9789   1145   1267   -999  B    O  
ATOM   2074  N   VAL B 285     -54.145  -9.790   4.135  1.00 52.79      B    N  
ANISOU 2074  N   VAL B 285     3564   7422   9073    994    977  -1649  B    N  
ATOM   2075  CA  VAL B 285     -53.758 -11.206   4.268  1.00 44.21      B    C  
ANISOU 2075  CA  VAL B 285     2447   6182   8170   1008    953  -1910  B    C  
ATOM   2076  C   VAL B 285     -54.816 -12.053   4.958  1.00 49.80      B    C  
ANISOU 2076  C   VAL B 285     3193   6680   9050    920    810  -2068  B    C  
ATOM   2077  O   VAL B 285     -55.175 -11.794   6.109  1.00 58.69      B    O  
ANISOU 2077  O   VAL B 285     4365   7599  10334    818    744  -1908  B    O  
ATOM   2078  CB  VAL B 285     -52.464 -11.346   5.038  1.00 40.98      B    C  
ANISOU 2078  CB  VAL B 285     2007   5569   7994    982   1013  -1782  B    C  
ATOM   2079  CG1 VAL B 285     -52.097 -12.816   5.181  1.00 39.26      B    C  
ANISOU 2079  CG1 VAL B 285     1741   5182   7993   1001   1003  -2033  B    C  
ATOM   2080  CG2 VAL B 285     -51.375 -10.602   4.320  1.00 39.27      B    C  
ANISOU 2080  CG2 VAL B 285     1729   5552   7639   1076   1151  -1613  B    C  
ATOM   2081  N   GLU B 286     -55.328 -13.063   4.265  1.00 56.15      B    N  
ANISOU 2081  N   GLU B 286     3966   7539   9829    965    757  -2378  B    N  
ATOM   2082  CA  GLU B 286     -56.401 -13.865   4.844  1.00 54.08      B    C  
ANISOU 2082  CA  GLU B 286     3714   7079   9754    882    610  -2509  B    C  
ATOM   2083  C   GLU B 286     -55.900 -14.414   6.173  1.00 62.22      B    C  
ANISOU 2083  C   GLU B 286     4723   7775  11142    807    592  -2415  B    C  
ATOM   2084  O   GLU B 286     -54.753 -14.839   6.263  1.00 58.28      B    O  
ANISOU 2084  O   GLU B 286     4175   7195  10773    842    677  -2437  B    O  
ATOM   2085  CB  GLU B 286     -56.803 -15.010   3.917  1.00 55.55      B    C  
ANISOU 2085  CB  GLU B 286     3852   7328   9927    940    547  -2891  B    C  
ATOM   2086  CG  GLU B 286     -57.381 -14.574   2.575  1.00 75.35      B    C  
ANISOU 2086  CG  GLU B 286     6366  10206  12058   1020    545  -3012  B    C  
ATOM   2087  CD  GLU B 286     -58.824 -14.095   2.664  1.00 98.84      B    C  
ANISOU 2087  CD  GLU B 286     9380  13245  14931    940    427  -2923  B    C  
ATOM   2088  OE1 GLU B 286     -59.377 -14.000   3.786  1.00105.92      B    O  
ANISOU 2088  OE1 GLU B 286    10308  13906  16032    835    356  -2744  B    O  
ATOM   2089  OE2 GLU B 286     -59.409 -13.810   1.597  1.00106.69      B    O  
ANISOU 2089  OE2 GLU B 286    10365  14549  15625    994    408  -3018  B    O  
ATOM   2090  N   GLY B 287     -56.735 -14.372   7.210  1.00 57.63      B    N  
ANISOU 2090  N   GLY B 287     4168   7021  10707    715    492  -2283  B    N  
ATOM   2091  CA  GLY B 287     -56.344 -14.880   8.516  1.00 43.03      B    C  
ANISOU 2091  CA  GLY B 287     2279   4893   9178    654    472  -2170  B    C  
ATOM   2092  C   GLY B 287     -55.645 -13.872   9.429  1.00 49.11      B    C  
ANISOU 2092  C   GLY B 287     3098   5622   9939    615    527  -1870  B    C  
ATOM   2093  O   GLY B 287     -55.426 -14.154  10.617  1.00 51.02      B    O  
ANISOU 2093  O   GLY B 287     3310   5669  10407    562    498  -1744  B    O  
ATOM   2094  N   VAL B 288     -55.279 -12.706   8.891  1.00 44.73      B    N  
ANISOU 2094  N   VAL B 288     2603   5255   9137    642    601  -1752  B    N  
ATOM   2095  CA  VAL B 288     -54.683 -11.640   9.696  1.00 39.21      B    C  
ANISOU 2095  CA  VAL B 288     1955   4510   8433    598    634  -1484  B    C  
ATOM   2096  C   VAL B 288     -55.665 -10.469   9.781  1.00 50.30      B    C  
ANISOU 2096  C   VAL B 288     3457   6004   9649    577    597  -1336  B    C  
ATOM   2097  O   VAL B 288     -56.190 -10.028   8.755  1.00 50.05      B    O  
ANISOU 2097  O   VAL B 288     3441   6179   9397    623    623  -1377  B    O  
ATOM   2098  CB  VAL B 288     -53.363 -11.157   9.094  1.00 36.91      B    C  
ANISOU 2098  CB  VAL B 288     1630   4324   8068    643    752  -1417  B    C  
ATOM   2099  CG1 VAL B 288     -52.850  -9.918   9.825  1.00 31.41      B    C  
ANISOU 2099  CG1 VAL B 288      986   3583   7367    587    762  -1147  B    C  
ATOM   2100  CG2 VAL B 288     -52.328 -12.287   9.103  1.00 49.01      B    C  
ANISOU 2100  CG2 VAL B 288     3066   5755   9801    670    804  -1533  B    C  
ATOM   2101  N   PHE B 289     -55.920  -9.979  10.994  1.00 42.94      B    N  
ANISOU 2101  N   PHE B 289     2584   4933   8800    519    543  -1164  B    N  
ATOM   2102  CA  PHE B 289     -56.881  -8.894  11.193  1.00 28.47      B    C  
ANISOU 2102  CA  PHE B 289      848   3152   6814    509    515  -1021  B    C  
ATOM   2103  C   PHE B 289     -56.271  -7.672  11.868  1.00 38.26      B    C  
ANISOU 2103  C   PHE B 289     2156   4337   8043    476    538   -816  B    C  
ATOM   2104  O   PHE B 289     -55.307  -7.798  12.608  1.00 49.58      B    O  
ANISOU 2104  O   PHE B 289     3568   5647   9624    441    533   -770  B    O  
ATOM   2105  CB  PHE B 289     -58.095  -9.422  11.966  1.00 45.98      B    C  
ANISOU 2105  CB  PHE B 289     3085   5269   9115    491    415  -1023  B    C  
ATOM   2106  CG  PHE B 289     -58.664 -10.679  11.377  1.00 45.68      B    C  
ANISOU 2106  CG  PHE B 289     2965   5243   9149    508    368  -1230  B    C  
ATOM   2107  CD1 PHE B 289     -58.166 -11.910  11.754  1.00 40.57      B    C  
ANISOU 2107  CD1 PHE B 289     2219   4445   8749    497    343  -1342  B    C  
ATOM   2108  CD2 PHE B 289     -59.659 -10.627  10.415  1.00 48.33      B    C  
ANISOU 2108  CD2 PHE B 289     3308   5738   9316    531    345  -1313  B    C  
ATOM   2109  CE1 PHE B 289     -58.637 -13.055  11.190  1.00 46.03      B    C  
ANISOU 2109  CE1 PHE B 289     2829   5118   9542    510    293  -1551  B    C  
ATOM   2110  CE2 PHE B 289     -60.152 -11.783   9.847  1.00 45.06      B    C  
ANISOU 2110  CE2 PHE B 289     2815   5326   8980    538    280  -1531  B    C  
ATOM   2111  CZ  PHE B 289     -59.630 -12.995  10.236  1.00 58.72      B    C  
ANISOU 2111  CZ  PHE B 289     4454   6877  10981    527    252  -1660  B    C  
ATOM   2112  N   ALA B 290     -56.833  -6.487  11.621  1.00 37.68      B    N  
ANISOU 2112  N   ALA B 290     2154   4350   7811    485    559   -694  B    N  
ATOM   2113  CA  ALA B 290     -56.318  -5.279  12.257  1.00 34.33      B    C  
ANISOU 2113  CA  ALA B 290     1795   3846   7404    453    567   -519  B    C  
ATOM   2114  C   ALA B 290     -57.439  -4.535  12.949  1.00 37.95      B    C  
ANISOU 2114  C   ALA B 290     2364   4254   7803    454    523   -419  B    C  
ATOM   2115  O   ALA B 290     -58.471  -4.292  12.353  1.00 49.65      B    O  
ANISOU 2115  O   ALA B 290     3864   5853   9149    489    542   -404  B    O  
ATOM   2116  CB  ALA B 290     -55.617  -4.398  11.247  1.00 37.00      B    C  
ANISOU 2116  CB  ALA B 290     2090   4315   7655    475    661   -430  B    C  
ATOM   2117  N   ALA B 291     -57.231  -4.192  14.218  1.00 35.83      B    N  
ANISOU 2117  N   ALA B 291     2164   3825   7628    424    464   -352  B    N  
ATOM   2118  CA  ALA B 291     -58.232  -3.500  15.015  1.00 38.66      B    C  
ANISOU 2118  CA  ALA B 291     2633   4126   7929    445    426   -265  B    C  
ATOM   2119  C   ALA B 291     -57.610  -2.302  15.742  1.00 33.98      B    C  
ANISOU 2119  C   ALA B 291     2122   3415   7374    416    409   -172  B    C  
ATOM   2120  O   ALA B 291     -56.427  -2.316  16.075  1.00 43.51      B    O  
ANISOU 2120  O   ALA B 291     3293   4545   8693    366    385   -179  B    O  
ATOM   2121  CB  ALA B 291     -58.905  -4.477  16.011  1.00 28.67      B    C  
ANISOU 2121  CB  ALA B 291     1370   2793   6729    466    347   -300  B    C  
ATOM   2122  N   GLY B 292     -58.398  -1.256  15.952  1.00 35.33      B    N  
ANISOU 2122  N   GLY B 292     2394   3566   7463    449    419    -84  B    N  
ATOM   2123  CA  GLY B 292     -57.985  -0.130  16.763  1.00 31.13      B    C  
ANISOU 2123  CA  GLY B 292     1954   2893   6981    429    384    -28  B    C  
ATOM   2124  C   GLY B 292     -57.271   0.974  16.020  1.00 42.08      B    C  
ANISOU 2124  C   GLY B 292     3311   4265   8412    394    440     56  B    C  
ATOM   2125  O   GLY B 292     -57.353   1.081  14.792  1.00 36.58      B    O  
ANISOU 2125  O   GLY B 292     2532   3707   7661    408    530    109  B    O  
ATOM   2126  N   ASP B 293     -56.569   1.822  16.767  1.00 28.86      B    N  
ANISOU 2126  N   ASP B 293     1690   2430   6845    350    381     76  B    N  
ATOM   2127  CA  ASP B 293     -55.926   2.994  16.142  1.00 34.96      B    C  
ANISOU 2127  CA  ASP B 293     2421   3152   7712    315    423    186  B    C  
ATOM   2128  C   ASP B 293     -54.866   2.625  15.086  1.00 44.52      B    C  
ANISOU 2128  C   ASP B 293     3468   4466   8980    280    480    235  B    C  
ATOM   2129  O   ASP B 293     -54.493   3.470  14.273  1.00 40.07      B    O  
ANISOU 2129  O   ASP B 293     2826   3926   8473    276    547    370  B    O  
ATOM   2130  CB  ASP B 293     -55.291   3.926  17.182  1.00 41.73      B    C  
ANISOU 2130  CB  ASP B 293     3357   3790   8708    261    321    175  B    C  
ATOM   2131  CG  ASP B 293     -56.292   4.806  17.871  1.00 42.82      B    C  
ANISOU 2131  CG  ASP B 293     3646   3827   8799    318    304    166  B    C  
ATOM   2132  OD1 ASP B 293     -57.495   4.493  17.877  1.00 38.54      B    O  
ANISOU 2132  OD1 ASP B 293     3161   3376   8106    400    353    164  B    O  
ATOM   2133  OD2 ASP B 293     -55.860   5.820  18.420  1.00 63.13      B    O  
ANISOU 2133  OD2 ASP B 293     6274   6218  11493    283    241    161  B    O  
ATOM   2134  N   VAL B 294     -54.381   1.383  15.078  1.00 27.49      B    N  
ANISOU 2134  N   VAL B 294     1249   2374   6821    268    464    143  B    N  
ATOM   2135  CA  VAL B 294     -53.370   1.040  14.091  1.00 42.32      B    C  
ANISOU 2135  CA  VAL B 294     2979   4355   8744    257    530    189  B    C  
ATOM   2136  C   VAL B 294     -54.028   1.055  12.716  1.00 48.06      B    C  
ANISOU 2136  C   VAL B 294     3638   5302   9320    334    651    234  B    C  
ATOM   2137  O   VAL B 294     -53.354   1.009  11.705  1.00 42.55      B    O  
ANISOU 2137  O   VAL B 294     2812   4739   8616    359    731    300  B    O  
ATOM   2138  CB  VAL B 294     -52.753  -0.337  14.306  1.00 37.09      B    C  
ANISOU 2138  CB  VAL B 294     2259   3715   8118    242    506     76  B    C  
ATOM   2139  CG1 VAL B 294     -53.736  -1.399  13.852  1.00 34.97      B    C  
ANISOU 2139  CG1 VAL B 294     1988   3585   7716    306    543    -44  B    C  
ATOM   2140  CG2 VAL B 294     -51.538  -0.451  13.484  1.00 28.80      B    C  
ANISOU 2140  CG2 VAL B 294     1070   2733   7142    235    569    149  B    C  
ATOM   2141  N   GLN B 295     -55.355   1.104  12.677  1.00 46.25      B    N  
ANISOU 2141  N   GLN B 295     3484   5132   8956    380    665    208  B    N  
ATOM   2142  CA  GLN B 295     -56.035   1.239  11.402  1.00 28.46      B    C  
ANISOU 2142  CA  GLN B 295     1160   3107   6547    447    769    267  B    C  
ATOM   2143  C   GLN B 295     -57.161   2.230  11.395  1.00 41.01      B    C  
ANISOU 2143  C   GLN B 295     2817   4698   8069    476    802    379  B    C  
ATOM   2144  O   GLN B 295     -58.071   2.081  10.619  1.00 44.40      B    O  
ANISOU 2144  O   GLN B 295     3215   5314   8339    528    861    395  B    O  
ATOM   2145  CB  GLN B 295     -56.578  -0.087  10.908  1.00 29.86      B    C  
ANISOU 2145  CB  GLN B 295     1308   3443   6593    486    772    107  B    C  
ATOM   2146  CG  GLN B 295     -57.426  -0.798  11.876  1.00 27.03      B    C  
ANISOU 2146  CG  GLN B 295     1050   2982   6236    475    684     -7  B    C  
ATOM   2147  CD  GLN B 295     -58.921  -0.490  11.689  1.00 49.51      B    C  
ANISOU 2147  CD  GLN B 295     3955   5914   8944    518    701     42  B    C  
ATOM   2148  NE2 GLN B 295     -59.576  -0.033  12.758  1.00 25.97      B    N  
ANISOU 2148  NE2 GLN B 295     1093   2785   5991    518    652     88  B    N  
ATOM   2149  OE1 GLN B 295     -59.473  -0.672  10.602  1.00 41.90      B    O  
ANISOU 2149  OE1 GLN B 295     2924   5159   7837    557    755     38  B    O  
ATOM   2150  N   ASP B 296     -57.091   3.247  12.239  1.00 46.45      B    N  
ANISOU 2150  N   ASP B 296     3591   5180   8879    445    764    453  B    N  
ATOM   2151  CA  ASP B 296     -58.124   4.260  12.274  1.00 44.90      B    C  
ANISOU 2151  CA  ASP B 296     3457   4959   8644    482    809    568  B    C  
ATOM   2152  C   ASP B 296     -57.524   5.596  12.696  1.00 37.79      B    C  
ANISOU 2152  C   ASP B 296     2573   3848   7939    446    798    681  B    C  
ATOM   2153  O   ASP B 296     -57.040   5.714  13.820  1.00 43.78      B    O  
ANISOU 2153  O   ASP B 296     3428   4392   8815    398    691    591  B    O  
ATOM   2154  CB  ASP B 296     -59.214   3.839  13.272  1.00 29.35      B    C  
ANISOU 2154  CB  ASP B 296     1640   2918   6596    509    745    470  B    C  
ATOM   2155  CG  ASP B 296     -60.122   5.003  13.662  1.00 40.36      B    C  
ANISOU 2155  CG  ASP B 296     3133   4212   7992    550    780    582  B    C  
ATOM   2156  OD1 ASP B 296     -60.422   5.812  12.764  1.00 38.75      B    O  
ANISOU 2156  OD1 ASP B 296     2851   4098   7773    575    886    745  B    O  
ATOM   2157  OD2 ASP B 296     -60.517   5.096  14.850  1.00 47.20      B    O  
ANISOU 2157  OD2 ASP B 296     4141   4923   8871    569    710    515  B    O  
ATOM   2158  N   LYS B 297     -57.559   6.596  11.818  1.00 41.47      B    N  
ANISOU 2158  N   LYS B 297     2933   4375   8448    470    902    879  B    N  
ATOM   2159  CA  LYS B 297     -57.035   7.909  12.208  1.00 51.30      B    C  
ANISOU 2159  CA  LYS B 297     4177   5384   9928    432    885    991  B    C  
ATOM   2160  C   LYS B 297     -58.156   8.922  12.349  1.00 50.43      B    C  
ANISOU 2160  C   LYS B 297     4140   5200   9821    482    946   1092  B    C  
ATOM   2161  O   LYS B 297     -57.914  10.077  12.711  1.00 53.53      B    O  
ANISOU 2161  O   LYS B 297     4546   5369  10424    460    936   1170  B    O  
ATOM   2162  CB  LYS B 297     -55.930   8.411  11.264  1.00 57.14      B    C  
ANISOU 2162  CB  LYS B 297     4713   6180  10819    412    944   1179  B    C  
ATOM   2163  CG  LYS B 297     -56.378   8.820   9.868  1.00 52.80      B    C  
ANISOU 2163  CG  LYS B 297     3987   5893  10179    489   1107   1406  B    C  
ATOM   2164  CD  LYS B 297     -55.280   9.670   9.224  1.00 59.40      B    C  
ANISOU 2164  CD  LYS B 297     4618   6706  11244    475   1156   1643  B    C  
ATOM   2165  CE  LYS B 297     -55.528   9.985   7.757  1.00 60.30      B    C  
ANISOU 2165  CE  LYS B 297     4511   7141  11258    569   1325   1899  B    C  
ATOM   2166  NZ  LYS B 297     -55.547   8.734   6.931  1.00 67.39      B    N  
ANISOU 2166  NZ  LYS B 297     5353   8385  11865    630   1368   1798  B    N  
ATOM   2167  N   LYS B 298     -59.378   8.449  12.112  1.00 42.30      B    N  
ANISOU 2167  N   LYS B 298     3157   4341   8573    547   1003   1083  B    N  
ATOM   2168  CA  LYS B 298     -60.572   9.296  12.036  1.00 47.15      B    C  
ANISOU 2168  CA  LYS B 298     3813   4949   9155    610   1095   1219  B    C  
ATOM   2169  C   LYS B 298     -61.278   9.474  13.370  1.00 49.55      B    C  
ANISOU 2169  C   LYS B 298     4332   5040   9456    638   1024   1098  B    C  
ATOM   2170  O   LYS B 298     -61.571  10.586  13.773  1.00 55.29      B    O  
ANISOU 2170  O   LYS B 298     5120   5579  10310    663   1054   1168  B    O  
ATOM   2171  CB  LYS B 298     -61.565   8.688  11.052  1.00 49.41      B    C  
ANISOU 2171  CB  LYS B 298     4024   5554   9197    667   1187   1294  B    C  
ATOM   2172  CG  LYS B 298     -62.661   9.625  10.591  1.00 53.18      B    C  
ANISOU 2172  CG  LYS B 298     4469   6094   9645    730   1317   1515  B    C  
ATOM   2173  CD  LYS B 298     -63.550   8.893   9.620  1.00 56.00      B    C  
ANISOU 2173  CD  LYS B 298     4741   6791   9746    770   1380   1568  B    C  
ATOM   2174  CE  LYS B 298     -64.623   9.778   9.039  1.00 76.70      B    C  
ANISOU 2174  CE  LYS B 298     7295   9524  12323    830   1520   1825  B    C  
ATOM   2175  NZ  LYS B 298     -65.648   8.920   8.364  1.00 97.22      B    N  
ANISOU 2175  NZ  LYS B 298     9854  12432  14655    859   1537   1831  B    N  
ATOM   2176  N   TYR B 299     -61.553   8.372  14.048  1.00 40.54      B    N  
ANISOU 2176  N   TYR B 299     3294   3933   8176    645    937    923  B    N  
ATOM   2177  CA  TYR B 299     -62.171   8.402  15.358  1.00 34.37      B    C  
ANISOU 2177  CA  TYR B 299     2702   2994   7362    694    868    812  B    C  
ATOM   2178  C   TYR B 299     -61.146   8.404  16.498  1.00 46.37      B    C  
ANISOU 2178  C   TYR B 299     4311   4301   9009    642    724    635  B    C  
ATOM   2179  O   TYR B 299     -61.150   9.297  17.345  1.00 39.51      B    O  
ANISOU 2179  O   TYR B 299     3557   3219   8236    663    685    590  B    O  
ATOM   2180  CB  TYR B 299     -63.100   7.194  15.477  1.00 37.84      B    C  
ANISOU 2180  CB  TYR B 299     3173   3606   7598    742    853    762  B    C  
ATOM   2181  CG  TYR B 299     -64.121   7.226  14.397  1.00 44.37      B    C  
ANISOU 2181  CG  TYR B 299     3915   4645   8298    783    972    930  B    C  
ATOM   2182  CD1 TYR B 299     -65.096   8.208  14.393  1.00 43.13      B    C  
ANISOU 2182  CD1 TYR B 299     3805   4453   8131    853   1071   1091  B    C  
ATOM   2183  CD2 TYR B 299     -64.085   6.328  13.346  1.00 32.82      B    C  
ANISOU 2183  CD2 TYR B 299     2317   3423   6730    754    990    929  B    C  
ATOM   2184  CE1 TYR B 299     -66.029   8.287  13.384  1.00 45.73      B    C  
ANISOU 2184  CE1 TYR B 299     4038   4994   8343    886   1182   1274  B    C  
ATOM   2185  CE2 TYR B 299     -65.016   6.398  12.323  1.00 30.20      B    C  
ANISOU 2185  CE2 TYR B 299     1895   3313   6266    788   1088   1081  B    C  
ATOM   2186  CZ  TYR B 299     -65.995   7.391  12.345  1.00 51.86      B    C  
ANISOU 2186  CZ  TYR B 299     4676   6029   8997    850   1186   1269  B    C  
ATOM   2187  OH  TYR B 299     -66.948   7.495  11.339  1.00 32.52      B    O  
ANISOU 2187  OH  TYR B 299     2126   3818   6412    882   1285   1447  B    O  
ATOM   2188  N   ARG B 300     -60.307   7.377  16.567  1.00 31.93      B    N  
ANISOU 2188  N   ARG B 300     2428   2532   7173    580    643    524  B    N  
ATOM   2189  CA  ARG B 300     -59.226   7.394  17.537  1.00 46.35      B    C  
ANISOU 2189  CA  ARG B 300     4303   4183   9124    516    508    385  B    C  
ATOM   2190  C   ARG B 300     -59.718   7.452  18.954  1.00 53.57      B    C  
ANISOU 2190  C   ARG B 300     5394   4984   9978    578    421    257  B    C  
ATOM   2191  O   ARG B 300     -59.182   8.232  19.725  1.00 55.60      B    O  
ANISOU 2191  O   ARG B 300     5730   5045  10352    555    336    176  B    O  
ATOM   2192  CB  ARG B 300     -58.375   8.642  17.329  1.00 37.46      B    C  
ANISOU 2192  CB  ARG B 300     3131   2875   8226    454    502    452  B    C  
ATOM   2193  CG  ARG B 300     -57.507   8.616  16.079  1.00 44.58      B    C  
ANISOU 2193  CG  ARG B 300     3833   3880   9225    391    566    589  B    C  
ATOM   2194  CD  ARG B 300     -56.489   9.778  16.078  1.00 49.40      B    C  
ANISOU 2194  CD  ARG B 300     4381   4273  10117    318    524    662  B    C  
ATOM   2195  NE  ARG B 300     -57.044  10.958  15.440  1.00 62.18      B    N  
ANISOU 2195  NE  ARG B 300     5948   5843  11835    359    639    846  B    N  
ATOM   2196  CZ  ARG B 300     -57.331  12.078  16.083  1.00 65.55      B    C  
ANISOU 2196  CZ  ARG B 300     6474   6024  12409    372    611    828  B    C  
ATOM   2197  NH1 ARG B 300     -57.079  12.179  17.386  1.00 74.76      B    N  
ANISOU 2197  NH1 ARG B 300     7803   6985  13617    349    459    614  B    N  
ATOM   2198  NH2 ARG B 300     -57.853  13.099  15.417  1.00 73.90      B    N  
ANISOU 2198  NH2 ARG B 300     7457   7045  13576    414    737   1023  B    N  
ATOM   2199  N   GLN B 301     -60.725   6.654  19.311  1.00 47.66      B    N  
ANISOU 2199  N   GLN B 301     4699   4357   9052    663    435    242  B    N  
ATOM   2200  CA  GLN B 301     -61.196   6.637  20.691  1.00 28.11      B    C  
ANISOU 2200  CA  GLN B 301     2375   1813   6493    750    358    142  B    C  
ATOM   2201  C   GLN B 301     -61.003   5.272  21.283  1.00 31.42      B    C  
ANISOU 2201  C   GLN B 301     2758   2340   6839    749    278     64  B    C  
ATOM   2202  O   GLN B 301     -60.951   4.294  20.570  1.00 41.52      B    O  
ANISOU 2202  O   GLN B 301     3917   3754   8106    710    307     98  B    O  
ATOM   2203  CB  GLN B 301     -62.657   7.009  20.793  1.00 34.88      B    C  
ANISOU 2203  CB  GLN B 301     3324   2706   7223    882    451    237  B    C  
ATOM   2204  CG  GLN B 301     -63.012   8.300  20.158  1.00 32.62      B    C  
ANISOU 2204  CG  GLN B 301     3053   2326   7014    897    556    350  B    C  
ATOM   2205  CD  GLN B 301     -62.488   9.474  20.937  1.00 47.70      B    C  
ANISOU 2205  CD  GLN B 301     5075   3990   9058    898    494    244  B    C  
ATOM   2206  NE2 GLN B 301     -61.784  10.326  20.253  1.00 31.65      B    N  
ANISOU 2206  NE2 GLN B 301     2965   1838   7224    811    518    296  B    N  
ATOM   2207  OE1 GLN B 301     -62.723   9.622  22.135  1.00 51.24      B    O  
ANISOU 2207  OE1 GLN B 301     5669   4361   9439    984    423    118  B    O  
ATOM   2208  N   ALA B 302     -60.891   5.225  22.599  1.00 33.42      B    N  
ANISOU 2208  N   ALA B 302     3107   2539   7051    800    177    -42  B    N  
ATOM   2209  CA  ALA B 302     -60.820   3.961  23.286  1.00 40.11      B    C  
ANISOU 2209  CA  ALA B 302     3903   3500   7837    822    110    -79  B    C  
ATOM   2210  C   ALA B 302     -62.087   3.174  22.968  1.00 45.05      B    C  
ANISOU 2210  C   ALA B 302     4493   4273   8352    912    188     37  B    C  
ATOM   2211  O   ALA B 302     -62.007   2.005  22.589  1.00 38.99      B    O  
ANISOU 2211  O   ALA B 302     3599   3607   7609    873    186     57  B    O  
ATOM   2212  CB  ALA B 302     -60.629   4.154  24.804  1.00 30.79      B    C  
ANISOU 2212  CB  ALA B 302     2830   2276   6593    892     -3   -191  B    C  
ATOM   2213  N   ILE B 303     -63.256   3.806  23.071  1.00 44.57      B    N  
ANISOU 2213  N   ILE B 303     4532   4214   8190   1028    258    120  B    N  
ATOM   2214  CA  ILE B 303     -64.498   3.060  22.819  1.00 29.77      B    C  
ANISOU 2214  CA  ILE B 303     2611   2478   6222   1110    319    254  B    C  
ATOM   2215  C   ILE B 303     -64.599   2.537  21.378  1.00 33.62      B    C  
ANISOU 2215  C   ILE B 303     2966   3058   6752   1019    381    316  B    C  
ATOM   2216  O   ILE B 303     -64.986   1.419  21.178  1.00 31.04      B    O  
ANISOU 2216  O   ILE B 303     2540   2835   6420   1020    367    348  B    O  
ATOM   2217  CB  ILE B 303     -65.791   3.801  23.284  1.00 30.55      B    C  
ANISOU 2217  CB  ILE B 303     2838   2576   6197   1271    388    361  B    C  
ATOM   2218  CG1 ILE B 303     -66.970   2.846  23.276  1.00 30.92      B    C  
ANISOU 2218  CG1 ILE B 303     2815   2767   6165   1357    417    514  B    C  
ATOM   2219  CG2 ILE B 303     -66.059   5.077  22.462  1.00 25.98      B    C  
ANISOU 2219  CG2 ILE B 303     2317   1912   5643   1256    492    421  B    C  
ATOM   2220  CD1 ILE B 303     -66.787   1.630  24.214  1.00 31.18      B    C  
ANISOU 2220  CD1 ILE B 303     2769   2875   6202   1397    321    494  B    C  
ATOM   2221  N   THR B 304     -64.207   3.305  20.369  1.00 30.66      B    N  
ANISOU 2221  N   THR B 304     2572   2650   6428    942    444    329  B    N  
ATOM   2222  CA  THR B 304     -64.243   2.757  19.000  1.00 25.33      B    C  
ANISOU 2222  CA  THR B 304     1760   2105   5758    871    497    371  B    C  
ATOM   2223  C   THR B 304     -63.215   1.624  18.835  1.00 35.82      B    C  
ANISOU 2223  C   THR B 304     2974   3465   7170    782    429    253  B    C  
ATOM   2224  O   THR B 304     -63.494   0.611  18.193  1.00 41.04      B    O  
ANISOU 2224  O   THR B 304     3532   4243   7819    763    432    244  B    O  
ATOM   2225  CB  THR B 304     -64.028   3.858  17.892  1.00 24.91      B    C  
ANISOU 2225  CB  THR B 304     1680   2050   5734    826    595    447  B    C  
ATOM   2226  CG2 THR B 304     -65.171   4.834  17.877  1.00 26.07      B    C  
ANISOU 2226  CG2 THR B 304     1909   2186   5812    915    686    592  B    C  
ATOM   2227  OG1 THR B 304     -62.819   4.590  18.166  1.00 40.69      B    O  
ANISOU 2227  OG1 THR B 304     3702   3898   7862    764    557    377  B    O  
ATOM   2228  N   ALA B 305     -62.025   1.806  19.408  1.00 28.97      B    N  
ANISOU 2228  N   ALA B 305     2120   2488   6397    727    365    160  B    N  
ATOM   2229  CA  ALA B 305     -60.963   0.810  19.333  1.00 27.72      B    C  
ANISOU 2229  CA  ALA B 305     1853   2345   6333    647    311     68  B    C  
ATOM   2230  C   ALA B 305     -61.402  -0.508  20.012  1.00 43.77      B    C  
ANISOU 2230  C   ALA B 305     3836   4432   8363    690    254     47  B    C  
ATOM   2231  O   ALA B 305     -61.140  -1.599  19.493  1.00 40.38      B    O  
ANISOU 2231  O   ALA B 305     3283   4062   7995    648    251      2  B    O  
ATOM   2232  CB  ALA B 305     -59.672   1.353  19.953  1.00 24.66      B    C  
ANISOU 2232  CB  ALA B 305     1492   1828   6049    581    243      2  B    C  
ATOM   2233  N   ALA B 306     -62.062  -0.403  21.168  1.00 31.66      B    N  
ANISOU 2233  N   ALA B 306     2385   2876   6769    784    215     84  B    N  
ATOM   2234  CA  ALA B 306     -62.661  -1.564  21.840  1.00 33.93      B    C  
ANISOU 2234  CA  ALA B 306     2604   3224   7062    850    173    122  B    C  
ATOM   2235  C   ALA B 306     -63.651  -2.263  20.906  1.00 39.43      B    C  
ANISOU 2235  C   ALA B 306     3218   4013   7752    860    216    183  B    C  
ATOM   2236  O   ALA B 306     -63.562  -3.452  20.679  1.00 24.95      B    O  
ANISOU 2236  O   ALA B 306     1253   2210   6018    827    187    152  B    O  
ATOM   2237  CB  ALA B 306     -63.393  -1.140  23.138  1.00 23.06      B    C  
ANISOU 2237  CB  ALA B 306     1334   1845   5583    986    146    192  B    C  
ATOM   2238  N   GLY B 307     -64.612  -1.518  20.372  1.00 34.36      B    N  
ANISOU 2238  N   GLY B 307     2644   3408   7002    903    282    270  B    N  
ATOM   2239  CA  GLY B 307     -65.528  -2.081  19.404  1.00 24.66      B    C  
ANISOU 2239  CA  GLY B 307     1335   2281   5753    897    311    324  B    C  
ATOM   2240  C   GLY B 307     -64.816  -2.859  18.293  1.00 32.96      B    C  
ANISOU 2240  C   GLY B 307     2261   3379   6882    792    307    198  B    C  
ATOM   2241  O   GLY B 307     -65.203  -3.971  17.952  1.00 33.49      B    O  
ANISOU 2241  O   GLY B 307     2219   3493   7011    779    269    167  B    O  
ATOM   2242  N   SER B 308     -63.782  -2.254  17.722  1.00 30.41      B    N  
ANISOU 2242  N   SER B 308     1951   3042   6563    726    344    126  B    N  
ATOM   2243  CA  SER B 308     -63.038  -2.858  16.615  1.00 30.66      B    C  
ANISOU 2243  CA  SER B 308     1870   3140   6640    650    360     13  B    C  
ATOM   2244  C   SER B 308     -62.304  -4.128  17.065  1.00 40.83      B    C  
ANISOU 2244  C   SER B 308     3063   4371   8081    617    294    -96  B    C  
ATOM   2245  O   SER B 308     -62.170  -5.070  16.308  1.00 40.93      B    O  
ANISOU 2245  O   SER B 308     2970   4436   8146    586    290   -197  B    O  
ATOM   2246  CB  SER B 308     -62.045  -1.827  16.056  1.00 27.11      B    C  
ANISOU 2246  CB  SER B 308     1444   2683   6175    606    421     12  B    C  
ATOM   2247  OG  SER B 308     -61.116  -2.396  15.173  1.00 42.54      B    O  
ANISOU 2247  OG  SER B 308     3291   4698   8174    552    440    -88  B    O  
ATOM   2248  N   GLY B 309     -61.825  -4.150  18.297  1.00 34.07      B    N  
ANISOU 2248  N   GLY B 309     2236   3412   7296    629    245    -79  B    N  
ATOM   2249  CA  GLY B 309     -61.132  -5.320  18.788  1.00 41.10      B    C  
ANISOU 2249  CA  GLY B 309     3016   4254   8346    601    194   -144  B    C  
ATOM   2250  C   GLY B 309     -62.099  -6.474  18.890  1.00 34.23      B    C  
ANISOU 2250  C   GLY B 309     2051   3405   7552    640    154   -125  B    C  
ATOM   2251  O   GLY B 309     -61.788  -7.587  18.508  1.00 37.55      B    O  
ANISOU 2251  O   GLY B 309     2353   3806   8106    598    137   -215  B    O  
ATOM   2252  N   CYS B 310     -63.282  -6.203  19.407  1.00 38.78      B    N  
ANISOU 2252  N   CYS B 310     2683   4001   8049    717    140      0  B    N  
ATOM   2253  CA  CYS B 310     -64.344  -7.191  19.407  1.00 31.49      B    C  
ANISOU 2253  CA  CYS B 310     1710   3081   7175    719     97     57  B    C  
ATOM   2254  C   CYS B 310     -64.574  -7.751  17.997  1.00 40.56      B    C  
ANISOU 2254  C   CYS B 310     2762   4290   8361    676    102    -65  B    C  
ATOM   2255  O   CYS B 310     -64.637  -8.964  17.808  1.00 54.26      B    O  
ANISOU 2255  O   CYS B 310     4390   5976  10250    637     51   -136  B    O  
ATOM   2256  CB  CYS B 310     -65.634  -6.600  19.957  1.00 39.69      B    C  
ANISOU 2256  CB  CYS B 310     2840   4156   8084    804    101    236  B    C  
ATOM   2257  SG  CYS B 310     -67.073  -7.718  19.828  1.00 38.37      B    S  
ANISOU 2257  SG  CYS B 310     2589   3997   7992    804     46    348  B    S  
ATOM   2258  N   MET B 311     -64.687  -6.871  17.007  1.00 38.97      B    N  
ANISOU 2258  N   MET B 311     2605   4191   8010    675    162    -91  B    N  
ATOM   2259  CA  MET B 311     -64.838  -7.290  15.604  1.00 33.87      B    C  
ANISOU 2259  CA  MET B 311     1892   3645   7331    628    170   -220  B    C  
ATOM   2260  C   MET B 311     -63.706  -8.205  15.123  1.00 43.26      B    C  
ANISOU 2260  C   MET B 311     2982   4803   8654    575    163   -417  B    C  
ATOM   2261  O   MET B 311     -63.949  -9.216  14.486  1.00 40.26      B    O  
ANISOU 2261  O   MET B 311     2501   4437   8359    555    119   -548  B    O  
ATOM   2262  CB  MET B 311     -64.941  -6.068  14.690  1.00 31.04      B    C  
ANISOU 2262  CB  MET B 311     1617   3416   6761    627    253   -182  B    C  
ATOM   2263  CG  MET B 311     -66.329  -5.424  14.706  1.00 44.54      B    C  
ANISOU 2263  CG  MET B 311     3384   5195   8343    676    265     -8  B    C  
ATOM   2264  SD  MET B 311     -66.287  -3.829  13.927  1.00 35.65      B    S  
ANISOU 2264  SD  MET B 311     2347   4185   7015    684    383     89  B    S  
ATOM   2265  CE  MET B 311     -67.897  -3.244  14.411  1.00 45.93      B    C  
ANISOU 2265  CE  MET B 311     3718   5507   8228    759    396    321  B    C  
ATOM   2266  N   ALA B 312     -62.469  -7.828  15.423  1.00 36.35      B    N  
ANISOU 2266  N   ALA B 312     2135   3877   7799    554    205   -437  B    N  
ATOM   2267  CA  ALA B 312     -61.329  -8.629  15.057  1.00 37.54      B    C  
ANISOU 2267  CA  ALA B 312     2194   3993   8077    515    217   -590  B    C  
ATOM   2268  C   ALA B 312     -61.448 -10.043  15.640  1.00 49.17      B    C  
ANISOU 2268  C   ALA B 312     3539   5350   9793    513    147   -639  B    C  
ATOM   2269  O   ALA B 312     -61.251 -11.007  14.926  1.00 45.33      B    O  
ANISOU 2269  O   ALA B 312     2954   4856   9413    495    137   -804  B    O  
ATOM   2270  CB  ALA B 312     -60.055  -7.975  15.505  1.00 41.05      B    C  
ANISOU 2270  CB  ALA B 312     2680   4387   8531    490    260   -552  B    C  
ATOM   2271  N   ALA B 313     -61.788 -10.186  16.919  1.00 43.48      B    N  
ANISOU 2271  N   ALA B 313     2847   4527   9146    524     98   -494  B    N  
ATOM   2272  CA  ALA B 313     -62.004 -11.528  17.478  1.00 38.39      B    C  
ANISOU 2272  CA  ALA B 313     2112   3750   8725    503     34   -492  B    C  
ATOM   2273  C   ALA B 313     -63.080 -12.318  16.720  1.00 50.32      B    C  
ANISOU 2273  C   ALA B 313     3524   5275  10319    512    -23   -571  B    C  
ATOM   2274  O   ALA B 313     -62.830 -13.446  16.264  1.00 44.34      B    O  
ANISOU 2274  O   ALA B 313     2630   4448   9768    489    -50   -726  B    O  
ATOM   2275  CB  ALA B 313     -62.344 -11.467  18.944  1.00 40.92      B    C  
ANISOU 2275  CB  ALA B 313     2490   3999   9059    521     -0   -286  B    C  
ATOM   2276  N   LEU B 314     -64.269 -11.733  16.571  1.00 27.31      B    N  
ANISOU 2276  N   LEU B 314      665   2450   7261    546    -44   -470  B    N  
ATOM   2277  CA  LEU B 314     -65.348 -12.447  15.887  1.00 44.21      B    C  
ANISOU 2277  CA  LEU B 314     2697   4613   9486    547   -119   -527  B    C  
ATOM   2278  C   LEU B 314     -64.998 -12.739  14.413  1.00 53.70      B    C  
ANISOU 2278  C   LEU B 314     3840   5914  10651    517   -112   -796  B    C  
ATOM   2279  O   LEU B 314     -65.315 -13.810  13.903  1.00 56.14      B    O  
ANISOU 2279  O   LEU B 314     4031   6167  11131    490   -188   -948  B    O  
ATOM   2280  CB  LEU B 314     -66.719 -11.730  16.021  1.00 26.73      B    C  
ANISOU 2280  CB  LEU B 314      557   2485   7112    589   -140   -331  B    C  
ATOM   2281  CG  LEU B 314     -67.175 -11.426  17.458  1.00 41.83      B    C  
ANISOU 2281  CG  LEU B 314     2571   4317   9004    624   -138    -65  B    C  
ATOM   2282  CD1 LEU B 314     -68.553 -10.896  17.484  1.00 25.15      B    C  
ANISOU 2282  CD1 LEU B 314      506   2284   6766    672   -151    122  B    C  
ATOM   2283  CD2 LEU B 314     -67.088 -12.611  18.375  1.00 36.89      B    C  
ANISOU 2283  CD2 LEU B 314     1855   3525   8635    603   -194     -1  B    C  
ATOM   2284  N   ASP B 315     -64.338 -11.805  13.732  1.00 39.49      B    N  
ANISOU 2284  N   ASP B 315     2147   4240   8618    512    -23   -852  B    N  
ATOM   2285  CA  ASP B 315     -63.929 -12.053  12.353  1.00 43.09      B    C  
ANISOU 2285  CA  ASP B 315     2579   4811   8983    492      0  -1092  B    C  
ATOM   2286  C   ASP B 315     -63.044 -13.271  12.230  1.00 48.06      B    C  
ANISOU 2286  C   ASP B 315     3095   5318   9847    477    -13  -1299  B    C  
ATOM   2287  O   ASP B 315     -63.215 -14.052  11.277  1.00 52.53      B    O  
ANISOU 2287  O   ASP B 315     3594   5917  10449    469    -58  -1531  B    O  
ATOM   2288  CB  ASP B 315     -63.211 -10.838  11.764  1.00 28.10      B    C  
ANISOU 2288  CB  ASP B 315      783   3067   6825    505    113  -1066  B    C  
ATOM   2289  CG  ASP B 315     -64.183  -9.742  11.372  1.00 44.13      B    C  
ANISOU 2289  CG  ASP B 315     2896   5258   8611    522    134   -921  B    C  
ATOM   2290  OD1 ASP B 315     -65.412 -10.033  11.386  1.00 36.21      B    O  
ANISOU 2290  OD1 ASP B 315     1870   4269   7621    520     55   -875  B    O  
ATOM   2291  OD2 ASP B 315     -63.715  -8.616  11.052  1.00 45.94      B    O  
ANISOU 2291  OD2 ASP B 315     3199   5593   8663    536    229   -839  B    O  
ATOM   2292  N   ALA B 316     -62.121 -13.411  13.196  1.00 31.50      B    N  
ANISOU 2292  N   ALA B 316      975   3085   7907    476     26  -1218  B    N  
ATOM   2293  CA  ALA B 316     -61.099 -14.450  13.215  1.00 40.42      B    C  
ANISOU 2293  CA  ALA B 316     1996   4090   9272    467     44  -1365  B    C  
ATOM   2294  C   ALA B 316     -61.754 -15.762  13.586  1.00 53.41      B    C  
ANISOU 2294  C   ALA B 316     3490   5566  11235    456    -56  -1410  B    C  
ATOM   2295  O   ALA B 316     -61.462 -16.826  13.034  1.00 66.64      B    O  
ANISOU 2295  O   ALA B 316     5062   7157  13102    449    -77  -1630  B    O  
ATOM   2296  CB  ALA B 316     -59.997 -14.108  14.235  1.00 39.36      B    C  
ANISOU 2296  CB  ALA B 316     1873   3881   9202    462    110  -1212  B    C  
ATOM   2297  N   GLU B 317     -62.638 -15.679  14.558  1.00 47.83      B    N  
ANISOU 2297  N   GLU B 317     2764   4806  10601    465   -117  -1189  B    N  
ATOM   2298  CA  GLU B 317     -63.394 -16.827  14.969  1.00 50.13      B    C  
ANISOU 2298  CA  GLU B 317     2896   4942  11208    459   -220  -1167  B    C  
ATOM   2299  C   GLU B 317     -64.185 -17.359  13.774  1.00 57.02      B    C  
ANISOU 2299  C   GLU B 317     3731   5844  12091    434   -309  -1396  B    C  
ATOM   2300  O   GLU B 317     -64.251 -18.569  13.538  1.00 61.99      B    O  
ANISOU 2300  O   GLU B 317     4212   6320  13020    412   -380  -1559  B    O  
ATOM   2301  CB  GLU B 317     -64.320 -16.433  16.105  1.00 37.79      B    C  
ANISOU 2301  CB  GLU B 317     1434   3331   9594    461   -259   -857  B    C  
ATOM   2302  CG  GLU B 317     -65.238 -17.547  16.483  1.00 70.33      B    C  
ANISOU 2302  CG  GLU B 317     5411   7287  14023    451   -367   -784  B    C  
ATOM   2303  CD  GLU B 317     -66.011 -17.250  17.733  1.00 87.56      B    C  
ANISOU 2303  CD  GLU B 317     7676   9427  16165    469   -380   -443  B    C  
ATOM   2304  OE1 GLU B 317     -65.984 -16.084  18.206  1.00 76.07      B    O  
ANISOU 2304  OE1 GLU B 317     6397   8093  14413    495   -317   -298  B    O  
ATOM   2305  OE2 GLU B 317     -66.641 -18.201  18.239  1.00 91.86      B    O  
ANISOU 2305  OE2 GLU B 317     8091   9818  16994    463   -453   -321  B    O  
ATOM   2306  N   HIS B 318     -64.763 -16.441  13.009  1.00 45.60      B    N  
ANISOU 2306  N   HIS B 318     2416   4594  10317    433   -306  -1412  B    N  
ATOM   2307  CA  HIS B 318     -65.547 -16.796  11.818  1.00 51.25      B    C  
ANISOU 2307  CA  HIS B 318     3110   5394  10970    407   -397  -1625  B    C  
ATOM   2308  C   HIS B 318     -64.666 -17.344  10.697  1.00 63.82      B    C  
ANISOU 2308  C   HIS B 318     4684   7020  12544    406   -369  -1979  B    C  
ATOM   2309  O   HIS B 318     -65.075 -18.215   9.930  1.00 73.11      B    O  
ANISOU 2309  O   HIS B 318     5782   8165  13833    386   -470  -2231  B    O  
ATOM   2310  CB  HIS B 318     -66.339 -15.587  11.324  1.00 59.14      B    C  
ANISOU 2310  CB  HIS B 318     4240   6626  11605    415   -382  -1510  B    C  
ATOM   2311  CG  HIS B 318     -67.175 -15.864  10.119  1.00 77.04      B    C  
ANISOU 2311  CG  HIS B 318     6482   9023  13769    385   -480  -1703  B    C  
ATOM   2312  CD2 HIS B 318     -68.431 -16.354   9.998  1.00 91.86      B    C  
ANISOU 2312  CD2 HIS B 318     8278  10871  15754    349   -625  -1682  B    C  
ATOM   2313  ND1 HIS B 318     -66.725 -15.641   8.832  1.00 76.26      B    N  
ANISOU 2313  ND1 HIS B 318     6430   9128  13418    396   -440  -1949  B    N  
ATOM   2314  CE1 HIS B 318     -67.668 -15.982   7.974  1.00 85.02      B    C  
ANISOU 2314  CE1 HIS B 318     7495  10342  14469    366   -560  -2092  B    C  
ATOM   2315  NE2 HIS B 318     -68.713 -16.417   8.654  1.00 95.33      B    N  
ANISOU 2315  NE2 HIS B 318     8723  11497  16001    329   -680  -1934  B    N  
ATOM   2316  N   TYR B 319     -63.445 -16.842  10.616  1.00 58.41      B    N  
ANISOU 2316  N   TYR B 319     4071   6398  11726    436   -234  -1997  B    N  
ATOM   2317  CA  TYR B 319     -62.489 -17.329   9.640  1.00 61.70      B    C  
ANISOU 2317  CA  TYR B 319     4468   6857  12118    462   -180  -2297  B    C  
ATOM   2318  C   TYR B 319     -61.888 -18.677  10.021  1.00 61.67      B    C  
ANISOU 2318  C   TYR B 319     4322   6595  12517    457   -197  -2435  B    C  
ATOM   2319  O   TYR B 319     -61.461 -19.422   9.147  1.00 68.18      B    O  
ANISOU 2319  O   TYR B 319     5101   7409  13397    482   -197  -2743  B    O  
ATOM   2320  CB  TYR B 319     -61.367 -16.320   9.475  1.00 49.79      B    C  
ANISOU 2320  CB  TYR B 319     3063   5495  10359    500    -26  -2218  B    C  
ATOM   2321  CG  TYR B 319     -60.160 -16.892   8.801  1.00 47.67      B    C  
ANISOU 2321  CG  TYR B 319     2754   5230  10128    545     57  -2452  B    C  
ATOM   2322  CD1 TYR B 319     -59.984 -16.745   7.439  1.00 52.75      B    C  
ANISOU 2322  CD1 TYR B 319     3429   6104  10509    603     93  -2676  B    C  
ATOM   2323  CD2 TYR B 319     -59.188 -17.561   9.519  1.00 52.00      B    C  
ANISOU 2323  CD2 TYR B 319     3223   5572  10960    544    109  -2431  B    C  
ATOM   2324  CE1 TYR B 319     -58.878 -17.231   6.816  1.00 50.68      B    C  
ANISOU 2324  CE1 TYR B 319     3133   5864  10258    668    182  -2878  B    C  
ATOM   2325  CE2 TYR B 319     -58.051 -18.057   8.895  1.00 53.46      B    C  
ANISOU 2325  CE2 TYR B 319     3373   5763  11177    598    203  -2626  B    C  
ATOM   2326  CZ  TYR B 319     -57.912 -17.888   7.539  1.00 55.73      B    C  
ANISOU 2326  CZ  TYR B 319     3703   6278  11194    666    241  -2852  B    C  
ATOM   2327  OH  TYR B 319     -56.823 -18.384   6.877  1.00 61.93      B    O  
ANISOU 2327  OH  TYR B 319     4453   7088  11989    744    341  -3045  B    O  
ATOM   2328  N   LEU B 320     -61.819 -18.974  11.317  1.00 60.05      B    N  
ANISOU 2328  N   LEU B 320     4038   6192  12587    438   -202  -2206  B    N  
ATOM   2329  CA  LEU B 320     -61.332 -20.285  11.759  1.00 60.88      B    C  
ANISOU 2329  CA  LEU B 320     3971   6041  13121    432   -216  -2288  B    C  
ATOM   2330  C   LEU B 320     -62.345 -21.335  11.385  1.00 63.89      B    C  
ANISOU 2330  C   LEU B 320     4229   6285  13762    404   -370  -2465  B    C  
ATOM   2331  O   LEU B 320     -61.988 -22.438  11.004  1.00 77.30      B    O  
ANISOU 2331  O   LEU B 320     5811   7819  15740    407   -392  -2714  B    O  
ATOM   2332  CB  LEU B 320     -61.092 -20.336  13.269  1.00 40.70      B    C  
ANISOU 2332  CB  LEU B 320     1333   3346  10785    427   -188  -1962  B    C  
ATOM   2333  CG  LEU B 320     -59.842 -19.569  13.683  1.00 48.86      B    C  
ANISOU 2333  CG  LEU B 320     2451   4459  11655    444    -48  -1834  B    C  
ATOM   2334  CD1 LEU B 320     -59.749 -19.419  15.188  1.00 49.07      B    C  
ANISOU 2334  CD1 LEU B 320     2446   4399  11800    431    -40  -1503  B    C  
ATOM   2335  CD2 LEU B 320     -58.643 -20.321  13.137  1.00 35.60      B    C  
ANISOU 2335  CD2 LEU B 320      703   2699  10123    461     38  -2050  B    C  
ATOM   2336  N   GLN B 321     -63.618 -20.981  11.488  1.00 61.76      B    N  
ANISOU 2336  N   GLN B 321     3978   6075  13412    377   -480  -2333  B    N  
ATOM   2337  CA  GLN B 321     -64.681 -21.944  11.239  1.00 73.94      B    C  
ANISOU 2337  CA  GLN B 321     5385   7475  15236    336   -652  -2452  B    C  
ATOM   2338  C   GLN B 321     -64.791 -22.295   9.759  1.00 79.89      B    C  
ANISOU 2338  C   GLN B 321     6173   8320  15861    330   -719  -2873  B    C  
ATOM   2339  O   GLN B 321     -65.276 -23.357   9.414  1.00 86.48      B    O  
ANISOU 2339  O   GLN B 321     6878   8983  16997    297   -857  -3089  B    O  
ATOM   2340  CB  GLN B 321     -66.023 -21.428  11.770  1.00 57.52      B    C  
ANISOU 2340  CB  GLN B 321     3310   5450  13096    316   -746  -2157  B    C  
ATOM   2341  CG  GLN B 321     -66.085 -21.349  13.296  1.00 57.45      B    C  
ANISOU 2341  CG  GLN B 321     3221   5330  13278    342   -710  -1759  B    C  
ATOM   2342  CD  GLN B 321     -67.286 -20.532  13.784  1.00 79.94      B    C  
ANISOU 2342  CD  GLN B 321     6125   8298  15950    354   -758  -1446  B    C  
ATOM   2343  NE2 GLN B 321     -67.462 -20.474  15.104  1.00 65.85      B    N  
ANISOU 2343  NE2 GLN B 321     4280   6439  14299    395   -734  -1100  B    N  
ATOM   2344  OE1 GLN B 321     -68.032 -19.949  12.984  1.00 81.55      B    O  
ANISOU 2344  OE1 GLN B 321     6433   8670  15882    334   -806  -1508  B    O  
ATOM   2345  N   GLU B 322     -64.340 -21.397   8.893  1.00 84.87      B    N  
ANISOU 2345  N   GLU B 322     6967   9228  16052    368   -626  -2985  B    N  
ATOM   2346  CA  GLU B 322     -64.395 -21.628   7.456  1.00 80.69      B    C  
ANISOU 2346  CA  GLU B 322     6474   8856  15328    386   -676  -3377  B    C  
ATOM   2347  C   GLU B 322     -63.057 -22.170   6.963  1.00 90.62      B    C  
ANISOU 2347  C   GLU B 322     7723  10075  16633    453   -561  -3653  B    C  
ATOM   2348  O   GLU B 322     -62.684 -21.973   5.812  1.00104.67      B    O  
ANISOU 2348  O   GLU B 322     9578  12079  18113    513   -520  -3918  B    O  
ATOM   2349  CB  GLU B 322     -64.744 -20.328   6.726  1.00 83.03      B    C  
ANISOU 2349  CB  GLU B 322     6924   9520  15104    407   -633  -3308  B    C  
ATOM   2350  CG  GLU B 322     -66.041 -19.706   7.209  1.00101.27      B    C  
ANISOU 2350  CG  GLU B 322     9251  11880  17346    353   -722  -3009  B    C  
ATOM   2351  CD  GLU B 322     -66.406 -18.441   6.456  1.00116.84      B    C  
ANISOU 2351  CD  GLU B 322    11353  14207  18833    374   -670  -2928  B    C  
ATOM   2352  OE1 GLU B 322     -65.508 -17.593   6.246  1.00114.34      B    O  
ANISOU 2352  OE1 GLU B 322    11134  14057  18254    430   -509  -2872  B    O  
ATOM   2353  OE2 GLU B 322     -67.596 -18.295   6.083  1.00120.25      B    O  
ANISOU 2353  OE2 GLU B 322    11774  14749  19168    333   -791  -2896  B    O  
ATOM   2354  N   VAL B 323     -62.341 -22.868   7.835  1.00 85.69      B    N  
ANISOU 2354  N   VAL B 323     6994   9179  16385    453   -505  -3575  B    N  
ATOM   2355  CA  VAL B 323     -60.975 -23.263   7.532  1.00 92.56      B    C  
ANISOU 2355  CA  VAL B 323     7858  10009  17302    523   -363  -3754  B    C  
ATOM   2356  C   VAL B 323     -60.501 -24.427   8.399  1.00 93.04      B    C  
ANISOU 2356  C   VAL B 323     7740   9710  17900    507   -352  -3725  B    C  
ATOM   2357  O   VAL B 323     -61.114 -25.496   8.402  1.00 88.34      B    O  
ANISOU 2357  O   VAL B 323     7004   8881  17680    472   -487  -3884  B    O  
ATOM   2358  CB  VAL B 323     -60.023 -22.064   7.710  1.00 85.56      B    C  
ANISOU 2358  CB  VAL B 323     7099   9333  16077    566   -181  -3521  B    C  
ATOM   2359  CG1 VAL B 323     -58.752 -22.493   8.419  1.00 86.22      B    C  
ANISOU 2359  CG1 VAL B 323     7110   9235  16416    590    -47  -3426  B    C  
ATOM   2360  CG2 VAL B 323     -59.717 -21.421   6.365  1.00 81.19      B    C  
ANISOU 2360  CG2 VAL B 323     6667   9108  15073    643   -118  -3730  B    C  
TER   
HETATM 2361  P   FAD B 400     -55.635   0.797  20.700  1.00 29.22      F    P  
HETATM 2362  PA  FAD B 400     -53.175   1.719  21.905  1.00 31.73      F    P  
HETATM 2363  O1P FAD B 400     -55.776   0.953  19.211  1.00 26.51      F    O  
HETATM 2364  O2P FAD B 400     -56.225  -0.381  21.387  1.00 40.91      F    O  
HETATM 2365  O3P FAD B 400     -54.078   0.741  21.017  1.00 44.29      F    O  
HETATM 2366  C5' FAD B 400     -56.488   3.327  20.791  1.00 27.15      F    C  
HETATM 2367  O5' FAD B 400     -56.204   2.091  21.437  1.00 38.55      F    O  
HETATM 2368  C4' FAD B 400     -56.879   4.201  21.996  1.00 38.04      F    C  
HETATM 2369  O4' FAD B 400     -56.007   3.876  23.093  1.00 27.28      F    O  
HETATM 2370  C3' FAD B 400     -56.860   5.700  21.690  1.00 28.93      F    C  
HETATM 2371  O3' FAD B 400     -57.751   5.957  20.602  1.00 34.97      F    O  
HETATM 2372  C2' FAD B 400     -57.238   6.565  22.889  1.00 34.09      F    C  
HETATM 2373  O2' FAD B 400     -56.267   6.359  23.922  1.00 42.52      F    O  
HETATM 2374  C1' FAD B 400     -57.364   8.073  22.579  1.00 22.98      F    C  
HETATM 2375  C1B FAD B 400     -48.397  -2.098  22.482  1.00 49.80      F    C  
HETATM 2376  N1  FAD B 400     -59.793   8.187  23.917  1.00 37.57      F    N  
HETATM 2377  N1A FAD B 400     -45.489  -5.715  20.391  1.00 45.86      F    N  
HETATM 2378  O1A FAD B 400     -53.704   2.240  23.216  1.00 36.16      F    O  
HETATM 2379  C2  FAD B 400     -60.998   8.168  24.507  1.00 33.95      F    C  
HETATM 2380  C2A FAD B 400     -46.142  -5.748  21.554  1.00 38.69      F    C  
HETATM 2381  C2B FAD B 400     -48.033  -0.684  22.874  1.00 41.54      F    C  
HETATM 2382  O2  FAD B 400     -61.910   7.508  23.970  1.00 49.12      F    O  
HETATM 2383  O2A FAD B 400     -52.563   2.596  20.843  1.00 30.60      F    O  
HETATM 2384  O2B FAD B 400     -47.111  -0.728  23.963  1.00 59.17      F    O  
HETATM 2385  C3B FAD B 400     -49.328  -0.113  23.368  1.00 48.17      F    C  
HETATM 2386  N3  FAD B 400     -61.214   8.865  25.650  1.00 29.29      F    N  
HETATM 2387  N3A FAD B 400     -46.868  -4.706  21.954  1.00 41.56      F    N  
HETATM 2388  O3B FAD B 400     -49.417  -0.365  24.775  1.00 51.19      F    O  
HETATM 2389  C4  FAD B 400     -60.234   9.610  26.204  1.00 32.37      F    C  
HETATM 2390  C4A FAD B 400     -46.942  -3.609  21.177  1.00 44.42      F    C  
HETATM 2391  C4B FAD B 400     -50.401  -0.944  22.692  1.00 51.64      F    C  
HETATM 2392  C4X FAD B 400     -58.966   9.618  25.611  1.00 35.57      F    C  
HETATM 2393  O4  FAD B 400     -60.454  10.236  27.269  1.00 30.23      F    O  
HETATM 2394  O4B FAD B 400     -49.778  -2.098  22.131  1.00 52.92      F    O  
HETATM 2395  C5A FAD B 400     -46.270  -3.550  19.968  1.00 27.35      F    C  
HETATM 2396  C5B FAD B 400     -51.185  -0.107  21.683  1.00 33.70      F    C  
HETATM 2397  C5X FAD B 400     -56.741  10.304  25.549  1.00 50.04      F    C  
HETATM 2398  N5  FAD B 400     -57.944  10.320  26.160  1.00 46.87      F    N  
HETATM 2399  O5B FAD B 400     -52.153   0.611  22.467  1.00 46.43      F    O  
HETATM 2400  C6  FAD B 400     -55.677  11.004  26.109  1.00 42.47      F    C  
HETATM 2401  C6A FAD B 400     -45.522  -4.634  19.590  1.00 29.80      F    C  
HETATM 2402  N6A FAD B 400     -44.849  -4.609  18.419  1.00 34.52      F    N  
HETATM 2403  C7  FAD B 400     -54.438  10.984  25.469  1.00 43.03      F    C  
HETATM 2404  C7M FAD B 400     -53.264  11.741  26.026  1.00 27.42      F    C  
HETATM 2405  N7A FAD B 400     -46.528  -2.351  19.398  1.00 38.15      F    N  
HETATM 2406  C8  FAD B 400     -54.267  10.257  24.313  1.00 51.61      F    C  
HETATM 2407  C8A FAD B 400     -47.332  -1.681  20.254  1.00 47.51      F    C  
HETATM 2408  C8M FAD B 400     -52.920  10.203  23.635  1.00 31.81      F    C  
HETATM 2409  C9  FAD B 400     -55.330   9.554  23.764  1.00 42.06      F    C  
HETATM 2410  C9A FAD B 400     -56.563   9.572  24.373  1.00 36.84      F    C  
HETATM 2411  N9A FAD B 400     -47.567  -2.448  21.330  1.00 48.19      F    N  
HETATM 2412  C10 FAD B 400     -58.761   8.886  24.443  1.00 30.66      F    C  
HETATM 2413  N10 FAD B 400     -57.560   8.854  23.835  1.00 42.75      F    N  
HETATM 2414  O   HOH B2001     -44.874  -1.724  30.469  1.00 44.90      J    O  
HETATM 2415  O   HOH B2002     -54.980   2.975  25.682  1.00 32.20      J    O  
HETATM 2416  O   HOH B2003     -65.515   7.349  31.322  1.00 41.96      J    O  
HETATM 2417  O   HOH B2004     -62.563  11.620  28.608  1.00 47.45      J    O  
HETATM 2418  O   HOH B2005     -68.304   2.317  36.581  1.00 49.65      J    O  
HETATM 2419  O   HOH B2006     -53.963  -7.829  34.708  1.00 59.69      J    O  
HETATM 2420  O   HOH B2007     -57.425 -11.453  36.436  1.00 50.14      J    O  
HETATM 2421  O   HOH B2008     -39.722  -3.036  23.647  1.00 51.01      J    O  
HETATM 2422  O   HOH B2009     -54.650  -2.654  21.323  1.00 45.72      J    O  
HETATM 2423  O   HOH B2010     -54.330   7.630  18.029  1.00 53.55      J    O  
HETATM 2424  O   HOH B2011     -46.054  -2.374  25.834  1.00 45.39      J    O  
HETATM 2425  O   HOH B2012     -54.830  -0.366  17.249  1.00 40.99      J    O  
HETATM 2426  O   HOH B2013     -64.076   6.127  24.875  1.00 32.91      J    O  
HETATM 2427  O   HOH B2014     -58.363  11.798  28.634  1.00 39.62      J    O  
CONECT 2361 2363 2364 2365 2367
CONECT 2362 2365 2378 2383 2399
CONECT 2363 2361
CONECT 2364 2361
CONECT 2365 2361 2362
CONECT 2366 2367 2368
CONECT 2367 2361 2366
CONECT 2368 2366 2369 2370
CONECT 2369 2368
CONECT 2370 2368 2371 2372
CONECT 2371 2370
CONECT 2372 2370 2373 2374
CONECT 2373 2372
CONECT 2374 2372 2413
CONECT 2375 2381 2394 2411
CONECT 2376 2379 2412
CONECT 2377 2380 2401
CONECT 2378 2362
CONECT 2379 2376 2382 2386
CONECT 2380 2377 2387
CONECT 2381 2375 2384 2385
CONECT 2382 2379
CONECT 2383 2362
CONECT 2384 2381
CONECT 2385 2381 2388 2391
CONECT 2386 2379 2389
CONECT 2387 2380 2390
CONECT 2388 2385
CONECT 2389 2386 2392 2393
CONECT 2390 2387 2395 2411
CONECT 2391 2385 2394 2396
CONECT 2392 2389 2398 2412
CONECT 2393 2389
CONECT 2394 2375 2391
CONECT 2395 2390 2401 2405
CONECT 2396 2391 2399
CONECT 2397 2398 2400 2410
CONECT 2398 2392 2397
CONECT 2399 2362 2396
CONECT 2400 2397 2403
CONECT 2401 2377 2395 2402
CONECT 2402 2401
CONECT 2403 2400 2404 2406
CONECT 2404 2403
CONECT 2405 2395 2407
CONECT 2406 2403 2408 2409
CONECT 2407 2405 2411
CONECT 2408 2406
CONECT 2409 2406 2410
CONECT 2410 2397 2409 2413
CONECT 2411 2375 2390 2407
CONECT 2412 2376 2392 2413
CONECT 2413 2374 2410 2412
END



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.