CNRS Nantes University UFIP UFIP
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***    ***

elNémo ID: 22050420564918830

Job options:

ID        	=	 22050420564918830
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


CRYST1   80.651   80.651  150.120  90.00  90.00  90.00 P 43 21 2     8
ATOM      1  N   TYR A 572     -33.930   5.615 -16.353  1.00 53.79      A    N  
ATOM      2  CA  TYR A 572     -33.118   5.159 -17.472  1.00 47.05      A    C  
ATOM      3  C   TYR A 572     -32.155   6.272 -17.826  1.00 34.51      A    C  
ATOM      4  O   TYR A 572     -32.510   7.456 -17.768  1.00 37.71      A    O  
ATOM      5  CB  TYR A 572     -33.940   4.885 -18.732  1.00 51.42      A    C  
ATOM      6  CG  TYR A 572     -33.047   4.642 -19.938  1.00 43.63      A    C  
ATOM      7  CD1 TYR A 572     -32.235   3.511 -19.995  1.00 32.83      A    C  
ATOM      8  CD2 TYR A 572     -32.979   5.557 -20.994  1.00 38.04      A    C  
ATOM      9  CE1 TYR A 572     -31.377   3.284 -21.060  1.00 43.51      A    C  
ATOM     10  CE2 TYR A 572     -32.116   5.339 -22.084  1.00 34.63      A    C  
ATOM     11  CZ  TYR A 572     -31.316   4.195 -22.106  1.00 37.73      A    C  
ATOM     12  OH  TYR A 572     -30.432   3.932 -23.132  1.00 34.65      A    O  
ATOM     13  N   GLU A 573     -30.947   5.882 -18.214  1.00 38.92      A    N  
ATOM     14  CA  GLU A 573     -29.935   6.837 -18.622  1.00 35.77      A    C  
ATOM     15  C   GLU A 573     -28.820   6.074 -19.326  1.00 35.50      A    C  
ATOM     16  O   GLU A 573     -28.406   5.012 -18.851  1.00 31.71      A    O  
ATOM     17  CB  GLU A 573     -29.382   7.554 -17.392  1.00 41.14      A    C  
ATOM     18  CG  GLU A 573     -28.532   8.770 -17.722  1.00 61.33      A    C  
ATOM     19  CD  GLU A 573     -27.986   9.461 -16.484  1.00 64.41      A    C  
ATOM     20  OE1 GLU A 573     -27.256  10.462 -16.635  1.00 77.64      A    O  
ATOM     21  OE2 GLU A 573     -28.288   9.006 -15.363  1.00 73.74      A    O1-
ATOM     22  N   SER A 574     -28.341   6.571 -20.463  1.00 29.83      A    N  
ATOM     23  CA  SER A 574     -27.242   5.867 -21.107  1.00 31.01      A    C  
ATOM     24  C   SER A 574     -26.003   6.166 -20.269  1.00 27.72      A    C  
ATOM     25  O   SER A 574     -25.838   7.275 -19.743  1.00 29.82      A    O  
ATOM     26  CB  SER A 574     -26.991   6.346 -22.544  1.00 38.07      A    C  
ATOM     27  OG  SER A 574     -25.893   5.623 -23.134  1.00 30.19      A    O  
ATOM     28  N   GLN A 575     -25.131   5.182 -20.152  1.00 22.86      A    N  
ATOM     29  CA  GLN A 575     -23.906   5.366 -19.393  1.00 25.74      A    C  
ATOM     30  C   GLN A 575     -22.837   5.929 -20.311  1.00 30.14      A    C  
ATOM     31  O   GLN A 575     -21.740   6.237 -19.874  1.00 25.98      A    O  
ATOM     32  CB  GLN A 575     -23.480   4.039 -18.754  1.00 26.92      A    C  
ATOM     33  CG  GLN A 575     -24.559   3.481 -17.817  1.00 24.47      A    C  
ATOM     34  CD  GLN A 575     -25.033   4.505 -16.784  1.00 33.51      A    C  
ATOM     35  NE2 GLN A 575     -24.107   5.289 -16.266  1.00 34.77      A    N  
ATOM     36  OE1 GLN A 575     -26.223   4.585 -16.465  1.00 44.25      A    O  
ATOM     37  N   LEU A 576     -23.165   6.056 -21.596  1.00 25.21      A    N  
ATOM     38  CA  LEU A 576     -22.228   6.649 -22.546  1.00 30.81      A    C  
ATOM     39  C   LEU A 576     -22.569   8.150 -22.439  1.00 25.46      A    C  
ATOM     40  O   LEU A 576     -23.696   8.569 -22.727  1.00 27.21      A    O  
ATOM     41  CB  LEU A 576     -22.486   6.123 -23.962  1.00 32.02      A    C  
ATOM     42  CG  LEU A 576     -21.488   6.552 -25.041  1.00 39.10      A    C  
ATOM     43  CD1 LEU A 576     -20.095   6.115 -24.652  1.00 41.43      A    C  
ATOM     44  CD2 LEU A 576     -21.874   5.934 -26.382  1.00 44.20      A    C  
ATOM     45  N   GLN A 577     -21.604   8.954 -22.017  1.00 25.85      A    N  
ATOM     46  CA  GLN A 577     -21.883  10.374 -21.799  1.00 26.38      A    C  
ATOM     47  C   GLN A 577     -20.784  11.319 -22.239  1.00 25.76      A    C  
ATOM     48  O   GLN A 577     -19.594  10.989 -22.142  1.00 28.93      A    O  
ATOM     49  CB  GLN A 577     -22.110  10.622 -20.317  1.00 31.20      A    C  
ATOM     50  CG  GLN A 577     -23.250   9.852 -19.730  1.00 44.95      A    C  
ATOM     51  CD  GLN A 577     -24.285  10.759 -19.127  1.00 55.40      A    C  
ATOM     52  NE2 GLN A 577     -25.296  10.167 -18.505  1.00 66.74      A    N  
ATOM     53  OE1 GLN A 577     -24.185  11.986 -19.223  1.00 64.42      A    O  
ATOM     54  N   MET A 578     -21.182  12.503 -22.700  1.00 23.99      A    N  
ATOM     55  CA  MET A 578     -20.187  13.493 -23.067  1.00 27.80      A    C  
ATOM     56  C   MET A 578     -19.896  14.307 -21.807  1.00 24.77      A    C  
ATOM     57  O   MET A 578     -20.798  14.567 -21.008  1.00 24.27      A    O  
ATOM     58  CB  MET A 578     -20.714  14.419 -24.169  1.00 26.94      A    C  
ATOM     59  CG  MET A 578     -19.636  15.303 -24.786  1.00 38.65      A    C  
ATOM     60  SD  MET A 578     -20.291  16.292 -26.168  1.00 45.88      A    S  
ATOM     61  CE  MET A 578     -20.612  14.995 -27.349  1.00 38.12      A    C  
ATOM     62  N   VAL A 579     -18.631  14.677 -21.621  1.00 28.51      A    N  
ATOM     63  CA  VAL A 579     -18.225  15.491 -20.479  1.00 36.10      A    C  
ATOM     64  C   VAL A 579     -17.410  16.690 -20.978  1.00 38.90      A    C  
ATOM     65  O   VAL A 579     -16.962  16.719 -22.125  1.00 30.82      A    O  
ATOM     66  CB  VAL A 579     -17.333  14.703 -19.461  1.00 27.98      A    C  
ATOM     67  CG1 VAL A 579     -18.073  13.465 -18.947  1.00 28.06      A    C  
ATOM     68  CG2 VAL A 579     -15.985  14.331 -20.110  1.00 24.38      A    C  
ATOM     69  N   GLN A 580     -17.242  17.681 -20.111  1.00 35.35      A    N  
ATOM     70  CA  GLN A 580     -16.449  18.873 -20.432  1.00 31.01      A    C  
ATOM     71  C   GLN A 580     -15.549  19.130 -19.252  1.00 29.18      A    C  
ATOM     72  O   GLN A 580     -16.026  19.422 -18.153  1.00 28.82      A    O  
ATOM     73  CB  GLN A 580     -17.320  20.105 -20.656  1.00 31.18      A    C  
ATOM     74  CG  GLN A 580     -16.471  21.373 -20.892  1.00 36.79      A    C  
ATOM     75  CD  GLN A 580     -17.297  22.505 -21.427  1.00 49.98      A    C  
ATOM     76  NE2 GLN A 580     -18.192  22.186 -22.350  1.00 45.64      A    N  
ATOM     77  OE1 GLN A 580     -17.138  23.660 -21.021  1.00 59.67      A    O  
ATOM     78  N   VAL A 581     -14.250  18.999 -19.487  1.00 31.68      A    N  
ATOM     79  CA  VAL A 581     -13.250  19.187 -18.449  1.00 40.70      A    C  
ATOM     80  C   VAL A 581     -13.084  20.671 -18.106  1.00 50.21      A    C  
ATOM     81  O   VAL A 581     -13.015  21.525 -18.991  1.00 45.26      A    O  
ATOM     82  CB  VAL A 581     -11.921  18.564 -18.892  1.00 40.96      A    C  
ATOM     83  CG1 VAL A 581     -10.886  18.721 -17.815  1.00 49.10      A    C  
ATOM     84  CG2 VAL A 581     -12.140  17.080 -19.196  1.00 41.03      A    C  
ATOM     85  N   THR A 582     -13.045  20.950 -16.807  1.00 48.35      A    N  
ATOM     86  CA  THR A 582     -12.947  22.301 -16.268  1.00 53.37      A    C  
ATOM     87  C   THR A 582     -11.619  22.629 -15.588  1.00 56.17      A    C  
ATOM     88  O   THR A 582     -11.297  23.793 -15.369  1.00 61.58      A    O  
ATOM     89  CB  THR A 582     -14.079  22.527 -15.255  1.00 49.45      A    C  
ATOM     90  CG2 THR A 582     -13.816  23.752 -14.408  1.00 69.01      A    C  
ATOM     91  OG1 THR A 582     -15.316  22.681 -15.960  1.00 60.95      A    O  
ATOM     92  N   GLY A 583     -10.859  21.604 -15.232  1.00 61.93      A    N  
ATOM     93  CA  GLY A 583      -9.586  21.837 -14.581  1.00 55.51      A    C  
ATOM     94  C   GLY A 583      -8.649  20.692 -14.877  1.00 59.87      A    C  
ATOM     95  O   GLY A 583      -8.971  19.809 -15.672  1.00 52.55      A    O  
ATOM     96  N   SER A 584      -7.488  20.705 -14.235  1.00 57.09      A    N  
ATOM     97  CA  SER A 584      -6.498  19.661 -14.442  1.00 57.20      A    C  
ATOM     98  C   SER A 584      -6.740  18.489 -13.485  1.00 52.26      A    C  
ATOM     99  O   SER A 584      -6.218  17.398 -13.680  1.00 51.60      A    O  
ATOM    100  CB  SER A 584      -5.092  20.235 -14.232  1.00 56.53      A    C  
ATOM    101  OG  SER A 584      -4.958  20.773 -12.928  1.00 47.46      A    O  
ATOM    102  N   SER A 585      -7.535  18.729 -12.453  1.00 51.63      A    N  
ATOM    103  CA  SER A 585      -7.850  17.699 -11.475  1.00 53.02      A    C  
ATOM    104  C   SER A 585      -8.955  16.771 -11.991  1.00 49.98      A    C  
ATOM    105  O   SER A 585      -9.916  17.219 -12.627  1.00 46.58      A    O  
ATOM    106  CB  SER A 585      -8.282  18.352 -10.166  1.00 53.40      A    C  
ATOM    107  OG  SER A 585      -8.550  17.375  -9.183  1.00 69.93      A    O  
ATOM    108  N   ASP A 586      -8.819  15.480 -11.696  1.00 46.84      A    N  
ATOM    109  CA  ASP A 586      -9.783  14.472 -12.141  1.00 40.56      A    C  
ATOM    110  C   ASP A 586     -11.249  14.824 -11.947  1.00 36.05      A    C  
ATOM    111  O   ASP A 586     -12.071  14.547 -12.814  1.00 33.88      A    O  
ATOM    112  CB  ASP A 586      -9.506  13.130 -11.450  1.00 43.61      A    C  
ATOM    113  CG  ASP A 586      -8.326  12.387 -12.053  1.00 50.82      A    C  
ATOM    114  OD1 ASP A 586      -7.616  12.962 -12.917  1.00 48.17      A    O  
ATOM    115  OD2 ASP A 586      -8.106  11.218 -11.653  1.00 46.33      A    O1-
ATOM    116  N   ASN A 587     -11.590  15.445 -10.822  1.00 31.81      A    N  
ATOM    117  CA  ASN A 587     -12.986  15.758 -10.562  1.00 35.75      A    C  
ATOM    118  C   ASN A 587     -13.493  17.070 -11.165  1.00 29.12      A    C  
ATOM    119  O   ASN A 587     -14.656  17.420 -10.995  1.00 34.45      A    O  
ATOM    120  CB  ASN A 587     -13.256  15.732  -9.049  1.00 39.60      A    C  
ATOM    121  CG  ASN A 587     -12.648  16.919  -8.321  1.00 50.18      A    C  
ATOM    122  ND2 ASN A 587     -12.972  17.044  -7.043  1.00 60.20      A    N  
ATOM    123  OD1 ASN A 587     -11.895  17.707  -8.895  1.00 52.07      A    O  
ATOM    124  N   GLU A 588     -12.632  17.771 -11.890  1.00 32.62      A    N  
ATOM    125  CA  GLU A 588     -13.021  19.039 -12.501  1.00 37.35      A    C  
ATOM    126  C   GLU A 588     -13.574  18.851 -13.916  1.00 34.73      A    C  
ATOM    127  O   GLU A 588     -12.880  19.010 -14.932  1.00 34.29      A    O  
ATOM    128  CB  GLU A 588     -11.819  20.001 -12.484  1.00 38.18      A    C  
ATOM    129  CG  GLU A 588     -11.258  20.149 -11.061  1.00 45.42      A    C  
ATOM    130  CD  GLU A 588     -10.025  21.030 -10.955  1.00 47.21      A    C  
ATOM    131  OE1 GLU A 588      -9.082  20.874 -11.762  1.00 54.64      A    O  
ATOM    132  OE2 GLU A 588      -9.998  21.874 -10.035  1.00 62.42      A    O1-
ATOM    133  N   TYR A 589     -14.847  18.498 -13.968  1.00 32.68      A    N  
ATOM    134  CA  TYR A 589     -15.519  18.291 -15.243  1.00 35.00      A    C  
ATOM    135  C   TYR A 589     -16.980  18.204 -14.887  1.00 33.68      A    C  
ATOM    136  O   TYR A 589     -17.322  18.060 -13.714  1.00 33.75      A    O  
ATOM    137  CB  TYR A 589     -15.061  16.974 -15.887  1.00 29.53      A    C  
ATOM    138  CG  TYR A 589     -15.606  15.743 -15.185  1.00 26.21      A    C  
ATOM    139  CD1 TYR A 589     -16.909  15.287 -15.443  1.00 25.32      A    C  
ATOM    140  CD2 TYR A 589     -14.856  15.083 -14.201  1.00 27.47      A    C  
ATOM    141  CE1 TYR A 589     -17.451  14.209 -14.734  1.00 28.26      A    C  
ATOM    142  CE2 TYR A 589     -15.394  14.000 -13.482  1.00 34.19      A    C  
ATOM    143  CZ  TYR A 589     -16.689  13.571 -13.755  1.00 38.35      A    C  
ATOM    144  OH  TYR A 589     -17.235  12.518 -13.056  1.00 33.94      A    O  
ATOM    145  N   PHE A 590     -17.841  18.325 -15.888  1.00 32.05      A    N  
ATOM    146  CA  PHE A 590     -19.267  18.182 -15.659  1.00 27.34      A    C  
ATOM    147  C   PHE A 590     -19.832  17.415 -16.840  1.00 30.01      A    C  
ATOM    148  O   PHE A 590     -19.193  17.335 -17.888  1.00 30.17      A    O  
ATOM    149  CB  PHE A 590     -19.957  19.553 -15.452  1.00 37.99      A    C  
ATOM    150  CG  PHE A 590     -19.862  20.491 -16.624  1.00 34.01      A    C  
ATOM    151  CD1 PHE A 590     -20.913  20.602 -17.527  1.00 34.73      A    C  
ATOM    152  CD2 PHE A 590     -18.730  21.289 -16.805  1.00 32.76      A    C  
ATOM    153  CE1 PHE A 590     -20.840  21.505 -18.606  1.00 31.65      A    C  
ATOM    154  CE2 PHE A 590     -18.647  22.190 -17.875  1.00 35.06      A    C  
ATOM    155  CZ  PHE A 590     -19.713  22.295 -18.778  1.00 30.69      A    C  
ATOM    156  N   TYR A 591     -20.995  16.802 -16.661  1.00 28.78      A    N  
ATOM    157  CA  TYR A 591     -21.605  16.050 -17.743  1.00 36.21      A    C  
ATOM    158  C   TYR A 591     -22.394  16.973 -18.651  1.00 33.63      A    C  
ATOM    159  O   TYR A 591     -23.121  17.837 -18.178  1.00 30.27      A    O  
ATOM    160  CB  TYR A 591     -22.557  14.969 -17.203  1.00 34.07      A    C  
ATOM    161  CG  TYR A 591     -21.885  13.933 -16.335  1.00 39.78      A    C  
ATOM    162  CD1 TYR A 591     -22.009  13.968 -14.940  1.00 39.62      A    C  
ATOM    163  CD2 TYR A 591     -21.069  12.961 -16.904  1.00 38.88      A    C  
ATOM    164  CE1 TYR A 591     -21.325  13.053 -14.136  1.00 38.62      A    C  
ATOM    165  CE2 TYR A 591     -20.377  12.050 -16.116  1.00 43.65      A    C  
ATOM    166  CZ  TYR A 591     -20.506  12.100 -14.741  1.00 41.14      A    C  
ATOM    167  OH  TYR A 591     -19.778  11.221 -13.980  1.00 36.49      A    O  
ATOM    168  N   VAL A 592     -22.253  16.781 -19.955  1.00 31.34      A    N  
ATOM    169  CA  VAL A 592     -23.006  17.576 -20.905  1.00 27.53      A    C  
ATOM    170  C   VAL A 592     -24.425  16.991 -20.952  1.00 28.49      A    C  
ATOM    171  O   VAL A 592     -24.606  15.807 -21.199  1.00 35.84      A    O  
ATOM    172  CB  VAL A 592     -22.369  17.512 -22.314  1.00 24.27      A    C  
ATOM    173  CG1 VAL A 592     -23.243  18.231 -23.317  1.00 23.71      A    C  
ATOM    174  CG2 VAL A 592     -20.964  18.114 -22.284  1.00 26.60      A    C  
ATOM    175  N   ASP A 593     -25.421  17.820 -20.673  1.00 27.46      A    N  
ATOM    176  CA  ASP A 593     -26.819  17.400 -20.707  1.00 33.92      A    C  
ATOM    177  C   ASP A 593     -27.434  18.022 -21.982  1.00 37.78      A    C  
ATOM    178  O   ASP A 593     -27.453  19.245 -22.151  1.00 32.74      A    O  
ATOM    179  CB  ASP A 593     -27.528  17.913 -19.453  1.00 35.73      A    C  
ATOM    180  CG  ASP A 593     -28.975  17.487 -19.379  1.00 44.25      A    C  
ATOM    181  OD1 ASP A 593     -29.609  17.326 -20.436  1.00 52.56      A    O  
ATOM    182  OD2 ASP A 593     -29.490  17.334 -18.254  1.00 54.63      A    O1-
ATOM    183  N   PHE A 594     -27.926  17.180 -22.883  1.00 32.40      A    N  
ATOM    184  CA  PHE A 594     -28.490  17.675 -24.140  1.00 36.77      A    C  
ATOM    185  C   PHE A 594     -29.954  18.064 -24.056  1.00 33.52      A    C  
ATOM    186  O   PHE A 594     -30.573  18.387 -25.067  1.00 31.72      A    O  
ATOM    187  CB  PHE A 594     -28.326  16.616 -25.239  1.00 28.87      A    C  
ATOM    188  CG  PHE A 594     -26.905  16.429 -25.695  1.00 37.91      A    C  
ATOM    189  CD1 PHE A 594     -26.037  15.585 -25.003  1.00 28.57      A    C  
ATOM    190  CD2 PHE A 594     -26.427  17.123 -26.800  1.00 30.68      A    C  
ATOM    191  CE1 PHE A 594     -24.705  15.437 -25.408  1.00 28.99      A    C  
ATOM    192  CE2 PHE A 594     -25.097  16.983 -27.212  1.00 35.29      A    C  
ATOM    193  CZ  PHE A 594     -24.235  16.138 -26.512  1.00 30.07      A    C  
ATOM    194  N   ARG A 595     -30.518  18.041 -22.859  1.00 25.75      A    N  
ATOM    195  CA  ARG A 595     -31.931  18.357 -22.732  1.00 26.58      A    C  
ATOM    196  C   ARG A 595     -32.304  19.704 -23.373  1.00 31.49      A    C  
ATOM    197  O   ARG A 595     -33.316  19.795 -24.070  1.00 29.15      A    O  
ATOM    198  CB  ARG A 595     -32.348  18.310 -21.261  1.00 31.18      A    C  
ATOM    199  CG  ARG A 595     -33.845  18.497 -21.032  1.00 43.19      A    C  
ATOM    200  CD  ARG A 595     -34.255  18.037 -19.630  1.00 50.46      A    C  
ATOM    201  NE  ARG A 595     -33.363  18.571 -18.602  1.00 59.66      A    N  
ATOM    202  CZ  ARG A 595     -33.364  18.185 -17.329  1.00 63.36      A    C  
ATOM    203  NH1 ARG A 595     -34.209  17.252 -16.912  1.00 63.23      A    N1+
ATOM    204  NH2 ARG A 595     -32.518  18.737 -16.469  1.00 61.97      A    N  
ATOM    205  N   GLU A 596     -31.479  20.735 -23.176  1.00 25.76      A    N  
ATOM    206  CA  GLU A 596     -31.777  22.049 -23.752  1.00 28.77      A    C  
ATOM    207  C   GLU A 596     -31.371  22.176 -25.232  1.00 24.51      A    C  
ATOM    208  O   GLU A 596     -31.689  23.173 -25.860  1.00 27.13      A    O  
ATOM    209  CB  GLU A 596     -31.097  23.182 -22.942  1.00 25.41      A    C  
ATOM    210  CG  GLU A 596     -31.376  23.204 -21.422  1.00 27.30      A    C  
ATOM    211  CD  GLU A 596     -32.846  23.408 -21.064  1.00 35.77      A    C  
ATOM    212  OE1 GLU A 596     -33.205  23.188 -19.890  1.00 41.43      A    O  
ATOM    213  OE2 GLU A 596     -33.644  23.792 -21.943  1.00 33.16      A    O1-
ATOM    214  N   TYR A 597     -30.664  21.192 -25.788  1.00 26.41      A    N  
ATOM    215  CA  TYR A 597     -30.258  21.283 -27.199  1.00 31.65      A    C  
ATOM    216  C   TYR A 597     -31.404  20.883 -28.141  1.00 28.46      A    C  
ATOM    217  O   TYR A 597     -32.402  20.324 -27.691  1.00 26.21      A    O  
ATOM    218  CB  TYR A 597     -29.027  20.416 -27.456  1.00 23.48      A    C  
ATOM    219  CG  TYR A 597     -27.761  20.973 -26.841  1.00 27.92      A    C  
ATOM    220  CD1 TYR A 597     -27.594  21.028 -25.445  1.00 25.02      A    C  
ATOM    221  CD2 TYR A 597     -26.762  21.517 -27.647  1.00 29.46      A    C  
ATOM    222  CE1 TYR A 597     -26.453  21.622 -24.873  1.00 28.71      A    C  
ATOM    223  CE2 TYR A 597     -25.628  22.116 -27.092  1.00 24.29      A    C  
ATOM    224  CZ  TYR A 597     -25.484  22.166 -25.703  1.00 36.13      A    C  
ATOM    225  OH  TYR A 597     -24.381  22.785 -25.160  1.00 31.22      A    O  
ATOM    226  N   GLU A 598     -31.294  21.191 -29.430  1.00 27.50      A    N  
ATOM    227  CA  GLU A 598     -32.380  20.820 -30.350  1.00 27.48      A    C  
ATOM    228  C   GLU A 598     -31.997  19.582 -31.159  1.00 26.25      A    C  
ATOM    229  O   GLU A 598     -30.835  19.369 -31.473  1.00 35.44      A    O  
ATOM    230  CB  GLU A 598     -32.732  21.965 -31.315  1.00 33.21      A    C  
ATOM    231  CG  GLU A 598     -33.313  23.249 -30.673  1.00 36.27      A    C  
ATOM    232  CD  GLU A 598     -34.456  22.988 -29.695  1.00 41.53      A    C  
ATOM    233  OE1 GLU A 598     -35.293  22.097 -29.951  1.00 48.55      A    O  
ATOM    234  OE2 GLU A 598     -34.526  23.688 -28.669  1.00 43.48      A    O1-
ATOM    235  N   TYR A 599     -32.989  18.762 -31.475  1.00 29.16      A    N  
ATOM    236  CA  TYR A 599     -32.769  17.547 -32.247  1.00 26.70      A    C  
ATOM    237  C   TYR A 599     -32.784  17.862 -33.744  1.00 26.58      A    C  
ATOM    238  O   TYR A 599     -33.686  18.535 -34.228  1.00 26.45      A    O  
ATOM    239  CB  TYR A 599     -33.858  16.519 -31.887  1.00 24.96      A    C  
ATOM    240  CG  TYR A 599     -34.031  15.376 -32.870  1.00 23.24      A    C  
ATOM    241  CD1 TYR A 599     -35.242  15.212 -33.534  1.00 24.35      A    C  
ATOM    242  CD2 TYR A 599     -33.019  14.437 -33.093  1.00 23.81      A    C  
ATOM    243  CE1 TYR A 599     -35.471  14.148 -34.390  1.00 25.37      A    C  
ATOM    244  CE2 TYR A 599     -33.238  13.337 -33.973  1.00 31.21      A    C  
ATOM    245  CZ  TYR A 599     -34.490  13.223 -34.612  1.00 25.88      A    C  
ATOM    246  OH  TYR A 599     -34.784  12.214 -35.493  1.00 30.07      A    O  
ATOM    247  N   ASP A 600     -31.774  17.383 -34.466  1.00 25.85      A    N  
ATOM    248  CA  ASP A 600     -31.672  17.634 -35.903  1.00 26.71      A    C  
ATOM    249  C   ASP A 600     -32.574  16.657 -36.661  1.00 24.33      A    C  
ATOM    250  O   ASP A 600     -32.311  15.455 -36.691  1.00 25.03      A    O  
ATOM    251  CB  ASP A 600     -30.205  17.493 -36.342  1.00 23.78      A    C  
ATOM    252  CG  ASP A 600     -29.980  17.928 -37.791  1.00 29.70      A    C  
ATOM    253  OD1 ASP A 600     -28.832  18.277 -38.105  1.00 26.74      A    O  
ATOM    254  OD2 ASP A 600     -30.930  17.909 -38.613  1.00 27.18      A    O1-
ATOM    255  N   LEU A 601     -33.635  17.187 -37.262  1.00 23.65      A    N  
ATOM    256  CA  LEU A 601     -34.622  16.374 -37.973  1.00 27.48      A    C  
ATOM    257  C   LEU A 601     -34.151  15.611 -39.190  1.00 31.27      A    C  
ATOM    258  O   LEU A 601     -34.917  14.843 -39.755  1.00 30.72      A    O  
ATOM    259  CB  LEU A 601     -35.845  17.217 -38.343  1.00 22.94      A    C  
ATOM    260  CG  LEU A 601     -36.565  17.780 -37.105  1.00 35.71      A    C  
ATOM    261  CD1 LEU A 601     -37.511  18.931 -37.477  1.00 26.24      A    C  
ATOM    262  CD2 LEU A 601     -37.305  16.635 -36.417  1.00 30.79      A    C  
ATOM    263  N   LYS A 602     -32.900  15.794 -39.594  1.00 28.21      A    N  
ATOM    264  CA  LYS A 602     -32.427  15.047 -40.752  1.00 30.20      A    C  
ATOM    265  C   LYS A 602     -32.306  13.573 -40.361  1.00 38.89      A    C  
ATOM    266  O   LYS A 602     -32.179  12.716 -41.224  1.00 24.66      A    O  
ATOM    267  CB  LYS A 602     -31.079  15.585 -41.248  1.00 26.03      A    C  
ATOM    268  CG  LYS A 602     -29.917  15.398 -40.284  1.00 31.91      A    C  
ATOM    269  CD  LYS A 602     -28.586  15.704 -40.956  1.00 32.94      A    C  
ATOM    270  CE  LYS A 602     -27.448  15.605 -39.952  1.00 40.06      A    C  
ATOM    271  NZ  LYS A 602     -26.165  16.122 -40.505  1.00 39.62      A    N1+
ATOM    272  N   TRP A 603     -32.360  13.281 -39.058  1.00 32.89      A    N  
ATOM    273  CA  TRP A 603     -32.263  11.891 -38.583  1.00 30.82      A    C  
ATOM    274  C   TRP A 603     -33.602  11.151 -38.529  1.00 25.51      A    C  
ATOM    275  O   TRP A 603     -33.629   9.922 -38.362  1.00 27.44      A    O  
ATOM    276  CB  TRP A 603     -31.650  11.834 -37.176  1.00 28.28      A    C  
ATOM    277  CG  TRP A 603     -30.202  12.211 -37.139  1.00 17.01      A    C  
ATOM    278  CD1 TRP A 603     -29.670  13.469 -36.924  1.00 22.17      A    C  
ATOM    279  CD2 TRP A 603     -29.095  11.337 -37.350  1.00 21.34      A    C  
ATOM    280  CE2 TRP A 603     -27.917  12.119 -37.253  1.00 18.36      A    C  
ATOM    281  CE3 TRP A 603     -28.977   9.959 -37.608  1.00 22.88      A    C  
ATOM    282  NE1 TRP A 603     -28.295  13.416 -36.996  1.00 18.21      A    N  
ATOM    283  CZ2 TRP A 603     -26.637  11.568 -37.400  1.00 27.81      A    C  
ATOM    284  CZ3 TRP A 603     -27.696   9.417 -37.758  1.00 24.95      A    C  
ATOM    285  CH2 TRP A 603     -26.548  10.223 -37.650  1.00 25.75      A    C  
ATOM    286  N   GLU A 604     -34.694  11.905 -38.644  1.00 22.74      A    N  
ATOM    287  CA  GLU A 604     -36.042  11.362 -38.557  1.00 28.71      A    C  
ATOM    288  C   GLU A 604     -36.301  10.335 -39.677  1.00 40.46      A    C  
ATOM    289  O   GLU A 604     -36.074  10.609 -40.855  1.00 32.59      A    O  
ATOM    290  CB  GLU A 604     -37.040  12.522 -38.619  1.00 24.85      A    C  
ATOM    291  CG  GLU A 604     -38.431  12.225 -38.077  1.00 31.81      A    C  
ATOM    292  CD  GLU A 604     -38.438  11.857 -36.597  1.00 35.97      A    C  
ATOM    293  OE1 GLU A 604     -37.492  12.202 -35.857  1.00 33.55      A    O  
ATOM    294  OE2 GLU A 604     -39.418  11.231 -36.165  1.00 32.35      A    O1-
ATOM    295  N   PHE A 605     -36.778   9.154 -39.284  1.00 33.92      A    N  
ATOM    296  CA  PHE A 605     -37.035   8.039 -40.196  1.00 30.25      A    C  
ATOM    297  C   PHE A 605     -38.510   7.674 -40.128  1.00 35.10      A    C  
ATOM    298  O   PHE A 605     -39.136   7.810 -39.077  1.00 37.23      A    O  
ATOM    299  CB  PHE A 605     -36.170   6.850 -39.763  1.00 33.33      A    C  
ATOM    300  CG  PHE A 605     -36.163   5.699 -40.730  1.00 36.35      A    C  
ATOM    301  CD1 PHE A 605     -35.431   5.765 -41.920  1.00 30.75      A    C  
ATOM    302  CD2 PHE A 605     -36.878   4.540 -40.444  1.00 34.29      A    C  
ATOM    303  CE1 PHE A 605     -35.414   4.693 -42.801  1.00 39.35      A    C  
ATOM    304  CE2 PHE A 605     -36.866   3.458 -41.328  1.00 41.88      A    C  
ATOM    305  CZ  PHE A 605     -36.132   3.536 -42.505  1.00 40.52      A    C  
ATOM    306  N   PRO A 606     -39.096   7.206 -41.250  1.00 35.02      A    N  
ATOM    307  CA  PRO A 606     -40.521   6.837 -41.249  1.00 39.33      A    C  
ATOM    308  C   PRO A 606     -40.703   5.558 -40.423  1.00 35.10      A    C  
ATOM    309  O   PRO A 606     -40.095   4.545 -40.741  1.00 34.22      A    O  
ATOM    310  CB  PRO A 606     -40.823   6.597 -42.740  1.00 33.85      A    C  
ATOM    311  CG  PRO A 606     -39.762   7.361 -43.452  1.00 37.36      A    C  
ATOM    312  CD  PRO A 606     -38.537   7.077 -42.602  1.00 35.00      A    C  
ATOM    313  N   ARG A 607     -41.528   5.582 -39.380  1.00 35.16      A    N  
ATOM    314  CA  ARG A 607     -41.669   4.370 -38.585  1.00 41.24      A    C  
ATOM    315  C   ARG A 607     -42.284   3.203 -39.376  1.00 45.59      A    C  
ATOM    316  O   ARG A 607     -42.112   2.044 -39.007  1.00 41.44      A    O  
ATOM    317  CB  ARG A 607     -42.442   4.645 -37.283  1.00 39.34      A    C  
ATOM    318  CG  ARG A 607     -43.858   5.156 -37.446  1.00 45.43      A    C  
ATOM    319  CD  ARG A 607     -44.459   5.554 -36.088  1.00 44.25      A    C  
ATOM    320  NE  ARG A 607     -43.772   6.681 -35.445  1.00 45.03      A    N  
ATOM    321  CZ  ARG A 607     -43.102   6.601 -34.293  1.00 51.49      A    C  
ATOM    322  NH1 ARG A 607     -43.014   5.445 -33.647  1.00 39.50      A    N1+
ATOM    323  NH2 ARG A 607     -42.533   7.682 -33.767  1.00 45.31      A    N  
ATOM    324  N   GLU A 608     -42.956   3.500 -40.487  1.00 47.40      A    N  
ATOM    325  CA  GLU A 608     -43.547   2.440 -41.302  1.00 42.35      A    C  
ATOM    326  C   GLU A 608     -42.464   1.676 -42.080  1.00 39.67      A    C  
ATOM    327  O   GLU A 608     -42.700   0.569 -42.550  1.00 39.70      A    O  
ATOM    328  CB  GLU A 608     -44.590   3.020 -42.272  1.00 51.99      A    C  
ATOM    329  CG  GLU A 608     -44.015   3.826 -43.435  1.00 60.86      A    C  
ATOM    330  CD  GLU A 608     -45.096   4.453 -44.310  1.00 64.57      A    C  
ATOM    331  OE1 GLU A 608     -44.757   4.987 -45.387  1.00 56.00      A    O  
ATOM    332  OE2 GLU A 608     -46.284   4.417 -43.919  1.00 63.54      A    O1-
ATOM    333  N   ASN A 609     -41.278   2.258 -42.229  1.00 31.34      A    N  
ATOM    334  CA  ASN A 609     -40.208   1.555 -42.934  1.00 31.76      A    C  
ATOM    335  C   ASN A 609     -39.443   0.595 -42.028  1.00 30.25      A    C  
ATOM    336  O   ASN A 609     -38.376   0.096 -42.402  1.00 35.22      A    O  
ATOM    337  CB  ASN A 609     -39.215   2.532 -43.562  1.00 41.05      A    C  
ATOM    338  CG  ASN A 609     -39.809   3.286 -44.739  1.00 44.62      A    C  
ATOM    339  ND2 ASN A 609     -41.126   3.257 -44.854  1.00 38.59      A    N  
ATOM    340  OD1 ASN A 609     -39.088   3.897 -45.520  1.00 54.73      A    O  
ATOM    341  N   LEU A 610     -39.983   0.365 -40.839  1.00 36.33      A    N  
ATOM    342  CA  LEU A 610     -39.381  -0.541 -39.863  1.00 45.19      A    C  
ATOM    343  C   LEU A 610     -40.213  -1.816 -39.776  1.00 44.80      A    C  
ATOM    344  O   LEU A 610     -41.412  -1.756 -39.509  1.00 38.15      A    O  
ATOM    345  CB  LEU A 610     -39.343   0.087 -38.457  1.00 38.66      A    C  
ATOM    346  CG  LEU A 610     -38.373   1.224 -38.142  1.00 37.75      A    C  
ATOM    347  CD1 LEU A 610     -38.573   1.696 -36.688  1.00 32.58      A    C  
ATOM    348  CD2 LEU A 610     -36.950   0.733 -38.356  1.00 37.14      A    C  
ATOM    349  N   GLU A 611     -39.580  -2.962 -40.006  1.00 39.96      A    N  
ATOM    350  CA  GLU A 611     -40.292  -4.231 -39.886  1.00 49.76      A    C  
ATOM    351  C   GLU A 611     -39.736  -4.893 -38.623  1.00 38.14      A    C  
ATOM    352  O   GLU A 611     -38.635  -5.421 -38.633  1.00 32.98      A    O  
ATOM    353  CB  GLU A 611     -40.027  -5.106 -41.110  1.00 51.96      A    C  
ATOM    354  CG  GLU A 611     -41.034  -6.226 -41.283  1.00 69.04      A    C  
ATOM    355  CD  GLU A 611     -41.007  -6.793 -42.686  1.00 80.23      A    C  
ATOM    356  OE1 GLU A 611     -41.161  -6.000 -43.643  1.00 78.50      A    O  
ATOM    357  OE2 GLU A 611     -40.835  -8.024 -42.830  1.00 86.52      A    O1-
ATOM    358  N   PHE A 612     -40.491  -4.841 -37.535  1.00 33.39      A    N  
ATOM    359  CA  PHE A 612     -40.021  -5.402 -36.276  1.00 41.27      A    C  
ATOM    360  C   PHE A 612     -39.898  -6.919 -36.255  1.00 48.01      A    C  
ATOM    361  O   PHE A 612     -40.760  -7.639 -36.753  1.00 47.90      A    O  
ATOM    362  CB  PHE A 612     -40.907  -4.924 -35.119  1.00 39.20      A    C  
ATOM    363  CG  PHE A 612     -40.686  -3.472 -34.746  1.00 43.73      A    C  
ATOM    364  CD1 PHE A 612     -41.687  -2.523 -34.947  1.00 51.74      A    C  
ATOM    365  CD2 PHE A 612     -39.460  -3.055 -34.216  1.00 44.01      A    C  
ATOM    366  CE1 PHE A 612     -41.474  -1.171 -34.626  1.00 50.31      A    C  
ATOM    367  CE2 PHE A 612     -39.234  -1.710 -33.893  1.00 37.47      A    C  
ATOM    368  CZ  PHE A 612     -40.241  -0.767 -34.098  1.00 42.89      A    C  
ATOM    369  N   GLY A 613     -38.789  -7.381 -35.687  1.00 50.17      A    N  
ATOM    370  CA  GLY A 613     -38.512  -8.797 -35.579  1.00 44.84      A    C  
ATOM    371  C   GLY A 613     -38.511  -9.215 -34.120  1.00 46.54      A    C  
ATOM    372  O   GLY A 613     -39.412  -8.845 -33.367  1.00 40.96      A    O  
ATOM    373  N   LYS A 614     -37.490  -9.966 -33.715  1.00 41.11      A    N  
ATOM    374  CA  LYS A 614     -37.387 -10.455 -32.334  1.00 51.71      A    C  
ATOM    375  C   LYS A 614     -36.813  -9.444 -31.339  1.00 49.84      A    C  
ATOM    376  O   LYS A 614     -36.078  -8.521 -31.714  1.00 46.80      A    O  
ATOM    377  CB  LYS A 614     -36.502 -11.701 -32.283  1.00 52.29      A    C  
ATOM    378  CG  LYS A 614     -35.024 -11.378 -32.470  1.00 57.08      A    C  
ATOM    379  CD  LYS A 614     -34.144 -12.609 -32.345  1.00 72.15      A    C  
ATOM    380  CE  LYS A 614     -32.667 -12.251 -32.499  1.00 73.84      A    C  
ATOM    381  NZ  LYS A 614     -31.785 -13.456 -32.478  1.00 76.54      A    N1+
ATOM    382  N   VAL A 615     -37.147  -9.645 -30.067  1.00 52.06      A    N  
ATOM    383  CA  VAL A 615     -36.648  -8.806 -28.985  1.00 51.19      A    C  
ATOM    384  C   VAL A 615     -35.198  -9.224 -28.762  1.00 45.24      A    C  
ATOM    385  O   VAL A 615     -34.905 -10.415 -28.700  1.00 50.21      A    O  
ATOM    386  CB  VAL A 615     -37.430  -9.045 -27.680  1.00 47.27      A    C  
ATOM    387  CG1 VAL A 615     -36.825  -8.226 -26.547  1.00 45.95      A    C  
ATOM    388  CG2 VAL A 615     -38.877  -8.683 -27.877  1.00 51.28      A    C  
ATOM    389  N   LEU A 616     -34.292  -8.258 -28.667  1.00 45.86      A    N  
ATOM    390  CA  LEU A 616     -32.878  -8.567 -28.447  1.00 43.05      A    C  
ATOM    391  C   LEU A 616     -32.549  -8.646 -26.961  1.00 45.07      A    C  
ATOM    392  O   LEU A 616     -31.568  -9.268 -26.559  1.00 49.73      A    O  
ATOM    393  CB  LEU A 616     -31.987  -7.503 -29.082  1.00 49.15      A    C  
ATOM    394  CG  LEU A 616     -31.957  -7.398 -30.599  1.00 52.13      A    C  
ATOM    395  CD1 LEU A 616     -30.895  -6.398 -30.991  1.00 48.02      A    C  
ATOM    396  CD2 LEU A 616     -31.647  -8.765 -31.208  1.00 53.50      A    C  
ATOM    397  N   GLY A 617     -33.370  -7.994 -26.156  1.00 43.36      A    N  
ATOM    398  CA  GLY A 617     -33.156  -7.985 -24.727  1.00 40.49      A    C  
ATOM    399  C   GLY A 617     -34.152  -7.005 -24.164  1.00 42.97      A    C  
ATOM    400  O   GLY A 617     -34.552  -6.054 -24.841  1.00 38.38      A    O  
ATOM    401  N   SER A 618     -34.559  -7.222 -22.925  1.00 41.22      A    N  
ATOM    402  CA  SER A 618     -35.530  -6.343 -22.319  1.00 30.30      A    C  
ATOM    403  C   SER A 618     -35.160  -6.019 -20.878  1.00 39.89      A    C  
ATOM    404  O   SER A 618     -34.338  -6.698 -20.278  1.00 44.92      A    O  
ATOM    405  CB  SER A 618     -36.899  -6.995 -22.385  1.00 35.66      A    C  
ATOM    406  OG  SER A 618     -37.903  -6.049 -22.076  1.00 56.84      A    O  
ATOM    407  N   GLY A 619     -35.771  -4.982 -20.323  1.00 37.72      A    N  
ATOM    408  CA  GLY A 619     -35.454  -4.606 -18.960  1.00 50.39      A    C  
ATOM    409  C   GLY A 619     -36.576  -3.835 -18.308  1.00 50.62      A    C  
ATOM    410  O   GLY A 619     -37.697  -3.818 -18.810  1.00 50.73      A    O  
ATOM    411  N   ALA A 620     -36.269  -3.176 -17.200  1.00 47.43      A    N  
ATOM    412  CA  ALA A 620     -37.274  -2.420 -16.469  1.00 49.06      A    C  
ATOM    413  C   ALA A 620     -37.775  -1.155 -17.147  1.00 50.29      A    C  
ATOM    414  O   ALA A 620     -38.898  -0.718 -16.893  1.00 48.76      A    O  
ATOM    415  CB  ALA A 620     -36.737  -2.067 -15.084  1.00 50.34      A    C  
ATOM    416  N   PHE A 621     -36.955  -0.564 -18.007  1.00 51.01      A    N  
ATOM    417  CA  PHE A 621     -37.325   0.693 -18.646  1.00 44.91      A    C  
ATOM    418  C   PHE A 621     -37.820   0.598 -20.070  1.00 40.88      A    C  
ATOM    419  O   PHE A 621     -38.468   1.517 -20.563  1.00 39.04      A    O  
ATOM    420  CB  PHE A 621     -36.129   1.639 -18.607  1.00 50.13      A    C  
ATOM    421  CG  PHE A 621     -35.597   1.864 -17.235  1.00 58.03      A    C  
ATOM    422  CD1 PHE A 621     -36.318   2.624 -16.317  1.00 60.69      A    C  
ATOM    423  CD2 PHE A 621     -34.396   1.280 -16.841  1.00 52.97      A    C  
ATOM    424  CE1 PHE A 621     -35.853   2.800 -15.021  1.00 64.43      A    C  
ATOM    425  CE2 PHE A 621     -33.921   1.446 -15.551  1.00 61.94      A    C  
ATOM    426  CZ  PHE A 621     -34.653   2.211 -14.636  1.00 66.03      A    C  
ATOM    427  N   GLY A 622     -37.499  -0.497 -20.741  1.00 40.48      A    N  
ATOM    428  CA  GLY A 622     -37.916  -0.636 -22.119  1.00 38.45      A    C  
ATOM    429  C   GLY A 622     -37.208  -1.817 -22.708  1.00 43.25      A    C  
ATOM    430  O   GLY A 622     -36.930  -2.785 -21.995  1.00 37.54      A    O  
ATOM    431  N   LYS A 623     -36.879  -1.737 -23.992  1.00 32.63      A    N  
ATOM    432  CA  LYS A 623     -36.223  -2.856 -24.645  1.00 36.92      A    C  
ATOM    433  C   LYS A 623     -35.573  -2.458 -25.954  1.00 38.33      A    C  
ATOM    434  O   LYS A 623     -35.771  -1.351 -26.449  1.00 35.52      A    O  
ATOM    435  CB  LYS A 623     -37.260  -3.948 -24.927  1.00 46.90      A    C  
ATOM    436  CG  LYS A 623     -38.384  -3.462 -25.853  1.00 52.73      A    C  
ATOM    437  CD  LYS A 623     -39.425  -4.523 -26.152  1.00 46.08      A    C  
ATOM    438  CE  LYS A 623     -40.500  -3.952 -27.066  1.00 52.27      A    C  
ATOM    439  NZ  LYS A 623     -41.633  -4.889 -27.246  1.00 52.94      A    N1+
ATOM    440  N   VAL A 624     -34.806  -3.389 -26.508  1.00 33.60      A    N  
ATOM    441  CA  VAL A 624     -34.138  -3.204 -27.781  1.00 37.17      A    C  
ATOM    442  C   VAL A 624     -34.678  -4.328 -28.673  1.00 49.00      A    C  
ATOM    443  O   VAL A 624     -34.593  -5.521 -28.323  1.00 35.47      A    O  
ATOM    444  CB  VAL A 624     -32.604  -3.314 -27.641  1.00 40.64      A    C  
ATOM    445  CG1 VAL A 624     -31.936  -3.141 -28.996  1.00 33.42      A    C  
ATOM    446  CG2 VAL A 624     -32.104  -2.247 -26.678  1.00 43.62      A    C  
ATOM    447  N   MET A 625     -35.244  -3.931 -29.812  1.00 38.01      A    N  
ATOM    448  CA  MET A 625     -35.848  -4.853 -30.768  1.00 40.77      A    C  
ATOM    449  C   MET A 625     -35.054  -4.971 -32.048  1.00 43.65      A    C  
ATOM    450  O   MET A 625     -34.403  -4.011 -32.482  1.00 39.17      A    O  
ATOM    451  CB  MET A 625     -37.230  -4.354 -31.170  1.00 45.08      A    C  
ATOM    452  CG  MET A 625     -38.236  -4.240 -30.069  1.00 50.16      A    C  
ATOM    453  SD  MET A 625     -38.870  -5.832 -29.671  1.00 62.88      A    S  
ATOM    454  CE  MET A 625     -39.556  -6.348 -31.291  1.00 54.19      A    C  
ATOM    455  N   ASN A 626     -35.102  -6.145 -32.665  1.00 37.49      A    N  
ATOM    456  CA  ASN A 626     -34.445  -6.274 -33.950  1.00 44.74      A    C  
ATOM    457  C   ASN A 626     -35.527  -5.824 -34.928  1.00 38.91      A    C  
ATOM    458  O   ASN A 626     -36.714  -5.762 -34.583  1.00 36.93      A    O  
ATOM    459  CB  ASN A 626     -34.035  -7.718 -34.273  1.00 48.44      A    C  
ATOM    460  CG  ASN A 626     -33.747  -7.917 -35.770  1.00 60.57      A    C  
ATOM    461  ND2 ASN A 626     -32.525  -7.590 -36.197  1.00 41.73      A    N  
ATOM    462  OD1 ASN A 626     -34.627  -8.333 -36.531  1.00 59.97      A    O  
ATOM    463  N   ALA A 627     -35.109  -5.455 -36.124  1.00 44.17      A    N  
ATOM    464  CA  ALA A 627     -36.054  -5.068 -37.155  1.00 37.38      A    C  
ATOM    465  C   ALA A 627     -35.303  -4.909 -38.455  1.00 38.31      A    C  
ATOM    466  O   ALA A 627     -34.069  -4.924 -38.499  1.00 36.95      A    O  
ATOM    467  CB  ALA A 627     -36.778  -3.760 -36.784  1.00 33.51      A    C  
ATOM    468  N   THR A 628     -36.069  -4.816 -39.530  1.00 39.38      A    N  
ATOM    469  CA  THR A 628     -35.507  -4.601 -40.844  1.00 43.88      A    C  
ATOM    470  C   THR A 628     -35.917  -3.167 -41.155  1.00 34.47      A    C  
ATOM    471  O   THR A 628     -37.056  -2.756 -40.876  1.00 33.84      A    O  
ATOM    472  CB  THR A 628     -36.132  -5.561 -41.895  1.00 53.25      A    C  
ATOM    473  CG2 THR A 628     -35.606  -5.243 -43.283  1.00 47.54      A    C  
ATOM    474  OG1 THR A 628     -35.798  -6.918 -41.565  1.00 52.74      A    O  
ATOM    475  N   ALA A 629     -34.995  -2.397 -41.712  1.00 33.05      A    N  
ATOM    476  CA  ALA A 629     -35.327  -1.025 -42.044  1.00 37.76      A    C  
ATOM    477  C   ALA A 629     -35.217  -0.815 -43.547  1.00 40.49      A    C  
ATOM    478  O   ALA A 629     -34.180  -1.089 -44.159  1.00 40.31      A    O  
ATOM    479  CB  ALA A 629     -34.397  -0.043 -41.294  1.00 23.80      A    C  
ATOM    480  N   TYR A 630     -36.292  -0.311 -44.135  1.00 44.40      A    N  
ATOM    481  CA  TYR A 630     -36.306  -0.059 -45.568  1.00 50.26      A    C  
ATOM    482  C   TYR A 630     -35.665   1.273 -45.946  1.00 41.70      A    C  
ATOM    483  O   TYR A 630     -36.178   2.327 -45.615  1.00 42.93      A    O  
ATOM    484  CB  TYR A 630     -37.740  -0.063 -46.105  1.00 62.37      A    C  
ATOM    485  CG  TYR A 630     -38.481  -1.374 -45.983  1.00 81.92      A    C  
ATOM    486  CD1 TYR A 630     -37.822  -2.597 -46.146  1.00 89.18      A    C  
ATOM    487  CD2 TYR A 630     -39.864  -1.392 -45.776  1.00 90.09      A    C  
ATOM    488  CE1 TYR A 630     -38.523  -3.806 -46.110  1.00 91.03      A    C  
ATOM    489  CE2 TYR A 630     -40.574  -2.594 -45.743  1.00 94.61      A    C  
ATOM    490  CZ  TYR A 630     -39.900  -3.795 -45.911  1.00 95.13      A    C  
ATOM    491  OH  TYR A 630     -40.605  -4.978 -45.894  1.00 93.23      A    O  
ATOM    492  N   GLY A 631     -34.536   1.208 -46.638  1.00 43.76      A    N  
ATOM    493  CA  GLY A 631     -33.873   2.405 -47.110  1.00 48.95      A    C  
ATOM    494  C   GLY A 631     -33.205   3.334 -46.123  1.00 55.84      A    C  
ATOM    495  O   GLY A 631     -32.983   4.498 -46.443  1.00 49.74      A    O  
ATOM    496  N   ILE A 632     -32.867   2.846 -44.935  1.00 55.56      A    N  
ATOM    497  CA  ILE A 632     -32.219   3.703 -43.959  1.00 47.34      A    C  
ATOM    498  C   ILE A 632     -30.765   3.900 -44.373  1.00 52.26      A    C  
ATOM    499  O   ILE A 632     -30.164   4.947 -44.116  1.00 50.61      A    O  
ATOM    500  CB  ILE A 632     -32.271   3.074 -42.553  1.00 54.91      A    C  
ATOM    501  CG1 ILE A 632     -32.093   4.170 -41.492  1.00 46.82      A    C  
ATOM    502  CG2 ILE A 632     -31.191   1.982 -42.428  1.00 37.83      A    C  
ATOM    503  CD1 ILE A 632     -32.334   3.704 -40.073  1.00 44.47      A    C  
ATOM    504  N   SER A 633     -30.221   2.881 -45.030  1.00 58.20      A    N  
ATOM    505  CA  SER A 633     -28.835   2.865 -45.495  1.00 70.76      A    C  
ATOM    506  C   SER A 633     -28.656   3.641 -46.793  1.00 76.60      A    C  
ATOM    507  O   SER A 633     -29.572   3.705 -47.612  1.00 80.36      A    O  
ATOM    508  CB  SER A 633     -28.382   1.416 -45.703  1.00 76.04      A    C  
ATOM    509  OG  SER A 633     -29.305   0.710 -46.523  1.00 69.49      A    O  
ATOM    510  N   LYS A 634     -27.466   4.209 -46.979  1.00 80.55      A    N  
ATOM    511  CA  LYS A 634     -27.143   5.000 -48.169  1.00 90.86      A    C  
ATOM    512  C   LYS A 634     -27.820   4.526 -49.462  1.00 93.86      A    C  
ATOM    513  O   LYS A 634     -28.074   5.326 -50.370  1.00 89.00      A    O  
ATOM    514  CB  LYS A 634     -25.623   5.043 -48.371  1.00 91.44      A    C  
ATOM    515  CG  LYS A 634     -24.865   5.648 -47.197  1.00 91.50      A    C  
ATOM    516  CD  LYS A 634     -23.386   5.835 -47.514  1.00 95.83      A    C  
ATOM    517  CE  LYS A 634     -23.176   6.832 -48.652  1.00 94.53      A    C  
ATOM    518  NZ  LYS A 634     -21.730   7.095 -48.912  1.00 92.15      A    N1+
ATOM    519  N   THR A 635     -28.113   3.231 -49.539  1.00 94.53      A    N  
ATOM    520  CA  THR A 635     -28.758   2.662 -50.715  1.00 94.10      A    C  
ATOM    521  C   THR A 635     -30.240   2.372 -50.481  1.00 92.44      A    C  
ATOM    522  O   THR A 635     -30.704   2.333 -49.338  1.00 85.52      A    O  
ATOM    523  CB  THR A 635     -28.062   1.357 -51.148  1.00 94.09      A    C  
ATOM    524  CG2 THR A 635     -26.708   1.658 -51.773  1.00 95.25      A    C  
ATOM    525  OG1 THR A 635     -27.888   0.508 -50.007  1.00 94.95      A    O  
ATOM    526  N   GLY A 636     -30.974   2.175 -51.576  1.00 88.49      A    N  
ATOM    527  CA  GLY A 636     -32.393   1.881 -51.487  1.00 80.99      A    C  
ATOM    528  C   GLY A 636     -32.615   0.432 -51.095  1.00 81.65      A    C  
ATOM    529  O   GLY A 636     -33.563  -0.210 -51.546  1.00 78.97      A    O  
ATOM    530  N   VAL A 637     -31.728  -0.075 -50.242  1.00 79.02      A    N  
ATOM    531  CA  VAL A 637     -31.783  -1.451 -49.766  1.00 77.82      A    C  
ATOM    532  C   VAL A 637     -32.346  -1.523 -48.345  1.00 77.02      A    C  
ATOM    533  O   VAL A 637     -32.429  -0.509 -47.649  1.00 80.17      A    O  
ATOM    534  CB  VAL A 637     -30.369  -2.063 -49.760  1.00 78.44      A    C  
ATOM    535  CG1 VAL A 637     -30.434  -3.547 -49.450  1.00 76.51      A    C  
ATOM    536  CG2 VAL A 637     -29.702  -1.816 -51.099  1.00 78.57      A    C  
ATOM    537  N   SER A 638     -32.740  -2.719 -47.918  1.00 66.76      A    N  
ATOM    538  CA  SER A 638     -33.257  -2.895 -46.567  1.00 64.50      A    C  
ATOM    539  C   SER A 638     -32.169  -3.584 -45.745  1.00 62.94      A    C  
ATOM    540  O   SER A 638     -31.479  -4.476 -46.244  1.00 61.82      A    O  
ATOM    541  CB  SER A 638     -34.519  -3.754 -46.568  1.00 51.47      A    C  
ATOM    542  OG  SER A 638     -34.184  -5.109 -46.792  1.00 63.75      A    O  
ATOM    543  N   ILE A 639     -32.007  -3.161 -44.492  1.00 51.41      A    N  
ATOM    544  CA  ILE A 639     -30.999  -3.758 -43.628  1.00 45.19      A    C  
ATOM    545  C   ILE A 639     -31.529  -4.030 -42.236  1.00 38.27      A    C  
ATOM    546  O   ILE A 639     -32.617  -3.579 -41.862  1.00 38.54      A    O  
ATOM    547  CB  ILE A 639     -29.751  -2.868 -43.486  1.00 51.19      A    C  
ATOM    548  CG1 ILE A 639     -30.126  -1.543 -42.811  1.00 45.12      A    C  
ATOM    549  CG2 ILE A 639     -29.120  -2.638 -44.847  1.00 54.99      A    C  
ATOM    550  CD1 ILE A 639     -28.926  -0.696 -42.417  1.00 52.68      A    C  
ATOM    551  N   GLN A 640     -30.751  -4.798 -41.482  1.00 43.70      A    N  
ATOM    552  CA  GLN A 640     -31.097  -5.147 -40.112  1.00 45.27      A    C  
ATOM    553  C   GLN A 640     -30.648  -4.014 -39.193  1.00 37.27      A    C  
ATOM    554  O   GLN A 640     -29.574  -3.440 -39.380  1.00 35.66      A    O  
ATOM    555  CB  GLN A 640     -30.387  -6.441 -39.710  1.00 48.75      A    C  
ATOM    556  CG  GLN A 640     -30.785  -7.627 -40.562  1.00 55.36      A    C  
ATOM    557  CD  GLN A 640     -32.282  -7.814 -40.590  1.00 64.27      A    C  
ATOM    558  NE2 GLN A 640     -32.883  -7.613 -41.762  1.00 68.68      A    N  
ATOM    559  OE1 GLN A 640     -32.902  -8.118 -39.565  1.00 63.04      A    O  
ATOM    560  N   VAL A 641     -31.467  -3.701 -38.202  1.00 39.47      A    N  
ATOM    561  CA  VAL A 641     -31.120  -2.642 -37.256  1.00 40.45      A    C  
ATOM    562  C   VAL A 641     -31.568  -3.057 -35.850  1.00 34.76      A    C  
ATOM    563  O   VAL A 641     -32.275  -4.043 -35.693  1.00 34.92      A    O  
ATOM    564  CB  VAL A 641     -31.815  -1.303 -37.638  1.00 30.50      A    C  
ATOM    565  CG1 VAL A 641     -31.438  -0.890 -39.060  1.00 36.49      A    C  
ATOM    566  CG2 VAL A 641     -33.308  -1.452 -37.500  1.00 22.84      A    C  
ATOM    567  N   ALA A 642     -31.137  -2.302 -34.842  1.00 34.06      A    N  
ATOM    568  CA  ALA A 642     -31.490  -2.550 -33.450  1.00 30.42      A    C  
ATOM    569  C   ALA A 642     -32.270  -1.312 -33.035  1.00 28.24      A    C  
ATOM    570  O   ALA A 642     -31.812  -0.201 -33.220  1.00 34.75      A    O  
ATOM    571  CB  ALA A 642     -30.221  -2.706 -32.597  1.00 27.73      A    C  
ATOM    572  N   VAL A 643     -33.447  -1.500 -32.469  1.00 28.91      A    N  
ATOM    573  CA  VAL A 643     -34.289  -0.377 -32.095  1.00 29.93      A    C  
ATOM    574  C   VAL A 643     -34.503  -0.225 -30.596  1.00 38.30      A    C  
ATOM    575  O   VAL A 643     -35.100  -1.098 -29.953  1.00 31.80      A    O  
ATOM    576  CB  VAL A 643     -35.685  -0.519 -32.772  1.00 32.26      A    C  
ATOM    577  CG1 VAL A 643     -36.525   0.691 -32.487  1.00 27.72      A    C  
ATOM    578  CG2 VAL A 643     -35.518  -0.728 -34.270  1.00 34.15      A    C  
ATOM    579  N   LYS A 644     -34.027   0.884 -30.034  1.00 33.48      A    N  
ATOM    580  CA  LYS A 644     -34.222   1.127 -28.604  1.00 32.73      A    C  
ATOM    581  C   LYS A 644     -35.572   1.782 -28.398  1.00 31.87      A    C  
ATOM    582  O   LYS A 644     -35.980   2.648 -29.177  1.00 35.08      A    O  
ATOM    583  CB  LYS A 644     -33.157   2.067 -28.036  1.00 32.17      A    C  
ATOM    584  CG  LYS A 644     -31.751   1.514 -27.927  1.00 33.49      A    C  
ATOM    585  CD  LYS A 644     -30.934   2.379 -26.940  1.00 37.89      A    C  
ATOM    586  CE  LYS A 644     -29.491   1.920 -26.874  1.00 40.51      A    C  
ATOM    587  NZ  LYS A 644     -28.747   2.575 -25.770  1.00 42.15      A    N1+
ATOM    588  N   MET A 645     -36.272   1.390 -27.345  1.00 29.84      A    N  
ATOM    589  CA  MET A 645     -37.572   1.989 -27.049  1.00 33.05      A    C  
ATOM    590  C   MET A 645     -37.918   1.844 -25.575  1.00 37.20      A    C  
ATOM    591  O   MET A 645     -37.346   1.022 -24.871  1.00 38.43      A    O  
ATOM    592  CB  MET A 645     -38.669   1.351 -27.904  1.00 33.07      A    C  
ATOM    593  CG  MET A 645     -38.706  -0.168 -27.855  1.00 42.66      A    C  
ATOM    594  SD  MET A 645     -39.962  -0.843 -28.975  1.00 48.33      A    S  
ATOM    595  CE  MET A 645     -39.022  -1.176 -30.408  1.00 39.72      A    C  
ATOM    596  N   LEU A 646     -38.859   2.650 -25.114  1.00 40.40      A    N  
ATOM    597  CA  LEU A 646     -39.251   2.604 -23.716  1.00 47.04      A    C  
ATOM    598  C   LEU A 646     -40.505   1.798 -23.476  1.00 49.65      A    C  
ATOM    599  O   LEU A 646     -41.262   1.502 -24.399  1.00 44.84      A    O  
ATOM    600  CB  LEU A 646     -39.484   4.018 -23.172  1.00 37.49      A    C  
ATOM    601  CG  LEU A 646     -38.285   4.966 -23.116  1.00 46.35      A    C  
ATOM    602  CD1 LEU A 646     -38.736   6.306 -22.563  1.00 46.18      A    C  
ATOM    603  CD2 LEU A 646     -37.196   4.368 -22.242  1.00 39.81      A    C  
ATOM    604  N   LYS A 647     -40.703   1.467 -22.206  1.00 48.65      A    N  
ATOM    605  CA  LYS A 647     -41.866   0.744 -21.729  1.00 57.47      A    C  
ATOM    606  C   LYS A 647     -43.054   1.612 -22.143  1.00 57.31      A    C  
ATOM    607  O   LYS A 647     -42.951   2.839 -22.148  1.00 56.98      A    O  
ATOM    608  CB  LYS A 647     -41.818   0.678 -20.199  1.00 60.62      A    C  
ATOM    609  CG  LYS A 647     -42.350  -0.594 -19.568  1.00 69.39      A    C  
ATOM    610  CD  LYS A 647     -41.305  -1.699 -19.578  1.00 76.88      A    C  
ATOM    611  CE  LYS A 647     -41.779  -2.902 -18.766  1.00 79.80      A    C  
ATOM    612  NZ  LYS A 647     -40.775  -4.002 -18.740  1.00 78.62      A    N1+
ATOM    613  N   GLU A 648     -44.173   0.988 -22.490  1.00 63.50      A    N  
ATOM    614  CA  GLU A 648     -45.363   1.742 -22.873  1.00 60.69      A    C  
ATOM    615  C   GLU A 648     -45.822   2.589 -21.690  1.00 56.91      A    C  
ATOM    616  O   GLU A 648     -46.121   3.771 -21.840  1.00 61.48      A    O  
ATOM    617  CB  GLU A 648     -46.479   0.786 -23.288  1.00 69.22      A    C  
ATOM    618  CG  GLU A 648     -46.149  -0.043 -24.523  1.00 84.99      A    C  
ATOM    619  CD  GLU A 648     -47.170  -1.136 -24.788  1.00 91.86      A    C  
ATOM    620  OE1 GLU A 648     -48.383  -0.829 -24.798  1.00 91.66      A    O  
ATOM    621  OE2 GLU A 648     -46.756  -2.301 -24.992  1.00 96.48      A    O1-
ATOM    622  N   ARG A 655     -38.596   9.492 -21.363  1.00 34.48      A    N  
ATOM    623  CA  ARG A 655     -38.692   9.936 -22.764  1.00 47.68      A    C  
ATOM    624  C   ARG A 655     -37.657  11.005 -23.085  1.00 42.77      A    C  
ATOM    625  O   ARG A 655     -36.971  10.910 -24.102  1.00 36.69      A    O  
ATOM    626  CB  ARG A 655     -40.087  10.486 -23.098  1.00 45.12      A    C  
ATOM    627  CG  ARG A 655     -41.190   9.437 -23.183  1.00 58.39      A    C  
ATOM    628  CD  ARG A 655     -42.396   9.926 -23.999  1.00 56.97      A    C  
ATOM    629  NE  ARG A 655     -43.001  11.146 -23.460  1.00 68.56      A    N  
ATOM    630  CZ  ARG A 655     -43.554  11.252 -22.253  1.00 74.29      A    C  
ATOM    631  NH1 ARG A 655     -43.589  10.206 -21.433  1.00 77.19      A    N1+
ATOM    632  NH2 ARG A 655     -44.072  12.408 -21.860  1.00 70.02      A    N  
ATOM    633  N   GLU A 656     -37.539  12.014 -22.221  1.00 36.63      A    N  
ATOM    634  CA  GLU A 656     -36.562  13.081 -22.438  1.00 41.57      A    C  
ATOM    635  C   GLU A 656     -35.159  12.469 -22.340  1.00 43.61      A    C  
ATOM    636  O   GLU A 656     -34.227  12.856 -23.065  1.00 37.38      A    O  
ATOM    637  CB  GLU A 656     -36.743  14.193 -21.395  1.00 52.95      A    C  
ATOM    638  CG  GLU A 656     -36.264  15.563 -21.868  1.00 56.67      A    C  
ATOM    639  CD  GLU A 656     -36.819  15.915 -23.242  1.00 67.95      A    C  
ATOM    640  OE1 GLU A 656     -38.059  15.998 -23.380  1.00 65.65      A    O  
ATOM    641  OE2 GLU A 656     -36.017  16.094 -24.186  1.00 58.47      A    O1-
ATOM    642  N   ALA A 657     -35.022  11.486 -21.452  1.00 38.29      A    N  
ATOM    643  CA  ALA A 657     -33.749  10.800 -21.280  1.00 34.62      A    C  
ATOM    644  C   ALA A 657     -33.365  10.090 -22.584  1.00 26.00      A    C  
ATOM    645  O   ALA A 657     -32.197  10.098 -22.998  1.00 28.64      A    O  
ATOM    646  CB  ALA A 657     -33.857   9.793 -20.152  1.00 37.02      A    C  
ATOM    647  N   LEU A 658     -34.350   9.490 -23.246  1.00 31.22      A    N  
ATOM    648  CA  LEU A 658     -34.066   8.794 -24.498  1.00 33.43      A    C  
ATOM    649  C   LEU A 658     -33.785   9.851 -25.582  1.00 28.75      A    C  
ATOM    650  O   LEU A 658     -32.933   9.653 -26.445  1.00 34.18      A    O  
ATOM    651  CB  LEU A 658     -35.243   7.885 -24.885  1.00 30.92      A    C  
ATOM    652  CG  LEU A 658     -34.974   6.826 -25.964  1.00 30.14      A    C  
ATOM    653  CD1 LEU A 658     -33.762   5.983 -25.598  1.00 25.83      A    C  
ATOM    654  CD2 LEU A 658     -36.225   5.951 -26.146  1.00 32.07      A    C  
ATOM    655  N   MET A 659     -34.487  10.979 -25.524  1.00 32.67      A    N  
ATOM    656  CA  MET A 659     -34.237  12.052 -26.490  1.00 30.40      A    C  
ATOM    657  C   MET A 659     -32.805  12.579 -26.321  1.00 33.86      A    C  
ATOM    658  O   MET A 659     -32.131  12.866 -27.309  1.00 32.09      A    O  
ATOM    659  CB  MET A 659     -35.245  13.205 -26.312  1.00 24.50      A    C  
ATOM    660  CG  MET A 659     -36.634  12.919 -26.905  1.00 31.26      A    C  
ATOM    661  SD  MET A 659     -36.581  12.386 -28.692  1.00 39.36      A    S  
ATOM    662  CE  MET A 659     -36.196  13.984 -29.506  1.00 38.92      A    C  
ATOM    663  N   SER A 660     -32.334  12.684 -25.073  1.00 29.97      A    N  
ATOM    664  CA  SER A 660     -30.982  13.185 -24.811  1.00 25.42      A    C  
ATOM    665  C   SER A 660     -29.931  12.232 -25.316  1.00 21.54      A    C  
ATOM    666  O   SER A 660     -28.865  12.641 -25.789  1.00 28.49      A    O  
ATOM    667  CB  SER A 660     -30.760  13.445 -23.298  1.00 26.59      A    C  
ATOM    668  OG  SER A 660     -31.491  14.600 -22.882  1.00 26.44      A    O  
ATOM    669  N   GLU A 661     -30.205  10.941 -25.173  1.00 23.25      A    N  
ATOM    670  CA  GLU A 661     -29.273   9.960 -25.659  1.00 21.02      A    C  
ATOM    671  C   GLU A 661     -29.227  10.117 -27.189  1.00 16.64      A    C  
ATOM    672  O   GLU A 661     -28.162  10.093 -27.781  1.00 18.21      A    O  
ATOM    673  CB  GLU A 661     -29.739   8.542 -25.298  1.00 23.02      A    C  
ATOM    674  CG  GLU A 661     -28.845   7.490 -25.898  1.00 26.69      A    C  
ATOM    675  CD  GLU A 661     -29.251   6.057 -25.550  1.00 36.00      A    C  
ATOM    676  OE1 GLU A 661     -28.562   5.148 -26.035  1.00 31.84      A    O  
ATOM    677  OE2 GLU A 661     -30.235   5.842 -24.806  1.00 33.64      A    O1-
ATOM    678  N   LEU A 662     -30.398  10.248 -27.808  1.00 22.26      A    N  
ATOM    679  CA  LEU A 662     -30.491  10.439 -29.262  1.00 24.71      A    C  
ATOM    680  C   LEU A 662     -29.645  11.653 -29.684  1.00 24.21      A    C  
ATOM    681  O   LEU A 662     -28.754  11.546 -30.542  1.00 26.37      A    O  
ATOM    682  CB  LEU A 662     -31.953  10.679 -29.666  1.00 19.90      A    C  
ATOM    683  CG  LEU A 662     -32.232  11.114 -31.118  1.00 26.57      A    C  
ATOM    684  CD1 LEU A 662     -31.609  10.117 -32.098  1.00 19.50      A    C  
ATOM    685  CD2 LEU A 662     -33.725  11.216 -31.343  1.00 23.12      A    C  
ATOM    686  N   LYS A 663     -29.921  12.812 -29.070  1.00 25.07      A    N  
ATOM    687  CA  LYS A 663     -29.189  14.028 -29.425  1.00 25.31      A    C  
ATOM    688  C   LYS A 663     -27.707  13.816 -29.270  1.00 30.66      A    C  
ATOM    689  O   LYS A 663     -26.919  14.232 -30.112  1.00 25.08      A    O  
ATOM    690  CB  LYS A 663     -29.619  15.207 -28.546  1.00 28.56      A    C  
ATOM    691  CG  LYS A 663     -31.059  15.669 -28.756  1.00 29.60      A    C  
ATOM    692  CD  LYS A 663     -31.450  16.640 -27.649  1.00 23.27      A    C  
ATOM    693  CE  LYS A 663     -32.923  16.787 -27.535  1.00 31.62      A    C  
ATOM    694  NZ  LYS A 663     -33.275  17.726 -26.445  1.00 25.86      A    N1+
ATOM    695  N   MET A 664     -27.326  13.148 -28.188  1.00 30.76      A    N  
ATOM    696  CA  MET A 664     -25.918  12.896 -27.944  1.00 26.62      A    C  
ATOM    697  C   MET A 664     -25.307  12.054 -29.076  1.00 29.68      A    C  
ATOM    698  O   MET A 664     -24.233  12.377 -29.594  1.00 26.27      A    O  
ATOM    699  CB  MET A 664     -25.749  12.208 -26.580  1.00 31.70      A    C  
ATOM    700  CG  MET A 664     -24.306  11.952 -26.144  1.00 41.46      A    C  
ATOM    701  SD  MET A 664     -23.537  10.495 -26.891  1.00 50.85      A    S  
ATOM    702  CE  MET A 664     -22.526   9.945 -25.538  1.00 49.19      A    C  
ATOM    703  N   MET A 665     -25.988  10.986 -29.481  1.00 24.22      A    N  
ATOM    704  CA  MET A 665     -25.426  10.140 -30.536  1.00 29.78      A    C  
ATOM    705  C   MET A 665     -25.398  10.827 -31.914  1.00 26.95      A    C  
ATOM    706  O   MET A 665     -24.563  10.492 -32.748  1.00 27.90      A    O  
ATOM    707  CB  MET A 665     -26.184   8.811 -30.617  1.00 26.98      A    C  
ATOM    708  CG  MET A 665     -26.062   7.941 -29.344  1.00 32.44      A    C  
ATOM    709  SD  MET A 665     -24.345   7.580 -28.890  1.00 33.13      A    S  
ATOM    710  CE  MET A 665     -23.889   6.207 -30.083  1.00 25.44      A    C  
ATOM    711  N   THR A 666     -26.304  11.774 -32.157  1.00 26.19      A    N  
ATOM    712  CA  THR A 666     -26.285  12.489 -33.441  1.00 35.66      A    C  
ATOM    713  C   THR A 666     -25.063  13.423 -33.522  1.00 37.32      A    C  
ATOM    714  O   THR A 666     -24.661  13.825 -34.604  1.00 33.00      A    O  
ATOM    715  CB  THR A 666     -27.528  13.382 -33.662  1.00 29.43      A    C  
ATOM    716  CG2 THR A 666     -28.798  12.554 -33.705  1.00 27.56      A    C  
ATOM    717  OG1 THR A 666     -27.602  14.375 -32.629  1.00 36.22      A    O  
ATOM    718  N   GLN A 667     -24.487  13.759 -32.372  1.00 31.30      A    N  
ATOM    719  CA  GLN A 667     -23.334  14.654 -32.306  1.00 33.09      A    C  
ATOM    720  C   GLN A 667     -22.002  13.929 -32.286  1.00 35.56      A    C  
ATOM    721  O   GLN A 667     -20.967  14.523 -32.554  1.00 32.61      A    O  
ATOM    722  CB  GLN A 667     -23.410  15.512 -31.041  1.00 40.55      A    C  
ATOM    723  CG  GLN A 667     -24.640  16.376 -30.946  1.00 61.37      A    C  
ATOM    724  CD  GLN A 667     -24.350  17.829 -31.252  1.00 74.23      A    C  
ATOM    725  NE2 GLN A 667     -24.523  18.688 -30.251  1.00 79.12      A    N  
ATOM    726  OE1 GLN A 667     -23.966  18.179 -32.369  1.00 80.71      A    O  
ATOM    727  N   LEU A 668     -22.030  12.643 -31.954  1.00 37.25      A    N  
ATOM    728  CA  LEU A 668     -20.812  11.854 -31.840  1.00 36.90      A    C  
ATOM    729  C   LEU A 668     -20.041  11.609 -33.130  1.00 36.89      A    C  
ATOM    730  O   LEU A 668     -18.810  11.667 -33.144  1.00 34.43      A    O  
ATOM    731  CB  LEU A 668     -21.141  10.489 -31.221  1.00 37.69      A    C  
ATOM    732  CG  LEU A 668     -20.367   9.889 -30.048  1.00 38.91      A    C  
ATOM    733  CD1 LEU A 668     -20.237   8.392 -30.294  1.00 37.93      A    C  
ATOM    734  CD2 LEU A 668     -19.009  10.518 -29.878  1.00 41.25      A    C  
ATOM    735  N   GLY A 669     -20.757  11.336 -34.213  1.00 39.02      A    N  
ATOM    736  CA  GLY A 669     -20.080  11.005 -35.450  1.00 41.45      A    C  
ATOM    737  C   GLY A 669     -19.925   9.486 -35.379  1.00 50.42      A    C  
ATOM    738  O   GLY A 669     -20.039   8.904 -34.303  1.00 53.01      A    O  
ATOM    739  N   SER A 670     -19.661   8.834 -36.500  1.00 42.82      A    N  
ATOM    740  CA  SER A 670     -19.540   7.383 -36.502  1.00 38.73      A    C  
ATOM    741  C   SER A 670     -18.114   6.840 -36.403  1.00 35.64      A    C  
ATOM    742  O   SER A 670     -17.131   7.532 -36.686  1.00 33.35      A    O  
ATOM    743  CB  SER A 670     -20.198   6.825 -37.762  1.00 41.43      A    C  
ATOM    744  OG  SER A 670     -19.554   7.360 -38.904  1.00 50.51      A    O  
ATOM    745  N   HIS A 671     -18.020   5.581 -35.983  1.00 34.15      A    N  
ATOM    746  CA  HIS A 671     -16.743   4.901 -35.861  1.00 32.96      A    C  
ATOM    747  C   HIS A 671     -16.988   3.391 -36.039  1.00 26.94      A    C  
ATOM    748  O   HIS A 671     -18.052   2.883 -35.696  1.00 35.74      A    O  
ATOM    749  CB  HIS A 671     -16.101   5.182 -34.502  1.00 31.48      A    C  
ATOM    750  CG  HIS A 671     -14.765   4.522 -34.330  1.00 34.08      A    C  
ATOM    751  CD2 HIS A 671     -14.438   3.237 -34.052  1.00 29.52      A    C  
ATOM    752  ND1 HIS A 671     -13.571   5.186 -34.524  1.00 32.51      A    N  
ATOM    753  CE1 HIS A 671     -12.567   4.338 -34.375  1.00 31.51      A    C  
ATOM    754  NE2 HIS A 671     -13.067   3.148 -34.088  1.00 34.97      A    N  
ATOM    755  N   GLU A 672     -16.016   2.686 -36.602  1.00 32.67      A    N  
ATOM    756  CA  GLU A 672     -16.174   1.251 -36.822  1.00 38.90      A    C  
ATOM    757  C   GLU A 672     -16.404   0.429 -35.542  1.00 33.94      A    C  
ATOM    758  O   GLU A 672     -17.129  -0.563 -35.566  1.00 31.56      A    O  
ATOM    759  CB  GLU A 672     -14.959   0.659 -37.565  1.00 38.43      A    C  
ATOM    760  CG  GLU A 672     -14.953  -0.892 -37.475  1.00 57.25      A    C  
ATOM    761  CD  GLU A 672     -14.116  -1.618 -38.535  1.00 56.88      A    C  
ATOM    762  OE1 GLU A 672     -12.908  -1.329 -38.682  1.00 58.72      A    O  
ATOM    763  OE2 GLU A 672     -14.680  -2.505 -39.209  1.00 51.46      A    O1-
ATOM    764  N   ASN A 673     -15.798   0.855 -34.440  1.00 37.52      A    N  
ATOM    765  CA  ASN A 673     -15.894   0.134 -33.168  1.00 28.53      A    C  
ATOM    766  C   ASN A 673     -16.882   0.686 -32.158  1.00 36.30      A    C  
ATOM    767  O   ASN A 673     -16.741   0.468 -30.942  1.00 27.68      A    O  
ATOM    768  CB  ASN A 673     -14.507   0.049 -32.570  1.00 24.98      A    C  
ATOM    769  CG  ASN A 673     -13.515  -0.554 -33.550  1.00 26.61      A    C  
ATOM    770  ND2 ASN A 673     -13.827  -1.757 -34.038  1.00 27.30      A    N  
ATOM    771  OD1 ASN A 673     -12.488   0.045 -33.863  1.00 37.47      A    O  
ATOM    772  N   ILE A 674     -17.887   1.387 -32.678  1.00 26.45      A    N  
ATOM    773  CA  ILE A 674     -18.959   1.949 -31.862  1.00 28.61      A    C  
ATOM    774  C   ILE A 674     -20.257   1.510 -32.517  1.00 35.54      A    C  
ATOM    775  O   ILE A 674     -20.314   1.377 -33.738  1.00 28.46      A    O  
ATOM    776  CB  ILE A 674     -18.925   3.511 -31.867  1.00 32.67      A    C  
ATOM    777  CG1 ILE A 674     -17.622   4.018 -31.239  1.00 34.52      A    C  
ATOM    778  CG2 ILE A 674     -20.140   4.066 -31.127  1.00 27.03      A    C  
ATOM    779  CD1 ILE A 674     -17.487   3.674 -29.768  1.00 30.42      A    C  
ATOM    780  N   VAL A 675     -21.285   1.249 -31.721  1.00 26.22      A    N  
ATOM    781  CA  VAL A 675     -22.586   0.907 -32.285  1.00 23.60      A    C  
ATOM    782  C   VAL A 675     -23.153   2.275 -32.653  1.00 39.31      A    C  
ATOM    783  O   VAL A 675     -23.543   3.059 -31.780  1.00 27.73      A    O  
ATOM    784  CB  VAL A 675     -23.509   0.246 -31.280  1.00 31.48      A    C  
ATOM    785  CG1 VAL A 675     -24.912   0.184 -31.844  1.00 29.53      A    C  
ATOM    786  CG2 VAL A 675     -23.003  -1.184 -30.962  1.00 32.24      A    C  
ATOM    787  N   ASN A 676     -23.184   2.555 -33.953  1.00 36.56      A    N  
ATOM    788  CA  ASN A 676     -23.632   3.852 -34.455  1.00 30.67      A    C  
ATOM    789  C   ASN A 676     -25.128   4.056 -34.626  1.00 22.27      A    C  
ATOM    790  O   ASN A 676     -25.876   3.141 -34.979  1.00 32.36      A    O  
ATOM    791  CB  ASN A 676     -22.925   4.143 -35.793  1.00 27.74      A    C  
ATOM    792  CG  ASN A 676     -21.407   4.012 -35.699  1.00 29.25      A    C  
ATOM    793  ND2 ASN A 676     -20.843   3.105 -36.491  1.00 32.66      A    N  
ATOM    794  OD1 ASN A 676     -20.747   4.721 -34.931  1.00 31.53      A    O  
ATOM    795  N   LEU A 677     -25.563   5.288 -34.385  1.00 22.53      A    N  
ATOM    796  CA  LEU A 677     -26.964   5.656 -34.568  1.00 24.82      A    C  
ATOM    797  C   LEU A 677     -27.216   5.742 -36.084  1.00 28.65      A    C  
ATOM    798  O   LEU A 677     -26.352   6.204 -36.816  1.00 26.09      A    O  
ATOM    799  CB  LEU A 677     -27.223   7.029 -33.958  1.00 35.72      A    C  
ATOM    800  CG  LEU A 677     -28.626   7.574 -34.188  1.00 30.00      A    C  
ATOM    801  CD1 LEU A 677     -29.584   6.941 -33.188  1.00 27.33      A    C  
ATOM    802  CD2 LEU A 677     -28.596   9.088 -34.065  1.00 29.82      A    C  
ATOM    803  N   LEU A 678     -28.387   5.319 -36.548  1.00 29.63      A    N  
ATOM    804  CA  LEU A 678     -28.702   5.371 -37.979  1.00 33.25      A    C  
ATOM    805  C   LEU A 678     -29.916   6.271 -38.242  1.00 38.38      A    C  
ATOM    806  O   LEU A 678     -30.047   6.861 -39.319  1.00 30.91      A    O  
ATOM    807  CB  LEU A 678     -28.995   3.954 -38.513  1.00 26.62      A    C  
ATOM    808  CG  LEU A 678     -27.842   2.942 -38.455  1.00 30.79      A    C  
ATOM    809  CD1 LEU A 678     -28.317   1.554 -38.925  1.00 25.28      A    C  
ATOM    810  CD2 LEU A 678     -26.686   3.456 -39.302  1.00 27.76      A    C  
ATOM    811  N   GLY A 679     -30.803   6.366 -37.257  1.00 28.98      A    N  
ATOM    812  CA  GLY A 679     -31.980   7.199 -37.405  1.00 27.06      A    C  
ATOM    813  C   GLY A 679     -32.851   7.164 -36.164  1.00 30.88      A    C  
ATOM    814  O   GLY A 679     -32.501   6.511 -35.179  1.00 27.19      A    O  
ATOM    815  N   ALA A 680     -33.984   7.861 -36.214  1.00 27.66      A    N  
ATOM    816  CA  ALA A 680     -34.920   7.912 -35.090  1.00 33.97      A    C  
ATOM    817  C   ALA A 680     -36.328   8.260 -35.549  1.00 28.74      A    C  
ATOM    818  O   ALA A 680     -36.520   8.886 -36.576  1.00 34.14      A    O  
ATOM    819  CB  ALA A 680     -34.456   8.949 -34.039  1.00 26.09      A    C  
ATOM    820  N   CYS A 681     -37.302   7.847 -34.754  1.00 28.05      A    N  
ATOM    821  CA  CYS A 681     -38.714   8.102 -34.993  1.00 26.41      A    C  
ATOM    822  C   CYS A 681     -39.151   8.772 -33.696  1.00 32.30      A    C  
ATOM    823  O   CYS A 681     -39.202   8.137 -32.646  1.00 33.16      A    O  
ATOM    824  CB  CYS A 681     -39.463   6.776 -35.180  1.00 27.71      A    C  
ATOM    825  SG  CYS A 681     -38.742   5.730 -36.426  1.00 33.71      A    S  
ATOM    826  N   THR A 682     -39.490  10.050 -33.774  1.00 30.00      A    N  
ATOM    827  CA  THR A 682     -39.831  10.819 -32.585  1.00 33.51      A    C  
ATOM    828  C   THR A 682     -41.074  11.692 -32.684  1.00 38.51      A    C  
ATOM    829  O   THR A 682     -41.402  12.380 -31.729  1.00 37.58      A    O  
ATOM    830  CB  THR A 682     -38.688  11.790 -32.281  1.00 40.59      A    C  
ATOM    831  CG2 THR A 682     -37.348  11.056 -32.279  1.00 31.63      A    C  
ATOM    832  OG1 THR A 682     -38.649  12.792 -33.319  1.00 32.21      A    O  
ATOM    833  N   LEU A 683     -41.771  11.666 -33.813  1.00 41.75      A    N  
ATOM    834  CA  LEU A 683     -42.892  12.574 -33.992  1.00 37.80      A    C  
ATOM    835  C   LEU A 683     -44.322  12.072 -33.976  1.00 42.32      A    C  
ATOM    836  O   LEU A 683     -45.178  12.685 -33.348  1.00 44.24      A    O  
ATOM    837  CB  LEU A 683     -42.670  13.367 -35.284  1.00 42.41      A    C  
ATOM    838  CG  LEU A 683     -41.408  14.234 -35.357  1.00 46.29      A    C  
ATOM    839  CD1 LEU A 683     -41.166  14.716 -36.789  1.00 45.42      A    C  
ATOM    840  CD2 LEU A 683     -41.567  15.411 -34.406  1.00 41.50      A    C  
ATOM    841  N   SER A 684     -44.598  10.979 -34.671  1.00 43.72      A    N  
ATOM    842  CA  SER A 684     -45.968  10.480 -34.740  1.00 46.79      A    C  
ATOM    843  C   SER A 684     -46.224   9.217 -33.935  1.00 52.99      A    C  
ATOM    844  O   SER A 684     -47.145   8.459 -34.245  1.00 51.82      A    O  
ATOM    845  CB  SER A 684     -46.343  10.217 -36.198  1.00 44.18      A    C  
ATOM    846  OG  SER A 684     -45.520   9.196 -36.738  1.00 44.14      A    O  
ATOM    847  N   GLY A 685     -45.417   8.990 -32.905  1.00 53.16      A    N  
ATOM    848  CA  GLY A 685     -45.594   7.802 -32.091  1.00 50.10      A    C  
ATOM    849  C   GLY A 685     -44.496   7.668 -31.061  1.00 49.53      A    C  
ATOM    850  O   GLY A 685     -43.694   8.577 -30.895  1.00 42.96      A    O  
ATOM    851  N   PRO A 686     -44.432   6.542 -30.344  1.00 48.76      A    N  
ATOM    852  CA  PRO A 686     -43.374   6.401 -29.344  1.00 47.01      A    C  
ATOM    853  C   PRO A 686     -41.985   6.591 -29.947  1.00 46.99      A    C  
ATOM    854  O   PRO A 686     -41.758   6.331 -31.138  1.00 36.52      A    O  
ATOM    855  CB  PRO A 686     -43.599   4.988 -28.796  1.00 41.10      A    C  
ATOM    856  CG  PRO A 686     -44.246   4.275 -29.943  1.00 53.53      A    C  
ATOM    857  CD  PRO A 686     -45.221   5.307 -30.458  1.00 49.96      A    C  
ATOM    858  N   ILE A 687     -41.057   7.041 -29.109  1.00 31.42      A    N  
ATOM    859  CA  ILE A 687     -39.689   7.282 -29.530  1.00 33.47      A    C  
ATOM    860  C   ILE A 687     -38.877   6.020 -29.812  1.00 39.72      A    C  
ATOM    861  O   ILE A 687     -38.794   5.122 -28.974  1.00 39.87      A    O  
ATOM    862  CB  ILE A 687     -38.942   8.101 -28.468  1.00 31.43      A    C  
ATOM    863  CG1 ILE A 687     -39.666   9.433 -28.245  1.00 34.57      A    C  
ATOM    864  CG2 ILE A 687     -37.497   8.308 -28.902  1.00 29.90      A    C  
ATOM    865  CD1 ILE A 687     -39.114  10.265 -27.107  1.00 47.57      A    C  
ATOM    866  N   TYR A 688     -38.274   5.954 -30.997  1.00 29.27      A    N  
ATOM    867  CA  TYR A 688     -37.431   4.822 -31.346  1.00 25.72      A    C  
ATOM    868  C   TYR A 688     -36.065   5.320 -31.775  1.00 31.84      A    C  
ATOM    869  O   TYR A 688     -35.970   6.206 -32.629  1.00 32.61      A    O  
ATOM    870  CB  TYR A 688     -37.964   4.020 -32.549  1.00 38.66      A    C  
ATOM    871  CG  TYR A 688     -39.355   3.447 -32.455  1.00 42.19      A    C  
ATOM    872  CD1 TYR A 688     -39.906   3.053 -31.233  1.00 39.59      A    C  
ATOM    873  CD2 TYR A 688     -40.100   3.239 -33.617  1.00 45.89      A    C  
ATOM    874  CE1 TYR A 688     -41.175   2.458 -31.177  1.00 42.64      A    C  
ATOM    875  CE2 TYR A 688     -41.354   2.649 -33.579  1.00 50.36      A    C  
ATOM    876  CZ  TYR A 688     -41.889   2.260 -32.365  1.00 59.63      A    C  
ATOM    877  OH  TYR A 688     -43.138   1.680 -32.363  1.00 52.97      A    O  
ATOM    878  N   LEU A 689     -35.004   4.751 -31.215  1.00 27.86      A    N  
ATOM    879  CA  LEU A 689     -33.669   5.139 -31.658  1.00 27.04      A    C  
ATOM    880  C   LEU A 689     -33.211   3.925 -32.467  1.00 34.12      A    C  
ATOM    881  O   LEU A 689     -33.259   2.796 -31.975  1.00 33.67      A    O  
ATOM    882  CB  LEU A 689     -32.734   5.395 -30.475  1.00 29.71      A    C  
ATOM    883  CG  LEU A 689     -33.218   6.328 -29.347  1.00 36.47      A    C  
ATOM    884  CD1 LEU A 689     -31.976   6.938 -28.698  1.00 26.28      A    C  
ATOM    885  CD2 LEU A 689     -34.135   7.424 -29.853  1.00 25.77      A    C  
ATOM    886  N   ILE A 690     -32.791   4.160 -33.705  1.00 30.20      A    N  
ATOM    887  CA  ILE A 690     -32.372   3.096 -34.608  1.00 27.33      A    C  
ATOM    888  C   ILE A 690     -30.857   3.017 -34.721  1.00 23.81      A    C  
ATOM    889  O   ILE A 690     -30.180   3.971 -35.148  1.00 30.36      A    O  
ATOM    890  CB  ILE A 690     -32.991   3.321 -36.023  1.00 33.17      A    C  
ATOM    891  CG1 ILE A 690     -34.494   3.578 -35.887  1.00 26.86      A    C  
ATOM    892  CG2 ILE A 690     -32.745   2.103 -36.925  1.00 25.16      A    C  
ATOM    893  CD1 ILE A 690     -35.140   4.158 -37.175  1.00 34.29      A    C  
ATOM    894  N   PHE A 691     -30.324   1.866 -34.335  1.00 26.29      A    N  
ATOM    895  CA  PHE A 691     -28.895   1.646 -34.363  1.00 22.57      A    C  
ATOM    896  C   PHE A 691     -28.487   0.531 -35.309  1.00 24.09      A    C  
ATOM    897  O   PHE A 691     -29.332  -0.237 -35.785  1.00 29.28      A    O  
ATOM    898  CB  PHE A 691     -28.388   1.283 -32.952  1.00 35.76      A    C  
ATOM    899  CG  PHE A 691     -28.463   2.420 -31.946  1.00 25.97      A    C  
ATOM    900  CD1 PHE A 691     -29.633   2.676 -31.247  1.00 32.51      A    C  
ATOM    901  CD2 PHE A 691     -27.344   3.216 -31.696  1.00 33.73      A    C  
ATOM    902  CE1 PHE A 691     -29.697   3.715 -30.298  1.00 25.93      A    C  
ATOM    903  CE2 PHE A 691     -27.396   4.256 -30.752  1.00 37.06      A    C  
ATOM    904  CZ  PHE A 691     -28.578   4.502 -30.054  1.00 28.00      A    C  
ATOM    905  N   GLU A 692     -27.184   0.465 -35.566  1.00 25.31      A    N  
ATOM    906  CA  GLU A 692     -26.582  -0.596 -36.357  1.00 29.80      A    C  
ATOM    907  C   GLU A 692     -26.923  -1.879 -35.587  1.00 40.95      A    C  
ATOM    908  O   GLU A 692     -26.995  -1.867 -34.353  1.00 37.91      A    O  
ATOM    909  CB  GLU A 692     -25.055  -0.438 -36.378  1.00 31.85      A    C  
ATOM    910  CG  GLU A 692     -24.538   0.681 -37.268  1.00 34.44      A    C  
ATOM    911  CD  GLU A 692     -23.029   0.839 -37.197  1.00 42.13      A    C  
ATOM    912  OE1 GLU A 692     -22.442   1.299 -38.200  1.00 49.31      A    O  
ATOM    913  OE2 GLU A 692     -22.421   0.522 -36.145  1.00 39.33      A    O1-
ATOM    914  N   TYR A 693     -27.133  -2.972 -36.311  1.00 38.34      A    N  
ATOM    915  CA  TYR A 693     -27.460  -4.264 -35.700  1.00 40.47      A    C  
ATOM    916  C   TYR A 693     -26.199  -5.122 -35.611  1.00 39.18      A    C  
ATOM    917  O   TYR A 693     -25.362  -5.114 -36.513  1.00 40.79      A    O  
ATOM    918  CB  TYR A 693     -28.520  -4.991 -36.534  1.00 41.02      A    C  
ATOM    919  CG  TYR A 693     -28.825  -6.397 -36.071  1.00 51.15      A    C  
ATOM    920  CD1 TYR A 693     -29.344  -6.641 -34.795  1.00 50.78      A    C  
ATOM    921  CD2 TYR A 693     -28.587  -7.494 -36.909  1.00 54.26      A    C  
ATOM    922  CE1 TYR A 693     -29.617  -7.940 -34.364  1.00 53.64      A    C  
ATOM    923  CE2 TYR A 693     -28.855  -8.799 -36.489  1.00 49.55      A    C  
ATOM    924  CZ  TYR A 693     -29.371  -9.012 -35.219  1.00 58.15      A    C  
ATOM    925  OH  TYR A 693     -29.654 -10.295 -34.811  1.00 57.14      A    O  
ATOM    926  N   CYS A 694     -26.051  -5.841 -34.508  1.00 37.48      A    N  
ATOM    927  CA  CYS A 694     -24.885  -6.700 -34.318  1.00 36.04      A    C  
ATOM    928  C   CYS A 694     -25.438  -8.128 -34.172  1.00 42.76      A    C  
ATOM    929  O   CYS A 694     -25.965  -8.500 -33.117  1.00 41.97      A    O  
ATOM    930  CB  CYS A 694     -24.103  -6.243 -33.068  1.00 36.46      A    C  
ATOM    931  SG  CYS A 694     -23.339  -4.578 -33.230  1.00 35.68      A    S  
ATOM    932  N   CYS A 695     -25.329  -8.911 -35.249  1.00 35.68      A    N  
ATOM    933  CA  CYS A 695     -25.870 -10.271 -35.288  1.00 41.20      A    C  
ATOM    934  C   CYS A 695     -25.478 -11.274 -34.195  1.00 37.65      A    C  
ATOM    935  O   CYS A 695     -26.300 -12.102 -33.823  1.00 44.73      A    O  
ATOM    936  CB  CYS A 695     -25.620 -10.897 -36.678  1.00 27.96      A    C  
ATOM    937  SG  CYS A 695     -23.917 -10.868 -37.276  1.00 50.80      A    S  
ATOM    938  N   TYR A 696     -24.263 -11.195 -33.657  1.00 45.28      A    N  
ATOM    939  CA  TYR A 696     -23.829 -12.164 -32.641  1.00 42.35      A    C  
ATOM    940  C   TYR A 696     -23.925 -11.799 -31.149  1.00 41.98      A    C  
ATOM    941  O   TYR A 696     -23.213 -12.378 -30.328  1.00 40.28      A    O  
ATOM    942  CB  TYR A 696     -22.406 -12.608 -32.962  1.00 34.34      A    C  
ATOM    943  CG  TYR A 696     -22.261 -13.137 -34.371  1.00 52.87      A    C  
ATOM    944  CD1 TYR A 696     -23.099 -14.146 -34.850  1.00 52.31      A    C  
ATOM    945  CD2 TYR A 696     -21.293 -12.624 -35.229  1.00 59.24      A    C  
ATOM    946  CE1 TYR A 696     -22.976 -14.628 -36.158  1.00 60.55      A    C  
ATOM    947  CE2 TYR A 696     -21.159 -13.096 -36.533  1.00 68.24      A    C  
ATOM    948  CZ  TYR A 696     -22.003 -14.094 -36.993  1.00 64.52      A    C  
ATOM    949  OH  TYR A 696     -21.877 -14.532 -38.290  1.00 69.94      A    O  
ATOM    950  N   GLY A 697     -24.810 -10.860 -30.809  1.00 41.80      A    N  
ATOM    951  CA  GLY A 697     -24.997 -10.442 -29.428  1.00 41.27      A    C  
ATOM    952  C   GLY A 697     -23.807  -9.826 -28.695  1.00 32.40      A    C  
ATOM    953  O   GLY A 697     -22.777  -9.506 -29.289  1.00 32.35      A    O  
ATOM    954  N   ASP A 698     -23.958  -9.685 -27.377  1.00 38.28      A    N  
ATOM    955  CA  ASP A 698     -22.929  -9.079 -26.533  1.00 28.42      A    C  
ATOM    956  C   ASP A 698     -21.674  -9.944 -26.407  1.00 23.75      A    C  
ATOM    957  O   ASP A 698     -21.747 -11.194 -26.354  1.00 31.53      A    O  
ATOM    958  CB  ASP A 698     -23.510  -8.772 -25.146  1.00 33.36      A    C  
ATOM    959  CG  ASP A 698     -23.750 -10.032 -24.323  1.00 31.03      A    C  
ATOM    960  OD1 ASP A 698     -24.897 -10.531 -24.280  1.00 30.63      A    O  
ATOM    961  OD2 ASP A 698     -22.772 -10.518 -23.730  1.00 32.40      A    O1-
ATOM    962  N   LEU A 699     -20.518  -9.289 -26.382  1.00 22.87      A    N  
ATOM    963  CA  LEU A 699     -19.243  -9.995 -26.287  1.00 24.47      A    C  
ATOM    964  C   LEU A 699     -19.105 -10.973 -25.074  1.00 29.36      A    C  
ATOM    965  O   LEU A 699     -18.379 -11.953 -25.170  1.00 26.66      A    O  
ATOM    966  CB  LEU A 699     -18.106  -8.985 -26.254  1.00 26.41      A    C  
ATOM    967  CG  LEU A 699     -16.678  -9.522 -26.070  1.00 28.83      A    C  
ATOM    968  CD1 LEU A 699     -16.247 -10.385 -27.298  1.00 31.42      A    C  
ATOM    969  CD2 LEU A 699     -15.747  -8.328 -25.905  1.00 20.90      A    C  
ATOM    970  N   LEU A 700     -19.776 -10.715 -23.948  1.00 31.76      A    N  
ATOM    971  CA  LEU A 700     -19.652 -11.627 -22.795  1.00 31.55      A    C  
ATOM    972  C   LEU A 700     -20.257 -12.995 -23.118  1.00 24.81      A    C  
ATOM    973  O   LEU A 700     -19.625 -14.023 -22.914  1.00 29.69      A    O  
ATOM    974  CB  LEU A 700     -20.344 -11.072 -21.540  1.00 24.24      A    C  
ATOM    975  CG  LEU A 700     -20.222 -11.978 -20.294  1.00 28.86      A    C  
ATOM    976  CD1 LEU A 700     -18.739 -12.187 -19.943  1.00 27.44      A    C  
ATOM    977  CD2 LEU A 700     -20.972 -11.345 -19.117  1.00 26.25      A    C  
ATOM    978  N   ASN A 701     -21.491 -13.000 -23.601  1.00 27.74      A    N  
ATOM    979  CA  ASN A 701     -22.127 -14.251 -23.983  1.00 31.40      A    C  
ATOM    980  C   ASN A 701     -21.414 -14.929 -25.141  1.00 30.84      A    C  
ATOM    981  O   ASN A 701     -21.324 -16.152 -25.194  1.00 34.70      A    O  
ATOM    982  CB  ASN A 701     -23.594 -14.013 -24.312  1.00 32.39      A    C  
ATOM    983  CG  ASN A 701     -24.450 -14.003 -23.072  1.00 44.35      A    C  
ATOM    984  ND2 ASN A 701     -25.146 -12.891 -22.829  1.00 42.83      A    N  
ATOM    985  OD1 ASN A 701     -24.478 -14.990 -22.321  1.00 40.67      A    O  
ATOM    986  N   TYR A 702     -20.869 -14.132 -26.049  1.00 34.94      A    N  
ATOM    987  CA  TYR A 702     -20.158 -14.667 -27.206  1.00 35.56      A    C  
ATOM    988  C   TYR A 702     -18.953 -15.458 -26.700  1.00 39.06      A    C  
ATOM    989  O   TYR A 702     -18.691 -16.581 -27.136  1.00 38.30      A    O  
ATOM    990  CB  TYR A 702     -19.683 -13.524 -28.109  1.00 30.10      A    C  
ATOM    991  CG  TYR A 702     -18.935 -13.965 -29.345  1.00 33.06      A    C  
ATOM    992  CD1 TYR A 702     -19.610 -14.239 -30.538  1.00 33.71      A    C  
ATOM    993  CD2 TYR A 702     -17.547 -14.082 -29.331  1.00 33.38      A    C  
ATOM    994  CE1 TYR A 702     -18.915 -14.612 -31.693  1.00 39.15      A    C  
ATOM    995  CE2 TYR A 702     -16.841 -14.455 -30.470  1.00 44.97      A    C  
ATOM    996  CZ  TYR A 702     -17.530 -14.715 -31.650  1.00 39.00      A    C  
ATOM    997  OH  TYR A 702     -16.822 -15.041 -32.782  1.00 46.57      A    O  
ATOM    998  N   LEU A 703     -18.217 -14.852 -25.779  1.00 36.63      A    N  
ATOM    999  CA  LEU A 703     -17.049 -15.495 -25.212  1.00 37.77      A    C  
ATOM   1000  C   LEU A 703     -17.426 -16.770 -24.463  1.00 31.26      A    C  
ATOM   1001  O   LEU A 703     -16.824 -17.812 -24.675  1.00 33.65      A    O  
ATOM   1002  CB  LEU A 703     -16.326 -14.535 -24.265  1.00 43.10      A    C  
ATOM   1003  CG  LEU A 703     -15.622 -13.313 -24.865  1.00 33.24      A    C  
ATOM   1004  CD1 LEU A 703     -15.228 -12.378 -23.733  1.00 45.83      A    C  
ATOM   1005  CD2 LEU A 703     -14.391 -13.741 -25.651  1.00 30.54      A    C  
ATOM   1006  N   ARG A 704     -18.440 -16.693 -23.608  1.00 29.67      A    N  
ATOM   1007  CA  ARG A 704     -18.849 -17.859 -22.836  1.00 32.79      A    C  
ATOM   1008  C   ARG A 704     -19.353 -18.975 -23.738  1.00 39.84      A    C  
ATOM   1009  O   ARG A 704     -19.071 -20.136 -23.476  1.00 36.90      A    O  
ATOM   1010  CB  ARG A 704     -19.910 -17.469 -21.801  1.00 32.73      A    C  
ATOM   1011  CG  ARG A 704     -19.567 -16.139 -21.149  1.00 38.72      A    C  
ATOM   1012  CD  ARG A 704     -19.564 -16.102 -19.665  1.00 41.92      A    C  
ATOM   1013  NE  ARG A 704     -20.800 -15.541 -19.172  1.00 36.17      A    N  
ATOM   1014  CZ  ARG A 704     -20.944 -14.892 -18.019  1.00 34.17      A    C  
ATOM   1015  NH1 ARG A 704     -19.920 -14.678 -17.199  1.00 36.29      A    N1+
ATOM   1016  NH2 ARG A 704     -22.157 -14.513 -17.649  1.00 32.14      A    N  
ATOM   1017  N   SER A 705     -20.081 -18.620 -24.798  1.00 41.33      A    N  
ATOM   1018  CA  SER A 705     -20.614 -19.603 -25.740  1.00 42.80      A    C  
ATOM   1019  C   SER A 705     -19.487 -20.303 -26.504  1.00 44.70      A    C  
ATOM   1020  O   SER A 705     -19.727 -21.305 -27.169  1.00 48.14      A    O  
ATOM   1021  CB  SER A 705     -21.557 -18.940 -26.760  1.00 36.27      A    C  
ATOM   1022  OG  SER A 705     -20.811 -18.278 -27.770  1.00 41.54      A    O  
ATOM   1023  N   LYS A 706     -18.264 -19.785 -26.415  1.00 40.87      A    N  
ATOM   1024  CA  LYS A 706     -17.151 -20.409 -27.118  1.00 40.83      A    C  
ATOM   1025  C   LYS A 706     -16.067 -21.037 -26.236  1.00 45.71      A    C  
ATOM   1026  O   LYS A 706     -14.962 -21.328 -26.706  1.00 38.26      A    O  
ATOM   1027  CB  LYS A 706     -16.529 -19.405 -28.092  1.00 43.37      A    C  
ATOM   1028  CG  LYS A 706     -17.530 -18.985 -29.154  1.00 56.87      A    C  
ATOM   1029  CD  LYS A 706     -16.881 -18.390 -30.375  1.00 58.24      A    C  
ATOM   1030  CE  LYS A 706     -17.934 -18.139 -31.441  1.00 53.74      A    C  
ATOM   1031  NZ  LYS A 706     -18.662 -19.389 -31.797  1.00 51.00      A    N1+
ATOM   1032  N   ARG A 707     -16.376 -21.265 -24.964  1.00 47.05      A    N  
ATOM   1033  CA  ARG A 707     -15.392 -21.869 -24.063  1.00 50.72      A    C  
ATOM   1034  C   ARG A 707     -15.018 -23.281 -24.503  1.00 48.72      A    C  
ATOM   1035  O   ARG A 707     -13.892 -23.720 -24.314  1.00 52.49      A    O  
ATOM   1036  CB  ARG A 707     -15.931 -21.926 -22.631  1.00 45.57      A    C  
ATOM   1037  CG  ARG A 707     -15.867 -20.615 -21.910  1.00 36.56      A    C  
ATOM   1038  CD  ARG A 707     -16.593 -20.669 -20.585  1.00 34.09      A    C  
ATOM   1039  NE  ARG A 707     -16.517 -19.353 -19.969  1.00 32.26      A    N  
ATOM   1040  CZ  ARG A 707     -16.853 -19.077 -18.715  1.00 38.18      A    C  
ATOM   1041  NH1 ARG A 707     -16.739 -17.832 -18.268  1.00 33.62      A    N1+
ATOM   1042  NH2 ARG A 707     -17.304 -20.034 -17.912  1.00 37.91      A    N  
ATOM   1043  N   GLU A 708     -15.973 -23.983 -25.096  1.00 52.77      A    N  
ATOM   1044  CA  GLU A 708     -15.748 -25.349 -25.544  1.00 59.77      A    C  
ATOM   1045  C   GLU A 708     -15.309 -25.396 -27.004  1.00 61.99      A    C  
ATOM   1046  O   GLU A 708     -15.197 -26.469 -27.592  1.00 66.97      A    O  
ATOM   1047  CB  GLU A 708     -17.037 -26.148 -25.352  1.00 58.81      A    C  
ATOM   1048  CG  GLU A 708     -16.822 -27.560 -24.910  1.00 73.75      A    C  
ATOM   1049  CD  GLU A 708     -18.067 -28.152 -24.315  1.00 78.91      A    C  
ATOM   1050  OE1 GLU A 708     -19.098 -28.192 -25.023  1.00 80.14      A    O  
ATOM   1051  OE2 GLU A 708     -18.014 -28.573 -23.138  1.00 84.17      A    O1-
ATOM   1052  N   LYS A 709     -15.053 -24.230 -27.586  1.00 63.27      A    N  
ATOM   1053  CA  LYS A 709     -14.648 -24.158 -28.984  1.00 65.26      A    C  
ATOM   1054  C   LYS A 709     -13.525 -23.167 -29.240  1.00 64.87      A    C  
ATOM   1055  O   LYS A 709     -13.598 -22.342 -30.153  1.00 69.70      A    O  
ATOM   1056  CB  LYS A 709     -15.865 -23.829 -29.859  1.00 66.61      A    C  
ATOM   1057  CG  LYS A 709     -16.889 -24.963 -29.894  1.00 78.03      A    C  
ATOM   1058  CD  LYS A 709     -16.229 -26.258 -30.385  1.00 86.98      A    C  
ATOM   1059  CE  LYS A 709     -16.903 -27.513 -29.832  1.00 89.08      A    C  
ATOM   1060  NZ  LYS A 709     -18.295 -27.696 -30.323  1.00 89.88      A    N1+
ATOM   1061  N   PHE A 710     -12.490 -23.259 -28.415  1.00 56.84      A    N  
ATOM   1062  CA  PHE A 710     -11.315 -22.412 -28.532  1.00 60.45      A    C  
ATOM   1063  C   PHE A 710     -10.172 -23.335 -28.933  1.00 63.73      A    C  
ATOM   1064  O   PHE A 710     -10.026 -24.427 -28.378  1.00 60.41      A    O  
ATOM   1065  CB  PHE A 710     -10.988 -21.748 -27.194  1.00 51.04      A    C  
ATOM   1066  CG  PHE A 710      -9.824 -20.799 -27.261  1.00 47.85      A    C  
ATOM   1067  CD1 PHE A 710     -10.014 -19.463 -27.612  1.00 40.02      A    C  
ATOM   1068  CD2 PHE A 710      -8.534 -21.242 -26.981  1.00 40.95      A    C  
ATOM   1069  CE1 PHE A 710      -8.933 -18.577 -27.682  1.00 49.94      A    C  
ATOM   1070  CE2 PHE A 710      -7.446 -20.368 -27.048  1.00 48.27      A    C  
ATOM   1071  CZ  PHE A 710      -7.641 -19.033 -27.398  1.00 43.83      A    C  
ATOM   1072  N   LEU A 783     -12.908 -19.882 -32.165  1.00 52.05      A    N  
ATOM   1073  CA  LEU A 783     -12.282 -18.690 -31.605  1.00 43.33      A    C  
ATOM   1074  C   LEU A 783     -10.818 -18.956 -31.267  1.00 43.29      A    C  
ATOM   1075  O   LEU A 783     -10.495 -19.966 -30.657  1.00 43.96      A    O  
ATOM   1076  CB  LEU A 783     -13.037 -18.264 -30.346  1.00 49.08      A    C  
ATOM   1077  CG  LEU A 783     -12.692 -16.895 -29.764  1.00 56.97      A    C  
ATOM   1078  CD1 LEU A 783     -13.092 -15.793 -30.746  1.00 59.28      A    C  
ATOM   1079  CD2 LEU A 783     -13.426 -16.720 -28.447  1.00 58.05      A    C  
ATOM   1080  N   THR A 784      -9.939 -18.034 -31.653  1.00 42.77      A    N  
ATOM   1081  CA  THR A 784      -8.502 -18.165 -31.396  1.00 39.31      A    C  
ATOM   1082  C   THR A 784      -7.960 -17.038 -30.519  1.00 41.01      A    C  
ATOM   1083  O   THR A 784      -8.650 -16.060 -30.245  1.00 44.85      A    O  
ATOM   1084  CB  THR A 784      -7.690 -18.088 -32.697  1.00 42.14      A    C  
ATOM   1085  CG2 THR A 784      -8.130 -19.184 -33.684  1.00 47.67      A    C  
ATOM   1086  OG1 THR A 784      -7.891 -16.794 -33.291  1.00 44.64      A    O  
ATOM   1087  N   PHE A 785      -6.696 -17.170 -30.137  1.00 36.93      A    N  
ATOM   1088  CA  PHE A 785      -6.011 -16.184 -29.318  1.00 43.65      A    C  
ATOM   1089  C   PHE A 785      -5.870 -14.881 -30.111  1.00 49.67      A    C  
ATOM   1090  O   PHE A 785      -5.935 -13.778 -29.557  1.00 45.33      A    O  
ATOM   1091  CB  PHE A 785      -4.627 -16.697 -28.938  1.00 27.20      A    C  
ATOM   1092  CG  PHE A 785      -3.751 -15.653 -28.305  1.00 38.98      A    C  
ATOM   1093  CD1 PHE A 785      -3.897 -15.323 -26.961  1.00 34.67      A    C  
ATOM   1094  CD2 PHE A 785      -2.819 -14.960 -29.067  1.00 36.66      A    C  
ATOM   1095  CE1 PHE A 785      -3.129 -14.318 -26.383  1.00 33.84      A    C  
ATOM   1096  CE2 PHE A 785      -2.045 -13.950 -28.504  1.00 38.30      A    C  
ATOM   1097  CZ  PHE A 785      -2.200 -13.625 -27.155  1.00 49.11      A    C  
ATOM   1098  N   GLU A 786      -5.651 -15.020 -31.411  1.00 42.89      A    N  
ATOM   1099  CA  GLU A 786      -5.515 -13.863 -32.286  1.00 41.29      A    C  
ATOM   1100  C   GLU A 786      -6.839 -13.086 -32.279  1.00 27.41      A    C  
ATOM   1101  O   GLU A 786      -6.843 -11.864 -32.272  1.00 35.10      A    O  
ATOM   1102  CB  GLU A 786      -5.155 -14.322 -33.706  1.00 48.92      A    C  
ATOM   1103  CG  GLU A 786      -3.731 -14.899 -33.852  1.00 62.18      A    C  
ATOM   1104  CD  GLU A 786      -3.428 -16.107 -32.941  1.00 62.99      A    C  
ATOM   1105  OE1 GLU A 786      -4.221 -17.076 -32.901  1.00 54.09      A    O  
ATOM   1106  OE2 GLU A 786      -2.370 -16.091 -32.274  1.00 66.85      A    O1-
ATOM   1107  N   ASP A 787      -7.961 -13.800 -32.292  1.00 29.15      A    N  
ATOM   1108  CA  ASP A 787      -9.269 -13.143 -32.226  1.00 33.03      A    C  
ATOM   1109  C   ASP A 787      -9.368 -12.364 -30.903  1.00 41.68      A    C  
ATOM   1110  O   ASP A 787      -9.848 -11.229 -30.868  1.00 40.18      A    O  
ATOM   1111  CB  ASP A 787     -10.393 -14.172 -32.246  1.00 31.43      A    C  
ATOM   1112  CG  ASP A 787     -10.478 -14.928 -33.558  1.00 49.43      A    C  
ATOM   1113  OD1 ASP A 787     -11.036 -16.045 -33.557  1.00 44.17      A    O  
ATOM   1114  OD2 ASP A 787     -10.002 -14.403 -34.583  1.00 41.96      A    O1-
ATOM   1115  N   LEU A 788      -8.922 -12.987 -29.815  1.00 35.08      A    N  
ATOM   1116  CA  LEU A 788      -8.969 -12.351 -28.499  1.00 41.52      A    C  
ATOM   1117  C   LEU A 788      -8.220 -11.018 -28.524  1.00 36.33      A    C  
ATOM   1118  O   LEU A 788      -8.750  -9.992 -28.104  1.00 32.18      A    O  
ATOM   1119  CB  LEU A 788      -8.359 -13.284 -27.449  1.00 30.36      A    C  
ATOM   1120  CG  LEU A 788      -9.258 -14.124 -26.540  1.00 47.11      A    C  
ATOM   1121  CD1 LEU A 788     -10.536 -14.547 -27.219  1.00 33.29      A    C  
ATOM   1122  CD2 LEU A 788      -8.451 -15.305 -26.056  1.00 37.55      A    C  
ATOM   1123  N   LEU A 789      -6.986 -11.048 -29.026  1.00 36.58      A    N  
ATOM   1124  CA  LEU A 789      -6.147  -9.857 -29.130  1.00 37.98      A    C  
ATOM   1125  C   LEU A 789      -6.837  -8.803 -30.012  1.00 40.45      A    C  
ATOM   1126  O   LEU A 789      -6.798  -7.599 -29.719  1.00 37.47      A    O  
ATOM   1127  CB  LEU A 789      -4.792 -10.241 -29.731  1.00 48.62      A    C  
ATOM   1128  CG  LEU A 789      -3.585  -9.369 -29.399  1.00 56.54      A    C  
ATOM   1129  CD1 LEU A 789      -3.825  -7.943 -29.857  1.00 65.84      A    C  
ATOM   1130  CD2 LEU A 789      -3.347  -9.397 -27.902  1.00 67.11      A    C  
ATOM   1131  N   CYS A 790      -7.494  -9.267 -31.076  1.00 39.90      A    N  
ATOM   1132  CA  CYS A 790      -8.203  -8.375 -31.993  1.00 44.05      A    C  
ATOM   1133  C   CYS A 790      -9.405  -7.694 -31.317  1.00 34.74      A    C  
ATOM   1134  O   CYS A 790      -9.672  -6.519 -31.561  1.00 30.49      A    O  
ATOM   1135  CB  CYS A 790      -8.688  -9.135 -33.229  1.00 39.06      A    C  
ATOM   1136  SG  CYS A 790      -9.271  -8.006 -34.528  1.00 53.93      A    S  
ATOM   1137  N   PHE A 791     -10.141  -8.441 -30.496  1.00 34.79      A    N  
ATOM   1138  CA  PHE A 791     -11.269  -7.859 -29.772  1.00 35.07      A    C  
ATOM   1139  C   PHE A 791     -10.722  -6.750 -28.872  1.00 32.40      A    C  
ATOM   1140  O   PHE A 791     -11.247  -5.625 -28.836  1.00 33.48      A    O  
ATOM   1141  CB  PHE A 791     -11.954  -8.923 -28.908  1.00 34.81      A    C  
ATOM   1142  CG  PHE A 791     -12.774  -9.918 -29.699  1.00 37.83      A    C  
ATOM   1143  CD1 PHE A 791     -12.981 -11.210 -29.218  1.00 37.26      A    C  
ATOM   1144  CD2 PHE A 791     -13.337  -9.563 -30.919  1.00 36.57      A    C  
ATOM   1145  CE1 PHE A 791     -13.737 -12.137 -29.944  1.00 35.45      A    C  
ATOM   1146  CE2 PHE A 791     -14.097 -10.481 -31.653  1.00 37.44      A    C  
ATOM   1147  CZ  PHE A 791     -14.295 -11.774 -31.159  1.00 42.31      A    C  
ATOM   1148  N   ALA A 792      -9.628  -7.068 -28.186  1.00 30.28      A    N  
ATOM   1149  CA  ALA A 792      -9.002  -6.145 -27.260  1.00 31.09      A    C  
ATOM   1150  C   ALA A 792      -8.556  -4.859 -27.944  1.00 32.64      A    C  
ATOM   1151  O   ALA A 792      -8.780  -3.760 -27.430  1.00 33.07      A    O  
ATOM   1152  CB  ALA A 792      -7.826  -6.824 -26.587  1.00 27.22      A    C  
ATOM   1153  N   TYR A 793      -7.900  -5.015 -29.090  1.00 38.88      A    N  
ATOM   1154  CA  TYR A 793      -7.394  -3.897 -29.880  1.00 27.39      A    C  
ATOM   1155  C   TYR A 793      -8.565  -3.029 -30.359  1.00 18.76      A    C  
ATOM   1156  O   TYR A 793      -8.507  -1.792 -30.305  1.00 28.67      A    O  
ATOM   1157  CB  TYR A 793      -6.619  -4.447 -31.088  1.00 37.33      A    C  
ATOM   1158  CG  TYR A 793      -6.153  -3.394 -32.064  1.00 42.49      A    C  
ATOM   1159  CD1 TYR A 793      -5.202  -2.442 -31.695  1.00 46.49      A    C  
ATOM   1160  CD2 TYR A 793      -6.658  -3.353 -33.362  1.00 48.58      A    C  
ATOM   1161  CE1 TYR A 793      -4.761  -1.474 -32.590  1.00 52.96      A    C  
ATOM   1162  CE2 TYR A 793      -6.220  -2.388 -34.273  1.00 55.09      A    C  
ATOM   1163  CZ  TYR A 793      -5.273  -1.454 -33.878  1.00 57.17      A    C  
ATOM   1164  OH  TYR A 793      -4.841  -0.498 -34.765  1.00 65.06      A    O  
ATOM   1165  N   GLN A 794      -9.620  -3.684 -30.835  1.00 23.10      A    N  
ATOM   1166  CA  GLN A 794     -10.795  -2.959 -31.312  1.00 30.66      A    C  
ATOM   1167  C   GLN A 794     -11.500  -2.126 -30.226  1.00 38.98      A    C  
ATOM   1168  O   GLN A 794     -11.961  -1.001 -30.485  1.00 32.26      A    O  
ATOM   1169  CB  GLN A 794     -11.792  -3.932 -31.930  1.00 29.05      A    C  
ATOM   1170  CG  GLN A 794     -11.385  -4.421 -33.328  1.00 30.82      A    C  
ATOM   1171  CD  GLN A 794     -12.406  -5.373 -33.883  1.00 19.50      A    C  
ATOM   1172  NE2 GLN A 794     -12.090  -6.662 -33.826  1.00 32.39      A    N  
ATOM   1173  OE1 GLN A 794     -13.494  -4.977 -34.309  1.00 36.24      A    O  
ATOM   1174  N   VAL A 795     -11.599  -2.675 -29.021  1.00 32.02      A    N  
ATOM   1175  CA  VAL A 795     -12.257  -1.944 -27.941  1.00 26.97      A    C  
ATOM   1176  C   VAL A 795     -11.389  -0.746 -27.581  1.00 18.95      A    C  
ATOM   1177  O   VAL A 795     -11.913   0.329 -27.319  1.00 34.05      A    O  
ATOM   1178  CB  VAL A 795     -12.515  -2.871 -26.707  1.00 28.07      A    C  
ATOM   1179  CG1 VAL A 795     -13.086  -2.079 -25.523  1.00 19.30      A    C  
ATOM   1180  CG2 VAL A 795     -13.518  -3.927 -27.097  1.00 20.08      A    C  
ATOM   1181  N   ALA A 796     -10.063  -0.918 -27.609  1.00 22.82      A    N  
ATOM   1182  CA  ALA A 796      -9.171   0.194 -27.288  1.00 27.91      A    C  
ATOM   1183  C   ALA A 796      -9.355   1.320 -28.319  1.00 35.38      A    C  
ATOM   1184  O   ALA A 796      -9.370   2.515 -27.975  1.00 30.84      A    O  
ATOM   1185  CB  ALA A 796      -7.715  -0.275 -27.254  1.00 25.95      A    C  
ATOM   1186  N   LYS A 797      -9.504   0.933 -29.579  1.00 34.10      A    N  
ATOM   1187  CA  LYS A 797      -9.708   1.894 -30.658  1.00 38.88      A    C  
ATOM   1188  C   LYS A 797     -11.051   2.621 -30.469  1.00 27.01      A    C  
ATOM   1189  O   LYS A 797     -11.141   3.849 -30.625  1.00 30.98      A    O  
ATOM   1190  CB  LYS A 797      -9.673   1.175 -32.013  1.00 45.55      A    C  
ATOM   1191  CG  LYS A 797      -9.738   2.102 -33.210  1.00 64.82      A    C  
ATOM   1192  CD  LYS A 797      -8.591   3.127 -33.220  1.00 77.92      A    C  
ATOM   1193  CE  LYS A 797      -7.227   2.504 -33.528  1.00 84.97      A    C  
ATOM   1194  NZ  LYS A 797      -6.137   3.538 -33.637  1.00 70.10      A    N1+
ATOM   1195  N   GLY A 798     -12.096   1.873 -30.140  1.00 31.17      A    N  
ATOM   1196  CA  GLY A 798     -13.379   2.513 -29.905  1.00 28.24      A    C  
ATOM   1197  C   GLY A 798     -13.268   3.506 -28.742  1.00 30.21      A    C  
ATOM   1198  O   GLY A 798     -13.785   4.627 -28.810  1.00 29.62      A    O  
ATOM   1199  N   MET A 799     -12.575   3.120 -27.677  1.00 26.76      A    N  
ATOM   1200  CA  MET A 799     -12.429   4.019 -26.520  1.00 28.15      A    C  
ATOM   1201  C   MET A 799     -11.559   5.237 -26.866  1.00 29.07      A    C  
ATOM   1202  O   MET A 799     -11.731   6.328 -26.316  1.00 31.45      A    O  
ATOM   1203  CB  MET A 799     -11.835   3.263 -25.324  1.00 28.69      A    C  
ATOM   1204  CG  MET A 799     -12.800   2.258 -24.685  1.00 20.11      A    C  
ATOM   1205  SD  MET A 799     -14.426   3.002 -24.257  1.00 29.35      A    S  
ATOM   1206  CE  MET A 799     -13.935   4.431 -23.239  1.00 28.29      A    C  
ATOM   1207  N   GLU A 800     -10.622   5.046 -27.784  1.00 32.52      A    N  
ATOM   1208  CA  GLU A 800      -9.753   6.134 -28.221  1.00 31.81      A    C  
ATOM   1209  C   GLU A 800     -10.635   7.158 -28.945  1.00 27.94      A    C  
ATOM   1210  O   GLU A 800     -10.482   8.372 -28.766  1.00 30.49      A    O  
ATOM   1211  CB  GLU A 800      -8.671   5.576 -29.150  1.00 37.15      A    C  
ATOM   1212  CG  GLU A 800      -7.720   6.608 -29.731  1.00 41.77      A    C  
ATOM   1213  CD  GLU A 800      -6.667   5.951 -30.608  1.00 53.23      A    C  
ATOM   1214  OE1 GLU A 800      -7.044   5.102 -31.451  1.00 50.33      A    O  
ATOM   1215  OE2 GLU A 800      -5.474   6.279 -30.458  1.00 43.76      A    O1-
ATOM   1216  N   PHE A 801     -11.582   6.662 -29.740  1.00 27.47      A    N  
ATOM   1217  CA  PHE A 801     -12.520   7.542 -30.445  1.00 30.57      A    C  
ATOM   1218  C   PHE A 801     -13.346   8.319 -29.416  1.00 35.75      A    C  
ATOM   1219  O   PHE A 801     -13.496   9.546 -29.516  1.00 33.51      A    O  
ATOM   1220  CB  PHE A 801     -13.441   6.713 -31.367  1.00 24.82      A    C  
ATOM   1221  CG  PHE A 801     -14.539   7.510 -32.021  1.00 33.77      A    C  
ATOM   1222  CD1 PHE A 801     -15.864   7.392 -31.578  1.00 30.78      A    C  
ATOM   1223  CD2 PHE A 801     -14.255   8.376 -33.081  1.00 34.58      A    C  
ATOM   1224  CE1 PHE A 801     -16.900   8.132 -32.185  1.00 34.99      A    C  
ATOM   1225  CE2 PHE A 801     -15.272   9.121 -33.702  1.00 26.84      A    C  
ATOM   1226  CZ  PHE A 801     -16.604   8.999 -33.251  1.00 30.92      A    C  
ATOM   1227  N   LEU A 802     -13.875   7.611 -28.415  1.00 33.96      A    N  
ATOM   1228  CA  LEU A 802     -14.670   8.272 -27.380  1.00 31.56      A    C  
ATOM   1229  C   LEU A 802     -13.866   9.342 -26.627  1.00 24.39      A    C  
ATOM   1230  O   LEU A 802     -14.375  10.432 -26.356  1.00 26.18      A    O  
ATOM   1231  CB  LEU A 802     -15.249   7.243 -26.401  1.00 31.61      A    C  
ATOM   1232  CG  LEU A 802     -16.252   6.275 -27.053  1.00 35.50      A    C  
ATOM   1233  CD1 LEU A 802     -16.864   5.347 -26.002  1.00 32.60      A    C  
ATOM   1234  CD2 LEU A 802     -17.346   7.076 -27.762  1.00 30.75      A    C  
ATOM   1235  N   GLU A 803     -12.614   9.043 -26.297  1.00 27.03      A    N  
ATOM   1236  CA  GLU A 803     -11.780  10.024 -25.622  1.00 36.31      A    C  
ATOM   1237  C   GLU A 803     -11.627  11.277 -26.493  1.00 42.60      A    C  
ATOM   1238  O   GLU A 803     -11.699  12.405 -26.000  1.00 35.21      A    O  
ATOM   1239  CB  GLU A 803     -10.387   9.462 -25.340  1.00 30.66      A    C  
ATOM   1240  CG  GLU A 803      -9.449  10.527 -24.772  1.00 34.54      A    C  
ATOM   1241  CD  GLU A 803      -8.100   9.967 -24.398  1.00 40.43      A    C  
ATOM   1242  OE1 GLU A 803      -7.681   8.985 -25.038  1.00 56.56      A    O  
ATOM   1243  OE2 GLU A 803      -7.453  10.517 -23.478  1.00 51.14      A    O1-
ATOM   1244  N   PHE A 804     -11.405  11.057 -27.789  1.00 42.72      A    N  
ATOM   1245  CA  PHE A 804     -11.241  12.144 -28.741  1.00 39.97      A    C  
ATOM   1246  C   PHE A 804     -12.504  13.003 -28.811  1.00 37.06      A    C  
ATOM   1247  O   PHE A 804     -12.420  14.224 -28.907  1.00 33.12      A    O  
ATOM   1248  CB  PHE A 804     -10.917  11.589 -30.131  1.00 51.70      A    C  
ATOM   1249  CG  PHE A 804     -10.878  12.639 -31.210  1.00 55.31      A    C  
ATOM   1250  CD1 PHE A 804      -9.975  13.697 -31.141  1.00 54.28      A    C  
ATOM   1251  CD2 PHE A 804     -11.741  12.565 -32.300  1.00 51.55      A    C  
ATOM   1252  CE1 PHE A 804      -9.931  14.664 -32.141  1.00 58.51      A    C  
ATOM   1253  CE2 PHE A 804     -11.706  13.529 -33.304  1.00 55.65      A    C  
ATOM   1254  CZ  PHE A 804     -10.799  14.579 -33.225  1.00 56.65      A    C  
ATOM   1255  N   LYS A 805     -13.668  12.364 -28.766  1.00 28.01      A    N  
ATOM   1256  CA  LYS A 805     -14.937  13.083 -28.807  1.00 26.94      A    C  
ATOM   1257  C   LYS A 805     -15.389  13.585 -27.430  1.00 30.74      A    C  
ATOM   1258  O   LYS A 805     -16.545  13.952 -27.252  1.00 25.86      A    O  
ATOM   1259  CB  LYS A 805     -16.024  12.197 -29.416  1.00 29.49      A    C  
ATOM   1260  CG  LYS A 805     -15.800  11.872 -30.898  1.00 39.73      A    C  
ATOM   1261  CD  LYS A 805     -15.624  13.156 -31.715  1.00 42.86      A    C  
ATOM   1262  CE  LYS A 805     -15.335  12.890 -33.186  1.00 51.33      A    C  
ATOM   1263  NZ  LYS A 805     -16.569  12.824 -34.018  1.00 52.01      A    N1+
ATOM   1264  N   SER A 806     -14.475  13.586 -26.463  1.00 30.61      A    N  
ATOM   1265  CA  SER A 806     -14.758  14.053 -25.103  1.00 34.95      A    C  
ATOM   1266  C   SER A 806     -15.919  13.343 -24.376  1.00 23.27      A    C  
ATOM   1267  O   SER A 806     -16.731  13.963 -23.685  1.00 30.69      A    O  
ATOM   1268  CB  SER A 806     -14.992  15.567 -25.120  1.00 38.77      A    C  
ATOM   1269  OG  SER A 806     -14.917  16.101 -23.808  1.00 40.79      A    O  
ATOM   1270  N   CYS A 807     -15.963  12.026 -24.518  1.00 27.77      A    N  
ATOM   1271  CA  CYS A 807     -16.981  11.204 -23.879  1.00 33.33      A    C  
ATOM   1272  C   CYS A 807     -16.357  10.201 -22.946  1.00 28.37      A    C  
ATOM   1273  O   CYS A 807     -15.177   9.916 -23.038  1.00 31.30      A    O  
ATOM   1274  CB  CYS A 807     -17.779  10.414 -24.919  1.00 30.06      A    C  
ATOM   1275  SG  CYS A 807     -18.704  11.456 -26.016  1.00 37.88      A    S  
ATOM   1276  N   VAL A 808     -17.158   9.688 -22.020  1.00 27.15      A    N  
ATOM   1277  CA  VAL A 808     -16.682   8.644 -21.121  1.00 26.37      A    C  
ATOM   1278  C   VAL A 808     -17.789   7.605 -21.101  1.00 24.42      A    C  
ATOM   1279  O   VAL A 808     -18.941   7.913 -21.441  1.00 33.70      A    O  
ATOM   1280  CB  VAL A 808     -16.478   9.131 -19.668  1.00 30.70      A    C  
ATOM   1281  CG1 VAL A 808     -15.327  10.131 -19.600  1.00 24.77      A    C  
ATOM   1282  CG2 VAL A 808     -17.785   9.717 -19.135  1.00 30.86      A    C  
ATOM   1283  N   HIS A 809     -17.437   6.378 -20.728  1.00 25.97      A    N  
ATOM   1284  CA  HIS A 809     -18.425   5.313 -20.584  1.00 24.72      A    C  
ATOM   1285  C   HIS A 809     -18.413   4.956 -19.087  1.00 24.61      A    C  
ATOM   1286  O   HIS A 809     -17.386   4.508 -18.549  1.00 22.91      A    O  
ATOM   1287  CB  HIS A 809     -18.045   4.071 -21.410  1.00 23.67      A    C  
ATOM   1288  CG  HIS A 809     -19.205   3.164 -21.685  1.00 26.04      A    C  
ATOM   1289  CD2 HIS A 809     -19.579   2.508 -22.811  1.00 24.93      A    C  
ATOM   1290  ND1 HIS A 809     -20.183   2.907 -20.749  1.00 20.09      A    N  
ATOM   1291  CE1 HIS A 809     -21.115   2.139 -21.287  1.00 31.71      A    C  
ATOM   1292  NE2 HIS A 809     -20.773   1.885 -22.538  1.00 28.91      A    N  
ATOM   1293  N   ARG A 810     -19.539   5.151 -18.419  1.00 24.30      A    N  
ATOM   1294  CA  ARG A 810     -19.612   4.865 -16.988  1.00 34.49      A    C  
ATOM   1295  C   ARG A 810     -19.927   3.396 -16.688  1.00 35.04      A    C  
ATOM   1296  O   ARG A 810     -20.042   3.004 -15.533  1.00 32.88      A    O  
ATOM   1297  CB  ARG A 810     -20.656   5.773 -16.326  1.00 27.22      A    C  
ATOM   1298  CG  ARG A 810     -20.354   7.275 -16.461  1.00 35.93      A    C  
ATOM   1299  CD  ARG A 810     -21.297   8.128 -15.601  1.00 37.88      A    C  
ATOM   1300  NE  ARG A 810     -22.704   7.949 -15.954  1.00 55.84      A    N  
ATOM   1301  CZ  ARG A 810     -23.664   8.833 -15.678  1.00 70.03      A    C  
ATOM   1302  NH1 ARG A 810     -24.925   8.589 -16.031  1.00 61.05      A    N1+
ATOM   1303  NH2 ARG A 810     -23.360   9.969 -15.058  1.00 64.49      A    N  
ATOM   1304  N   ASP A 811     -20.062   2.588 -17.735  1.00 27.66      A    N  
ATOM   1305  CA  ASP A 811     -20.347   1.169 -17.560  1.00 18.35      A    C  
ATOM   1306  C   ASP A 811     -19.646   0.352 -18.638  1.00 20.66      A    C  
ATOM   1307  O   ASP A 811     -20.259  -0.464 -19.327  1.00 24.82      A    O  
ATOM   1308  CB  ASP A 811     -21.873   0.932 -17.591  1.00 19.79      A    C  
ATOM   1309  CG  ASP A 811     -22.284  -0.465 -17.075  1.00 18.80      A    C  
ATOM   1310  OD1 ASP A 811     -23.483  -0.798 -17.223  1.00 20.03      A    O  
ATOM   1311  OD2 ASP A 811     -21.430  -1.210 -16.523  1.00 22.07      A    O1-
ATOM   1312  N   LEU A 812     -18.353   0.594 -18.802  1.00 21.58      A    N  
ATOM   1313  CA  LEU A 812     -17.580  -0.133 -19.792  1.00 19.92      A    C  
ATOM   1314  C   LEU A 812     -17.383  -1.559 -19.256  1.00 32.84      A    C  
ATOM   1315  O   LEU A 812     -16.890  -1.727 -18.145  1.00 25.79      A    O  
ATOM   1316  CB  LEU A 812     -16.210   0.525 -19.991  1.00 18.02      A    C  
ATOM   1317  CG  LEU A 812     -15.329  -0.253 -20.983  1.00 23.99      A    C  
ATOM   1318  CD1 LEU A 812     -16.015  -0.367 -22.340  1.00 28.58      A    C  
ATOM   1319  CD2 LEU A 812     -13.978   0.445 -21.120  1.00 19.30      A    C  
ATOM   1320  N   ALA A 813     -17.789  -2.564 -20.034  1.00 19.86      A    N  
ATOM   1321  CA  ALA A 813     -17.662  -3.995 -19.658  1.00 21.67      A    C  
ATOM   1322  C   ALA A 813     -17.991  -4.832 -20.900  1.00 26.37      A    C  
ATOM   1323  O   ALA A 813     -18.594  -4.333 -21.856  1.00 24.90      A    O  
ATOM   1324  CB  ALA A 813     -18.652  -4.373 -18.482  1.00 15.56      A    C  
ATOM   1325  N   ALA A 814     -17.602  -6.103 -20.878  1.00 23.92      A    N  
ATOM   1326  CA  ALA A 814     -17.837  -6.978 -22.023  1.00 28.31      A    C  
ATOM   1327  C   ALA A 814     -19.315  -7.104 -22.375  1.00 32.87      A    C  
ATOM   1328  O   ALA A 814     -19.656  -7.342 -23.530  1.00 26.89      A    O  
ATOM   1329  CB  ALA A 814     -17.209  -8.364 -21.771  1.00 28.28      A    C  
ATOM   1330  N   ARG A 815     -20.198  -6.928 -21.394  1.00 21.80      A    N  
ATOM   1331  CA  ARG A 815     -21.639  -7.019 -21.672  1.00 23.55      A    C  
ATOM   1332  C   ARG A 815     -22.131  -5.812 -22.509  1.00 26.22      A    C  
ATOM   1333  O   ARG A 815     -23.214  -5.870 -23.092  1.00 28.95      A    O  
ATOM   1334  CB  ARG A 815     -22.445  -7.133 -20.359  1.00 25.75      A    C  
ATOM   1335  CG  ARG A 815     -22.133  -6.022 -19.341  1.00 23.23      A    C  
ATOM   1336  CD  ARG A 815     -22.912  -6.153 -17.993  1.00 25.96      A    C  
ATOM   1337  NE  ARG A 815     -22.537  -5.024 -17.152  1.00 21.77      A    N  
ATOM   1338  CZ  ARG A 815     -21.484  -5.003 -16.343  1.00 28.37      A    C  
ATOM   1339  NH1 ARG A 815     -21.205  -3.897 -15.651  1.00 26.55      A    N1+
ATOM   1340  NH2 ARG A 815     -20.753  -6.102 -16.169  1.00 22.70      A    N  
ATOM   1341  N   ASN A 816     -21.336  -4.736 -22.568  1.00 28.33      A    N  
ATOM   1342  CA  ASN A 816     -21.700  -3.536 -23.347  1.00 28.70      A    C  
ATOM   1343  C   ASN A 816     -20.850  -3.384 -24.617  1.00 30.37      A    C  
ATOM   1344  O   ASN A 816     -20.641  -2.273 -25.121  1.00 29.65      A    O  
ATOM   1345  CB  ASN A 816     -21.563  -2.261 -22.508  1.00 18.69      A    C  
ATOM   1346  CG  ASN A 816     -22.758  -2.007 -21.624  1.00 31.48      A    C  
ATOM   1347  ND2 ASN A 816     -23.924  -2.404 -22.090  1.00 21.36      A    N  
ATOM   1348  OD1 ASN A 816     -22.636  -1.446 -20.530  1.00 42.70      A    O  
ATOM   1349  N   VAL A 817     -20.327  -4.504 -25.107  1.00 29.94      A    N  
ATOM   1350  CA  VAL A 817     -19.557  -4.526 -26.340  1.00 32.30      A    C  
ATOM   1351  C   VAL A 817     -20.299  -5.564 -27.184  1.00 37.46      A    C  
ATOM   1352  O   VAL A 817     -20.577  -6.658 -26.693  1.00 35.01      A    O  
ATOM   1353  CB  VAL A 817     -18.089  -4.981 -26.105  1.00 25.91      A    C  
ATOM   1354  CG1 VAL A 817     -17.365  -5.133 -27.459  1.00 27.91      A    C  
ATOM   1355  CG2 VAL A 817     -17.347  -3.960 -25.240  1.00 24.82      A    C  
ATOM   1356  N   LEU A 818     -20.661  -5.221 -28.419  1.00 34.17      A    N  
ATOM   1357  CA  LEU A 818     -21.393  -6.170 -29.282  1.00 31.26      A    C  
ATOM   1358  C   LEU A 818     -20.556  -6.681 -30.466  1.00 27.84      A    C  
ATOM   1359  O   LEU A 818     -19.662  -5.992 -30.957  1.00 36.46      A    O  
ATOM   1360  CB  LEU A 818     -22.710  -5.556 -29.789  1.00 24.72      A    C  
ATOM   1361  CG  LEU A 818     -23.715  -4.992 -28.765  1.00 30.63      A    C  
ATOM   1362  CD1 LEU A 818     -25.051  -4.717 -29.465  1.00 29.48      A    C  
ATOM   1363  CD2 LEU A 818     -23.934  -5.962 -27.611  1.00 30.42      A    C  
ATOM   1364  N   VAL A 819     -20.858  -7.902 -30.911  1.00 35.55      A    N  
ATOM   1365  CA  VAL A 819     -20.118  -8.550 -31.991  1.00 37.56      A    C  
ATOM   1366  C   VAL A 819     -20.908  -8.649 -33.300  1.00 30.84      A    C  
ATOM   1367  O   VAL A 819     -22.063  -9.029 -33.282  1.00 24.97      A    O  
ATOM   1368  CB  VAL A 819     -19.705  -9.982 -31.559  1.00 38.32      A    C  
ATOM   1369  CG1 VAL A 819     -18.749 -10.579 -32.569  1.00 40.01      A    C  
ATOM   1370  CG2 VAL A 819     -19.073  -9.944 -30.155  1.00 35.86      A    C  
ATOM   1371  N   THR A 820     -20.287  -8.271 -34.411  1.00 37.74      A    N  
ATOM   1372  CA  THR A 820     -20.927  -8.358 -35.731  1.00 46.56      A    C  
ATOM   1373  C   THR A 820     -20.128  -9.267 -36.656  1.00 47.62      A    C  
ATOM   1374  O   THR A 820     -19.139  -9.865 -36.235  1.00 36.00      A    O  
ATOM   1375  CB  THR A 820     -21.099  -6.980 -36.447  1.00 51.43      A    C  
ATOM   1376  CG2 THR A 820     -22.307  -6.277 -35.938  1.00 59.89      A    C  
ATOM   1377  OG1 THR A 820     -19.939  -6.161 -36.246  1.00 48.12      A    O  
ATOM   1378  N   HIS A 821     -20.530  -9.319 -37.927  1.00 48.67      A    N  
ATOM   1379  CA  HIS A 821     -19.936 -10.216 -38.919  1.00 43.14      A    C  
ATOM   1380  C   HIS A 821     -18.464 -10.621 -38.993  1.00 46.64      A    C  
ATOM   1381  O   HIS A 821     -18.151 -11.796 -38.795  1.00 64.64      A    O  
ATOM   1382  CB  HIS A 821     -20.427  -9.814 -40.317  1.00 41.16      A    C  
ATOM   1383  CG  HIS A 821     -21.881 -10.091 -40.513  1.00 35.55      A    C  
ATOM   1384  CD2 HIS A 821     -22.560 -11.263 -40.564  1.00 38.67      A    C  
ATOM   1385  ND1 HIS A 821     -22.836  -9.096 -40.498  1.00 43.45      A    N  
ATOM   1386  CE1 HIS A 821     -24.041  -9.643 -40.525  1.00 45.66      A    C  
ATOM   1387  NE2 HIS A 821     -23.902 -10.957 -40.562  1.00 41.92      A    N  
ATOM   1388  N   GLY A 822     -17.545  -9.714 -39.273  1.00 44.59      A    N  
ATOM   1389  CA  GLY A 822     -16.171 -10.183 -39.392  1.00 35.60      A    C  
ATOM   1390  C   GLY A 822     -15.379 -10.212 -38.101  1.00 43.41      A    C  
ATOM   1391  O   GLY A 822     -14.198  -9.843 -38.094  1.00 41.03      A    O  
ATOM   1392  N   LYS A 823     -16.000 -10.662 -37.012  1.00 43.87      A    N  
ATOM   1393  CA  LYS A 823     -15.301 -10.681 -35.728  1.00 53.19      A    C  
ATOM   1394  C   LYS A 823     -15.083  -9.219 -35.293  1.00 46.64      A    C  
ATOM   1395  O   LYS A 823     -14.165  -8.924 -34.532  1.00 44.14      A    O  
ATOM   1396  CB  LYS A 823     -13.931 -11.364 -35.878  1.00 56.09      A    C  
ATOM   1397  CG  LYS A 823     -13.698 -12.594 -35.017  1.00 59.24      A    C  
ATOM   1398  CD  LYS A 823     -14.581 -13.750 -35.424  1.00 53.82      A    C  
ATOM   1399  CE  LYS A 823     -14.090 -15.038 -34.788  1.00 61.09      A    C  
ATOM   1400  NZ  LYS A 823     -14.865 -16.227 -35.244  1.00 63.41      A    N1+
ATOM   1401  N   VAL A 824     -15.903  -8.305 -35.808  1.00 42.54      A    N  
ATOM   1402  CA  VAL A 824     -15.777  -6.890 -35.449  1.00 41.12      A    C  
ATOM   1403  C   VAL A 824     -16.659  -6.595 -34.232  1.00 32.29      A    C  
ATOM   1404  O   VAL A 824     -17.819  -7.024 -34.172  1.00 33.32      A    O  
ATOM   1405  CB  VAL A 824     -16.210  -5.959 -36.620  1.00 40.96      A    C  
ATOM   1406  CG1 VAL A 824     -16.200  -4.494 -36.161  1.00 40.81      A    C  
ATOM   1407  CG2 VAL A 824     -15.263  -6.133 -37.804  1.00 40.57      A    C  
ATOM   1408  N   VAL A 825     -16.107  -5.886 -33.255  1.00 32.40      A    N  
ATOM   1409  CA  VAL A 825     -16.891  -5.552 -32.067  1.00 32.94      A    C  
ATOM   1410  C   VAL A 825     -17.109  -4.044 -31.986  1.00 34.64      A    C  
ATOM   1411  O   VAL A 825     -16.294  -3.253 -32.473  1.00 30.10      A    O  
ATOM   1412  CB  VAL A 825     -16.205  -6.046 -30.789  1.00 27.07      A    C  
ATOM   1413  CG1 VAL A 825     -16.123  -7.584 -30.818  1.00 30.78      A    C  
ATOM   1414  CG2 VAL A 825     -14.839  -5.446 -30.673  1.00 22.25      A    C  
ATOM   1415  N   LYS A 826     -18.217  -3.668 -31.360  1.00 29.65      A    N  
ATOM   1416  CA  LYS A 826     -18.626  -2.274 -31.232  1.00 30.34      A    C  
ATOM   1417  C   LYS A 826     -19.090  -1.963 -29.810  1.00 33.42      A    C  
ATOM   1418  O   LYS A 826     -19.912  -2.686 -29.244  1.00 25.81      A    O  
ATOM   1419  CB  LYS A 826     -19.792  -1.995 -32.194  1.00 26.65      A    C  
ATOM   1420  CG  LYS A 826     -19.420  -2.068 -33.705  1.00 31.34      A    C  
ATOM   1421  CD  LYS A 826     -20.687  -2.074 -34.579  1.00 36.38      A    C  
ATOM   1422  CE  LYS A 826     -20.361  -1.753 -36.054  1.00 35.82      A    C  
ATOM   1423  NZ  LYS A 826     -19.727  -0.394 -36.200  1.00 33.46      A    N1+
ATOM   1424  N   ILE A 827     -18.580  -0.866 -29.264  1.00 35.53      A    N  
ATOM   1425  CA  ILE A 827     -18.942  -0.433 -27.930  1.00 29.54      A    C  
ATOM   1426  C   ILE A 827     -20.300   0.266 -27.962  1.00 31.63      A    C  
ATOM   1427  O   ILE A 827     -20.599   1.014 -28.888  1.00 26.88      A    O  
ATOM   1428  CB  ILE A 827     -17.903   0.558 -27.396  1.00 25.09      A    C  
ATOM   1429  CG1 ILE A 827     -16.501  -0.057 -27.485  1.00 27.56      A    C  
ATOM   1430  CG2 ILE A 827     -18.261   0.990 -25.980  1.00 30.54      A    C  
ATOM   1431  CD1 ILE A 827     -15.382   0.905 -27.026  1.00 25.13      A    C  
ATOM   1432  N   CYS A 828     -21.129   0.014 -26.958  1.00 25.22      A    N  
ATOM   1433  CA  CYS A 828     -22.428   0.687 -26.845  1.00 30.92      A    C  
ATOM   1434  C   CYS A 828     -22.865   0.682 -25.386  1.00 31.79      A    C  
ATOM   1435  O   CYS A 828     -22.084   0.355 -24.496  1.00 30.29      A    O  
ATOM   1436  CB  CYS A 828     -23.503  -0.037 -27.645  1.00 31.66      A    C  
ATOM   1437  SG  CYS A 828     -23.966  -1.637 -26.898  1.00 37.05      A    S  
ATOM   1438  N   ASP A 829     -24.114   1.075 -25.166  1.00 33.60      A    N  
ATOM   1439  CA  ASP A 829     -24.728   1.002 -23.855  1.00 33.35      A    C  
ATOM   1440  C   ASP A 829     -25.981   0.205 -24.167  1.00 31.88      A    C  
ATOM   1441  O   ASP A 829     -26.910   0.707 -24.807  1.00 31.56      A    O  
ATOM   1442  CB  ASP A 829     -25.133   2.362 -23.279  1.00 39.34      A    C  
ATOM   1443  CG  ASP A 829     -25.715   2.231 -21.858  1.00 39.48      A    C  
ATOM   1444  OD1 ASP A 829     -25.060   2.676 -20.895  1.00 51.36      A    O  
ATOM   1445  OD2 ASP A 829     -26.817   1.666 -21.699  1.00 35.76      A    O1-
ATOM   1446  N   PHE A 830     -25.988  -1.048 -23.733  1.00 29.98      A    N  
ATOM   1447  CA  PHE A 830     -27.104  -1.951 -23.963  1.00 32.66      A    C  
ATOM   1448  C   PHE A 830     -27.920  -2.124 -22.695  1.00 40.09      A    C  
ATOM   1449  O   PHE A 830     -28.634  -3.127 -22.535  1.00 36.05      A    O  
ATOM   1450  CB  PHE A 830     -26.576  -3.315 -24.414  1.00 40.58      A    C  
ATOM   1451  CG  PHE A 830     -27.305  -3.887 -25.590  1.00 46.50      A    C  
ATOM   1452  CD1 PHE A 830     -27.538  -3.108 -26.723  1.00 43.87      A    C  
ATOM   1453  CD2 PHE A 830     -27.714  -5.221 -25.592  1.00 53.85      A    C  
ATOM   1454  CE1 PHE A 830     -28.166  -3.649 -27.844  1.00 51.79      A    C  
ATOM   1455  CE2 PHE A 830     -28.342  -5.775 -26.709  1.00 48.58      A    C  
ATOM   1456  CZ  PHE A 830     -28.569  -4.987 -27.838  1.00 58.55      A    C  
ATOM   1457  N   GLY A 831     -27.784  -1.158 -21.791  1.00 31.84      A    N  
ATOM   1458  CA  GLY A 831     -28.525  -1.206 -20.551  1.00 34.31      A    C  
ATOM   1459  C   GLY A 831     -30.027  -1.346 -20.742  1.00 43.10      A    C  
ATOM   1460  O   GLY A 831     -30.694  -2.031 -19.966  1.00 39.28      A    O  
ATOM   1461  N   LEU A 832     -30.583  -0.714 -21.769  1.00 37.26      A    N  
ATOM   1462  CA  LEU A 832     -32.030  -0.799 -21.979  1.00 39.72      A    C  
ATOM   1463  C   LEU A 832     -32.460  -2.234 -22.296  1.00 32.53      A    C  
ATOM   1464  O   LEU A 832     -33.604  -2.621 -22.043  1.00 37.50      A    O  
ATOM   1465  CB  LEU A 832     -32.463   0.132 -23.126  1.00 30.69      A    C  
ATOM   1466  CG  LEU A 832     -33.956   0.424 -23.289  1.00 41.59      A    C  
ATOM   1467  CD1 LEU A 832     -34.440   1.240 -22.081  1.00 34.03      A    C  
ATOM   1468  CD2 LEU A 832     -34.200   1.215 -24.599  1.00 42.74      A    C  
ATOM   1469  N   ALA A 833     -31.541  -3.016 -22.854  1.00 32.42      A    N  
ATOM   1470  CA  ALA A 833     -31.841  -4.391 -23.225  1.00 41.83      A    C  
ATOM   1471  C   ALA A 833     -31.591  -5.405 -22.108  1.00 47.86      A    C  
ATOM   1472  O   ALA A 833     -31.397  -6.594 -22.383  1.00 43.18      A    O  
ATOM   1473  CB  ALA A 833     -31.038  -4.794 -24.475  1.00 38.69      A    C  
ATOM   1474  N   ARG A 834     -31.560  -4.951 -20.859  1.00 44.80      A    N  
ATOM   1475  CA  ARG A 834     -31.384  -5.901 -19.778  1.00 45.98      A    C  
ATOM   1476  C   ARG A 834     -31.970  -5.440 -18.462  1.00 43.20      A    C  
ATOM   1477  O   ARG A 834     -32.055  -4.246 -18.172  1.00 44.04      A    O  
ATOM   1478  CB  ARG A 834     -29.912  -6.281 -19.609  1.00 49.29      A    C  
ATOM   1479  CG  ARG A 834     -29.014  -5.160 -19.218  1.00 44.92      A    C  
ATOM   1480  CD  ARG A 834     -27.562  -5.610 -19.071  1.00 52.74      A    C  
ATOM   1481  NE  ARG A 834     -26.773  -4.409 -18.865  1.00 58.68      A    N  
ATOM   1482  CZ  ARG A 834     -25.863  -3.939 -19.708  1.00 52.97      A    C  
ATOM   1483  NH1 ARG A 834     -25.566  -4.576 -20.841  1.00 34.52      A    N1+
ATOM   1484  NH2 ARG A 834     -25.314  -2.768 -19.443  1.00 42.43      A    N  
ATOM   1485  N   ASP A 835     -32.408  -6.412 -17.672  1.00 49.52      A    N  
ATOM   1486  CA  ASP A 835     -32.992  -6.137 -16.374  1.00 46.71      A    C  
ATOM   1487  C   ASP A 835     -31.870  -6.067 -15.355  1.00 44.39      A    C  
ATOM   1488  O   ASP A 835     -31.316  -7.093 -14.954  1.00 41.90      A    O  
ATOM   1489  CB  ASP A 835     -33.974  -7.244 -16.007  1.00 58.15      A    C  
ATOM   1490  CG  ASP A 835     -34.738  -6.935 -14.744  1.00 55.74      A    C  
ATOM   1491  OD1 ASP A 835     -34.275  -7.321 -13.652  1.00 62.21      A    O  
ATOM   1492  OD2 ASP A 835     -35.797  -6.286 -14.846  1.00 63.53      A    O1-
ATOM   1493  N   ILE A 836     -31.518  -4.855 -14.950  1.00 43.94      A    N  
ATOM   1494  CA  ILE A 836     -30.440  -4.680 -13.992  1.00 58.16      A    C  
ATOM   1495  C   ILE A 836     -30.726  -5.405 -12.678  1.00 57.31      A    C  
ATOM   1496  O   ILE A 836     -29.805  -5.885 -12.028  1.00 60.41      A    O  
ATOM   1497  CB  ILE A 836     -30.155  -3.168 -13.737  1.00 63.54      A    C  
ATOM   1498  CG1 ILE A 836     -31.404  -2.468 -13.192  1.00 74.94      A    C  
ATOM   1499  CG2 ILE A 836     -29.712  -2.494 -15.049  1.00 55.72      A    C  
ATOM   1500  CD1 ILE A 836     -31.665  -2.689 -11.703  1.00 83.58      A    C  
ATOM   1501  N   MET A 837     -32.003  -5.504 -12.309  1.00 57.23      A    N  
ATOM   1502  CA  MET A 837     -32.404  -6.175 -11.073  1.00 57.86      A    C  
ATOM   1503  C   MET A 837     -32.029  -7.659 -11.101  1.00 58.57      A    C  
ATOM   1504  O   MET A 837     -31.675  -8.240 -10.082  1.00 54.97      A    O  
ATOM   1505  CB  MET A 837     -33.915  -6.038 -10.860  1.00 66.40      A    C  
ATOM   1506  CG  MET A 837     -34.359  -6.146  -9.406  1.00 74.26      A    C  
ATOM   1507  SD  MET A 837     -34.197  -4.577  -8.511  1.00 91.89      A    S  
ATOM   1508  CE  MET A 837     -32.368  -4.339  -8.491  1.00 74.42      A    C  
ATOM   1509  N   SER A 838     -32.115  -8.278 -12.272  1.00 54.44      A    N  
ATOM   1510  CA  SER A 838     -31.763  -9.680 -12.387  1.00 52.49      A    C  
ATOM   1511  C   SER A 838     -30.271  -9.863 -12.698  1.00 54.08      A    C  
ATOM   1512  O   SER A 838     -29.822 -10.983 -12.946  1.00 49.78      A    O  
ATOM   1513  CB  SER A 838     -32.595 -10.352 -13.479  1.00 59.76      A    C  
ATOM   1514  OG  SER A 838     -32.125  -9.989 -14.763  1.00 77.03      A    O  
ATOM   1515  N   ASP A 839     -29.495  -8.778 -12.685  1.00 43.27      A    N  
ATOM   1516  CA  ASP A 839     -28.062  -8.901 -12.980  1.00 39.84      A    C  
ATOM   1517  C   ASP A 839     -27.253  -8.586 -11.718  1.00 29.96      A    C  
ATOM   1518  O   ASP A 839     -27.170  -7.441 -11.292  1.00 38.75      A    O  
ATOM   1519  CB  ASP A 839     -27.694  -7.963 -14.143  1.00 36.49      A    C  
ATOM   1520  CG  ASP A 839     -26.288  -8.185 -14.657  1.00 39.83      A    C  
ATOM   1521  OD1 ASP A 839     -26.048  -7.935 -15.862  1.00 53.20      A    O  
ATOM   1522  OD2 ASP A 839     -25.422  -8.597 -13.862  1.00 44.41      A    O1-
ATOM   1523  N   SER A 840     -26.670  -9.617 -11.112  1.00 39.27      A    N  
ATOM   1524  CA  SER A 840     -25.896  -9.448  -9.881  1.00 41.65      A    C  
ATOM   1525  C   SER A 840     -24.574  -8.677 -10.015  1.00 43.21      A    C  
ATOM   1526  O   SER A 840     -23.870  -8.472  -9.027  1.00 43.42      A    O  
ATOM   1527  CB  SER A 840     -25.630 -10.816  -9.231  1.00 48.42      A    C  
ATOM   1528  OG  SER A 840     -24.958 -11.710 -10.112  1.00 50.43      A    O  
ATOM   1529  N   ASN A 841     -24.238  -8.240 -11.222  1.00 39.54      A    N  
ATOM   1530  CA  ASN A 841     -23.003  -7.475 -11.408  1.00 35.88      A    C  
ATOM   1531  C   ASN A 841     -23.246  -6.005 -11.030  1.00 34.74      A    C  
ATOM   1532  O   ASN A 841     -22.313  -5.184 -10.936  1.00 31.46      A    O  
ATOM   1533  CB  ASN A 841     -22.515  -7.627 -12.852  1.00 38.71      A    C  
ATOM   1534  CG  ASN A 841     -22.057  -9.053 -13.157  1.00 37.16      A    C  
ATOM   1535  ND2 ASN A 841     -22.686  -9.691 -14.131  1.00 33.23      A    N  
ATOM   1536  OD1 ASN A 841     -21.146  -9.570 -12.507  1.00 52.04      A    O  
ATOM   1537  N   TYR A 842     -24.512  -5.677 -10.803  1.00 26.60      A    N  
ATOM   1538  CA  TYR A 842     -24.859  -4.332 -10.398  1.00 33.38      A    C  
ATOM   1539  C   TYR A 842     -25.320  -4.347  -8.939  1.00 35.07      A    C  
ATOM   1540  O   TYR A 842     -26.250  -5.060  -8.576  1.00 37.52      A    O  
ATOM   1541  CB  TYR A 842     -25.964  -3.783 -11.295  1.00 26.59      A    C  
ATOM   1542  CG  TYR A 842     -25.534  -3.544 -12.733  1.00 31.09      A    C  
ATOM   1543  CD1 TYR A 842     -25.062  -2.295 -13.146  1.00 27.52      A    C  
ATOM   1544  CD2 TYR A 842     -25.603  -4.570 -13.678  1.00 24.88      A    C  
ATOM   1545  CE1 TYR A 842     -24.672  -2.073 -14.474  1.00 28.06      A    C  
ATOM   1546  CE2 TYR A 842     -25.217  -4.369 -14.992  1.00 31.76      A    C  
ATOM   1547  CZ  TYR A 842     -24.754  -3.120 -15.385  1.00 25.62      A    C  
ATOM   1548  OH  TYR A 842     -24.379  -2.945 -16.681  1.00 31.07      A    O  
ATOM   1549  N   VAL A 843     -24.672  -3.556  -8.103  1.00 35.13      A    N  
ATOM   1550  CA  VAL A 843     -25.037  -3.505  -6.700  1.00 39.14      A    C  
ATOM   1551  C   VAL A 843     -25.965  -2.331  -6.443  1.00 33.67      A    C  
ATOM   1552  O   VAL A 843     -25.664  -1.216  -6.863  1.00 31.31      A    O  
ATOM   1553  CB  VAL A 843     -23.781  -3.369  -5.818  1.00 36.92      A    C  
ATOM   1554  CG1 VAL A 843     -24.153  -3.475  -4.364  1.00 46.02      A    C  
ATOM   1555  CG2 VAL A 843     -22.784  -4.459  -6.183  1.00 39.94      A    C  
ATOM   1556  N   VAL A 844     -27.084  -2.593  -5.760  1.00 33.93      A    N  
ATOM   1557  CA  VAL A 844     -28.081  -1.564  -5.426  1.00 38.28      A    C  
ATOM   1558  C   VAL A 844     -27.613  -0.603  -4.333  1.00 37.89      A    C  
ATOM   1559  O   VAL A 844     -27.137  -1.036  -3.303  1.00 39.57      A    O  
ATOM   1560  CB  VAL A 844     -29.420  -2.220  -4.967  1.00 41.20      A    C  
ATOM   1561  CG1 VAL A 844     -30.378  -1.165  -4.416  1.00 33.69      A    C  
ATOM   1562  CG2 VAL A 844     -30.070  -2.945  -6.136  1.00 36.39      A    C  
ATOM   1563  N   ARG A 845     -27.758   0.699  -4.568  1.00 36.08      A    N  
ATOM   1564  CA  ARG A 845     -27.349   1.727  -3.603  1.00 44.80      A    C  
ATOM   1565  C   ARG A 845     -28.254   2.943  -3.804  1.00 45.78      A    C  
ATOM   1566  O   ARG A 845     -27.973   3.800  -4.641  1.00 48.96      A    O  
ATOM   1567  CB  ARG A 845     -25.890   2.140  -3.852  1.00 54.46      A    C  
ATOM   1568  CG  ARG A 845     -25.103   2.537  -2.611  1.00 60.56      A    C  
ATOM   1569  CD  ARG A 845     -25.786   3.621  -1.778  1.00 76.55      A    C  
ATOM   1570  NE  ARG A 845     -25.020   3.911  -0.562  1.00 85.97      A    N  
ATOM   1571  CZ  ARG A 845     -25.374   4.789   0.376  1.00 87.18      A    C  
ATOM   1572  NH1 ARG A 845     -26.497   5.489   0.258  1.00 83.82      A    N1+
ATOM   1573  NH2 ARG A 845     -24.599   4.962   1.441  1.00 79.62      A    N  
ATOM   1574  N   GLY A 846     -29.342   3.022  -3.049  1.00 44.75      A    N  
ATOM   1575  CA  GLY A 846     -30.239   4.147  -3.227  1.00 48.39      A    C  
ATOM   1576  C   GLY A 846     -30.732   4.167  -4.664  1.00 50.55      A    C  
ATOM   1577  O   GLY A 846     -31.266   3.169  -5.151  1.00 50.82      A    O  
ATOM   1578  N   ASN A 847     -30.546   5.287  -5.358  1.00 51.90      A    N  
ATOM   1579  CA  ASN A 847     -31.004   5.388  -6.742  1.00 59.11      A    C  
ATOM   1580  C   ASN A 847     -29.964   4.928  -7.748  1.00 54.71      A    C  
ATOM   1581  O   ASN A 847     -30.138   5.099  -8.956  1.00 54.47      A    O  
ATOM   1582  CB  ASN A 847     -31.435   6.823  -7.067  1.00 66.58      A    C  
ATOM   1583  CG  ASN A 847     -32.867   7.107  -6.643  1.00 78.75      A    C  
ATOM   1584  ND2 ASN A 847     -33.543   6.087  -6.130  1.00 80.21      A    N  
ATOM   1585  OD1 ASN A 847     -33.360   8.228  -6.782  1.00 92.70      A    O  
ATOM   1586  N   ALA A 848     -28.888   4.324  -7.255  1.00 45.22      A    N  
ATOM   1587  CA  ALA A 848     -27.850   3.860  -8.153  1.00 39.04      A    C  
ATOM   1588  C   ALA A 848     -27.758   2.334  -8.250  1.00 39.62      A    C  
ATOM   1589  O   ALA A 848     -28.131   1.607  -7.331  1.00 40.31      A    O  
ATOM   1590  CB  ALA A 848     -26.517   4.456  -7.742  1.00 36.83      A    C  
ATOM   1591  N   ARG A 849     -27.300   1.867  -9.405  1.00 35.92      A    N  
ATOM   1592  CA  ARG A 849     -27.118   0.439  -9.676  1.00 36.87      A    C  
ATOM   1593  C   ARG A 849     -25.710   0.424 -10.229  1.00 40.38      A    C  
ATOM   1594  O   ARG A 849     -25.494   0.692 -11.407  1.00 36.13      A    O  
ATOM   1595  CB  ARG A 849     -28.111  -0.029 -10.722  1.00 39.24      A    C  
ATOM   1596  CG  ARG A 849     -29.547   0.334 -10.384  1.00 41.59      A    C  
ATOM   1597  CD  ARG A 849     -30.085  -0.472  -9.215  1.00 42.37      A    C  
ATOM   1598  NE  ARG A 849     -31.492  -0.151  -9.008  1.00 42.67      A    N  
ATOM   1599  CZ  ARG A 849     -31.937   0.846  -8.251  1.00 46.19      A    C  
ATOM   1600  NH1 ARG A 849     -31.087   1.630  -7.595  1.00 36.05      A    N1+
ATOM   1601  NH2 ARG A 849     -33.239   1.082  -8.183  1.00 46.37      A    N  
ATOM   1602  N   LEU A 850     -24.760   0.114  -9.353  1.00 31.03      A    N  
ATOM   1603  CA  LEU A 850     -23.347   0.155  -9.683  1.00 27.76      A    C  
ATOM   1604  C   LEU A 850     -22.621  -1.142 -10.045  1.00 32.07      A    C  
ATOM   1605  O   LEU A 850     -22.705  -2.138  -9.341  1.00 31.13      A    O  
ATOM   1606  CB  LEU A 850     -22.607   0.818  -8.521  1.00 34.00      A    C  
ATOM   1607  CG  LEU A 850     -23.182   2.164  -8.053  1.00 46.47      A    C  
ATOM   1608  CD1 LEU A 850     -22.635   2.520  -6.682  1.00 46.56      A    C  
ATOM   1609  CD2 LEU A 850     -22.841   3.238  -9.064  1.00 39.86      A    C  
ATOM   1610  N   PRO A 851     -21.881  -1.122 -11.162  1.00 31.83      A    N  
ATOM   1611  CA  PRO A 851     -21.101  -2.264 -11.656  1.00 28.95      A    C  
ATOM   1612  C   PRO A 851     -19.780  -2.238 -10.867  1.00 25.13      A    C  
ATOM   1613  O   PRO A 851     -18.687  -2.065 -11.420  1.00 20.72      A    O  
ATOM   1614  CB  PRO A 851     -20.925  -1.940 -13.142  1.00 27.89      A    C  
ATOM   1615  CG  PRO A 851     -20.810  -0.452 -13.149  1.00 28.93      A    C  
ATOM   1616  CD  PRO A 851     -21.824   0.022 -12.098  1.00 25.33      A    C  
ATOM   1617  N   VAL A 852     -19.902  -2.415  -9.558  1.00 25.66      A    N  
ATOM   1618  CA  VAL A 852     -18.757  -2.339  -8.654  1.00 22.12      A    C  
ATOM   1619  C   VAL A 852     -17.452  -3.022  -9.053  1.00 15.96      A    C  
ATOM   1620  O   VAL A 852     -16.384  -2.412  -8.935  1.00 19.88      A    O  
ATOM   1621  CB  VAL A 852     -19.168  -2.802  -7.231  1.00 29.72      A    C  
ATOM   1622  CG1 VAL A 852     -17.961  -2.857  -6.335  1.00 31.03      A    C  
ATOM   1623  CG2 VAL A 852     -20.197  -1.801  -6.658  1.00 23.95      A    C  
ATOM   1624  N   LYS A 853     -17.524  -4.271  -9.540  1.00 18.43      A    N  
ATOM   1625  CA  LYS A 853     -16.296  -4.958  -9.913  1.00 14.79      A    C  
ATOM   1626  C   LYS A 853     -15.571  -4.373 -11.144  1.00 22.36      A    C  
ATOM   1627  O   LYS A 853     -14.425  -4.714 -11.411  1.00 21.12      A    O  
ATOM   1628  CB  LYS A 853     -16.569  -6.458 -10.094  1.00 22.21      A    C  
ATOM   1629  CG  LYS A 853     -16.767  -7.169  -8.751  1.00 21.46      A    C  
ATOM   1630  CD  LYS A 853     -16.879  -8.684  -8.940  1.00 23.33      A    C  
ATOM   1631  CE  LYS A 853     -16.916  -9.434  -7.604  1.00 20.42      A    C  
ATOM   1632  NZ  LYS A 853     -16.954 -10.925  -7.844  1.00 21.53      A    N1+
ATOM   1633  N   TRP A 854     -16.238  -3.488 -11.881  1.00 19.97      A    N  
ATOM   1634  CA  TRP A 854     -15.625  -2.844 -13.045  1.00 23.68      A    C  
ATOM   1635  C   TRP A 854     -15.145  -1.415 -12.740  1.00 28.27      A    C  
ATOM   1636  O   TRP A 854     -14.406  -0.806 -13.522  1.00 23.64      A    O  
ATOM   1637  CB  TRP A 854     -16.630  -2.796 -14.201  1.00 21.53      A    C  
ATOM   1638  CG  TRP A 854     -16.764  -4.123 -14.930  1.00 22.73      A    C  
ATOM   1639  CD1 TRP A 854     -16.153  -4.481 -16.099  1.00 24.79      A    C  
ATOM   1640  CD2 TRP A 854     -17.507  -5.271 -14.495  1.00 22.00      A    C  
ATOM   1641  CE2 TRP A 854     -17.300  -6.295 -15.453  1.00 22.04      A    C  
ATOM   1642  CE3 TRP A 854     -18.323  -5.534 -13.389  1.00 20.00      A    C  
ATOM   1643  NE1 TRP A 854     -16.470  -5.790 -16.421  1.00 23.65      A    N  
ATOM   1644  CZ2 TRP A 854     -17.880  -7.565 -15.336  1.00 20.54      A    C  
ATOM   1645  CZ3 TRP A 854     -18.906  -6.811 -13.270  1.00 21.48      A    C  
ATOM   1646  CH2 TRP A 854     -18.678  -7.804 -14.239  1.00 24.05      A    C  
ATOM   1647  N   MET A 855     -15.528  -0.905 -11.579  1.00 21.55      A    N  
ATOM   1648  CA  MET A 855     -15.203   0.482 -11.194  1.00 19.24      A    C  
ATOM   1649  C   MET A 855     -13.824   0.863 -10.657  1.00 29.16      A    C  
ATOM   1650  O   MET A 855     -13.271   0.219  -9.757  1.00 28.40      A    O  
ATOM   1651  CB  MET A 855     -16.265   0.974 -10.199  1.00 20.61      A    C  
ATOM   1652  CG  MET A 855     -17.663   1.064 -10.834  1.00 23.67      A    C  
ATOM   1653  SD  MET A 855     -19.002   1.268  -9.641  1.00 28.09      A    S  
ATOM   1654  CE  MET A 855     -18.644   2.926  -8.958  1.00 27.72      A    C  
ATOM   1655  N   ALA A 856     -13.288   1.955 -11.201  1.00 23.21      A    N  
ATOM   1656  CA  ALA A 856     -12.003   2.470 -10.753  1.00 24.68      A    C  
ATOM   1657  C   ALA A 856     -12.225   2.928  -9.317  1.00 20.75      A    C  
ATOM   1658  O   ALA A 856     -13.342   3.267  -8.922  1.00 19.20      A    O  
ATOM   1659  CB  ALA A 856     -11.560   3.668 -11.613  1.00 24.66      A    C  
ATOM   1660  N   PRO A 857     -11.158   2.954  -8.516  1.00 24.01      A    N  
ATOM   1661  CA  PRO A 857     -11.260   3.383  -7.114  1.00 25.80      A    C  
ATOM   1662  C   PRO A 857     -11.874   4.783  -6.985  1.00 29.61      A    C  
ATOM   1663  O   PRO A 857     -12.722   5.008  -6.109  1.00 28.12      A    O  
ATOM   1664  CB  PRO A 857      -9.807   3.377  -6.635  1.00 27.31      A    C  
ATOM   1665  CG  PRO A 857      -9.139   2.391  -7.506  1.00 34.21      A    C  
ATOM   1666  CD  PRO A 857      -9.781   2.576  -8.867  1.00 21.23      A    C  
ATOM   1667  N   GLU A 858     -11.449   5.727  -7.839  1.00 25.86      A    N  
ATOM   1668  CA  GLU A 858     -11.999   7.088  -7.756  1.00 25.02      A    C  
ATOM   1669  C   GLU A 858     -13.511   7.115  -8.057  1.00 32.17      A    C  
ATOM   1670  O   GLU A 858     -14.235   7.990  -7.577  1.00 28.08      A    O  
ATOM   1671  CB  GLU A 858     -11.237   8.070  -8.668  1.00 35.35      A    C  
ATOM   1672  CG  GLU A 858     -11.371   7.881 -10.183  1.00 29.00      A    C  
ATOM   1673  CD  GLU A 858     -10.392   6.885 -10.749  1.00 34.70      A    C  
ATOM   1674  OE1 GLU A 858     -10.174   6.905 -11.987  1.00 29.84      A    O  
ATOM   1675  OE2 GLU A 858      -9.844   6.073  -9.961  1.00 29.59      A    O1-
ATOM   1676  N   SER A 859     -13.999   6.144  -8.827  1.00 23.49      A    N  
ATOM   1677  CA  SER A 859     -15.440   6.079  -9.105  1.00 23.76      A    C  
ATOM   1678  C   SER A 859     -16.134   5.450  -7.880  1.00 27.03      A    C  
ATOM   1679  O   SER A 859     -17.218   5.868  -7.475  1.00 28.11      A    O  
ATOM   1680  CB  SER A 859     -15.718   5.205 -10.347  1.00 27.68      A    C  
ATOM   1681  OG  SER A 859     -14.952   5.615 -11.473  1.00 28.41      A    O  
ATOM   1682  N   LEU A 860     -15.517   4.417  -7.313  1.00 27.75      A    N  
ATOM   1683  CA  LEU A 860     -16.081   3.739  -6.145  1.00 35.97      A    C  
ATOM   1684  C   LEU A 860     -16.170   4.665  -4.923  1.00 29.36      A    C  
ATOM   1685  O   LEU A 860     -17.204   4.759  -4.267  1.00 33.42      A    O  
ATOM   1686  CB  LEU A 860     -15.207   2.553  -5.737  1.00 30.04      A    C  
ATOM   1687  CG  LEU A 860     -15.233   1.240  -6.497  1.00 35.49      A    C  
ATOM   1688  CD1 LEU A 860     -14.150   0.311  -5.911  1.00 36.33      A    C  
ATOM   1689  CD2 LEU A 860     -16.630   0.628  -6.376  1.00 35.38      A    C  
ATOM   1690  N   PHE A 861     -15.071   5.348  -4.643  1.00 29.96      A    N  
ATOM   1691  CA  PHE A 861     -14.984   6.201  -3.462  1.00 38.84      A    C  
ATOM   1692  C   PHE A 861     -15.288   7.685  -3.608  1.00 46.78      A    C  
ATOM   1693  O   PHE A 861     -15.475   8.360  -2.605  1.00 44.27      A    O  
ATOM   1694  CB  PHE A 861     -13.594   6.027  -2.857  1.00 29.64      A    C  
ATOM   1695  CG  PHE A 861     -13.196   4.587  -2.696  1.00 30.92      A    C  
ATOM   1696  CD1 PHE A 861     -12.041   4.097  -3.288  1.00 29.49      A    C  
ATOM   1697  CD2 PHE A 861     -14.009   3.710  -1.988  1.00 34.82      A    C  
ATOM   1698  CE1 PHE A 861     -11.699   2.755  -3.183  1.00 37.84      A    C  
ATOM   1699  CE2 PHE A 861     -13.674   2.356  -1.878  1.00 40.48      A    C  
ATOM   1700  CZ  PHE A 861     -12.518   1.883  -2.478  1.00 36.53      A    C  
ATOM   1701  N   GLU A 862     -15.335   8.199  -4.835  1.00 43.95      A    N  
ATOM   1702  CA  GLU A 862     -15.601   9.620  -5.028  1.00 35.08      A    C  
ATOM   1703  C   GLU A 862     -16.681   9.933  -6.068  1.00 39.32      A    C  
ATOM   1704  O   GLU A 862     -17.005  11.090  -6.292  1.00 36.58      A    O  
ATOM   1705  CB  GLU A 862     -14.303  10.316  -5.405  1.00 43.26      A    C  
ATOM   1706  CG  GLU A 862     -13.216  10.130  -4.370  1.00 54.13      A    C  
ATOM   1707  CD  GLU A 862     -11.857   9.889  -4.998  1.00 68.44      A    C  
ATOM   1708  OE1 GLU A 862     -11.310  10.825  -5.624  1.00 72.44      A    O  
ATOM   1709  OE2 GLU A 862     -11.340   8.753  -4.873  1.00 70.92      A    O1-
ATOM   1710  N   GLY A 863     -17.243   8.910  -6.706  1.00 31.66      A    N  
ATOM   1711  CA  GLY A 863     -18.259   9.168  -7.710  1.00 33.35      A    C  
ATOM   1712  C   GLY A 863     -17.686   9.886  -8.930  1.00 28.22      A    C  
ATOM   1713  O   GLY A 863     -18.419  10.506  -9.684  1.00 40.49      A    O  
ATOM   1714  N   ILE A 864     -16.372   9.784  -9.119  1.00 29.05      A    N  
ATOM   1715  CA  ILE A 864     -15.639  10.399 -10.238  1.00 35.86      A    C  
ATOM   1716  C   ILE A 864     -15.539   9.428 -11.433  1.00 42.22      A    C  
ATOM   1717  O   ILE A 864     -15.216   8.245 -11.247  1.00 32.77      A    O  
ATOM   1718  CB  ILE A 864     -14.190  10.767  -9.763  1.00 40.64      A    C  
ATOM   1719  CG1 ILE A 864     -14.239  11.957  -8.801  1.00 56.84      A    C  
ATOM   1720  CG2 ILE A 864     -13.284  11.102 -10.935  1.00 45.41      A    C  
ATOM   1721  CD1 ILE A 864     -12.887  12.260  -8.141  1.00 61.68      A    C  
ATOM   1722  N   TYR A 865     -15.815   9.922 -12.645  1.00 34.46      A    N  
ATOM   1723  CA  TYR A 865     -15.720   9.107 -13.872  1.00 30.04      A    C  
ATOM   1724  C   TYR A 865     -15.032   9.872 -14.996  1.00 31.35      A    C  
ATOM   1725  O   TYR A 865     -15.633  10.754 -15.607  1.00 28.87      A    O  
ATOM   1726  CB  TYR A 865     -17.091   8.688 -14.411  1.00 32.17      A    C  
ATOM   1727  CG  TYR A 865     -17.872   7.758 -13.533  1.00 32.72      A    C  
ATOM   1728  CD1 TYR A 865     -18.742   8.262 -12.565  1.00 34.65      A    C  
ATOM   1729  CD2 TYR A 865     -17.729   6.364 -13.647  1.00 30.12      A    C  
ATOM   1730  CE1 TYR A 865     -19.455   7.412 -11.725  1.00 38.53      A    C  
ATOM   1731  CE2 TYR A 865     -18.443   5.495 -12.805  1.00 35.67      A    C  
ATOM   1732  CZ  TYR A 865     -19.302   6.032 -11.849  1.00 39.91      A    C  
ATOM   1733  OH  TYR A 865     -20.017   5.206 -11.015  1.00 45.26      A    O  
ATOM   1734  N   THR A 866     -13.789   9.510 -15.286  1.00 27.18      A    N  
ATOM   1735  CA  THR A 866     -13.038  10.158 -16.348  1.00 30.41      A    C  
ATOM   1736  C   THR A 866     -12.630   9.111 -17.380  1.00 29.39      A    C  
ATOM   1737  O   THR A 866     -12.931   7.914 -17.234  1.00 28.48      A    O  
ATOM   1738  CB  THR A 866     -11.753  10.816 -15.795  1.00 23.79      A    C  
ATOM   1739  CG2 THR A 866     -12.066  11.739 -14.579  1.00 30.47      A    C  
ATOM   1740  OG1 THR A 866     -10.866   9.782 -15.373  1.00 32.22      A    O  
ATOM   1741  N   ILE A 867     -11.944   9.547 -18.427  1.00 28.09      A    N  
ATOM   1742  CA  ILE A 867     -11.492   8.605 -19.429  1.00 29.64      A    C  
ATOM   1743  C   ILE A 867     -10.468   7.661 -18.759  1.00 30.42      A    C  
ATOM   1744  O   ILE A 867     -10.345   6.489 -19.135  1.00 31.23      A    O  
ATOM   1745  CB  ILE A 867     -10.867   9.329 -20.665  1.00 31.25      A    C  
ATOM   1746  CG1 ILE A 867     -10.703   8.334 -21.818  1.00 28.92      A    C  
ATOM   1747  CG2 ILE A 867      -9.527   9.939 -20.311  1.00 28.11      A    C  
ATOM   1748  CD1 ILE A 867     -12.074   7.828 -22.385  1.00 29.71      A    C  
ATOM   1749  N   LYS A 868      -9.757   8.163 -17.751  1.00 27.55      A    N  
ATOM   1750  CA  LYS A 868      -8.771   7.334 -17.037  1.00 27.38      A    C  
ATOM   1751  C   LYS A 868      -9.482   6.245 -16.214  1.00 23.44      A    C  
ATOM   1752  O   LYS A 868      -8.945   5.152 -16.012  1.00 29.16      A    O  
ATOM   1753  CB  LYS A 868      -7.915   8.190 -16.098  1.00 39.18      A    C  
ATOM   1754  CG  LYS A 868      -6.969   9.180 -16.788  1.00 48.36      A    C  
ATOM   1755  CD  LYS A 868      -6.295  10.081 -15.742  1.00 59.83      A    C  
ATOM   1756  CE  LYS A 868      -5.263  11.014 -16.345  1.00 68.20      A    C  
ATOM   1757  NZ  LYS A 868      -4.135  10.260 -16.965  1.00 80.94      A    N1+
ATOM   1758  N   SER A 869     -10.673   6.554 -15.708  1.00 21.66      A    N  
ATOM   1759  CA  SER A 869     -11.430   5.547 -14.959  1.00 24.34      A    C  
ATOM   1760  C   SER A 869     -11.766   4.445 -15.984  1.00 29.43      A    C  
ATOM   1761  O   SER A 869     -11.783   3.254 -15.660  1.00 25.33      A    O  
ATOM   1762  CB  SER A 869     -12.719   6.166 -14.405  1.00 21.56      A    C  
ATOM   1763  OG  SER A 869     -12.420   7.293 -13.602  1.00 34.18      A    O  
ATOM   1764  N   ASP A 870     -12.032   4.855 -17.224  1.00 22.15      A    N  
ATOM   1765  CA  ASP A 870     -12.344   3.894 -18.268  1.00 26.76      A    C  
ATOM   1766  C   ASP A 870     -11.153   3.006 -18.599  1.00 19.48      A    C  
ATOM   1767  O   ASP A 870     -11.330   1.869 -19.028  1.00 30.85      A    O  
ATOM   1768  CB  ASP A 870     -12.846   4.582 -19.539  1.00 28.05      A    C  
ATOM   1769  CG  ASP A 870     -14.344   4.833 -19.504  1.00 27.15      A    C  
ATOM   1770  OD1 ASP A 870     -15.098   3.924 -19.077  1.00 29.32      A    O  
ATOM   1771  OD2 ASP A 870     -14.772   5.924 -19.918  1.00 27.89      A    O1-
ATOM   1772  N   VAL A 871      -9.942   3.511 -18.402  1.00 24.09      A    N  
ATOM   1773  CA  VAL A 871      -8.777   2.685 -18.651  1.00 23.70      A    C  
ATOM   1774  C   VAL A 871      -8.782   1.551 -17.616  1.00 27.54      A    C  
ATOM   1775  O   VAL A 871      -8.437   0.407 -17.924  1.00 25.31      A    O  
ATOM   1776  CB  VAL A 871      -7.456   3.506 -18.561  1.00 33.06      A    C  
ATOM   1777  CG1 VAL A 871      -6.250   2.569 -18.610  1.00 30.17      A    C  
ATOM   1778  CG2 VAL A 871      -7.381   4.487 -19.745  1.00 31.93      A    C  
ATOM   1779  N   TRP A 872      -9.190   1.864 -16.393  1.00 28.86      A    N  
ATOM   1780  CA  TRP A 872      -9.269   0.847 -15.350  1.00 27.21      A    C  
ATOM   1781  C   TRP A 872     -10.330  -0.197 -15.756  1.00 20.40      A    C  
ATOM   1782  O   TRP A 872     -10.064  -1.410 -15.793  1.00 24.01      A    O  
ATOM   1783  CB  TRP A 872      -9.657   1.484 -14.018  1.00 26.36      A    C  
ATOM   1784  CG  TRP A 872      -9.888   0.472 -12.914  1.00 28.70      A    C  
ATOM   1785  CD1 TRP A 872     -10.930  -0.405 -12.810  1.00 25.08      A    C  
ATOM   1786  CD2 TRP A 872      -9.069   0.259 -11.760  1.00 25.77      A    C  
ATOM   1787  CE2 TRP A 872      -9.683  -0.763 -10.994  1.00 29.15      A    C  
ATOM   1788  CE3 TRP A 872      -7.873   0.834 -11.291  1.00 23.49      A    C  
ATOM   1789  NE1 TRP A 872     -10.815  -1.151 -11.661  1.00 25.31      A    N  
ATOM   1790  CZ2 TRP A 872      -9.142  -1.226  -9.786  1.00 29.06      A    C  
ATOM   1791  CZ3 TRP A 872      -7.335   0.373 -10.090  1.00 33.04      A    C  
ATOM   1792  CH2 TRP A 872      -7.973  -0.649  -9.351  1.00 32.08      A    C  
ATOM   1793  N   SER A 873     -11.532   0.274 -16.071  1.00 21.39      A    N  
ATOM   1794  CA  SER A 873     -12.589  -0.643 -16.474  1.00 24.34      A    C  
ATOM   1795  C   SER A 873     -12.130  -1.454 -17.703  1.00 27.38      A    C  
ATOM   1796  O   SER A 873     -12.405  -2.652 -17.824  1.00 22.82      A    O  
ATOM   1797  CB  SER A 873     -13.862   0.145 -16.790  1.00 23.74      A    C  
ATOM   1798  OG  SER A 873     -14.357   0.777 -15.628  1.00 45.84      A    O  
ATOM   1799  N   TYR A 874     -11.421  -0.803 -18.614  1.00 23.58      A    N  
ATOM   1800  CA  TYR A 874     -10.928  -1.502 -19.797  1.00 24.16      A    C  
ATOM   1801  C   TYR A 874     -10.009  -2.672 -19.372  1.00 27.70      A    C  
ATOM   1802  O   TYR A 874     -10.007  -3.738 -19.991  1.00 26.54      A    O  
ATOM   1803  CB  TYR A 874     -10.154  -0.538 -20.698  1.00 23.96      A    C  
ATOM   1804  CG  TYR A 874      -9.526  -1.212 -21.889  1.00 24.05      A    C  
ATOM   1805  CD1 TYR A 874     -10.298  -1.611 -22.965  1.00 26.60      A    C  
ATOM   1806  CD2 TYR A 874      -8.157  -1.466 -21.923  1.00 26.79      A    C  
ATOM   1807  CE1 TYR A 874      -9.724  -2.254 -24.063  1.00 35.20      A    C  
ATOM   1808  CE2 TYR A 874      -7.573  -2.110 -23.007  1.00 33.37      A    C  
ATOM   1809  CZ  TYR A 874      -8.361  -2.500 -24.072  1.00 30.60      A    C  
ATOM   1810  OH  TYR A 874      -7.793  -3.152 -25.146  1.00 37.86      A    O  
ATOM   1811  N   GLY A 875      -9.215  -2.461 -18.329  1.00 24.67      A    N  
ATOM   1812  CA  GLY A 875      -8.356  -3.534 -17.860  1.00 22.15      A    C  
ATOM   1813  C   GLY A 875      -9.200  -4.706 -17.360  1.00 21.26      A    C  
ATOM   1814  O   GLY A 875      -8.840  -5.881 -17.559  1.00 28.89      A    O  
ATOM   1815  N   ILE A 876     -10.324  -4.402 -16.705  1.00 22.43      A    N  
ATOM   1816  CA  ILE A 876     -11.201  -5.464 -16.223  1.00 21.44      A    C  
ATOM   1817  C   ILE A 876     -11.790  -6.178 -17.460  1.00 24.59      A    C  
ATOM   1818  O   ILE A 876     -11.878  -7.417 -17.508  1.00 20.94      A    O  
ATOM   1819  CB  ILE A 876     -12.351  -4.901 -15.321  1.00 21.86      A    C  
ATOM   1820  CG1 ILE A 876     -11.762  -4.123 -14.125  1.00 28.14      A    C  
ATOM   1821  CG2 ILE A 876     -13.274  -6.057 -14.853  1.00 18.60      A    C  
ATOM   1822  CD1 ILE A 876     -10.929  -4.955 -13.087  1.00 17.73      A    C  
ATOM   1823  N   LEU A 877     -12.170  -5.407 -18.473  1.00 21.17      A    N  
ATOM   1824  CA  LEU A 877     -12.732  -5.996 -19.693  1.00 24.03      A    C  
ATOM   1825  C   LEU A 877     -11.682  -6.905 -20.391  1.00 18.08      A    C  
ATOM   1826  O   LEU A 877     -12.029  -7.946 -20.983  1.00 25.33      A    O  
ATOM   1827  CB  LEU A 877     -13.223  -4.876 -20.636  1.00 24.36      A    C  
ATOM   1828  CG  LEU A 877     -14.075  -5.234 -21.869  1.00 25.33      A    C  
ATOM   1829  CD1 LEU A 877     -14.830  -4.003 -22.382  1.00 24.49      A    C  
ATOM   1830  CD2 LEU A 877     -13.182  -5.796 -22.960  1.00 27.06      A    C  
ATOM   1831  N   LEU A 878     -10.407  -6.512 -20.299  1.00 21.45      A    N  
ATOM   1832  CA  LEU A 878      -9.325  -7.304 -20.882  1.00 25.98      A    C  
ATOM   1833  C   LEU A 878      -9.298  -8.665 -20.156  1.00 36.02      A    C  
ATOM   1834  O   LEU A 878      -9.171  -9.731 -20.782  1.00 29.27      A    O  
ATOM   1835  CB  LEU A 878      -7.974  -6.590 -20.704  1.00 23.00      A    C  
ATOM   1836  CG  LEU A 878      -7.480  -5.571 -21.731  1.00 37.91      A    C  
ATOM   1837  CD1 LEU A 878      -6.031  -5.218 -21.409  1.00 34.99      A    C  
ATOM   1838  CD2 LEU A 878      -7.557  -6.171 -23.128  1.00 40.61      A    C  
ATOM   1839  N   TRP A 879      -9.424  -8.621 -18.834  1.00 25.31      A    N  
ATOM   1840  CA  TRP A 879      -9.439  -9.849 -18.044  1.00 30.32      A    C  
ATOM   1841  C   TRP A 879     -10.665 -10.692 -18.488  1.00 16.87      A    C  
ATOM   1842  O   TRP A 879     -10.577 -11.907 -18.640  1.00 28.08      A    O  
ATOM   1843  CB  TRP A 879      -9.510  -9.520 -16.549  1.00 29.04      A    C  
ATOM   1844  CG  TRP A 879      -9.155 -10.693 -15.667  1.00 22.79      A    C  
ATOM   1845  CD1 TRP A 879      -7.915 -11.017 -15.180  1.00 26.25      A    C  
ATOM   1846  CD2 TRP A 879     -10.052 -11.683 -15.169  1.00 20.14      A    C  
ATOM   1847  CE2 TRP A 879      -9.293 -12.580 -14.374  1.00 25.41      A    C  
ATOM   1848  CE3 TRP A 879     -11.433 -11.902 -15.310  1.00 19.87      A    C  
ATOM   1849  NE1 TRP A 879      -7.993 -12.150 -14.396  1.00 28.09      A    N  
ATOM   1850  CZ2 TRP A 879      -9.874 -13.680 -13.723  1.00 26.82      A    C  
ATOM   1851  CZ3 TRP A 879     -12.002 -12.982 -14.662  1.00 23.05      A    C  
ATOM   1852  CH2 TRP A 879     -11.232 -13.859 -13.878  1.00 19.35      A    C  
ATOM   1853  N   GLU A 880     -11.806 -10.044 -18.704  1.00 22.32      A    N  
ATOM   1854  CA  GLU A 880     -12.966 -10.788 -19.181  1.00 23.23      A    C  
ATOM   1855  C   GLU A 880     -12.642 -11.496 -20.520  1.00 27.22      A    C  
ATOM   1856  O   GLU A 880     -12.974 -12.664 -20.724  1.00 24.55      A    O  
ATOM   1857  CB  GLU A 880     -14.147  -9.851 -19.404  1.00 28.40      A    C  
ATOM   1858  CG  GLU A 880     -14.790  -9.310 -18.150  1.00 22.68      A    C  
ATOM   1859  CD  GLU A 880     -16.004  -8.505 -18.495  1.00 20.77      A    C  
ATOM   1860  OE1 GLU A 880     -15.861  -7.284 -18.773  1.00 20.80      A    O  
ATOM   1861  OE2 GLU A 880     -17.107  -9.092 -18.509  1.00 20.93      A    O1-
ATOM   1862  N   ILE A 881     -12.015 -10.775 -21.441  1.00 25.09      A    N  
ATOM   1863  CA  ILE A 881     -11.663 -11.367 -22.732  1.00 33.41      A    C  
ATOM   1864  C   ILE A 881     -10.691 -12.566 -22.581  1.00 28.75      A    C  
ATOM   1865  O   ILE A 881     -10.944 -13.657 -23.096  1.00 31.32      A    O  
ATOM   1866  CB  ILE A 881     -11.008 -10.297 -23.684  1.00 28.94      A    C  
ATOM   1867  CG1 ILE A 881     -12.072  -9.258 -24.106  1.00 29.80      A    C  
ATOM   1868  CG2 ILE A 881     -10.343 -10.999 -24.909  1.00 29.58      A    C  
ATOM   1869  CD1 ILE A 881     -11.520  -8.040 -24.882  1.00 28.21      A    C  
ATOM   1870  N   PHE A 882      -9.597 -12.372 -21.856  1.00 30.26      A    N  
ATOM   1871  CA  PHE A 882      -8.632 -13.439 -21.730  1.00 29.25      A    C  
ATOM   1872  C   PHE A 882      -8.905 -14.549 -20.708  1.00 31.70      A    C  
ATOM   1873  O   PHE A 882      -8.028 -15.361 -20.414  1.00 25.27      A    O  
ATOM   1874  CB  PHE A 882      -7.235 -12.836 -21.581  1.00 26.57      A    C  
ATOM   1875  CG  PHE A 882      -6.792 -12.091 -22.807  1.00 34.87      A    C  
ATOM   1876  CD1 PHE A 882      -7.022 -10.712 -22.931  1.00 27.99      A    C  
ATOM   1877  CD2 PHE A 882      -6.216 -12.773 -23.872  1.00 31.86      A    C  
ATOM   1878  CE1 PHE A 882      -6.683 -10.030 -24.104  1.00 41.48      A    C  
ATOM   1879  CE2 PHE A 882      -5.874 -12.106 -25.050  1.00 36.30      A    C  
ATOM   1880  CZ  PHE A 882      -6.109 -10.729 -25.168  1.00 37.48      A    C  
ATOM   1881  N   SER A 883     -10.141 -14.597 -20.216  1.00 29.58      A    N  
ATOM   1882  CA  SER A 883     -10.576 -15.645 -19.290  1.00 35.05      A    C  
ATOM   1883  C   SER A 883     -11.802 -16.258 -19.957  1.00 37.08      A    C  
ATOM   1884  O   SER A 883     -12.432 -17.173 -19.426  1.00 28.25      A    O  
ATOM   1885  CB  SER A 883     -11.006 -15.053 -17.942  1.00 26.69      A    C  
ATOM   1886  OG  SER A 883     -12.270 -14.405 -18.060  1.00 25.21      A    O  
ATOM   1887  N   LEU A 884     -12.131 -15.740 -21.139  1.00 27.50      A    N  
ATOM   1888  CA  LEU A 884     -13.321 -16.157 -21.873  1.00 23.65      A    C  
ATOM   1889  C   LEU A 884     -14.615 -15.913 -21.092  1.00 27.89      A    C  
ATOM   1890  O   LEU A 884     -15.514 -16.762 -21.036  1.00 26.91      A    O  
ATOM   1891  CB  LEU A 884     -13.273 -17.621 -22.341  1.00 25.91      A    C  
ATOM   1892  CG  LEU A 884     -12.205 -18.002 -23.383  1.00 37.65      A    C  
ATOM   1893  CD1 LEU A 884     -12.550 -19.365 -23.997  1.00 30.06      A    C  
ATOM   1894  CD2 LEU A 884     -12.148 -16.969 -24.486  1.00 30.97      A    C  
ATOM   1895  N   GLY A 885     -14.710 -14.734 -20.480  1.00 23.64      A    N  
ATOM   1896  CA  GLY A 885     -15.959 -14.390 -19.834  1.00 22.31      A    C  
ATOM   1897  C   GLY A 885     -16.231 -14.741 -18.393  1.00 26.28      A    C  
ATOM   1898  O   GLY A 885     -17.397 -14.854 -17.999  1.00 28.49      A    O  
ATOM   1899  N   VAL A 886     -15.178 -14.894 -17.602  1.00 24.04      A    N  
ATOM   1900  CA  VAL A 886     -15.375 -15.201 -16.200  1.00 25.86      A    C  
ATOM   1901  C   VAL A 886     -15.689 -13.898 -15.456  1.00 26.42      A    C  
ATOM   1902  O   VAL A 886     -15.172 -12.827 -15.802  1.00 22.30      A    O  
ATOM   1903  CB  VAL A 886     -14.103 -15.852 -15.573  1.00 30.42      A    C  
ATOM   1904  CG1 VAL A 886     -14.317 -16.072 -14.053  1.00 22.68      A    C  
ATOM   1905  CG2 VAL A 886     -13.783 -17.194 -16.294  1.00 24.27      A    C  
ATOM   1906  N   ASN A 887     -16.555 -13.989 -14.456  1.00 24.83      A    N  
ATOM   1907  CA  ASN A 887     -16.879 -12.838 -13.618  1.00 29.17      A    C  
ATOM   1908  C   ASN A 887     -15.556 -12.364 -12.976  1.00 19.41      A    C  
ATOM   1909  O   ASN A 887     -14.762 -13.185 -12.523  1.00 27.03      A    O  
ATOM   1910  CB  ASN A 887     -17.861 -13.274 -12.511  1.00 32.22      A    C  
ATOM   1911  CG  ASN A 887     -18.407 -12.103 -11.702  1.00 45.13      A    C  
ATOM   1912  ND2 ASN A 887     -18.141 -12.104 -10.393  1.00 38.84      A    N  
ATOM   1913  OD1 ASN A 887     -19.068 -11.215 -12.244  1.00 45.64      A    O  
ATOM   1914  N   PRO A 888     -15.292 -11.035 -12.953  1.00 24.85      A    N  
ATOM   1915  CA  PRO A 888     -14.063 -10.486 -12.351  1.00 26.01      A    C  
ATOM   1916  C   PRO A 888     -14.001 -10.868 -10.851  1.00 22.57      A    C  
ATOM   1917  O   PRO A 888     -15.045 -11.035 -10.222  1.00 20.47      A    O  
ATOM   1918  CB  PRO A 888     -14.233  -8.964 -12.530  1.00 21.41      A    C  
ATOM   1919  CG  PRO A 888     -15.085  -8.859 -13.752  1.00 31.89      A    C  
ATOM   1920  CD  PRO A 888     -16.099  -9.965 -13.567  1.00 26.34      A    C  
ATOM   1921  N   TYR A 889     -12.796 -10.974 -10.292  1.00 18.75      A    N  
ATOM   1922  CA  TYR A 889     -12.614 -11.338  -8.879  1.00 25.71      A    C  
ATOM   1923  C   TYR A 889     -13.544 -12.523  -8.555  1.00 24.34      A    C  
ATOM   1924  O   TYR A 889     -14.356 -12.475  -7.612  1.00 23.59      A    O  
ATOM   1925  CB  TYR A 889     -12.939 -10.128  -7.986  1.00 21.20      A    C  
ATOM   1926  CG  TYR A 889     -12.270  -8.829  -8.421  1.00 21.25      A    C  
ATOM   1927  CD1 TYR A 889     -12.926  -7.929  -9.282  1.00 22.87      A    C  
ATOM   1928  CD2 TYR A 889     -10.997  -8.483  -7.954  1.00 22.33      A    C  
ATOM   1929  CE1 TYR A 889     -12.330  -6.718  -9.657  1.00 18.61      A    C  
ATOM   1930  CE2 TYR A 889     -10.393  -7.259  -8.324  1.00 23.38      A    C  
ATOM   1931  CZ  TYR A 889     -11.059  -6.392  -9.167  1.00 24.52      A    C  
ATOM   1932  OH  TYR A 889     -10.468  -5.197  -9.519  1.00 27.12      A    O  
ATOM   1933  N   PRO A 890     -13.427 -13.615  -9.340  1.00 23.16      A    N  
ATOM   1934  CA  PRO A 890     -14.258 -14.809  -9.171  1.00 20.70      A    C  
ATOM   1935  C   PRO A 890     -14.252 -15.372  -7.761  1.00 27.65      A    C  
ATOM   1936  O   PRO A 890     -13.190 -15.594  -7.177  1.00 23.33      A    O  
ATOM   1937  CB  PRO A 890     -13.703 -15.784 -10.224  1.00 17.69      A    C  
ATOM   1938  CG  PRO A 890     -12.253 -15.354 -10.364  1.00 23.89      A    C  
ATOM   1939  CD  PRO A 890     -12.340 -13.852 -10.312  1.00 25.47      A    C  
ATOM   1940  N   GLY A 891     -15.451 -15.564  -7.216  1.00 23.91      A    N  
ATOM   1941  CA  GLY A 891     -15.575 -16.114  -5.877  1.00 30.05      A    C  
ATOM   1942  C   GLY A 891     -15.539 -15.064  -4.780  1.00 32.95      A    C  
ATOM   1943  O   GLY A 891     -15.832 -15.366  -3.628  1.00 34.28      A    O  
ATOM   1944  N   ILE A 892     -15.175 -13.830  -5.118  1.00 27.81      A    N  
ATOM   1945  CA  ILE A 892     -15.117 -12.775  -4.112  1.00 21.81      A    C  
ATOM   1946  C   ILE A 892     -16.425 -11.995  -4.142  1.00 27.24      A    C  
ATOM   1947  O   ILE A 892     -16.793 -11.421  -5.167  1.00 28.45      A    O  
ATOM   1948  CB  ILE A 892     -13.921 -11.839  -4.375  1.00 20.38      A    C  
ATOM   1949  CG1 ILE A 892     -12.625 -12.653  -4.342  1.00 22.65      A    C  
ATOM   1950  CG2 ILE A 892     -13.874 -10.692  -3.330  1.00 22.73      A    C  
ATOM   1951  CD1 ILE A 892     -11.376 -11.825  -4.667  1.00 25.84      A    C  
ATOM   1952  N   PRO A 893     -17.143 -11.955  -3.010  1.00 25.37      A    N  
ATOM   1953  CA  PRO A 893     -18.419 -11.229  -2.963  1.00 22.06      A    C  
ATOM   1954  C   PRO A 893     -18.245  -9.719  -2.858  1.00 25.30      A    C  
ATOM   1955  O   PRO A 893     -17.179  -9.226  -2.484  1.00 19.86      A    O  
ATOM   1956  CB  PRO A 893     -19.102 -11.807  -1.719  1.00 25.09      A    C  
ATOM   1957  CG  PRO A 893     -17.923 -12.054  -0.791  1.00 27.00      A    C  
ATOM   1958  CD  PRO A 893     -16.892 -12.670  -1.736  1.00 36.37      A    C  
ATOM   1959  N   VAL A 894     -19.297  -8.986  -3.211  1.00 21.26      A    N  
ATOM   1960  CA  VAL A 894     -19.253  -7.536  -3.073  1.00 26.11      A    C  
ATOM   1961  C   VAL A 894     -19.814  -7.194  -1.687  1.00 25.07      A    C  
ATOM   1962  O   VAL A 894     -20.993  -7.400  -1.418  1.00 25.02      A    O  
ATOM   1963  CB  VAL A 894     -20.095  -6.818  -4.156  1.00 25.42      A    C  
ATOM   1964  CG1 VAL A 894     -19.995  -5.303  -3.959  1.00 23.77      A    C  
ATOM   1965  CG2 VAL A 894     -19.595  -7.212  -5.541  1.00 27.16      A    C  
ATOM   1966  N   ASP A 895     -18.944  -6.701  -0.811  1.00 27.26      A    N  
ATOM   1967  CA  ASP A 895     -19.298  -6.312   0.554  1.00 31.10      A    C  
ATOM   1968  C   ASP A 895     -18.231  -5.309   1.014  1.00 33.07      A    C  
ATOM   1969  O   ASP A 895     -17.395  -4.905   0.204  1.00 29.37      A    O  
ATOM   1970  CB  ASP A 895     -19.359  -7.548   1.480  1.00 23.41      A    C  
ATOM   1971  CG  ASP A 895     -18.050  -8.385   1.497  1.00 25.35      A    C  
ATOM   1972  OD1 ASP A 895     -16.965  -7.896   1.074  1.00 25.98      A    O  
ATOM   1973  OD2 ASP A 895     -18.119  -9.560   1.961  1.00 28.29      A    O1-
ATOM   1974  N   ALA A 896     -18.247  -4.897   2.282  1.00 30.31      A    N  
ATOM   1975  CA  ALA A 896     -17.248  -3.927   2.777  1.00 27.93      A    C  
ATOM   1976  C   ALA A 896     -15.810  -4.408   2.534  1.00 20.55      A    C  
ATOM   1977  O   ALA A 896     -14.928  -3.598   2.267  1.00 26.11      A    O  
ATOM   1978  CB  ALA A 896     -17.453  -3.630   4.287  1.00 24.53      A    C  
ATOM   1979  N   ASN A 897     -15.570  -5.719   2.636  1.00 18.45      A    N  
ATOM   1980  CA  ASN A 897     -14.217  -6.242   2.383  1.00 19.04      A    C  
ATOM   1981  C   ASN A 897     -13.784  -6.076   0.911  1.00 23.49      A    C  
ATOM   1982  O   ASN A 897     -12.592  -5.997   0.618  1.00 25.13      A    O  
ATOM   1983  CB  ASN A 897     -14.125  -7.732   2.761  1.00 20.38      A    C  
ATOM   1984  CG  ASN A 897     -14.151  -7.948   4.270  1.00 29.50      A    C  
ATOM   1985  ND2 ASN A 897     -14.541  -9.130   4.704  1.00 18.50      A    N  
ATOM   1986  OD1 ASN A 897     -13.809  -7.055   5.025  1.00 24.88      A    O  
ATOM   1987  N   PHE A 898     -14.735  -6.058  -0.018  1.00 27.16      A    N  
ATOM   1988  CA  PHE A 898     -14.358  -5.891  -1.419  1.00 22.66      A    C  
ATOM   1989  C   PHE A 898     -13.795  -4.476  -1.613  1.00 21.36      A    C  
ATOM   1990  O   PHE A 898     -12.758  -4.291  -2.264  1.00 22.32      A    O  
ATOM   1991  CB  PHE A 898     -15.546  -6.095  -2.366  1.00 24.49      A    C  
ATOM   1992  CG  PHE A 898     -15.194  -5.840  -3.801  1.00 24.86      A    C  
ATOM   1993  CD1 PHE A 898     -15.396  -4.582  -4.363  1.00 26.32      A    C  
ATOM   1994  CD2 PHE A 898     -14.516  -6.809  -4.544  1.00 24.30      A    C  
ATOM   1995  CE1 PHE A 898     -14.912  -4.287  -5.642  1.00 33.49      A    C  
ATOM   1996  CE2 PHE A 898     -14.027  -6.525  -5.817  1.00 27.99      A    C  
ATOM   1997  CZ  PHE A 898     -14.226  -5.250  -6.366  1.00 20.22      A    C  
ATOM   1998  N   TYR A 899     -14.478  -3.485  -1.029  1.00 25.68      A    N  
ATOM   1999  CA  TYR A 899     -14.012  -2.106  -1.141  1.00 31.27      A    C  
ATOM   2000  C   TYR A 899     -12.630  -1.953  -0.525  1.00 34.70      A    C  
ATOM   2001  O   TYR A 899     -11.766  -1.282  -1.098  1.00 24.73      A    O  
ATOM   2002  CB  TYR A 899     -14.994  -1.133  -0.483  1.00 35.72      A    C  
ATOM   2003  CG  TYR A 899     -16.312  -1.058  -1.214  1.00 46.03      A    C  
ATOM   2004  CD1 TYR A 899     -17.297  -2.016  -1.003  1.00 56.64      A    C  
ATOM   2005  CD2 TYR A 899     -16.563  -0.057  -2.153  1.00 53.32      A    C  
ATOM   2006  CE1 TYR A 899     -18.494  -1.988  -1.698  1.00 52.46      A    C  
ATOM   2007  CE2 TYR A 899     -17.766  -0.024  -2.862  1.00 57.81      A    C  
ATOM   2008  CZ  TYR A 899     -18.723  -0.997  -2.620  1.00 55.17      A    C  
ATOM   2009  OH  TYR A 899     -19.926  -0.984  -3.275  1.00 64.63      A    O  
ATOM   2010  N   LYS A 900     -12.411  -2.585   0.631  1.00 24.76      A    N  
ATOM   2011  CA  LYS A 900     -11.103  -2.504   1.283  1.00 22.75      A    C  
ATOM   2012  C   LYS A 900     -10.010  -3.148   0.424  1.00 21.79      A    C  
ATOM   2013  O   LYS A 900      -8.894  -2.643   0.358  1.00 28.31      A    O  
ATOM   2014  CB  LYS A 900     -11.153  -3.170   2.669  1.00 28.16      A    C  
ATOM   2015  CG  LYS A 900     -11.903  -2.354   3.719  1.00 37.25      A    C  
ATOM   2016  CD  LYS A 900     -12.070  -3.111   5.044  1.00 46.61      A    C  
ATOM   2017  CE  LYS A 900     -10.736  -3.556   5.654  1.00 32.60      A    C  
ATOM   2018  NZ  LYS A 900     -10.997  -4.181   6.987  1.00 38.79      A    N1+
ATOM   2019  N   LEU A 901     -10.335  -4.264  -0.223  1.00 24.60      A    N  
ATOM   2020  CA  LEU A 901      -9.389  -4.954  -1.101  1.00 29.33      A    C  
ATOM   2021  C   LEU A 901      -8.892  -3.987  -2.187  1.00 22.72      A    C  
ATOM   2022  O   LEU A 901      -7.689  -3.854  -2.417  1.00 27.81      A    O  
ATOM   2023  CB  LEU A 901     -10.060  -6.135  -1.822  1.00 30.27      A    C  
ATOM   2024  CG  LEU A 901     -10.341  -7.466  -1.140  1.00 49.63      A    C  
ATOM   2025  CD1 LEU A 901     -10.850  -8.453  -2.192  1.00 40.30      A    C  
ATOM   2026  CD2 LEU A 901      -9.063  -7.998  -0.488  1.00 53.28      A    C  
ATOM   2027  N   ILE A 902      -9.839  -3.372  -2.893  1.00 27.82      A    N  
ATOM   2028  CA  ILE A 902      -9.509  -2.427  -3.954  1.00 26.95      A    C  
ATOM   2029  C   ILE A 902      -8.658  -1.295  -3.378  1.00 29.55      A    C  
ATOM   2030  O   ILE A 902      -7.591  -1.001  -3.889  1.00 25.36      A    O  
ATOM   2031  CB  ILE A 902     -10.783  -1.823  -4.596  1.00 24.42      A    C  
ATOM   2032  CG1 ILE A 902     -11.627  -2.942  -5.211  1.00 23.50      A    C  
ATOM   2033  CG2 ILE A 902     -10.395  -0.844  -5.675  1.00 25.25      A    C  
ATOM   2034  CD1 ILE A 902     -10.916  -3.696  -6.357  1.00 27.38      A    C  
ATOM   2035  N   GLN A 903      -9.131  -0.678  -2.302  1.00 32.67      A    N  
ATOM   2036  CA  GLN A 903      -8.388   0.409  -1.660  1.00 31.83      A    C  
ATOM   2037  C   GLN A 903      -6.940   0.010  -1.346  1.00 29.31      A    C  
ATOM   2038  O   GLN A 903      -6.026   0.828  -1.452  1.00 34.99      A    O  
ATOM   2039  CB  GLN A 903      -9.085   0.820  -0.365  1.00 35.18      A    C  
ATOM   2040  CG  GLN A 903      -8.299   1.802   0.476  1.00 49.47      A    C  
ATOM   2041  CD  GLN A 903      -8.202   3.183  -0.170  1.00 63.68      A    C  
ATOM   2042  NE2 GLN A 903      -9.193   3.528  -0.985  1.00 58.43      A    N  
ATOM   2043  OE1 GLN A 903      -7.250   3.930   0.075  1.00 62.60      A    O  
ATOM   2044  N   ASN A 904      -6.731  -1.248  -0.959  1.00 28.88      A    N  
ATOM   2045  CA  ASN A 904      -5.392  -1.722  -0.620  1.00 28.87      A    C  
ATOM   2046  C   ASN A 904      -4.524  -2.095  -1.819  1.00 30.49      A    C  
ATOM   2047  O   ASN A 904      -3.378  -2.439  -1.644  1.00 29.38      A    O  
ATOM   2048  CB  ASN A 904      -5.479  -2.919   0.322  1.00 31.76      A    C  
ATOM   2049  CG  ASN A 904      -5.910  -2.528   1.721  1.00 40.35      A    C  
ATOM   2050  ND2 ASN A 904      -5.200  -1.578   2.321  1.00 34.88      A    N  
ATOM   2051  OD1 ASN A 904      -6.861  -3.078   2.258  1.00 44.43      A    O  
ATOM   2052  N   GLY A 905      -5.071  -2.077  -3.027  1.00 29.66      A    N  
ATOM   2053  CA  GLY A 905      -4.240  -2.395  -4.186  1.00 27.05      A    C  
ATOM   2054  C   GLY A 905      -4.342  -3.806  -4.723  1.00 27.49      A    C  
ATOM   2055  O   GLY A 905      -3.568  -4.208  -5.588  1.00 27.57      A    O  
ATOM   2056  N   PHE A 906      -5.305  -4.563  -4.214  1.00 23.53      A    N  
ATOM   2057  CA  PHE A 906      -5.535  -5.940  -4.679  1.00 29.09      A    C  
ATOM   2058  C   PHE A 906      -5.834  -5.927  -6.191  1.00 33.07      A    C  
ATOM   2059  O   PHE A 906      -6.608  -5.094  -6.664  1.00 31.41      A    O  
ATOM   2060  CB  PHE A 906      -6.741  -6.528  -3.924  1.00 24.65      A    C  
ATOM   2061  CG  PHE A 906      -6.970  -8.001  -4.164  1.00 30.84      A    C  
ATOM   2062  CD1 PHE A 906      -6.495  -8.941  -3.267  1.00 30.82      A    C  
ATOM   2063  CD2 PHE A 906      -7.710  -8.438  -5.264  1.00 28.48      A    C  
ATOM   2064  CE1 PHE A 906      -6.755 -10.302  -3.451  1.00 32.41      A    C  
ATOM   2065  CE2 PHE A 906      -7.972  -9.792  -5.451  1.00 32.43      A    C  
ATOM   2066  CZ  PHE A 906      -7.493 -10.722  -4.541  1.00 29.36      A    C  
ATOM   2067  N   LYS A 907      -5.214  -6.851  -6.927  1.00 31.29      A    N  
ATOM   2068  CA  LYS A 907      -5.401  -6.995  -8.374  1.00 34.28      A    C  
ATOM   2069  C   LYS A 907      -5.582  -8.467  -8.738  1.00 32.83      A    C  
ATOM   2070  O   LYS A 907      -5.064  -9.365  -8.065  1.00 29.75      A    O  
ATOM   2071  CB  LYS A 907      -4.192  -6.465  -9.151  1.00 28.65      A    C  
ATOM   2072  CG  LYS A 907      -4.013  -4.949  -9.132  1.00 30.44      A    C  
ATOM   2073  CD  LYS A 907      -2.703  -4.580  -9.827  1.00 36.22      A    C  
ATOM   2074  CE  LYS A 907      -2.286  -3.152  -9.539  1.00 41.15      A    C  
ATOM   2075  NZ  LYS A 907      -2.043  -2.955  -8.077  1.00 58.93      A    N1+
ATOM   2076  N   MET A 908      -6.311  -8.715  -9.816  1.00 31.57      A    N  
ATOM   2077  CA  MET A 908      -6.538 -10.081 -10.248  1.00 27.84      A    C  
ATOM   2078  C   MET A 908      -5.270 -10.687 -10.811  1.00 28.41      A    C  
ATOM   2079  O   MET A 908      -4.381  -9.965 -11.277  1.00 27.04      A    O  
ATOM   2080  CB  MET A 908      -7.622 -10.143 -11.330  1.00 26.24      A    C  
ATOM   2081  CG  MET A 908      -9.052  -9.900 -10.824  1.00 24.69      A    C  
ATOM   2082  SD  MET A 908     -10.279 -10.234 -12.092  1.00 25.81      A    S  
ATOM   2083  CE  MET A 908     -10.353  -8.619 -12.971  1.00 14.17      A    C  
ATOM   2084  N   ASP A 909      -5.222 -12.019 -10.777  1.00 27.28      A    N  
ATOM   2085  CA  ASP A 909      -4.129 -12.804 -11.331  1.00 34.02      A    C  
ATOM   2086  C   ASP A 909      -4.265 -12.854 -12.848  1.00 33.08      A    C  
ATOM   2087  O   ASP A 909      -5.329 -12.553 -13.408  1.00 27.48      A    O  
ATOM   2088  CB  ASP A 909      -4.197 -14.241 -10.823  1.00 35.56      A    C  
ATOM   2089  CG  ASP A 909      -3.926 -14.350  -9.347  1.00 39.92      A    C  
ATOM   2090  OD1 ASP A 909      -4.547 -15.219  -8.702  1.00 49.21      A    O  
ATOM   2091  OD2 ASP A 909      -3.089 -13.572  -8.842  1.00 36.71      A    O1-
ATOM   2092  N   GLN A 910      -3.190 -13.266 -13.507  1.00 35.25      A    N  
ATOM   2093  CA  GLN A 910      -3.180 -13.391 -14.959  1.00 27.39      A    C  
ATOM   2094  C   GLN A 910      -4.172 -14.477 -15.387  1.00 29.34      A    C  
ATOM   2095  O   GLN A 910      -4.081 -15.618 -14.943  1.00 32.68      A    O  
ATOM   2096  CB  GLN A 910      -1.764 -13.752 -15.424  1.00 31.14      A    C  
ATOM   2097  CG  GLN A 910      -1.644 -14.100 -16.907  1.00 38.19      A    C  
ATOM   2098  CD  GLN A 910      -0.192 -14.358 -17.337  1.00 39.30      A    C  
ATOM   2099  NE2 GLN A 910       0.763 -13.845 -16.566  1.00 39.08      A    N  
ATOM   2100  OE1 GLN A 910       0.054 -14.994 -18.358  1.00 44.51      A    O  
ATOM   2101  N   PRO A 911      -5.155 -14.131 -16.238  1.00 28.80      A    N  
ATOM   2102  CA  PRO A 911      -6.113 -15.154 -16.665  1.00 25.54      A    C  
ATOM   2103  C   PRO A 911      -5.424 -16.146 -17.617  1.00 31.06      A    C  
ATOM   2104  O   PRO A 911      -4.377 -15.831 -18.202  1.00 30.40      A    O  
ATOM   2105  CB  PRO A 911      -7.222 -14.337 -17.322  1.00 28.54      A    C  
ATOM   2106  CG  PRO A 911      -6.467 -13.168 -17.908  1.00 26.37      A    C  
ATOM   2107  CD  PRO A 911      -5.440 -12.823 -16.859  1.00 31.10      A    C  
ATOM   2108  N   PHE A 912      -6.010 -17.332 -17.767  1.00 28.38      A    N  
ATOM   2109  CA  PHE A 912      -5.422 -18.389 -18.584  1.00 34.79      A    C  
ATOM   2110  C   PHE A 912      -4.982 -18.018 -20.011  1.00 43.32      A    C  
ATOM   2111  O   PHE A 912      -3.841 -18.279 -20.397  1.00 39.88      A    O  
ATOM   2112  CB  PHE A 912      -6.373 -19.591 -18.648  1.00 35.20      A    C  
ATOM   2113  CG  PHE A 912      -5.772 -20.803 -19.315  1.00 48.10      A    C  
ATOM   2114  CD1 PHE A 912      -4.792 -21.559 -18.665  1.00 41.80      A    C  
ATOM   2115  CD2 PHE A 912      -6.148 -21.162 -20.616  1.00 45.27      A    C  
ATOM   2116  CE1 PHE A 912      -4.185 -22.660 -19.303  1.00 48.49      A    C  
ATOM   2117  CE2 PHE A 912      -5.552 -22.261 -21.269  1.00 47.03      A    C  
ATOM   2118  CZ  PHE A 912      -4.567 -23.010 -20.610  1.00 49.43      A    C  
ATOM   2119  N   TYR A 913      -5.864 -17.410 -20.798  1.00 37.92      A    N  
ATOM   2120  CA  TYR A 913      -5.501 -17.074 -22.170  1.00 34.44      A    C  
ATOM   2121  C   TYR A 913      -4.619 -15.857 -22.383  1.00 33.44      A    C  
ATOM   2122  O   TYR A 913      -4.236 -15.568 -23.510  1.00 39.89      A    O  
ATOM   2123  CB  TYR A 913      -6.758 -16.962 -23.014  1.00 25.54      A    C  
ATOM   2124  CG  TYR A 913      -7.586 -18.216 -22.933  1.00 30.88      A    C  
ATOM   2125  CD1 TYR A 913      -8.629 -18.333 -22.018  1.00 31.68      A    C  
ATOM   2126  CD2 TYR A 913      -7.292 -19.316 -23.742  1.00 37.57      A    C  
ATOM   2127  CE1 TYR A 913      -9.366 -19.522 -21.906  1.00 29.09      A    C  
ATOM   2128  CE2 TYR A 913      -8.015 -20.501 -23.640  1.00 33.58      A    C  
ATOM   2129  CZ  TYR A 913      -9.045 -20.600 -22.727  1.00 39.62      A    C  
ATOM   2130  OH  TYR A 913      -9.744 -21.783 -22.630  1.00 34.38      A    O  
ATOM   2131  N   ALA A 914      -4.289 -15.133 -21.320  1.00 33.79      A    N  
ATOM   2132  CA  ALA A 914      -3.429 -13.976 -21.504  1.00 33.55      A    C  
ATOM   2133  C   ALA A 914      -1.962 -14.402 -21.506  1.00 42.71      A    C  
ATOM   2134  O   ALA A 914      -1.593 -15.423 -20.931  1.00 43.08      A    O  
ATOM   2135  CB  ALA A 914      -3.661 -12.961 -20.405  1.00 32.85      A    C  
ATOM   2136  N   THR A 915      -1.132 -13.612 -22.170  1.00 37.72      A    N  
ATOM   2137  CA  THR A 915       0.298 -13.870 -22.225  1.00 41.95      A    C  
ATOM   2138  C   THR A 915       0.770 -12.945 -21.131  1.00 43.78      A    C  
ATOM   2139  O   THR A 915      -0.026 -12.144 -20.629  1.00 42.43      A    O  
ATOM   2140  CB  THR A 915       0.901 -13.429 -23.590  1.00 39.56      A    C  
ATOM   2141  CG2 THR A 915       0.400 -14.325 -24.722  1.00 30.17      A    C  
ATOM   2142  OG1 THR A 915       0.506 -12.079 -23.859  1.00 39.24      A    O  
ATOM   2143  N   GLU A 916       2.040 -13.039 -20.751  1.00 43.13      A    N  
ATOM   2144  CA  GLU A 916       2.554 -12.176 -19.699  1.00 43.91      A    C  
ATOM   2145  C   GLU A 916       2.578 -10.703 -20.117  1.00 47.14      A    C  
ATOM   2146  O   GLU A 916       2.412  -9.822 -19.275  1.00 46.68      A    O  
ATOM   2147  CB  GLU A 916       3.960 -12.602 -19.289  1.00 52.02      A    C  
ATOM   2148  CG  GLU A 916       4.450 -11.886 -18.046  1.00 69.47      A    C  
ATOM   2149  CD  GLU A 916       5.958 -11.801 -17.969  1.00 79.04      A    C  
ATOM   2150  OE1 GLU A 916       6.475 -11.290 -16.948  1.00 83.99      A    O  
ATOM   2151  OE2 GLU A 916       6.627 -12.237 -18.932  1.00 80.31      A    O1-
ATOM   2152  N   GLU A 917       2.795 -10.433 -21.405  1.00 41.41      A    N  
ATOM   2153  CA  GLU A 917       2.836  -9.046 -21.898  1.00 45.27      A    C  
ATOM   2154  C   GLU A 917       1.450  -8.408 -21.760  1.00 33.48      A    C  
ATOM   2155  O   GLU A 917       1.324  -7.262 -21.328  1.00 40.49      A    O  
ATOM   2156  CB  GLU A 917       3.278  -8.983 -23.371  1.00 46.81      A    C  
ATOM   2157  CG  GLU A 917       4.518  -9.803 -23.715  1.00 58.36      A    C  
ATOM   2158  CD  GLU A 917       4.216 -11.296 -23.824  1.00 73.36      A    C  
ATOM   2159  OE1 GLU A 917       4.583 -12.061 -22.899  1.00 65.38      A    O  
ATOM   2160  OE2 GLU A 917       3.597 -11.701 -24.839  1.00 79.68      A    O1-
ATOM   2161  N   ILE A 918       0.418  -9.154 -22.142  1.00 36.06      A    N  
ATOM   2162  CA  ILE A 918      -0.949  -8.664 -22.011  1.00 40.18      A    C  
ATOM   2163  C   ILE A 918      -1.267  -8.415 -20.529  1.00 45.43      A    C  
ATOM   2164  O   ILE A 918      -1.857  -7.391 -20.183  1.00 48.76      A    O  
ATOM   2165  CB  ILE A 918      -1.953  -9.662 -22.607  1.00 38.47      A    C  
ATOM   2166  CG1 ILE A 918      -1.874  -9.603 -24.142  1.00 41.68      A    C  
ATOM   2167  CG2 ILE A 918      -3.369  -9.335 -22.140  1.00 31.19      A    C  
ATOM   2168  CD1 ILE A 918      -2.767 -10.590 -24.840  1.00 47.45      A    C  
ATOM   2169  N   TYR A 919      -0.842  -9.328 -19.656  1.00 41.55      A    N  
ATOM   2170  CA  TYR A 919      -1.100  -9.173 -18.225  1.00 38.07      A    C  
ATOM   2171  C   TYR A 919      -0.412  -7.946 -17.654  1.00 36.79      A    C  
ATOM   2172  O   TYR A 919      -0.923  -7.309 -16.729  1.00 38.14      A    O  
ATOM   2173  CB  TYR A 919      -0.655 -10.415 -17.446  1.00 35.71      A    C  
ATOM   2174  CG  TYR A 919      -0.977 -10.321 -15.975  1.00 34.75      A    C  
ATOM   2175  CD1 TYR A 919      -2.285 -10.067 -15.546  1.00 31.63      A    C  
ATOM   2176  CD2 TYR A 919       0.016 -10.472 -15.011  1.00 35.97      A    C  
ATOM   2177  CE1 TYR A 919      -2.594  -9.964 -14.196  1.00 33.76      A    C  
ATOM   2178  CE2 TYR A 919      -0.282 -10.371 -13.650  1.00 38.32      A    C  
ATOM   2179  CZ  TYR A 919      -1.596 -10.116 -13.254  1.00 37.78      A    C  
ATOM   2180  OH  TYR A 919      -1.907 -10.012 -11.919  1.00 36.76      A    O  
ATOM   2181  N   ILE A 920       0.758  -7.616 -18.192  1.00 41.15      A    N  
ATOM   2182  CA  ILE A 920       1.485  -6.435 -17.727  1.00 39.43      A    C  
ATOM   2183  C   ILE A 920       0.673  -5.186 -18.097  1.00 37.36      A    C  
ATOM   2184  O   ILE A 920       0.655  -4.197 -17.368  1.00 39.26      A    O  
ATOM   2185  CB  ILE A 920       2.896  -6.350 -18.377  1.00 49.25      A    C  
ATOM   2186  CG1 ILE A 920       3.808  -7.432 -17.787  1.00 52.36      A    C  
ATOM   2187  CG2 ILE A 920       3.500  -4.970 -18.148  1.00 39.69      A    C  
ATOM   2188  CD1 ILE A 920       5.164  -7.547 -18.491  1.00 45.94      A    C  
ATOM   2189  N   ILE A 921       0.002  -5.245 -19.238  1.00 36.25      A    N  
ATOM   2190  CA  ILE A 921      -0.830  -4.143 -19.692  1.00 40.37      A    C  
ATOM   2191  C   ILE A 921      -2.046  -4.041 -18.761  1.00 35.36      A    C  
ATOM   2192  O   ILE A 921      -2.407  -2.951 -18.314  1.00 37.55      A    O  
ATOM   2193  CB  ILE A 921      -1.271  -4.374 -21.160  1.00 40.80      A    C  
ATOM   2194  CG1 ILE A 921      -0.086  -4.110 -22.096  1.00 37.03      A    C  
ATOM   2195  CG2 ILE A 921      -2.455  -3.489 -21.509  1.00 34.51      A    C  
ATOM   2196  CD1 ILE A 921      -0.353  -4.510 -23.541  1.00 55.72      A    C  
ATOM   2197  N   MET A 922      -2.657  -5.183 -18.456  1.00 33.76      A    N  
ATOM   2198  CA  MET A 922      -3.802  -5.215 -17.546  1.00 35.92      A    C  
ATOM   2199  C   MET A 922      -3.460  -4.558 -16.217  1.00 31.02      A    C  
ATOM   2200  O   MET A 922      -4.217  -3.728 -15.722  1.00 33.94      A    O  
ATOM   2201  CB  MET A 922      -4.221  -6.653 -17.228  1.00 35.18      A    C  
ATOM   2202  CG  MET A 922      -4.980  -7.377 -18.290  1.00 40.08      A    C  
ATOM   2203  SD  MET A 922      -5.492  -8.988 -17.639  1.00 40.93      A    S  
ATOM   2204  CE  MET A 922      -5.816  -9.832 -19.167  1.00 42.86      A    C  
ATOM   2205  N   GLN A 923      -2.331  -4.976 -15.633  1.00 34.07      A    N  
ATOM   2206  CA  GLN A 923      -1.873  -4.465 -14.350  1.00 30.72      A    C  
ATOM   2207  C   GLN A 923      -1.673  -2.955 -14.335  1.00 31.46      A    C  
ATOM   2208  O   GLN A 923      -1.954  -2.311 -13.339  1.00 29.99      A    O  
ATOM   2209  CB  GLN A 923      -0.555  -5.141 -13.935  1.00 37.12      A    C  
ATOM   2210  CG  GLN A 923      -0.698  -6.583 -13.449  1.00 42.22      A    C  
ATOM   2211  CD  GLN A 923       0.655  -7.235 -13.142  1.00 56.46      A    C  
ATOM   2212  NE2 GLN A 923       0.857  -7.616 -11.890  1.00 48.89      A    N  
ATOM   2213  OE1 GLN A 923       1.503  -7.389 -14.027  1.00 52.35      A    O  
ATOM   2214  N   SER A 924      -1.159  -2.397 -15.426  1.00 31.87      A    N  
ATOM   2215  CA  SER A 924      -0.932  -0.958 -15.490  1.00 31.47      A    C  
ATOM   2216  C   SER A 924      -2.281  -0.241 -15.567  1.00 26.79      A    C  
ATOM   2217  O   SER A 924      -2.419   0.889 -15.103  1.00 30.24      A    O  
ATOM   2218  CB  SER A 924      -0.070  -0.599 -16.712  1.00 38.21      A    C  
ATOM   2219  OG  SER A 924      -0.726  -0.939 -17.922  1.00 47.25      A    O  
ATOM   2220  N   CYS A 925      -3.283  -0.903 -16.148  1.00 25.59      A    N  
ATOM   2221  CA  CYS A 925      -4.604  -0.283 -16.218  1.00 28.34      A    C  
ATOM   2222  C   CYS A 925      -5.173  -0.159 -14.813  1.00 31.80      A    C  
ATOM   2223  O   CYS A 925      -6.029   0.688 -14.557  1.00 26.21      A    O  
ATOM   2224  CB  CYS A 925      -5.558  -1.118 -17.077  1.00 31.37      A    C  
ATOM   2225  SG  CYS A 925      -5.246  -1.069 -18.875  1.00 33.43      A    S  
ATOM   2226  N   TRP A 926      -4.678  -0.996 -13.898  1.00 30.88      A    N  
ATOM   2227  CA  TRP A 926      -5.176  -1.006 -12.524  1.00 33.46      A    C  
ATOM   2228  C   TRP A 926      -4.302  -0.230 -11.537  1.00 33.51      A    C  
ATOM   2229  O   TRP A 926      -4.291  -0.507 -10.337  1.00 35.07      A    O  
ATOM   2230  CB  TRP A 926      -5.383  -2.464 -12.046  1.00 25.22      A    C  
ATOM   2231  CG  TRP A 926      -6.328  -3.282 -12.953  1.00 22.83      A    C  
ATOM   2232  CD1 TRP A 926      -7.417  -2.818 -13.652  1.00 23.38      A    C  
ATOM   2233  CD2 TRP A 926      -6.247  -4.692 -13.236  1.00 23.07      A    C  
ATOM   2234  CE2 TRP A 926      -7.310  -5.010 -14.107  1.00 24.03      A    C  
ATOM   2235  CE3 TRP A 926      -5.375  -5.716 -12.833  1.00 30.17      A    C  
ATOM   2236  NE1 TRP A 926      -8.010  -3.852 -14.355  1.00 22.81      A    N  
ATOM   2237  CZ2 TRP A 926      -7.525  -6.305 -14.580  1.00 22.27      A    C  
ATOM   2238  CZ3 TRP A 926      -5.593  -7.007 -13.306  1.00 23.49      A    C  
ATOM   2239  CH2 TRP A 926      -6.659  -7.285 -14.168  1.00 26.69      A    C  
ATOM   2240  N   ALA A 927      -3.567   0.753 -12.041  1.00 35.20      A    N  
ATOM   2241  CA  ALA A 927      -2.733   1.565 -11.167  1.00 32.44      A    C  
ATOM   2242  C   ALA A 927      -3.741   2.330 -10.331  1.00 36.38      A    C  
ATOM   2243  O   ALA A 927      -4.713   2.864 -10.865  1.00 29.85      A    O  
ATOM   2244  CB  ALA A 927      -1.855   2.520 -11.992  1.00 30.72      A    C  
ATOM   2245  N   PHE A 928      -3.532   2.368  -9.019  1.00 33.16      A    N  
ATOM   2246  CA  PHE A 928      -4.475   3.055  -8.144  1.00 32.30      A    C  
ATOM   2247  C   PHE A 928      -4.579   4.533  -8.539  1.00 37.00      A    C  
ATOM   2248  O   PHE A 928      -5.676   5.105  -8.634  1.00 32.54      A    O  
ATOM   2249  CB  PHE A 928      -4.031   2.932  -6.679  1.00 28.44      A    C  
ATOM   2250  CG  PHE A 928      -5.109   3.293  -5.700  1.00 34.72      A    C  
ATOM   2251  CD1 PHE A 928      -6.070   2.357  -5.327  1.00 34.80      A    C  
ATOM   2252  CD2 PHE A 928      -5.205   4.585  -5.198  1.00 37.18      A    C  
ATOM   2253  CE1 PHE A 928      -7.114   2.709  -4.471  1.00 38.58      A    C  
ATOM   2254  CE2 PHE A 928      -6.248   4.946  -4.341  1.00 35.33      A    C  
ATOM   2255  CZ  PHE A 928      -7.202   4.006  -3.980  1.00 32.57      A    C  
ATOM   2256  N   ASP A 929      -3.414   5.133  -8.760  1.00 33.68      A    N  
ATOM   2257  CA  ASP A 929      -3.267   6.534  -9.153  1.00 38.69      A    C  
ATOM   2258  C   ASP A 929      -3.634   6.616 -10.630  1.00 31.10      A    C  
ATOM   2259  O   ASP A 929      -2.941   6.046 -11.468  1.00 32.25      A    O  
ATOM   2260  CB  ASP A 929      -1.804   6.935  -8.927  1.00 38.64      A    C  
ATOM   2261  CG  ASP A 929      -1.522   8.392  -9.237  1.00 46.76      A    C  
ATOM   2262  OD1 ASP A 929      -0.424   8.847  -8.847  1.00 48.27      A    O  
ATOM   2263  OD2 ASP A 929      -2.364   9.074  -9.862  1.00 41.95      A    O1-
ATOM   2264  N   SER A 930      -4.712   7.320 -10.956  1.00 34.66      A    N  
ATOM   2265  CA  SER A 930      -5.146   7.408 -12.355  1.00 39.29      A    C  
ATOM   2266  C   SER A 930      -4.085   7.923 -13.331  1.00 41.98      A    C  
ATOM   2267  O   SER A 930      -4.063   7.509 -14.491  1.00 35.59      A    O  
ATOM   2268  CB  SER A 930      -6.410   8.267 -12.473  1.00 31.30      A    C  
ATOM   2269  OG  SER A 930      -6.158   9.614 -12.116  1.00 37.65      A    O  
ATOM   2270  N   ARG A 931      -3.214   8.819 -12.862  1.00 42.29      A    N  
ATOM   2271  CA  ARG A 931      -2.146   9.383 -13.701  1.00 39.99      A    C  
ATOM   2272  C   ARG A 931      -1.185   8.314 -14.200  1.00 41.62      A    C  
ATOM   2273  O   ARG A 931      -0.613   8.442 -15.274  1.00 43.79      A    O  
ATOM   2274  CB  ARG A 931      -1.322  10.424 -12.930  1.00 46.23      A    C  
ATOM   2275  CG  ARG A 931      -2.044  11.704 -12.562  1.00 47.81      A    C  
ATOM   2276  CD  ARG A 931      -2.985  11.504 -11.391  1.00 73.98      A    C  
ATOM   2277  NE  ARG A 931      -3.514  12.773 -10.892  1.00 87.97      A    N  
ATOM   2278  CZ  ARG A 931      -4.275  13.606 -11.599  1.00 92.77      A    C  
ATOM   2279  NH1 ARG A 931      -4.607  13.312 -12.851  1.00 96.94      A    N1+
ATOM   2280  NH2 ARG A 931      -4.703  14.739 -11.053  1.00 85.81      A    N  
ATOM   2281  N   LYS A 932      -1.007   7.257 -13.415  1.00 42.96      A    N  
ATOM   2282  CA  LYS A 932      -0.083   6.191 -13.784  1.00 36.50      A    C  
ATOM   2283  C   LYS A 932      -0.602   5.192 -14.799  1.00 34.91      A    C  
ATOM   2284  O   LYS A 932       0.170   4.406 -15.328  1.00 40.88      A    O  
ATOM   2285  CB  LYS A 932       0.378   5.442 -12.532  1.00 46.92      A    C  
ATOM   2286  CG  LYS A 932       1.073   6.328 -11.498  1.00 48.43      A    C  
ATOM   2287  CD  LYS A 932       1.527   5.513 -10.297  1.00 63.51      A    C  
ATOM   2288  CE  LYS A 932       2.240   6.388  -9.276  1.00 75.19      A    C  
ATOM   2289  NZ  LYS A 932       3.396   7.115  -9.884  1.00 82.48      A    N1+
ATOM   2290  N   ARG A 933      -1.903   5.208 -15.071  1.00 32.86      A    N  
ATOM   2291  CA  ARG A 933      -2.484   4.281 -16.035  1.00 37.09      A    C  
ATOM   2292  C   ARG A 933      -2.149   4.734 -17.436  1.00 37.84      A    C  
ATOM   2293  O   ARG A 933      -1.937   5.914 -17.676  1.00 34.22      A    O  
ATOM   2294  CB  ARG A 933      -4.014   4.236 -15.896  1.00 33.08      A    C  
ATOM   2295  CG  ARG A 933      -4.496   3.921 -14.480  1.00 31.62      A    C  
ATOM   2296  CD  ARG A 933      -6.008   4.075 -14.300  1.00 37.77      A    C  
ATOM   2297  NE  ARG A 933      -6.298   4.104 -12.876  1.00 28.41      A    N  
ATOM   2298  CZ  ARG A 933      -7.370   4.640 -12.310  1.00 31.12      A    C  
ATOM   2299  NH1 ARG A 933      -8.323   5.210 -13.040  1.00 30.45      A    N1+
ATOM   2300  NH2 ARG A 933      -7.447   4.662 -10.989  1.00 28.26      A    N  
ATOM   2301  N   PRO A 934      -2.086   3.795 -18.384  1.00 37.96      A    N  
ATOM   2302  CA  PRO A 934      -1.779   4.221 -19.745  1.00 38.11      A    C  
ATOM   2303  C   PRO A 934      -2.992   4.907 -20.380  1.00 43.86      A    C  
ATOM   2304  O   PRO A 934      -4.107   4.888 -19.845  1.00 35.18      A    O  
ATOM   2305  CB  PRO A 934      -1.428   2.914 -20.444  1.00 36.78      A    C  
ATOM   2306  CG  PRO A 934      -2.269   1.894 -19.695  1.00 36.27      A    C  
ATOM   2307  CD  PRO A 934      -2.086   2.326 -18.268  1.00 33.68      A    C  
ATOM   2308  N   SER A 935      -2.761   5.513 -21.531  1.00 40.28      A    N  
ATOM   2309  CA  SER A 935      -3.814   6.199 -22.253  1.00 37.76      A    C  
ATOM   2310  C   SER A 935      -4.357   5.230 -23.298  1.00 29.10      A    C  
ATOM   2311  O   SER A 935      -3.702   4.241 -23.651  1.00 34.08      A    O  
ATOM   2312  CB  SER A 935      -3.230   7.430 -22.962  1.00 40.88      A    C  
ATOM   2313  OG  SER A 935      -2.353   7.019 -24.007  1.00 38.91      A    O  
ATOM   2314  N   PHE A 936      -5.538   5.523 -23.826  1.00 29.14      A    N  
ATOM   2315  CA  PHE A 936      -6.086   4.658 -24.842  1.00 36.41      A    C  
ATOM   2316  C   PHE A 936      -5.219   4.681 -26.099  1.00 38.79      A    C  
ATOM   2317  O   PHE A 936      -4.939   3.631 -26.677  1.00 38.62      A    O  
ATOM   2318  CB  PHE A 936      -7.547   5.021 -25.109  1.00 34.33      A    C  
ATOM   2319  CG  PHE A 936      -8.480   4.424 -24.096  1.00 31.69      A    C  
ATOM   2320  CD1 PHE A 936      -8.535   3.035 -23.938  1.00 32.90      A    C  
ATOM   2321  CD2 PHE A 936      -9.249   5.234 -23.264  1.00 31.35      A    C  
ATOM   2322  CE1 PHE A 936      -9.349   2.443 -22.951  1.00 36.38      A    C  
ATOM   2323  CE2 PHE A 936     -10.071   4.670 -22.270  1.00 32.25      A    C  
ATOM   2324  CZ  PHE A 936     -10.119   3.263 -22.114  1.00 29.01      A    C  
ATOM   2325  N   PRO A 937      -4.777   5.872 -26.542  1.00 46.38      A    N  
ATOM   2326  CA  PRO A 937      -3.933   5.810 -27.742  1.00 44.69      A    C  
ATOM   2327  C   PRO A 937      -2.697   4.954 -27.412  1.00 43.70      A    C  
ATOM   2328  O   PRO A 937      -2.192   4.239 -28.273  1.00 47.91      A    O  
ATOM   2329  CB  PRO A 937      -3.622   7.285 -28.042  1.00 40.45      A    C  
ATOM   2330  CG  PRO A 937      -3.921   8.008 -26.755  1.00 54.96      A    C  
ATOM   2331  CD  PRO A 937      -5.089   7.263 -26.166  1.00 44.38      A    C  
ATOM   2332  N   ASN A 938      -2.232   5.006 -26.160  1.00 45.95      A    N  
ATOM   2333  CA  ASN A 938      -1.095   4.170 -25.745  1.00 52.41      A    C  
ATOM   2334  C   ASN A 938      -1.499   2.705 -25.926  1.00 53.45      A    C  
ATOM   2335  O   ASN A 938      -0.809   1.934 -26.587  1.00 58.29      A    O  
ATOM   2336  CB  ASN A 938      -0.754   4.329 -24.251  1.00 54.07      A    C  
ATOM   2337  CG  ASN A 938       0.002   5.601 -23.930  1.00 63.11      A    C  
ATOM   2338  ND2 ASN A 938      -0.132   6.054 -22.678  1.00 48.88      A    N  
ATOM   2339  OD1 ASN A 938       0.722   6.159 -24.771  1.00 52.14      A    O  
ATOM   2340  N   LEU A 939      -2.627   2.333 -25.319  1.00 44.98      A    N  
ATOM   2341  CA  LEU A 939      -3.110   0.962 -25.382  1.00 41.00      A    C  
ATOM   2342  C   LEU A 939      -3.321   0.479 -26.806  1.00 41.66      A    C  
ATOM   2343  O   LEU A 939      -3.037  -0.679 -27.128  1.00 36.00      A    O  
ATOM   2344  CB  LEU A 939      -4.411   0.827 -24.582  1.00 37.01      A    C  
ATOM   2345  CG  LEU A 939      -4.237   1.047 -23.078  1.00 41.91      A    C  
ATOM   2346  CD1 LEU A 939      -5.589   1.261 -22.410  1.00 38.37      A    C  
ATOM   2347  CD2 LEU A 939      -3.503  -0.141 -22.479  1.00 41.83      A    C  
ATOM   2348  N   THR A 940      -3.833   1.351 -27.665  1.00 34.63      A    N  
ATOM   2349  CA  THR A 940      -4.074   0.948 -29.048  1.00 45.09      A    C  
ATOM   2350  C   THR A 940      -2.765   0.554 -29.762  1.00 49.63      A    C  
ATOM   2351  O   THR A 940      -2.764  -0.326 -30.628  1.00 51.44      A    O  
ATOM   2352  CB  THR A 940      -4.807   2.064 -29.815  1.00 42.40      A    C  
ATOM   2353  CG2 THR A 940      -5.065   1.654 -31.246  1.00 50.57      A    C  
ATOM   2354  OG1 THR A 940      -6.074   2.306 -29.180  1.00 50.63      A    O  
ATOM   2355  N   SER A 941      -1.655   1.190 -29.387  1.00 47.57      A    N  
ATOM   2356  CA  SER A 941      -0.361   0.869 -29.988  1.00 56.41      A    C  
ATOM   2357  C   SER A 941       0.171  -0.447 -29.439  1.00 56.70      A    C  
ATOM   2358  O   SER A 941       0.513  -1.353 -30.200  1.00 60.82      A    O  
ATOM   2359  CB  SER A 941       0.649   1.981 -29.716  1.00 56.43      A    C  
ATOM   2360  OG  SER A 941       0.277   3.159 -30.404  1.00 72.87      A    O  
ATOM   2361  N   PHE A 942       0.246  -0.545 -28.114  1.00 55.02      A    N  
ATOM   2362  CA  PHE A 942       0.715  -1.763 -27.466  1.00 54.59      A    C  
ATOM   2363  C   PHE A 942      -0.016  -2.958 -28.087  1.00 57.01      A    C  
ATOM   2364  O   PHE A 942       0.605  -3.906 -28.562  1.00 61.68      A    O  
ATOM   2365  CB  PHE A 942       0.408  -1.731 -25.960  1.00 63.63      A    C  
ATOM   2366  CG  PHE A 942       0.997  -0.548 -25.223  1.00 72.67      A    C  
ATOM   2367  CD1 PHE A 942       0.568  -0.246 -23.928  1.00 73.97      A    C  
ATOM   2368  CD2 PHE A 942       1.985   0.250 -25.801  1.00 77.86      A    C  
ATOM   2369  CE1 PHE A 942       1.111   0.832 -23.215  1.00 71.77      A    C  
ATOM   2370  CE2 PHE A 942       2.536   1.333 -25.094  1.00 77.04      A    C  
ATOM   2371  CZ  PHE A 942       2.096   1.620 -23.798  1.00 72.95      A    C  
ATOM   2372  N   LEU A 943      -1.345  -2.896 -28.097  1.00 54.34      A    N  
ATOM   2373  CA  LEU A 943      -2.145  -3.985 -28.637  1.00 52.59      A    C  
ATOM   2374  C   LEU A 943      -1.975  -4.164 -30.135  1.00 57.33      A    C  
ATOM   2375  O   LEU A 943      -1.863  -5.293 -30.613  1.00 48.40      A    O  
ATOM   2376  CB  LEU A 943      -3.621  -3.777 -28.290  1.00 51.40      A    C  
ATOM   2377  CG  LEU A 943      -3.873  -3.792 -26.777  1.00 48.84      A    C  
ATOM   2378  CD1 LEU A 943      -5.334  -3.584 -26.508  1.00 39.87      A    C  
ATOM   2379  CD2 LEU A 943      -3.410  -5.113 -26.190  1.00 47.50      A    C  
ATOM   2380  N   GLY A 944      -1.969  -3.056 -30.874  1.00 59.64      A    N  
ATOM   2381  CA  GLY A 944      -1.792  -3.143 -32.313  1.00 56.70      A    C  
ATOM   2382  C   GLY A 944      -0.510  -3.915 -32.561  1.00 62.54      A    C  
ATOM   2383  O   GLY A 944      -0.438  -4.771 -33.443  1.00 65.98      A    O  
ATOM   2384  N   CYS A 945       0.505  -3.619 -31.756  1.00 65.46      A    N  
ATOM   2385  CA  CYS A 945       1.789  -4.300 -31.871  1.00 71.45      A    C  
ATOM   2386  C   CYS A 945       1.656  -5.773 -31.489  1.00 72.69      A    C  
ATOM   2387  O   CYS A 945       2.004  -6.651 -32.277  1.00 76.19      A    O  
ATOM   2388  CB  CYS A 945       2.836  -3.608 -30.991  1.00 71.39      A    C  
ATOM   2389  SG  CYS A 945       3.350  -1.976 -31.619  1.00 77.45      A    S  
ATOM   2390  N   GLN A 946       1.154  -6.048 -30.287  1.00 71.07      A    N  
ATOM   2391  CA  GLN A 946       0.974  -7.432 -29.853  1.00 66.73      A    C  
ATOM   2392  C   GLN A 946       0.307  -8.214 -30.979  1.00 63.35      A    C  
ATOM   2393  O   GLN A 946       0.596  -9.392 -31.180  1.00 63.97      A    O  
ATOM   2394  CB  GLN A 946       0.099  -7.507 -28.595  1.00 63.81      A    C  
ATOM   2395  CG  GLN A 946       0.841  -7.413 -27.265  1.00 65.67      A    C  
ATOM   2396  CD  GLN A 946       1.790  -8.581 -27.030  1.00 66.21      A    C  
ATOM   2397  NE2 GLN A 946       1.234  -9.751 -26.708  1.00 68.76      A    N  
ATOM   2398  OE1 GLN A 946       3.008  -8.437 -27.143  1.00 61.19      A    O  
ATOM   2399  N   LEU A 947      -0.588  -7.551 -31.705  1.00 62.07      A    N  
ATOM   2400  CA  LEU A 947      -1.294  -8.181 -32.816  1.00 69.95      A    C  
ATOM   2401  C   LEU A 947      -0.312  -8.437 -33.948  1.00 73.31      A    C  
ATOM   2402  O   LEU A 947      -0.404  -7.724 -34.968  1.00 76.89      A    O  
ATOM   2403  CB  LEU A 947      -2.431  -7.282 -33.323  1.00 63.45      A    C  
ATOM   2404  CG  LEU A 947      -3.879  -7.757 -33.152  1.00 60.05      A    C  
ATOM   2405  CD1 LEU A 947      -4.817  -6.718 -33.746  1.00 58.70      A    C  
ATOM   2406  CD2 LEU A 947      -4.089  -9.111 -33.823  1.00 48.98      A    C  
TER   
END


A second structure was input as follows:


CRYST1   82.367   82.367  146.469  90.00  90.00  90.00 P 43 21 2     8
ATOM      1  N   ARG A 571     -35.299   6.935 -12.502  1.00125.37      A    N  
ANISOU    1  N   ARG A 571    13724  22053  11856  -3004   -225   5546  A    N  
ATOM      2  CA  ARG A 571     -35.095   7.862 -13.673  1.00117.25      A    C  
ANISOU    2  CA  ARG A 571    13026  20399  11126  -2628   -123   4765  A    C  
ATOM      3  C   ARG A 571     -34.056   7.319 -14.666  1.00116.17      A    C  
ANISOU    3  C   ARG A 571    13533  18977  11631  -2821   -404   4468  A    C  
ATOM      4  O   ARG A 571     -32.971   6.909 -14.246  1.00109.54      A    O  
ANISOU    4  O   ARG A 571    13012  17694  10914  -2804   -530   4383  A    O  
ATOM      5  CB  ARG A 571     -34.669   9.257 -13.197  1.00113.08      A    C  
ANISOU    5  CB  ARG A 571    12507  20188  10269  -1839    168   4049  A    C  
ATOM      6  N   TYR A 572     -34.389   7.322 -15.965  1.00110.72      A    N  
ANISOU    6  N   TYR A 572    13009  17758  11301  -2954   -504   4300  A    N  
ATOM      7  CA  TYR A 572     -33.499   6.791 -17.016  1.00102.69      A    C  
ANISOU    7  CA  TYR A 572    12552  15640  10827  -3066   -787   4010  A    C  
ATOM      8  C   TYR A 572     -32.314   7.731 -17.275  1.00 93.79      A    C  
ANISOU    8  C   TYR A 572    11757  14098   9782  -2525   -612   3258  A    C  
ATOM      9  O   TYR A 572     -32.467   8.959 -17.267  1.00 85.07      A    O  
ANISOU    9  O   TYR A 572    10518  13324   8479  -2102   -330   2860  A    O  
ATOM     10  CB  TYR A 572     -34.250   6.526 -18.347  1.00107.80      A    C  
ANISOU   10  CB  TYR A 572    13251  15916  11791  -3326   -963   4052  A    C  
ATOM     11  CG  TYR A 572     -33.329   6.032 -19.458  1.00107.32      A    C  
ANISOU   11  CG  TYR A 572    13741  14831  12205  -3314  -1257   3687  A    C  
ATOM     12  CD1 TYR A 572     -32.826   4.721 -19.444  1.00114.04      A    C  
ANISOU   12  CD1 TYR A 572    14909  15096  13327  -3643  -1733   3964  A    C  
ATOM     13  CD2 TYR A 572     -32.895   6.894 -20.485  1.00107.36      A    C  
ANISOU   13  CD2 TYR A 572    13947  14494  12351  -2921  -1091   3059  A    C  
ATOM     14  CE1 TYR A 572     -31.951   4.269 -20.434  1.00110.75      A    C  
ANISOU   14  CE1 TYR A 572    14982  13835  13265  -3509  -2027   3570  A    C  
ATOM     15  CE2 TYR A 572     -32.016   6.455 -21.479  1.00101.34      A    C  
ANISOU   15  CE2 TYR A 572    13620  12957  11929  -2837  -1339   2735  A    C  
ATOM     16  CZ  TYR A 572     -31.548   5.140 -21.451  1.00108.36      A    C  
ANISOU   16  CZ  TYR A 572    14808  13328  13037  -3089  -1800   2959  A    C  
ATOM     17  OH  TYR A 572     -30.682   4.678 -22.407  1.00 94.78      A    O  
ANISOU   17  OH  TYR A 572    13501  10930  11582  -2905  -2078   2597  A    O  
ATOM     18  N   GLU A 573     -31.145   7.132 -17.513  1.00 86.32      A    N  
ANISOU   18  N   GLU A 573    11237  12433   9128  -2546   -835   3093  A    N  
ATOM     19  CA  GLU A 573     -29.972   7.855 -17.990  1.00 85.97      A    C  
ANISOU   19  CA  GLU A 573    11498  11938   9230  -2135   -740   2471  A    C  
ATOM     20  C   GLU A 573     -29.085   6.936 -18.850  1.00 74.91      A    C  
ANISOU   20  C   GLU A 573    10519   9740   8204  -2236  -1069   2358  A    C  
ATOM     21  O   GLU A 573     -28.860   5.779 -18.489  1.00 74.10      A    O  
ANISOU   21  O   GLU A 573    10569   9394   8192  -2504  -1385   2678  A    O  
ATOM     22  CB  GLU A 573     -29.181   8.421 -16.799  1.00 90.39      A    C  
ANISOU   22  CB  GLU A 573    12032  12779   9531  -1818   -577   2300  A    C  
ATOM     23  CG  GLU A 573     -28.352   9.655 -17.150  1.00 94.53      A    C  
ANISOU   23  CG  GLU A 573    12697  13108  10110  -1375   -424   1703  A    C  
ATOM     24  CD  GLU A 573     -27.618  10.274 -15.964  1.00 98.67      A    C  
ANISOU   24  CD  GLU A 573    13210  13883  10398  -1051   -331   1515  A    C  
ATOM     25  OE1 GLU A 573     -27.410   9.600 -14.930  1.00 95.72      A    O  
ANISOU   25  OE1 GLU A 573    12802  13712   9855  -1145   -382   1792  A    O  
ATOM     26  OE2 GLU A 573     -27.224  11.454 -16.079  1.00102.46      A    O1-
ANISOU   26  OE2 GLU A 573    13730  14325  10874   -703   -253   1093  A    O1-
ATOM     27  N   SER A 574     -28.598   7.464 -19.977  1.00 69.69      A    N  
ANISOU   27  N   SER A 574    10031   8718   7730  -1993  -1025   1913  A    N  
ATOM     28  CA  SER A 574     -27.520   6.840 -20.769  1.00 63.90      A    C  
ANISOU   28  CA  SER A 574     9661   7375   7245  -1889  -1277   1671  A    C  
ATOM     29  C   SER A 574     -26.204   6.718 -19.943  1.00 59.22      A    C  
ANISOU   29  C   SER A 574     9225   6689   6587  -1704  -1295   1545  A    C  
ATOM     30  O   SER A 574     -25.877   7.603 -19.146  1.00 57.50      A    O  
ANISOU   30  O   SER A 574     8871   6793   6185  -1520  -1037   1428  A    O  
ATOM     31  CB  SER A 574     -27.272   7.652 -22.057  1.00 60.24      A    C  
ANISOU   31  CB  SER A 574     9233   6763   6894  -1626  -1147   1260  A    C  
ATOM     32  OG  SER A 574     -27.012   9.009 -21.791  1.00 71.06      A    O  
ANISOU   32  OG  SER A 574    10446   8420   8133  -1381   -829   1021  A    O  
ATOM     33  N   GLN A 575     -25.495   5.606 -20.113  1.00 54.28      A    N  
ANISOU   33  N   GLN A 575     8898   5620   6107  -1731  -1649   1558  A    N  
ATOM     34  CA  GLN A 575     -24.158   5.405 -19.523  1.00 60.19      A    C  
ANISOU   34  CA  GLN A 575     9823   6232   6814  -1518  -1705   1393  A    C  
ATOM     35  C   GLN A 575     -22.988   6.025 -20.312  1.00 48.32      A    C  
ANISOU   35  C   GLN A 575     8395   4614   5348  -1126  -1596    930  A    C  
ATOM     36  O   GLN A 575     -21.919   6.243 -19.753  1.00 50.86      A    O  
ANISOU   36  O   GLN A 575     8757   4973   5596   -935  -1536    787  A    O  
ATOM     37  CB  GLN A 575     -23.898   3.912 -19.293  1.00 66.91      A    C  
ANISOU   37  CB  GLN A 575    10970   6671   7782  -1683  -2195   1612  A    C  
ATOM     38  CG  GLN A 575     -24.926   3.213 -18.400  1.00 79.07      A    C  
ANISOU   38  CG  GLN A 575    12405   8352   9285  -2152  -2370   2200  A    C  
ATOM     39  CD  GLN A 575     -25.052   3.821 -16.994  1.00 90.33      A    C  
ANISOU   39  CD  GLN A 575    13539  10366  10415  -2194  -2029   2416  A    C  
ATOM     40  NE2 GLN A 575     -26.287   3.883 -16.480  1.00 99.95      A    N  
ANISOU   40  NE2 GLN A 575    14434  12063  11482  -2509  -1931   2869  A    N  
ATOM     41  OE1 GLN A 575     -24.053   4.225 -16.375  1.00 86.28      A    O  
ANISOU   41  OE1 GLN A 575    13071   9926   9785  -1921  -1874   2179  A    O  
ATOM     42  N   LEU A 576     -23.179   6.279 -21.591  1.00 45.34      A    N  
ANISOU   42  N   LEU A 576     8011   4145   5070  -1022  -1588    742  A    N  
ATOM     43  CA  LEU A 576     -22.261   7.078 -22.382  1.00 46.91      A    C  
ANISOU   43  CA  LEU A 576     8155   4408   5259   -707  -1429    409  A    C  
ATOM     44  C   LEU A 576     -22.656   8.521 -22.122  1.00 42.85      A    C  
ANISOU   44  C   LEU A 576     7381   4216   4684   -731  -1080    390  A    C  
ATOM     45  O   LEU A 576     -23.830   8.867 -22.256  1.00 48.15      A    O  
ANISOU   45  O   LEU A 576     7925   5011   5357   -887   -981    502  A    O  
ATOM     46  CB  LEU A 576     -22.373   6.726 -23.865  1.00 52.75      A    C  
ANISOU   46  CB  LEU A 576     8973   4981   6089   -567  -1588    247  A    C  
ATOM     47  CG  LEU A 576     -21.351   7.379 -24.791  1.00 59.06      A    C  
ANISOU   47  CG  LEU A 576     9670   5942   6829   -235  -1465    -24  A    C  
ATOM     48  CD1 LEU A 576     -19.920   7.002 -24.418  1.00 61.02      A    C  
ANISOU   48  CD1 LEU A 576     9999   6207   6979     21  -1567   -152  A    C  
ATOM     49  CD2 LEU A 576     -21.634   6.934 -26.210  1.00 66.61      A    C  
ANISOU   49  CD2 LEU A 576    10689   6803   7817    -67  -1639   -168  A    C  
ATOM     50  N   GLN A 577     -21.694   9.322 -21.676  1.00 38.91      A    N  
ANISOU   50  N   GLN A 577     6815   3840   4127   -571   -953    257  A    N  
ATOM     51  CA  GLN A 577     -21.905  10.716 -21.287  1.00 41.37      A    C  
ANISOU   51  CA  GLN A 577     6947   4375   4398   -545   -749    199  A    C  
ATOM     52  C   GLN A 577     -20.800  11.561 -21.899  1.00 41.74      A    C  
ANISOU   52  C   GLN A 577     6926   4424   4508   -389   -729     38  A    C  
ATOM     53  O   GLN A 577     -19.628  11.162 -21.882  1.00 39.65      A    O  
ANISOU   53  O   GLN A 577     6715   4120   4231   -274   -813     -9  A    O  
ATOM     54  CB  GLN A 577     -21.823  10.866 -19.756  1.00 44.64      A    C  
ANISOU   54  CB  GLN A 577     7351   4944   4667   -538   -715    261  A    C  
ATOM     55  CG  GLN A 577     -23.041  10.372 -18.986  1.00 57.60      A    C  
ANISOU   55  CG  GLN A 577     8928   6787   6170   -708   -686    505  A    C  
ATOM     56  CD  GLN A 577     -24.302  11.174 -19.291  1.00 64.17      A    C  
ANISOU   56  CD  GLN A 577     9569   7862   6950   -731   -546    510  A    C  
ATOM     57  NE2 GLN A 577     -25.449  10.494 -19.444  1.00 65.64      A    N  
ANISOU   57  NE2 GLN A 577     9677   8157   7105   -954   -560    766  A    N  
ATOM     58  OE1 GLN A 577     -24.235  12.391 -19.415  1.00 63.23      A    O  
ANISOU   58  OE1 GLN A 577     9379   7815   6832   -557   -473    296  A    O  
ATOM     59  N   MET A 578     -21.171  12.731 -22.411  1.00 40.68      A    N  
ANISOU   59  N   MET A 578     6656   4365   4434   -394   -648    -12  A    N  
ATOM     60  CA  MET A 578     -20.184  13.766 -22.768  1.00 40.74      A    C  
ANISOU   60  CA  MET A 578     6558   4404   4518   -332   -683    -62  A    C  
ATOM     61  C   MET A 578     -19.828  14.554 -21.525  1.00 37.04      A    C  
ANISOU   61  C   MET A 578     6104   3939   4029   -292   -746   -113  A    C  
ATOM     62  O   MET A 578     -20.687  14.784 -20.671  1.00 36.90      A    O  
ANISOU   62  O   MET A 578     6117   3980   3923   -264   -718   -156  A    O  
ATOM     63  CB  MET A 578     -20.725  14.687 -23.855  1.00 44.61      A    C  
ANISOU   63  CB  MET A 578     6924   4920   5107   -382   -655    -56  A    C  
ATOM     64  CG  MET A 578     -19.651  15.535 -24.530  1.00 59.96      A    C  
ANISOU   64  CG  MET A 578     8714   6928   7139   -393   -740     15  A    C  
ATOM     65  SD  MET A 578     -20.160  16.321 -26.080  1.00 64.92      A    S  
ANISOU   65  SD  MET A 578     9177   7627   7861   -472   -723    103  A    S  
ATOM     66  CE  MET A 578     -20.549  14.900 -27.098  1.00 51.89      A    C  
ANISOU   66  CE  MET A 578     7560   6063   6094   -359   -609     58  A    C  
ATOM     67  N   VAL A 579     -18.547  14.922 -21.409  1.00 35.57      A    N  
ANISOU   67  N   VAL A 579     5876   3743   3896   -260   -853   -105  A    N  
ATOM     68  CA  VAL A 579     -18.038  15.714 -20.300  1.00 39.79      A    C  
ANISOU   68  CA  VAL A 579     6443   4230   4444   -209   -994   -169  A    C  
ATOM     69  C   VAL A 579     -17.288  16.938 -20.826  1.00 41.36      A    C  
ANISOU   69  C   VAL A 579     6519   4369   4826   -292  -1193   -101  A    C  
ATOM     70  O   VAL A 579     -16.772  16.932 -21.947  1.00 38.54      A    O  
ANISOU   70  O   VAL A 579     6003   4111   4530   -385  -1176     53  A    O  
ATOM     71  CB  VAL A 579     -17.174  14.872 -19.320  1.00 39.23      A    C  
ANISOU   71  CB  VAL A 579     6462   4177   4267   -131  -1009   -179  A    C  
ATOM     72  CG1 VAL A 579     -17.975  13.659 -18.855  1.00 42.41      A    C  
ANISOU   72  CG1 VAL A 579     6980   4616   4517   -123   -884   -155  A    C  
ATOM     73  CG2 VAL A 579     -15.843  14.431 -19.919  1.00 38.99      A    C  
ANISOU   73  CG2 VAL A 579     6345   4206   4263   -126  -1047    -98  A    C  
ATOM     74  N   GLN A 580     -17.237  17.975 -20.009  1.00 43.79      A    N  
ANISOU   74  N   GLN A 580     6892   4540   5205   -247  -1425   -195  A    N  
ATOM     75  CA  GLN A 580     -16.375  19.138 -20.267  1.00 46.36      A    C  
ANISOU   75  CA  GLN A 580     7135   4730   5750   -378  -1748    -78  A    C  
ATOM     76  C   GLN A 580     -15.449  19.297 -19.087  1.00 44.78      A    C  
ANISOU   76  C   GLN A 580     7014   4443   5556   -306  -1959   -141  A    C  
ATOM     77  O   GLN A 580     -15.894  19.414 -17.960  1.00 43.67      A    O  
ANISOU   77  O   GLN A 580     7044   4236   5311    -96  -2027   -373  A    O  
ATOM     78  CB  GLN A 580     -17.194  20.406 -20.487  1.00 51.33      A    C  
ANISOU   78  CB  GLN A 580     7823   5156   6526   -385  -1997   -152  A    C  
ATOM     79  CG  GLN A 580     -16.350  21.659 -20.757  1.00 55.52      A    C  
ANISOU   79  CG  GLN A 580     8296   5462   7339   -587  -2457     33  A    C  
ATOM     80  CD  GLN A 580     -17.188  22.852 -21.207  1.00 56.82      A    C  
ANISOU   80  CD  GLN A 580     8540   5376   7674   -609  -2759    -16  A    C  
ATOM     81  NE2 GLN A 580     -16.825  24.050 -20.750  1.00 64.06      A    N  
ANISOU   81  NE2 GLN A 580     9584   5938   8817   -636  -3328    -39  A    N  
ATOM     82  OE1 GLN A 580     -18.149  22.698 -21.949  1.00 53.83      A    O  
ANISOU   82  OE1 GLN A 580     8129   5090   7234   -591  -2536    -42  A    O  
ATOM     83  N   VAL A 581     -14.158  19.314 -19.370  1.00 51.22      A    N  
ANISOU   83  N   VAL A 581     7673   5324   6465   -460  -2068     78  A    N  
ATOM     84  CA  VAL A 581     -13.125  19.530 -18.364  1.00 60.71      A    C  
ANISOU   84  CA  VAL A 581     8917   6439   7709   -435  -2312     61  A    C  
ATOM     85  C   VAL A 581     -13.112  21.028 -17.973  1.00 68.02      A    C  
ANISOU   85  C   VAL A 581     9944   7018   8884   -493  -2833     26  A    C  
ATOM     86  O   VAL A 581     -13.261  21.890 -18.844  1.00 59.77      A    O  
ANISOU   86  O   VAL A 581     8808   5860   8042   -701  -3049    210  A    O  
ATOM     87  CB  VAL A 581     -11.764  19.001 -18.896  1.00 70.13      A    C  
ANISOU   87  CB  VAL A 581     9851   7907   8887   -575  -2252    340  A    C  
ATOM     88  CG1 VAL A 581     -10.611  19.393 -17.999  1.00 76.12      A    C  
ANISOU   88  CG1 VAL A 581    10603   8583   9738   -615  -2561    389  A    C  
ATOM     89  CG2 VAL A 581     -11.825  17.473 -19.037  1.00 66.36      A    C  
ANISOU   89  CG2 VAL A 581     9388   7677   8150   -395  -1857    253  A    C  
ATOM     90  N   THR A 582     -12.977  21.301 -16.666  1.00 69.39      A    N  
ANISOU   90  N   THR A 582    10323   7014   9028   -282  -3073   -222  A    N  
ATOM     91  CA  THR A 582     -12.984  22.664 -16.078  1.00 73.54      A    C  
ANISOU   91  CA  THR A 582    11032   7144   9765   -218  -3680   -367  A    C  
ATOM     92  C   THR A 582     -11.731  22.956 -15.222  1.00 81.10      A    C  
ANISOU   92  C   THR A 582    12024   7945  10847   -257  -4065   -330  A    C  
ATOM     93  O   THR A 582     -11.711  23.913 -14.434  1.00 81.05      A    O  
ANISOU   93  O   THR A 582    12242   7583  10971    -99  -4615   -546  A    O  
ATOM     94  CB  THR A 582     -14.245  22.882 -15.196  1.00 73.47      A    C  
ANISOU   94  CB  THR A 582    11280   7090   9545    227  -3703   -819  A    C  
ATOM     95  CG2 THR A 582     -15.500  22.790 -16.028  1.00 72.25      A    C  
ANISOU   95  CG2 THR A 582    11082   7065   9306    246  -3417   -842  A    C  
ATOM     96  OG1 THR A 582     -14.288  21.908 -14.135  1.00 68.07      A    O  
ANISOU   96  OG1 THR A 582    10651   6672   8540    496  -3389  -1002  A    O  
ATOM     97  N   GLY A 583     -10.678  22.161 -15.409  1.00 78.83      A    N  
ANISOU   97  N   GLY A 583    11518   7919  10516   -437  -3831    -72  A    N  
ATOM     98  CA  GLY A 583      -9.495  22.188 -14.547  1.00 72.90      A    C  
ANISOU   98  CA  GLY A 583    10771   7108   9822   -449  -4095    -43  A    C  
ATOM     99  C   GLY A 583      -8.687  20.914 -14.714  1.00 71.16      A    C  
ANISOU   99  C   GLY A 583    10335   7301   9399   -486  -3646    120  A    C  
ATOM    100  O   GLY A 583      -9.117  19.997 -15.402  1.00 63.58      A    O  
ANISOU  100  O   GLY A 583     9280   6624   8252   -453  -3177    154  A    O  
ATOM    101  N   SER A 584      -7.538  20.858 -14.048  1.00 70.09      A    N  
ANISOU  101  N   SER A 584    10152   7178   9301   -516  -3844    186  A    N  
ATOM    102  CA  SER A 584      -6.545  19.790 -14.225  1.00 70.55      A    C  
ANISOU  102  CA  SER A 584     9981   7638   9188   -540  -3534    357  A    C  
ATOM    103  C   SER A 584      -6.761  18.531 -13.348  1.00 66.94      A    C  
ANISOU  103  C   SER A 584     9725   7289   8418   -192  -3168     50  A    C  
ATOM    104  O   SER A 584      -6.296  17.455 -13.728  1.00 65.45      A    O  
ANISOU  104  O   SER A 584     9403   7418   8048   -143  -2856    130  A    O  
ATOM    105  CB  SER A 584      -5.128  20.369 -13.987  1.00 76.47      A    C  
ANISOU  105  CB  SER A 584    10527   8394  10134   -779  -3957    638  A    C  
ATOM    106  OG  SER A 584      -4.908  20.726 -12.620  1.00 77.02      A    O  
ANISOU  106  OG  SER A 584    10874   8129  10263   -605  -4301    367  A    O  
ATOM    107  N   SER A 585      -7.404  18.675 -12.177  1.00 64.14      A    N  
ANISOU  107  N   SER A 585     9678   6707   7986     67  -3257   -281  A    N  
ATOM    108  CA  SER A 585      -7.737  17.530 -11.298  1.00 66.25      A    C  
ANISOU  108  CA  SER A 585    10121   7104   7947    353  -2940   -498  A    C  
ATOM    109  C   SER A 585      -8.912  16.665 -11.846  1.00 63.10      A    C  
ANISOU  109  C   SER A 585     9758   6853   7365    404  -2517   -519  A    C  
ATOM    110  O   SER A 585      -9.835  17.180 -12.496  1.00 55.03      A    O  
ANISOU  110  O   SER A 585     8722   5774   6412    340  -2493   -517  A    O  
ATOM    111  CB  SER A 585      -8.058  17.988  -9.863  1.00 69.52      A    C  
ANISOU  111  CB  SER A 585    10788   7356   8271    641  -3174   -804  A    C  
ATOM    112  OG  SER A 585      -6.895  18.413  -9.178  1.00 84.73      A    O  
ANISOU  112  OG  SER A 585    12722   9155  10317    639  -3536   -812  A    O  
ATOM    113  N   ASP A 586      -8.871  15.366 -11.532  1.00 61.01      A    N  
ANISOU  113  N   ASP A 586     9557   6742   6881    514  -2248   -533  A    N  
ATOM    114  CA  ASP A 586      -9.879  14.375 -11.985  1.00 54.85      A    C  
ANISOU  114  CA  ASP A 586     8830   6061   5950    525  -1931   -505  A    C  
ATOM    115  C   ASP A 586     -11.330  14.768 -11.703  1.00 50.53      A    C  
ANISOU  115  C   ASP A 586     8369   5509   5322    588  -1862   -603  A    C  
ATOM    116  O   ASP A 586     -12.184  14.495 -12.535  1.00 45.54      A    O  
ANISOU  116  O   ASP A 586     7697   4918   4690    495  -1686   -530  A    O  
ATOM    117  CB  ASP A 586      -9.634  12.997 -11.346  1.00 57.26      A    C  
ANISOU  117  CB  ASP A 586     9263   6441   6053    637  -1802   -503  A    C  
ATOM    118  CG  ASP A 586      -8.405  12.292 -11.891  1.00 63.22      A    C  
ANISOU  118  CG  ASP A 586     9930   7269   6820    644  -1819   -431  A    C  
ATOM    119  OD1 ASP A 586      -7.656  12.889 -12.683  1.00 63.30      A    O  
ANISOU  119  OD1 ASP A 586     9723   7366   6962    556  -1904   -345  A    O  
ATOM    120  OD2 ASP A 586      -8.184  11.126 -11.501  1.00 58.62      A    O1-
ANISOU  120  OD2 ASP A 586     9484   6695   6092    752  -1778   -443  A    O1-
ATOM    121  N   ASN A 587     -11.596  15.406 -10.552  1.00 50.26      A    N  
ANISOU  121  N   ASN A 587     8436   5472   5190    787  -2018   -781  A    N  
ATOM    122  CA  ASN A 587     -12.964  15.836 -10.209  1.00 52.29      A    C  
ANISOU  122  CA  ASN A 587     8727   5852   5288    943  -1970   -902  A    C  
ATOM    123  C   ASN A 587     -13.447  17.130 -10.893  1.00 51.88      A    C  
ANISOU  123  C   ASN A 587     8644   5640   5429    928  -2172  -1000  A    C  
ATOM    124  O   ASN A 587     -14.611  17.485 -10.714  1.00 54.92      A    O  
ANISOU  124  O   ASN A 587     9040   6166   5661   1097  -2134  -1123  A    O  
ATOM    125  CB  ASN A 587     -13.233  15.838  -8.687  1.00 55.34      A    C  
ANISOU  125  CB  ASN A 587     9205   6450   5371   1266  -2025  -1068  A    C  
ATOM    126  CG  ASN A 587     -12.386  16.842  -7.907  1.00 61.55      A    C  
ANISOU  126  CG  ASN A 587    10090   7058   6239   1476  -2427  -1304  A    C  
ATOM    127  ND2 ASN A 587     -12.477  16.763  -6.591  1.00 69.77      A    N  
ANISOU  127  ND2 ASN A 587    11207   8317   6985   1801  -2481  -1463  A    N  
ATOM    128  OD1 ASN A 587     -11.655  17.658  -8.464  1.00 61.83      A    O  
ANISOU  128  OD1 ASN A 587    10122   6782   6589   1339  -2717  -1314  A    O  
ATOM    129  N   GLU A 588     -12.594  17.792 -11.692  1.00 54.69      A    N  
ANISOU  129  N   GLU A 588     8934   5751   6094    720  -2396   -909  A    N  
ATOM    130  CA  GLU A 588     -12.928  19.075 -12.345  1.00 57.06      A    C  
ANISOU  130  CA  GLU A 588     9223   5831   6626    655  -2689   -948  A    C  
ATOM    131  C   GLU A 588     -13.455  18.820 -13.756  1.00 52.24      A    C  
ANISOU  131  C   GLU A 588     8468   5279   6101    414  -2435   -747  A    C  
ATOM    132  O   GLU A 588     -12.722  18.855 -14.750  1.00 51.71      A    O  
ANISOU  132  O   GLU A 588     8242   5184   6224    149  -2452   -507  A    O  
ATOM    133  CB  GLU A 588     -11.736  20.052 -12.317  1.00 62.51      A    C  
ANISOU  133  CB  GLU A 588     9908   6227   7616    520  -3177   -887  A    C  
ATOM    134  CG  GLU A 588     -11.402  20.529 -10.902  1.00 69.97      A    C  
ANISOU  134  CG  GLU A 588    11048   7045   8492    825  -3537  -1166  A    C  
ATOM    135  CD  GLU A 588     -10.099  21.329 -10.797  1.00 80.03      A    C  
ANISOU  135  CD  GLU A 588    12314   8010  10084    640  -4061  -1056  A    C  
ATOM    136  OE1 GLU A 588      -9.049  20.874 -11.304  1.00 83.65      A    O  
ANISOU  136  OE1 GLU A 588    12568   8562  10652    340  -3960   -745  A    O  
ATOM    137  OE2 GLU A 588     -10.115  22.414 -10.182  1.00 87.27      A    O1-
ANISOU  137  OE2 GLU A 588    13423   8609  11127    819  -4621  -1283  A    O1-
ATOM    138  N   TYR A 589     -14.747  18.513 -13.796  1.00 46.55      A    N  
ANISOU  138  N   TYR A 589     7773   4717   5196    531  -2193   -833  A    N  
ATOM    139  CA  TYR A 589     -15.502  18.333 -15.018  1.00 43.10      A    C  
ANISOU  139  CA  TYR A 589     7234   4329   4813    363  -1977   -704  A    C  
ATOM    140  C   TYR A 589     -16.973  18.390 -14.666  1.00 42.79      A    C  
ANISOU  140  C   TYR A 589     7234   4464   4558    566  -1851   -860  A    C  
ATOM    141  O   TYR A 589     -17.334  18.261 -13.504  1.00 45.41      A    O  
ANISOU  141  O   TYR A 589     7628   4987   4639    824  -1845  -1008  A    O  
ATOM    142  CB  TYR A 589     -15.175  16.984 -15.711  1.00 43.01      A    C  
ANISOU  142  CB  TYR A 589     7133   4454   4754    197  -1656   -498  A    C  
ATOM    143  CG  TYR A 589     -15.705  15.775 -14.964  1.00 42.81      A    C  
ANISOU  143  CG  TYR A 589     7186   4606   4473    294  -1420   -506  A    C  
ATOM    144  CD1 TYR A 589     -14.966  15.203 -13.920  1.00 44.97      A    C  
ANISOU  144  CD1 TYR A 589     7540   4918   4628    390  -1449   -525  A    C  
ATOM    145  CD2 TYR A 589     -16.970  15.235 -15.253  1.00 41.06      A    C  
ANISOU  145  CD2 TYR A 589     6949   4520   4131    263  -1208   -453  A    C  
ATOM    146  CE1 TYR A 589     -15.460  14.109 -13.194  1.00 43.74      A    C  
ANISOU  146  CE1 TYR A 589     7449   4926   4243    434  -1286   -460  A    C  
ATOM    147  CE2 TYR A 589     -17.472  14.148 -14.541  1.00 44.92      A    C  
ANISOU  147  CE2 TYR A 589     7482   5182   4405    276  -1062   -360  A    C  
ATOM    148  CZ  TYR A 589     -16.718  13.590 -13.512  1.00 44.53      A    C  
ANISOU  148  CZ  TYR A 589     7514   5163   4241    353  -1108   -349  A    C  
ATOM    149  OH  TYR A 589     -17.214  12.531 -12.830  1.00 49.25      A    O  
ANISOU  149  OH  TYR A 589     8144   5930   4639    317  -1009   -187  A    O  
ATOM    150  N   PHE A 590     -17.815  18.555 -15.675  1.00 42.59      A    N  
ANISOU  150  N   PHE A 590     7138   4448   4597    461  -1742   -804  A    N  
ATOM    151  CA  PHE A 590     -19.257  18.373 -15.520  1.00 41.66      A    C  
ANISOU  151  CA  PHE A 590     6989   4592   4250    603  -1551   -877  A    C  
ATOM    152  C   PHE A 590     -19.766  17.626 -16.718  1.00 41.16      A    C  
ANISOU  152  C   PHE A 590     6825   4564   4248    351  -1279   -672  A    C  
ATOM    153  O   PHE A 590     -19.063  17.527 -17.737  1.00 44.00      A    O  
ANISOU  153  O   PHE A 590     7144   4754   4818    142  -1284   -536  A    O  
ATOM    154  CB  PHE A 590     -19.977  19.719 -15.318  1.00 48.38      A    C  
ANISOU  154  CB  PHE A 590     7894   5404   5086    875  -1835  -1144  A    C  
ATOM    155  CG  PHE A 590     -19.826  20.693 -16.467  1.00 45.85      A    C  
ANISOU  155  CG  PHE A 590     7586   4741   5094    704  -2078  -1113  A    C  
ATOM    156  CD1 PHE A 590     -18.701  21.512 -16.569  1.00 47.15      A    C  
ANISOU  156  CD1 PHE A 590     7821   4547   5545    592  -2478  -1082  A    C  
ATOM    157  CD2 PHE A 590     -20.814  20.802 -17.434  1.00 46.53      A    C  
ANISOU  157  CD2 PHE A 590     7594   4880   5204    629  -1940  -1071  A    C  
ATOM    158  CE1 PHE A 590     -18.561  22.414 -17.621  1.00 46.12      A    C  
ANISOU  158  CE1 PHE A 590     7671   4134   5719    376  -2744   -959  A    C  
ATOM    159  CE2 PHE A 590     -20.681  21.709 -18.491  1.00 49.79      A    C  
ANISOU  159  CE2 PHE A 590     8011   4997   5910    459  -2180  -1004  A    C  
ATOM    160  CZ  PHE A 590     -19.547  22.509 -18.584  1.00 44.97      A    C  
ANISOU  160  CZ  PHE A 590     7458   4047   5581    317  -2587   -923  A    C  
ATOM    161  N   TYR A 591     -20.980  17.103 -16.587  1.00 41.40      A    N  
ANISOU  161  N   TYR A 591     6791   4868   4071    388  -1068   -634  A    N  
ATOM    162  CA  TYR A 591     -21.631  16.320 -17.619  1.00 42.73      A    C  
ANISOU  162  CA  TYR A 591     6885   5064   4284    165   -857   -451  A    C  
ATOM    163  C   TYR A 591     -22.426  17.274 -18.517  1.00 46.51      A    C  
ANISOU  163  C   TYR A 591     7309   5497   4866    181   -902   -539  A    C  
ATOM    164  O   TYR A 591     -23.148  18.136 -18.005  1.00 49.75      A    O  
ANISOU  164  O   TYR A 591     7705   6048   5149    419  -1002   -723  A    O  
ATOM    165  CB  TYR A 591     -22.583  15.272 -16.998  1.00 45.07      A    C  
ANISOU  165  CB  TYR A 591     7112   5686   4325    128   -668   -286  A    C  
ATOM    166  CG  TYR A 591     -21.886  14.200 -16.194  1.00 46.77      A    C  
ANISOU  166  CG  TYR A 591     7399   5918   4454     66   -653   -143  A    C  
ATOM    167  CD1 TYR A 591     -21.100  13.235 -16.828  1.00 46.67      A    C  
ANISOU  167  CD1 TYR A 591     7485   5641   4604   -115   -669    -26  A    C  
ATOM    168  CD2 TYR A 591     -22.000  14.141 -14.799  1.00 57.03      A    C  
ANISOU  168  CD2 TYR A 591     8666   7525   5477    235   -651   -138  A    C  
ATOM    169  CE1 TYR A 591     -20.442  12.245 -16.106  1.00 48.30      A    C  
ANISOU  169  CE1 TYR A 591     7791   5819   4742   -148   -711     85  A    C  
ATOM    170  CE2 TYR A 591     -21.346  13.145 -14.063  1.00 58.99      A    C  
ANISOU  170  CE2 TYR A 591     8989   7771   5652    161   -659     19  A    C  
ATOM    171  CZ  TYR A 591     -20.584  12.187 -14.732  1.00 52.46      A    C  
ANISOU  171  CZ  TYR A 591     8294   6609   5030    -46   -701    132  A    C  
ATOM    172  OH  TYR A 591     -19.922  11.206 -14.051  1.00 54.43      A    O  
ANISOU  172  OH  TYR A 591     8650   6807   5222    -96   -764    263  A    O  
ATOM    173  N   VAL A 592     -22.294  17.107 -19.834  1.00 43.38      A    N  
ANISOU  173  N   VAL A 592     6880   4938   4665    -20   -851   -428  A    N  
ATOM    174  CA  VAL A 592     -23.091  17.850 -20.833  1.00 47.15      A    C  
ANISOU  174  CA  VAL A 592     7300   5373   5244    -46   -869   -465  A    C  
ATOM    175  C   VAL A 592     -24.494  17.237 -21.038  1.00 49.64      A    C  
ANISOU  175  C   VAL A 592     7529   5923   5410    -77   -661   -405  A    C  
ATOM    176  O   VAL A 592     -24.628  16.120 -21.531  1.00 53.38      A    O  
ANISOU  176  O   VAL A 592     7988   6402   5894   -253   -525   -237  A    O  
ATOM    177  CB  VAL A 592     -22.370  17.908 -22.190  1.00 48.38      A    C  
ANISOU  177  CB  VAL A 592     7411   5347   5623   -234   -893   -336  A    C  
ATOM    178  CG1 VAL A 592     -23.215  18.595 -23.275  1.00 46.44      A    C  
ANISOU  178  CG1 VAL A 592     7104   5068   5475   -279   -904   -341  A    C  
ATOM    179  CG2 VAL A 592     -21.002  18.575 -22.034  1.00 46.68      A    C  
ANISOU  179  CG2 VAL A 592     7206   4976   5553   -264  -1124   -304  A    C  
ATOM    180  N   ASP A 593     -25.517  18.003 -20.655  1.00 54.78      A    N  
ANISOU  180  N   ASP A 593     8124   6771   5919    119   -694   -549  A    N  
ATOM    181  CA  ASP A 593     -26.943  17.715 -20.891  1.00 53.88      A    C  
ANISOU  181  CA  ASP A 593     7866   6953   5651    109   -529   -487  A    C  
ATOM    182  C   ASP A 593     -27.380  18.375 -22.246  1.00 52.12      A    C  
ANISOU  182  C   ASP A 593     7634   6543   5625     46   -568   -538  A    C  
ATOM    183  O   ASP A 593     -27.325  19.607 -22.427  1.00 58.94      A    O  
ANISOU  183  O   ASP A 593     8557   7257   6580    205   -781   -727  A    O  
ATOM    184  CB  ASP A 593     -27.770  18.263 -19.702  1.00 66.53      A    C  
ANISOU  184  CB  ASP A 593     9366   8995   6916    451   -556   -644  A    C  
ATOM    185  CG  ASP A 593     -29.037  17.458 -19.418  1.00 75.21      A    C  
ANISOU  185  CG  ASP A 593    10227  10614   7736    385   -330   -424  A    C  
ATOM    186  OD1 ASP A 593     -29.718  17.048 -20.371  1.00 87.50      A    O  
ANISOU  186  OD1 ASP A 593    11707  12143   9395    157   -227   -270  A    O  
ATOM    187  OD2 ASP A 593     -29.355  17.243 -18.228  1.00 80.67      A    O1-
ANISOU  187  OD2 ASP A 593    10780  11780   8089    557   -277   -374  A    O1-
ATOM    188  N   PHE A 594     -27.810  17.538 -23.184  1.00 50.54      A    N  
ANISOU  188  N   PHE A 594     7379   6327   5497   -183   -417   -362  A    N  
ATOM    189  CA  PHE A 594     -28.340  17.970 -24.486  1.00 47.10      A    C  
ANISOU  189  CA  PHE A 594     6912   5777   5208   -248   -416   -379  A    C  
ATOM    190  C   PHE A 594     -29.831  18.335 -24.479  1.00 39.81      A    C  
ANISOU  190  C   PHE A 594     5854   5146   4128   -137   -355   -441  A    C  
ATOM    191  O   PHE A 594     -30.383  18.617 -25.524  1.00 44.13      A    O  
ANISOU  191  O   PHE A 594     6370   5619   4779   -191   -345   -451  A    O  
ATOM    192  CB  PHE A 594     -28.122  16.872 -25.505  1.00 54.78      A    C  
ANISOU  192  CB  PHE A 594     7898   6614   6302   -476   -327   -207  A    C  
ATOM    193  CG  PHE A 594     -26.706  16.678 -25.884  1.00 54.31      A    C  
ANISOU  193  CG  PHE A 594     7920   6344   6372   -517   -394   -176  A    C  
ATOM    194  CD1 PHE A 594     -25.879  15.848 -25.119  1.00 53.09      A    C  
ANISOU  194  CD1 PHE A 594     7839   6170   6164   -530   -401   -120  A    C  
ATOM    195  CD2 PHE A 594     -26.206  17.265 -27.056  1.00 51.86      A    C  
ANISOU  195  CD2 PHE A 594     7579   5918   6207   -541   -451   -166  A    C  
ATOM    196  CE1 PHE A 594     -24.561  15.640 -25.503  1.00 56.39      A    C  
ANISOU  196  CE1 PHE A 594     8294   6473   6660   -527   -462    -96  A    C  
ATOM    197  CE2 PHE A 594     -24.896  17.050 -27.447  1.00 53.66      A    C  
ANISOU  197  CE2 PHE A 594     7799   6098   6490   -560   -498    -89  A    C  
ATOM    198  CZ  PHE A 594     -24.071  16.245 -26.667  1.00 57.82      A    C  
ANISOU  198  CZ  PHE A 594     8395   6624   6951   -535   -501    -73  A    C  
ATOM    199  N   ARG A 595     -30.462  18.346 -23.314  1.00 39.59      A    N  
ANISOU  199  N   ARG A 595     5717   5510   3816     44   -315   -476  A    N  
ATOM    200  CA  ARG A 595     -31.860  18.635 -23.165  1.00 45.99      A    C  
ANISOU  200  CA  ARG A 595     6330   6754   4390    200   -245   -515  A    C  
ATOM    201  C   ARG A 595     -32.306  19.970 -23.758  1.00 45.38      A    C  
ANISOU  201  C   ARG A 595     6298   6573   4373    449   -411   -797  A    C  
ATOM    202  O   ARG A 595     -33.410  20.041 -24.321  1.00 47.12      A    O  
ANISOU  202  O   ARG A 595     6375   7001   4526    456   -331   -784  A    O  
ATOM    203  CB  ARG A 595     -32.211  18.554 -21.686  1.00 49.79      A    C  
ANISOU  203  CB  ARG A 595     6655   7777   4485    445   -204   -520  A    C  
ATOM    204  CG  ARG A 595     -33.654  18.755 -21.313  1.00 60.90      A    C  
ANISOU  204  CG  ARG A 595     7760   9854   5525    663   -108   -515  A    C  
ATOM    205  CD  ARG A 595     -33.952  18.135 -19.945  1.00 77.01      A    C  
ANISOU  205  CD  ARG A 595     9552  12558   7150    749     13   -309  A    C  
ATOM    206  NE  ARG A 595     -32.913  18.332 -18.916  1.00 83.59      A    N  
ANISOU  206  NE  ARG A 595    10539  13313   7908    964    -97   -462  A    N  
ATOM    207  CZ  ARG A 595     -32.970  17.843 -17.669  1.00 91.33      A    C  
ANISOU  207  CZ  ARG A 595    11332  14847   8522   1069    -13   -297  A    C  
ATOM    208  NH1 ARG A 595     -34.027  17.140 -17.229  1.00 87.41      A    N1+
ANISOU  208  NH1 ARG A 595    10443  15096   7674    959    178     82  A    N1+
ATOM    209  NH2 ARG A 595     -31.957  18.081 -16.833  1.00 90.80      A    N  
ANISOU  209  NH2 ARG A 595    11445  14629   8426   1277   -140   -478  A    N  
ATOM    210  N   GLU A 596     -31.450  20.994 -23.620  1.00 41.99      A    N  
ANISOU  210  N   GLU A 596     6068   5804   4081    629   -686  -1025  A    N  
ATOM    211  CA  GLU A 596     -31.716  22.343 -24.144  1.00 41.89      A    C  
ANISOU  211  CA  GLU A 596     6166   5570   4182    849   -976  -1279  A    C  
ATOM    212  C   GLU A 596     -31.306  22.537 -25.608  1.00 39.47      A    C  
ANISOU  212  C   GLU A 596     5939   4825   4231    540  -1023  -1140  A    C  
ATOM    213  O   GLU A 596     -31.609  23.559 -26.147  1.00 39.74      A    O  
ANISOU  213  O   GLU A 596     6051   4673   4376    656  -1265  -1280  A    O  
ATOM    214  CB  GLU A 596     -31.051  23.425 -23.290  1.00 41.84      A    C  
ANISOU  214  CB  GLU A 596     6356   5360   4181   1181  -1380  -1565  A    C  
ATOM    215  CG  GLU A 596     -31.317  23.343 -21.794  1.00 43.73      A    C  
ANISOU  215  CG  GLU A 596     6524   6066   4024   1580  -1380  -1749  A    C  
ATOM    216  CD  GLU A 596     -32.754  23.541 -21.399  1.00 46.45      A    C  
ANISOU  216  CD  GLU A 596     6655   7037   3955   1981  -1301  -1925  A    C  
ATOM    217  OE1 GLU A 596     -33.641  23.852 -22.235  1.00 49.77      A    O  
ANISOU  217  OE1 GLU A 596     7006   7504   4400   1993  -1281  -1959  A    O  
ATOM    218  OE2 GLU A 596     -32.999  23.401 -20.198  1.00 50.95      A    O1-
ANISOU  218  OE2 GLU A 596     7099   8129   4132   2324  -1263  -2029  A    O1-
ATOM    219  N   TYR A 597     -30.615  21.575 -26.212  1.00 36.67      A    N  
ANISOU  219  N   TYR A 597     5563   4345   4024    194   -829   -875  A    N  
ATOM    220  CA  TYR A 597     -30.205  21.620 -27.620  1.00 40.57      A    C  
ANISOU  220  CA  TYR A 597     6071   4575   4770    -53   -833   -718  A    C  
ATOM    221  C   TYR A 597     -31.334  21.085 -28.501  1.00 40.28      A    C  
ANISOU  221  C   TYR A 597     5914   4702   4687   -133   -624   -659  A    C  
ATOM    222  O   TYR A 597     -32.223  20.375 -28.021  1.00 37.28      A    O  
ANISOU  222  O   TYR A 597     5423   4627   4114   -108   -448   -643  A    O  
ATOM    223  CB  TYR A 597     -28.920  20.801 -27.846  1.00 38.23      A    C  
ANISOU  223  CB  TYR A 597     5787   4162   4578   -276   -750   -512  A    C  
ATOM    224  CG  TYR A 597     -27.682  21.438 -27.246  1.00 37.12      A    C  
ANISOU  224  CG  TYR A 597     5738   3826   4540   -261   -993   -513  A    C  
ATOM    225  CD1 TYR A 597     -27.466  21.428 -25.867  1.00 38.60      A    C  
ANISOU  225  CD1 TYR A 597     5995   4075   4598    -92  -1058   -646  A    C  
ATOM    226  CD2 TYR A 597     -26.707  22.048 -28.060  1.00 39.04      A    C  
ANISOU  226  CD2 TYR A 597     5969   3867   4998   -430  -1179   -340  A    C  
ATOM    227  CE1 TYR A 597     -26.337  22.022 -25.297  1.00 40.85      A    C  
ANISOU  227  CE1 TYR A 597     6377   4152   4994    -79  -1327   -656  A    C  
ATOM    228  CE2 TYR A 597     -25.557  22.648 -27.501  1.00 41.16      A    C  
ANISOU  228  CE2 TYR A 597     6297   3958   5386   -472  -1455   -282  A    C  
ATOM    229  CZ  TYR A 597     -25.378  22.623 -26.118  1.00 42.91      A    C  
ANISOU  229  CZ  TYR A 597     6627   4170   5505   -292  -1538   -464  A    C  
ATOM    230  OH  TYR A 597     -24.266  23.185 -25.530  1.00 46.66      A    O  
ANISOU  230  OH  TYR A 597     7173   4447   6107   -327  -1844   -422  A    O  
ATOM    231  N   GLU A 598     -31.314  21.469 -29.771  1.00 39.34      A    N  
ANISOU  231  N   GLU A 598     5796   4412   4738   -241   -672   -595  A    N  
ATOM    232  CA  GLU A 598     -32.351  21.034 -30.721  1.00 41.42      A    C  
ANISOU  232  CA  GLU A 598     5963   4792   4983   -307   -514   -557  A    C  
ATOM    233  C   GLU A 598     -31.901  19.813 -31.519  1.00 36.34      A    C  
ANISOU  233  C   GLU A 598     5295   4120   4392   -505   -359   -378  A    C  
ATOM    234  O   GLU A 598     -30.754  19.711 -31.928  1.00 37.81      A    O  
ANISOU  234  O   GLU A 598     5511   4190   4665   -572   -398   -280  A    O  
ATOM    235  CB  GLU A 598     -32.820  22.165 -31.646  1.00 38.66      A    C  
ANISOU  235  CB  GLU A 598     5628   4316   4744   -249   -675   -625  A    C  
ATOM    236  CG  GLU A 598     -33.301  23.446 -30.936  1.00 43.96      A    C  
ANISOU  236  CG  GLU A 598     6380   4954   5369     30   -948   -870  A    C  
ATOM    237  CD  GLU A 598     -34.454  23.262 -29.951  1.00 44.94      A    C  
ANISOU  237  CD  GLU A 598     6404   5471   5202    292   -844  -1059  A    C  
ATOM    238  OE1 GLU A 598     -35.279  22.343 -30.151  1.00 46.12      A    O  
ANISOU  238  OE1 GLU A 598     6387   5908   5230    194   -578   -956  A    O  
ATOM    239  OE2 GLU A 598     -34.528  24.034 -28.960  1.00 57.46      A    O1-
ANISOU  239  OE2 GLU A 598     8057   7115   6658    611  -1065  -1295  A    O1-
ATOM    240  N   TYR A 599     -32.847  18.905 -31.723  1.00 34.85      A    N  
ANISOU  240  N   TYR A 599     5041   4067   4133   -570   -229   -340  A    N  
ATOM    241  CA  TYR A 599     -32.651  17.663 -32.466  1.00 36.10      A    C  
ANISOU  241  CA  TYR A 599     5222   4157   4336   -698   -182   -229  A    C  
ATOM    242  C   TYR A 599     -32.679  17.957 -33.960  1.00 35.09      A    C  
ANISOU  242  C   TYR A 599     5076   3958   4298   -681   -203   -238  A    C  
ATOM    243  O   TYR A 599     -33.605  18.619 -34.434  1.00 36.85      A    O  
ANISOU  243  O   TYR A 599     5241   4227   4534   -652   -200   -293  A    O  
ATOM    244  CB  TYR A 599     -33.757  16.679 -32.102  1.00 38.58      A    C  
ANISOU  244  CB  TYR A 599     5476   4606   4577   -817   -139   -142  A    C  
ATOM    245  CG  TYR A 599     -33.969  15.518 -33.041  1.00 38.87      A    C  
ANISOU  245  CG  TYR A 599     5568   4505   4697   -932   -210    -67  A    C  
ATOM    246  CD1 TYR A 599     -32.990  14.541 -33.214  1.00 38.48      A    C  
ANISOU  246  CD1 TYR A 599     5663   4268   4691   -931   -318    -47  A    C  
ATOM    247  CD2 TYR A 599     -35.183  15.372 -33.735  1.00 39.60      A    C  
ANISOU  247  CD2 TYR A 599     5580   4653   4815  -1005   -223    -42  A    C  
ATOM    248  CE1 TYR A 599     -33.196  13.457 -34.074  1.00 37.75      A    C  
ANISOU  248  CE1 TYR A 599     5670   4007   4668   -958   -488    -40  A    C  
ATOM    249  CE2 TYR A 599     -35.402  14.294 -34.579  1.00 39.75      A    C  
ANISOU  249  CE2 TYR A 599     5684   4494   4927  -1089   -375      1  A    C  
ATOM    250  CZ  TYR A 599     -34.408  13.334 -34.746  1.00 37.67      A    C  
ANISOU  250  CZ  TYR A 599     5601   4005   4708  -1047   -534    -15  A    C  
ATOM    251  OH  TYR A 599     -34.625  12.270 -35.575  1.00 37.86      A    O  
ANISOU  251  OH  TYR A 599     5756   3812   4818  -1055   -782    -31  A    O  
ATOM    252  N   ASP A 600     -31.673  17.449 -34.672  1.00 32.44      A    N  
ANISOU  252  N   ASP A 600     4773   3570   3984   -659   -229   -189  A    N  
ATOM    253  CA  ASP A 600     -31.503  17.671 -36.086  1.00 33.96      A    C  
ANISOU  253  CA  ASP A 600     4906   3803   4192   -597   -244   -169  A    C  
ATOM    254  C   ASP A 600     -32.417  16.680 -36.830  1.00 36.30      A    C  
ANISOU  254  C   ASP A 600     5237   4074   4479   -581   -260   -230  A    C  
ATOM    255  O   ASP A 600     -32.177  15.460 -36.799  1.00 35.28      A    O  
ANISOU  255  O   ASP A 600     5207   3871   4326   -551   -343   -253  A    O  
ATOM    256  CB  ASP A 600     -30.035  17.533 -36.488  1.00 31.15      A    C  
ANISOU  256  CB  ASP A 600     4507   3547   3783   -516   -271    -82  A    C  
ATOM    257  CG  ASP A 600     -29.791  17.850 -37.946  1.00 34.39      A    C  
ANISOU  257  CG  ASP A 600     4782   4147   4139   -423   -275     -7  A    C  
ATOM    258  OD1 ASP A 600     -30.723  17.801 -38.788  1.00 36.66      A    O  
ANISOU  258  OD1 ASP A 600     5063   4435   4430   -386   -265    -70  A    O  
ATOM    259  OD2 ASP A 600     -28.651  18.169 -38.275  1.00 41.66      A    O1-
ANISOU  259  OD2 ASP A 600     5567   5272   4989   -387   -291    148  A    O1-
ATOM    260  N   LEU A 601     -33.413  17.232 -37.534  1.00 33.63      A    N  
ANISOU  260  N   LEU A 601     4837   3765   4174   -589   -239   -261  A    N  
ATOM    261  CA  LEU A 601     -34.480  16.448 -38.189  1.00 34.12      A    C  
ANISOU  261  CA  LEU A 601     4921   3788   4255   -606   -288   -310  A    C  
ATOM    262  C   LEU A 601     -34.054  15.618 -39.373  1.00 33.35      A    C  
ANISOU  262  C   LEU A 601     4881   3671   4119   -442   -400   -374  A    C  
ATOM    263  O   LEU A 601     -34.832  14.753 -39.812  1.00 37.49      A    O  
ANISOU  263  O   LEU A 601     5479   4082   4683   -452   -536   -431  A    O  
ATOM    264  CB  LEU A 601     -35.702  17.325 -38.565  1.00 34.14      A    C  
ANISOU  264  CB  LEU A 601     4827   3857   4287   -636   -238   -341  A    C  
ATOM    265  CG  LEU A 601     -36.412  17.975 -37.380  1.00 38.84      A    C  
ANISOU  265  CG  LEU A 601     5356   4546   4854   -698   -177   -344  A    C  
ATOM    266  CD1 LEU A 601     -37.301  19.131 -37.818  1.00 45.01      A    C  
ANISOU  266  CD1 LEU A 601     6059   5403   5638   -622   -169   -426  A    C  
ATOM    267  CD2 LEU A 601     -37.223  16.965 -36.582  1.00 41.50      A    C  
ANISOU  267  CD2 LEU A 601     5652   4965   5152   -849   -181   -259  A    C  
ATOM    268  N   LYS A 602     -32.841  15.818 -39.890  1.00 35.21      A    N  
ANISOU  268  N   LYS A 602     5072   4050   4257   -270   -386   -360  A    N  
ATOM    269  CA  LYS A 602     -32.298  14.903 -40.924  1.00 37.75      A    C  
ANISOU  269  CA  LYS A 602     5436   4459   4450     11   -519   -470  A    C  
ATOM    270  C   LYS A 602     -32.145  13.434 -40.459  1.00 37.50      A    C  
ANISOU  270  C   LYS A 602     5620   4199   4431     77   -746   -586  A    C  
ATOM    271  O   LYS A 602     -32.008  12.542 -41.293  1.00 36.09      A    O  
ANISOU  271  O   LYS A 602     5547   4000   4168    353   -967   -753  A    O  
ATOM    272  CB  LYS A 602     -30.968  15.430 -41.506  1.00 39.80      A    C  
ANISOU  272  CB  LYS A 602     5516   5078   4527    204   -445   -376  A    C  
ATOM    273  CG  LYS A 602     -29.738  15.191 -40.631  1.00 48.63      A    C  
ANISOU  273  CG  LYS A 602     6636   6254   5587    224   -440   -320  A    C  
ATOM    274  CD  LYS A 602     -28.489  15.810 -41.232  1.00 53.13      A    C  
ANISOU  274  CD  LYS A 602     6945   7278   5965    360   -368   -141  A    C  
ATOM    275  CE  LYS A 602     -27.280  15.479 -40.377  1.00 56.94      A    C  
ANISOU  275  CE  LYS A 602     7420   7835   6379    397   -380    -98  A    C  
ATOM    276  NZ  LYS A 602     -26.074  16.170 -40.896  1.00 66.07      A    N1+
ANISOU  276  NZ  LYS A 602     8249   9506   7348    461   -316    167  A    N1+
ATOM    277  N   TRP A 603     -32.092  13.199 -39.142  1.00 33.98      A    N  
ANISOU  277  N   TRP A 603     5249   3591   4072   -137   -738   -503  A    N  
ATOM    278  CA  TRP A 603     -32.080  11.837 -38.590  1.00 38.83      A    C  
ANISOU  278  CA  TRP A 603     6082   3932   4741   -160  -1007   -543  A    C  
ATOM    279  C   TRP A 603     -33.453  11.139 -38.573  1.00 38.92      A    C  
ANISOU  279  C   TRP A 603     6189   3687   4913   -389  -1217   -491  A    C  
ATOM    280  O   TRP A 603     -33.505   9.925 -38.381  1.00 39.56      A    O  
ANISOU  280  O   TRP A 603     6479   3479   5073   -418  -1565   -500  A    O  
ATOM    281  CB  TRP A 603     -31.452  11.841 -37.187  1.00 36.48      A    C  
ANISOU  281  CB  TRP A 603     5800   3608   4451   -311   -926   -427  A    C  
ATOM    282  CG  TRP A 603     -29.997  12.199 -37.218  1.00 37.45      A    C  
ANISOU  282  CG  TRP A 603     5856   3941   4431    -87   -829   -466  A    C  
ATOM    283  CD1 TRP A 603     -29.436  13.445 -37.060  1.00 35.05      A    C  
ANISOU  283  CD1 TRP A 603     5360   3872   4086   -125   -593   -365  A    C  
ATOM    284  CD2 TRP A 603     -28.905  11.289 -37.411  1.00 38.41      A    C  
ANISOU  284  CD2 TRP A 603     6091   4077   4426    213  -1019   -597  A    C  
ATOM    285  CE2 TRP A 603     -27.711  12.053 -37.370  1.00 38.97      A    C  
ANISOU  285  CE2 TRP A 603     5971   4479   4358    326   -830   -533  A    C  
ATOM    286  CE3 TRP A 603     -28.820   9.911 -37.617  1.00 37.72      A    C  
ANISOU  286  CE3 TRP A 603     6255   3749   4329    414  -1389   -764  A    C  
ATOM    287  NE1 TRP A 603     -28.069  13.363 -37.169  1.00 36.39      A    N  
ANISOU  287  NE1 TRP A 603     5471   4242   4114     82   -598   -370  A    N  
ATOM    288  CZ2 TRP A 603     -26.434  11.469 -37.517  1.00 39.96      A    C  
ANISOU  288  CZ2 TRP A 603     6097   4795   4289    655   -935   -630  A    C  
ATOM    289  CZ3 TRP A 603     -27.556   9.330 -37.771  1.00 45.18      A    C  
ANISOU  289  CZ3 TRP A 603     7257   4826   5084    798  -1533   -923  A    C  
ATOM    290  CH2 TRP A 603     -26.372  10.117 -37.717  1.00 42.30      A    C  
ANISOU  290  CH2 TRP A 603     6645   4892   4537    925  -1270   -853  A    C  
ATOM    291  N   GLU A 604     -34.544  11.885 -38.789  1.00 36.70      A    N  
ANISOU  291  N   GLU A 604     5448   3679   4817   -395  -1684    569  A    N  
ATOM    292  CA  GLU A 604     -35.896  11.352 -38.665  1.00 37.60      A    C  
ANISOU  292  CA  GLU A 604     5434   3776   5078   -396  -1778    437  A    C  
ATOM    293  C   GLU A 604     -36.214  10.354 -39.786  1.00 43.19      A    C  
ANISOU  293  C   GLU A 604     6266   4534   5610   -410  -1930    437  A    C  
ATOM    294  O   GLU A 604     -36.008  10.660 -40.975  1.00 41.76      A    O  
ANISOU  294  O   GLU A 604     6238   4384   5245   -366  -2086    558  A    O  
ATOM    295  CB  GLU A 604     -36.931  12.480 -38.651  1.00 41.30      A    C  
ANISOU  295  CB  GLU A 604     5723   4120   5847   -332  -1955    423  A    C  
ATOM    296  CG  GLU A 604     -38.301  12.084 -38.114  1.00 44.41      A    C  
ANISOU  296  CG  GLU A 604     5877   4506   6493   -326  -1974    264  A    C  
ATOM    297  CD  GLU A 604     -38.365  11.849 -36.610  1.00 44.67      A    C  
ANISOU  297  CD  GLU A 604     5756   4615   6603   -324  -1695    129  A    C  
ATOM    298  OE1 GLU A 604     -37.427  12.187 -35.861  1.00 42.21      A    O  
ANISOU  298  OE1 GLU A 604     5518   4333   6187   -296  -1538    110  A    O  
ATOM    299  OE2 GLU A 604     -39.391  11.296 -36.154  1.00 42.85      A    O1-
ANISOU  299  OE2 GLU A 604     5316   4426   6540   -347  -1634     50  A    O1-
ATOM    300  N   PHE A 605     -36.734   9.190 -39.380  1.00 39.70      A    N  
ANISOU  300  N   PHE A 605     5756   4096   5234   -466  -1897    308  A    N  
ATOM    301  CA  PHE A 605     -37.010   8.042 -40.238  1.00 44.76      A    C  
ANISOU  301  CA  PHE A 605     6498   4738   5770   -478  -2067    236  A    C  
ATOM    302  C   PHE A 605     -38.489   7.655 -40.080  1.00 45.52      A    C  
ANISOU  302  C   PHE A 605     6358   4728   6211   -531  -2231    144  A    C  
ATOM    303  O   PHE A 605     -39.023   7.786 -38.977  1.00 48.03      A    O  
ANISOU  303  O   PHE A 605     6441   5027   6782   -582  -2065    132  A    O  
ATOM    304  CB  PHE A 605     -36.101   6.890 -39.806  1.00 44.35      A    C  
ANISOU  304  CB  PHE A 605     6556   4728   5568   -518  -1891    182  A    C  
ATOM    305  CG  PHE A 605     -36.191   5.667 -40.677  1.00 45.06      A    C  
ANISOU  305  CG  PHE A 605     6775   4791   5554   -502  -2087     60  A    C  
ATOM    306  CD1 PHE A 605     -35.569   5.638 -41.928  1.00 47.44      A    C  
ANISOU  306  CD1 PHE A 605     7314   5202   5509   -381  -2206     41  A    C  
ATOM    307  CD2 PHE A 605     -36.866   4.517 -40.232  1.00 43.77      A    C  
ANISOU  307  CD2 PHE A 605     6493   4496   5642   -598  -2154    -35  A    C  
ATOM    308  CE1 PHE A 605     -35.640   4.493 -42.728  1.00 51.25      A    C  
ANISOU  308  CE1 PHE A 605     7932   5664   5876   -318  -2419   -143  A    C  
ATOM    309  CE2 PHE A 605     -36.936   3.375 -41.025  1.00 45.27      A    C  
ANISOU  309  CE2 PHE A 605     6799   4606   5796   -571  -2396   -190  A    C  
ATOM    310  CZ  PHE A 605     -36.326   3.364 -42.273  1.00 49.18      A    C  
ANISOU  310  CZ  PHE A 605     7550   5213   5923   -412  -2543   -280  A    C  
ATOM    311  N   PRO A 606     -39.160   7.192 -41.154  1.00 49.01      A    N  
ANISOU  311  N   PRO A 606     6840   5112   6668   -507  -2556     73  A    N  
ATOM    312  CA  PRO A 606     -40.595   6.866 -40.990  1.00 51.28      A    C  
ANISOU  312  CA  PRO A 606     6839   5271   7374   -572  -2735     -7  A    C  
ATOM    313  C   PRO A 606     -40.828   5.573 -40.192  1.00 50.35      A    C  
ANISOU  313  C   PRO A 606     6576   5081   7473   -716  -2610    -54  A    C  
ATOM    314  O   PRO A 606     -40.258   4.555 -40.558  1.00 51.00      A    O  
ANISOU  314  O   PRO A 606     6844   5131   7403   -731  -2678   -119  A    O  
ATOM    315  CB  PRO A 606     -41.109   6.722 -42.443  1.00 53.88      A    C  
ANISOU  315  CB  PRO A 606     7294   5548   7631   -488  -3182    -88  A    C  
ATOM    316  CG  PRO A 606     -39.960   7.049 -43.342  1.00 53.89      A    C  
ANISOU  316  CG  PRO A 606     7661   5698   7119   -365  -3185    -22  A    C  
ATOM    317  CD  PRO A 606     -38.707   6.886 -42.527  1.00 52.52      A    C  
ANISOU  317  CD  PRO A 606     7573   5618   6764   -407  -2786     41  A    C  
ATOM    318  N   ARG A 607     -41.619   5.652 -39.108  1.00 54.20      A    N  
ANISOU  318  N   ARG A 607     6734   5554   8304   -806  -2419     -6  A    N  
ATOM    319  CA  ARG A 607     -42.117   4.475 -38.290  1.00 60.03      A    C  
ANISOU  319  CA  ARG A 607     7254   6216   9339   -977  -2293     35  A    C  
ATOM    320  C   ARG A 607     -42.480   3.250 -39.103  1.00 55.45      A    C  
ANISOU  320  C   ARG A 607     6696   5437   8938  -1057  -2639    -54  A    C  
ATOM    321  O   ARG A 607     -42.050   2.145 -38.795  1.00 59.17      A    O  
ANISOU  321  O   ARG A 607     7236   5821   9424  -1153  -2589    -30  A    O  
ATOM    322  CB  ARG A 607     -43.414   4.767 -37.483  1.00 66.47      A    C  
ANISOU  322  CB  ARG A 607     7620   7043  10591  -1048  -2159     93  A    C  
ATOM    323  CG  ARG A 607     -43.487   6.104 -36.832  1.00 71.49      A    C  
ANISOU  323  CG  ARG A 607     8151   7840  11174   -922  -1931     94  A    C  
ATOM    324  CD  ARG A 607     -44.459   6.226 -35.677  1.00 71.08      A    C  
ANISOU  324  CD  ARG A 607     7680   7893  11434   -963  -1634    149  A    C  
ATOM    325  NE  ARG A 607     -43.803   7.205 -34.820  1.00 71.08      A    N  
ANISOU  325  NE  ARG A 607     7776   8076  11156   -818  -1345    122  A    N  
ATOM    326  CZ  ARG A 607     -43.014   6.948 -33.776  1.00 63.13      A    C  
ANISOU  326  CZ  ARG A 607     6895   7216   9877   -826  -1015    193  A    C  
ATOM    327  NH1 ARG A 607     -42.845   5.708 -33.290  1.00 58.95      A    N1+
ANISOU  327  NH1 ARG A 607     6380   6689   9329   -986   -866    347  A    N1+
ATOM    328  NH2 ARG A 607     -42.427   7.980 -33.160  1.00 61.52      A    N  
ANISOU  328  NH2 ARG A 607     6790   7139   9446   -661   -861    107  A    N  
ATOM    329  N   GLU A 608     -43.296   3.474 -40.128  1.00 57.86      A    N  
ANISOU  329  N   GLU A 608     6936   5645   9402  -1004  -3032   -170  A    N  
ATOM    330  CA  GLU A 608     -43.869   2.399 -40.953  1.00 63.66      A    C  
ANISOU  330  CA  GLU A 608     7645   6156  10388  -1059  -3461   -314  A    C  
ATOM    331  C   GLU A 608     -42.846   1.642 -41.819  1.00 61.58      A    C  
ANISOU  331  C   GLU A 608     7796   5866   9737   -957  -3660   -472  A    C  
ATOM    332  O   GLU A 608     -43.151   0.564 -42.303  1.00 61.62      A    O  
ANISOU  332  O   GLU A 608     7800   5659   9956  -1000  -3992   -623  A    O  
ATOM    333  CB  GLU A 608     -45.067   2.906 -41.786  1.00 69.86      A    C  
ANISOU  333  CB  GLU A 608     8238   6849  11458  -1004  -3874   -416  A    C  
ATOM    334  CG  GLU A 608     -44.752   3.874 -42.924  1.00 77.67      A    C  
ANISOU  334  CG  GLU A 608     9531   7952  12028   -781  -4123   -491  A    C  
ATOM    335  N   ASN A 609     -41.645   2.205 -41.997  1.00 57.79      A    N  
ANISOU  335  N   ASN A 609     7638   5593   8725   -816  -3461   -448  A    N  
ATOM    336  CA  ASN A 609     -40.506   1.477 -42.581  1.00 58.91      A    C  
ANISOU  336  CA  ASN A 609     8132   5770   8482   -707  -3513   -581  A    C  
ATOM    337  C   ASN A 609     -39.759   0.539 -41.596  1.00 58.65      A    C  
ANISOU  337  C   ASN A 609     8106   5670   8508   -814  -3242   -522  A    C  
ATOM    338  O   ASN A 609     -38.752  -0.060 -41.980  1.00 55.26      A    O  
ANISOU  338  O   ASN A 609     7939   5265   7792   -708  -3259   -644  A    O  
ATOM    339  CB  ASN A 609     -39.524   2.472 -43.236  1.00 59.42      A    C  
ANISOU  339  CB  ASN A 609     8493   6098   7986   -518  -3399   -542  A    C  
ATOM    340  CG  ASN A 609     -40.083   3.115 -44.505  1.00 63.13      A    C  
ANISOU  340  CG  ASN A 609     9070   6625   8291   -371  -3761   -609  A    C  
ATOM    341  ND2 ASN A 609     -39.186   3.645 -45.331  1.00 66.47      A    N  
ANISOU  341  ND2 ASN A 609     9797   7274   8184   -198  -3720   -576  A    N  
ATOM    342  OD1 ASN A 609     -41.294   3.148 -44.735  1.00 63.50      A    O  
ANISOU  342  OD1 ASN A 609     8918   6526   8684   -411  -4070   -666  A    O  
ATOM    343  N   LEU A 610     -40.227   0.424 -40.347  1.00 58.96      A    N  
ANISOU  343  N   LEU A 610     7864   5646   8893  -1002  -2989   -331  A    N  
ATOM    344  CA  LEU A 610     -39.770  -0.605 -39.402  1.00 59.67      A    C  
ANISOU  344  CA  LEU A 610     7931   5623   9116  -1129  -2807   -230  A    C  
ATOM    345  C   LEU A 610     -40.759  -1.751 -39.324  1.00 60.65      A    C  
ANISOU  345  C   LEU A 610     7814   5438   9791  -1313  -3060   -225  A    C  
ATOM    346  O   LEU A 610     -41.933  -1.520 -39.041  1.00 64.72      A    O  
ANISOU  346  O   LEU A 610     7994   5903  10695  -1442  -3073   -121  A    O  
ATOM    347  CB  LEU A 610     -39.617  -0.017 -38.004  1.00 56.94      A    C  
ANISOU  347  CB  LEU A 610     7448   5441   8745  -1210  -2346     19  A    C  
ATOM    348  CG  LEU A 610     -38.623   1.128 -37.857  1.00 54.61      A    C  
ANISOU  348  CG  LEU A 610     7341   5400   8007  -1060  -2097     34  A    C  
ATOM    349  CD1 LEU A 610     -38.678   1.639 -36.426  1.00 53.37      A    C  
ANISOU  349  CD1 LEU A 610     7024   5378   7877  -1122  -1714    223  A    C  
ATOM    350  CD2 LEU A 610     -37.207   0.684 -38.211  1.00 51.42      A    C  
ANISOU  350  CD2 LEU A 610     7254   5026   7259   -948  -2093    -56  A    C  
ATOM    351  N   GLU A 611     -40.282  -2.970 -39.573  1.00 61.90      A    N  
ANISOU  351  N   GLU A 611     8118   5375  10028  -1319  -3271   -340  A    N  
ATOM    352  CA  GLU A 611     -41.048  -4.203 -39.322  1.00 70.69      A    C  
ANISOU  352  CA  GLU A 611     8998   6123  11739  -1530  -3504   -284  A    C  
ATOM    353  C   GLU A 611     -40.360  -4.859 -38.121  1.00 68.35      A    C  
ANISOU  353  C   GLU A 611     8720   5780  11470  -1652  -3188    -23  A    C  
ATOM    354  O   GLU A 611     -39.239  -5.352 -38.241  1.00 61.39      A    O  
ANISOU  354  O   GLU A 611     8124   4869  10331  -1529  -3213   -137  A    O  
ATOM    355  CB  GLU A 611     -41.056  -5.110 -40.558  1.00 73.83      A    C  
ANISOU  355  CB  GLU A 611     9558   6246  12248  -1420  -4071   -649  A    C  
ATOM    356  CG  GLU A 611     -41.988  -6.316 -40.461  1.00 84.94      A    C  
ANISOU  356  CG  GLU A 611    10685   7201  14387  -1647  -4427   -624  A    C  
ATOM    357  N   PHE A 612     -41.019  -4.801 -36.961  1.00 69.34      A    N  
ANISOU  357  N   PHE A 612     8539   5935  11873  -1868  -2876    332  A    N  
ATOM    358  CA  PHE A 612     -40.482  -5.350 -35.714  1.00 69.36      A    C  
ANISOU  358  CA  PHE A 612     8552   5934  11867  -1987  -2557    647  A    C  
ATOM    359  C   PHE A 612     -40.454  -6.887 -35.665  1.00 73.13      A    C  
ANISOU  359  C   PHE A 612     9014   5978  12794  -2142  -2843    722  A    C  
ATOM    360  O   PHE A 612     -41.461  -7.539 -35.922  1.00 72.01      A    O  
ANISOU  360  O   PHE A 612     8600   5530  13229  -2327  -3120    765  A    O  
ATOM    361  CB  PHE A 612     -41.244  -4.784 -34.503  1.00 70.29      A    C  
ANISOU  361  CB  PHE A 612     8351   6278  12078  -2140  -2110   1009  A    C  
ATOM    362  CG  PHE A 612     -40.912  -3.353 -34.227  1.00 67.63      A    C  
ANISOU  362  CG  PHE A 612     8099   6348  11251  -1957  -1788    949  A    C  
ATOM    363  CD1 PHE A 612     -39.661  -3.017 -33.690  1.00 62.39      A    C  
ANISOU  363  CD1 PHE A 612     7732   5879  10095  -1816  -1557    956  A    C  
ATOM    364  CD2 PHE A 612     -41.811  -2.331 -34.534  1.00 67.54      A    C  
ANISOU  364  CD2 PHE A 612     7866   6487  11308  -1914  -1765    865  A    C  
ATOM    365  CE1 PHE A 612     -39.315  -1.689 -33.458  1.00 61.88      A    C  
ANISOU  365  CE1 PHE A 612     7739   6134   9640  -1650  -1319    879  A    C  
ATOM    366  CE2 PHE A 612     -41.474  -0.998 -34.295  1.00 66.71      A    C  
ANISOU  366  CE2 PHE A 612     7844   6699  10803  -1736  -1520    793  A    C  
ATOM    367  CZ  PHE A 612     -40.224  -0.676 -33.752  1.00 65.48      A    C  
ANISOU  367  CZ  PHE A 612     7982   6716  10181  -1610  -1301    800  A    C  
ATOM    368  N   GLY A 613     -39.276  -7.431 -35.350  1.00 70.76      A    N  
ANISOU  368  N   GLY A 613     8995   5628  12264  -2059  -2805    728  A    N  
ATOM    369  CA  GLY A 613     -39.077  -8.833 -35.032  1.00 75.26      A    C  
ANISOU  369  CA  GLY A 613     9573   5790  13233  -2196  -3018    869  A    C  
ATOM    370  C   GLY A 613     -39.050  -8.987 -33.518  1.00 75.44      A    C  
ANISOU  370  C   GLY A 613     9488   5909  13267  -2383  -2598   1392  A    C  
ATOM    371  O   GLY A 613     -39.885  -8.377 -32.802  1.00 77.98      A    O  
ANISOU  371  O   GLY A 613     9539   6470  13620  -2521  -2248   1684  A    O  
ATOM    372  N   LYS A 614     -38.081  -9.775 -33.034  1.00 73.85      A    N  
ANISOU  372  N   LYS A 614     9502   5547  13009  -2357  -2631   1499  A    N  
ATOM    373  CA  LYS A 614     -38.026 -10.205 -31.627  1.00 78.14      A    C  
ANISOU  373  CA  LYS A 614     9985   6105  13600  -2538  -2329   2034  A    C  
ATOM    374  C   LYS A 614     -37.353  -9.191 -30.697  1.00 70.67      A    C  
ANISOU  374  C   LYS A 614     9191   5656  12005  -2396  -1856   2154  A    C  
ATOM    375  O   LYS A 614     -36.591  -8.310 -31.138  1.00 64.39      A    O  
ANISOU  375  O   LYS A 614     8601   5115  10748  -2145  -1809   1810  A    O  
ATOM    376  CB  LYS A 614     -37.321 -11.566 -31.499  1.00 86.98      A    C  
ANISOU  376  CB  LYS A 614    11267   6773  15009  -2573  -2645   2120  A    C  
ATOM    377  CG  LYS A 614     -38.092 -12.728 -32.110  1.00 98.06      A    C  
ANISOU  377  CG  LYS A 614    12473   7605  17181  -2772  -3124   2109  A    C  
ATOM    378  N   VAL A 615     -37.640  -9.353 -29.404  1.00 69.67      A    N  
ANISOU  378  N   VAL A 615     8956   5655  11862  -2558  -1521   2656  A    N  
ATOM    379  CA  VAL A 615     -37.041  -8.564 -28.331  1.00 68.75      A    C  
ANISOU  379  CA  VAL A 615     8990   5979  11152  -2426  -1111   2804  A    C  
ATOM    380  C   VAL A 615     -35.634  -9.109 -28.126  1.00 69.67      A    C  
ANISOU  380  C   VAL A 615     9455   5959  11055  -2278  -1280   2751  A    C  
ATOM    381  O   VAL A 615     -35.456 -10.324 -28.003  1.00 68.02      A    O  
ANISOU  381  O   VAL A 615     9286   5360  11197  -2397  -1522   2957  A    O  
ATOM    382  CB  VAL A 615     -37.821  -8.660 -26.989  1.00 77.35      A    C  
ANISOU  382  CB  VAL A 615     9867   7281  12242  -2622   -696   3377  A    C  
ATOM    383  CG1 VAL A 615     -37.194  -7.759 -25.917  1.00 77.05      A    C  
ANISOU  383  CG1 VAL A 615    10020   7733  11522  -2423   -315   3438  A    C  
ATOM    384  CG2 VAL A 615     -39.290  -8.276 -27.169  1.00 82.72      A    C  
ANISOU  384  CG2 VAL A 615    10122   8060  13250  -2788   -529   3462  A    C  
ATOM    385  N   LEU A 616     -34.657  -8.197 -28.091  1.00 67.18      A    N  
ANISOU  385  N   LEU A 616     9363   5940  10221  -2022  -1174   2478  A    N  
ATOM    386  CA  LEU A 616     -33.240  -8.507 -27.835  1.00 67.45      A    C  
ANISOU  386  CA  LEU A 616     9698   5916  10015  -1844  -1299   2396  A    C  
ATOM    387  C   LEU A 616     -32.850  -8.349 -26.365  1.00 68.97      A    C  
ANISOU  387  C   LEU A 616    10005   6365   9834  -1821  -1026   2754  A    C  
ATOM    388  O   LEU A 616     -32.001  -9.083 -25.875  1.00 68.65      A    O  
ANISOU  388  O   LEU A 616    10156   6158   9770  -1777  -1172   2896  A    O  
ATOM    389  CB  LEU A 616     -32.339  -7.629 -28.718  1.00 60.49      A    C  
ANISOU  389  CB  LEU A 616     8958   5186   8838  -1584  -1370   1895  A    C  
ATOM    390  CG  LEU A 616     -32.554  -7.836 -30.226  1.00 60.18      A    C  
ANISOU  390  CG  LEU A 616     8875   4931   9061  -1548  -1665   1519  A    C  
ATOM    391  CD1 LEU A 616     -31.806  -6.771 -30.991  1.00 53.85      A    C  
ANISOU  391  CD1 LEU A 616     8179   4381   7900  -1315  -1624   1133  A    C  
ATOM    392  CD2 LEU A 616     -32.150  -9.243 -30.700  1.00 63.06      A    C  
ANISOU  392  CD2 LEU A 616     9324   4837   9800  -1550  -2057   1443  A    C  
ATOM    393  N   GLY A 617     -33.434  -7.368 -25.685  1.00 72.53      A    N  
ANISOU  393  N   GLY A 617    10355   7228   9976  -1814   -658   2861  A    N  
ATOM    394  CA  GLY A 617     -33.338  -7.263 -24.232  1.00 73.96      A    C  
ANISOU  394  CA  GLY A 617    10623   7698   9780  -1795   -375   3231  A    C  
ATOM    395  C   GLY A 617     -34.301  -6.249 -23.642  1.00 78.41      A    C  
ANISOU  395  C   GLY A 617    10997   8705  10090  -1791     38   3307  A    C  
ATOM    396  O   GLY A 617     -34.759  -5.341 -24.342  1.00 74.54      A    O  
ANISOU  396  O   GLY A 617    10358   8328   9637  -1738     84   2985  A    O  
ATOM    397  N   SER A 618     -34.592  -6.420 -22.351  1.00 88.62      A    N  
ANISOU  397  N   SER A 618    12301  10254  11114  -1827    331   3738  A    N  
ATOM    398  CA  SER A 618     -35.442  -5.516 -21.558  1.00 91.27      A    C  
ANISOU  398  CA  SER A 618    12474  11082  11123  -1770    772   3828  A    C  
ATOM    399  C   SER A 618     -34.731  -5.088 -20.271  1.00 90.02      A    C  
ANISOU  399  C   SER A 618    12592  11307  10303  -1538    942   3905  A    C  
ATOM    400  O   SER A 618     -34.015  -5.878 -19.661  1.00 87.91      A    O  
ANISOU  400  O   SER A 618    12566  10938   9898  -1540    820   4185  A    O  
ATOM    401  CB  SER A 618     -36.754  -6.205 -21.185  1.00 94.40      A    C  
ANISOU  401  CB  SER A 618    12544  11492  11831  -2050   1041   4343  A    C  
ATOM    402  OG  SER A 618     -37.474  -6.563 -22.344  1.00 93.32      A    O  
ANISOU  402  OG  SER A 618    12131  10996  12332  -2255    842   4242  A    O  
ATOM    403  N   GLY A 619     -34.905  -3.820 -19.903  1.00 94.69      A    N  
ANISOU  403  N   GLY A 619    13159  12312  10507  -1317   1168   3618  A    N  
ATOM    404  CA  GLY A 619     -34.633  -3.318 -18.556  1.00 96.85      A    C  
ANISOU  404  CA  GLY A 619    13625  13047  10128  -1083   1404   3694  A    C  
ATOM    405  C   GLY A 619     -35.964  -2.993 -17.910  1.00101.47      A    C  
ANISOU  405  C   GLY A 619    13923  14053  10578  -1107   1896   3919  A    C  
ATOM    406  O   GLY A 619     -37.017  -3.491 -18.342  1.00 98.11      A    O  
ANISOU  406  O   GLY A 619    13159  13507  10611  -1368   2040   4176  A    O  
ATOM    407  N   ALA A 620     -35.912  -2.160 -16.873  1.00104.83      A    N  
ANISOU  407  N   ALA A 620    14467  14976  10389   -819   2140   3800  A    N  
ATOM    408  CA  ALA A 620     -37.120  -1.640 -16.219  1.00112.23      A    C  
ANISOU  408  CA  ALA A 620    15125  16404  11115   -748   2644   3903  A    C  
ATOM    409  C   ALA A 620     -37.787  -0.579 -17.100  1.00110.15      A    C  
ANISOU  409  C   ALA A 620    14555  16116  11181   -691   2650   3419  A    C  
ATOM    410  O   ALA A 620     -38.966  -0.710 -17.452  1.00108.86      A    O  
ANISOU  410  O   ALA A 620    13990  15966  11407   -872   2883   3580  A    O  
ATOM    411  CB  ALA A 620     -36.783  -1.059 -14.855  1.00114.74      A    C  
ANISOU  411  CB  ALA A 620    15704  17270  10621   -395   2857   3845  A    C  
ATOM    412  N   PHE A 621     -37.009   0.443 -17.472  1.00105.66      A    N  
ANISOU  412  N   PHE A 621    14164  15477  10505   -454   2362   2855  A    N  
ATOM    413  CA  PHE A 621     -37.506   1.617 -18.214  1.00 98.92      A    C  
ANISOU  413  CA  PHE A 621    13080  14609   9899   -344   2323   2377  A    C  
ATOM    414  C   PHE A 621     -37.627   1.476 -19.752  1.00 89.72      A    C  
ANISOU  414  C   PHE A 621    11750  12955   9383   -575   2017   2255  A    C  
ATOM    415  O   PHE A 621     -38.078   2.418 -20.406  1.00 84.68      A    O  
ANISOU  415  O   PHE A 621    10925  12287   8963   -496   1964   1910  A    O  
ATOM    416  CB  PHE A 621     -36.644   2.843 -17.865  1.00 96.03      A    C  
ANISOU  416  CB  PHE A 621    12963  14377   9149     15   2142   1856  A    C  
ATOM    417  N   GLY A 622     -37.255   0.330 -20.332  1.00 83.93      A    N  
ANISOU  417  N   GLY A 622    11093  11846   8951   -832   1798   2518  A    N  
ATOM    418  CA  GLY A 622     -37.355   0.146 -21.787  1.00 76.14      A    C  
ANISOU  418  CA  GLY A 622     9985  10432   8511  -1011   1493   2374  A    C  
ATOM    419  C   GLY A 622     -36.892  -1.186 -22.355  1.00 75.62      A    C  
ANISOU  419  C   GLY A 622    10027   9954   8751  -1248   1227   2617  A    C  
ATOM    420  O   GLY A 622     -36.661  -2.141 -21.615  1.00 79.42      A    O  
ANISOU  420  O   GLY A 622    10622  10429   9123  -1340   1294   3001  A    O  
ATOM    421  N   LYS A 623     -36.766  -1.238 -23.682  1.00 70.70      A    N  
ANISOU  421  N   LYS A 623     9372   8986   8505  -1327    910   2386  A    N  
ATOM    422  CA  LYS A 623     -36.359  -2.460 -24.401  1.00 65.45      A    C  
ANISOU  422  CA  LYS A 623     8793   7899   8175  -1510    605   2508  A    C  
ATOM    423  C   LYS A 623     -35.654  -2.172 -25.724  1.00 60.87      A    C  
ANISOU  423  C   LYS A 623     8334   7068   7726  -1436    252   2110  A    C  
ATOM    424  O   LYS A 623     -35.781  -1.080 -26.291  1.00 60.23      A    O  
ANISOU  424  O   LYS A 623     8195   7086   7604  -1318    236   1804  A    O  
ATOM    425  CB  LYS A 623     -37.557  -3.405 -24.622  1.00 70.22      A    C  
ANISOU  425  CB  LYS A 623     9088   8317   9277  -1796    643   2836  A    C  
ATOM    426  CG  LYS A 623     -38.828  -2.755 -25.154  1.00 73.42      A    C  
ANISOU  426  CG  LYS A 623     9125   8804   9968  -1846    745   2715  A    C  
ATOM    427  CD  LYS A 623     -39.932  -3.776 -25.416  1.00 75.49      A    C  
ANISOU  427  CD  LYS A 623     9052   8818  10811  -2151    718   3037  A    C  
ATOM    428  N   VAL A 624     -34.882  -3.159 -26.173  1.00 57.68      A    N  
ANISOU  428  N   VAL A 624     8102   6351   7464  -1491    -22   2132  A    N  
ATOM    429  CA  VAL A 624     -34.216  -3.144 -27.470  1.00 52.94      A    C  
ANISOU  429  CA  VAL A 624     7609   5521   6985  -1423   -338   1795  A    C  
ATOM    430  C   VAL A 624     -34.807  -4.291 -28.276  1.00 56.09      A    C  
ANISOU  430  C   VAL A 624     7895   5559   7858  -1611   -579   1865  A    C  
ATOM    431  O   VAL A 624     -34.781  -5.450 -27.829  1.00 56.25      A    O  
ANISOU  431  O   VAL A 624     7937   5364   8071  -1745   -649   2145  A    O  
ATOM    432  CB  VAL A 624     -32.698  -3.300 -27.360  1.00 50.70      A    C  
ANISOU  432  CB  VAL A 624     7610   5183   6469  -1269   -479   1676  A    C  
ATOM    433  CG1 VAL A 624     -32.023  -3.054 -28.712  1.00 49.09      A    C  
ANISOU  433  CG1 VAL A 624     7481   4851   6322  -1162   -714   1315  A    C  
ATOM    434  CG2 VAL A 624     -32.157  -2.304 -26.345  1.00 53.48      A    C  
ANISOU  434  CG2 VAL A 624     8064   5857   6401  -1101   -283   1645  A    C  
ATOM    435  N   MET A 625     -35.337  -3.943 -29.452  1.00 54.83      A    N  
ANISOU  435  N   MET A 625     7622   5320   7892  -1612   -738   1612  A    N  
ATOM    436  CA  MET A 625     -35.995  -4.866 -30.362  1.00 58.27      A    C  
ANISOU  436  CA  MET A 625     7937   5416   8787  -1756  -1032   1582  A    C  
ATOM    437  C   MET A 625     -35.285  -4.906 -31.710  1.00 54.21      A    C  
ANISOU  437  C   MET A 625     7605   4756   8236  -1601  -1355   1187  A    C  
ATOM    438  O   MET A 625     -34.862  -3.886 -32.236  1.00 55.38      A    O  
ANISOU  438  O   MET A 625     7841   5108   8094  -1434  -1316    950  A    O  
ATOM    439  CB  MET A 625     -37.462  -4.461 -30.543  1.00 64.19      A    C  
ANISOU  439  CB  MET A 625     8352   6222   9817  -1887   -955   1642  A    C  
ATOM    440  CG  MET A 625     -38.350  -4.960 -29.409  1.00 74.07      A    C  
ANISOU  440  CG  MET A 625     9349   7510  11285  -2103   -691   2089  A    C  
ATOM    441  SD  MET A 625     -40.083  -4.518 -29.557  1.00 86.40      A    S  
ANISOU  441  SD  MET A 625    10433   9150  13244  -2255   -569   2171  A    S  
ATOM    442  CE  MET A 625     -40.658  -5.825 -30.641  1.00 87.07      A    C  
ANISOU  442  CE  MET A 625    10378   8690  14016  -2468  -1071   2140  A    C  
ATOM    443  N   ASN A 626     -35.157  -6.108 -32.254  1.00 55.72      A    N  
ANISOU  443  N   ASN A 626     7849   4594   8729  -1649  -1676   1128  A    N  
ATOM    444  CA  ASN A 626     -34.754  -6.317 -33.631  1.00 57.40      A    C  
ANISOU  444  CA  ASN A 626     8196   4665   8949  -1497  -2008    733  A    C  
ATOM    445  C   ASN A 626     -35.859  -5.794 -34.562  1.00 59.44      A    C  
ANISOU  445  C   ASN A 626     8289   4946   9350  -1526  -2139    575  A    C  
ATOM    446  O   ASN A 626     -37.053  -5.845 -34.221  1.00 57.85      A    O  
ANISOU  446  O   ASN A 626     7816   4685   9479  -1723  -2102    777  A    O  
ATOM    447  CB  ASN A 626     -34.524  -7.822 -33.892  1.00 63.33      A    C  
ANISOU  447  CB  ASN A 626     9011   4985  10065  -1537  -2362    689  A    C  
ATOM    448  CG  ASN A 626     -34.173  -8.129 -35.339  1.00 65.45      A    C  
ANISOU  448  CG  ASN A 626     9423   5124  10322  -1337  -2726    225  A    C  
ATOM    449  ND2 ASN A 626     -33.023  -7.641 -35.806  1.00 65.60      A    N  
ANISOU  449  ND2 ASN A 626     9651   5365   9910  -1084  -2653    -23  A    N  
ATOM    450  OD1 ASN A 626     -34.954  -8.759 -36.037  1.00 75.79      A    O  
ANISOU  450  OD1 ASN A 626    10640   6155  12000  -1402  -3065     89  A    O  
ATOM    451  N   ALA A 627     -35.447  -5.281 -35.717  1.00 54.38      A    N  
ANISOU  451  N   ALA A 627     7799   4409   8455  -1325  -2285    237  A    N  
ATOM    452  CA  ALA A 627     -36.380  -4.958 -36.797  1.00 57.64      A    C  
ANISOU  452  CA  ALA A 627     8118   4797   8985  -1310  -2525     42  A    C  
ATOM    453  C   ALA A 627     -35.696  -5.004 -38.148  1.00 54.33      A    C  
ANISOU  453  C   ALA A 627     7948   4404   8292  -1063  -2784   -339  A    C  
ATOM    454  O   ALA A 627     -34.466  -4.928 -38.237  1.00 52.99      A    O  
ANISOU  454  O   ALA A 627     7986   4367   7780   -892  -2671   -437  A    O  
ATOM    455  CB  ALA A 627     -37.005  -3.588 -36.566  1.00 56.18      A    C  
ANISOU  455  CB  ALA A 627     7783   4899   8664  -1328  -2276    150  A    C  
ATOM    456  N   THR A 628     -36.510  -5.164 -39.187  1.00 59.21      A    N  
ANISOU  456  N   THR A 628     8528   4903   9067  -1036  -3137   -554  A    N  
ATOM    457  CA  THR A 628     -36.087  -4.902 -40.564  1.00 63.27      A    C  
ANISOU  457  CA  THR A 628     9274   5554   9211   -773  -3350   -900  A    C  
ATOM    458  C   THR A 628     -36.407  -3.425 -40.863  1.00 57.18      A    C  
ANISOU  458  C   THR A 628     8475   5101   8150   -730  -3177   -816  A    C  
ATOM    459  O   THR A 628     -37.509  -2.951 -40.567  1.00 56.58      A    O  
ANISOU  459  O   THR A 628     8163   4995   8338   -881  -3177   -669  A    O  
ATOM    460  CB  THR A 628     -36.748  -5.890 -41.537  1.00 67.71      A    C  
ANISOU  460  CB  THR A 628     9851   5813  10063   -728  -3887  -1212  A    C  
ATOM    461  CG2 THR A 628     -36.337  -5.625 -42.988  1.00 73.09      A    C  
ANISOU  461  CG2 THR A 628    10806   6697  10268   -413  -4106  -1583  A    C  
ATOM    462  OG1 THR A 628     -36.306  -7.204 -41.189  1.00 68.72      A    O  
ANISOU  462  OG1 THR A 628    10013   5616  10481   -756  -4042  -1278  A    O  
ATOM    463  N   ALA A 629     -35.419  -2.703 -41.393  1.00 55.67      A    N  
ANISOU  463  N   ALA A 629     8497   5201   7456   -530  -3016   -885  A    N  
ATOM    464  CA  ALA A 629     -35.565  -1.285 -41.753  1.00 55.41      A    C  
ANISOU  464  CA  ALA A 629     8467   5438   7147   -477  -2878   -782  A    C  
ATOM    465  C   ALA A 629     -35.493  -1.180 -43.280  1.00 58.59      A    C  
ANISOU  465  C   ALA A 629     9089   5969   7202   -249  -3151  -1024  A    C  
ATOM    466  O   ALA A 629     -34.472  -1.552 -43.880  1.00 57.25      A    O  
ANISOU  466  O   ALA A 629     9137   5925   6688    -54  -3133  -1194  A    O  
ATOM    467  CB  ALA A 629     -34.486  -0.434 -41.101  1.00 49.11      A    C  
ANISOU  467  CB  ALA A 629     7713   4866   6078   -453  -2468   -598  A    C  
ATOM    468  N   TYR A 630     -36.572  -0.670 -43.882  1.00 60.87      A    N  
ANISOU  468  N   TYR A 630     9312   6247   7568   -257  -3399  -1038  A    N  
ATOM    469  CA  TYR A 630     -36.713  -0.534 -45.350  1.00 71.28      A    C  
ANISOU  469  CA  TYR A 630    10850   7697   8537    -34  -3721  -1251  A    C  
ATOM    470  C   TYR A 630     -36.228   0.872 -45.747  1.00 66.45      A    C  
ANISOU  470  C   TYR A 630    10347   7412   7488     59  -3480  -1035  A    C  
ATOM    471  O   TYR A 630     -36.742   1.882 -45.264  1.00 61.13      A    O  
ANISOU  471  O   TYR A 630     9505   6744   6977    -63  -3363   -798  A    O  
ATOM    472  CB  TYR A 630     -38.168  -0.809 -45.796  1.00 73.60      A    C  
ANISOU  472  CB  TYR A 630    11006   7760   9199    -90  -4195  -1385  A    C  
ATOM    473  CG  TYR A 630     -38.614  -2.254 -45.525  1.00 90.12      A    C  
ANISOU  473  CG  TYR A 630    12981   9481  11778   -190  -4487  -1590  A    C  
ATOM    474  CD1 TYR A 630     -38.937  -2.687 -44.220  1.00 89.20      A    C  
ANISOU  474  CD1 TYR A 630    12574   9134  12184   -464  -4297  -1381  A    C  
ATOM    475  CD2 TYR A 630     -38.712  -3.206 -46.569  1.00103.55      A    C  
ANISOU  475  CD2 TYR A 630    14865  11053  13426     -5  -4973  -1987  A    C  
ATOM    476  CE1 TYR A 630     -39.330  -4.003 -43.959  1.00 95.60      A    C  
ANISOU  476  CE1 TYR A 630    13261   9570  13491   -587  -4565  -1497  A    C  
ATOM    477  CE2 TYR A 630     -39.103  -4.536 -46.312  1.00102.21      A    C  
ANISOU  477  CE2 TYR A 630    14572  10474  13788   -109  -5288  -2172  A    C  
ATOM    478  CZ  TYR A 630     -39.411  -4.931 -45.003  1.00 97.58      A    C  
ANISOU  478  CZ  TYR A 630    13677   9634  13764   -420  -5079  -1894  A    C  
ATOM    479  OH  TYR A 630     -39.800  -6.222 -44.701  1.00 88.96      A    O  
ANISOU  479  OH  TYR A 630    12439   8108  13253   -561  -5379  -1992  A    O  
ATOM    480  N   GLY A 631     -35.181   0.920 -46.564  1.00 69.88      A    N  
ANISOU  480  N   GLY A 631    11041   8113   7396    276  -3382  -1104  A    N  
ATOM    481  CA  GLY A 631     -34.652   2.175 -47.096  1.00 67.31      A    C  
ANISOU  481  CA  GLY A 631    10828   8096   6650    362  -3171   -860  A    C  
ATOM    482  C   GLY A 631     -33.855   3.064 -46.168  1.00 64.09      A    C  
ANISOU  482  C   GLY A 631    10297   7765   6290    234  -2726   -550  A    C  
ATOM    483  O   GLY A 631     -33.721   4.254 -46.447  1.00 74.29      A    O  
ANISOU  483  O   GLY A 631    11604   9206   7417    237  -2611   -292  A    O  
ATOM    484  N   ILE A 632     -33.301   2.513 -45.088  1.00 60.42      A    N  
ANISOU  484  N   ILE A 632     9718   7183   6056    130  -2509   -568  A    N  
ATOM    485  CA  ILE A 632     -32.470   3.299 -44.161  1.00 58.11      A    C  
ANISOU  485  CA  ILE A 632     9318   6951   5813     30  -2133   -323  A    C  
ATOM    486  C   ILE A 632     -31.004   3.517 -44.600  1.00 63.13      A    C  
ANISOU  486  C   ILE A 632    10068   7845   6073    161  -1860   -256  A    C  
ATOM    487  O   ILE A 632     -30.375   4.473 -44.132  1.00 63.60      A    O  
ANISOU  487  O   ILE A 632    10038   7970   6157     88  -1609    -15  A    O  
ATOM    488  CB  ILE A 632     -32.556   2.749 -42.707  1.00 55.53      A    C  
ANISOU  488  CB  ILE A 632     8814   6406   5880   -136  -2024   -328  A    C  
ATOM    489  CG1 ILE A 632     -32.180   3.830 -41.691  1.00 51.94      A    C  
ANISOU  489  CG1 ILE A 632     8223   5978   5533   -242  -1748    -96  A    C  
ATOM    490  CG2 ILE A 632     -31.684   1.509 -42.500  1.00 55.74      A    C  
ANISOU  490  CG2 ILE A 632     8917   6386   5877    -72  -1981   -503  A    C  
ATOM    491  CD1 ILE A 632     -32.699   3.557 -40.305  1.00 53.02      A    C  
ANISOU  491  CD1 ILE A 632     8184   5945   6015   -393  -1680    -68  A    C  
ATOM    492  N   SER A 633     -30.474   2.665 -45.485  1.00 74.50      A    N  
ANISOU  492  N   SER A 633    11681   9428   7199    360  -1916   -476  A    N  
ATOM    493  CA  SER A 633     -29.051   2.686 -45.881  1.00 82.91      A    C  
ANISOU  493  CA  SER A 633    12808  10763   7930    507  -1621   -447  A    C  
ATOM    494  C   SER A 633     -28.851   3.296 -47.265  1.00 75.71      A    C  
ANISOU  494  C   SER A 633    12063  10197   6508    684  -1586   -340  A    C  
ATOM    495  O   SER A 633     -29.356   2.777 -48.251  1.00 81.54      A    O  
ANISOU  495  O   SER A 633    12990  11026   6965    864  -1842   -561  A    O  
ATOM    496  CB  SER A 633     -28.499   1.263 -45.863  1.00 90.74      A    C  
ANISOU  496  CB  SER A 633    13860  11703   8914    653  -1672   -793  A    C  
ATOM    497  OG  SER A 633     -29.316   0.400 -46.636  1.00 98.15      A    O  
ANISOU  497  OG  SER A 633    14950  12568   9775    786  -2045  -1107  A    O  
ATOM    498  N   VAL A 637     -33.361  -1.681 -51.006  1.00103.81      A    N  
ANISOU  498  N   VAL A 637    16402  13125   9917   1480  -4094  -2402  A    N  
ATOM    499  CA  VAL A 637     -32.369  -2.120 -50.011  1.00108.56      A    C  
ANISOU  499  CA  VAL A 637    16862  13638  10747   1384  -3723  -2352  A    C  
ATOM    500  C   VAL A 637     -33.004  -2.165 -48.607  1.00108.45      A    C  
ANISOU  500  C   VAL A 637    16547  13211  11447   1008  -3702  -2135  A    C  
ATOM    501  O   VAL A 637     -33.598  -1.170 -48.173  1.00110.14      A    O  
ANISOU  501  O   VAL A 637    16617  13412  11818    800  -3601  -1802  A    O  
ATOM    502  CB  VAL A 637     -31.112  -1.193 -49.967  1.00112.96      A    C  
ANISOU  502  CB  VAL A 637    17425  14596  10897   1422  -3148  -2024  A    C  
ATOM    503  CG1 VAL A 637     -29.953  -1.888 -49.254  1.00111.28      A    C  
ANISOU  503  CG1 VAL A 637    17122  14335  10824   1442  -2864  -2115  A    C  
ATOM    504  CG2 VAL A 637     -30.666  -0.756 -51.363  1.00112.44      A    C  
ANISOU  504  CG2 VAL A 637    17623  15023  10076   1740  -3082  -2055  A    C  
ATOM    505  N   SER A 638     -32.879  -3.308 -47.920  1.00 97.07      A    N  
ANISOU  505  N   SER A 638    15015  11445  10421    942  -3799  -2319  A    N  
ATOM    506  CA  SER A 638     -33.359  -3.498 -46.535  1.00 85.39      A    C  
ANISOU  506  CA  SER A 638    13265   9615   9566    606  -3731  -2089  A    C  
ATOM    507  C   SER A 638     -32.289  -4.131 -45.668  1.00 85.33      A    C  
ANISOU  507  C   SER A 638    13216   9522   9683    586  -3475  -2071  A    C  
ATOM    508  O   SER A 638     -31.565  -5.013 -46.139  1.00 89.52      A    O  
ANISOU  508  O   SER A 638    13887  10048  10078    817  -3580  -2393  A    O  
ATOM    509  CB  SER A 638     -34.590  -4.390 -46.501  1.00 85.54      A    C  
ANISOU  509  CB  SER A 638    13172   9216  10114    486  -4219  -2269  A    C  
ATOM    510  OG  SER A 638     -35.707  -3.658 -46.931  1.00 95.95      A    O  
ANISOU  510  OG  SER A 638    14427  10561  11470    421  -4418  -2186  A    O  
ATOM    511  N   ILE A 639     -32.211  -3.692 -44.403  1.00 77.55      A    N  
ANISOU  511  N   ILE A 639    12042   8468   8955    335  -3170  -1722  A    N  
ATOM    512  CA  ILE A 639     -31.240  -4.215 -43.427  1.00 69.83      A    C  
ANISOU  512  CA  ILE A 639    11018   7398   8118    294  -2946  -1651  A    C  
ATOM    513  C   ILE A 639     -31.885  -4.512 -42.078  1.00 63.72      A    C  
ANISOU  513  C   ILE A 639    10039   6320   7851     -6  -2925  -1396  A    C  
ATOM    514  O   ILE A 639     -32.963  -4.008 -41.754  1.00 67.05      A    O  
ANISOU  514  O   ILE A 639    10310   6688   8478   -197  -2946  -1210  A    O  
ATOM    515  CB  ILE A 639     -30.038  -3.255 -43.214  1.00 70.59      A    C  
ANISOU  515  CB  ILE A 639    11128   7832   7863    359  -2504  -1463  A    C  
ATOM    516  CG1 ILE A 639     -30.471  -1.881 -42.654  1.00 65.61      A    C  
ANISOU  516  CG1 ILE A 639    10368   7324   7238    165  -2271  -1107  A    C  
ATOM    517  CG2 ILE A 639     -29.269  -3.083 -44.517  1.00 71.52      A    C  
ANISOU  517  CG2 ILE A 639    11424   8284   7467    662  -2457  -1672  A    C  
ATOM    518  CD1 ILE A 639     -29.319  -1.064 -42.118  1.00 62.71      A    C  
ANISOU  518  CD1 ILE A 639     9958   7162   6706    167  -1891   -905  A    C  
ATOM    519  N   GLN A 640     -31.179  -5.308 -41.291  1.00 63.15      A    N  
ANISOU  519  N   GLN A 640     9958   6079   7958    -27  -2866  -1373  A    N  
ATOM    520  CA  GLN A 640     -31.496  -5.491 -39.877  1.00 57.87      A    C  
ANISOU  520  CA  GLN A 640     9128   5217   7644   -287  -2741  -1054  A    C  
ATOM    521  C   GLN A 640     -31.022  -4.285 -39.084  1.00 48.10      A    C  
ANISOU  521  C   GLN A 640     7837   4257   6184   -346  -2334   -780  A    C  
ATOM    522  O   GLN A 640     -29.996  -3.679 -39.414  1.00 46.18      A    O  
ANISOU  522  O   GLN A 640     7679   4263   5602   -188  -2148   -832  A    O  
ATOM    523  CB  GLN A 640     -30.850  -6.769 -39.338  1.00 62.67      A    C  
ANISOU  523  CB  GLN A 640     9776   5535   8502   -268  -2863  -1106  A    C  
ATOM    524  CG  GLN A 640     -31.407  -8.031 -39.969  1.00 67.28      A    C  
ANISOU  524  CG  GLN A 640    10384   5746   9433   -236  -3326  -1374  A    C  
ATOM    525  CD  GLN A 640     -32.861  -8.244 -39.596  1.00 72.00      A    C  
ANISOU  525  CD  GLN A 640    10782   6085  10489   -523  -3493  -1171  A    C  
ATOM    526  NE2 GLN A 640     -33.773  -8.036 -40.547  1.00 81.53      A    N  
ANISOU  526  NE2 GLN A 640    11962   7291  11723   -500  -3744  -1358  A    N  
ATOM    527  OE1 GLN A 640     -33.160  -8.572 -38.452  1.00 81.33      A    O  
ANISOU  527  OE1 GLN A 640    11823   7089  11989   -760  -3389   -830  A    O  
ATOM    528  N   VAL A 641     -31.812  -3.914 -38.076  1.00 46.16      A    N  
ANISOU  528  N   VAL A 641     7428   3969   6141   -567  -2206   -497  A    N  
ATOM    529  CA  VAL A 641     -31.454  -2.874 -37.108  1.00 43.81      A    C  
ANISOU  529  CA  VAL A 641     7074   3881   5691   -620  -1868   -265  A    C  
ATOM    530  C   VAL A 641     -31.839  -3.307 -35.694  1.00 43.37      A    C  
ANISOU  530  C   VAL A 641     6907   3697   5874   -804  -1762      1  A    C  
ATOM    531  O   VAL A 641     -32.624  -4.241 -35.516  1.00 42.80      A    O  
ANISOU  531  O   VAL A 641     6750   3379   6133   -941  -1923     72  A    O  
ATOM    532  CB  VAL A 641     -32.106  -1.503 -37.439  1.00 42.93      A    C  
ANISOU  532  CB  VAL A 641     6881   3979   5453   -637  -1766   -209  A    C  
ATOM    533  CG1 VAL A 641     -31.573  -0.975 -38.758  1.00 45.60      A    C  
ANISOU  533  CG1 VAL A 641     7353   4492   5481   -452  -1821   -385  A    C  
ATOM    534  CG2 VAL A 641     -33.627  -1.564 -37.459  1.00 45.97      A    C  
ANISOU  534  CG2 VAL A 641     7092   4243   6132   -786  -1902   -151  A    C  
ATOM    535  N   ALA A 642     -31.289  -2.596 -34.709  1.00 40.73      A    N  
ANISOU  535  N   ALA A 642     6570   3535   5370   -802  -1500    156  A    N  
ATOM    536  CA  ALA A 642     -31.692  -2.717 -33.304  1.00 43.33      A    C  
ANISOU  536  CA  ALA A 642     6810   3857   5795   -942  -1336    430  A    C  
ATOM    537  C   ALA A 642     -32.354  -1.410 -32.914  1.00 40.34      A    C  
ANISOU  537  C   ALA A 642     6304   3710   5315   -967  -1127    503  A    C  
ATOM    538  O   ALA A 642     -31.775  -0.349 -33.128  1.00 42.56      A    O  
ANISOU  538  O   ALA A 642     6630   4162   5380   -853  -1045    405  A    O  
ATOM    539  CB  ALA A 642     -30.494  -2.983 -32.436  1.00 43.71      A    C  
ANISOU  539  CB  ALA A 642     6986   3922   5701   -870  -1257    498  A    C  
ATOM    540  N   VAL A 643     -33.560  -1.491 -32.356  1.00 41.56      A    N  
ANISOU  540  N   VAL A 643     6273   3855   5663  -1113  -1047    677  A    N  
ATOM    541  CA  VAL A 643     -34.369  -0.314 -32.056  1.00 43.08      A    C  
ANISOU  541  CA  VAL A 643     6301   4249   5818  -1114   -872    703  A    C  
ATOM    542  C   VAL A 643     -34.544  -0.217 -30.549  1.00 48.35      A    C  
ANISOU  542  C   VAL A 643     6904   5073   6393  -1149   -597    920  A    C  
ATOM    543  O   VAL A 643     -35.176  -1.086 -29.931  1.00 49.06      A    O  
ANISOU  543  O   VAL A 643     6887   5096   6658  -1295   -529   1155  A    O  
ATOM    544  CB  VAL A 643     -35.771  -0.361 -32.711  1.00 47.23      A    C  
ANISOU  544  CB  VAL A 643     6604   4689   6655  -1222   -988    694  A    C  
ATOM    545  CG1 VAL A 643     -36.512   0.964 -32.465  1.00 44.66      A    C  
ANISOU  545  CG1 VAL A 643     6102   4569   6299  -1175   -827    675  A    C  
ATOM    546  CG2 VAL A 643     -35.681  -0.645 -34.214  1.00 45.88      A    C  
ANISOU  546  CG2 VAL A 643     6527   4362   6543  -1171  -1312    473  A    C  
ATOM    547  N   LYS A 644     -34.035   0.871 -29.986  1.00 44.57      A    N  
ANISOU  547  N   LYS A 644     6481   4805   5648  -1012   -450    846  A    N  
ATOM    548  CA  LYS A 644     -34.151   1.169 -28.567  1.00 45.88      A    C  
ANISOU  548  CA  LYS A 644     6620   5184   5627   -974   -199    979  A    C  
ATOM    549  C   LYS A 644     -35.419   2.015 -28.308  1.00 48.41      A    C  
ANISOU  549  C   LYS A 644     6686   5680   6027   -967    -24    968  A    C  
ATOM    550  O   LYS A 644     -35.696   2.963 -29.049  1.00 45.60      A    O  
ANISOU  550  O   LYS A 644     6255   5323   5750   -901   -110    778  A    O  
ATOM    551  CB  LYS A 644     -32.890   1.906 -28.145  1.00 43.95      A    C  
ANISOU  551  CB  LYS A 644     6565   5040   5092   -800   -205    836  A    C  
ATOM    552  CG  LYS A 644     -32.762   2.156 -26.661  1.00 53.78      A    C  
ANISOU  552  CG  LYS A 644     7861   6510   6063   -706    -12    918  A    C  
ATOM    553  CD  LYS A 644     -31.367   2.665 -26.334  1.00 54.59      A    C  
ANISOU  553  CD  LYS A 644     8160   6632   5951   -548   -119    762  A    C  
ATOM    554  CE  LYS A 644     -31.221   2.836 -24.840  1.00 68.73      A    C  
ANISOU  554  CE  LYS A 644    10041   8651   7423   -425     17    817  A    C  
ATOM    555  NZ  LYS A 644     -29.792   3.052 -24.485  1.00 76.55      A    N1+
ANISOU  555  NZ  LYS A 644    11224   9606   8256   -290   -157    689  A    N1+
ATOM    556  N   MET A 645     -36.178   1.663 -27.269  1.00 52.33      A    N  
ANISOU  556  N   MET A 645     7042   6331   6509  -1026    225   1188  A    N  
ATOM    557  CA  MET A 645     -37.469   2.316 -26.942  1.00 56.79      A    C  
ANISOU  557  CA  MET A 645     7306   7090   7181  -1013    438   1192  A    C  
ATOM    558  C   MET A 645     -37.808   2.201 -25.465  1.00 61.68      A    C  
ANISOU  558  C   MET A 645     7864   8018   7554   -971    795   1400  A    C  
ATOM    559  O   MET A 645     -37.281   1.330 -24.766  1.00 62.35      A    O  
ANISOU  559  O   MET A 645     8111   8114   7464  -1026    859   1641  A    O  
ATOM    560  CB  MET A 645     -38.619   1.714 -27.766  1.00 58.49      A    C  
ANISOU  560  CB  MET A 645     7248   7122   7854  -1211    346   1292  A    C  
ATOM    561  CG  MET A 645     -38.998   0.274 -27.417  1.00 63.21      A    C  
ANISOU  561  CG  MET A 645     7759   7594   8666  -1443    401   1647  A    C  
ATOM    562  SD  MET A 645     -40.136  -0.530 -28.564  1.00 70.13      A    S  
ANISOU  562  SD  MET A 645     8340   8137  10167  -1683    143   1703  A    S  
ATOM    563  CE  MET A 645     -39.086  -0.793 -29.992  1.00 64.60      A    C  
ANISOU  563  CE  MET A 645     7966   7124   9455  -1625   -323   1410  A    C  
ATOM    564  N   LEU A 646     -38.708   3.069 -25.016  1.00 66.46      A    N  
ANISOU  564  N   LEU A 646     8233   8879   8139   -857   1022   1309  A    N  
ATOM    565  CA  LEU A 646     -39.212   3.043 -23.644  1.00 73.17      A    C  
ANISOU  565  CA  LEU A 646     8980  10104   8717   -780   1421   1489  A    C  
ATOM    566  C   LEU A 646     -40.407   2.103 -23.542  1.00 78.80      A    C  
ANISOU  566  C   LEU A 646     9353  10830   9756  -1024   1640   1867  A    C  
ATOM    567  O   LEU A 646     -41.099   1.862 -24.537  1.00 80.25      A    O  
ANISOU  567  O   LEU A 646     9306  10764  10421  -1192   1473   1865  A    O  
ATOM    568  CB  LEU A 646     -39.633   4.442 -23.191  1.00 75.38      A    C  
ANISOU  568  CB  LEU A 646     9136  10672   8834   -500   1572   1166  A    C  
ATOM    569  CG  LEU A 646     -38.518   5.487 -23.108  1.00 75.26      A    C  
ANISOU  569  CG  LEU A 646     9411  10645   8537   -251   1361    797  A    C  
ATOM    570  CD1 LEU A 646     -39.107   6.883 -22.993  1.00 77.07      A    C  
ANISOU  570  CD1 LEU A 646     9459  11026   8798     -1   1404    439  A    C  
ATOM    571  CD2 LEU A 646     -37.545   5.229 -21.965  1.00 75.57      A    C  
ANISOU  571  CD2 LEU A 646     9763  10874   8077   -124   1435    859  A    C  
ATOM    572  N   LYS A 647     -40.648   1.605 -22.326  1.00 89.64      A    N  
ANISOU  572  N   LYS A 647    10691  12504  10863  -1034   2006   2198  A    N  
ATOM    573  CA  LYS A 647     -41.869   0.844 -21.996  1.00 92.84      A    C  
ANISOU  573  CA  LYS A 647    10706  13007  11563  -1256   2319   2616  A    C  
ATOM    574  C   LYS A 647     -43.056   1.803 -21.874  1.00 95.84      A    C  
ANISOU  574  C   LYS A 647    10674  13680  12062  -1119   2592   2436  A    C  
ATOM    575  O   LYS A 647     -42.864   2.999 -21.626  1.00 92.16      A    O  
ANISOU  575  O   LYS A 647    10286  13433  11296   -808   2623   2040  A    O  
ATOM    576  CB  LYS A 647     -41.690   0.056 -20.695  1.00 94.15      A    C  
ANISOU  576  CB  LYS A 647    10983  13445  11344  -1296   2656   3082  A    C  
ATOM    577  N   GLU A 648     -44.268   1.269 -22.050  1.00101.11      A    N  
ANISOU  577  N   GLU A 648    10881  14320  13215  -1347   2762   2715  A    N  
ATOM    578  CA  GLU A 648     -45.509   2.062 -22.005  1.00103.19      A    C  
ANISOU  578  CA  GLU A 648    10667  14834  13707  -1239   3017   2567  A    C  
ATOM    579  C   GLU A 648     -45.828   2.524 -20.584  1.00108.09      A    C  
ANISOU  579  C   GLU A 648    11192  16068  13809   -990   3585   2638  A    C  
ATOM    580  O   GLU A 648     -45.383   3.591 -20.162  1.00106.87      A    O  
ANISOU  580  O   GLU A 648    11243  16160  13205   -633   3611   2233  A    O  
ATOM    581  CB  GLU A 648     -46.690   1.259 -22.564  1.00108.03      A    C  
ANISOU  581  CB  GLU A 648    10776  15229  15043  -1576   3023   2878  A    C  
ATOM    582  N   ASP A 651     -42.804   7.813 -18.493  1.00 94.13      A    N  
ANISOU  582  N   ASP A 651    10682  15135   9950    800   3222    445  A    N  
ATOM    583  CA  ASP A 651     -43.147   9.200 -18.151  1.00104.86      A    C  
ANISOU  583  CA  ASP A 651    11925  16698  11221   1213   3238   -101  A    C  
ATOM    584  C   ASP A 651     -42.456  10.220 -19.065  1.00104.36      A    C  
ANISOU  584  C   ASP A 651    12028  16174  11449   1295   2682   -539  A    C  
ATOM    585  O   ASP A 651     -41.592   9.854 -19.863  1.00110.48      A    O  
ANISOU  585  O   ASP A 651    13046  16545  12384   1059   2328   -419  A    O  
ATOM    586  CB  ASP A 651     -42.806   9.479 -16.680  1.00109.56      A    C  
ANISOU  586  CB  ASP A 651    12746  17816  11067   1585   3510   -256  A    C  
ATOM    587  N   SER A 652     -42.853  11.489 -18.947  1.00107.24      A    N  
ANISOU  587  N   SER A 652    12243  16604  11898   1634   2616  -1028  A    N  
ATOM    588  CA  SER A 652     -42.282  12.590 -19.753  1.00105.64      A    C  
ANISOU  588  CA  SER A 652    12161  15962  12016   1728   2093  -1424  A    C  
ATOM    589  C   SER A 652     -40.791  12.884 -19.476  1.00104.47      A    C  
ANISOU  589  C   SER A 652    12481  15654  11558   1820   1759  -1598  A    C  
ATOM    590  O   SER A 652     -40.071  13.329 -20.380  1.00 96.58      A    O  
ANISOU  590  O   SER A 652    11618  14208  10868   1714   1327  -1687  A    O  
ATOM    591  CB  SER A 652     -43.111  13.870 -19.581  1.00105.52      A    C  
ANISOU  591  CB  SER A 652    11855  16040  12199   2096   2091  -1910  A    C  
ATOM    592  N   SER A 653     -40.343  12.651 -18.238  1.00103.22      A    N  
ANISOU  592  N   SER A 653    12550  15871  10798   2020   1955  -1635  A    N  
ATOM    593  CA  SER A 653     -38.908  12.699 -17.882  1.00 99.39      A    C  
ANISOU  593  CA  SER A 653    12500  15258  10006   2077   1644  -1739  A    C  
ATOM    594  C   SER A 653     -38.071  11.591 -18.554  1.00 94.55      A    C  
ANISOU  594  C   SER A 653    12088  14355   9481   1677   1504  -1291  A    C  
ATOM    595  O   SER A 653     -36.910  11.823 -18.927  1.00 85.81      A    O  
ANISOU  595  O   SER A 653    11225  12924   8454   1631   1117  -1389  A    O  
ATOM    596  CB  SER A 653     -38.727  12.628 -16.358  1.00103.56      A    C  
ANISOU  596  CB  SER A 653    13228  16302   9817   2409   1886  -1866  A    C  
ATOM    597  N   GLU A 654     -38.663  10.401 -18.696  1.00 93.82      A    N  
ANISOU  597  N   GLU A 654    11866  14371   9410   1399   1811   -812  A    N  
ATOM    598  CA  GLU A 654     -38.012   9.246 -19.352  1.00 92.24      A    C  
ANISOU  598  CA  GLU A 654    11822  13890   9334   1034   1686   -400  A    C  
ATOM    599  C   GLU A 654     -37.837   9.522 -20.856  1.00 80.35      A    C  
ANISOU  599  C   GLU A 654    10243  11900   8385    828   1336   -448  A    C  
ATOM    600  O   GLU A 654     -36.791   9.240 -21.431  1.00 79.48      A    O  
ANISOU  600  O   GLU A 654    10355  11499   8345    688   1055   -385  A    O  
ATOM    601  CB  GLU A 654     -38.829   7.942 -19.183  1.00102.98      A    C  
ANISOU  601  CB  GLU A 654    13011  15428  10689    782   2065    115  A    C  
ATOM    602  CG  GLU A 654     -39.315   7.560 -17.778  1.00115.46      A    C  
ANISOU  602  CG  GLU A 654    14576  17553  11742    939   2527    300  A    C  
ATOM    603  CD  GLU A 654     -38.225   7.537 -16.723  1.00122.08      A    C  
ANISOU  603  CD  GLU A 654    15833  18585  11966   1158   2452    228  A    C  
ATOM    604  OE1 GLU A 654     -37.085   7.143 -17.038  1.00130.74      A    O  
ANISOU  604  OE1 GLU A 654    17220  19374  13081   1036   2116    290  A    O  
ATOM    605  OE2 GLU A 654     -38.518   7.893 -15.561  1.00130.49      A    O1-
ANISOU  605  OE2 GLU A 654    16931  20133  12515   1470   2728    104  A    O1-
ATOM    606  N   ARG A 655     -38.908  10.038 -21.464  1.00 77.58      A    N  
ANISOU  606  N   ARG A 655     9566  11501   8409    825   1376   -543  A    N  
ATOM    607  CA  ARG A 655     -38.966  10.508 -22.864  1.00 70.75      A    C  
ANISOU  607  CA  ARG A 655     8607  10235   8040    692   1051   -617  A    C  
ATOM    608  C   ARG A 655     -37.844  11.515 -23.191  1.00 62.73      A    C  
ANISOU  608  C   ARG A 655     7816   8952   7065    813    664   -905  A    C  
ATOM    609  O   ARG A 655     -37.101  11.340 -24.165  1.00 57.06      A    O  
ANISOU  609  O   ARG A 655     7231   7926   6523    627    408   -793  A    O  
ATOM    610  CB  ARG A 655     -40.357  11.137 -23.118  1.00 75.14      A    C  
ANISOU  610  CB  ARG A 655     8767  10856   8926    782   1157   -753  A    C  
ATOM    611  CG  ARG A 655     -40.736  11.415 -24.556  1.00 77.10      A    C  
ANISOU  611  CG  ARG A 655     8873  10743   9679    624    863   -739  A    C  
ATOM    612  N   GLU A 656     -37.708  12.527 -22.341  1.00 63.61      A    N  
ANISOU  612  N   GLU A 656     7961   9196   7013   1130    631  -1269  A    N  
ATOM    613  CA  GLU A 656     -36.683  13.566 -22.496  1.00 66.65      A    C  
ANISOU  613  CA  GLU A 656     8516   9310   7498   1258    246  -1558  A    C  
ATOM    614  C   GLU A 656     -35.250  13.029 -22.411  1.00 59.13      A    C  
ANISOU  614  C   GLU A 656     7873   8244   6349   1146     88  -1433  A    C  
ATOM    615  O   GLU A 656     -34.387  13.448 -23.187  1.00 52.91      A    O  
ANISOU  615  O   GLU A 656     7166   7124   5812   1050   -219  -1446  A    O  
ATOM    616  CB  GLU A 656     -36.884  14.683 -21.460  1.00 76.60      A    C  
ANISOU  616  CB  GLU A 656     9745  10741   8619   1657    220  -2025  A    C  
ATOM    617  CG  GLU A 656     -36.105  15.968 -21.714  1.00 84.04      A    C  
ANISOU  617  CG  GLU A 656    10764  11322   9845   1794   -232  -2363  A    C  
ATOM    618  CD  GLU A 656     -36.655  16.787 -22.876  1.00 88.98      A    C  
ANISOU  618  CD  GLU A 656    11173  11604  11032   1724   -449  -2385  A    C  
ATOM    619  OE1 GLU A 656     -37.258  17.843 -22.604  1.00 93.86      A    O  
ANISOU  619  OE1 GLU A 656    11631  12191  11841   1996   -553  -2747  A    O  
ATOM    620  OE2 GLU A 656     -36.486  16.391 -24.054  1.00 82.92      A    O1-
ANISOU  620  OE2 GLU A 656    10403  10600  10502   1422   -536  -2056  A    O1-
ATOM    621  N   ALA A 657     -35.009  12.108 -21.485  1.00 56.52      A    N  
ANISOU  621  N   ALA A 657     7696   8192   5589   1159    302  -1286  A    N  
ATOM    622  CA  ALA A 657     -33.687  11.451 -21.361  1.00 60.41      A    C  
ANISOU  622  CA  ALA A 657     8465   8584   5904   1058    151  -1145  A    C  
ATOM    623  C   ALA A 657     -33.307  10.651 -22.596  1.00 50.71      A    C  
ANISOU  623  C   ALA A 657     7244   7079   4945    732     70   -829  A    C  
ATOM    624  O   ALA A 657     -32.139  10.642 -23.016  1.00 47.51      A    O  
ANISOU  624  O   ALA A 657     6980   6447   4626    660   -170   -820  A    O  
ATOM    625  CB  ALA A 657     -33.638  10.551 -20.123  1.00 66.63      A    C  
ANISOU  625  CB  ALA A 657     9415   9731   6171   1139    396   -997  A    C  
ATOM    626  N   LEU A 658     -34.294   9.998 -23.198  1.00 49.44      A    N  
ANISOU  626  N   LEU A 658     6911   6938   4935    550    258   -592  A    N  
ATOM    627  CA  LEU A 658     -34.048   9.275 -24.450  1.00 46.63      A    C  
ANISOU  627  CA  LEU A 658     6561   6325   4830    281    151   -355  A    C  
ATOM    628  C   LEU A 658     -33.746  10.219 -25.610  1.00 40.13      A    C  
ANISOU  628  C   LEU A 658     5690   5221   4335    256   -116   -482  A    C  
ATOM    629  O   LEU A 658     -32.911   9.897 -26.454  1.00 39.16      A    O  
ANISOU  629  O   LEU A 658     5671   4905   4302    121   -267   -373  A    O  
ATOM    630  CB  LEU A 658     -35.216   8.344 -24.785  1.00 46.42      A    C  
ANISOU  630  CB  LEU A 658     6352   6362   4923    101    361    -99  A    C  
ATOM    631  CG  LEU A 658     -34.975   7.270 -25.833  1.00 49.24      A    C  
ANISOU  631  CG  LEU A 658     6757   6496   5454   -150    257    138  A    C  
ATOM    632  CD1 LEU A 658     -33.726   6.440 -25.591  1.00 49.03      A    C  
ANISOU  632  CD1 LEU A 658     6988   6405   5238   -197    180    250  A    C  
ATOM    633  CD2 LEU A 658     -36.177   6.346 -25.885  1.00 56.00      A    C  
ANISOU  633  CD2 LEU A 658     7411   7413   6453   -312    445    373  A    C  
ATOM    634  N   MET A 659     -34.429  11.365 -25.649  1.00 40.28      A    N  
ANISOU  634  N   MET A 659     5548   5227   4531    396   -168   -696  A    N  
ATOM    635  CA  MET A 659     -34.135  12.423 -26.635  1.00 41.40      A    C  
ANISOU  635  CA  MET A 659     5651   5088   4993    392   -445   -790  A    C  
ATOM    636  C   MET A 659     -32.720  12.983 -26.456  1.00 39.89      A    C  
ANISOU  636  C   MET A 659     5621   4743   4794    446   -664   -896  A    C  
ATOM    637  O   MET A 659     -32.025  13.245 -27.435  1.00 36.36      A    O  
ANISOU  637  O   MET A 659     5203   4070   4544    326   -839   -790  A    O  
ATOM    638  CB  MET A 659     -35.155  13.585 -26.554  1.00 43.32      A    C  
ANISOU  638  CB  MET A 659     5681   5317   5460    568   -494  -1022  A    C  
ATOM    639  CG  MET A 659     -36.494  13.306 -27.205  1.00 48.68      A    C  
ANISOU  639  CG  MET A 659     6136   6027   6331    483   -394   -909  A    C  
ATOM    640  SD  MET A 659     -36.405  12.872 -28.972  1.00 49.15      A    S  
ANISOU  640  SD  MET A 659     6230   5833   6613    218   -586   -627  A    S  
ATOM    641  CE  MET A 659     -35.557  14.324 -29.590  1.00 42.62      A    C  
ANISOU  641  CE  MET A 659     5473   4710   6012    287   -921   -718  A    C  
ATOM    642  N   SER A 660     -32.303  13.166 -25.207  1.00 38.99      A    N  
ANISOU  642  N   SER A 660     5600   4766   4450    632   -656  -1099  A    N  
ATOM    643  CA  SER A 660     -30.941  13.636 -24.934  1.00 39.99      A    C  
ANISOU  643  CA  SER A 660     5857   4734   4605    685   -902  -1220  A    C  
ATOM    644  C   SER A 660     -29.897  12.668 -25.455  1.00 43.19      A    C  
ANISOU  644  C   SER A 660     6384   5068   4961    488   -908   -964  A    C  
ATOM    645  O   SER A 660     -28.918  13.078 -26.093  1.00 37.74      A    O  
ANISOU  645  O   SER A 660     5691   4151   4499    409  -1100   -925  A    O  
ATOM    646  CB  SER A 660     -30.752  13.894 -23.458  1.00 40.30      A    C  
ANISOU  646  CB  SER A 660     5997   4962   4352    949   -920  -1509  A    C  
ATOM    647  OG  SER A 660     -31.544  15.038 -23.126  1.00 45.75      A    O  
ANISOU  647  OG  SER A 660     6555   5655   5173   1171   -986  -1824  A    O  
ATOM    648  N   GLU A 661     -30.132  11.381 -25.216  1.00 40.08      A    N  
ANISOU  648  N   GLU A 661     6068   4856   4303    408   -694   -774  A    N  
ATOM    649  CA  GLU A 661     -29.244  10.372 -25.721  1.00 38.41      A    C  
ANISOU  649  CA  GLU A 661     5961   4571   4063    249   -705   -561  A    C  
ATOM    650  C   GLU A 661     -29.204  10.408 -27.243  1.00 38.26      A    C  
ANISOU  650  C   GLU A 661     5859   4371   4305     78   -753   -412  A    C  
ATOM    651  O   GLU A 661     -28.139  10.273 -27.832  1.00 36.36      A    O  
ANISOU  651  O   GLU A 661     5657   4009   4150      6   -847   -338  A    O  
ATOM    652  CB  GLU A 661     -29.682   9.010 -25.218  1.00 40.73      A    C  
ANISOU  652  CB  GLU A 661     6336   5047   4094    192   -495   -373  A    C  
ATOM    653  CG  GLU A 661     -28.870   7.829 -25.728  1.00 42.73      A    C  
ANISOU  653  CG  GLU A 661     6692   5201   4343     48   -524   -173  A    C  
ATOM    654  CD  GLU A 661     -29.334   6.509 -25.105  1.00 49.53      A    C  
ANISOU  654  CD  GLU A 661     7631   6192   4996     -9   -357     36  A    C  
ATOM    655  OE1 GLU A 661     -29.902   6.496 -23.989  1.00 59.33      A    O  
ANISOU  655  OE1 GLU A 661     8897   7650   5997     89   -214     42  A    O  
ATOM    656  OE2 GLU A 661     -29.126   5.468 -25.743  1.00 44.56      A    O1-
ANISOU  656  OE2 GLU A 661     7036   5448   4448   -147   -370    203  A    O1-
ATOM    657  N   LEU A 662     -30.368  10.546 -27.865  1.00 40.20      A    N  
ANISOU  657  N   LEU A 662     5989   4627   4658     27   -681   -363  A    N  
ATOM    658  CA  LEU A 662     -30.443  10.665 -29.313  1.00 36.60      A    C  
ANISOU  658  CA  LEU A 662     5480   4030   4394   -100   -753   -232  A    C  
ATOM    659  C   LEU A 662     -29.605  11.842 -29.798  1.00 36.72      A    C  
ANISOU  659  C   LEU A 662     5465   3866   4622    -82   -939   -264  A    C  
ATOM    660  O   LEU A 662     -28.769  11.672 -30.696  1.00 34.08      A    O  
ANISOU  660  O   LEU A 662     5163   3456   4332   -178   -974   -119  A    O  
ATOM    661  CB  LEU A 662     -31.889  10.821 -29.784  1.00 34.98      A    C  
ANISOU  661  CB  LEU A 662     5138   3849   4303   -121   -712   -214  A    C  
ATOM    662  CG  LEU A 662     -32.136  11.174 -31.240  1.00 33.86      A    C  
ANISOU  662  CG  LEU A 662     4954   3574   4336   -206   -840   -102  A    C  
ATOM    663  CD1 LEU A 662     -31.472  10.168 -32.158  1.00 37.17      A    C  
ANISOU  663  CD1 LEU A 662     5496   3984   4642   -323   -834     54  A    C  
ATOM    664  CD2 LEU A 662     -33.632  11.221 -31.478  1.00 39.41      A    C  
ANISOU  664  CD2 LEU A 662     5504   4308   5164   -205   -827   -117  A    C  
ATOM    665  N   LYS A 663     -29.838  13.012 -29.201  1.00 36.00      A    N  
ANISOU  665  N   LYS A 663     5295   3706   4676     47  -1052   -452  A    N  
ATOM    666  CA  LYS A 663     -29.100  14.229 -29.572  1.00 38.78      A    C  
ANISOU  666  CA  LYS A 663     5585   3824   5323     52  -1272   -470  A    C  
ATOM    667  C   LYS A 663     -27.591  13.988 -29.406  1.00 41.19      A    C  
ANISOU  667  C   LYS A 663     5950   4076   5626      8  -1326   -428  A    C  
ATOM    668  O   LYS A 663     -26.827  14.303 -30.312  1.00 40.30      A    O  
ANISOU  668  O   LYS A 663     5786   3830   5697   -105  -1385   -246  A    O  
ATOM    669  CB  LYS A 663     -29.542  15.442 -28.767  1.00 36.64      A    C  
ANISOU  669  CB  LYS A 663     5229   3457   5234    234  -1434   -748  A    C  
ATOM    670  CG  LYS A 663     -30.970  15.939 -29.034  1.00 40.37      A    C  
ANISOU  670  CG  LYS A 663     5581   3933   5825    300  -1427   -807  A    C  
ATOM    671  CD  LYS A 663     -31.369  16.942 -27.950  1.00 41.58      A    C  
ANISOU  671  CD  LYS A 663     5661   4052   6085    549  -1554  -1175  A    C  
ATOM    672  CE  LYS A 663     -32.816  17.230 -27.902  1.00 41.89      A    C  
ANISOU  672  CE  LYS A 663     5557   4175   6185    668  -1486  -1297  A    C  
ATOM    673  NZ  LYS A 663     -33.152  18.040 -26.728  1.00 45.50      A    N1+
ANISOU  673  NZ  LYS A 663     5956   4671   6660    960  -1562  -1708  A    N1+
ATOM    674  N   MET A 664     -27.180  13.358 -28.306  1.00 40.40      A    N  
ANISOU  674  N   MET A 664     5948   4099   5304     95  -1290   -562  A    N  
ATOM    675  CA  MET A 664     -25.762  13.038 -28.110  1.00 38.55      A    C  
ANISOU  675  CA  MET A 664     5750   3810   5087     68  -1368   -538  A    C  
ATOM    676  C   MET A 664     -25.210  12.172 -29.261  1.00 38.44      A    C  
ANISOU  676  C   MET A 664     5740   3817   5049    -91  -1237   -276  A    C  
ATOM    677  O   MET A 664     -24.158  12.488 -29.818  1.00 39.28      A    O  
ANISOU  677  O   MET A 664     5758   3809   5358   -161  -1300   -174  A    O  
ATOM    678  CB  MET A 664     -25.524  12.386 -26.756  1.00 39.85      A    C  
ANISOU  678  CB  MET A 664     6051   4123   4966    203  -1368   -700  A    C  
ATOM    679  CG  MET A 664     -24.076  11.944 -26.487  1.00 47.20      A    C  
ANISOU  679  CG  MET A 664     7016   4995   5923    195  -1483   -688  A    C  
ATOM    680  SD  MET A 664     -23.924  10.954 -25.003  1.00 61.97      A    S  
ANISOU  680  SD  MET A 664     9098   7065   7383    350  -1484   -798  A    S  
ATOM    681  CE  MET A 664     -24.745   9.423 -25.480  1.00 67.47      A    C  
ANISOU  681  CE  MET A 664     9883   7929   7823    224  -1180   -528  A    C  
ATOM    682  N   MET A 665     -25.922  11.113 -29.614  1.00 34.86      A    N  
ANISOU  682  N   MET A 665     5368   3508   4372   -137  -1063   -180  A    N  
ATOM    683  CA  MET A 665     -25.458  10.187 -30.631  1.00 39.28      A    C  
ANISOU  683  CA  MET A 665     5956   4102   4867   -235   -963     -8  A    C  
ATOM    684  C   MET A 665     -25.471  10.788 -32.058  1.00 43.32      A    C  
ANISOU  684  C   MET A 665     6386   4561   5513   -322   -954    160  A    C  
ATOM    685  O   MET A 665     -24.650  10.392 -32.878  1.00 44.60      A    O  
ANISOU  685  O   MET A 665     6536   4754   5655   -366   -888    280  A    O  
ATOM    686  CB  MET A 665     -26.263   8.880 -30.582  1.00 40.22      A    C  
ANISOU  686  CB  MET A 665     6181   4339   4762   -255   -841     23  A    C  
ATOM    687  CG  MET A 665     -26.131   8.094 -29.285  1.00 42.86      A    C  
ANISOU  687  CG  MET A 665     6616   4741   4926   -190   -825    -42  A    C  
ATOM    688  SD  MET A 665     -24.455   7.605 -28.839  1.00 48.14      A    S  
ANISOU  688  SD  MET A 665     7334   5360   5597   -139   -922    -69  A    S  
ATOM    689  CE  MET A 665     -24.089   6.391 -30.127  1.00 53.36      A    C  
ANISOU  689  CE  MET A 665     8013   6009   6252   -215   -842     52  A    C  
ATOM    690  N   THR A 666     -26.363  11.745 -32.335  1.00 38.38      A    N  
ANISOU  690  N   THR A 666     5701   3870   5012   -326  -1019    172  A    N  
ATOM    691  CA  THR A 666     -26.330  12.481 -33.608  1.00 38.83      A    C  
ANISOU  691  CA  THR A 666     5694   3861   5198   -401  -1048    376  A    C  
ATOM    692  C   THR A 666     -25.061  13.337 -33.753  1.00 43.52      A    C  
ANISOU  692  C   THR A 666     6168   4323   6046   -448  -1112    490  A    C  
ATOM    693  O   THR A 666     -24.573  13.529 -34.865  1.00 51.07      A    O  
ANISOU  693  O   THR A 666     7079   5300   7025   -527  -1045    735  A    O  
ATOM    694  CB  THR A 666     -27.560  13.396 -33.842  1.00 37.89      A    C  
ANISOU  694  CB  THR A 666     5527   3654   5214   -384  -1159    375  A    C  
ATOM    695  CG2 THR A 666     -28.812  12.619 -33.909  1.00 37.55      A    C  
ANISOU  695  CG2 THR A 666     5539   3729   4997   -365  -1099    310  A    C  
ATOM    696  OG1 THR A 666     -27.654  14.406 -32.836  1.00 39.58      A    O  
ANISOU  696  OG1 THR A 666     5657   3719   5661   -303  -1306    197  A    O  
ATOM    697  N   GLN A 667     -24.563  13.851 -32.634  1.00 42.86      A    N  
ANISOU  697  N   GLN A 667     6022   4112   6149   -394  -1247    317  A    N  
ATOM    698  CA  GLN A 667     -23.393  14.721 -32.612  1.00 45.14      A    C  
ANISOU  698  CA  GLN A 667     6151   4216   6783   -448  -1369    396  A    C  
ATOM    699  C   GLN A 667     -22.056  14.005 -32.494  1.00 46.79      A    C  
ANISOU  699  C   GLN A 667     6312   4491   6976   -468  -1291    421  A    C  
ATOM    700  O   GLN A 667     -21.034  14.580 -32.828  1.00 43.80      A    O  
ANISOU  700  O   GLN A 667     5751   3995   6896   -552  -1327    575  A    O  
ATOM    701  CB  GLN A 667     -23.553  15.763 -31.497  1.00 48.88      A    C  
ANISOU  701  CB  GLN A 667     6570   4474   7529   -354  -1636    146  A    C  
ATOM    702  CG  GLN A 667     -24.759  16.707 -31.687  1.00 63.98      A    C  
ANISOU  702  CG  GLN A 667     8467   6265   9576   -318  -1752    118  A    C  
ATOM    703  CD  GLN A 667     -24.802  17.426 -33.052  1.00 75.09      A    C  
ANISOU  703  CD  GLN A 667     9783   7550  11196   -462  -1759    479  A    C  
ATOM    704  NE2 GLN A 667     -25.886  17.224 -33.824  1.00 70.75      A    N  
ANISOU  704  NE2 GLN A 667     9315   7111  10457   -466  -1675    588  A    N  
ATOM    705  OE1 GLN A 667     -23.867  18.152 -33.404  1.00 78.82      A    O  
ANISOU  705  OE1 GLN A 667    10107   7831  12009   -571  -1851    679  A    O  
ATOM    706  N   LEU A 668     -22.060  12.752 -32.057  1.00 43.33      A    N  
ANISOU  706  N   LEU A 668     6010   4223   6233   -397  -1190    294  A    N  
ATOM    707  CA  LEU A 668     -20.825  12.046 -31.767  1.00 44.61      A    C  
ANISOU  707  CA  LEU A 668     6124   4419   6407   -378  -1168    265  A    C  
ATOM    708  C   LEU A 668     -19.995  11.716 -33.034  1.00 47.11      A    C  
ANISOU  708  C   LEU A 668     6322   4836   6742   -455   -968    504  A    C  
ATOM    709  O   LEU A 668     -18.758  11.768 -33.000  1.00 41.56      A    O  
ANISOU  709  O   LEU A 668     5440   4092   6260   -474   -974    547  A    O  
ATOM    710  CB  LEU A 668     -21.166  10.790 -30.962  1.00 43.16      A    C  
ANISOU  710  CB  LEU A 668     6134   4361   5902   -277  -1139     96  A    C  
ATOM    711  CG  LEU A 668     -20.070   9.900 -30.428  1.00 45.67      A    C  
ANISOU  711  CG  LEU A 668     6453   4699   6200   -216  -1173     24  A    C  
ATOM    712  CD1 LEU A 668     -19.264  10.649 -29.363  1.00 47.47      A    C  
ANISOU  712  CD1 LEU A 668     6589   4772   6677   -159  -1429   -127  A    C  
ATOM    713  CD2 LEU A 668     -20.692   8.624 -29.894  1.00 44.33      A    C  
ANISOU  713  CD2 LEU A 668     6499   4642   5704   -150  -1122    -46  A    C  
ATOM    714  N   GLY A 669     -20.686  11.443 -34.149  1.00 46.66      A    N  
ANISOU  714  N   GLY A 669     6348   4921   6461   -486   -802    651  A    N  
ATOM    715  CA  GLY A 669     -20.079  10.905 -35.353  1.00 45.15      A    C  
ANISOU  715  CA  GLY A 669     6108   4912   6134   -497   -580    824  A    C  
ATOM    716  C   GLY A 669     -20.026   9.390 -35.217  1.00 46.16      A    C  
ANISOU  716  C   GLY A 669     6377   5172   5990   -388   -512    643  A    C  
ATOM    717  O   GLY A 669     -20.298   8.833 -34.158  1.00 45.51      A    O  
ANISOU  717  O   GLY A 669     6401   5022   5868   -336   -631    452  A    O  
ATOM    718  N   SER A 670     -19.662   8.733 -36.307  1.00 41.39      A    N  
ANISOU  718  N   SER A 670     5774   4758   5195   -342   -325    711  A    N  
ATOM    719  CA  SER A 670     -19.677   7.299 -36.392  1.00 42.78      A    C  
ANISOU  719  CA  SER A 670     6085   5027   5142   -225   -290    530  A    C  
ATOM    720  C   SER A 670     -18.263   6.765 -36.280  1.00 39.75      A    C  
ANISOU  720  C   SER A 670     5541   4686   4878   -143   -216    473  A    C  
ATOM    721  O   SER A 670     -17.294   7.454 -36.576  1.00 44.19      A    O  
ANISOU  721  O   SER A 670     5866   5285   5638   -182   -109    622  A    O  
ATOM    722  CB  SER A 670     -20.352   6.853 -37.701  1.00 46.86      A    C  
ANISOU  722  CB  SER A 670     6738   5725   5342   -175   -185    560  A    C  
ATOM    723  OG  SER A 670     -19.538   7.221 -38.789  1.00 55.06      A    O  
ANISOU  723  OG  SER A 670     7644   6960   6314   -149     26    735  A    O  
ATOM    724  N   HIS A 671     -18.158   5.515 -35.854  1.00 37.44      A    N  
ANISOU  724  N   HIS A 671     5356   4367   4503    -34   -285    270  A    N  
ATOM    725  CA  HIS A 671     -16.867   4.827 -35.786  1.00 35.76      A    C  
ANISOU  725  CA  HIS A 671     4996   4185   4408     84   -242    173  A    C  
ATOM    726  C   HIS A 671     -17.124   3.330 -35.941  1.00 37.66      A    C  
ANISOU  726  C   HIS A 671     5416   4428   4464    226   -293    -33  A    C  
ATOM    727  O   HIS A 671     -18.195   2.830 -35.545  1.00 39.35      A    O  
ANISOU  727  O   HIS A 671     5850   4536   4567    193   -431    -90  A    O  
ATOM    728  CB  HIS A 671     -16.164   5.214 -34.455  1.00 33.78      A    C  
ANISOU  728  CB  HIS A 671     4626   3746   4464     51   -430    141  A    C  
ATOM    729  CG  HIS A 671     -14.731   4.786 -34.378  1.00 34.11      A    C  
ANISOU  729  CG  HIS A 671     4436   3798   4725    156   -412     72  A    C  
ATOM    730  CD2 HIS A 671     -13.579   5.423 -34.703  1.00 36.17      A    C  
ANISOU  730  CD2 HIS A 671     4363   4111   5267    136   -297    177  A    C  
ATOM    731  ND1 HIS A 671     -14.362   3.537 -33.941  1.00 33.79      A    N  
ANISOU  731  ND1 HIS A 671     4471   3697   4671    303   -528   -115  A    N  
ATOM    732  CE1 HIS A 671     -13.046   3.424 -33.969  1.00 35.70      A    C  
ANISOU  732  CE1 HIS A 671     4439   3957   5170    390   -500   -157  A    C  
ATOM    733  NE2 HIS A 671     -12.548   4.559 -34.425  1.00 36.96      A    N  
ANISOU  733  NE2 HIS A 671     4331   4194   5517    284   -345     22  A    N  
ATOM    734  N   GLU A 672     -16.177   2.621 -36.547  1.00 39.21      A    N  
ANISOU  734  N   GLU A 672     5499   4739   4658    386   -183   -144  A    N  
ATOM    735  CA  GLU A 672     -16.326   1.179 -36.815  1.00 46.41      A    C  
ANISOU  735  CA  GLU A 672     6565   5623   5447    554   -264   -379  A    C  
ATOM    736  C   GLU A 672     -16.583   0.332 -35.535  1.00 41.92      A    C  
ANISOU  736  C   GLU A 672     6143   4772   5011    545   -548   -468  A    C  
ATOM    737  O   GLU A 672     -17.305  -0.656 -35.574  1.00 44.50      A    O  
ANISOU  737  O   GLU A 672     6664   4986   5257    582   -680   -575  A    O  
ATOM    738  CB  GLU A 672     -15.094   0.610 -37.574  1.00 53.74      A    C  
ANISOU  738  CB  GLU A 672     7300   6723   6396    774   -101   -527  A    C  
ATOM    739  CG  GLU A 672     -15.429  -0.641 -38.397  1.00 65.11      A    C  
ANISOU  739  CG  GLU A 672     8910   8208   7619    982   -139   -796  A    C  
ATOM    740  CD  GLU A 672     -14.229  -1.510 -38.781  1.00 77.44      A    C  
ANISOU  740  CD  GLU A 672    10301   9857   9264   1256    -69  -1042  A    C  
ATOM    741  OE1 GLU A 672     -13.068  -1.030 -38.783  1.00 83.40      A    O  
ANISOU  741  OE1 GLU A 672    10750  10749  10187   1295    120   -971  A    O  
ATOM    742  OE2 GLU A 672     -14.459  -2.697 -39.109  1.00 71.78      A    O1-
ANISOU  742  OE2 GLU A 672     9738   9057   8479   1443   -218  -1325  A    O1-
ATOM    743  N   ASN A 673     -15.949   0.732 -34.441  1.00 41.76      A    N  
ANISOU  743  N   ASN A 673     6021   4640   5205    500   -651   -407  A    N  
ATOM    744  CA  ASN A 673     -16.042   0.093 -33.115  1.00 41.20      A    C  
ANISOU  744  CA  ASN A 673     6087   4344   5224    499   -912   -431  A    C  
ATOM    745  C   ASN A 673     -16.993   0.706 -32.070  1.00 40.07      A    C  
ANISOU  745  C   ASN A 673     6093   4125   5005    344  -1011   -297  A    C  
ATOM    746  O   ASN A 673     -16.802   0.508 -30.838  1.00 36.83      A    O  
ANISOU  746  O   ASN A 673     5757   3592   4646    356  -1201   -279  A    O  
ATOM    747  CB  ASN A 673     -14.629  -0.028 -32.563  1.00 38.68      A    C  
ANISOU  747  CB  ASN A 673     5573   3963   5161    612  -1011   -500  A    C  
ATOM    748  CG  ASN A 673     -13.694  -0.753 -33.520  1.00 40.44      A    C  
ANISOU  748  CG  ASN A 673     5624   4274   5469    806   -901   -666  A    C  
ATOM    749  ND2 ASN A 673     -14.051  -1.956 -33.898  1.00 42.06      A    N  
ANISOU  749  ND2 ASN A 673     5986   4405   5589    924   -974   -813  A    N  
ATOM    750  OD1 ASN A 673     -12.643  -0.239 -33.875  1.00 45.08      A    O  
ANISOU  750  OD1 ASN A 673     5918   4984   6227    857   -763   -668  A    O  
ATOM    751  N   ILE A 674     -18.008   1.426 -32.564  1.00 38.40      A    N  
ANISOU  751  N   ILE A 674     5929   4006   4657    227   -889   -212  A    N  
ATOM    752  CA  ILE A 674     -19.148   1.905 -31.782  1.00 39.46      A    C  
ANISOU  752  CA  ILE A 674     6195   4103   4693    107   -939   -119  A    C  
ATOM    753  C   ILE A 674     -20.422   1.359 -32.449  1.00 37.74      A    C  
ANISOU  753  C   ILE A 674     6110   3894   4334     50   -893   -102  A    C  
ATOM    754  O   ILE A 674     -20.451   1.201 -33.656  1.00 34.50      A    O  
ANISOU  754  O   ILE A 674     5675   3564   3871     87   -807   -155  A    O  
ATOM    755  CB  ILE A 674     -19.182   3.442 -31.755  1.00 41.04      A    C  
ANISOU  755  CB  ILE A 674     6275   4369   4952     27   -879    -51  A    C  
ATOM    756  CG1 ILE A 674     -17.874   4.016 -31.200  1.00 45.92      A    C  
ANISOU  756  CG1 ILE A 674     6717   4941   5790     73   -966    -83  A    C  
ATOM    757  CG2 ILE A 674     -20.380   3.982 -30.982  1.00 47.32      A    C  
ANISOU  757  CG2 ILE A 674     7183   5149   5646    -51   -918     -7  A    C  
ATOM    758  CD1 ILE A 674     -17.583   3.751 -29.746  1.00 48.47      A    C  
ANISOU  758  CD1 ILE A 674     7132   5159   6125    134  -1189   -145  A    C  
ATOM    759  N   VAL A 675     -21.462   1.079 -31.654  1.00 34.55      A    N  
ANISOU  759  N   VAL A 675     5834   3422   3870    -29   -954    -29  A    N  
ATOM    760  CA  VAL A 675     -22.810   0.816 -32.164  1.00 32.96      A    C  
ANISOU  760  CA  VAL A 675     5701   3216   3607   -119   -927      9  A    C  
ATOM    761  C   VAL A 675     -23.364   2.177 -32.584  1.00 37.68      A    C  
ANISOU  761  C   VAL A 675     6219   3935   4164   -182   -823     49  A    C  
ATOM    762  O   VAL A 675     -23.717   3.002 -31.741  1.00 40.93      A    O  
ANISOU  762  O   VAL A 675     6609   4370   4574   -223   -811     99  A    O  
ATOM    763  CB  VAL A 675     -23.722   0.114 -31.116  1.00 41.14      A    C  
ANISOU  763  CB  VAL A 675     6840   4153   4637   -200   -988    127  A    C  
ATOM    764  CG1 VAL A 675     -25.137  -0.122 -31.648  1.00 41.78      A    C  
ANISOU  764  CG1 VAL A 675     6925   4211   4737   -311   -970    172  A    C  
ATOM    765  CG2 VAL A 675     -23.120  -1.231 -30.683  1.00 40.57      A    C  
ANISOU  765  CG2 VAL A 675     6855   3913   4645   -143  -1131    134  A    C  
ATOM    766  N   ASN A 676     -23.423   2.406 -33.899  1.00 37.46      A    N  
ANISOU  766  N   ASN A 676     6156   3985   4093   -166   -767     19  A    N  
ATOM    767  CA  ASN A 676     -23.775   3.704 -34.457  1.00 37.38      A    C  
ANISOU  767  CA  ASN A 676     6069   4068   4064   -215   -694     93  A    C  
ATOM    768  C   ASN A 676     -25.272   3.873 -34.625  1.00 37.30      A    C  
ANISOU  768  C   ASN A 676     6097   4044   4031   -295   -730    126  A    C  
ATOM    769  O   ASN A 676     -25.997   2.921 -34.960  1.00 36.46      A    O  
ANISOU  769  O   ASN A 676     6063   3887   3905   -309   -799     80  A    O  
ATOM    770  CB  ASN A 676     -23.080   3.928 -35.815  1.00 38.04      A    C  
ANISOU  770  CB  ASN A 676     6103   4283   4067   -149   -600    100  A    C  
ATOM    771  CG  ASN A 676     -21.573   3.897 -35.687  1.00 39.21      A    C  
ANISOU  771  CG  ASN A 676     6137   4465   4295    -73   -531     82  A    C  
ATOM    772  ND2 ASN A 676     -20.912   2.958 -36.389  1.00 36.00      A    N  
ANISOU  772  ND2 ASN A 676     5741   4129   3811     54   -487    -30  A    N  
ATOM    773  OD1 ASN A 676     -20.995   4.714 -34.950  1.00 38.28      A    O  
ANISOU  773  OD1 ASN A 676     5905   4302   4337   -112   -537    143  A    O  
ATOM    774  N   LEU A 677     -25.700   5.118 -34.423  1.00 38.18      A    N  
ANISOU  774  N   LEU A 677     6135   4177   4197   -341   -711    193  A    N  
ATOM    775  CA  LEU A 677     -27.051   5.573 -34.713  1.00 39.01      A    C  
ANISOU  775  CA  LEU A 677     6222   4278   4321   -398   -747    224  A    C  
ATOM    776  C   LEU A 677     -27.255   5.667 -36.203  1.00 39.75      A    C  
ANISOU  776  C   LEU A 677     6346   4435   4323   -381   -777    253  A    C  
ATOM    777  O   LEU A 677     -26.392   6.214 -36.915  1.00 37.56      A    O  
ANISOU  777  O   LEU A 677     6050   4237   3985   -344   -716    324  A    O  
ATOM    778  CB  LEU A 677     -27.288   6.959 -34.115  1.00 41.55      A    C  
ANISOU  778  CB  LEU A 677     6447   4584   4757   -410   -748    255  A    C  
ATOM    779  CG  LEU A 677     -28.742   7.453 -34.143  1.00 41.27      A    C  
ANISOU  779  CG  LEU A 677     6355   4535   4792   -443   -790    257  A    C  
ATOM    780  CD1 LEU A 677     -29.523   6.754 -33.041  1.00 39.15      A    C  
ANISOU  780  CD1 LEU A 677     6076   4274   4524   -461   -743    213  A    C  
ATOM    781  CD2 LEU A 677     -28.800   8.965 -34.019  1.00 47.36      A    C  
ANISOU  781  CD2 LEU A 677     7029   5260   5705   -422   -836    273  A    C  
ATOM    782  N   LEU A 678     -28.383   5.110 -36.659  1.00 39.58      A    N  
ANISOU  782  N   LEU A 678     6363   4384   4290   -406   -875    211  A    N  
ATOM    783  CA  LEU A 678     -28.826   5.183 -38.056  1.00 41.72      A    C  
ANISOU  783  CA  LEU A 678     6694   4719   4440   -368   -967    211  A    C  
ATOM    784  C   LEU A 678     -29.996   6.137 -38.303  1.00 39.78      A    C  
ANISOU  784  C   LEU A 678     6380   4447   4287   -413  -1064    283  A    C  
ATOM    785  O   LEU A 678     -30.128   6.649 -39.395  1.00 40.82      A    O  
ANISOU  785  O   LEU A 678     6560   4648   4300   -373  -1135    350  A    O  
ATOM    786  CB  LEU A 678     -29.202   3.782 -38.556  1.00 41.11      A    C  
ANISOU  786  CB  LEU A 678     6712   4594   4315   -334  -1097     60  A    C  
ATOM    787  CG  LEU A 678     -28.070   2.748 -38.542  1.00 43.33      A    C  
ANISOU  787  CG  LEU A 678     7068   4880   4516   -246  -1052    -51  A    C  
ATOM    788  CD1 LEU A 678     -28.599   1.438 -39.100  1.00 42.94      A    C  
ANISOU  788  CD1 LEU A 678     7109   4726   4480   -202  -1252   -233  A    C  
ATOM    789  CD2 LEU A 678     -26.829   3.198 -39.319  1.00 43.96      A    C  
ANISOU  789  CD2 LEU A 678     7169   5149   4384   -130   -911    -25  A    C  
ATOM    790  N   GLY A 679     -30.854   6.336 -37.309  1.00 40.76      A    N  
ANISOU  790  N   GLY A 679     6391   4486   4609   -479  -1068    271  A    N  
ATOM    791  CA  GLY A 679     -31.999   7.243 -37.434  1.00 38.39      A    C  
ANISOU  791  CA  GLY A 679     5984   4150   4455   -498  -1164    306  A    C  
ATOM    792  C   GLY A 679     -32.894   7.155 -36.218  1.00 36.03      A    C  
ANISOU  792  C   GLY A 679     5536   3805   4349   -545  -1106    259  A    C  
ATOM    793  O   GLY A 679     -32.602   6.428 -35.268  1.00 34.56      A    O  
ANISOU  793  O   GLY A 679     5355   3626   4149   -572   -989    239  A    O  
ATOM    794  N   ALA A 680     -34.008   7.863 -36.269  1.00 37.64      A    N  
ANISOU  794  N   ALA A 680     5600   3977   4725   -543  -1186    254  A    N  
ATOM    795  CA  ALA A 680     -34.935   7.901 -35.146  1.00 38.02      A    C  
ANISOU  795  CA  ALA A 680     5462   4034   4948   -561  -1087    209  A    C  
ATOM    796  C   ALA A 680     -36.337   8.252 -35.585  1.00 38.54      A    C  
ANISOU  796  C   ALA A 680     5346   4054   5243   -565  -1225    187  A    C  
ATOM    797  O   ALA A 680     -36.529   8.864 -36.630  1.00 38.92      A    O  
ANISOU  797  O   ALA A 680     5427   4049   5312   -528  -1422    208  A    O  
ATOM    798  CB  ALA A 680     -34.449   8.913 -34.115  1.00 39.89      A    C  
ANISOU  798  CB  ALA A 680     5663   4311   5182   -481   -967    166  A    C  
ATOM    799  N   CYS A 681     -37.305   7.861 -34.761  1.00 39.36      A    N  
ANISOU  799  N   CYS A 681     5247   4190   5519   -606  -1114    166  A    N  
ATOM    800  CA  CYS A 681     -38.729   8.148 -34.970  1.00 44.55      A    C  
ANISOU  800  CA  CYS A 681     5647   4812   6468   -609  -1213    132  A    C  
ATOM    801  C   CYS A 681     -39.152   8.849 -33.692  1.00 45.06      A    C  
ANISOU  801  C   CYS A 681     5514   4994   6615   -524   -985     69  A    C  
ATOM    802  O   CYS A 681     -39.093   8.254 -32.635  1.00 45.96      A    O  
ANISOU  802  O   CYS A 681     5588   5227   6647   -556   -739    106  A    O  
ATOM    803  CB  CYS A 681     -39.524   6.854 -35.200  1.00 45.62      A    C  
ANISOU  803  CB  CYS A 681     5668   4886   6779   -747  -1275    175  A    C  
ATOM    804  SG  CYS A 681     -38.774   5.750 -36.421  1.00 48.30      A    S  
ANISOU  804  SG  CYS A 681     6295   5111   6947   -801  -1513    172  A    S  
ATOM    805  N   THR A 682     -39.498  10.129 -33.795  1.00 45.32      A    N  
ANISOU  805  N   THR A 682     5447   4995   6779   -395  -1080    -27  A    N  
ATOM    806  CA  THR A 682     -39.714  11.005 -32.642  1.00 44.99      A    C  
ANISOU  806  CA  THR A 682     5257   5059   6778   -244   -906   -166  A    C  
ATOM    807  C   THR A 682     -41.004  11.824 -32.662  1.00 49.67      A    C  
ANISOU  807  C   THR A 682     5538   5632   7702   -131   -980   -288  A    C  
ATOM    808  O   THR A 682     -41.314  12.448 -31.638  1.00 51.73      A    O  
ANISOU  808  O   THR A 682     5642   6016   7995     27   -808   -449  A    O  
ATOM    809  CB  THR A 682     -38.538  12.000 -32.473  1.00 46.37      A    C  
ANISOU  809  CB  THR A 682     5631   5174   6814   -136   -969   -235  A    C  
ATOM    810  CG2 THR A 682     -37.188  11.262 -32.372  1.00 42.60      A    C  
ANISOU  810  CG2 THR A 682     5423   4724   6041   -224   -892   -136  A    C  
ATOM    811  OG1 THR A 682     -38.522  12.954 -33.557  1.00 45.94      A    O  
ANISOU  811  OG1 THR A 682     5608   4927   6920   -104  -1260   -208  A    O  
ATOM    812  N   LEU A 683     -41.747  11.833 -33.782  1.00 51.16      A    N  
ANISOU  812  N   LEU A 683     5633   5679   8127   -180  -1246   -242  A    N  
ATOM    813  CA  LEU A 683     -42.786  12.832 -34.025  1.00 59.57      A    C  
ANISOU  813  CA  LEU A 683     6438   6660   9538    -44  -1421   -362  A    C  
ATOM    814  C   LEU A 683     -44.213  12.313 -33.900  1.00 63.70      A    C  
ANISOU  814  C   LEU A 683     6574   7244  10385    -79  -1366   -386  A    C  
ATOM    815  O   LEU A 683     -45.043  12.996 -33.300  1.00 70.67      A    O  
ANISOU  815  O   LEU A 683     7148   8194  11509     76  -1276   -542  A    O  
ATOM    816  CB  LEU A 683     -42.568  13.509 -35.394  1.00 59.27      A    C  
ANISOU  816  CB  LEU A 683     6570   6396   9553    -32  -1824   -283  A    C  
ATOM    817  CG  LEU A 683     -41.296  14.372 -35.545  1.00 59.52      A    C  
ANISOU  817  CG  LEU A 683     6884   6334   9396     18  -1896   -232  A    C  
ATOM    818  CD1 LEU A 683     -41.246  14.986 -36.931  1.00 58.08      A    C  
ANISOU  818  CD1 LEU A 683     6838   5962   9267     17  -2264    -77  A    C  
ATOM    819  CD2 LEU A 683     -41.146  15.487 -34.507  1.00 61.05      A    C  
ANISOU  819  CD2 LEU A 683     6978   6509   9707    198  -1814   -425  A    C  
ATOM    820  N   SER A 684     -44.504  11.143 -34.468  1.00 63.00      A    N  
ANISOU  820  N   SER A 684     6476   7119  10342   -269  -1435   -251  A    N  
ATOM    821  CA  SER A 684     -45.895  10.666 -34.625  1.00 68.78      A    C  
ANISOU  821  CA  SER A 684     6809   7832  11491   -336  -1492   -250  A    C  
ATOM    822  C   SER A 684     -46.231   9.437 -33.767  1.00 72.39      A    C  
ANISOU  822  C   SER A 684     7071   8437  11996   -505  -1149   -124  A    C  
ATOM    823  O   SER A 684     -47.145   8.674 -34.101  1.00 77.97      A    O  
ANISOU  823  O   SER A 684     7506   9067  13053   -648  -1247    -53  A    O  
ATOM    824  CB  SER A 684     -46.164  10.380 -36.113  1.00 67.83      A    C  
ANISOU  824  CB  SER A 684     6786   7487  11499   -410  -1964   -211  A    C  
ATOM    825  OG  SER A 684     -45.516   9.198 -36.557  1.00 67.02      A    O  
ANISOU  825  OG  SER A 684     6946   7343  11176   -577  -2014   -103  A    O  
ATOM    826  N   GLY A 685     -45.521   9.272 -32.651  1.00 72.38      A    N  
ANISOU  826  N   GLY A 685     7192   8636  11674   -487   -774    -82  A    N  
ATOM    827  CA  GLY A 685     -45.622   8.065 -31.822  1.00 68.33      A    C  
ANISOU  827  CA  GLY A 685     6578   8259  11125   -660   -447    115  A    C  
ATOM    828  C   GLY A 685     -44.507   7.972 -30.785  1.00 66.05      A    C  
ANISOU  828  C   GLY A 685     6575   8157  10364   -609   -144    159  A    C  
ATOM    829  O   GLY A 685     -43.774   8.951 -30.586  1.00 58.96      A    O  
ANISOU  829  O   GLY A 685     5885   7299   9218   -422   -164     -7  A    O  
ATOM    830  N   PRO A 686     -44.358   6.793 -30.129  1.00 66.90      A    N  
ANISOU  830  N   PRO A 686     6694   8350  10376   -778     97    392  A    N  
ATOM    831  CA  PRO A 686     -43.273   6.634 -29.150  1.00 65.15      A    C  
ANISOU  831  CA  PRO A 686     6766   8296   9691   -723    338    448  A    C  
ATOM    832  C   PRO A 686     -41.870   6.781 -29.760  1.00 60.14      A    C  
ANISOU  832  C   PRO A 686     6575   7496   8782   -692     80    364  A    C  
ATOM    833  O   PRO A 686     -41.675   6.522 -30.947  1.00 59.61      A    O  
ANISOU  833  O   PRO A 686     6622   7193   8833   -779   -238    354  A    O  
ATOM    834  CB  PRO A 686     -43.502   5.225 -28.566  1.00 67.30      A    C  
ANISOU  834  CB  PRO A 686     6947   8615  10007   -948    562    777  A    C  
ATOM    835  CG  PRO A 686     -44.498   4.563 -29.454  1.00 71.91      A    C  
ANISOU  835  CG  PRO A 686     7244   8971  11107  -1152    353    872  A    C  
ATOM    836  CD  PRO A 686     -45.291   5.647 -30.111  1.00 69.36      A    C  
ANISOU  836  CD  PRO A 686     6692   8613  11047  -1013    172    629  A    C  
ATOM    837  N   ILE A 687     -40.919   7.218 -28.943  1.00 53.80      A    N  
ANISOU  837  N   ILE A 687     5997   6834   7611   -551    216    293  A    N  
ATOM    838  CA  ILE A 687     -39.564   7.485 -29.405  1.00 51.40      A    C  
ANISOU  838  CA  ILE A 687     6048   6396   7085   -509      9    214  A    C  
ATOM    839  C   ILE A 687     -38.865   6.166 -29.721  1.00 51.44      A    C  
ANISOU  839  C   ILE A 687     6257   6279   7010   -687    -55    398  A    C  
ATOM    840  O   ILE A 687     -38.822   5.281 -28.865  1.00 54.08      A    O  
ANISOU  840  O   ILE A 687     6598   6710   7239   -763    147    574  A    O  
ATOM    841  CB  ILE A 687     -38.763   8.331 -28.395  1.00 50.08      A    C  
ANISOU  841  CB  ILE A 687     6028   6384   6614   -305    124     59  A    C  
ATOM    842  CG1 ILE A 687     -39.408   9.716 -28.312  1.00 53.50      A    C  
ANISOU  842  CG1 ILE A 687     6272   6856   7198   -103     88   -184  A    C  
ATOM    843  CG2 ILE A 687     -37.289   8.484 -28.821  1.00 48.62      A    C  
ANISOU  843  CG2 ILE A 687     6164   6052   6258   -296    -76     21  A    C  
ATOM    844  CD1 ILE A 687     -38.902  10.556 -27.178  1.00 63.16      A    C  
ANISOU  844  CD1 ILE A 687     7579   8245   8172    135    193   -398  A    C  
ATOM    845  N   TYR A 688     -38.332   6.060 -30.945  1.00 45.65      A    N  
ANISOU  845  N   TYR A 688     5685   5342   6318   -732   -337    358  A    N  
ATOM    846  CA  TYR A 688     -37.488   4.941 -31.368  1.00 44.53      A    C  
ANISOU  846  CA  TYR A 688     5763   5070   6085   -838   -442    448  A    C  
ATOM    847  C   TYR A 688     -36.129   5.475 -31.760  1.00 40.43      A    C  
ANISOU  847  C   TYR A 688     5504   4524   5334   -736   -543    350  A    C  
ATOM    848  O   TYR A 688     -36.058   6.411 -32.544  1.00 44.25      A    O  
ANISOU  848  O   TYR A 688     6001   4967   5844   -666   -684    255  A    O  
ATOM    849  CB  TYR A 688     -38.102   4.204 -32.563  1.00 47.31      A    C  
ANISOU  849  CB  TYR A 688     6057   5230   6689   -959   -690    461  A    C  
ATOM    850  CG  TYR A 688     -39.471   3.537 -32.364  1.00 50.84      A    C  
ANISOU  850  CG  TYR A 688     6195   5636   7488  -1104   -654    578  A    C  
ATOM    851  CD1 TYR A 688     -39.925   3.108 -31.106  1.00 55.24      A    C  
ANISOU  851  CD1 TYR A 688     6578   6326   8083  -1177   -348    765  A    C  
ATOM    852  CD2 TYR A 688     -40.315   3.309 -33.471  1.00 56.49      A    C  
ANISOU  852  CD2 TYR A 688     6778   6178   8506  -1171   -941    517  A    C  
ATOM    853  CE1 TYR A 688     -41.183   2.502 -30.951  1.00 60.14      A    C  
ANISOU  853  CE1 TYR A 688     6860   6909   9082  -1336   -289    920  A    C  
ATOM    854  CE2 TYR A 688     -41.570   2.698 -33.326  1.00 61.99      A    C  
ANISOU  854  CE2 TYR A 688     7141   6802   9612  -1323   -942    626  A    C  
ATOM    855  CZ  TYR A 688     -42.007   2.293 -32.061  1.00 61.30      A    C  
ANISOU  855  CZ  TYR A 688     6839   6844   9607  -1420   -597    845  A    C  
ATOM    856  OH  TYR A 688     -43.245   1.677 -31.895  1.00 63.22      A    O  
ANISOU  856  OH  TYR A 688     6696   7020  10304  -1596   -561   1006  A    O  
ATOM    857  N   LEU A 689     -35.062   4.903 -31.199  1.00 37.76      A    N  
ANISOU  857  N   LEU A 689     5350   4201   4796   -732   -476    398  A    N  
ATOM    858  CA  LEU A 689     -33.688   5.149 -31.649  1.00 35.92      A    C  
ANISOU  858  CA  LEU A 689     5325   3924   4399   -663   -573    329  A    C  
ATOM    859  C   LEU A 689     -33.241   3.912 -32.404  1.00 36.67      A    C  
ANISOU  859  C   LEU A 689     5542   3891   4501   -735   -696    365  A    C  
ATOM    860  O   LEU A 689     -33.264   2.824 -31.849  1.00 39.46      A    O  
ANISOU  860  O   LEU A 689     5917   4196   4880   -808   -656    463  A    O  
ATOM    861  CB  LEU A 689     -32.735   5.416 -30.478  1.00 39.52      A    C  
ANISOU  861  CB  LEU A 689     5881   4475   4660   -573   -459    312  A    C  
ATOM    862  CG  LEU A 689     -32.708   6.834 -29.914  1.00 40.40      A    C  
ANISOU  862  CG  LEU A 689     5935   4673   4742   -439   -427    181  A    C  
ATOM    863  CD1 LEU A 689     -34.071   7.255 -29.412  1.00 40.76      A    C  
ANISOU  863  CD1 LEU A 689     5779   4828   4881   -411   -309    154  A    C  
ATOM    864  CD2 LEU A 689     -31.679   6.900 -28.788  1.00 39.94      A    C  
ANISOU  864  CD2 LEU A 689     6004   4687   4482   -342   -383    136  A    C  
ATOM    865  N   ILE A 690     -32.797   4.093 -33.645  1.00 37.77      A    N  
ANISOU  865  N   ILE A 690     5767   3979   4605   -697   -845    288  A    N  
ATOM    866  CA  ILE A 690     -32.507   2.991 -34.556  1.00 38.58      A    C  
ANISOU  866  CA  ILE A 690     5979   3976   4704   -714   -994    246  A    C  
ATOM    867  C   ILE A 690     -30.988   2.925 -34.645  1.00 35.48      A    C  
ANISOU  867  C   ILE A 690     5738   3618   4125   -622   -959    206  A    C  
ATOM    868  O   ILE A 690     -30.348   3.889 -35.080  1.00 38.18      A    O  
ANISOU  868  O   ILE A 690     6102   4044   4362   -552   -929    190  A    O  
ATOM    869  CB  ILE A 690     -33.130   3.219 -35.958  1.00 38.58      A    C  
ANISOU  869  CB  ILE A 690     5975   3950   4734   -695  -1188    169  A    C  
ATOM    870  CG1 ILE A 690     -34.656   3.427 -35.852  1.00 39.75      A    C  
ANISOU  870  CG1 ILE A 690     5918   4056   5128   -777  -1245    200  A    C  
ATOM    871  CG2 ILE A 690     -32.831   2.030 -36.874  1.00 37.82      A    C  
ANISOU  871  CG2 ILE A 690     6011   3757   4602   -666  -1369     58  A    C  
ATOM    872  CD1 ILE A 690     -35.277   4.117 -37.050  1.00 40.88      A    C  
ANISOU  872  CD1 ILE A 690     6044   4200   5288   -728  -1445    140  A    C  
ATOM    873  N   PHE A 691     -30.441   1.778 -34.247  1.00 36.43      A    N  
ANISOU  873  N   PHE A 691     5936   3653   4251   -630   -974    208  A    N  
ATOM    874  CA  PHE A 691     -29.014   1.483 -34.269  1.00 38.34      A    C  
ANISOU  874  CA  PHE A 691     6288   3904   4375   -533   -960    152  A    C  
ATOM    875  C   PHE A 691     -28.675   0.333 -35.223  1.00 39.33      A    C  
ANISOU  875  C   PHE A 691     6508   3930   4507   -473  -1110     21  A    C  
ATOM    876  O   PHE A 691     -29.539  -0.495 -35.566  1.00 41.14      A    O  
ANISOU  876  O   PHE A 691     6734   4019   4878   -531  -1262    -13  A    O  
ATOM    877  CB  PHE A 691     -28.553   1.058 -32.870  1.00 37.61      A    C  
ANISOU  877  CB  PHE A 691     6220   3780   4290   -548   -891    244  A    C  
ATOM    878  CG  PHE A 691     -28.623   2.143 -31.847  1.00 39.10      A    C  
ANISOU  878  CG  PHE A 691     6352   4091   4412   -542   -763    303  A    C  
ATOM    879  CD1 PHE A 691     -27.562   3.064 -31.705  1.00 42.85      A    C  
ANISOU  879  CD1 PHE A 691     6832   4637   4811   -452   -736    244  A    C  
ATOM    880  CD2 PHE A 691     -29.715   2.240 -30.990  1.00 37.21      A    C  
ANISOU  880  CD2 PHE A 691     6036   3898   4204   -612   -674    404  A    C  
ATOM    881  CE1 PHE A 691     -27.617   4.065 -30.736  1.00 39.99      A    C  
ANISOU  881  CE1 PHE A 691     6428   4356   4412   -418   -679    240  A    C  
ATOM    882  CE2 PHE A 691     -29.769   3.239 -30.009  1.00 42.22      A    C  
ANISOU  882  CE2 PHE A 691     6631   4669   4741   -554   -565    397  A    C  
ATOM    883  CZ  PHE A 691     -28.724   4.153 -29.886  1.00 38.51      A    C  
ANISOU  883  CZ  PHE A 691     6195   4235   4200   -449   -595    293  A    C  
ATOM    884  N   GLU A 692     -27.388   0.254 -35.564  1.00 40.22      A    N  
ANISOU  884  N   GLU A 692     6681   4099   4501   -346  -1079    -66  A    N  
ATOM    885  CA  GLU A 692     -26.804  -0.900 -36.254  1.00 44.29      A    C  
ANISOU  885  CA  GLU A 692     7284   4532   5013   -230  -1203   -238  A    C  
ATOM    886  C   GLU A 692     -27.067  -2.171 -35.459  1.00 43.41      A    C  
ANISOU  886  C   GLU A 692     7203   4172   5119   -297  -1340   -207  A    C  
ATOM    887  O   GLU A 692     -26.984  -2.150 -34.223  1.00 43.72      A    O  
ANISOU  887  O   GLU A 692     7222   4175   5217   -375  -1269    -37  A    O  
ATOM    888  CB  GLU A 692     -25.288  -0.778 -36.354  1.00 50.21      A    C  
ANISOU  888  CB  GLU A 692     8033   5389   5657    -86  -1098   -304  A    C  
ATOM    889  CG  GLU A 692     -24.759   0.325 -37.244  1.00 56.00      A    C  
ANISOU  889  CG  GLU A 692     8718   6361   6199    -15   -944   -294  A    C  
ATOM    890  CD  GLU A 692     -23.253   0.498 -37.125  1.00 55.67      A    C  
ANISOU  890  CD  GLU A 692     8597   6413   6141     91   -811   -308  A    C  
ATOM    891  OE1 GLU A 692     -22.705   0.424 -35.993  1.00 44.53      A    O  
ANISOU  891  OE1 GLU A 692     7143   4907   4869     62   -818   -258  A    O  
ATOM    892  OE2 GLU A 692     -22.604   0.760 -38.161  1.00 62.48      A    O1-
ANISOU  892  OE2 GLU A 692     9426   7466   6845    208   -694   -355  A    O1-
ATOM    893  N   TYR A 693     -27.370  -3.246 -36.181  1.00 39.72      A    N  
ANISOU  893  N   TYR A 693     6793   3535   4764   -254  -1555   -368  A    N  
ATOM    894  CA  TYR A 693     -27.614  -4.556 -35.615  1.00 42.68      A    C  
ANISOU  894  CA  TYR A 693     7191   3608   5417   -321  -1743   -332  A    C  
ATOM    895  C   TYR A 693     -26.285  -5.295 -35.594  1.00 43.40      A    C  
ANISOU  895  C   TYR A 693     7356   3622   5510   -144  -1807   -477  A    C  
ATOM    896  O   TYR A 693     -25.526  -5.252 -36.569  1.00 44.14      A    O  
ANISOU  896  O   TYR A 693     7485   3842   5444     58  -1804   -726  A    O  
ATOM    897  CB  TYR A 693     -28.621  -5.326 -36.475  1.00 46.24      A    C  
ANISOU  897  CB  TYR A 693     7646   3858   6066   -354  -2015   -477  A    C  
ATOM    898  CG  TYR A 693     -29.012  -6.695 -35.945  1.00 46.52      A    C  
ANISOU  898  CG  TYR A 693     7673   3511   6492   -464  -2253   -404  A    C  
ATOM    899  CD1 TYR A 693     -29.684  -6.829 -34.721  1.00 48.17      A    C  
ANISOU  899  CD1 TYR A 693     7785   3615   6901   -697  -2166    -44  A    C  
ATOM    900  CD2 TYR A 693     -28.755  -7.854 -36.679  1.00 50.07      A    C  
ANISOU  900  CD2 TYR A 693     8203   3699   7122   -331  -2573   -685  A    C  
ATOM    901  CE1 TYR A 693     -30.056  -8.082 -34.231  1.00 53.86      A    C  
ANISOU  901  CE1 TYR A 693     8483   3969   8014   -829  -2377    104  A    C  
ATOM    902  CE2 TYR A 693     -29.136  -9.122 -36.208  1.00 56.24      A    C  
ANISOU  902  CE2 TYR A 693     8963   4059   8345   -450  -2841   -595  A    C  
ATOM    903  CZ  TYR A 693     -29.783  -9.235 -34.979  1.00 57.12      A    C  
ANISOU  903  CZ  TYR A 693     8969   4058   8676   -719  -2737   -163  A    C  
ATOM    904  OH  TYR A 693     -30.158 -10.472 -34.495  1.00 62.52      A    O  
ANISOU  904  OH  TYR A 693     9617   4315   9822   -867  -2987      8  A    O  
ATOM    905  N   CYS A 694     -26.020  -5.969 -34.481  1.00 45.13      A    N  
ANISOU  905  N   CYS A 694     7601   5017   4532   -768  -2497    186  A    N  
ATOM    906  CA  CYS A 694     -24.811  -6.742 -34.268  1.00 43.09      A    C  
ANISOU  906  CA  CYS A 694     7522   4676   4176   -722  -2290     65  A    C  
ATOM    907  C   CYS A 694     -25.251  -8.196 -34.051  1.00 44.93      A    C  
ANISOU  907  C   CYS A 694     7820   4804   4446   -875  -2469     29  A    C  
ATOM    908  O   CYS A 694     -25.640  -8.580 -32.934  1.00 41.56      A    O  
ANISOU  908  O   CYS A 694     7137   4428   4225   -958  -2453     83  A    O  
ATOM    909  CB  CYS A 694     -24.068  -6.176 -33.078  1.00 43.82      A    C  
ANISOU  909  CB  CYS A 694     7379   4862   4406   -622  -1990     75  A    C  
ATOM    910  SG  CYS A 694     -23.448  -4.506 -33.357  1.00 44.92      A    S  
ANISOU  910  SG  CYS A 694     7506   5076   4484   -479  -1806    119  A    S  
ATOM    911  N   CYS A 695     -25.181  -8.985 -35.126  1.00 43.39      A    N  
ANISOU  911  N   CYS A 695     7996   4455   4036   -916  -2641    -58  A    N  
ATOM    912  CA  CYS A 695     -25.875 -10.271 -35.223  1.00 51.60      A    C  
ANISOU  912  CA  CYS A 695     9168   5353   5084  -1107  -2927    -74  A    C  
ATOM    913  C   CYS A 695     -25.452 -11.339 -34.226  1.00 46.74      A    C  
ANISOU  913  C   CYS A 695     8540   4656   4565  -1145  -2837   -120  A    C  
ATOM    914  O   CYS A 695     -26.255 -12.205 -33.937  1.00 54.28      A    O  
ANISOU  914  O   CYS A 695     9472   5536   5617  -1355  -3071    -69  A    O  
ATOM    915  CB  CYS A 695     -25.801 -10.854 -36.673  1.00 56.76      A    C  
ANISOU  915  CB  CYS A 695    10309   5823   5436  -1117  -3141   -183  A    C  
ATOM    916  SG  CYS A 695     -24.113 -11.140 -37.301  1.00 62.42      A    S  
ANISOU  916  SG  CYS A 695    11437   6440   5841   -851  -2841   -378  A    S  
ATOM    917  N   TYR A 696     -24.236 -11.274 -33.690  1.00 48.64      A    N  
ANISOU  917  N   TYR A 696     8784   4913   4784   -962  -2521   -197  A    N  
ATOM    918  CA  TYR A 696     -23.764 -12.264 -32.679  1.00 47.78      A    C  
ANISOU  918  CA  TYR A 696     8666   4721   4766   -972  -2434   -234  A    C  
ATOM    919  C   TYR A 696     -23.960 -11.883 -31.205  1.00 50.90      A    C  
ANISOU  919  C   TYR A 696     8643   5273   5422  -1013  -2285   -120  A    C  
ATOM    920  O   TYR A 696     -23.518 -12.629 -30.321  1.00 49.66      A    O  
ANISOU  920  O   TYR A 696     8480   5056   5332  -1015  -2203   -140  A    O  
ATOM    921  CB  TYR A 696     -22.306 -12.640 -32.971  1.00 49.92      A    C  
ANISOU  921  CB  TYR A 696     9211   4907   4848   -737  -2212   -392  A    C  
ATOM    922  CG  TYR A 696     -22.152 -13.255 -34.343  1.00 57.29      A    C  
ANISOU  922  CG  TYR A 696    10606   5664   5497   -686  -2363   -520  A    C  
ATOM    923  CD1 TYR A 696     -22.787 -14.470 -34.658  1.00 59.92      A    C  
ANISOU  923  CD1 TYR A 696    11229   5765   5772   -841  -2678   -563  A    C  
ATOM    924  CD2 TYR A 696     -21.424 -12.605 -35.354  1.00 55.71      A    C  
ANISOU  924  CD2 TYR A 696    10575   5524   5068   -501  -2208   -590  A    C  
ATOM    925  CE1 TYR A 696     -22.688 -15.031 -35.933  1.00 61.20      A    C  
ANISOU  925  CE1 TYR A 696    11864   5744   5646   -788  -2841   -695  A    C  
ATOM    926  CE2 TYR A 696     -21.310 -13.164 -36.624  1.00 56.76      A    C  
ANISOU  926  CE2 TYR A 696    11158   5502   4904   -440  -2338   -713  A    C  
ATOM    927  CZ  TYR A 696     -21.937 -14.374 -36.901  1.00 60.07      A    C  
ANISOU  927  CZ  TYR A 696    11884   5678   5262   -571  -2656   -776  A    C  
ATOM    928  OH  TYR A 696     -21.829 -14.922 -38.135  1.00 62.32      A    O  
ANISOU  928  OH  TYR A 696    12654   5791   5234   -501  -2798   -911  A    O  
ATOM    929  N   GLY A 697     -24.629 -10.754 -30.921  1.00 47.20      A    N  
ANISOU  929  N   GLY A 697     7851   4995   5087  -1032  -2256     -4  A    N  
ATOM    930  CA  GLY A 697     -24.963 -10.383 -29.523  1.00 40.77      A    C  
ANISOU  930  CA  GLY A 697     6655   4337   4498  -1064  -2127    103  A    C  
ATOM    931  C   GLY A 697     -23.765  -9.892 -28.745  1.00 39.25      A    C  
ANISOU  931  C   GLY A 697     6396   4198   4319   -881  -1814     51  A    C  
ATOM    932  O   GLY A 697     -22.767  -9.459 -29.337  1.00 39.81      A    O  
ANISOU  932  O   GLY A 697     6625   4249   4251   -725  -1675    -35  A    O  
ATOM    933  N   ASP A 698     -23.853  -9.960 -27.417  1.00 35.83      A    N  
ANISOU  933  N   ASP A 698     5726   3846   4043   -911  -1705    114  A    N  
ATOM    934  CA  ASP A 698     -22.823  -9.381 -26.563  1.00 36.59      A    C  
ANISOU  934  CA  ASP A 698     5727   4009   4167   -758  -1438     82  A    C  
ATOM    935  C   ASP A 698     -21.566 -10.261 -26.528  1.00 37.61      A    C  
ANISOU  935  C   ASP A 698     6081   4009   4201   -671  -1346    -28  A    C  
ATOM    936  O   ASP A 698     -21.641 -11.499 -26.648  1.00 36.69      A    O  
ANISOU  936  O   ASP A 698     6151   3742   4047   -747  -1479    -61  A    O  
ATOM    937  CB  ASP A 698     -23.337  -9.100 -25.139  1.00 38.05      A    C  
ANISOU  937  CB  ASP A 698     5608   4327   4523   -800  -1352    181  A    C  
ATOM    938  CG  ASP A 698     -23.601 -10.368 -24.340  1.00 37.64      A    C  
ANISOU  938  CG  ASP A 698     5555   4213   4532   -947  -1418    223  A    C  
ATOM    939  OD1 ASP A 698     -24.637 -11.004 -24.552  1.00 44.00      A    O  
ANISOU  939  OD1 ASP A 698     6337   5002   5380  -1133  -1616    300  A    O  
ATOM    940  OD2 ASP A 698     -22.749 -10.743 -23.520  1.00 42.04      A    O1-
ANISOU  940  OD2 ASP A 698     6147   4732   5093   -889  -1287    189  A    O1-
ATOM    941  N   LEU A 699     -20.437  -9.595 -26.339  1.00 33.15      A    N  
ANISOU  941  N   LEU A 699     5491   3503   3603   -513  -1132    -75  A    N  
ATOM    942  CA  LEU A 699     -19.132 -10.237 -26.329  1.00 38.88      A    C  
ANISOU  942  CA  LEU A 699     6371   4158   4243   -383  -1014   -172  A    C  
ATOM    943  C   LEU A 699     -18.947 -11.243 -25.175  1.00 38.35      A    C  
ANISOU  943  C   LEU A 699     6283   4025   4265   -412  -1017   -164  A    C  
ATOM    944  O   LEU A 699     -18.255 -12.249 -25.359  1.00 37.77      A    O  
ANISOU  944  O   LEU A 699     6416   3822   4112   -330  -1030   -247  A    O  
ATOM    945  CB  LEU A 699     -18.016  -9.169 -26.311  1.00 32.83      A    C  
ANISOU  945  CB  LEU A 699     5515   3512   3447   -244   -792   -188  A    C  
ATOM    946  CG  LEU A 699     -16.557  -9.619 -26.199  1.00 32.90      A    C  
ANISOU  946  CG  LEU A 699     5588   3519   3391    -89   -635   -265  A    C  
ATOM    947  CD1 LEU A 699     -16.103 -10.425 -27.396  1.00 38.19      A    C  
ANISOU  947  CD1 LEU A 699     6539   4095   3876     17   -658   -369  A    C  
ATOM    948  CD2 LEU A 699     -15.641  -8.429 -25.993  1.00 37.32      A    C  
ANISOU  948  CD2 LEU A 699     5987   4228   3965    -26   -444   -235  A    C  
ATOM    949  N   LEU A 700     -19.535 -10.974 -24.005  1.00 38.65      A    N  
ANISOU  949  N   LEU A 700     6092   4146   4447   -507  -1001    -67  A    N  
ATOM    950  CA  LEU A 700     -19.426 -11.902 -22.862  1.00 39.84      A    C  
ANISOU  950  CA  LEU A 700     6233   4237   4668   -555  -1009    -36  A    C  
ATOM    951  C   LEU A 700     -20.021 -13.266 -23.148  1.00 38.09      A    C  
ANISOU  951  C   LEU A 700     6218   3834   4421   -691  -1220    -31  A    C  
ATOM    952  O   LEU A 700     -19.334 -14.278 -22.964  1.00 38.13      A    O  
ANISOU  952  O   LEU A 700     6419   3688   4381   -631  -1244    -88  A    O  
ATOM    953  CB  LEU A 700     -20.071 -11.339 -21.589  1.00 37.47      A    C  
ANISOU  953  CB  LEU A 700     5663   4077   4496   -640   -945     77  A    C  
ATOM    954  CG  LEU A 700     -19.901 -12.154 -20.307  1.00 38.21      A    C  
ANISOU  954  CG  LEU A 700     5744   4133   4642   -690   -929    126  A    C  
ATOM    955  CD1 LEU A 700     -18.433 -12.279 -19.958  1.00 39.33      A    C  
ANISOU  955  CD1 LEU A 700     5965   4234   4743   -514   -813     44  A    C  
ATOM    956  CD2 LEU A 700     -20.668 -11.508 -19.171  1.00 37.04      A    C  
ANISOU  956  CD2 LEU A 700     5339   4150   4586   -764   -852    238  A    C  
ATOM    957  N   ASN A 701     -21.286 -13.280 -23.584  1.00 39.81      A    N  
ANISOU  957  N   ASN A 701     6395   4062   4670   -874  -1389     43  A    N  
ATOM    958  CA  ASN A 701     -21.966 -14.517 -24.058  1.00 44.64      A    C  
ANISOU  958  CA  ASN A 701     7229   4485   5249  -1054  -1645     56  A    C  
ATOM    959  C   ASN A 701     -21.267 -15.166 -25.253  1.00 43.32      A    C  
ANISOU  959  C   ASN A 701     7441   4115   4906   -931  -1729    -97  A    C  
ATOM    960  O   ASN A 701     -21.269 -16.393 -25.384  1.00 45.01      A    O  
ANISOU  960  O   ASN A 701     7935   4103   5064   -995  -1897   -132  A    O  
ATOM    961  CB  ASN A 701     -23.454 -14.276 -24.400  1.00 49.81      A    C  
ANISOU  961  CB  ASN A 701     7725   5227   5975  -1281  -1826    177  A    C  
ATOM    962  CG  ASN A 701     -24.345 -14.218 -23.155  1.00 62.31      A    C  
ANISOU  962  CG  ASN A 701     8990   6968   7718  -1454  -1798    348  A    C  
ATOM    963  ND2 ASN A 701     -25.128 -13.145 -23.019  1.00 57.35      A    N  
ANISOU  963  ND2 ASN A 701     8045   6570   7175  -1458  -1738    433  A    N  
ATOM    964  OD1 ASN A 701     -24.348 -15.147 -22.339  1.00 56.35      A    O  
ANISOU  964  OD1 ASN A 701     8287   6127   6997  -1573  -1832    407  A    O  
ATOM    965  N   TYR A 702     -20.686 -14.343 -26.121  1.00 42.35      A    N  
ANISOU  965  N   TYR A 702     7345   4065   4680   -754  -1613   -183  A    N  
ATOM    966  CA  TYR A 702     -19.940 -14.844 -27.283  1.00 45.84      A    C  
ANISOU  966  CA  TYR A 702     8137   4357   4921   -594  -1638   -335  A    C  
ATOM    967  C   TYR A 702     -18.711 -15.625 -26.813  1.00 44.46      A    C  
ANISOU  967  C   TYR A 702     8107   4081   4703   -396  -1521   -427  A    C  
ATOM    968  O   TYR A 702     -18.522 -16.765 -27.206  1.00 48.95      A    O  
ANISOU  968  O   TYR A 702     9009   4424   5165   -352  -1654   -516  A    O  
ATOM    969  CB  TYR A 702     -19.534 -13.686 -28.201  1.00 42.21      A    C  
ANISOU  969  CB  TYR A 702     7637   4042   4359   -457  -1497   -377  A    C  
ATOM    970  CG  TYR A 702     -18.774 -14.084 -29.444  1.00 45.34      A    C  
ANISOU  970  CG  TYR A 702     8377   4334   4518   -276  -1482   -524  A    C  
ATOM    971  CD1 TYR A 702     -19.444 -14.393 -30.633  1.00 48.14      A    C  
ANISOU  971  CD1 TYR A 702     9007   4565   4721   -351  -1698   -568  A    C  
ATOM    972  CD2 TYR A 702     -17.373 -14.125 -29.440  1.00 47.04      A    C  
ANISOU  972  CD2 TYR A 702     8634   4592   4647    -21  -1247   -615  A    C  
ATOM    973  CE1 TYR A 702     -18.738 -14.739 -31.783  1.00 50.85      A    C  
ANISOU  973  CE1 TYR A 702     9694   4819   4809   -162  -1665   -712  A    C  
ATOM    974  CE2 TYR A 702     -16.659 -14.491 -30.574  1.00 47.55      A    C  
ANISOU  974  CE2 TYR A 702     9000   4593   4474    177  -1197   -749  A    C  
ATOM    975  CZ  TYR A 702     -17.339 -14.787 -31.742  1.00 50.14      A    C  
ANISOU  975  CZ  TYR A 702     9631   4789   4630    114  -1396   -803  A    C  
ATOM    976  OH  TYR A 702     -16.614 -15.119 -32.851  1.00 56.34      A    O  
ANISOU  976  OH  TYR A 702    10735   5523   5150    332  -1324   -943  A    O  
ATOM    977  N   LEU A 703     -17.901 -14.993 -25.973  1.00 43.53      A    N  
ANISOU  977  N   LEU A 703     7748   4124   4669   -274  -1292   -404  A    N  
ATOM    978  CA  LEU A 703     -16.720 -15.633 -25.382  1.00 44.73      A    C  
ANISOU  978  CA  LEU A 703     7966   4221   4809    -79  -1181   -467  A    C  
ATOM    979  C   LEU A 703     -17.092 -16.929 -24.665  1.00 43.29      A    C  
ANISOU  979  C   LEU A 703     7951   3822   4677   -185  -1364   -439  A    C  
ATOM    980  O   LEU A 703     -16.455 -17.963 -24.879  1.00 47.49      A    O  
ANISOU  980  O   LEU A 703     8770   4160   5112    -30  -1418   -539  A    O  
ATOM    981  CB  LEU A 703     -16.009 -14.674 -24.429  1.00 43.26      A    C  
ANISOU  981  CB  LEU A 703     7453   4250   4734     -6   -959   -411  A    C  
ATOM    982  CG  LEU A 703     -15.295 -13.461 -25.051  1.00 44.31      A    C  
ANISOU  982  CG  LEU A 703     7447   4578   4809    118   -761   -436  A    C  
ATOM    983  CD1 LEU A 703     -14.955 -12.465 -23.965  1.00 41.32      A    C  
ANISOU  983  CD1 LEU A 703     6757   4378   4566     96   -618   -352  A    C  
ATOM    984  CD2 LEU A 703     -14.046 -13.829 -25.816  1.00 48.56      A    C  
ANISOU  984  CD2 LEU A 703     8137   5115   5199    374   -640   -554  A    C  
ATOM    985  N   ARG A 704     -18.167 -16.884 -23.880  1.00 46.05      A    N  
ANISOU  985  N   ARG A 704     8136   4198   5161   -448  -1465   -298  A    N  
ATOM    986  CA  ARG A 704     -18.633 -18.054 -23.116  1.00 44.22      A    C  
ANISOU  986  CA  ARG A 704     8042   3778   4984   -612  -1641   -227  A    C  
ATOM    987  C   ARG A 704     -19.085 -19.210 -23.981  1.00 49.08      A    C  
ANISOU  987  C   ARG A 704     9053   4106   5490   -702  -1910   -285  A    C  
ATOM    988  O   ARG A 704     -18.830 -20.352 -23.627  1.00 46.48      A    O  
ANISOU  988  O   ARG A 704     8987   3540   5135   -693  -2032   -303  A    O  
ATOM    989  CB  ARG A 704     -19.745 -17.669 -22.149  1.00 45.70      A    C  
ANISOU  989  CB  ARG A 704     7932   4108   5323   -885  -1662    -44  A    C  
ATOM    990  CG  ARG A 704     -19.208 -16.858 -20.995  1.00 43.79      A    C  
ANISOU  990  CG  ARG A 704     7398   4072   5168   -790  -1432      6  A    C  
ATOM    991  CD  ARG A 704     -20.294 -16.169 -20.215  1.00 43.85      A    C  
ANISOU  991  CD  ARG A 704     7090   4279   5294   -992  -1396    162  A    C  
ATOM    992  NE  ARG A 704     -19.729 -15.639 -18.993  1.00 41.75      A    N  
ANISOU  992  NE  ARG A 704     6636   4149   5080   -902  -1210    199  A    N  
ATOM    993  CZ  ARG A 704     -20.410 -15.135 -17.965  1.00 40.82      A    C  
ANISOU  993  CZ  ARG A 704     6271   4201   5040  -1017  -1131    324  A    C  
ATOM    994  NH1 ARG A 704     -21.748 -15.054 -17.971  1.00 38.28      A    N1+
ANISOU  994  NH1 ARG A 704     5797   3972   4774  -1229  -1205    444  A    N1+
ATOM    995  NH2 ARG A 704     -19.718 -14.716 -16.902  1.00 38.73      A    N  
ANISOU  995  NH2 ARG A 704     5907   4022   4786   -908   -979    330  A    N  
ATOM    996  N   SER A 705     -19.728 -18.908 -25.110  1.00 46.98      A    N  
ANISOU  996  N   SER A 705     8857   3843   5152   -782  -2019   -316  A    N  
ATOM    997  CA  SER A 705     -20.164 -19.942 -26.049  1.00 51.73      A    C  
ANISOU  997  CA  SER A 705     9875   4157   5623   -874  -2302   -386  A    C  
ATOM    998  C   SER A 705     -19.014 -20.581 -26.842  1.00 53.95      A    C  
ANISOU  998  C   SER A 705    10555   4244   5699   -543  -2270   -595  A    C  
ATOM    999  O   SER A 705     -19.236 -21.602 -27.490  1.00 59.11      A    O  
ANISOU  999  O   SER A 705    11633   4603   6223   -579  -2513   -677  A    O  
ATOM   1000  CB  SER A 705     -21.179 -19.370 -27.040  1.00 51.24      A    C  
ANISOU 1000  CB  SER A 705     9768   4172   5531  -1049  -2443   -356  A    C  
ATOM   1001  OG  SER A 705     -20.533 -18.456 -27.909  1.00 55.89      A    O  
ANISOU 1001  OG  SER A 705    10332   4901   6001   -807  -2258   -465  A    O  
ATOM   1002  N   LYS A 706     -17.836 -19.947 -26.848  1.00 56.48      A    N  
ANISOU 1002  N   LYS A 706    10742   4737   5980   -229  -1979   -678  A    N  
ATOM   1003  CA  LYS A 706     -16.649 -20.421 -27.572  1.00 61.19      A    C  
ANISOU 1003  CA  LYS A 706    11635   5230   6383    135  -1882   -867  A    C  
ATOM   1004  C   LYS A 706     -15.622 -21.138 -26.696  1.00 59.64      A    C  
ANISOU 1004  C   LYS A 706    11489   4949   6222    363  -1797   -904  A    C  
ATOM   1005  O   LYS A 706     -14.533 -21.429 -27.183  1.00 64.75      A    O  
ANISOU 1005  O   LYS A 706    12301   5573   6730    713  -1669  -1050  A    O  
ATOM   1006  CB  LYS A 706     -15.960 -19.231 -28.274  1.00 58.82      A    C  
ANISOU 1006  CB  LYS A 706    11135   5212   6003    334  -1606   -918  A    C  
ATOM   1007  CG  LYS A 706     -16.826 -18.492 -29.279  1.00 62.51      A    C  
ANISOU 1007  CG  LYS A 706    11598   5755   6399    168  -1685   -896  A    C  
ATOM   1008  CD  LYS A 706     -17.088 -19.274 -30.540  1.00 66.10      A    C  
ANISOU 1008  CD  LYS A 706    12533   5966   6617    206  -1890  -1032  A    C  
ATOM   1009  CE  LYS A 706     -17.978 -18.484 -31.497  1.00 65.84      A    C  
ANISOU 1009  CE  LYS A 706    12478   6020   6516     30  -1990   -992  A    C  
ATOM   1010  NZ  LYS A 706     -18.872 -19.393 -32.265  1.00 73.96      A    N1+
ANISOU 1010  NZ  LYS A 706    13922   6761   7417   -140  -2350  -1043  A    N1+
ATOM   1011  N   ARG A 707     -15.955 -21.438 -25.435  1.00 61.38      A    N  
ANISOU 1011  N   ARG A 707    11574   5134   6616    183  -1867   -769  A    N  
ATOM   1012  CA  ARG A 707     -15.002 -22.063 -24.485  1.00 65.17      A    C  
ANISOU 1012  CA  ARG A 707    12079   5541   7140    388  -1804   -780  A    C  
ATOM   1013  C   ARG A 707     -14.537 -23.465 -24.841  1.00 64.39      A    C  
ANISOU 1013  C   ARG A 707    12481   5085   6898    599  -1972   -916  A    C  
ATOM   1014  O   ARG A 707     -13.374 -23.804 -24.597  1.00 65.35      A    O  
ANISOU 1014  O   ARG A 707    12645   5198   6986    944  -1852  -1000  A    O  
ATOM   1015  CB  ARG A 707     -15.587 -22.132 -23.068  1.00 63.31      A    C  
ANISOU 1015  CB  ARG A 707    11640   5324   7091    116  -1868   -592  A    C  
ATOM   1016  CG  ARG A 707     -15.610 -20.807 -22.374  1.00 58.22      A    C  
ANISOU 1016  CG  ARG A 707    10508   5030   6583     41  -1648   -482  A    C  
ATOM   1017  CD  ARG A 707     -16.073 -20.955 -20.945  1.00 51.86      A    C  
ANISOU 1017  CD  ARG A 707     9544   4240   5920   -176  -1689   -312  A    C  
ATOM   1018  NE  ARG A 707     -16.029 -19.661 -20.277  1.00 47.51      A    N  
ANISOU 1018  NE  ARG A 707     8569   4010   5474   -207  -1476   -231  A    N  
ATOM   1019  CZ  ARG A 707     -16.467 -19.410 -19.042  1.00 46.00      A    C  
ANISOU 1019  CZ  ARG A 707     8166   3922   5391   -381  -1446    -84  A    C  
ATOM   1020  NH1 ARG A 707     -17.000 -20.361 -18.272  1.00 46.78      A    N1+
ANISOU 1020  NH1 ARG A 707     8403   3854   5516   -569  -1602     25  A    N1+
ATOM   1021  NH2 ARG A 707     -16.371 -18.183 -18.570  1.00 44.88      A    N  
ANISOU 1021  NH2 ARG A 707     7691   4048   5314   -370  -1259    -43  A    N  
ATOM   1022  N   GLU A 708     -15.462 -24.292 -25.319  1.00 71.43      A    N  
ANISOU 1022  N   GLU A 708    13744   5677   7719    383  -2270   -925  A    N  
ATOM   1023  CA  GLU A 708     -15.112 -25.627 -25.839  1.00 81.66      A    C  
ANISOU 1023  CA  GLU A 708    15609   6576   8842    583  -2470  -1079  A    C  
ATOM   1024  C   GLU A 708     -14.415 -25.524 -27.202  1.00 82.89      A    C  
ANISOU 1024  C   GLU A 708    15985   6746   8763    944  -2352  -1298  A    C  
ATOM   1025  O   GLU A 708     -13.557 -26.340 -27.500  1.00 88.51      A    O  
ANISOU 1025  O   GLU A 708    17039   7263   9328   1312  -2351  -1460  A    O  
ATOM   1026  CB  GLU A 708     -16.340 -26.547 -25.937  1.00 92.58      A    C  
ANISOU 1026  CB  GLU A 708    17353   7610  10213    197  -2861  -1011  A    C  
ATOM   1027  CG  GLU A 708     -16.836 -27.077 -24.601  1.00 96.39      A    C  
ANISOU 1027  CG  GLU A 708    17769   7984  10871    -98  -3004   -811  A    C  
ATOM   1028  N   LYS A 709     -14.769 -24.508 -27.998  1.00 84.44      A    N  
ANISOU 1028  N   LYS A 709    15982   7184   8916    856  -2241  -1298  A    N  
ATOM   1029  CA  LYS A 709     -14.271 -24.322 -29.371  1.00 84.12      A    C  
ANISOU 1029  CA  LYS A 709    16155   7180   8625   1138  -2130  -1482  A    C  
ATOM   1030  C   LYS A 709     -13.083 -23.332 -29.500  1.00 80.80      A    C  
ANISOU 1030  C   LYS A 709    15365   7148   8189   1462  -1724  -1516  A    C  
ATOM   1031  O   LYS A 709     -12.950 -22.666 -30.539  1.00 87.27      A    O  
ANISOU 1031  O   LYS A 709    16173   8132   8852   1550  -1585  -1581  A    O  
ATOM   1032  CB  LYS A 709     -15.458 -23.870 -30.259  1.00 90.00      A    C  
ANISOU 1032  CB  LYS A 709    16965   7923   9307    814  -2305  -1447  A    C  
ATOM   1033  CG  LYS A 709     -16.666 -24.803 -30.224  1.00 96.24      A    C  
ANISOU 1033  CG  LYS A 709    18092   8359  10115    449  -2727  -1395  A    C  
ATOM   1034  N   PHE A 710     -12.233 -23.225 -28.465  1.00 71.47      A    N  
ANISOU 1034  N   PHE A 710    13884   6113   7158   1618  -1548  -1459  A    N  
ATOM   1035  CA  PHE A 710     -11.031 -22.375 -28.506  1.00 66.21      A    C  
ANISOU 1035  CA  PHE A 710    12856   5810   6492   1906  -1189  -1473  A    C  
ATOM   1036  C   PHE A 710      -9.822 -23.216 -28.909  1.00 75.81      A    C  
ANISOU 1036  C   PHE A 710    14322   6948   7535   2404  -1081  -1649  A    C  
ATOM   1037  O   PHE A 710      -9.610 -24.283 -28.342  1.00 80.53      A    O  
ANISOU 1037  O   PHE A 710    15159   7283   8155   2538  -1232  -1691  A    O  
ATOM   1038  CB  PHE A 710     -10.769 -21.697 -27.157  1.00 66.43      A    C  
ANISOU 1038  CB  PHE A 710    12393   6066   6780   1786  -1071  -1305  A    C  
ATOM   1039  CG  PHE A 710      -9.672 -20.665 -27.207  1.00 64.79      A    C  
ANISOU 1039  CG  PHE A 710    11780   6246   6593   1982   -739  -1286  A    C  
ATOM   1040  CD1 PHE A 710      -9.955 -19.343 -27.533  1.00 62.82      A    C  
ANISOU 1040  CD1 PHE A 710    11233   6261   6373   1788   -601  -1200  A    C  
ATOM   1041  CD2 PHE A 710      -8.338 -21.023 -26.969  1.00 70.08      A    C  
ANISOU 1041  CD2 PHE A 710    12369   7013   7245   2364   -575  -1347  A    C  
ATOM   1042  CE1 PHE A 710      -8.937 -18.392 -27.601  1.00 63.00      A    C  
ANISOU 1042  CE1 PHE A 710    10902   6625   6410   1929   -315  -1165  A    C  
ATOM   1043  CE2 PHE A 710      -7.317 -20.075 -27.039  1.00 67.06      A    C  
ANISOU 1043  CE2 PHE A 710    11587   7008   6887   2510   -279  -1307  A    C  
ATOM   1044  CZ  PHE A 710      -7.616 -18.759 -27.346  1.00 60.47      A    C  
ANISOU 1044  CZ  PHE A 710    10475   6420   6082   2272   -153  -1212  A    C  
ATOM   1045  N   SER A 762      -9.027 -22.715 -29.860  1.00 83.51      A    N  
ANISOU 1045  N   SER A 762    15230   8162   8336   2683   -813  -1741  A    N  
ATOM   1046  CA  SER A 762      -7.810 -23.387 -30.359  1.00 91.09      A    C  
ANISOU 1046  CA  SER A 762    16371   9130   9108   3211   -645  -1910  A    C  
ATOM   1047  C   SER A 762      -6.552 -22.721 -29.804  1.00 94.83      A    C  
ANISOU 1047  C   SER A 762    16317  10006   9706   3431   -324  -1834  A    C  
ATOM   1048  O   SER A 762      -6.282 -21.552 -30.099  1.00 97.70      A    O  
ANISOU 1048  O   SER A 762    16309  10727  10086   3343    -87  -1748  A    O  
ATOM   1049  CB  SER A 762      -7.785 -23.350 -31.892  1.00 94.92      A    C  
ANISOU 1049  CB  SER A 762    17169   9625   9270   3386   -554  -2065  A    C  
ATOM   1050  OG  SER A 762      -6.638 -24.013 -32.415  1.00103.60      A    O  
ANISOU 1050  OG  SER A 762    18453  10748  10161   3930   -369  -2238  A    O  
ATOM   1051  N   ASN A 781     -16.567 -20.496 -36.773  1.00 96.84      A    N  
ANISOU 1051  N   ASN A 781    18358   9330   9107    874  -2167  -1732  A    N  
ATOM   1052  CA  ASN A 781     -16.809 -21.373 -35.624  1.00103.01      A    C  
ANISOU 1052  CA  ASN A 781    19115   9911  10114    751  -2334  -1687  A    C  
ATOM   1053  C   ASN A 781     -15.736 -21.279 -34.513  1.00104.56      A    C  
ANISOU 1053  C   ASN A 781    18965  10275  10487    973  -2023  -1655  A    C  
ATOM   1054  O   ASN A 781     -16.076 -21.040 -33.346  1.00105.58      A    O  
ANISOU 1054  O   ASN A 781    18725  10485  10907    761  -2035  -1497  A    O  
ATOM   1055  CB  ASN A 781     -16.939 -22.823 -36.094  1.00101.60      A    C  
ANISOU 1055  CB  ASN A 781    19575   9299   9731    821  -2634  -1858  A    C  
ATOM   1056  N   VAL A 782     -14.462 -21.450 -34.889  1.00 92.24      A    N  
ANISOU 1056  N   VAL A 782    17517   8787   8743   1398  -1748  -1800  A    N  
ATOM   1057  CA  VAL A 782     -13.329 -21.558 -33.936  1.00 85.27      A    C  
ANISOU 1057  CA  VAL A 782    16367   8035   7995   1660  -1487  -1794  A    C  
ATOM   1058  C   VAL A 782     -12.806 -20.165 -33.494  1.00 72.96      A    C  
ANISOU 1058  C   VAL A 782    14216   6906   6598   1642  -1157  -1650  A    C  
ATOM   1059  O   VAL A 782     -12.648 -19.261 -34.310  1.00 74.37      A    O  
ANISOU 1059  O   VAL A 782    14304   7305   6650   1668   -988  -1639  A    O  
ATOM   1060  CB  VAL A 782     -12.174 -22.428 -34.526  1.00 93.63      A    C  
ANISOU 1060  CB  VAL A 782    17794   8993   8788   2157  -1345  -2012  A    C  
ATOM   1061  CG1 VAL A 782     -11.031 -22.627 -33.527  1.00 90.24      A    C  
ANISOU 1061  CG1 VAL A 782    17086   8692   8511   2436  -1119  -1998  A    C  
ATOM   1062  CG2 VAL A 782     -12.695 -23.801 -34.965  1.00 97.15      A    C  
ANISOU 1062  CG2 VAL A 782    18890   8965   9056   2178  -1701  -2167  A    C  
ATOM   1063  N   LEU A 783     -12.536 -20.023 -32.196  1.00 66.94      A    N  
ANISOU 1063  N   LEU A 783    13090   6239   6103   1588  -1086  -1536  A    N  
ATOM   1064  CA  LEU A 783     -11.911 -18.827 -31.621  1.00 61.62      A    C  
ANISOU 1064  CA  LEU A 783    11892   5931   5589   1588   -799  -1410  A    C  
ATOM   1065  C   LEU A 783     -10.426 -19.084 -31.350  1.00 59.03      A    C  
ANISOU 1065  C   LEU A 783    11450   5745   5234   1973   -535  -1475  A    C  
ATOM   1066  O   LEU A 783     -10.065 -20.162 -30.894  1.00 63.39      A    O  
ANISOU 1066  O   LEU A 783    12189   6101   5794   2158   -617  -1553  A    O  
ATOM   1067  CB  LEU A 783     -12.642 -18.423 -30.332  1.00 59.10      A    C  
ANISOU 1067  CB  LEU A 783    11244   5639   5572   1263   -907  -1236  A    C  
ATOM   1068  CG  LEU A 783     -12.420 -17.000 -29.818  1.00 57.92      A    C  
ANISOU 1068  CG  LEU A 783    10607   5818   5582   1154   -697  -1093  A    C  
ATOM   1069  CD1 LEU A 783     -13.049 -15.971 -30.737  1.00 63.60      A    C  
ANISOU 1069  CD1 LEU A 783    11293   6653   6220    996   -690  -1048  A    C  
ATOM   1070  CD2 LEU A 783     -13.010 -16.857 -28.430  1.00 62.73      A    C  
ANISOU 1070  CD2 LEU A 783    10959   6420   6454    914   -796   -955  A    C  
ATOM   1071  N   THR A 784      -9.582 -18.087 -31.625  1.00 58.07      A    N  
ANISOU 1071  N   THR A 784    11014   5966   5086   2083   -231  -1429  A    N  
ATOM   1072  CA  THR A 784      -8.127 -18.163 -31.418  1.00 57.92      A    C  
ANISOU 1072  CA  THR A 784    10792   6164   5053   2431     45  -1459  A    C  
ATOM   1073  C   THR A 784      -7.630 -17.058 -30.508  1.00 54.45      A    C  
ANISOU 1073  C   THR A 784     9815   6029   4846   2296    212  -1288  A    C  
ATOM   1074  O   THR A 784      -8.347 -16.085 -30.262  1.00 49.63      A    O  
ANISOU 1074  O   THR A 784     9016   5484   4356   1971    162  -1163  A    O  
ATOM   1075  CB  THR A 784      -7.379 -18.001 -32.748  1.00 63.99      A    C  
ANISOU 1075  CB  THR A 784    11678   7108   5526   2712    294  -1557  A    C  
ATOM   1076  CG2 THR A 784      -7.756 -19.093 -33.708  1.00 64.54      A    C  
ANISOU 1076  CG2 THR A 784    12328   6874   5322   2892    139  -1751  A    C  
ATOM   1077  OG1 THR A 784      -7.707 -16.735 -33.330  1.00 66.65      A    O  
ANISOU 1077  OG1 THR A 784    11846   7653   5826   2475    393  -1448  A    O  
ATOM   1078  N   PHE A 785      -6.390 -17.208 -30.034  1.00 55.32      A    N  
ANISOU 1078  N   PHE A 785     9689   6322   5010   2559    399  -1286  A    N  
ATOM   1079  CA  PHE A 785      -5.665 -16.142 -29.312  1.00 57.65      A    C  
ANISOU 1079  CA  PHE A 785     9476   6940   5487   2466    578  -1130  A    C  
ATOM   1080  C   PHE A 785      -5.602 -14.804 -30.089  1.00 55.51      A    C  
ANISOU 1080  C   PHE A 785     9016   6933   5140   2304    764  -1036  A    C  
ATOM   1081  O   PHE A 785      -5.741 -13.732 -29.502  1.00 51.45      A    O  
ANISOU 1081  O   PHE A 785     8206   6551   4792   2036    774   -891  A    O  
ATOM   1082  CB  PHE A 785      -4.240 -16.605 -28.931  1.00 59.33      A    C  
ANISOU 1082  CB  PHE A 785     9480   7335   5728   2823    753  -1153  A    C  
ATOM   1083  CG  PHE A 785      -3.407 -15.526 -28.280  1.00 56.28      A    C  
ANISOU 1083  CG  PHE A 785     8575   7294   5513   2717    921   -989  A    C  
ATOM   1084  CD1 PHE A 785      -3.673 -15.113 -26.975  1.00 54.86      A    C  
ANISOU 1084  CD1 PHE A 785     8176   7087   5581   2466    781   -872  A    C  
ATOM   1085  CD2 PHE A 785      -2.381 -14.890 -28.986  1.00 60.70      A    C  
ANISOU 1085  CD2 PHE A 785     8879   8211   5973   2845   1212   -941  A    C  
ATOM   1086  CE1 PHE A 785      -2.913 -14.100 -26.378  1.00 57.26      A    C  
ANISOU 1086  CE1 PHE A 785     8043   7682   6032   2348    901   -726  A    C  
ATOM   1087  CE2 PHE A 785      -1.624 -13.877 -28.401  1.00 59.51      A    C  
ANISOU 1087  CE2 PHE A 785     8259   8367   5983   2701   1336   -774  A    C  
ATOM   1088  CZ  PHE A 785      -1.890 -13.477 -27.101  1.00 58.00      A    C  
ANISOU 1088  CZ  PHE A 785     7883   8115   6040   2450   1166   -673  A    C  
ATOM   1089  N   GLU A 786      -5.418 -14.895 -31.398  1.00 57.19      A    N  
ANISOU 1089  N   GLU A 786     9445   7200   5086   2468    895  -1121  A    N  
ATOM   1090  CA  GLU A 786      -5.334 -13.727 -32.267  1.00 60.45      A    C  
ANISOU 1090  CA  GLU A 786     9743   7845   5379   2332   1071  -1031  A    C  
ATOM   1091  C   GLU A 786      -6.679 -12.957 -32.289  1.00 54.10      A    C  
ANISOU 1091  C   GLU A 786     9019   6894   4641   1949    863   -954  A    C  
ATOM   1092  O   GLU A 786      -6.692 -11.722 -32.186  1.00 48.97      A    O  
ANISOU 1092  O   GLU A 786     8119   6413   4074   1722    932   -808  A    O  
ATOM   1093  CB  GLU A 786      -4.877 -14.133 -33.687  1.00 67.38      A    C  
ANISOU 1093  CB  GLU A 786    10893   8797   5913   2622   1255  -1151  A    C  
ATOM   1094  CG  GLU A 786      -3.392 -14.535 -33.796  1.00 83.01      A    C  
ANISOU 1094  CG  GLU A 786    12676  11051   7813   3013   1552  -1186  A    C  
ATOM   1095  CD  GLU A 786      -3.008 -15.922 -33.220  1.00 89.25      A    C  
ANISOU 1095  CD  GLU A 786    13602  11664   8646   3357   1467  -1332  A    C  
ATOM   1096  OE1 GLU A 786      -3.868 -16.826 -33.077  1.00 79.70      A    O  
ANISOU 1096  OE1 GLU A 786    12782  10073   7426   3353   1190  -1452  A    O  
ATOM   1097  OE2 GLU A 786      -1.815 -16.118 -32.903  1.00 99.06      A    O1-
ANISOU 1097  OE2 GLU A 786    14555  13150   9932   3633   1669  -1316  A    O1-
ATOM   1098  N   ASP A 787      -7.791 -13.694 -32.367  1.00 49.31      A    N  
ANISOU 1098  N   ASP A 787     8752   5973   4012   1880    595  -1044  A    N  
ATOM   1099  CA  ASP A 787      -9.143 -13.110 -32.253  1.00 49.12      A    C  
ANISOU 1099  CA  ASP A 787     8768   5811   4083   1540    368   -968  A    C  
ATOM   1100  C   ASP A 787      -9.360 -12.343 -30.935  1.00 46.20      A    C  
ANISOU 1100  C   ASP A 787     8037   5508   4011   1309    325   -824  A    C  
ATOM   1101  O   ASP A 787      -9.949 -11.261 -30.935  1.00 43.80      A    O  
ANISOU 1101  O   ASP A 787     7609   5261   3772   1078    293   -717  A    O  
ATOM   1102  CB  ASP A 787     -10.237 -14.193 -32.404  1.00 51.76      A    C  
ANISOU 1102  CB  ASP A 787     9486   5807   4373   1495     67  -1074  A    C  
ATOM   1103  CG  ASP A 787     -10.265 -14.843 -33.789  1.00 57.24      A    C  
ANISOU 1103  CG  ASP A 787    10617   6388   4745   1674     48  -1223  A    C  
ATOM   1104  OD1 ASP A 787      -9.836 -14.215 -34.777  1.00 64.14      A    O  
ANISOU 1104  OD1 ASP A 787    11513   7442   5417   1749    236  -1218  A    O  
ATOM   1105  OD2 ASP A 787     -10.723 -16.004 -33.889  1.00 63.11      A    O1-
ANISOU 1105  OD2 ASP A 787    11712   6847   5420   1735   -165  -1343  A    O1-
ATOM   1106  N   LEU A 788      -8.865 -12.897 -29.826  1.00 43.41      A    N  
ANISOU 1106  N   LEU A 788     7537   5138   3819   1392    321   -827  A    N  
ATOM   1107  CA  LEU A 788      -8.956 -12.241 -28.516  1.00 43.69      A    C  
ANISOU 1107  CA  LEU A 788     7257   5237   4106   1205    290   -704  A    C  
ATOM   1108  C   LEU A 788      -8.175 -10.923 -28.497  1.00 42.18      A    C  
ANISOU 1108  C   LEU A 788     6750   5324   3953   1139    491   -588  A    C  
ATOM   1109  O   LEU A 788      -8.654  -9.899 -28.005  1.00 43.42      A    O  
ANISOU 1109  O   LEU A 788     6750   5514   4233    910    446   -482  A    O  
ATOM   1110  CB  LEU A 788      -8.461 -13.173 -27.388  1.00 43.44      A    C  
ANISOU 1110  CB  LEU A 788     7166   5134   4204   1333    243   -731  A    C  
ATOM   1111  CG  LEU A 788      -9.182 -14.513 -27.143  1.00 44.85      A    C  
ANISOU 1111  CG  LEU A 788     7653   5009   4378   1362     18   -817  A    C  
ATOM   1112  CD1 LEU A 788      -8.613 -15.184 -25.904  1.00 44.53      A    C  
ANISOU 1112  CD1 LEU A 788     7511   4927   4480   1462    -17   -804  A    C  
ATOM   1113  CD2 LEU A 788     -10.689 -14.362 -26.982  1.00 44.65      A    C  
ANISOU 1113  CD2 LEU A 788     7722   4824   4421   1063   -199   -766  A    C  
ATOM   1114  N   LEU A 789      -6.973 -10.978 -29.041  1.00 44.08      A    N  
ANISOU 1114  N   LEU A 789     6908   5760   4080   1344    708   -605  A    N  
ATOM   1115  CA  LEU A 789      -6.115  -9.798 -29.230  1.00 46.78      A    C  
ANISOU 1115  CA  LEU A 789     6965   6385   4423   1271    912   -481  A    C  
ATOM   1116  C   LEU A 789      -6.788  -8.750 -30.131  1.00 46.28      A    C  
ANISOU 1116  C   LEU A 789     7001   6331   4250   1069    911   -415  A    C  
ATOM   1117  O   LEU A 789      -6.756  -7.552 -29.829  1.00 45.00      A    O  
ANISOU 1117  O   LEU A 789     6651   6266   4183    857    931   -283  A    O  
ATOM   1118  CB  LEU A 789      -4.764 -10.243 -29.816  1.00 55.23      A    C  
ANISOU 1118  CB  LEU A 789     7944   7683   5358   1559   1159   -515  A    C  
ATOM   1119  CG  LEU A 789      -3.437  -9.595 -29.447  1.00 62.30      A    C  
ANISOU 1119  CG  LEU A 789     8430   8903   6337   1568   1360   -388  A    C  
ATOM   1120  CD1 LEU A 789      -3.310  -9.324 -27.959  1.00 58.91      A    C  
ANISOU 1120  CD1 LEU A 789     7749   8459   6177   1425   1233   -311  A    C  
ATOM   1121  CD2 LEU A 789      -2.315 -10.519 -29.919  1.00 64.79      A    C  
ANISOU 1121  CD2 LEU A 789     8701   9392   6526   1946   1561   -468  A    C  
ATOM   1122  N   CYS A 790      -7.426  -9.215 -31.207  1.00 45.92      A    N  
ANISOU 1122  N   CYS A 790     7283   6161   4005   1134    859   -507  A    N  
ATOM   1123  CA  CYS A 790      -8.167  -8.334 -32.101  1.00 47.58      A    C  
ANISOU 1123  CA  CYS A 790     7632   6350   4096    960    816   -450  A    C  
ATOM   1124  C   CYS A 790      -9.353  -7.638 -31.404  1.00 46.39      A    C  
ANISOU 1124  C   CYS A 790     7438   6055   4134    702    596   -377  A    C  
ATOM   1125  O   CYS A 790      -9.567  -6.428 -31.587  1.00 41.50      A    O  
ANISOU 1125  O   CYS A 790     6746   5495   3526    529    603   -263  A    O  
ATOM   1126  CB  CYS A 790      -8.653  -9.092 -33.331  1.00 52.75      A    C  
ANISOU 1126  CB  CYS A 790     8674   6876   4491   1088    762   -575  A    C  
ATOM   1127  SG  CYS A 790      -9.277  -7.987 -34.595  1.00 64.87      A    S  
ANISOU 1127  SG  CYS A 790    10381   8438   5829    917    746   -491  A    S  
ATOM   1128  N   PHE A 791     -10.101  -8.398 -30.609  1.00 43.73      A    N  
ANISOU 1128  N   PHE A 791     7148   5535   3934    688    406   -437  A    N  
ATOM   1129  CA  PHE A 791     -11.207  -7.845 -29.821  1.00 42.80      A    C  
ANISOU 1129  CA  PHE A 791     6950   5314   3998    480    224   -369  A    C  
ATOM   1130  C   PHE A 791     -10.724  -6.770 -28.859  1.00 43.59      A    C  
ANISOU 1130  C   PHE A 791     6759   5541   4264    372    305   -257  A    C  
ATOM   1131  O   PHE A 791     -11.332  -5.695 -28.778  1.00 42.88      A    O  
ANISOU 1131  O   PHE A 791     6624   5442   4228    218    244   -174  A    O  
ATOM   1132  CB  PHE A 791     -11.946  -8.924 -29.016  1.00 39.50      A    C  
ANISOU 1132  CB  PHE A 791     6596   4716   3697    476     42   -431  A    C  
ATOM   1133  CG  PHE A 791     -12.684  -9.965 -29.841  1.00 40.21      A    C  
ANISOU 1133  CG  PHE A 791     7005   4623   3650    515   -119   -530  A    C  
ATOM   1134  CD1 PHE A 791     -13.193  -9.711 -31.127  1.00 43.02      A    C  
ANISOU 1134  CD1 PHE A 791     7576   4948   3821    487   -176   -548  A    C  
ATOM   1135  CD2 PHE A 791     -12.934 -11.215 -29.270  1.00 44.89      A    C  
ANISOU 1135  CD2 PHE A 791     7707   5049   4299    555   -249   -598  A    C  
ATOM   1136  CE1 PHE A 791     -13.898 -10.692 -31.827  1.00 47.63      A    C  
ANISOU 1136  CE1 PHE A 791     8475   5342   4278    500   -365   -642  A    C  
ATOM   1137  CE2 PHE A 791     -13.635 -12.198 -29.966  1.00 49.52      A    C  
ANISOU 1137  CE2 PHE A 791     8614   5435   4765    557   -436   -685  A    C  
ATOM   1138  CZ  PHE A 791     -14.120 -11.935 -31.253  1.00 51.79      A    C  
ANISOU 1138  CZ  PHE A 791     9114   5696   4868    528   -500   -712  A    C  
ATOM   1139  N   ALA A 792      -9.625  -7.049 -28.162  1.00 39.53      A    N  
ANISOU 1139  N   ALA A 792     6065   5133   3820    464    425   -256  A    N  
ATOM   1140  CA  ALA A 792      -9.015  -6.072 -27.261  1.00 38.06      A    C  
ANISOU 1140  CA  ALA A 792     5618   5067   3775    354    486   -152  A    C  
ATOM   1141  C   ALA A 792      -8.617  -4.786 -27.989  1.00 36.86      A    C  
ANISOU 1141  C   ALA A 792     5419   5045   3543    237    593    -46  A    C  
ATOM   1142  O   ALA A 792      -8.937  -3.696 -27.536  1.00 36.51      A    O  
ANISOU 1142  O   ALA A 792     5309   4977   3586     70    532     39  A    O  
ATOM   1143  CB  ALA A 792      -7.803  -6.674 -26.559  1.00 40.40      A    C  
ANISOU 1143  CB  ALA A 792     5732   5480   4139    487    586   -165  A    C  
ATOM   1144  N   TYR A 793      -7.934  -4.941 -29.115  1.00 39.07      A    N  
ANISOU 1144  N   TYR A 793     5754   5451   3639    333    750    -51  A    N  
ATOM   1145  CA  TYR A 793      -7.541  -3.820 -29.977  1.00 40.69      A    C  
ANISOU 1145  CA  TYR A 793     5949   5785   3726    213    865     66  A    C  
ATOM   1146  C   TYR A 793      -8.732  -2.975 -30.411  1.00 38.36      A    C  
ANISOU 1146  C   TYR A 793     5839   5337   3399     61    713    107  A    C  
ATOM   1147  O   TYR A 793      -8.679  -1.754 -30.319  1.00 37.28      A    O  
ANISOU 1147  O   TYR A 793     5648   5219   3299   -112    703    226  A    O  
ATOM   1148  CB  TYR A 793      -6.761  -4.314 -31.196  1.00 43.97      A    C  
ANISOU 1148  CB  TYR A 793     6436   6362   3907    374   1071     40  A    C  
ATOM   1149  CG  TYR A 793      -6.370  -3.234 -32.184  1.00 47.77      A    C  
ANISOU 1149  CG  TYR A 793     6933   6989   4230    240   1205    176  A    C  
ATOM   1150  CD1 TYR A 793      -5.322  -2.345 -31.903  1.00 52.37      A    C  
ANISOU 1150  CD1 TYR A 793     7248   7778   4873     95   1342    333  A    C  
ATOM   1151  CD2 TYR A 793      -7.051  -3.091 -33.407  1.00 54.59      A    C  
ANISOU 1151  CD2 TYR A 793     8090   7779   4874    235   1178    163  A    C  
ATOM   1152  CE1 TYR A 793      -4.952  -1.347 -32.816  1.00 53.65      A    C  
ANISOU 1152  CE1 TYR A 793     7434   8069   4881    -63   1463    484  A    C  
ATOM   1153  CE2 TYR A 793      -6.691  -2.102 -34.326  1.00 61.15      A    C  
ANISOU 1153  CE2 TYR A 793     8961   8736   5538    102   1300    304  A    C  
ATOM   1154  CZ  TYR A 793      -5.642  -1.233 -34.026  1.00 60.06      A    C  
ANISOU 1154  CZ  TYR A 793     8555   8801   5464    -53   1449    470  A    C  
ATOM   1155  OH  TYR A 793      -5.292  -0.260 -34.923  1.00 61.21      A    O  
ANISOU 1155  OH  TYR A 793     8752   9065   5441   -216   1563    632  A    O  
ATOM   1156  N   GLN A 794      -9.803  -3.633 -30.836  1.00 39.14      A    N  
ANISOU 1156  N   GLN A 794     6157   5277   3438    125    572     11  A    N  
ATOM   1157  CA  GLN A 794     -10.993  -2.929 -31.322  1.00 39.81      A    C  
ANISOU 1157  CA  GLN A 794     6407   5230   3490     11    406     49  A    C  
ATOM   1158  C   GLN A 794     -11.716  -2.121 -30.251  1.00 37.32      A    C  
ANISOU 1158  C   GLN A 794     5976   4820   3382   -112    264    104  A    C  
ATOM   1159  O   GLN A 794     -12.148  -0.982 -30.496  1.00 37.74      A    O  
ANISOU 1159  O   GLN A 794     6080   4832   3428   -221    200    192  A    O  
ATOM   1160  CB  GLN A 794     -11.948  -3.893 -31.997  1.00 42.20      A    C  
ANISOU 1160  CB  GLN A 794     6947   5398   3689     94    264    -59  A    C  
ATOM   1161  CG  GLN A 794     -11.478  -4.365 -33.351  1.00 41.46      A    C  
ANISOU 1161  CG  GLN A 794     7069   5364   3322    206    374   -107  A    C  
ATOM   1162  CD  GLN A 794     -12.503  -5.291 -33.928  1.00 42.51      A    C  
ANISOU 1162  CD  GLN A 794     7466   5324   3360    257    177   -216  A    C  
ATOM   1163  NE2 GLN A 794     -12.261  -6.598 -33.864  1.00 46.61      A    N  
ANISOU 1163  NE2 GLN A 794     8080   5789   3839    409    182   -346  A    N  
ATOM   1164  OE1 GLN A 794     -13.554  -4.832 -34.359  1.00 41.82      A    O  
ANISOU 1164  OE1 GLN A 794     7497   5139   3252    154     -7   -179  A    O  
ATOM   1165  N   VAL A 795     -11.821  -2.690 -29.063  1.00 34.06      A    N  
ANISOU 1165  N   VAL A 795     5430   4372   3138    -80    220     53  A    N  
ATOM   1166  CA  VAL A 795     -12.439  -1.988 -27.945  1.00 31.89      A    C  
ANISOU 1166  CA  VAL A 795     5049   4028   3040   -165    114     93  A    C  
ATOM   1167  C   VAL A 795     -11.611  -0.774 -27.575  1.00 34.50      A    C  
ANISOU 1167  C   VAL A 795     5274   4425   3408   -271    192    192  A    C  
ATOM   1168  O   VAL A 795     -12.191   0.296 -27.343  1.00 35.56      A    O  
ANISOU 1168  O   VAL A 795     5444   4478   3589   -352    100    249  A    O  
ATOM   1169  CB  VAL A 795     -12.692  -2.909 -26.729  1.00 32.65      A    C  
ANISOU 1169  CB  VAL A 795     5040   4083   3282   -114     63     27  A    C  
ATOM   1170  CG1 VAL A 795     -13.257  -2.127 -25.547  1.00 32.92      A    C  
ANISOU 1170  CG1 VAL A 795     4972   4070   3465   -182    -13     66  A    C  
ATOM   1171  CG2 VAL A 795     -13.689  -4.000 -27.103  1.00 37.33      A    C  
ANISOU 1171  CG2 VAL A 795     5761   4579   3846    -65    -59    -47  A    C  
ATOM   1172  N   ALA A 796     -10.282  -0.927 -27.532  1.00 34.14      A    N  
ANISOU 1172  N   ALA A 796     5106   4523   3341   -268    346    217  A    N  
ATOM   1173  CA  ALA A 796      -9.388   0.205 -27.277  1.00 36.17      A    C  
ANISOU 1173  CA  ALA A 796     5258   4858   3626   -414    407    334  A    C  
ATOM   1174  C   ALA A 796      -9.525   1.331 -28.316  1.00 37.57      A    C  
ANISOU 1174  C   ALA A 796     5584   5014   3678   -536    405    439  A    C  
ATOM   1175  O   ALA A 796      -9.466   2.507 -27.943  1.00 35.89      A    O  
ANISOU 1175  O   ALA A 796     5381   4739   3516   -682    342    529  A    O  
ATOM   1176  CB  ALA A 796      -7.940  -0.239 -27.219  1.00 37.71      A    C  
ANISOU 1176  CB  ALA A 796     5260   5256   3813   -389    575    360  A    C  
ATOM   1177  N   LYS A 797      -9.657   0.952 -29.593  1.00 37.74      A    N  
ANISOU 1177  N   LYS A 797     5745   5074   3521   -474    465    428  A    N  
ATOM   1178  CA  LYS A 797      -9.917   1.902 -30.704  1.00 43.96      A    C  
ANISOU 1178  CA  LYS A 797     6720   5827   4154   -575    448    529  A    C  
ATOM   1179  C   LYS A 797     -11.234   2.652 -30.496  1.00 39.17      A    C  
ANISOU 1179  C   LYS A 797     6257   5012   3615   -603    230    533  A    C  
ATOM   1180  O   LYS A 797     -11.291   3.872 -30.674  1.00 41.58      A    O  
ANISOU 1180  O   LYS A 797     6658   5243   3899   -729    171    643  A    O  
ATOM   1181  CB  LYS A 797      -9.927   1.212 -32.096  1.00 47.47      A    C  
ANISOU 1181  CB  LYS A 797     7327   6342   4367   -475    536    493  A    C  
ATOM   1182  CG  LYS A 797      -8.634   1.334 -32.871  1.00 59.28      A    C  
ANISOU 1182  CG  LYS A 797     8767   8060   5698   -514    775    586  A    C  
ATOM   1183  CD  LYS A 797      -8.741   0.644 -34.225  1.00 70.79      A    C  
ANISOU 1183  CD  LYS A 797    10434   9570   6892   -384    859    531  A    C  
ATOM   1184  N   GLY A 798     -12.275   1.907 -30.131  1.00 36.51      A    N  
ANISOU 1184  N   GLY A 798     5931   4587   3355   -483    109    422  A    N  
ATOM   1185  CA  GLY A 798     -13.575   2.484 -29.790  1.00 38.81      A    C  
ANISOU 1185  CA  GLY A 798     6290   4721   3735   -469    -85    419  A    C  
ATOM   1186  C   GLY A 798     -13.469   3.498 -28.672  1.00 36.47      A    C  
ANISOU 1186  C   GLY A 798     5921   4357   3577   -534   -126    463  A    C  
ATOM   1187  O   GLY A 798     -13.995   4.606 -28.785  1.00 34.75      A    O  
ANISOU 1187  O   GLY A 798     5827   4020   3357   -567   -236    526  A    O  
ATOM   1188  N   MET A 799     -12.722   3.144 -27.630  1.00 33.78      A    N  
ANISOU 1188  N   MET A 799     5411   4082   3343   -547    -45    432  A    N  
ATOM   1189  CA  MET A 799     -12.509   4.041 -26.498  1.00 34.17      A    C  
ANISOU 1189  CA  MET A 799     5415   4062   3505   -614    -91    461  A    C  
ATOM   1190  C   MET A 799     -11.647   5.230 -26.814  1.00 37.24      A    C  
ANISOU 1190  C   MET A 799     5878   4433   3836   -788    -74    586  A    C  
ATOM   1191  O   MET A 799     -11.883   6.318 -26.267  1.00 37.55      A    O  
ANISOU 1191  O   MET A 799     6017   4328   3922   -843   -185    622  A    O  
ATOM   1192  CB  MET A 799     -11.944   3.280 -25.287  1.00 31.74      A    C  
ANISOU 1192  CB  MET A 799     4919   3828   3312   -586    -35    396  A    C  
ATOM   1193  CG  MET A 799     -12.937   2.308 -24.664  1.00 34.08      A    C  
ANISOU 1193  CG  MET A 799     5163   4101   3686   -447    -85    293  A    C  
ATOM   1194  SD  MET A 799     -14.504   3.053 -24.165  1.00 33.66      A    S  
ANISOU 1194  SD  MET A 799     5188   3907   3695   -369   -236    277  A    S  
ATOM   1195  CE  MET A 799     -13.971   4.340 -23.076  1.00 35.11      A    C  
ANISOU 1195  CE  MET A 799     5410   4002   3927   -438   -267    308  A    C  
ATOM   1196  N   GLU A 800     -10.661   5.035 -27.682  1.00 37.25      A    N  
ANISOU 1196  N   GLU A 800     5845   4580   3729   -875     64    657  A    N  
ATOM   1197  CA  GLU A 800      -9.840   6.143 -28.168  1.00 40.25      A    C  
ANISOU 1197  CA  GLU A 800     6292   4967   4032  -1083     91    813  A    C  
ATOM   1198  C   GLU A 800     -10.712   7.186 -28.899  1.00 40.49      A    C  
ANISOU 1198  C   GLU A 800     6596   4813   3975  -1113    -47    880  A    C  
ATOM   1199  O   GLU A 800     -10.522   8.395 -28.710  1.00 41.27      A    O  
ANISOU 1199  O   GLU A 800     6821   4780   4081  -1263   -140    980  A    O  
ATOM   1200  CB  GLU A 800      -8.729   5.633 -29.098  1.00 42.81      A    C  
ANISOU 1200  CB  GLU A 800     6509   5528   4229  -1140    298    883  A    C  
ATOM   1201  CG  GLU A 800      -7.633   6.653 -29.365  1.00 49.62      A    C  
ANISOU 1201  CG  GLU A 800     7348   6463   5041  -1400    357   1070  A    C  
ATOM   1202  CD  GLU A 800      -6.631   6.240 -30.444  1.00 54.07      A    C  
ANISOU 1202  CD  GLU A 800     7806   7294   5444  -1444    591   1162  A    C  
ATOM   1203  OE1 GLU A 800      -6.674   5.099 -30.916  1.00 55.02      A    O  
ANISOU 1203  OE1 GLU A 800     7875   7538   5490  -1245    714   1059  A    O  
ATOM   1204  OE2 GLU A 800      -5.787   7.085 -30.821  1.00 62.19      A    O1-
ANISOU 1204  OE2 GLU A 800     8813   8408   6410  -1683    653   1346  A    O1-
ATOM   1205  N   PHE A 801     -11.666   6.704 -29.710  1.00 38.52      A    N  
ANISOU 1205  N   PHE A 801     6452   4539   3644   -971    -85    825  A    N  
ATOM   1206  CA  PHE A 801     -12.659   7.577 -30.378  1.00 39.68      A    C  
ANISOU 1206  CA  PHE A 801     6849   4509   3720   -951   -249    877  A    C  
ATOM   1207  C   PHE A 801     -13.484   8.370 -29.345  1.00 37.67      A    C  
ANISOU 1207  C   PHE A 801     6650   4055   3607   -880   -424    839  A    C  
ATOM   1208  O   PHE A 801     -13.600   9.587 -29.442  1.00 39.47      A    O  
ANISOU 1208  O   PHE A 801     7075   4113   3808   -950   -540    927  A    O  
ATOM   1209  CB  PHE A 801     -13.553   6.750 -31.327  1.00 37.84      A    C  
ANISOU 1209  CB  PHE A 801     6684   4305   3389   -806   -283    812  A    C  
ATOM   1210  CG  PHE A 801     -14.675   7.535 -31.950  1.00 40.00      A    C  
ANISOU 1210  CG  PHE A 801     7181   4411   3608   -753   -480    858  A    C  
ATOM   1211  CD1 PHE A 801     -14.431   8.381 -33.038  1.00 42.25      A    C  
ANISOU 1211  CD1 PHE A 801     7697   4641   3714   -870   -504    999  A    C  
ATOM   1212  CD2 PHE A 801     -15.981   7.415 -31.471  1.00 39.31      A    C  
ANISOU 1212  CD2 PHE A 801     7063   4233   3640   -584   -642    775  A    C  
ATOM   1213  CE1 PHE A 801     -15.463   9.109 -33.624  1.00 46.15      A    C  
ANISOU 1213  CE1 PHE A 801     8411   4970   4155   -805   -709   1048  A    C  
ATOM   1214  CE2 PHE A 801     -17.016   8.144 -32.057  1.00 40.44      A    C  
ANISOU 1214  CE2 PHE A 801     7386   4239   3741   -508   -836    824  A    C  
ATOM   1215  CZ  PHE A 801     -16.760   8.982 -33.136  1.00 41.77      A    C  
ANISOU 1215  CZ  PHE A 801     7805   4331   3734   -610   -881    956  A    C  
ATOM   1216  N   LEU A 802     -13.999   7.680 -28.335  1.00 34.83      A    N  
ANISOU 1216  N   LEU A 802     6131   3717   3387   -738   -435    711  A    N  
ATOM   1217  CA  LEU A 802     -14.748   8.342 -27.257  1.00 34.64      A    C  
ANISOU 1217  CA  LEU A 802     6141   3541   3481   -635   -562    661  A    C  
ATOM   1218  C   LEU A 802     -13.915   9.370 -26.479  1.00 35.36      A    C  
ANISOU 1218  C   LEU A 802     6309   3523   3604   -778   -588    714  A    C  
ATOM   1219  O   LEU A 802     -14.416  10.460 -26.211  1.00 34.94      A    O  
ANISOU 1219  O   LEU A 802     6449   3268   3556   -737   -729    730  A    O  
ATOM   1220  CB  LEU A 802     -15.387   7.301 -26.310  1.00 33.92      A    C  
ANISOU 1220  CB  LEU A 802     5845   3530   3511   -478   -537    531  A    C  
ATOM   1221  CG  LEU A 802     -16.476   6.415 -26.938  1.00 35.20      A    C  
ANISOU 1221  CG  LEU A 802     5955   3756   3665   -347   -577    485  A    C  
ATOM   1222  CD1 LEU A 802     -16.964   5.464 -25.872  1.00 39.30      A    C  
ANISOU 1222  CD1 LEU A 802     6274   4352   4307   -247   -547    387  A    C  
ATOM   1223  CD2 LEU A 802     -17.651   7.206 -27.487  1.00 36.57      A    C  
ANISOU 1223  CD2 LEU A 802     6269   3812   3816   -238   -742    521  A    C  
ATOM   1224  N   GLU A 803     -12.659   9.036 -26.157  1.00 37.32      A    N  
ANISOU 1224  N   GLU A 803     6417   3896   3866   -938   -470    742  A    N  
ATOM   1225  CA  GLU A 803     -11.705  10.000 -25.585  1.00 38.36      A    C  
ANISOU 1225  CA  GLU A 803     6618   3941   4015  -1141   -513    823  A    C  
ATOM   1226  C   GLU A 803     -11.560  11.267 -26.452  1.00 42.19      A    C  
ANISOU 1226  C   GLU A 803     7370   4267   4392  -1304   -609    972  A    C  
ATOM   1227  O   GLU A 803     -11.613  12.399 -25.936  1.00 42.82      A    O  
ANISOU 1227  O   GLU A 803     7664   4121   4486  -1367   -763   1002  A    O  
ATOM   1228  CB  GLU A 803     -10.316   9.368 -25.320  1.00 41.87      A    C  
ANISOU 1228  CB  GLU A 803     6822   4598   4489  -1303   -370    860  A    C  
ATOM   1229  CG  GLU A 803      -9.277  10.395 -24.803  1.00 46.05      A    C  
ANISOU 1229  CG  GLU A 803     7407   5052   5037  -1567   -444    972  A    C  
ATOM   1230  CD  GLU A 803      -8.014   9.845 -24.140  1.00 50.25      A    C  
ANISOU 1230  CD  GLU A 803     7668   5782   5644  -1699   -357    994  A    C  
ATOM   1231  OE1 GLU A 803      -7.757   8.620 -24.110  1.00 65.27      A    O  
ANISOU 1231  OE1 GLU A 803     9325   7896   7577  -1583   -213    930  A    O  
ATOM   1232  OE2 GLU A 803      -7.262  10.687 -23.609  1.00 64.18      A    O1-
ANISOU 1232  OE2 GLU A 803     9478   7470   7436  -1925   -458   1082  A    O1-
ATOM   1233  N   PHE A 804     -11.384  11.059 -27.751  1.00 39.99      A    N  
ANISOU 1233  N   PHE A 804     7109   4093   3990  -1368   -525   1063  A    N  
ATOM   1234  CA  PHE A 804     -11.263  12.147 -28.727  1.00 46.63      A    C  
ANISOU 1234  CA  PHE A 804     8213   4804   4699  -1531   -602   1227  A    C  
ATOM   1235  C   PHE A 804     -12.548  12.990 -28.787  1.00 46.68      A    C  
ANISOU 1235  C   PHE A 804     8503   4535   4698  -1360   -815   1198  A    C  
ATOM   1236  O   PHE A 804     -12.470  14.188 -28.976  1.00 47.80      A    O  
ANISOU 1236  O   PHE A 804     8917   4460   4786  -1483   -954   1308  A    O  
ATOM   1237  CB  PHE A 804     -10.881  11.554 -30.113  1.00 48.93      A    C  
ANISOU 1237  CB  PHE A 804     8457   5302   4831  -1592   -439   1312  A    C  
ATOM   1238  CG  PHE A 804     -10.775  12.565 -31.240  1.00 55.69      A    C  
ANISOU 1238  CG  PHE A 804     9591   6051   5517  -1765   -498   1498  A    C  
ATOM   1239  CD1 PHE A 804      -9.635  13.364 -31.385  1.00 60.44      A    C  
ANISOU 1239  CD1 PHE A 804    10235   6664   6064  -2088   -464   1688  A    C  
ATOM   1240  CD2 PHE A 804     -11.797  12.675 -32.209  1.00 60.94      A    C  
ANISOU 1240  CD2 PHE A 804    10470   6619   6065  -1625   -594   1501  A    C  
ATOM   1241  CE1 PHE A 804      -9.530  14.283 -32.449  1.00 62.99      A    C  
ANISOU 1241  CE1 PHE A 804    10833   6886   6213  -2274   -515   1883  A    C  
ATOM   1242  CE2 PHE A 804     -11.694  13.588 -33.271  1.00 67.83      A    C  
ANISOU 1242  CE2 PHE A 804    11625   7387   6760  -1786   -656   1685  A    C  
ATOM   1243  CZ  PHE A 804     -10.559  14.395 -33.390  1.00 61.75      A    C  
ANISOU 1243  CZ  PHE A 804    10917   6616   5929  -2114   -609   1879  A    C  
ATOM   1244  N   LYS A 805     -13.715  12.365 -28.597  1.00 43.82      A    N  
ANISOU 1244  N   LYS A 805     8069   4185   4396  -1078   -848   1057  A    N  
ATOM   1245  CA  LYS A 805     -15.001  13.093 -28.545  1.00 44.32      A    C  
ANISOU 1245  CA  LYS A 805     8337   4029   4475   -861  -1043   1020  A    C  
ATOM   1246  C   LYS A 805     -15.389  13.672 -27.179  1.00 42.70      A    C  
ANISOU 1246  C   LYS A 805     8183   3656   4385   -725  -1143    920  A    C  
ATOM   1247  O   LYS A 805     -16.482  14.196 -27.042  1.00 48.57      A    O  
ANISOU 1247  O   LYS A 805     9057   4249   5150   -493  -1280    872  A    O  
ATOM   1248  CB  LYS A 805     -16.123  12.198 -29.109  1.00 44.22      A    C  
ANISOU 1248  CB  LYS A 805     8207   4132   4463   -639  -1046    945  A    C  
ATOM   1249  CG  LYS A 805     -15.945  11.862 -30.595  1.00 45.99      A    C  
ANISOU 1249  CG  LYS A 805     8498   4453   4525   -737  -1004   1041  A    C  
ATOM   1250  CD  LYS A 805     -16.090  13.083 -31.512  1.00 51.37      A    C  
ANISOU 1250  CD  LYS A 805     9517   4932   5071   -808  -1157   1190  A    C  
ATOM   1251  CE  LYS A 805     -15.638  12.761 -32.928  1.00 53.35      A    C  
ANISOU 1251  CE  LYS A 805     9845   5302   5123   -952  -1074   1301  A    C  
ATOM   1252  NZ  LYS A 805     -16.441  13.517 -33.900  1.00 59.67      A    N1+
ANISOU 1252  NZ  LYS A 805    10937   5933   5802   -889  -1271   1395  A    N1+
ATOM   1253  N   SER A 806     -14.491  13.613 -26.199  1.00 37.89      A    N  
ANISOU 1253  N   SER A 806     7483   3074   3837   -858  -1081    892  A    N  
ATOM   1254  CA  SER A 806     -14.718  14.100 -24.856  1.00 41.37      A    C  
ANISOU 1254  CA  SER A 806     7996   3366   4356   -746  -1163    789  A    C  
ATOM   1255  C   SER A 806     -15.885  13.350 -24.143  1.00 40.17      A    C  
ANISOU 1255  C   SER A 806     7661   3311   4292   -424  -1123    631  A    C  
ATOM   1256  O   SER A 806     -16.721  13.956 -23.476  1.00 44.86      A    O  
ANISOU 1256  O   SER A 806     8383   3754   4908   -198  -1220    553  A    O  
ATOM   1257  CB  SER A 806     -14.903  15.644 -24.854  1.00 42.75      A    C  
ANISOU 1257  CB  SER A 806     8573   3198   4471   -753  -1376    846  A    C  
ATOM   1258  OG  SER A 806     -14.717  16.073 -23.537  1.00 46.86      A    O  
ANISOU 1258  OG  SER A 806     9182   3584   5038   -721  -1438    753  A    O  
ATOM   1259  N   CYS A 807     -15.927  12.036 -24.314  1.00 37.87      A    N  
ANISOU 1259  N   CYS A 807     7077   3272   4040   -405   -979    593  A    N  
ATOM   1260  CA  CYS A 807     -16.954  11.186 -23.713  1.00 39.64      A    C  
ANISOU 1260  CA  CYS A 807     7096   3619   4346   -165   -931    476  A    C  
ATOM   1261  C   CYS A 807     -16.345  10.255 -22.704  1.00 39.57      A    C  
ANISOU 1261  C   CYS A 807     6871   3759   4403   -220   -804    406  A    C  
ATOM   1262  O   CYS A 807     -15.145  10.001 -22.753  1.00 42.65      A    O  
ANISOU 1262  O   CYS A 807     7210   4214   4781   -432   -736    451  A    O  
ATOM   1263  CB  CYS A 807     -17.676  10.370 -24.776  1.00 39.52      A    C  
ANISOU 1263  CB  CYS A 807     6955   3742   4318    -98   -913    495  A    C  
ATOM   1264  SG  CYS A 807     -18.677  11.415 -25.819  1.00 48.82      A    S  
ANISOU 1264  SG  CYS A 807     8370   4752   5429     34  -1098    567  A    S  
ATOM   1265  N   VAL A 808     -17.182   9.782 -21.775  1.00 35.73      A    N  
ANISOU 1265  N   VAL A 808     6257   3336   3983    -23   -774    307  A    N  
ATOM   1266  CA  VAL A 808     -16.847   8.684 -20.866  1.00 36.12      A    C  
ANISOU 1266  CA  VAL A 808     6090   3543   4090    -44   -656    245  A    C  
ATOM   1267  C   VAL A 808     -17.966   7.634 -20.974  1.00 39.74      A    C  
ANISOU 1267  C   VAL A 808     6341   4159   4601    103   -609    209  A    C  
ATOM   1268  O   VAL A 808     -19.140   7.980 -21.133  1.00 42.83      A    O  
ANISOU 1268  O   VAL A 808     6740   4530   5005    282   -669    203  A    O  
ATOM   1269  CB  VAL A 808     -16.663   9.144 -19.397  1.00 41.19      A    C  
ANISOU 1269  CB  VAL A 808     6804   4105   4740      8   -667    172  A    C  
ATOM   1270  CG1 VAL A 808     -15.489  10.118 -19.281  1.00 47.25      A    C  
ANISOU 1270  CG1 VAL A 808     7778   4713   5463   -189   -748    218  A    C  
ATOM   1271  CG2 VAL A 808     -17.926   9.779 -18.817  1.00 42.93      A    C  
ANISOU 1271  CG2 VAL A 808     7111   4245   4955    282   -713    106  A    C  
ATOM   1272  N   HIS A 809     -17.586   6.371 -20.889  1.00 35.45      A    N  
ANISOU 1272  N   HIS A 809     5615   3766   4090     24   -515    195  A    N  
ATOM   1273  CA  HIS A 809     -18.507   5.255 -20.769  1.00 36.03      A    C  
ANISOU 1273  CA  HIS A 809     5497   3976   4217    110   -480    168  A    C  
ATOM   1274  C   HIS A 809     -18.533   4.940 -19.273  1.00 38.85      A    C  
ANISOU 1274  C   HIS A 809     5769   4379   4612    165   -412    112  A    C  
ATOM   1275  O   HIS A 809     -17.543   4.555 -18.680  1.00 36.39      A    O  
ANISOU 1275  O   HIS A 809     5442   4083   4301     65   -360     95  A    O  
ATOM   1276  CB  HIS A 809     -17.990   4.070 -21.591  1.00 38.85      A    C  
ANISOU 1276  CB  HIS A 809     5771   4427   4562    -11   -436    184  A    C  
ATOM   1277  CG  HIS A 809     -19.061   3.143 -22.071  1.00 46.30      A    C  
ANISOU 1277  CG  HIS A 809     6602   5456   5535     37   -472    185  A    C  
ATOM   1278  CD2 HIS A 809     -19.435   2.790 -23.319  1.00 50.55      A    C  
ANISOU 1278  CD2 HIS A 809     7170   6005   6032     11   -539    214  A    C  
ATOM   1279  ND1 HIS A 809     -19.883   2.442 -21.220  1.00 39.97      A    N  
ANISOU 1279  ND1 HIS A 809     5642   4740   4805     99   -453    166  A    N  
ATOM   1280  CE1 HIS A 809     -20.726   1.711 -21.915  1.00 46.98      A    C  
ANISOU 1280  CE1 HIS A 809     6453   5687   5711     90   -519    189  A    C  
ATOM   1281  NE2 HIS A 809     -20.472   1.898 -23.195  1.00 50.40      A    N  
ANISOU 1281  NE2 HIS A 809     7009   6068   6072     43   -581    210  A    N  
ATOM   1282  N   ARG A 810     -19.668   5.067 -18.638  1.00 37.61      A    N  
ANISOU 1282  N   ARG A 810     5546   4262   4482    331   -407     89  A    N  
ATOM   1283  CA  ARG A 810     -19.735   4.750 -17.196  1.00 40.09      A    C  
ANISOU 1283  CA  ARG A 810     5794   4635   4802    388   -325     42  A    C  
ATOM   1284  C   ARG A 810     -19.978   3.254 -16.837  1.00 35.79      A    C  
ANISOU 1284  C   ARG A 810     5045   4249   4305    328   -253     56  A    C  
ATOM   1285  O   ARG A 810     -20.132   2.913 -15.683  1.00 36.91      A    O  
ANISOU 1285  O   ARG A 810     5130   4453   4439    367   -182     36  A    O  
ATOM   1286  CB  ARG A 810     -20.745   5.688 -16.566  1.00 40.22      A    C  
ANISOU 1286  CB  ARG A 810     5856   4628   4796    616   -328      9  A    C  
ATOM   1287  CG  ARG A 810     -20.313   7.133 -16.809  1.00 47.83      A    C  
ANISOU 1287  CG  ARG A 810     7091   5381   5701    656   -424    -10  A    C  
ATOM   1288  CD  ARG A 810     -20.924   8.053 -15.824  1.00 50.29      A    C  
ANISOU 1288  CD  ARG A 810     7523   5626   5958    891   -416    -78  A    C  
ATOM   1289  NE  ARG A 810     -22.352   8.155 -16.029  1.00 53.87      A    N  
ANISOU 1289  NE  ARG A 810     7838   6185   6444   1126   -402    -65  A    N  
ATOM   1290  CZ  ARG A 810     -23.171   8.844 -15.247  1.00 65.95      A    C  
ANISOU 1290  CZ  ARG A 810     9412   7717   7929   1405   -364   -122  A    C  
ATOM   1291  NH1 ARG A 810     -22.715   9.484 -14.159  1.00 72.68      A    N1+
ANISOU 1291  NH1 ARG A 810    10488   8444   8682   1482   -343   -210  A    N1+
ATOM   1292  NH2 ARG A 810     -24.471   8.890 -15.553  1.00 83.32      A    N  
ANISOU 1292  NH2 ARG A 810    11430  10053  10177   1621   -353    -90  A    N  
ATOM   1293  N   ASP A 811     -19.869   2.372 -17.826  1.00 33.49      A    N  
ANISOU 1293  N   ASP A 811     4686   3996   4041    217   -279     91  A    N  
ATOM   1294  CA  ASP A 811     -20.216   0.955 -17.726  1.00 30.31      A    C  
ANISOU 1294  CA  ASP A 811     4135   3701   3681    149   -254    113  A    C  
ATOM   1295  C   ASP A 811     -19.513   0.121 -18.791  1.00 29.05      A    C  
ANISOU 1295  C   ASP A 811     4011   3517   3512     25   -288    118  A    C  
ATOM   1296  O   ASP A 811     -20.135  -0.649 -19.504  1.00 32.10      A    O  
ANISOU 1296  O   ASP A 811     4344   3937   3915    -14   -343    143  A    O  
ATOM   1297  CB  ASP A 811     -21.740   0.775 -17.777  1.00 30.56      A    C  
ANISOU 1297  CB  ASP A 811     4008   3842   3760    225   -278    158  A    C  
ATOM   1298  CG  ASP A 811     -22.190  -0.582 -17.230  1.00 33.95      A    C  
ANISOU 1298  CG  ASP A 811     4286   4382   4231    137   -246    198  A    C  
ATOM   1299  OD1 ASP A 811     -21.394  -1.344 -16.626  1.00 30.77      A    O  
ANISOU 1299  OD1 ASP A 811     3917   3960   3814     53   -200    182  A    O  
ATOM   1300  OD2 ASP A 811     -23.358  -0.894 -17.436  1.00 33.22      A    O1-
ANISOU 1300  OD2 ASP A 811     4038   4396   4188    142   -282    259  A    O1-
ATOM   1301  N   LEU A 812     -18.201   0.309 -18.931  1.00 30.27      A    N  
ANISOU 1301  N   LEU A 812     4259   3615   3629    -34   -260     96  A    N  
ATOM   1302  CA  LEU A 812     -17.440  -0.429 -19.908  1.00 30.22      A    C  
ANISOU 1302  CA  LEU A 812     4287   3604   3591   -110   -260     93  A    C  
ATOM   1303  C   LEU A 812     -17.212  -1.828 -19.303  1.00 30.90      A    C  
ANISOU 1303  C   LEU A 812     4307   3727   3707   -139   -232     76  A    C  
ATOM   1304  O   LEU A 812     -16.707  -1.959 -18.194  1.00 33.01      A    O  
ANISOU 1304  O   LEU A 812     4543   4006   3993   -138   -190     65  A    O  
ATOM   1305  CB  LEU A 812     -16.121   0.241 -20.236  1.00 31.93      A    C  
ANISOU 1305  CB  LEU A 812     4580   3790   3761   -160   -222     97  A    C  
ATOM   1306  CG  LEU A 812     -15.242  -0.462 -21.283  1.00 35.76      A    C  
ANISOU 1306  CG  LEU A 812     5089   4307   4192   -205   -183     95  A    C  
ATOM   1307  CD1 LEU A 812     -15.919  -0.581 -22.640  1.00 35.14      A    C  
ANISOU 1307  CD1 LEU A 812     5090   4212   4050   -197   -237    105  A    C  
ATOM   1308  CD2 LEU A 812     -13.927   0.275 -21.418  1.00 38.03      A    C  
ANISOU 1308  CD2 LEU A 812     5395   4610   4446   -272   -127    126  A    C  
ATOM   1309  N   ALA A 813     -17.638  -2.839 -20.037  1.00 32.35      A    N  
ANISOU 1309  N   ALA A 813     4498   3910   3884   -167   -280     75  A    N  
ATOM   1310  CA  ALA A 813     -17.577  -4.259 -19.642  1.00 32.93      A    C  
ANISOU 1310  CA  ALA A 813     4557   3978   3977   -201   -291     65  A    C  
ATOM   1311  C   ALA A 813     -17.897  -5.101 -20.865  1.00 32.45      A    C  
ANISOU 1311  C   ALA A 813     4584   3871   3874   -232   -374     51  A    C  
ATOM   1312  O   ALA A 813     -18.489  -4.578 -21.818  1.00 34.07      A    O  
ANISOU 1312  O   ALA A 813     4822   4075   4049   -236   -433     64  A    O  
ATOM   1313  CB  ALA A 813     -18.587  -4.547 -18.545  1.00 31.20      A    C  
ANISOU 1313  CB  ALA A 813     4234   3804   3818   -223   -301    109  A    C  
ATOM   1314  N   ALA A 814     -17.539  -6.390 -20.849  1.00 29.76      A    N  
ANISOU 1314  N   ALA A 814     4310   3478   3520   -248   -398     23  A    N  
ATOM   1315  CA  ALA A 814     -17.778  -7.271 -22.003  1.00 29.74      A    C  
ANISOU 1315  CA  ALA A 814     4451   3398   3452   -270   -495    -10  A    C  
ATOM   1316  C   ALA A 814     -19.248  -7.446 -22.352  1.00 31.26      A    C  
ANISOU 1316  C   ALA A 814     4618   3583   3675   -371   -638     42  A    C  
ATOM   1317  O   ALA A 814     -19.586  -7.617 -23.534  1.00 36.53      A    O  
ANISOU 1317  O   ALA A 814     5406   4202   4273   -392   -739     22  A    O  
ATOM   1318  CB  ALA A 814     -17.106  -8.621 -21.834  1.00 32.25      A    C  
ANISOU 1318  CB  ALA A 814     4882   3628   3744   -243   -509    -58  A    C  
ATOM   1319  N   ARG A 815     -20.118  -7.404 -21.341  1.00 30.53      A    N  
ANISOU 1319  N   ARG A 815     4367   3556   3678   -433   -648    115  A    N  
ATOM   1320  CA  ARG A 815     -21.588  -7.354 -21.556  1.00 32.61      A    C  
ANISOU 1320  CA  ARG A 815     4519   3876   3995   -525   -768    193  A    C  
ATOM   1321  C   ARG A 815     -22.116  -6.163 -22.412  1.00 36.50      A    C  
ANISOU 1321  C   ARG A 815     4973   4422   4474   -466   -805    206  A    C  
ATOM   1322  O   ARG A 815     -23.200  -6.267 -22.966  1.00 32.29      A    O  
ANISOU 1322  O   ARG A 815     4384   3919   3967   -536   -946    260  A    O  
ATOM   1323  CB  ARG A 815     -22.344  -7.411 -20.229  1.00 33.49      A    C  
ANISOU 1323  CB  ARG A 815     4429   4096   4199   -575   -721    281  A    C  
ATOM   1324  CG  ARG A 815     -22.115  -6.211 -19.307  1.00 32.07      A    C  
ANISOU 1324  CG  ARG A 815     4137   4011   4037   -448   -567    277  A    C  
ATOM   1325  CD  ARG A 815     -22.970  -6.265 -18.028  1.00 34.66      A    C  
ANISOU 1325  CD  ARG A 815     4276   4471   4423   -475   -502    363  A    C  
ATOM   1326  NE  ARG A 815     -22.498  -5.159 -17.190  1.00 33.20      A    N  
ANISOU 1326  NE  ARG A 815     4072   4327   4216   -330   -364    325  A    N  
ATOM   1327  CZ  ARG A 815     -21.425  -5.172 -16.410  1.00 31.63      A    C  
ANISOU 1327  CZ  ARG A 815     3962   4077   3979   -296   -282    277  A    C  
ATOM   1328  NH1 ARG A 815     -20.712  -6.281 -16.229  1.00 34.35      A    N1+
ANISOU 1328  NH1 ARG A 815     4399   4342   4311   -373   -305    268  A    N1+
ATOM   1329  NH2 ARG A 815     -21.059  -4.056 -15.781  1.00 30.04      A    N  
ANISOU 1329  NH2 ARG A 815     3772   3894   3749   -179   -195    239  A    N  
ATOM   1330  N   ASN A 816     -21.367  -5.054 -22.473  1.00 31.93      A    N  
ANISOU 1330  N   ASN A 816     4425   3850   3858   -353   -697    169  A    N  
ATOM   1331  CA  ASN A 816     -21.704  -3.866 -23.264  1.00 37.91      A    C  
ANISOU 1331  CA  ASN A 816     5196   4622   4586   -288   -734    184  A    C  
ATOM   1332  C   ASN A 816     -20.860  -3.692 -24.545  1.00 39.49      A    C  
ANISOU 1332  C   ASN A 816     5603   4745   4657   -274   -741    136  A    C  
ATOM   1333  O   ASN A 816     -20.765  -2.584 -25.074  1.00 40.71      A    O  
ANISOU 1333  O   ASN A 816     5806   4894   4767   -221   -735    151  A    O  
ATOM   1334  CB  ASN A 816     -21.592  -2.625 -22.347  1.00 36.41      A    C  
ANISOU 1334  CB  ASN A 816     4918   4480   4438   -185   -624    195  A    C  
ATOM   1335  CG  ASN A 816     -22.682  -2.590 -21.295  1.00 37.66      A    C  
ANISOU 1335  CG  ASN A 816     4872   4747   4691   -160   -613    249  A    C  
ATOM   1336  ND2 ASN A 816     -22.359  -2.078 -20.124  1.00 40.06      A    N  
ANISOU 1336  ND2 ASN A 816     5133   5079   5011    -87   -491    235  A    N  
ATOM   1337  OD1 ASN A 816     -23.806  -3.022 -21.533  1.00 46.21      A    O  
ANISOU 1337  OD1 ASN A 816     5835   5899   5824   -209   -714    310  A    O  
ATOM   1338  N   VAL A 817     -20.241  -4.779 -25.020  1.00 31.60      A    N  
ANISOU 1338  N   VAL A 817     4738   3683   3585   -309   -748     81  A    N  
ATOM   1339  CA  VAL A 817     -19.567  -4.825 -26.309  1.00 31.74      A    C  
ANISOU 1339  CA  VAL A 817     4959   3649   3451   -285   -748     34  A    C  
ATOM   1340  C   VAL A 817     -20.341  -5.873 -27.119  1.00 36.73      A    C  
ANISOU 1340  C   VAL A 817     5716   4208   4031   -356   -932     16  A    C  
ATOM   1341  O   VAL A 817     -20.681  -6.916 -26.595  1.00 35.71      A    O  
ANISOU 1341  O   VAL A 817     5566   4041   3961   -422   -997     11  A    O  
ATOM   1342  CB  VAL A 817     -18.079  -5.156 -26.155  1.00 33.00      A    C  
ANISOU 1342  CB  VAL A 817     5178   3809   3553   -224   -585    -26  A    C  
ATOM   1343  CG1 VAL A 817     -17.384  -5.244 -27.503  1.00 37.50      A    C  
ANISOU 1343  CG1 VAL A 817     5945   4360   3943   -179   -550    -70  A    C  
ATOM   1344  CG2 VAL A 817     -17.397  -4.083 -25.324  1.00 35.58      A    C  
ANISOU 1344  CG2 VAL A 817     5377   4201   3941   -196   -450      7  A    C  
ATOM   1345  N   LEU A 818     -20.661  -5.554 -28.369  1.00 35.31      A    N  
ANISOU 1345  N   LEU A 818     5682   4000   3734   -360  -1035     18  A    N  
ATOM   1346  CA  LEU A 818     -21.398  -6.445 -29.243  1.00 37.79      A    C  
ANISOU 1346  CA  LEU A 818     6152   4231   3975   -440  -1244     -1  A    C  
ATOM   1347  C   LEU A 818     -20.504  -6.940 -30.367  1.00 40.35      A    C  
ANISOU 1347  C   LEU A 818     6775   4474   4081   -377  -1211    -97  A    C  
ATOM   1348  O   LEU A 818     -19.500  -6.322 -30.673  1.00 40.69      A    O  
ANISOU 1348  O   LEU A 818     6866   4564   4029   -282  -1033   -116  A    O  
ATOM   1349  CB  LEU A 818     -22.608  -5.725 -29.816  1.00 39.85      A    C  
ANISOU 1349  CB  LEU A 818     6354   4528   4259   -488  -1428     81  A    C  
ATOM   1350  CG  LEU A 818     -23.530  -5.058 -28.801  1.00 42.03      A    C  
ANISOU 1350  CG  LEU A 818     6320   4917   4731   -496  -1437    177  A    C  
ATOM   1351  CD1 LEU A 818     -24.703  -4.486 -29.562  1.00 43.58      A    C  
ANISOU 1351  CD1 LEU A 818     6475   5149   4935   -516  -1647    253  A    C  
ATOM   1352  CD2 LEU A 818     -24.027  -6.026 -27.722  1.00 49.24      A    C  
ANISOU 1352  CD2 LEU A 818     7064   5861   5786   -595  -1459    205  A    C  
ATOM   1353  N   VAL A 819     -20.910  -8.049 -30.976  1.00 42.63      A    N  
ANISOU 1353  N   VAL A 819     7269   4645   4285   -436  -1388   -150  A    N  
ATOM   1354  CA  VAL A 819     -20.130  -8.766 -31.990  1.00 40.99      A    C  
ANISOU 1354  CA  VAL A 819     7390   4339   3847   -349  -1368   -266  A    C  
ATOM   1355  C   VAL A 819     -21.012  -8.853 -33.227  1.00 41.27      A    C  
ANISOU 1355  C   VAL A 819     7646   4294   3739   -427  -1618   -267  A    C  
ATOM   1356  O   VAL A 819     -22.200  -9.207 -33.136  1.00 41.07      A    O  
ANISOU 1356  O   VAL A 819     7568   4223   3812   -584  -1869   -211  A    O  
ATOM   1357  CB  VAL A 819     -19.736 -10.195 -31.522  1.00 45.24      A    C  
ANISOU 1357  CB  VAL A 819     8052   4750   4388   -327  -1382   -355  A    C  
ATOM   1358  CG1 VAL A 819     -18.782 -10.862 -32.519  1.00 48.93      A    C  
ANISOU 1358  CG1 VAL A 819     8862   5128   4600   -165  -1314   -493  A    C  
ATOM   1359  CG2 VAL A 819     -19.110 -10.164 -30.133  1.00 42.82      A    C  
ANISOU 1359  CG2 VAL A 819     7498   4517   4254   -283  -1197   -329  A    C  
ATOM   1360  N   THR A 820     -20.419  -8.499 -34.360  1.00 40.46      A    N  
ANISOU 1360  N   THR A 820     7777   4194   3403   -328  -1548   -315  A    N  
ATOM   1361  CA  THR A 820     -21.070  -8.549 -35.668  1.00 51.12      A    C  
ANISOU 1361  CA  THR A 820     9403   5465   4557   -378  -1773   -329  A    C  
ATOM   1362  C   THR A 820     -20.162  -9.327 -36.653  1.00 51.63      A    C  
ANISOU 1362  C   THR A 820     9862   5436   4318   -239  -1697   -475  A    C  
ATOM   1363  O   THR A 820     -19.198  -9.971 -36.224  1.00 46.72      A    O  
ANISOU 1363  O   THR A 820     9267   4804   3682   -111  -1507   -562  A    O  
ATOM   1364  CB  THR A 820     -21.453  -7.131 -36.173  1.00 47.29      A    C  
ANISOU 1364  CB  THR A 820     8832   5082   4053   -392  -1789   -217  A    C  
ATOM   1365  CG2 THR A 820     -20.225  -6.255 -36.436  1.00 48.69      A    C  
ANISOU 1365  CG2 THR A 820     9031   5364   4105   -263  -1486   -210  A    C  
ATOM   1366  OG1 THR A 820     -22.220  -7.263 -37.381  1.00 55.41      A    O  
ANISOU 1366  OG1 THR A 820    10126   6024   4903   -457  -2060   -220  A    O  
ATOM   1367  N   HIS A 821     -20.473  -9.240 -37.950  1.00 55.36      A    N  
ANISOU 1367  N   HIS A 821    10639   5851   4544   -245  -1842   -500  A    N  
ATOM   1368  CA  HIS A 821     -19.763  -9.972 -39.025  1.00 59.76      A    C  
ANISOU 1368  CA  HIS A 821    11627   6316   4764    -99  -1793   -648  A    C  
ATOM   1369  C   HIS A 821     -18.283  -9.610 -39.072  1.00 59.56      A    C  
ANISOU 1369  C   HIS A 821    11571   6442   4617    112  -1392   -682  A    C  
ATOM   1370  O   HIS A 821     -17.925  -8.463 -38.806  1.00 55.91      A    O  
ANISOU 1370  O   HIS A 821    10854   6149   4239    103  -1207   -568  A    O  
ATOM   1371  CB  HIS A 821     -20.353  -9.636 -40.411  1.00 61.91      A    C  
ANISOU 1371  CB  HIS A 821    12211   6538   4774   -147  -1999   -639  A    C  
ATOM   1372  CG  HIS A 821     -21.804  -9.989 -40.570  1.00 66.59      A    C  
ANISOU 1372  CG  HIS A 821    12852   6997   5452   -361  -2429   -598  A    C  
ATOM   1373  CD2 HIS A 821     -22.906  -9.202 -40.641  1.00 63.06      A    C  
ANISOU 1373  CD2 HIS A 821    12222   6602   5136   -517  -2657   -455  A    C  
ATOM   1374  ND1 HIS A 821     -22.256 -11.294 -40.683  1.00 67.81      A    N  
ANISOU 1374  ND1 HIS A 821    13263   6942   5561   -440  -2689   -699  A    N  
ATOM   1375  CE1 HIS A 821     -23.573 -11.290 -40.814  1.00 68.32      A    C  
ANISOU 1375  CE1 HIS A 821    13273   6954   5733   -666  -3060   -608  A    C  
ATOM   1376  NE2 HIS A 821     -23.991 -10.035 -40.795  1.00 68.85      A    N  
ANISOU 1376  NE2 HIS A 821    13060   7189   5910   -698  -3041   -462  A    N  
ATOM   1377  N   GLY A 822     -17.447 -10.587 -39.427  1.00 58.71      A    N  
ANISOU 1377  N   GLY A 822    11727   6271   4307    301  -1272   -835  A    N  
ATOM   1378  CA  GLY A 822     -16.003 -10.379 -39.612  1.00 59.81      A    C  
ANISOU 1378  CA  GLY A 822    11843   6584   4297    527   -886   -871  A    C  
ATOM   1379  C   GLY A 822     -15.215 -10.220 -38.325  1.00 60.10      A    C  
ANISOU 1379  C   GLY A 822    11481   6754   4598    576   -653   -825  A    C  
ATOM   1380  O   GLY A 822     -14.139  -9.626 -38.330  1.00 69.48      A    O  
ANISOU 1380  O   GLY A 822    12510   8148   5742    684   -347   -782  A    O  
ATOM   1381  N   LYS A 823     -15.748 -10.770 -37.233  1.00 56.71      A    N  
ANISOU 1381  N   LYS A 823    10899   6214   4436    483   -809   -823  A    N  
ATOM   1382  CA  LYS A 823     -15.263 -10.567 -35.875  1.00 55.13      A    C  
ANISOU 1382  CA  LYS A 823    10319   6115   4513    479   -660   -760  A    C  
ATOM   1383  C   LYS A 823     -15.032  -9.099 -35.485  1.00 52.14      A    C  
ANISOU 1383  C   LYS A 823     9605   5939   4265    390   -502   -607  A    C  
ATOM   1384  O   LYS A 823     -14.130  -8.763 -34.690  1.00 51.93      A    O  
ANISOU 1384  O   LYS A 823     9315   6052   4364    445   -286   -566  A    O  
ATOM   1385  CB  LYS A 823     -14.057 -11.493 -35.624  1.00 65.95      A    C  
ANISOU 1385  CB  LYS A 823    11741   7497   5819    729   -461   -877  A    C  
ATOM   1386  CG  LYS A 823     -14.483 -12.964 -35.577  1.00 70.00      A    C  
ANISOU 1386  CG  LYS A 823    12558   7744   6296    775   -685  -1011  A    C  
ATOM   1387  CD  LYS A 823     -13.354 -13.935 -35.267  1.00 73.41      A    C  
ANISOU 1387  CD  LYS A 823    13061   8154   6677   1055   -520  -1132  A    C  
ATOM   1388  CE  LYS A 823     -13.753 -15.388 -35.550  1.00 73.61      A    C  
ANISOU 1388  CE  LYS A 823    13521   7867   6582   1126   -763  -1285  A    C  
ATOM   1389  N   VAL A 824     -15.901  -8.227 -36.006  1.00 49.20      A    N  
ANISOU 1389  N   VAL A 824     9256   5565   3874    244   -643   -518  A    N  
ATOM   1390  CA  VAL A 824     -15.889  -6.814 -35.645  1.00 46.86      A    C  
ANISOU 1390  CA  VAL A 824     8701   5401   3704    147   -558   -372  A    C  
ATOM   1391  C   VAL A 824     -16.634  -6.691 -34.308  1.00 39.15      A    C  
ANISOU 1391  C   VAL A 824     7443   4392   3040     33   -676   -315  A    C  
ATOM   1392  O   VAL A 824     -17.691  -7.278 -34.127  1.00 41.11      A    O  
ANISOU 1392  O   VAL A 824     7725   4524   3371    -51   -911   -330  A    O  
ATOM   1393  CB  VAL A 824     -16.509  -5.931 -36.747  1.00 47.83      A    C  
ANISOU 1393  CB  VAL A 824     8987   5519   3668     68   -672   -298  A    C  
ATOM   1394  CG1 VAL A 824     -16.735  -4.491 -36.273  1.00 46.70      A    C  
ANISOU 1394  CG1 VAL A 824     8608   5451   3683    -37   -654   -147  A    C  
ATOM   1395  CG2 VAL A 824     -15.589  -5.932 -37.963  1.00 50.08      A    C  
ANISOU 1395  CG2 VAL A 824     9524   5880   3625    185   -487   -334  A    C  
ATOM   1396  N   VAL A 825     -16.085  -5.923 -33.388  1.00 39.55      A    N  
ANISOU 1396  N   VAL A 825     7224   4553   3250     22   -517   -243  A    N  
ATOM   1397  CA  VAL A 825     -16.799  -5.606 -32.138  1.00 40.05      A    C  
ANISOU 1397  CA  VAL A 825     7035   4605   3577    -70   -605   -182  A    C  
ATOM   1398  C   VAL A 825     -17.061  -4.110 -31.995  1.00 37.70      A    C  
ANISOU 1398  C   VAL A 825     6607   4367   3351   -136   -595    -65  A    C  
ATOM   1399  O   VAL A 825     -16.319  -3.288 -32.518  1.00 37.27      A    O  
ANISOU 1399  O   VAL A 825     6593   4381   3187   -127   -462    -17  A    O  
ATOM   1400  CB  VAL A 825     -16.125  -6.165 -30.886  1.00 36.43      A    C  
ANISOU 1400  CB  VAL A 825     6397   4174   3269    -25   -487   -213  A    C  
ATOM   1401  CG1 VAL A 825     -16.044  -7.688 -30.989  1.00 41.64      A    C  
ANISOU 1401  CG1 VAL A 825     7224   4727   3870     44   -548   -325  A    C  
ATOM   1402  CG2 VAL A 825     -14.758  -5.541 -30.644  1.00 36.61      A    C  
ANISOU 1402  CG2 VAL A 825     6297   4334   3279     36   -242   -185  A    C  
ATOM   1403  N   LYS A 826     -18.111  -3.800 -31.252  1.00 35.24      A    N  
ANISOU 1403  N   LYS A 826     6142   4028   3219   -197   -735    -17  A    N  
ATOM   1404  CA  LYS A 826     -18.671  -2.465 -31.156  1.00 35.08      A    C  
ANISOU 1404  CA  LYS A 826     6040   4023   3265   -226   -787     79  A    C  
ATOM   1405  C   LYS A 826     -19.141  -2.192 -29.736  1.00 32.30      A    C  
ANISOU 1405  C   LYS A 826     5442   3695   3137   -231   -788    107  A    C  
ATOM   1406  O   LYS A 826     -19.946  -2.950 -29.199  1.00 38.37      A    O  
ANISOU 1406  O   LYS A 826     6113   4455   4011   -257   -890     93  A    O  
ATOM   1407  CB  LYS A 826     -19.857  -2.352 -32.097  1.00 34.89      A    C  
ANISOU 1407  CB  LYS A 826     6133   3945   3177   -257  -1018    112  A    C  
ATOM   1408  CG  LYS A 826     -19.472  -2.187 -33.548  1.00 38.52      A    C  
ANISOU 1408  CG  LYS A 826     6868   4383   3385   -250  -1023    111  A    C  
ATOM   1409  CD  LYS A 826     -20.691  -2.193 -34.444  1.00 39.35      A    C  
ANISOU 1409  CD  LYS A 826     7100   4427   3426   -286  -1294    140  A    C  
ATOM   1410  CE  LYS A 826     -20.315  -1.968 -35.907  1.00 43.18      A    C  
ANISOU 1410  CE  LYS A 826     7895   4886   3625   -278  -1303    145  A    C  
ATOM   1411  NZ  LYS A 826     -19.982  -0.534 -36.139  1.00 45.78      A    N1+
ANISOU 1411  NZ  LYS A 826     8243   5239   3912   -275  -1225    254  A    N1+
ATOM   1412  N   ILE A 827     -18.722  -1.062 -29.196  1.00 32.28      A    N  
ANISOU 1412  N   ILE A 827     5361   3716   3187   -218   -694    157  A    N  
ATOM   1413  CA  ILE A 827     -19.086  -0.630 -27.851  1.00 31.54      A    C  
ANISOU 1413  CA  ILE A 827     5077   3640   3268   -197   -679    175  A    C  
ATOM   1414  C   ILE A 827     -20.494  -0.070 -27.902  1.00 35.09      A    C  
ANISOU 1414  C   ILE A 827     5469   4078   3785   -162   -843    226  A    C  
ATOM   1415  O   ILE A 827     -20.792   0.767 -28.758  1.00 32.34      A    O  
ANISOU 1415  O   ILE A 827     5236   3690   3363   -143   -928    275  A    O  
ATOM   1416  CB  ILE A 827     -18.125   0.443 -27.318  1.00 34.03      A    C  
ANISOU 1416  CB  ILE A 827     5380   3957   3594   -198   -550    204  A    C  
ATOM   1417  CG1 ILE A 827     -16.693  -0.131 -27.326  1.00 32.43      A    C  
ANISOU 1417  CG1 ILE A 827     5184   3807   3331   -229   -389    171  A    C  
ATOM   1418  CG2 ILE A 827     -18.560   0.892 -25.908  1.00 35.40      A    C  
ANISOU 1418  CG2 ILE A 827     5402   4132   3917   -155   -547    206  A    C  
ATOM   1419  CD1 ILE A 827     -15.603   0.842 -27.010  1.00 35.62      A    C  
ANISOU 1419  CD1 ILE A 827     5574   4231   3730   -278   -279    220  A    C  
ATOM   1420  N   CYS A 828     -21.353  -0.536 -26.993  1.00 35.09      A    N  
ANISOU 1420  N   CYS A 828     5286   4126   3922   -149   -886    226  A    N  
ATOM   1421  CA  CYS A 828     -22.735  -0.097 -26.953  1.00 39.58      A    C  
ANISOU 1421  CA  CYS A 828     5735   4732   4573    -97  -1028    283  A    C  
ATOM   1422  C   CYS A 828     -23.001   0.546 -25.617  1.00 41.77      A    C  
ANISOU 1422  C   CYS A 828     5845   5057   4967     -3   -941    294  A    C  
ATOM   1423  O   CYS A 828     -22.265   0.325 -24.647  1.00 41.11      A    O  
ANISOU 1423  O   CYS A 828     5726   4982   4913    -16   -801    255  A    O  
ATOM   1424  CB  CYS A 828     -23.710  -1.259 -27.222  1.00 42.76      A    C  
ANISOU 1424  CB  CYS A 828     6052   5180   5016   -179  -1176    298  A    C  
ATOM   1425  SG  CYS A 828     -24.002  -2.410 -25.884  1.00 62.97      A    S  
ANISOU 1425  SG  CYS A 828     8401   7817   7707   -249  -1115    295  A    S  
ATOM   1426  N   ASP A 829     -24.035   1.384 -25.608  1.00 61.33      A    N  
ANISOU 1426  N   ASP A 829     8239   7564   7498    111  -1032    344  A    N  
ATOM   1427  CA  ASP A 829     -24.650   1.875 -24.394  1.00 75.70      A    C  
ANISOU 1427  CA  ASP A 829     9880   9461   9421    240   -968    353  A    C  
ATOM   1428  C   ASP A 829     -25.964   1.109 -24.233  1.00 77.84      A    C  
ANISOU 1428  C   ASP A 829     9896   9885   9793    225  -1054    411  A    C  
ATOM   1429  O   ASP A 829     -26.877   1.275 -25.077  1.00 61.58      A    O  
ANISOU 1429  O   ASP A 829     7788   7860   7748    251  -1224    469  A    O  
ATOM   1430  CB  ASP A 829     -24.909   3.372 -24.518  1.00 76.97      A    C  
ANISOU 1430  CB  ASP A 829    10130   9549   9565    413  -1010    370  A    C  
ATOM   1431  CG  ASP A 829     -25.460   3.989 -23.244  1.00 89.20      A    C  
ANISOU 1431  CG  ASP A 829    11543  11160  11188    597   -926    357  A    C  
ATOM   1432  OD1 ASP A 829     -25.608   3.313 -22.192  1.00 95.40      A    O  
ANISOU 1432  OD1 ASP A 829    12156  12060  12030    581   -814    342  A    O  
ATOM   1433  OD2 ASP A 829     -25.726   5.205 -23.290  1.00 77.14      A    O1-
ANISOU 1433  OD2 ASP A 829    10113   9553   9644    771   -972    360  A    O1-
ATOM   1434  N   PHE A 830     -26.032   0.315 -23.151  1.00 50.87      A    N  
ANISOU 1434  N   PHE A 830     6322   6565   6442    171   -947    408  A    N  
ATOM   1435  CA  PHE A 830     -27.208  -0.456 -22.679  1.00 76.64      A    C  
ANISOU 1435  CA  PHE A 830     9306  10004   9809    122   -985    485  A    C  
ATOM   1436  C   PHE A 830     -27.418  -1.716 -23.511  1.00 78.64      A    C  
ANISOU 1436  C   PHE A 830     9578  10242  10060    -95  -1140    517  A    C  
ATOM   1437  O   PHE A 830     -28.226  -2.576 -23.147  1.00 92.82      A    O  
ANISOU 1437  O   PHE A 830    11172  12159  11937   -213  -1188    592  A    O  
ATOM   1438  CB  PHE A 830     -28.520   0.379 -22.601  1.00104.58      A    C  
ANISOU 1438  CB  PHE A 830    12621  13691  13426    303  -1041    558  A    C  
ATOM   1439  CG  PHE A 830     -28.929   0.780 -21.210  1.00125.76      A    C  
ANISOU 1439  CG  PHE A 830    15112  16514  16156    463   -864    566  A    C  
ATOM   1440  CD1 PHE A 830     -29.740  -0.058 -20.431  1.00137.86      A    C  
ANISOU 1440  CD1 PHE A 830    16355  18258  17768    385   -807    650  A    C  
ATOM   1441  CD2 PHE A 830     -28.545   2.021 -20.681  1.00146.25      A    C  
ANISOU 1441  CD2 PHE A 830    17835  19031  18701    691   -760    496  A    C  
ATOM   1442  CE1 PHE A 830     -30.140   0.323 -19.144  1.00138.02      A    C  
ANISOU 1442  CE1 PHE A 830    16206  18433  17802    551   -619    660  A    C  
ATOM   1443  CE2 PHE A 830     -28.939   2.403 -19.396  1.00150.42      A    C  
ANISOU 1443  CE2 PHE A 830    18227  19685  19242    866   -595    487  A    C  
ATOM   1444  CZ  PHE A 830     -29.737   1.555 -18.625  1.00142.63      A    C  
ANISOU 1444  CZ  PHE A 830    16940  18933  18319    808   -509    568  A    C  
ATOM   1445  N   MET A 837     -31.711  -5.256 -11.185  1.00107.30      A    N  
ANISOU 1445  N   MET A 837    11364  15623  13783   -281    417   1269  A    N  
ATOM   1446  CA  MET A 837     -32.301  -6.028 -10.096  1.00113.49      A    C  
ANISOU 1446  CA  MET A 837    11957  16640  14524   -437    573   1442  A    C  
ATOM   1447  C   MET A 837     -31.930  -7.520 -10.169  1.00117.06      A    C  
ANISOU 1447  C   MET A 837    12538  16940  15002   -831    427   1541  A    C  
ATOM   1448  O   MET A 837     -31.332  -8.054  -9.232  1.00117.23      A    O  
ANISOU 1448  O   MET A 837    12734  16892  14917   -911    518   1553  A    O  
ATOM   1449  CB  MET A 837     -33.827  -5.853 -10.088  1.00119.90      A    C  
ANISOU 1449  CB  MET A 837    12295  17842  15419   -407    651   1619  A    C  
ATOM   1450  CG  MET A 837     -34.315  -4.420  -9.891  1.00115.20      A    C  
ANISOU 1450  CG  MET A 837    11559  17424  14788     27    814   1533  A    C  
ATOM   1451  N   SER A 838     -32.277  -8.173 -11.283  1.00121.62      A    N  
ANISOU 1451  N   SER A 838    13060  17445  15707  -1064    184   1607  A    N  
ATOM   1452  CA  SER A 838     -31.953  -9.606 -11.518  1.00123.60      A    C  
ANISOU 1452  CA  SER A 838    13484  17498  15982  -1430     -4   1686  A    C  
ATOM   1453  C   SER A 838     -30.445  -9.933 -11.707  1.00123.26      A    C  
ANISOU 1453  C   SER A 838    13888  17077  15868  -1411    -92   1509  A    C  
ATOM   1454  O   SER A 838     -30.027 -11.072 -11.460  1.00110.33      A    O  
ANISOU 1454  O   SER A 838    12437  15279  14206  -1639   -178   1563  A    O  
ATOM   1455  CB  SER A 838     -32.737 -10.136 -12.727  1.00119.01      A    C  
ANISOU 1455  CB  SER A 838    12762  16919  15538  -1666   -269   1784  A    C  
ATOM   1456  N   ASP A 839     -29.658  -8.940 -12.146  1.00103.83      A    N  
ANISOU 1456  N   ASP A 839    11587  14485  13378  -1139    -77   1312  A    N  
ATOM   1457  CA  ASP A 839     -28.219  -9.075 -12.440  1.00 80.56      A    C  
ANISOU 1457  CA  ASP A 839     9003  11228  10376  -1086   -148   1144  A    C  
ATOM   1458  C   ASP A 839     -27.361  -8.828 -11.177  1.00 72.37      A    C  
ANISOU 1458  C   ASP A 839     8110  10165   9221   -956     30   1084  A    C  
ATOM   1459  O   ASP A 839     -27.370  -7.721 -10.620  1.00 60.51      A    O  
ANISOU 1459  O   ASP A 839     6555   8774   7663   -723    189   1021  A    O  
ATOM   1460  CB  ASP A 839     -27.848  -8.069 -13.551  1.00 76.17      A    C  
ANISOU 1460  CB  ASP A 839     8521  10576   9844   -890   -217    993  A    C  
ATOM   1461  CG  ASP A 839     -26.511  -8.361 -14.214  1.00 71.25      A    C  
ANISOU 1461  CG  ASP A 839     8219   9667   9186   -884   -322    852  A    C  
ATOM   1462  OD1 ASP A 839     -25.521  -8.653 -13.517  1.00 57.54      A    O  
ANISOU 1462  OD1 ASP A 839     6658   7821   7384   -862   -261    800  A    O  
ATOM   1463  OD2 ASP A 839     -26.436  -8.266 -15.456  1.00 77.24      A    O1-
ANISOU 1463  OD2 ASP A 839     9050  10324   9974   -886   -464    794  A    O1-
ATOM   1464  N   SER A 840     -26.589  -9.837 -10.763  1.00 55.32      A    N  
ANISOU 1464  N   SER A 840     6164   7837   7018  -1094    -22   1095  A    N  
ATOM   1465  CA  SER A 840     -25.660  -9.694  -9.624  1.00 61.85      A    C  
ANISOU 1465  CA  SER A 840     7158   8612   7731   -987     98   1038  A    C  
ATOM   1466  C   SER A 840     -24.388  -8.854  -9.893  1.00 50.65      A    C  
ANISOU 1466  C   SER A 840     5933   7033   6281   -773     90    845  A    C  
ATOM   1467  O   SER A 840     -23.638  -8.574  -8.963  1.00 50.42      A    O  
ANISOU 1467  O   SER A 840     6025   6974   6160   -677    171    794  A    O  
ATOM   1468  CB  SER A 840     -25.253 -11.070  -9.089  1.00 66.69      A    C  
ANISOU 1468  CB  SER A 840     7939   9091   8308  -1194     21   1127  A    C  
ATOM   1469  OG  SER A 840     -24.517 -11.799 -10.055  1.00 80.70      A    O  
ANISOU 1469  OG  SER A 840     9918  10611  10135  -1259   -176   1055  A    O  
ATOM   1470  N   ASN A 841     -24.124  -8.465 -11.139  1.00 47.85      A    N  
ANISOU 1470  N   ASN A 841     5611   6579   5992   -718    -13    750  A    N  
ATOM   1471  CA  ASN A 841     -23.004  -7.530 -11.431  1.00 42.67      A    C  
ANISOU 1471  CA  ASN A 841     5097   5807   5307   -538     -6    595  A    C  
ATOM   1472  C   ASN A 841     -23.245  -6.050 -11.121  1.00 39.17      A    C  
ANISOU 1472  C   ASN A 841     4588   5467   4828   -336    109    536  A    C  
ATOM   1473  O   ASN A 841     -22.271  -5.299 -11.071  1.00 38.93      A    O  
ANISOU 1473  O   ASN A 841     4696   5337   4758   -223    116    428  A    O  
ATOM   1474  CB  ASN A 841     -22.504  -7.720 -12.848  1.00 46.08      A    C  
ANISOU 1474  CB  ASN A 841     5624   6091   5793   -560   -145    524  A    C  
ATOM   1475  CG  ASN A 841     -21.981  -9.129 -13.074  1.00 49.36      A    C  
ANISOU 1475  CG  ASN A 841     6187   6355   6215   -699   -260    541  A    C  
ATOM   1476  ND2 ASN A 841     -22.502  -9.808 -14.090  1.00 51.10      A    N  
ANISOU 1476  ND2 ASN A 841     6419   6517   6481   -818   -394    570  A    N  
ATOM   1477  OD1 ASN A 841     -21.121  -9.604 -12.320  1.00 46.51      A    O  
ANISOU 1477  OD1 ASN A 841     5946   5917   5810   -690   -244    528  A    O  
ATOM   1478  N   TYR A 842     -24.503  -5.657 -10.890  1.00 39.67      A    N  
ANISOU 1478  N   TYR A 842     4447   5725   4903   -289    192    610  A    N  
ATOM   1479  CA  TYR A 842     -24.870  -4.308 -10.474  1.00 40.21      A    C  
ANISOU 1479  CA  TYR A 842     4468   5891   4920    -59    309    556  A    C  
ATOM   1480  C   TYR A 842     -25.355  -4.321  -9.044  1.00 41.50      A    C  
ANISOU 1480  C   TYR A 842     4565   6223   4980     -5    483    615  A    C  
ATOM   1481  O   TYR A 842     -26.247  -5.080  -8.719  1.00 47.09      A    O  
ANISOU 1481  O   TYR A 842     5086   7101   5704   -125    536    755  A    O  
ATOM   1482  CB  TYR A 842     -25.973  -3.750 -11.374  1.00 40.88      A    C  
ANISOU 1482  CB  TYR A 842     4355   6089   5088     16    276    589  A    C  
ATOM   1483  CG  TYR A 842     -25.536  -3.563 -12.807  1.00 42.15      A    C  
ANISOU 1483  CG  TYR A 842     4610   6088   5317    -12    111    526  A    C  
ATOM   1484  CD1 TYR A 842     -24.954  -2.352 -13.234  1.00 42.45      A    C  
ANISOU 1484  CD1 TYR A 842     4795   6006   5326    154     91    413  A    C  
ATOM   1485  CD2 TYR A 842     -25.686  -4.591 -13.747  1.00 41.80      A    C  
ANISOU 1485  CD2 TYR A 842     4539   5997   5346   -212    -34    583  A    C  
ATOM   1486  CE1 TYR A 842     -24.551  -2.172 -14.555  1.00 39.81      A    C  
ANISOU 1486  CE1 TYR A 842     4555   5540   5032    119    -43    372  A    C  
ATOM   1487  CE2 TYR A 842     -25.281  -4.428 -15.072  1.00 45.71      A    C  
ANISOU 1487  CE2 TYR A 842     5146   6351   5869   -225   -172    522  A    C  
ATOM   1488  CZ  TYR A 842     -24.705  -3.214 -15.475  1.00 44.23      A    C  
ANISOU 1488  CZ  TYR A 842     5083   6074   5648    -59   -165    422  A    C  
ATOM   1489  OH  TYR A 842     -24.306  -3.054 -16.784  1.00 38.60      A    O  
ANISOU 1489  OH  TYR A 842     4487   5240   4941    -83   -286    379  A    O  
ATOM   1490  N   VAL A 843     -24.777  -3.466  -8.206  1.00 39.59      A    N  
ANISOU 1490  N   VAL A 843     4486   5936   4620    166    566    516  A    N  
ATOM   1491  CA  VAL A 843     -25.188  -3.282  -6.826  1.00 43.67      A    C  
ANISOU 1491  CA  VAL A 843     4993   6607   4994    269    746    544  A    C  
ATOM   1492  C   VAL A 843     -26.125  -2.100  -6.759  1.00 43.52      A    C  
ANISOU 1492  C   VAL A 843     4862   6734   4941    536    863    508  A    C  
ATOM   1493  O   VAL A 843     -25.780  -1.010  -7.229  1.00 41.13      A    O  
ANISOU 1493  O   VAL A 843     4689   6296   4641    703    802    384  A    O  
ATOM   1494  CB  VAL A 843     -23.983  -2.939  -5.912  1.00 48.11      A    C  
ANISOU 1494  CB  VAL A 843     5847   7013   5419    324    743    437  A    C  
ATOM   1495  CG1 VAL A 843     -24.420  -2.608  -4.475  1.00 55.24      A    C  
ANISOU 1495  CG1 VAL A 843     6792   8067   6131    466    931    446  A    C  
ATOM   1496  CG2 VAL A 843     -23.003  -4.078  -5.915  1.00 48.35      A    C  
ANISOU 1496  CG2 VAL A 843     5985   6906   5481    105    625    471  A    C  
ATOM   1497  N   VAL A 844     -27.253  -2.302  -6.096  1.00 45.31      A    N  
ANISOU 1497  N   VAL A 844     4863   7233   5119    586   1036    619  A    N  
ATOM   1498  CA  VAL A 844     -28.223  -1.244  -5.820  1.00 53.77      A    C  
ANISOU 1498  CA  VAL A 844     5806   8492   6133    893   1189    592  A    C  
ATOM   1499  C   VAL A 844     -27.705  -0.382  -4.664  1.00 57.45      A    C  
ANISOU 1499  C   VAL A 844     6555   8889   6383   1125   1303    456  A    C  
ATOM   1500  O   VAL A 844     -27.264  -0.928  -3.648  1.00 54.35      A    O  
ANISOU 1500  O   VAL A 844     6290   8503   5858   1032   1374    480  A    O  
ATOM   1501  CB  VAL A 844     -29.593  -1.853  -5.444  1.00 53.24      A    C  
ANISOU 1501  CB  VAL A 844     5360   8790   6079    854   1360    781  A    C  
ATOM   1502  CG1 VAL A 844     -30.581  -0.795  -4.961  1.00 56.67      A    C  
ANISOU 1502  CG1 VAL A 844     5647   9463   6424   1225   1564    754  A    C  
ATOM   1503  CG2 VAL A 844     -30.148  -2.614  -6.643  1.00 55.53      A    C  
ANISOU 1503  CG2 VAL A 844     5388   9128   6582    616   1203    911  A    C  
ATOM   1504  N   ARG A 845     -27.799   0.944  -4.829  1.00 62.67      A    N  
ANISOU 1504  N   ARG A 845     7334   9474   7004   1425   1304    320  A    N  
ATOM   1505  CA  ARG A 845     -27.398   1.941  -3.813  1.00 68.38      A    C  
ANISOU 1505  CA  ARG A 845     8371  10099   7511   1682   1384    168  A    C  
ATOM   1506  C   ARG A 845     -28.186   3.252  -4.070  1.00 68.68      A    C  
ANISOU 1506  C   ARG A 845     8398  10172   7527   2064   1436     77  A    C  
ATOM   1507  O   ARG A 845     -27.750   4.116  -4.843  1.00 70.88      A    O  
ANISOU 1507  O   ARG A 845     8857  10209   7867   2141   1267    -28  A    O  
ATOM   1508  CB  ARG A 845     -25.867   2.144  -3.857  1.00 74.80      A    C  
ANISOU 1508  CB  ARG A 845     9549  10570   8301   1544   1185     50  A    C  
ATOM   1509  CG  ARG A 845     -25.226   2.794  -2.629  1.00 92.63      A    C  
ANISOU 1509  CG  ARG A 845    12166  12706  10321   1684   1220    -79  A    C  
ATOM   1510  CD  ARG A 845     -23.684   2.681  -2.655  1.00111.69      A    C  
ANISOU 1510  CD  ARG A 845    14853  14837  12746   1460   1006   -141  A    C  
ATOM   1511  NE  ARG A 845     -23.051   2.356  -1.351  1.00107.73      A    N  
ANISOU 1511  NE  ARG A 845    14569  14313  12049   1408   1033   -161  A    N  
ATOM   1512  CZ  ARG A 845     -22.487   1.186  -0.982  1.00 94.15      A    C  
ANISOU 1512  CZ  ARG A 845    12818  12617  10339   1162   1000    -66  A    C  
ATOM   1513  NH1 ARG A 845     -22.443   0.110  -1.781  1.00 89.75      A    N1+
ANISOU 1513  NH1 ARG A 845    12027  12100   9973    931    945     55  A    N1+
ATOM   1514  NH2 ARG A 845     -21.949   1.082   0.237  1.00 92.25      A    N  
ANISOU 1514  NH2 ARG A 845    12814  12343   9895   1156   1008    -95  A    N  
ATOM   1515  N   GLY A 846     -29.364   3.355  -3.443  1.00 68.60      A    N  
ANISOU 1515  N   GLY A 846     8163  10475   7429   2300   1673    134  A    N  
ATOM   1516  CA  GLY A 846     -30.345   4.428  -3.697  1.00 72.57      A    C  
ANISOU 1516  CA  GLY A 846     8561  11085   7927   2700   1750     80  A    C  
ATOM   1517  C   GLY A 846     -30.795   4.472  -5.159  1.00 79.06      A    C  
ANISOU 1517  C   GLY A 846     9138  11902   9000   2644   1581    147  A    C  
ATOM   1518  O   GLY A 846     -31.341   3.485  -5.679  1.00 70.45      A    O  
ANISOU 1518  O   GLY A 846     7684  11017   8069   2405   1572    320  A    O  
ATOM   1519  N   ASN A 847     -30.525   5.604  -5.820  1.00 77.91      A    N  
ANISOU 1519  N   ASN A 847     9226  11499   8878   2842   1424     15  A    N  
ATOM   1520  CA  ASN A 847     -30.804   5.785  -7.246  1.00 77.90      A    C  
ANISOU 1520  CA  ASN A 847     9081  11435   9084   2799   1230     61  A    C  
ATOM   1521  C   ASN A 847     -29.844   5.017  -8.156  1.00 68.96      A    C  
ANISOU 1521  C   ASN A 847     8011  10102   8087   2375   1018    104  A    C  
ATOM   1522  O   ASN A 847     -30.198   4.737  -9.308  1.00 69.51      A    O  
ANISOU 1522  O   ASN A 847     7885  10199   8325   2256    882    188  A    O  
ATOM   1523  CB  ASN A 847     -30.787   7.277  -7.624  1.00 87.67      A    C  
ANISOU 1523  CB  ASN A 847    10599  12434  10278   3147   1124    -87  A    C  
ATOM   1524  N   ALA A 848     -28.655   4.663  -7.654  1.00 57.94      A    N  
ANISOU 1524  N   ALA A 848     6883   8519   6612   2162    985     48  A    N  
ATOM   1525  CA  ALA A 848     -27.588   4.098  -8.487  1.00 54.21      A    C  
ANISOU 1525  CA  ALA A 848     6518   7834   6244   1824    792     60  A    C  
ATOM   1526  C   ALA A 848     -27.654   2.556  -8.609  1.00 50.09      A    C  
ANISOU 1526  C   ALA A 848     5749   7467   5818   1497    804    204  A    C  
ATOM   1527  O   ALA A 848     -28.172   1.870  -7.732  1.00 50.21      A    O  
ANISOU 1527  O   ALA A 848     5598   7702   5778   1467    963    288  A    O  
ATOM   1528  CB  ALA A 848     -26.235   4.538  -7.943  1.00 52.34      A    C  
ANISOU 1528  CB  ALA A 848     6675   7323   5888   1770    726    -66  A    C  
ATOM   1529  N   ARG A 849     -27.131   2.056  -9.722  1.00 49.33      A    N  
ANISOU 1529  N   ARG A 849     5657   7240   5848   1262    630    233  A    N  
ATOM   1530  CA  ARG A 849     -26.989   0.635 -10.025  1.00 47.49      A    C  
ANISOU 1530  CA  ARG A 849     5285   7057   5700    949    583    342  A    C  
ATOM   1531  C   ARG A 849     -25.550   0.526 -10.475  1.00 43.31      A    C  
ANISOU 1531  C   ARG A 849     5021   6261   5175    790    447    263  A    C  
ATOM   1532  O   ARG A 849     -25.231   0.890 -11.592  1.00 50.13      A    O  
ANISOU 1532  O   ARG A 849     5953   6990   6104    766    314    232  A    O  
ATOM   1533  CB  ARG A 849     -27.949   0.185 -11.136  1.00 56.63      A    C  
ANISOU 1533  CB  ARG A 849     6168   8341   7007    863    491    453  A    C  
ATOM   1534  CG  ARG A 849     -29.413   0.542 -10.924  1.00 56.95      A    C  
ANISOU 1534  CG  ARG A 849     5900   8666   7073   1061    598    535  A    C  
ATOM   1535  CD  ARG A 849     -30.105  -0.355  -9.917  1.00 59.39      A    C  
ANISOU 1535  CD  ARG A 849     5965   9248   7352    966    769    668  A    C  
ATOM   1536  NE  ARG A 849     -31.518   0.039  -9.770  1.00 57.88      A    N  
ANISOU 1536  NE  ARG A 849     5426   9374   7193   1172    887    760  A    N  
ATOM   1537  CZ  ARG A 849     -32.000   0.979  -8.952  1.00 58.63      A    C  
ANISOU 1537  CZ  ARG A 849     5495   9607   7175   1521   1075    705  A    C  
ATOM   1538  NH1 ARG A 849     -31.204   1.682  -8.125  1.00 61.77      A    N1+
ANISOU 1538  NH1 ARG A 849     6233   9834   7404   1699   1160    551  A    N1+
ATOM   1539  NH2 ARG A 849     -33.318   1.209  -8.936  1.00 59.12      A    N  
ANISOU 1539  NH2 ARG A 849     5183   9993   7288   1705   1178    809  A    N  
ATOM   1540  N   LEU A 850     -24.672   0.062  -9.584  1.00 39.65      A    N  
ANISOU 1540  N   LEU A 850     4702   5734   4630    694    485    239  A    N  
ATOM   1541  CA  LEU A 850     -23.229   0.225  -9.737  1.00 40.27      A    C  
ANISOU 1541  CA  LEU A 850     5027   5586   4689    605    380    154  A    C  
ATOM   1542  C   LEU A 850     -22.548  -1.075 -10.189  1.00 40.85      A    C  
ANISOU 1542  C   LEU A 850     5077   5610   4833    360    299    206  A    C  
ATOM   1543  O   LEU A 850     -22.645  -2.082  -9.486  1.00 35.99      A    O  
ANISOU 1543  O   LEU A 850     4405   5072   4196    256    349    274  A    O  
ATOM   1544  CB  LEU A 850     -22.619   0.678  -8.413  1.00 41.91      A    C  
ANISOU 1544  CB  LEU A 850     5434   5742   4749    687    444     82  A    C  
ATOM   1545  CG  LEU A 850     -23.146   1.967  -7.771  1.00 51.92      A    C  
ANISOU 1545  CG  LEU A 850     6809   7017   5900    960    524      0  A    C  
ATOM   1546  CD1 LEU A 850     -22.628   2.099  -6.340  1.00 53.05      A    C  
ANISOU 1546  CD1 LEU A 850     7154   7132   5869   1006    588    -57  A    C  
ATOM   1547  CD2 LEU A 850     -22.781   3.192  -8.593  1.00 48.83      A    C  
ANISOU 1547  CD2 LEU A 850     6587   6431   5534   1051    401    -85  A    C  
ATOM   1548  N   PRO A 851     -21.819  -1.052 -11.329  1.00 38.97      A    N  
ANISOU 1548  N   PRO A 851     4908   5237   4663    279    178    175  A    N  
ATOM   1549  CA  PRO A 851     -21.045  -2.215 -11.777  1.00 34.22      A    C  
ANISOU 1549  CA  PRO A 851     4323   4570   4108     99    106    199  A    C  
ATOM   1550  C   PRO A 851     -19.721  -2.331 -10.995  1.00 32.11      A    C  
ANISOU 1550  C   PRO A 851     4205   4211   3783     64     99    152  A    C  
ATOM   1551  O   PRO A 851     -18.639  -2.057 -11.518  1.00 30.19      A    O  
ANISOU 1551  O   PRO A 851     4055   3861   3554     34     33    104  A    O  
ATOM   1552  CB  PRO A 851     -20.861  -1.924 -13.266  1.00 35.85      A    C  
ANISOU 1552  CB  PRO A 851     4550   4697   4375     78     10    176  A    C  
ATOM   1553  CG  PRO A 851     -20.736  -0.442 -13.315  1.00 37.72      A    C  
ANISOU 1553  CG  PRO A 851     4885   4874   4574    214     12    115  A    C  
ATOM   1554  CD  PRO A 851     -21.679   0.075 -12.276  1.00 36.15      A    C  
ANISOU 1554  CD  PRO A 851     4632   4779   4325    364    108    119  A    C  
ATOM   1555  N   VAL A 852     -19.833  -2.691  -9.714  1.00 33.60      A    N  
ANISOU 1555  N   VAL A 852     4407   4460   3899     69    167    178  A    N  
ATOM   1556  CA  VAL A 852     -18.750  -2.504  -8.716  1.00 33.94      A    C  
ANISOU 1556  CA  VAL A 852     4604   4431   3859     73    153    132  A    C  
ATOM   1557  C   VAL A 852     -17.413  -3.118  -9.133  1.00 29.76      A    C  
ANISOU 1557  C   VAL A 852     4124   3801   3381    -28     50    119  A    C  
ATOM   1558  O   VAL A 852     -16.361  -2.474  -9.030  1.00 28.70      A    O  
ANISOU 1558  O   VAL A 852     4084   3591   3230    -25     -7     66  A    O  
ATOM   1559  CB  VAL A 852     -19.208  -2.982  -7.290  1.00 36.96      A    C  
ANISOU 1559  CB  VAL A 852     4999   4910   4133     85    244    181  A    C  
ATOM   1560  CG1 VAL A 852     -18.049  -3.267  -6.349  1.00 35.81      A    C  
ANISOU 1560  CG1 VAL A 852     5005   4688   3913     41    186    162  A    C  
ATOM   1561  CG2 VAL A 852     -20.106  -1.918  -6.659  1.00 38.63      A    C  
ANISOU 1561  CG2 VAL A 852     5224   5209   4246    257    359    148  A    C  
ATOM   1562  N   LYS A 853     -17.454  -4.350  -9.614  1.00 28.06      A    N  
ANISOU 1562  N   LYS A 853     3846   3587   3227   -116     21    172  A    N  
ATOM   1563  CA  LYS A 853     -16.213  -5.041  -9.980  1.00 27.93      A    C  
ANISOU 1563  CA  LYS A 853     3872   3490   3250   -164    -61    157  A    C  
ATOM   1564  C   LYS A 853     -15.502  -4.461 -11.218  1.00 30.05      A    C  
ANISOU 1564  C   LYS A 853     4134   3714   3571   -153    -98    106  A    C  
ATOM   1565  O   LYS A 853     -14.353  -4.829 -11.464  1.00 31.63      A    O  
ANISOU 1565  O   LYS A 853     4344   3879   3793   -164   -143     90  A    O  
ATOM   1566  CB  LYS A 853     -16.467  -6.547 -10.151  1.00 32.21      A    C  
ANISOU 1566  CB  LYS A 853     4401   4012   3825   -238    -95    218  A    C  
ATOM   1567  CG  LYS A 853     -16.795  -7.268  -8.845  1.00 31.12      A    C  
ANISOU 1567  CG  LYS A 853     4301   3901   3623   -283    -75    291  A    C  
ATOM   1568  CD  LYS A 853     -16.797  -8.782  -9.057  1.00 29.70      A    C  
ANISOU 1568  CD  LYS A 853     4162   3646   3475   -370   -149    351  A    C  
ATOM   1569  CE  LYS A 853     -16.899  -9.574  -7.771  1.00 33.52      A    C  
ANISOU 1569  CE  LYS A 853     4721   4130   3886   -430   -152    439  A    C  
ATOM   1570  NZ  LYS A 853     -16.757 -11.049  -8.026  1.00 30.79      A    N1+
ANISOU 1570  NZ  LYS A 853     4468   3658   3572   -510   -260    495  A    N1+
ATOM   1571  N   TRP A 854     -16.167  -3.562 -11.966  1.00 28.27      A    N  
ANISOU 1571  N   TRP A 854     3884   3499   3357   -122    -76     89  A    N  
ATOM   1572  CA  TRP A 854     -15.577  -2.861 -13.115  1.00 29.95      A    C  
ANISOU 1572  CA  TRP A 854     4113   3672   3594   -124   -103     58  A    C  
ATOM   1573  C   TRP A 854     -15.113  -1.463 -12.805  1.00 30.91      A    C  
ANISOU 1573  C   TRP A 854     4309   3755   3681   -105   -115     27  A    C  
ATOM   1574  O   TRP A 854     -14.468  -0.846 -13.650  1.00 30.99      A    O  
ANISOU 1574  O   TRP A 854     4341   3732   3703   -139   -141     22  A    O  
ATOM   1575  CB  TRP A 854     -16.582  -2.853 -14.307  1.00 29.13      A    C  
ANISOU 1575  CB  TRP A 854     3970   3580   3519   -118   -108     72  A    C  
ATOM   1576  CG  TRP A 854     -16.676  -4.208 -14.970  1.00 29.87      A    C  
ANISOU 1576  CG  TRP A 854     4043   3667   3640   -168   -140     89  A    C  
ATOM   1577  CD1 TRP A 854     -16.046  -4.598 -16.115  1.00 29.30      A    C  
ANISOU 1577  CD1 TRP A 854     4009   3557   3566   -178   -166     66  A    C  
ATOM   1578  CD2 TRP A 854     -17.436  -5.365 -14.521  1.00 31.02      A    C  
ANISOU 1578  CD2 TRP A 854     4155   3830   3802   -217   -156    136  A    C  
ATOM   1579  CE2 TRP A 854     -17.215  -6.397 -15.466  1.00 28.07      A    C  
ANISOU 1579  CE2 TRP A 854     3833   3394   3439   -255   -218    126  A    C  
ATOM   1580  CE3 TRP A 854     -18.289  -5.613 -13.438  1.00 28.26      A    C  
ANISOU 1580  CE3 TRP A 854     3748   3544   3445   -239   -121    192  A    C  
ATOM   1581  NE1 TRP A 854     -16.380  -5.886 -16.427  1.00 28.16      A    N  
ANISOU 1581  NE1 TRP A 854     3886   3382   3431   -211   -211     76  A    N  
ATOM   1582  CZ2 TRP A 854     -17.769  -7.683 -15.328  1.00 29.43      A    C  
ANISOU 1582  CZ2 TRP A 854     4027   3531   3626   -334   -277    171  A    C  
ATOM   1583  CZ3 TRP A 854     -18.867  -6.905 -13.303  1.00 32.40      A    C  
ANISOU 1583  CZ3 TRP A 854     4258   4065   3988   -338   -161    258  A    C  
ATOM   1584  CH2 TRP A 854     -18.581  -7.924 -14.236  1.00 30.15      A    C  
ANISOU 1584  CH2 TRP A 854     4050   3681   3723   -393   -253    246  A    C  
ATOM   1585  N   MET A 855     -15.375  -0.966 -11.592  1.00 30.77      A    N  
ANISOU 1585  N   MET A 855     4353   3733   3605    -60   -103     11  A    N  
ATOM   1586  CA  MET A 855     -15.249   0.459 -11.316  1.00 31.86      A    C  
ANISOU 1586  CA  MET A 855     4615   3799   3693    -23   -133    -29  A    C  
ATOM   1587  C   MET A 855     -13.871   0.780 -10.746  1.00 33.01      A    C  
ANISOU 1587  C   MET A 855     4834   3890   3817   -109   -212    -41  A    C  
ATOM   1588  O   MET A 855     -13.382   0.102  -9.842  1.00 33.18      A    O  
ANISOU 1588  O   MET A 855     4848   3940   3817   -132   -228    -34  A    O  
ATOM   1589  CB  MET A 855     -16.321   0.918 -10.330  1.00 31.53      A    C  
ANISOU 1589  CB  MET A 855     4631   3777   3573    104    -76    -56  A    C  
ATOM   1590  CG  MET A 855     -17.685   1.050 -10.964  1.00 31.89      A    C  
ANISOU 1590  CG  MET A 855     4588   3883   3646    203    -18    -38  A    C  
ATOM   1591  SD  MET A 855     -19.022   1.177  -9.758  1.00 36.50      A    S  
ANISOU 1591  SD  MET A 855     5146   4580   4143    372    101    -42  A    S  
ATOM   1592  CE  MET A 855     -18.781   2.843  -9.165  1.00 37.38      A    C  
ANISOU 1592  CE  MET A 855     5513   4548   4141    516     63   -142  A    C  
ATOM   1593  N   ALA A 856     -13.284   1.860 -11.241  1.00 29.72      A    N  
ANISOU 1593  N   ALA A 856     4497   3393   3401   -167   -277    -47  A    N  
ATOM   1594  CA  ALA A 856     -12.060   2.395 -10.692  1.00 30.79      A    C  
ANISOU 1594  CA  ALA A 856     4706   3475   3518   -278   -380    -45  A    C  
ATOM   1595  C   ALA A 856     -12.301   2.866  -9.255  1.00 34.06      A    C  
ANISOU 1595  C   ALA A 856     5292   3823   3825   -219   -424   -100  A    C  
ATOM   1596  O   ALA A 856     -13.416   3.288  -8.938  1.00 34.64      A    O  
ANISOU 1596  O   ALA A 856     5462   3867   3832    -78   -367   -146  A    O  
ATOM   1597  CB  ALA A 856     -11.566   3.562 -11.517  1.00 32.73      A    C  
ANISOU 1597  CB  ALA A 856     5027   3633   3775   -377   -448    -22  A    C  
ATOM   1598  N   PRO A 857     -11.252   2.867  -8.413  1.00 34.84      A    N  
ANISOU 1598  N   PRO A 857     5437   3903   3898   -315   -530    -96  A    N  
ATOM   1599  CA  PRO A 857     -11.377   3.360  -7.031  1.00 33.96      A    C  
ANISOU 1599  CA  PRO A 857     5538   3712   3652   -268   -594   -156  A    C  
ATOM   1600  C   PRO A 857     -12.029   4.720  -6.894  1.00 35.30      A    C  
ANISOU 1600  C   PRO A 857     5953   3732   3726   -183   -622   -228  A    C  
ATOM   1601  O   PRO A 857     -12.908   4.892  -6.052  1.00 35.36      A    O  
ANISOU 1601  O   PRO A 857     6098   3725   3613    -18   -559   -293  A    O  
ATOM   1602  CB  PRO A 857      -9.928   3.412  -6.552  1.00 37.65      A    C  
ANISOU 1602  CB  PRO A 857     6009   4162   4134   -440   -761   -123  A    C  
ATOM   1603  CG  PRO A 857      -9.202   2.430  -7.400  1.00 37.31      A    C  
ANISOU 1603  CG  PRO A 857     5693   4254   4231   -512   -728    -44  A    C  
ATOM   1604  CD  PRO A 857      -9.857   2.507  -8.733  1.00 39.59      A    C  
ANISOU 1604  CD  PRO A 857     5897   4561   4583   -470   -609    -32  A    C  
ATOM   1605  N   GLU A 858     -11.604   5.675  -7.725  1.00 33.36      A    N  
ANISOU 1605  N   GLU A 858     5772   3378   3526   -285   -711   -211  A    N  
ATOM   1606  CA  GLU A 858     -12.152   7.035  -7.680  1.00 36.27      A    C  
ANISOU 1606  CA  GLU A 858     6418   3558   3805   -200   -770   -277  A    C  
ATOM   1607  C   GLU A 858     -13.644   7.069  -8.040  1.00 35.69      A    C  
ANISOU 1607  C   GLU A 858     6324   3521   3714     45   -617   -315  A    C  
ATOM   1608  O   GLU A 858     -14.352   7.978  -7.611  1.00 36.07      A    O  
ANISOU 1608  O   GLU A 858     6603   3448   3655    218   -627   -396  A    O  
ATOM   1609  CB  GLU A 858     -11.318   8.050  -8.506  1.00 36.30      A    C  
ANISOU 1609  CB  GLU A 858     6516   3420   3858   -401   -920   -224  A    C  
ATOM   1610  CG  GLU A 858     -11.308   7.899 -10.024  1.00 36.45      A    C  
ANISOU 1610  CG  GLU A 858     6344   3510   3995   -469   -851   -137  A    C  
ATOM   1611  CD  GLU A 858     -10.338   6.857 -10.580  1.00 41.70      A    C  
ANISOU 1611  CD  GLU A 858     6706   4365   4774   -627   -807    -43  A    C  
ATOM   1612  OE1 GLU A 858      -9.778   6.040  -9.805  1.00 35.50      A    O  
ANISOU 1612  OE1 GLU A 858     5811   3679   3998   -656   -815    -42  A    O  
ATOM   1613  OE2 GLU A 858     -10.157   6.825 -11.828  1.00 36.53      A    O1-
ANISOU 1613  OE2 GLU A 858     5929   3763   4187   -701   -759     29  A    O1-
ATOM   1614  N   SER A 859     -14.105   6.086  -8.825  1.00 32.67      A    N  
ANISOU 1614  N   SER A 859     5671   3306   3435     65   -488   -258  A    N  
ATOM   1615  CA  SER A 859     -15.538   5.904  -9.083  1.00 34.20      A    C  
ANISOU 1615  CA  SER A 859     5781   3584   3629    273   -352   -272  A    C  
ATOM   1616  C   SER A 859     -16.248   5.304  -7.879  1.00 35.61      A    C  
ANISOU 1616  C   SER A 859     5936   3877   3717    415   -237   -306  A    C  
ATOM   1617  O   SER A 859     -17.292   5.825  -7.460  1.00 35.53      A    O  
ANISOU 1617  O   SER A 859     6003   3874   3621    632   -160   -358  A    O  
ATOM   1618  CB  SER A 859     -15.774   5.076 -10.335  1.00 30.71      A    C  
ANISOU 1618  CB  SER A 859     5090   3262   3315    216   -290   -196  A    C  
ATOM   1619  OG  SER A 859     -14.948   5.528 -11.404  1.00 31.69      A    O  
ANISOU 1619  OG  SER A 859     5235   3306   3498     64   -378   -152  A    O  
ATOM   1620  N   LEU A 860     -15.673   4.237  -7.322  1.00 36.66      A    N  
ANISOU 1620  N   LEU A 860     5966   4104   3858    304   -223   -269  A    N  
ATOM   1621  CA  LEU A 860     -16.211   3.583  -6.117  1.00 40.12      A    C  
ANISOU 1621  CA  LEU A 860     6400   4652   4192    396   -120   -277  A    C  
ATOM   1622  C   LEU A 860     -16.332   4.479  -4.930  1.00 36.79      A    C  
ANISOU 1622  C   LEU A 860     6253   4140   3585    528   -137   -369  A    C  
ATOM   1623  O   LEU A 860     -17.372   4.480  -4.287  1.00 45.60      A    O  
ANISOU 1623  O   LEU A 860     7381   5351   4594    717      5   -394  A    O  
ATOM   1624  CB  LEU A 860     -15.344   2.404  -5.674  1.00 42.57      A    C  
ANISOU 1624  CB  LEU A 860     6621   5024   4529    242   -155   -220  A    C  
ATOM   1625  CG  LEU A 860     -15.424   1.098  -6.435  1.00 43.43      A    C  
ANISOU 1625  CG  LEU A 860     6483   5247   4771    159   -103   -134  A    C  
ATOM   1626  CD1 LEU A 860     -14.395   0.148  -5.829  1.00 51.68      A    C  
ANISOU 1626  CD1 LEU A 860     7514   6305   5818     44   -174    -95  A    C  
ATOM   1627  CD2 LEU A 860     -16.820   0.492  -6.347  1.00 44.68      A    C  
ANISOU 1627  CD2 LEU A 860     6514   5545   4919    255     50    -92  A    C  
ATOM   1628  N   PHE A 861     -15.262   5.219  -4.648  1.00 39.48      A    N  
ANISOU 1628  N   PHE A 861     6812   4309   3882    423   -312   -414  A    N  
ATOM   1629  CA  PHE A 861     -15.129   6.003  -3.418  1.00 42.93      A    C  
ANISOU 1629  CA  PHE A 861     7573   4622   4118    510   -381   -512  A    C  
ATOM   1630  C   PHE A 861     -15.548   7.434  -3.532  1.00 45.04      A    C  
ANISOU 1630  C   PHE A 861     8111   4701   4300    664   -434   -610  A    C  
ATOM   1631  O   PHE A 861     -15.954   7.995  -2.546  1.00 47.41      A    O  
ANISOU 1631  O   PHE A 861     8670   4937   4407    846   -414   -709  A    O  
ATOM   1632  CB  PHE A 861     -13.701   5.897  -2.852  1.00 44.56      A    C  
ANISOU 1632  CB  PHE A 861     7881   4743   4306    287   -579   -499  A    C  
ATOM   1633  CG  PHE A 861     -13.274   4.477  -2.630  1.00 46.97      A    C  
ANISOU 1633  CG  PHE A 861     7953   5214   4677    177   -542   -409  A    C  
ATOM   1634  CD1 PHE A 861     -14.026   3.635  -1.801  1.00 55.59      A    C  
ANISOU 1634  CD1 PHE A 861     9007   6447   5666    293   -388   -394  A    C  
ATOM   1635  CD2 PHE A 861     -12.167   3.945  -3.289  1.00 48.08      A    C  
ANISOU 1635  CD2 PHE A 861     7906   5380   4981    -29   -648   -328  A    C  
ATOM   1636  CE1 PHE A 861     -13.664   2.296  -1.641  1.00 55.72      A    C  
ANISOU 1636  CE1 PHE A 861     8841   6586   5746    191   -371   -302  A    C  
ATOM   1637  CE2 PHE A 861     -11.808   2.611  -3.134  1.00 46.31      A    C  
ANISOU 1637  CE2 PHE A 861     7487   5289   4819    -90   -620   -251  A    C  
ATOM   1638  CZ  PHE A 861     -12.559   1.788  -2.316  1.00 48.26      A    C  
ANISOU 1638  CZ  PHE A 861     7734   5635   4966     15   -495   -238  A    C  
ATOM   1639  N   GLU A 862     -15.407   8.046  -4.707  1.00 47.90      A    N  
ANISOU 1639  N   GLU A 862     8451   4961   4787    599   -511   -585  A    N  
ATOM   1640  CA  GLU A 862     -15.716   9.476  -4.880  1.00 51.65      A    C  
ANISOU 1640  CA  GLU A 862     9232   5207   5185    733   -603   -670  A    C  
ATOM   1641  C   GLU A 862     -16.783   9.770  -5.937  1.00 47.03      A    C  
ANISOU 1641  C   GLU A 862     8525   4657   4686    910   -504   -652  A    C  
ATOM   1642  O   GLU A 862     -17.227  10.895  -6.017  1.00 51.77      A    O  
ANISOU 1642  O   GLU A 862     9381   5078   5212   1086   -562   -726  A    O  
ATOM   1643  CB  GLU A 862     -14.429  10.249  -5.177  1.00 57.12      A    C  
ANISOU 1643  CB  GLU A 862    10122   5672   5909    463   -857   -652  A    C  
ATOM   1644  CG  GLU A 862     -13.328  10.156  -4.104  1.00 72.19      A    C  
ANISOU 1644  CG  GLU A 862    12184   7519   7728    280  -1015   -671  A    C  
ATOM   1645  CD  GLU A 862     -11.916  10.206  -4.695  1.00 86.93      A    C  
ANISOU 1645  CD  GLU A 862    13965   9336   9730    -81  -1207   -565  A    C  
ATOM   1646  OE1 GLU A 862     -11.206   9.175  -4.649  1.00 92.65      A    O  
ANISOU 1646  OE1 GLU A 862    14419  10238  10547   -237  -1192   -484  A    O  
ATOM   1647  OE2 GLU A 862     -11.517  11.263  -5.229  1.00 89.07      A    O1-
ANISOU 1647  OE2 GLU A 862    14427   9400  10016   -206  -1371   -553  A    O1-
ATOM   1648  N   GLY A 863     -17.241   8.766  -6.688  1.00 46.12      A    N  
ANISOU 1648  N   GLY A 863     8046   4762   4713    882   -370   -559  A    N  
ATOM   1649  CA  GLY A 863     -18.206   8.965  -7.768  1.00 47.34      A    C  
ANISOU 1649  CA  GLY A 863     8062   4964   4961   1018   -308   -525  A    C  
ATOM   1650  C   GLY A 863     -17.659   9.726  -8.975  1.00 45.19      A    C  
ANISOU 1650  C   GLY A 863     7885   4510   4774    877   -464   -484  A    C  
ATOM   1651  O   GLY A 863     -18.420  10.329  -9.675  1.00 43.67      A    O  
ANISOU 1651  O   GLY A 863     7722   4267   4603   1032   -469   -485  A    O  
ATOM   1652  N   ILE A 864     -16.346   9.650  -9.206  1.00 48.22      A    N  
ANISOU 1652  N   ILE A 864     8297   4820   5204    582   -587   -434  A    N  
ATOM   1653  CA  ILE A 864     -15.630  10.358 -10.264  1.00 47.57      A    C  
ANISOU 1653  CA  ILE A 864     8309   4582   5183    390   -730   -371  A    C  
ATOM   1654  C   ILE A 864     -15.569   9.389 -11.458  1.00 41.47      A    C  
ANISOU 1654  C   ILE A 864     7210   3996   4551    269   -645   -265  A    C  
ATOM   1655  O   ILE A 864     -15.209   8.225 -11.272  1.00 42.16      A    O  
ANISOU 1655  O   ILE A 864     7068   4260   4690    178   -565   -234  A    O  
ATOM   1656  CB  ILE A 864     -14.212  10.789  -9.743  1.00 51.17      A    C  
ANISOU 1656  CB  ILE A 864     8946   4893   5603    126   -903   -361  A    C  
ATOM   1657  CG1 ILE A 864     -14.365  11.943  -8.749  1.00 58.85      A    C  
ANISOU 1657  CG1 ILE A 864    10329   5616   6415    253  -1030   -477  A    C  
ATOM   1658  CG2 ILE A 864     -13.260  11.234 -10.849  1.00 52.21      A    C  
ANISOU 1658  CG2 ILE A 864     9077   4943   5816   -154  -1021   -249  A    C  
ATOM   1659  CD1 ILE A 864     -13.168  12.139  -7.834  1.00 67.28      A    C  
ANISOU 1659  CD1 ILE A 864    11566   6579   7419     28  -1198   -490  A    C  
ATOM   1660  N   TYR A 865     -15.937   9.869 -12.652  1.00 36.76      A    N  
ANISOU 1660  N   TYR A 865     6627   3344   3998    284   -674   -216  A    N  
ATOM   1661  CA  TYR A 865     -15.824   9.124 -13.934  1.00 38.28      A    C  
ANISOU 1661  CA  TYR A 865     6583   3674   4290    164   -620   -121  A    C  
ATOM   1662  C   TYR A 865     -15.087   9.969 -14.961  1.00 41.73      A    C  
ANISOU 1662  C   TYR A 865     7161   3966   4728    -23   -735    -41  A    C  
ATOM   1663  O   TYR A 865     -15.604  11.000 -15.409  1.00 41.41      A    O  
ANISOU 1663  O   TYR A 865     7329   3757   4649     68   -820    -40  A    O  
ATOM   1664  CB  TYR A 865     -17.197   8.748 -14.502  1.00 42.32      A    C  
ANISOU 1664  CB  TYR A 865     6947   4296   4836    371   -537   -120  A    C  
ATOM   1665  CG  TYR A 865     -17.985   7.843 -13.591  1.00 42.75      A    C  
ANISOU 1665  CG  TYR A 865     6823   4527   4894    519   -409   -164  A    C  
ATOM   1666  CD1 TYR A 865     -18.784   8.385 -12.571  1.00 44.21      A    C  
ANISOU 1666  CD1 TYR A 865     7115   4685   4999    758   -375   -244  A    C  
ATOM   1667  CD2 TYR A 865     -17.926   6.451 -13.721  1.00 43.12      A    C  
ANISOU 1667  CD2 TYR A 865     6612   4762   5007    425   -320   -123  A    C  
ATOM   1668  CE1 TYR A 865     -19.505   7.572 -11.714  1.00 46.46      A    C  
ANISOU 1668  CE1 TYR A 865     7227   5157   5270    877   -238   -263  A    C  
ATOM   1669  CE2 TYR A 865     -18.650   5.625 -12.863  1.00 42.67      A    C  
ANISOU 1669  CE2 TYR A 865     6406   4859   4946    526   -211   -139  A    C  
ATOM   1670  CZ  TYR A 865     -19.435   6.192 -11.866  1.00 45.80      A    C  
ANISOU 1670  CZ  TYR A 865     6884   5256   5262    741   -161   -200  A    C  
ATOM   1671  OH  TYR A 865     -20.155   5.407 -11.011  1.00 51.02      A    O  
ANISOU 1671  OH  TYR A 865     7390   6093   5902    827    -34   -196  A    O  
ATOM   1672  N   THR A 866     -13.864   9.545 -15.280  1.00 37.53      A    N  
ANISOU 1672  N   THR A 866     6518   3506   4235   -277   -736     33  A    N  
ATOM   1673  CA  THR A 866     -13.051  10.121 -16.336  1.00 37.14      A    C  
ANISOU 1673  CA  THR A 866     6529   3394   4188   -498   -801    142  A    C  
ATOM   1674  C   THR A 866     -12.690   9.034 -17.328  1.00 34.60      A    C  
ANISOU 1674  C   THR A 866     5939   3289   3919   -581   -678    211  A    C  
ATOM   1675  O   THR A 866     -12.922   7.843 -17.099  1.00 34.13      A    O  
ANISOU 1675  O   THR A 866     5670   3397   3901   -496   -571    171  A    O  
ATOM   1676  CB  THR A 866     -11.732  10.714 -15.792  1.00 37.35      A    C  
ANISOU 1676  CB  THR A 866     6660   3331   4200   -753   -919    188  A    C  
ATOM   1677  CG2 THR A 866     -11.997  11.724 -14.715  1.00 40.41      A    C  
ANISOU 1677  CG2 THR A 866     7360   3481   4513   -675  -1062    101  A    C  
ATOM   1678  OG1 THR A 866     -10.913   9.657 -15.275  1.00 38.57      A    O  
ANISOU 1678  OG1 THR A 866     6564   3681   4408   -842   -850    193  A    O  
ATOM   1679  N   ILE A 867     -12.050   9.444 -18.416  1.00 34.47      A    N  
ANISOU 1679  N   ILE A 867     5949   3263   3885   -760   -694    320  A    N  
ATOM   1680  CA  ILE A 867     -11.488   8.481 -19.364  1.00 34.96      A    C  
ANISOU 1680  CA  ILE A 867     5784   3532   3967   -844   -569    384  A    C  
ATOM   1681  C   ILE A 867     -10.454   7.543 -18.710  1.00 32.13      A    C  
ANISOU 1681  C   ILE A 867     5200   3345   3664   -925   -501    379  A    C  
ATOM   1682  O   ILE A 867     -10.337   6.389 -19.098  1.00 33.25      A    O  
ANISOU 1682  O   ILE A 867     5147   3658   3829   -870   -384    369  A    O  
ATOM   1683  CB  ILE A 867     -11.005   9.183 -20.674  1.00 40.00      A    C  
ANISOU 1683  CB  ILE A 867     6513   4142   4545  -1018   -581    515  A    C  
ATOM   1684  CG1 ILE A 867     -10.873   8.173 -21.821  1.00 41.99      A    C  
ANISOU 1684  CG1 ILE A 867     6587   4595   4775  -1004   -435    549  A    C  
ATOM   1685  CG2 ILE A 867      -9.738  10.005 -20.477  1.00 42.76      A    C  
ANISOU 1685  CG2 ILE A 867     6915   4445   4888  -1297   -655    622  A    C  
ATOM   1686  CD1 ILE A 867     -12.213   7.711 -22.376  1.00 38.42      A    C  
ANISOU 1686  CD1 ILE A 867     6162   4131   4303   -792   -424    484  A    C  
ATOM   1687  N   LYS A 868      -9.759   8.024 -17.689  1.00 34.02      A    N  
ANISOU 1687  N   LYS A 868     5487   3521   3918  -1036   -596    380  A    N  
ATOM   1688  CA  LYS A 868      -8.812   7.207 -16.926  1.00 38.08      A    C  
ANISOU 1688  CA  LYS A 868     5797   4183   4486  -1096   -570    377  A    C  
ATOM   1689  C   LYS A 868      -9.519   6.167 -16.048  1.00 36.11      A    C  
ANISOU 1689  C   LYS A 868     5476   3985   4260   -887   -517    264  A    C  
ATOM   1690  O   LYS A 868      -8.968   5.103 -15.843  1.00 34.78      A    O  
ANISOU 1690  O   LYS A 868     5110   3970   4136   -875   -453    263  A    O  
ATOM   1691  CB  LYS A 868      -7.881   8.100 -16.101  1.00 41.11      A    C  
ANISOU 1691  CB  LYS A 868     6276   4472   4872  -1303   -727    421  A    C  
ATOM   1692  CG  LYS A 868      -7.033   9.018 -16.968  1.00 46.72      A    C  
ANISOU 1692  CG  LYS A 868     7020   5163   5570  -1569   -778    569  A    C  
ATOM   1693  CD  LYS A 868      -6.087   9.902 -16.151  1.00 65.79      A    C  
ANISOU 1693  CD  LYS A 868     9530   7473   7992  -1822   -970    629  A    C  
ATOM   1694  CE  LYS A 868      -6.714  11.176 -15.583  1.00 68.94      A    C  
ANISOU 1694  CE  LYS A 868    10333   7544   8318  -1822  -1161    571  A    C  
ATOM   1695  NZ  LYS A 868      -5.937  11.663 -14.400  1.00 63.00      A    N1+
ANISOU 1695  NZ  LYS A 868     9682   6691   7564  -2000  -1362    569  A    N1+
ATOM   1696  N   SER A 869     -10.718   6.471 -15.535  1.00 35.23      A    N  
ANISOU 1696  N   SER A 869     5520   3753   4113   -720   -542    180  A    N  
ATOM   1697  CA  SER A 869     -11.613   5.454 -14.910  1.00 33.70      A    C  
ANISOU 1697  CA  SER A 869     5242   3633   3930   -529   -464    100  A    C  
ATOM   1698  C   SER A 869     -11.971   4.374 -15.916  1.00 29.46      A    C  
ANISOU 1698  C   SER A 869     4538   3228   3429   -472   -354    116  A    C  
ATOM   1699  O   SER A 869     -11.997   3.208 -15.580  1.00 31.83      A    O  
ANISOU 1699  O   SER A 869     4707   3630   3759   -418   -296     93  A    O  
ATOM   1700  CB  SER A 869     -12.931   6.071 -14.379  1.00 33.82      A    C  
ANISOU 1700  CB  SER A 869     5422   3533   3894   -346   -483     26  A    C  
ATOM   1701  OG  SER A 869     -12.676   7.258 -13.662  1.00 48.73      A    O  
ANISOU 1701  OG  SER A 869     7544   5249   5721   -378   -602     -1  A    O  
ATOM   1702  N   ASP A 870     -12.267   4.785 -17.144  1.00 31.65      A    N  
ANISOU 1702  N   ASP A 870     4857   3480   3687   -485   -345    157  A    N  
ATOM   1703  CA  ASP A 870     -12.505   3.854 -18.239  1.00 29.12      A    C  
ANISOU 1703  CA  ASP A 870     4426   3265   3373   -451   -265    172  A    C  
ATOM   1704  C   ASP A 870     -11.302   2.972 -18.565  1.00 29.05      A    C  
ANISOU 1704  C   ASP A 870     4264   3392   3380   -528   -193    202  A    C  
ATOM   1705  O   ASP A 870     -11.493   1.836 -18.930  1.00 29.89      A    O  
ANISOU 1705  O   ASP A 870     4284   3578   3494   -453   -132    175  A    O  
ATOM   1706  CB  ASP A 870     -12.972   4.588 -19.497  1.00 32.91      A    C  
ANISOU 1706  CB  ASP A 870     5017   3682   3804   -460   -289    217  A    C  
ATOM   1707  CG  ASP A 870     -14.428   4.961 -19.449  1.00 37.66      A    C  
ANISOU 1707  CG  ASP A 870     5702   4205   4404   -308   -340    180  A    C  
ATOM   1708  OD1 ASP A 870     -15.209   4.177 -18.872  1.00 35.90      A    O  
ANISOU 1708  OD1 ASP A 870     5382   4041   4218   -197   -312    129  A    O  
ATOM   1709  OD2 ASP A 870     -14.805   6.009 -20.033  1.00 35.11      A    O1-
ANISOU 1709  OD2 ASP A 870     5530   3769   4040   -299   -411    213  A    O1-
ATOM   1710  N   VAL A 871     -10.084   3.483 -18.440  1.00 30.28      A    N  
ANISOU 1710  N   VAL A 871     4387   3578   3542   -672   -208    262  A    N  
ATOM   1711  CA  VAL A 871      -8.889   2.636 -18.617  1.00 32.11      A    C  
ANISOU 1711  CA  VAL A 871     4428   3975   3799   -711   -131    295  A    C  
ATOM   1712  C   VAL A 871      -8.875   1.485 -17.606  1.00 32.72      A    C  
ANISOU 1712  C   VAL A 871     4410   4097   3927   -603   -129    230  A    C  
ATOM   1713  O   VAL A 871      -8.579   0.357 -17.994  1.00 33.11      A    O  
ANISOU 1713  O   VAL A 871     4352   4246   3983   -519    -54    214  A    O  
ATOM   1714  CB  VAL A 871      -7.576   3.459 -18.593  1.00 34.61      A    C  
ANISOU 1714  CB  VAL A 871     4680   4344   4124   -910   -161    397  A    C  
ATOM   1715  CG1 VAL A 871      -6.316   2.561 -18.509  1.00 34.40      A    C  
ANISOU 1715  CG1 VAL A 871     4404   4522   4144   -915    -90    431  A    C  
ATOM   1716  CG2 VAL A 871      -7.512   4.341 -19.848  1.00 37.73      A    C  
ANISOU 1716  CG2 VAL A 871     5159   4724   4451  -1026   -132    486  A    C  
ATOM   1717  N   TRP A 872      -9.203   1.777 -16.339  1.00 32.49      A    N  
ANISOU 1717  N   TRP A 872     4449   3981   3912   -596   -214    193  A    N  
ATOM   1718  CA  TRP A 872      -9.342   0.732 -15.295  1.00 30.46      A    C  
ANISOU 1718  CA  TRP A 872     4143   3749   3683   -501   -221    143  A    C  
ATOM   1719  C   TRP A 872     -10.350  -0.319 -15.715  1.00 29.51      A    C  
ANISOU 1719  C   TRP A 872     4020   3634   3559   -375   -158    101  A    C  
ATOM   1720  O   TRP A 872     -10.035  -1.511 -15.747  1.00 28.79      A    O  
ANISOU 1720  O   TRP A 872     3848   3602   3488   -314   -126     90  A    O  
ATOM   1721  CB  TRP A 872      -9.727   1.342 -13.925  1.00 32.19      A    C  
ANISOU 1721  CB  TRP A 872     4485   3869   3878   -504   -309    109  A    C  
ATOM   1722  CG  TRP A 872      -9.916   0.353 -12.804  1.00 28.46      A    C  
ANISOU 1722  CG  TRP A 872     3989   3419   3406   -423   -314     75  A    C  
ATOM   1723  CD1 TRP A 872     -10.919  -0.565 -12.674  1.00 27.94      A    C  
ANISOU 1723  CD1 TRP A 872     3920   3361   3334   -317   -257     47  A    C  
ATOM   1724  CD2 TRP A 872      -9.084   0.196 -11.667  1.00 28.87      A    C  
ANISOU 1724  CD2 TRP A 872     4028   3486   3456   -462   -396     82  A    C  
ATOM   1725  CE2 TRP A 872      -9.646  -0.833 -10.881  1.00 32.11      A    C  
ANISOU 1725  CE2 TRP A 872     4448   3905   3848   -366   -374     57  A    C  
ATOM   1726  CE3 TRP A 872      -7.929   0.836 -11.215  1.00 32.23      A    C  
ANISOU 1726  CE3 TRP A 872     4438   3916   3891   -589   -505    118  A    C  
ATOM   1727  NE1 TRP A 872     -10.755  -1.293 -11.540  1.00 30.81      A    N  
ANISOU 1727  NE1 TRP A 872     4282   3740   3686   -291   -285     42  A    N  
ATOM   1728  CZ2 TRP A 872      -9.068  -1.258  -9.688  1.00 29.89      A    C  
ANISOU 1728  CZ2 TRP A 872     4177   3634   3546   -371   -452     63  A    C  
ATOM   1729  CZ3 TRP A 872      -7.342   0.404 -10.018  1.00 34.71      A    C  
ANISOU 1729  CZ3 TRP A 872     4744   4248   4196   -595   -597    119  A    C  
ATOM   1730  CH2 TRP A 872      -7.911  -0.627  -9.273  1.00 31.54      A    C  
ANISOU 1730  CH2 TRP A 872     4370   3849   3764   -477   -569     89  A    C  
ATOM   1731  N   SER A 873     -11.549   0.127 -16.054  1.00 27.45      A    N  
ANISOU 1731  N   SER A 873     3852   3306   3274   -337   -158     83  A    N  
ATOM   1732  CA  SER A 873     -12.609  -0.780 -16.529  1.00 29.12      A    C  
ANISOU 1732  CA  SER A 873     4054   3524   3486   -255   -128     60  A    C  
ATOM   1733  C   SER A 873     -12.178  -1.562 -17.753  1.00 32.61      A    C  
ANISOU 1733  C   SER A 873     4459   4016   3916   -246    -84     64  A    C  
ATOM   1734  O   SER A 873     -12.481  -2.750 -17.865  1.00 29.60      A    O  
ANISOU 1734  O   SER A 873     4066   3641   3541   -193    -79     39  A    O  
ATOM   1735  CB  SER A 873     -13.873  -0.006 -16.883  1.00 30.32      A    C  
ANISOU 1735  CB  SER A 873     4279   3620   3620   -218   -149     58  A    C  
ATOM   1736  OG  SER A 873     -14.342   0.723 -15.790  1.00 33.00      A    O  
ANISOU 1736  OG  SER A 873     4672   3916   3951   -180   -172     41  A    O  
ATOM   1737  N   TYR A 874     -11.465  -0.897 -18.662  1.00 29.60      A    N  
ANISOU 1737  N   TYR A 874     4082   3664   3501   -301    -54     98  A    N  
ATOM   1738  CA  TYR A 874     -10.907  -1.579 -19.818  1.00 30.01      A    C  
ANISOU 1738  CA  TYR A 874     4109   3787   3509   -271     15     98  A    C  
ATOM   1739  C   TYR A 874      -9.955  -2.725 -19.399  1.00 29.68      A    C  
ANISOU 1739  C   TYR A 874     3964   3818   3494   -203     52     76  A    C  
ATOM   1740  O   TYR A 874      -9.983  -3.792 -20.003  1.00 34.12      A    O  
ANISOU 1740  O   TYR A 874     4553   4388   4024   -108     83     35  A    O  
ATOM   1741  CB  TYR A 874     -10.226  -0.595 -20.763  1.00 31.87      A    C  
ANISOU 1741  CB  TYR A 874     4352   4068   3688   -358     61    162  A    C  
ATOM   1742  CG  TYR A 874      -9.558  -1.269 -21.924  1.00 31.64      A    C  
ANISOU 1742  CG  TYR A 874     4295   4144   3584   -308    166    163  A    C  
ATOM   1743  CD1 TYR A 874     -10.300  -1.663 -23.019  1.00 33.40      A    C  
ANISOU 1743  CD1 TYR A 874     4639   4329   3721   -249    172    130  A    C  
ATOM   1744  CD2 TYR A 874      -8.201  -1.566 -21.899  1.00 31.39      A    C  
ANISOU 1744  CD2 TYR A 874     4113   4257   3559   -300    254    193  A    C  
ATOM   1745  CE1 TYR A 874      -9.707  -2.303 -24.097  1.00 35.31      A    C  
ANISOU 1745  CE1 TYR A 874     4897   4659   3859   -176    274    115  A    C  
ATOM   1746  CE2 TYR A 874      -7.589  -2.204 -22.972  1.00 36.81      A    C  
ANISOU 1746  CE2 TYR A 874     4774   5059   4155   -210    377    186  A    C  
ATOM   1747  CZ  TYR A 874      -8.358  -2.573 -24.061  1.00 36.94      A    C  
ANISOU 1747  CZ  TYR A 874     4956   5018   4062   -143    390    139  A    C  
ATOM   1748  OH  TYR A 874      -7.801  -3.215 -25.109  1.00 38.25      A    O  
ANISOU 1748  OH  TYR A 874     5141   5284   4107    -30    513    115  A    O  
ATOM   1749  N   GLY A 875      -9.119  -2.490 -18.402  1.00 29.66      A    N  
ANISOU 1749  N   GLY A 875     3867   3857   3544   -242     32    102  A    N  
ATOM   1750  CA  GLY A 875      -8.285  -3.553 -17.808  1.00 33.35      A    C  
ANISOU 1750  CA  GLY A 875     4237   4385   4051   -157     35     87  A    C  
ATOM   1751  C   GLY A 875      -9.093  -4.749 -17.332  1.00 29.70      A    C  
ANISOU 1751  C   GLY A 875     3856   3832   3597    -65     -9     34  A    C  
ATOM   1752  O   GLY A 875      -8.757  -5.888 -17.635  1.00 32.62      A    O  
ANISOU 1752  O   GLY A 875     4230   4207   3956     48      9      2  A    O  
ATOM   1753  N   ILE A 876     -10.205  -4.478 -16.649  1.00 29.26      A    N  
ANISOU 1753  N   ILE A 876     3876   3690   3550   -113    -64     30  A    N  
ATOM   1754  CA  ILE A 876     -11.126  -5.540 -16.205  1.00 29.93      A    C  
ANISOU 1754  CA  ILE A 876     4031   3701   3640    -75   -105     10  A    C  
ATOM   1755  C   ILE A 876     -11.683  -6.288 -17.426  1.00 30.74      A    C  
ANISOU 1755  C   ILE A 876     4211   3761   3707    -34    -99    -22  A    C  
ATOM   1756  O   ILE A 876     -11.726  -7.516 -17.435  1.00 30.52      A    O  
ANISOU 1756  O   ILE A 876     4246   3677   3675     22   -133    -45  A    O  
ATOM   1757  CB  ILE A 876     -12.282  -5.022 -15.320  1.00 27.22      A    C  
ANISOU 1757  CB  ILE A 876     3721   3319   3302   -130   -134     27  A    C  
ATOM   1758  CG1 ILE A 876     -11.774  -4.235 -14.076  1.00 32.90      A    C  
ANISOU 1758  CG1 ILE A 876     4422   4055   4022   -161   -155     41  A    C  
ATOM   1759  CG2 ILE A 876     -13.170  -6.166 -14.852  1.00 29.86      A    C  
ANISOU 1759  CG2 ILE A 876     4097   3606   3641   -127   -168     37  A    C  
ATOM   1760  CD1 ILE A 876     -10.953  -5.021 -13.062  1.00 31.19      A    C  
ANISOU 1760  CD1 ILE A 876     4185   3848   3817   -137   -198     52  A    C  
ATOM   1761  N   LEU A 877     -12.082  -5.533 -18.443  1.00 33.26      A    N  
ANISOU 1761  N   LEU A 877     4556   4092   3990    -66    -74    -21  A    N  
ATOM   1762  CA  LEU A 877     -12.614  -6.102 -19.681  1.00 31.47      A    C  
ANISOU 1762  CA  LEU A 877     4429   3824   3706    -39    -88    -52  A    C  
ATOM   1763  C   LEU A 877     -11.565  -6.973 -20.379  1.00 31.63      A    C  
ANISOU 1763  C   LEU A 877     4483   3865   3671     73    -37    -98  A    C  
ATOM   1764  O   LEU A 877     -11.918  -8.021 -20.905  1.00 31.94      A    O  
ANISOU 1764  O   LEU A 877     4649   3821   3665    127    -84   -145  A    O  
ATOM   1765  CB  LEU A 877     -13.178  -4.989 -20.568  1.00 30.41      A    C  
ANISOU 1765  CB  LEU A 877     4321   3700   3532    -92    -85    -30  A    C  
ATOM   1766  CG  LEU A 877     -13.939  -5.298 -21.880  1.00 37.59      A    C  
ANISOU 1766  CG  LEU A 877     5350   4564   4367    -88   -132    -51  A    C  
ATOM   1767  CD1 LEU A 877     -14.788  -4.101 -22.280  1.00 42.66      A    C  
ANISOU 1767  CD1 LEU A 877     5999   5204   5004   -143   -170     -9  A    C  
ATOM   1768  CD2 LEU A 877     -13.027  -5.616 -23.026  1.00 41.52      A    C  
ANISOU 1768  CD2 LEU A 877     5923   5096   4758    -19    -59    -87  A    C  
ATOM   1769  N   LEU A 878     -10.293  -6.552 -20.362  1.00 30.45      A    N  
ANISOU 1769  N   LEU A 878     4222   3827   3520    111     51    -81  A    N  
ATOM   1770  CA  LEU A 878      -9.193  -7.394 -20.836  1.00 31.64      A    C  
ANISOU 1770  CA  LEU A 878     4358   4038   3627    262    122   -120  A    C  
ATOM   1771  C   LEU A 878      -9.120  -8.711 -20.105  1.00 34.74      A    C  
ANISOU 1771  C   LEU A 878     4804   4340   4054    366     51   -160  A    C  
ATOM   1772  O   LEU A 878      -8.921  -9.741 -20.734  1.00 34.10      A    O  
ANISOU 1772  O   LEU A 878     4843   4206   3909    509     55   -225  A    O  
ATOM   1773  CB  LEU A 878      -7.824  -6.712 -20.720  1.00 34.16      A    C  
ANISOU 1773  CB  LEU A 878     4479   4532   3968    267    221    -66  A    C  
ATOM   1774  CG  LEU A 878      -7.392  -5.698 -21.772  1.00 45.28      A    C  
ANISOU 1774  CG  LEU A 878     5837   6063   5305    202    330    -16  A    C  
ATOM   1775  CD1 LEU A 878      -5.969  -5.256 -21.451  1.00 46.36      A    C  
ANISOU 1775  CD1 LEU A 878     5739   6388   5487    187    408     57  A    C  
ATOM   1776  CD2 LEU A 878      -7.446  -6.269 -23.174  1.00 47.81      A    C  
ANISOU 1776  CD2 LEU A 878     6287   6393   5485    321    413    -72  A    C  
ATOM   1777  N   TRP A 879      -9.274  -8.673 -18.779  1.00 35.23      A    N  
ANISOU 1777  N   TRP A 879     4809   4373   4202    301    -19   -121  A    N  
ATOM   1778  CA  TRP A 879      -9.296  -9.907 -17.971  1.00 34.48      A    C  
ANISOU 1778  CA  TRP A 879     4793   4172   4135    373   -107   -136  A    C  
ATOM   1779  C   TRP A 879     -10.477 -10.802 -18.384  1.00 32.52      A    C  
ANISOU 1779  C   TRP A 879     4749   3758   3848    342   -194   -168  A    C  
ATOM   1780  O   TRP A 879     -10.307 -12.019 -18.513  1.00 33.82      A    O  
ANISOU 1780  O   TRP A 879     5059   3809   3984    452   -253   -212  A    O  
ATOM   1781  CB  TRP A 879      -9.322  -9.595 -16.464  1.00 33.16      A    C  
ANISOU 1781  CB  TRP A 879     4549   4013   4039    287   -163    -76  A    C  
ATOM   1782  CG  TRP A 879      -8.990 -10.759 -15.610  1.00 33.46      A    C  
ANISOU 1782  CG  TRP A 879     4649   3969   4096    373   -246    -73  A    C  
ATOM   1783  CD1 TRP A 879      -7.771 -11.083 -15.126  1.00 35.70      A    C  
ANISOU 1783  CD1 TRP A 879     4843   4311   4408    499   -258    -66  A    C  
ATOM   1784  CD2 TRP A 879      -9.889 -11.761 -15.157  1.00 31.99      A    C  
ANISOU 1784  CD2 TRP A 879     4630   3624   3900    333   -343    -61  A    C  
ATOM   1785  CE2 TRP A 879      -9.134 -12.676 -14.381  1.00 34.80      A    C  
ANISOU 1785  CE2 TRP A 879     5027   3925   4271    446   -415    -50  A    C  
ATOM   1786  CE3 TRP A 879     -11.273 -11.958 -15.297  1.00 33.59      A    C  
ANISOU 1786  CE3 TRP A 879     4939   3735   4088    197   -386    -42  A    C  
ATOM   1787  NE1 TRP A 879      -7.839 -12.235 -14.384  1.00 36.58      A    N  
ANISOU 1787  NE1 TRP A 879     5082   4292   4523    561   -364    -58  A    N  
ATOM   1788  CZ2 TRP A 879      -9.707 -13.799 -13.752  1.00 33.91      A    C  
ANISOU 1788  CZ2 TRP A 879     5095   3643   4146    417   -530    -19  A    C  
ATOM   1789  CZ3 TRP A 879     -11.854 -13.071 -14.687  1.00 32.77      A    C  
ANISOU 1789  CZ3 TRP A 879     4982   3489   3980    147   -492     -3  A    C  
ATOM   1790  CH2 TRP A 879     -11.062 -13.984 -13.912  1.00 37.92      A    C  
ANISOU 1790  CH2 TRP A 879     5710   4064   4636    251   -563     10  A    C  
ATOM   1791  N   GLU A 880     -11.643 -10.196 -18.626  1.00 30.66      A    N  
ANISOU 1791  N   GLU A 880     4531   3507   3613    197   -217   -142  A    N  
ATOM   1792  CA  GLU A 880     -12.799 -10.936 -19.175  1.00 32.00      A    C  
ANISOU 1792  CA  GLU A 880     4863   3545   3749    132   -318   -156  A    C  
ATOM   1793  C   GLU A 880     -12.488 -11.601 -20.527  1.00 33.37      A    C  
ANISOU 1793  C   GLU A 880     5208   3652   3820    249   -323   -242  A    C  
ATOM   1794  O   GLU A 880     -12.804 -12.785 -20.724  1.00 34.21      A    O  
ANISOU 1794  O   GLU A 880     5511   3598   3890    272   -433   -279  A    O  
ATOM   1795  CB  GLU A 880     -14.032 -10.047 -19.358  1.00 33.44      A    C  
ANISOU 1795  CB  GLU A 880     4989   3763   3952    -16   -338   -109  A    C  
ATOM   1796  CG  GLU A 880     -14.609  -9.413 -18.126  1.00 31.73      A    C  
ANISOU 1796  CG  GLU A 880     4641   3607   3809   -110   -328    -36  A    C  
ATOM   1797  CD  GLU A 880     -15.888  -8.666 -18.449  1.00 33.57      A    C  
ANISOU 1797  CD  GLU A 880     4820   3878   4056   -206   -352      4  A    C  
ATOM   1798  OE1 GLU A 880     -15.825  -7.450 -18.793  1.00 32.27      A    O  
ANISOU 1798  OE1 GLU A 880     4592   3784   3885   -189   -296      3  A    O  
ATOM   1799  OE2 GLU A 880     -16.962  -9.287 -18.388  1.00 32.32      A    O1-
ANISOU 1799  OE2 GLU A 880     4682   3679   3918   -302   -438     46  A    O1-
ATOM   1800  N   ILE A 881     -11.835 -10.865 -21.432  1.00 35.84      A    N  
ANISOU 1800  N   ILE A 881     5470   4079   4070    323   -208   -271  A    N  
ATOM   1801  CA  ILE A 881     -11.474 -11.421 -22.773  1.00 38.59      A    C  
ANISOU 1801  CA  ILE A 881     5994   4389   4280    461   -181   -359  A    C  
ATOM   1802  C   ILE A 881     -10.542 -12.623 -22.627  1.00 39.51      A    C  
ANISOU 1802  C   ILE A 881     6207   4441   4364    672   -175   -428  A    C  
ATOM   1803  O   ILE A 881     -10.822 -13.711 -23.149  1.00 40.51      A    O  
ANISOU 1803  O   ILE A 881     6590   4394   4407    749   -272   -505  A    O  
ATOM   1804  CB  ILE A 881     -10.854 -10.351 -23.721  1.00 36.95      A    C  
ANISOU 1804  CB  ILE A 881     5697   4350   3993    494    -28   -352  A    C  
ATOM   1805  CG1 ILE A 881     -11.956  -9.362 -24.144  1.00 36.18      A    C  
ANISOU 1805  CG1 ILE A 881     5601   4251   3894    317    -80   -301  A    C  
ATOM   1806  CG2 ILE A 881     -10.227 -10.989 -24.972  1.00 40.08      A    C  
ANISOU 1806  CG2 ILE A 881     6262   4745   4219    686     46   -446  A    C  
ATOM   1807  CD1 ILE A 881     -11.487  -8.128 -24.873  1.00 38.66      A    C  
ANISOU 1807  CD1 ILE A 881     5834   4708   4147    295     43   -260  A    C  
ATOM   1808  N   PHE A 882      -9.441 -12.404 -21.914  1.00 37.37      A    N  
ANISOU 1808  N   PHE A 882     5741   4301   4158    768    -81   -400  A    N  
ATOM   1809  CA  PHE A 882      -8.394 -13.406 -21.783  1.00 39.93      A    C  
ANISOU 1809  CA  PHE A 882     6107   4606   4459   1015    -59   -459  A    C  
ATOM   1810  C   PHE A 882      -8.654 -14.493 -20.721  1.00 37.51      A    C  
ANISOU 1810  C   PHE A 882     5924   4110   4220   1024   -219   -452  A    C  
ATOM   1811  O   PHE A 882      -7.810 -15.346 -20.520  1.00 38.95      A    O  
ANISOU 1811  O   PHE A 882     6155   4252   4391   1246   -227   -496  A    O  
ATOM   1812  CB  PHE A 882      -7.032 -12.709 -21.665  1.00 38.47      A    C  
ANISOU 1812  CB  PHE A 882     5636   4674   4306   1122    107   -420  A    C  
ATOM   1813  CG  PHE A 882      -6.645 -12.004 -22.930  1.00 36.44      A    C  
ANISOU 1813  CG  PHE A 882     5328   4581   3937   1159    272   -433  A    C  
ATOM   1814  CD1 PHE A 882      -6.096 -12.728 -23.994  1.00 39.10      A    C  
ANISOU 1814  CD1 PHE A 882     5801   4933   4124   1411    366   -530  A    C  
ATOM   1815  CD2 PHE A 882      -6.896 -10.642 -23.107  1.00 38.08      A    C  
ANISOU 1815  CD2 PHE A 882     5395   4908   4164    949    329   -351  A    C  
ATOM   1816  CE1 PHE A 882      -5.776 -12.102 -25.191  1.00 44.00      A    C  
ANISOU 1816  CE1 PHE A 882     6397   5714   4608   1439    533   -532  A    C  
ATOM   1817  CE2 PHE A 882      -6.566 -10.002 -24.300  1.00 37.98      A    C  
ANISOU 1817  CE2 PHE A 882     5365   5036   4031    962    476   -344  A    C  
ATOM   1818  CZ  PHE A 882      -6.002 -10.736 -25.344  1.00 41.43      A    C  
ANISOU 1818  CZ  PHE A 882     5918   5513   4309   1201    587   -429  A    C  
ATOM   1819  N   SER A 883      -9.815 -14.454 -20.067  1.00 37.66      A    N  
ANISOU 1819  N   SER A 883     5988   4021   4300    793   -341   -389  A    N  
ATOM   1820  CA  SER A 883     -10.374 -15.596 -19.322  1.00 37.65      A    C  
ANISOU 1820  CA  SER A 883     6178   3801   4325    744   -512   -370  A    C  
ATOM   1821  C   SER A 883     -11.510 -16.315 -20.051  1.00 39.10      A    C  
ANISOU 1821  C   SER A 883     6636   3778   4441    632   -655   -401  A    C  
ATOM   1822  O   SER A 883     -12.000 -17.291 -19.527  1.00 39.22      A    O  
ANISOU 1822  O   SER A 883     6831   3598   4471    560   -810   -373  A    O  
ATOM   1823  CB  SER A 883     -10.873 -15.128 -17.936  1.00 35.87      A    C  
ANISOU 1823  CB  SER A 883     5799   3622   4206    547   -544   -252  A    C  
ATOM   1824  OG  SER A 883     -11.963 -14.211 -18.029  1.00 32.00      A    O  
ANISOU 1824  OG  SER A 883     5215   3203   3740    331   -527   -198  A    O  
ATOM   1825  N   LEU A 884     -11.890 -15.880 -21.266  1.00 38.89      A    N  
ANISOU 1825  N   LEU A 884     6659   3783   4333    610   -622   -453  A    N  
ATOM   1826  CA  LEU A 884     -13.118 -16.324 -21.943  1.00 38.35      A    C  
ANISOU 1826  CA  LEU A 884     6808   3551   4213    443   -784   -461  A    C  
ATOM   1827  C   LEU A 884     -14.406 -16.111 -21.116  1.00 37.03      A    C  
ANISOU 1827  C   LEU A 884     6533   3379   4157    145   -888   -329  A    C  
ATOM   1828  O   LEU A 884     -15.277 -16.969 -21.049  1.00 37.56      A    O  
ANISOU 1828  O   LEU A 884     6776   3270   4227    -12  -1068   -294  A    O  
ATOM   1829  CB  LEU A 884     -13.000 -17.766 -22.497  1.00 40.76      A    C  
ANISOU 1829  CB  LEU A 884     7495   3586   4407    570   -933   -562  A    C  
ATOM   1830  CG  LEU A 884     -11.821 -18.055 -23.441  1.00 46.94      A    C  
ANISOU 1830  CG  LEU A 884     8413   4378   5046    908   -817   -708  A    C  
ATOM   1831  CD1 LEU A 884     -11.917 -19.476 -23.959  1.00 49.29      A    C  
ANISOU 1831  CD1 LEU A 884     9147   4361   5218   1024   -999   -817  A    C  
ATOM   1832  CD2 LEU A 884     -11.711 -17.111 -24.626  1.00 49.77      A    C  
ANISOU 1832  CD2 LEU A 884     8701   4911   5300    947   -674   -752  A    C  
ATOM   1833  N   GLY A 885     -14.524 -14.918 -20.549  1.00 34.99      A    N  
ANISOU 1833  N   GLY A 885     5987   3326   3982     68   -769   -255  A    N  
ATOM   1834  CA  GLY A 885     -15.752 -14.459 -19.923  1.00 38.50      A    C  
ANISOU 1834  CA  GLY A 885     6286   3829   4512   -167   -815   -139  A    C  
ATOM   1835  C   GLY A 885     -16.003 -14.870 -18.482  1.00 35.45      A    C  
ANISOU 1835  C   GLY A 885     5839   3427   4204   -269   -844    -39  A    C  
ATOM   1836  O   GLY A 885     -17.154 -15.038 -18.092  1.00 41.12      A    O  
ANISOU 1836  O   GLY A 885     6519   4139   4965   -475   -925     60  A    O  
ATOM   1837  N   VAL A 886     -14.943 -15.032 -17.693  1.00 36.07      A    N  
ANISOU 1837  N   VAL A 886     5898   3514   4292   -132   -781    -52  A    N  
ATOM   1838  CA  VAL A 886     -15.079 -15.338 -16.269  1.00 35.26      A    C  
ANISOU 1838  CA  VAL A 886     5752   3406   4238   -217   -801     47  A    C  
ATOM   1839  C   VAL A 886     -15.469 -14.033 -15.565  1.00 34.52      A    C  
ANISOU 1839  C   VAL A 886     5403   3522   4192   -293   -678    110  A    C  
ATOM   1840  O   VAL A 886     -15.040 -12.936 -15.966  1.00 32.78      A    O  
ANISOU 1840  O   VAL A 886     5053   3429   3973   -211   -571     61  A    O  
ATOM   1841  CB  VAL A 886     -13.795 -16.030 -15.690  1.00 37.13      A    C  
ANISOU 1841  CB  VAL A 886     6082   3564   4462    -28   -812     12  A    C  
ATOM   1842  CG1 VAL A 886     -13.873 -16.208 -14.172  1.00 35.24      A    C  
ANISOU 1842  CG1 VAL A 886     5802   3335   4252   -114   -830    122  A    C  
ATOM   1843  CG2 VAL A 886     -13.585 -17.410 -16.346  1.00 33.28      A    C  
ANISOU 1843  CG2 VAL A 886     5898   2830   3915     64   -954    -52  A    C  
ATOM   1844  N   ASN A 887     -16.345 -14.151 -14.564  1.00 35.25      A    N  
ANISOU 1844  N   ASN A 887     5442   3644   4309   -454   -694    224  A    N  
ATOM   1845  CA  ASN A 887     -16.687 -13.028 -13.675  1.00 32.02      A    C  
ANISOU 1845  CA  ASN A 887     4831   3417   3918   -488   -574    277  A    C  
ATOM   1846  C   ASN A 887     -15.382 -12.503 -13.049  1.00 34.28      A    C  
ANISOU 1846  C   ASN A 887     5083   3751   4193   -336   -504    227  A    C  
ATOM   1847  O   ASN A 887     -14.586 -13.295 -12.539  1.00 31.85      A    O  
ANISOU 1847  O   ASN A 887     4877   3354   3872   -271   -558    228  A    O  
ATOM   1848  CB  ASN A 887     -17.660 -13.489 -12.563  1.00 37.93      A    C  
ANISOU 1848  CB  ASN A 887     5555   4191   4664   -659   -587    414  A    C  
ATOM   1849  CG  ASN A 887     -18.243 -12.333 -11.727  1.00 45.20      A    C  
ANISOU 1849  CG  ASN A 887     6283   5311   5578   -674   -449    462  A    C  
ATOM   1850  ND2 ASN A 887     -18.838 -11.331 -12.389  1.00 43.45      A    N  
ANISOU 1850  ND2 ASN A 887     5925   5199   5385   -654   -394    433  A    N  
ATOM   1851  OD1 ASN A 887     -18.211 -12.377 -10.495  1.00 47.79      A    O  
ANISOU 1851  OD1 ASN A 887     6608   5687   5864   -695   -401    526  A    O  
ATOM   1852  N   PRO A 888     -15.133 -11.180 -13.101  1.00 31.21      A    N  
ANISOU 1852  N   PRO A 888     4558   3490   3810   -283   -406    190  A    N  
ATOM   1853  CA  PRO A 888     -13.946 -10.646 -12.424  1.00 29.74      A    C  
ANISOU 1853  CA  PRO A 888     4330   3352   3617   -186   -369    162  A    C  
ATOM   1854  C   PRO A 888     -13.933 -10.939 -10.923  1.00 31.23      A    C  
ANISOU 1854  C   PRO A 888     4550   3542   3774   -222   -386    230  A    C  
ATOM   1855  O   PRO A 888     -14.998 -11.100 -10.318  1.00 31.72      A    O  
ANISOU 1855  O   PRO A 888     4615   3625   3811   -329   -370    305  A    O  
ATOM   1856  CB  PRO A 888     -14.058  -9.134 -12.655  1.00 30.16      A    C  
ANISOU 1856  CB  PRO A 888     4269   3516   3674   -183   -286    135  A    C  
ATOM   1857  CG  PRO A 888     -14.901  -8.979 -13.829  1.00 33.00      A    C  
ANISOU 1857  CG  PRO A 888     4620   3874   4046   -217   -282    121  A    C  
ATOM   1858  CD  PRO A 888     -15.860 -10.129 -13.829  1.00 35.14      A    C  
ANISOU 1858  CD  PRO A 888     4956   4075   4321   -310   -352    175  A    C  
ATOM   1859  N   TYR A 889     -12.730 -11.024 -10.355  1.00 31.26      A    N  
ANISOU 1859  N   TYR A 889     4566   3539   3772   -134   -421    214  A    N  
ATOM   1860  CA  TYR A 889     -12.521 -11.367  -8.953  1.00 30.46      A    C  
ANISOU 1860  CA  TYR A 889     4526   3424   3622   -152   -465    276  A    C  
ATOM   1861  C   TYR A 889     -13.333 -12.611  -8.604  1.00 28.69      A    C  
ANISOU 1861  C   TYR A 889     4433   3098   3372   -243   -520    361  A    C  
ATOM   1862  O   TYR A 889     -14.205 -12.557  -7.737  1.00 31.61      A    O  
ANISOU 1862  O   TYR A 889     4813   3512   3685   -354   -481    443  A    O  
ATOM   1863  CB  TYR A 889     -12.857 -10.178  -8.044  1.00 29.67      A    C  
ANISOU 1863  CB  TYR A 889     4374   3431   3467   -197   -396    288  A    C  
ATOM   1864  CG  TYR A 889     -12.155  -8.875  -8.450  1.00 31.25      A    C  
ANISOU 1864  CG  TYR A 889     4479   3701   3694   -148   -366    215  A    C  
ATOM   1865  CD1 TYR A 889     -10.859  -8.551  -7.987  1.00 34.58      A    C  
ANISOU 1865  CD1 TYR A 889     4877   4142   4119   -101   -433    198  A    C  
ATOM   1866  CD2 TYR A 889     -12.813  -7.938  -9.262  1.00 30.65      A    C  
ANISOU 1866  CD2 TYR A 889     4339   3671   3637   -167   -289    180  A    C  
ATOM   1867  CE1 TYR A 889     -10.241  -7.346  -8.351  1.00 35.64      A    C  
ANISOU 1867  CE1 TYR A 889     4929   4335   4277   -105   -422    155  A    C  
ATOM   1868  CE2 TYR A 889     -12.211  -6.734  -9.619  1.00 28.46      A    C  
ANISOU 1868  CE2 TYR A 889     4007   3432   3373   -150   -275    131  A    C  
ATOM   1869  CZ  TYR A 889     -10.922  -6.444  -9.182  1.00 32.97      A    C  
ANISOU 1869  CZ  TYR A 889     4559   4019   3950   -134   -340    122  A    C  
ATOM   1870  OH  TYR A 889     -10.364  -5.242  -9.546  1.00 32.24      A    O  
ANISOU 1870  OH  TYR A 889     4420   3958   3872   -161   -342     95  A    O  
ATOM   1871  N   PRO A 890     -13.090 -13.722  -9.340  1.00 30.62      A    N  
ANISOU 1871  N   PRO A 890     4785   3202   3646   -201   -608    344  A    N  
ATOM   1872  CA  PRO A 890     -13.973 -14.867  -9.258  1.00 31.89      A    C  
ANISOU 1872  CA  PRO A 890     5092   3235   3789   -329   -685    427  A    C  
ATOM   1873  C   PRO A 890     -14.019 -15.471  -7.860  1.00 34.58      A    C  
ANISOU 1873  C   PRO A 890     5541   3533   4065   -399   -736    541  A    C  
ATOM   1874  O   PRO A 890     -12.963 -15.710  -7.246  1.00 34.37      A    O  
ANISOU 1874  O   PRO A 890     5575   3464   4019   -278   -800    531  A    O  
ATOM   1875  CB  PRO A 890     -13.368 -15.856 -10.269  1.00 35.18      A    C  
ANISOU 1875  CB  PRO A 890     5655   3480   4232   -211   -790    355  A    C  
ATOM   1876  CG  PRO A 890     -11.942 -15.472 -10.350  1.00 35.18      A    C  
ANISOU 1876  CG  PRO A 890     5580   3535   4251      4   -769    271  A    C  
ATOM   1877  CD  PRO A 890     -11.953 -13.984 -10.240  1.00 31.89      A    C  
ANISOU 1877  CD  PRO A 890     4953   3316   3846    -26   -644    250  A    C  
ATOM   1878  N   GLY A 891     -15.243 -15.665  -7.367  1.00 38.70      A    N  
ANISOU 1878  N   GLY A 891     6068   4090   4549   -596   -703    658  A    N  
ATOM   1879  CA  GLY A 891     -15.513 -16.205  -6.040  1.00 34.89      A    C  
ANISOU 1879  CA  GLY A 891     5689   3592   3976   -705   -723    796  A    C  
ATOM   1880  C   GLY A 891     -15.415 -15.204  -4.904  1.00 35.71      A    C  
ANISOU 1880  C   GLY A 891     5706   3868   3994   -675   -608    809  A    C  
ATOM   1881  O   GLY A 891     -15.561 -15.605  -3.745  1.00 37.81      A    O  
ANISOU 1881  O   GLY A 891     6077   4133   4155   -751   -616    921  A    O  
ATOM   1882  N   ILE A 892     -15.162 -13.924  -5.210  1.00 33.51      A    N  
ANISOU 1882  N   ILE A 892     5272   3718   3740   -570   -513    699  A    N  
ATOM   1883  CA  ILE A 892     -15.077 -12.878  -4.198  1.00 35.75      A    C  
ANISOU 1883  CA  ILE A 892     5514   4139   3930   -531   -422    689  A    C  
ATOM   1884  C   ILE A 892     -16.411 -12.142  -4.268  1.00 34.60      A    C  
ANISOU 1884  C   ILE A 892     5231   4152   3762   -602   -261    716  A    C  
ATOM   1885  O   ILE A 892     -16.724 -11.597  -5.322  1.00 33.72      A    O  
ANISOU 1885  O   ILE A 892     4997   4076   3741   -576   -225    648  A    O  
ATOM   1886  CB  ILE A 892     -13.901 -11.917  -4.456  1.00 34.13      A    C  
ANISOU 1886  CB  ILE A 892     5251   3952   3764   -381   -448    559  A    C  
ATOM   1887  CG1 ILE A 892     -12.572 -12.704  -4.344  1.00 39.56      A    C  
ANISOU 1887  CG1 ILE A 892     6029   4520   4481   -289   -607    549  A    C  
ATOM   1888  CG2 ILE A 892     -13.973 -10.743  -3.482  1.00 34.55      A    C  
ANISOU 1888  CG2 ILE A 892     5300   4119   3707   -359   -371    538  A    C  
ATOM   1889  CD1 ILE A 892     -11.306 -11.920  -4.592  1.00 38.48      A    C  
ANISOU 1889  CD1 ILE A 892     5800   4423   4398   -168   -652    454  A    C  
ATOM   1890  N   PRO A 893     -17.194 -12.135  -3.167  1.00 35.94      A    N  
ANISOU 1890  N   PRO A 893     5418   4430   3805   -679   -161    821  A    N  
ATOM   1891  CA  PRO A 893     -18.476 -11.411  -3.196  1.00 36.02      A    C  
ANISOU 1891  CA  PRO A 893     5263   4629   3793   -706     11    850  A    C  
ATOM   1892  C   PRO A 893     -18.302  -9.884  -3.190  1.00 36.05      A    C  
ANISOU 1892  C   PRO A 893     5208   4720   3770   -539     97    717  A    C  
ATOM   1893  O   PRO A 893     -17.215  -9.352  -2.877  1.00 35.08      A    O  
ANISOU 1893  O   PRO A 893     5188   4528   3614   -440     31    623  A    O  
ATOM   1894  CB  PRO A 893     -19.209 -11.915  -1.936  1.00 39.72      A    C  
ANISOU 1894  CB  PRO A 893     5780   5202   4109   -819    105   1009  A    C  
ATOM   1895  CG  PRO A 893     -18.136 -12.399  -1.012  1.00 39.46      A    C  
ANISOU 1895  CG  PRO A 893     5972   5043   3977   -796     -5   1019  A    C  
ATOM   1896  CD  PRO A 893     -16.946 -12.776  -1.859  1.00 38.71      A    C  
ANISOU 1896  CD  PRO A 893     5939   4753   4018   -728   -193    923  A    C  
ATOM   1897  N   VAL A 894     -19.364  -9.197  -3.592  1.00 35.58      A    N  
ANISOU 1897  N   VAL A 894     4985   4800   3733   -514    222    715  A    N  
ATOM   1898  CA  VAL A 894     -19.430  -7.742  -3.522  1.00 33.63      A    C  
ANISOU 1898  CA  VAL A 894     4710   4625   3442   -347    310    602  A    C  
ATOM   1899  C   VAL A 894     -20.012  -7.424  -2.164  1.00 32.02      A    C  
ANISOU 1899  C   VAL A 894     4553   4565   3048   -296    462    649  A    C  
ATOM   1900  O   VAL A 894     -21.195  -7.655  -1.907  1.00 35.44      A    O  
ANISOU 1900  O   VAL A 894     4850   5173   3443   -338    604    759  A    O  
ATOM   1901  CB  VAL A 894     -20.261  -7.131  -4.674  1.00 37.52      A    C  
ANISOU 1901  CB  VAL A 894     5019   5187   4050   -305    354    571  A    C  
ATOM   1902  CG1 VAL A 894     -20.291  -5.617  -4.545  1.00 41.71      A    C  
ANISOU 1902  CG1 VAL A 894     5572   5754   4524   -115    425    454  A    C  
ATOM   1903  CG2 VAL A 894     -19.654  -7.505  -6.014  1.00 35.56      A    C  
ANISOU 1903  CG2 VAL A 894     4761   4797   3955   -356    209    525  A    C  
ATOM   1904  N   ASP A 895     -19.150  -6.943  -1.273  1.00 35.08      A    N  
ANISOU 1904  N   ASP A 895     5135   4888   3305   -214    427    577  A    N  
ATOM   1905  CA  ASP A 895     -19.528  -6.581   0.103  1.00 34.73      A    C  
ANISOU 1905  CA  ASP A 895     5206   4957   3032   -139    560    597  A    C  
ATOM   1906  C   ASP A 895     -18.517  -5.551   0.606  1.00 35.02      A    C  
ANISOU 1906  C   ASP A 895     5456   4880   2970    -13    471    449  A    C  
ATOM   1907  O   ASP A 895     -17.681  -5.133  -0.155  1.00 36.52      A    O  
ANISOU 1907  O   ASP A 895     5650   4939   3286     -4    332    358  A    O  
ATOM   1908  CB  ASP A 895     -19.626  -7.836   1.013  1.00 38.81      A    C  
ANISOU 1908  CB  ASP A 895     5798   5506   3443   -289    570    758  A    C  
ATOM   1909  CG  ASP A 895     -18.314  -8.669   1.073  1.00 40.58      A    C  
ANISOU 1909  CG  ASP A 895     6181   5525   3712   -376    345    764  A    C  
ATOM   1910  OD1 ASP A 895     -17.219  -8.132   0.772  1.00 36.02      A    O  
ANISOU 1910  OD1 ASP A 895     5672   4819   3193   -303    203    639  A    O  
ATOM   1911  OD2 ASP A 895     -18.398  -9.872   1.442  1.00 40.90      A    O1-
ANISOU 1911  OD2 ASP A 895     6272   5541   3728   -519    307    906  A    O1-
ATOM   1912  N   ALA A 896     -18.595  -5.134   1.858  1.00 35.34      A    N  
ANISOU 1912  N   ALA A 896     5678   4972   2777     72    546    431  A    N  
ATOM   1913  CA  ALA A 896     -17.630  -4.163   2.382  1.00 37.65      A    C  
ANISOU 1913  CA  ALA A 896     6210   5134   2962    165    423    292  A    C  
ATOM   1914  C   ALA A 896     -16.142  -4.628   2.300  1.00 41.16      A    C  
ANISOU 1914  C   ALA A 896     6739   5406   3494     50    167    284  A    C  
ATOM   1915  O   ALA A 896     -15.259  -3.801   2.109  1.00 38.54      A    O  
ANISOU 1915  O   ALA A 896     6492   4957   3195     76     22    176  A    O  
ATOM   1916  CB  ALA A 896     -17.996  -3.789   3.794  1.00 37.63      A    C  
ANISOU 1916  CB  ALA A 896     6425   5212   2660    273    539    279  A    C  
ATOM   1917  N   ASN A 897     -15.886  -5.935   2.400  1.00 39.21      A    N  
ANISOU 1917  N   ASN A 897     6458   5148   3293    -76    106    406  A    N  
ATOM   1918  CA  ASN A 897     -14.531  -6.467   2.177  1.00 38.42      A    C  
ANISOU 1918  CA  ASN A 897     6385   4908   3305   -146   -126    406  A    C  
ATOM   1919  C   ASN A 897     -13.999  -6.243   0.774  1.00 35.49      A    C  
ANISOU 1919  C   ASN A 897     5839   4472   3173   -153   -204    343  A    C  
ATOM   1920  O   ASN A 897     -12.804  -6.028   0.627  1.00 33.06      A    O  
ANISOU 1920  O   ASN A 897     5550   4081   2932   -162   -374    296  A    O  
ATOM   1921  CB  ASN A 897     -14.402  -7.954   2.550  1.00 35.96      A    C  
ANISOU 1921  CB  ASN A 897     6103   4571   2988   -248   -184    548  A    C  
ATOM   1922  CG  ASN A 897     -14.505  -8.197   4.041  1.00 35.32      A    C  
ANISOU 1922  CG  ASN A 897     6248   4524   2649   -258   -169    618  A    C  
ATOM   1923  ND2 ASN A 897     -14.919  -9.396   4.407  1.00 36.52      A    N  
ANISOU 1923  ND2 ASN A 897     6429   4690   2756   -358   -141    771  A    N  
ATOM   1924  OD1 ASN A 897     -14.219  -7.319   4.861  1.00 40.83      A    O  
ANISOU 1924  OD1 ASN A 897     7117   5222   3174   -185   -193    539  A    O  
ATOM   1925  N   PHE A 898     -14.872  -6.281  -0.232  1.00 32.61      A    N  
ANISOU 1925  N   PHE A 898     5301   4161   2927   -155    -83    352  A    N  
ATOM   1926  CA  PHE A 898     -14.488  -5.990  -1.578  1.00 32.28      A    C  
ANISOU 1926  CA  PHE A 898     5119   4071   3075   -154   -134    294  A    C  
ATOM   1927  C   PHE A 898     -13.961  -4.555  -1.746  1.00 35.89      A    C  
ANISOU 1927  C   PHE A 898     5625   4484   3526    -94   -182    177  A    C  
ATOM   1928  O   PHE A 898     -12.941  -4.343  -2.393  1.00 32.85      A    O  
ANISOU 1928  O   PHE A 898     5192   4036   3254   -124   -303    142  A    O  
ATOM   1929  CB  PHE A 898     -15.621  -6.221  -2.571  1.00 34.83      A    C  
ANISOU 1929  CB  PHE A 898     5275   4461   3499   -168    -12    327  A    C  
ATOM   1930  CG  PHE A 898     -15.178  -6.027  -3.973  1.00 31.64      A    C  
ANISOU 1930  CG  PHE A 898     4757   3999   3264   -170    -72    273  A    C  
ATOM   1931  CD1 PHE A 898     -14.422  -7.006  -4.600  1.00 34.94      A    C  
ANISOU 1931  CD1 PHE A 898     5140   4346   3790   -216   -173    297  A    C  
ATOM   1932  CD2 PHE A 898     -15.382  -4.798  -4.627  1.00 33.77      A    C  
ANISOU 1932  CD2 PHE A 898     4989   4276   3566   -107    -36    192  A    C  
ATOM   1933  CE1 PHE A 898     -13.932  -6.801  -5.887  1.00 33.30      A    C  
ANISOU 1933  CE1 PHE A 898     4841   4103   3709   -203   -210    244  A    C  
ATOM   1934  CE2 PHE A 898     -14.889  -4.594  -5.904  1.00 31.14      A    C  
ANISOU 1934  CE2 PHE A 898     4573   3895   3365   -120    -90    154  A    C  
ATOM   1935  CZ  PHE A 898     -14.157  -5.595  -6.529  1.00 34.65      A    C  
ANISOU 1935  CZ  PHE A 898     4966   4295   3903   -168   -165    180  A    C  
ATOM   1936  N   TYR A 899     -14.694  -3.604  -1.186  1.00 35.04      A    N  
ANISOU 1936  N   TYR A 899     5615   4415   3283     -7    -83    126  A    N  
ATOM   1937  CA  TYR A 899     -14.301  -2.206  -1.137  1.00 37.27      A    C  
ANISOU 1937  CA  TYR A 899     6024   4620   3519     51   -145     15  A    C  
ATOM   1938  C   TYR A 899     -12.916  -2.038  -0.477  1.00 38.82      A    C  
ANISOU 1938  C   TYR A 899     6362   4718   3668    -20   -351     -9  A    C  
ATOM   1939  O   TYR A 899     -12.066  -1.333  -1.030  1.00 35.04      A    O  
ANISOU 1939  O   TYR A 899     5874   4161   3278    -73   -479    -54  A    O  
ATOM   1940  CB  TYR A 899     -15.393  -1.352  -0.440  1.00 41.61      A    C  
ANISOU 1940  CB  TYR A 899     6702   5221   3888    201      3    -40  A    C  
ATOM   1941  CG  TYR A 899     -16.609  -1.011  -1.350  1.00 51.46      A    C  
ANISOU 1941  CG  TYR A 899     7783   6552   5218    296    160    -42  A    C  
ATOM   1942  CD1 TYR A 899     -17.618  -1.952  -1.629  1.00 49.73      A    C  
ANISOU 1942  CD1 TYR A 899     7358   6481   5055    275    301     63  A    C  
ATOM   1943  CD2 TYR A 899     -16.764   0.272  -1.903  1.00 56.48      A    C  
ANISOU 1943  CD2 TYR A 899     8478   7109   5870    398    145   -138  A    C  
ATOM   1944  CE1 TYR A 899     -18.720  -1.639  -2.438  1.00 52.77      A    C  
ANISOU 1944  CE1 TYR A 899     7573   6959   5521    354    415     72  A    C  
ATOM   1945  CE2 TYR A 899     -17.863   0.598  -2.703  1.00 61.99      A    C  
ANISOU 1945  CE2 TYR A 899     9029   7884   6641    503    265   -134  A    C  
ATOM   1946  CZ  TYR A 899     -18.838  -0.364  -2.971  1.00 61.59      A    C  
ANISOU 1946  CZ  TYR A 899     8743   8005   6654    483    398    -29  A    C  
ATOM   1947  OH  TYR A 899     -19.924  -0.040  -3.747  1.00 59.96      A    O  
ANISOU 1947  OH  TYR A 899     8370   7890   6524    581    491    -15  A    O  
ATOM   1948  N   LYS A 900     -12.681  -2.716   0.654  1.00 35.17      A    N  
ANISOU 1948  N   LYS A 900     6016   4272   3076    -38   -394     39  A    N  
ATOM   1949  CA  LYS A 900     -11.370  -2.713   1.294  1.00 39.14      A    C  
ANISOU 1949  CA  LYS A 900     6627   4698   3544   -110   -617     36  A    C  
ATOM   1950  C   LYS A 900     -10.272  -3.335   0.437  1.00 34.29      A    C  
ANISOU 1950  C   LYS A 900     5809   4073   3145   -194   -749     84  A    C  
ATOM   1951  O   LYS A 900      -9.192  -2.778   0.422  1.00 39.70      A    O  
ANISOU 1951  O   LYS A 900     6499   4711   3874   -258   -923     59  A    O  
ATOM   1952  CB  LYS A 900     -11.356  -3.401   2.671  1.00 42.34      A    C  
ANISOU 1952  CB  LYS A 900     7211   5122   3754   -107   -649     92  A    C  
ATOM   1953  CG  LYS A 900     -12.181  -2.700   3.732  1.00 50.99      A    C  
ANISOU 1953  CG  LYS A 900     8556   6236   4583    -10   -539     35  A    C  
ATOM   1954  CD  LYS A 900     -11.633  -2.870   5.155  1.00 54.45      A    C  
ANISOU 1954  CD  LYS A 900     9260   6637   4791    -27   -676     48  A    C  
ATOM   1955  CE  LYS A 900     -11.545  -4.310   5.593  1.00 50.65      A    C  
ANISOU 1955  CE  LYS A 900     8741   6205   4297    -85   -687    189  A    C  
ATOM   1956  NZ  LYS A 900     -11.660  -4.399   7.076  1.00 50.49      A    N1+
ANISOU 1956  NZ  LYS A 900     9020   6194   3970    -59   -702    211  A    N1+
ATOM   1957  N   LEU A 901     -10.553  -4.444  -0.261  1.00 33.13      A    N  
ANISOU 1957  N   LEU A 901     5494   3973   3122   -191   -669    152  A    N  
ATOM   1958  CA  LEU A 901      -9.573  -5.117  -1.130  1.00 37.43      A    C  
ANISOU 1958  CA  LEU A 901     5853   4514   3852   -219   -765    186  A    C  
ATOM   1959  C   LEU A 901      -9.060  -4.118  -2.161  1.00 34.69      A    C  
ANISOU 1959  C   LEU A 901     5388   4165   3626   -251   -787    130  A    C  
ATOM   1960  O   LEU A 901      -7.864  -3.957  -2.307  1.00 34.98      A    O  
ANISOU 1960  O   LEU A 901     5342   4208   3740   -299   -928    140  A    O  
ATOM   1961  CB  LEU A 901     -10.133  -6.327  -1.912  1.00 42.03      A    C  
ANISOU 1961  CB  LEU A 901     6320   5115   4536   -195   -665    242  A    C  
ATOM   1962  CG  LEU A 901     -10.763  -7.556  -1.269  1.00 55.47      A    C  
ANISOU 1962  CG  LEU A 901     8106   6807   6162   -199   -630    330  A    C  
ATOM   1963  CD1 LEU A 901     -10.681  -8.775  -2.178  1.00 62.64      A    C  
ANISOU 1963  CD1 LEU A 901     8917   7677   7207   -188   -641    374  A    C  
ATOM   1964  CD2 LEU A 901     -10.109  -7.820   0.069  1.00 72.24      A    C  
ANISOU 1964  CD2 LEU A 901    10390   8903   8155   -204   -768    371  A    C  
ATOM   1965  N   ILE A 902      -9.996  -3.446  -2.829  1.00 33.59      A    N  
ANISOU 1965  N   ILE A 902     5240   4027   3495   -229   -650     86  A    N  
ATOM   1966  CA  ILE A 902      -9.674  -2.503  -3.904  1.00 36.48      A    C  
ANISOU 1966  CA  ILE A 902     5520   4379   3962   -267   -656     47  A    C  
ATOM   1967  C   ILE A 902      -8.904  -1.330  -3.358  1.00 32.29      A    C  
ANISOU 1967  C   ILE A 902     5110   3784   3373   -341   -804     10  A    C  
ATOM   1968  O   ILE A 902      -7.896  -0.957  -3.939  1.00 32.33      A    O  
ANISOU 1968  O   ILE A 902     5007   3799   3480   -434   -901     30  A    O  
ATOM   1969  CB  ILE A 902     -10.938  -2.022  -4.653  1.00 34.16      A    C  
ANISOU 1969  CB  ILE A 902     5219   4087   3673   -210   -498     14  A    C  
ATOM   1970  CG1 ILE A 902     -11.602  -3.195  -5.387  1.00 32.34      A    C  
ANISOU 1970  CG1 ILE A 902     4852   3912   3523   -180   -391     60  A    C  
ATOM   1971  CG2 ILE A 902     -10.622  -0.909  -5.646  1.00 38.52      A    C  
ANISOU 1971  CG2 ILE A 902     5742   4599   4296   -255   -523    -19  A    C  
ATOM   1972  CD1 ILE A 902     -10.745  -3.927  -6.425  1.00 35.30      A    C  
ANISOU 1972  CD1 ILE A 902     5074   4303   4034   -205   -430     87  A    C  
ATOM   1973  N   GLN A 903      -9.364  -0.776  -2.239  1.00 34.43      A    N  
ANISOU 1973  N   GLN A 903     5613   3998   3472   -308   -824    -38  A    N  
ATOM   1974  CA  GLN A 903      -8.660   0.326  -1.559  1.00 38.25      A    C  
ANISOU 1974  CA  GLN A 903     6284   4384   3865   -387  -1004    -83  A    C  
ATOM   1975  C   GLN A 903      -7.198   0.007  -1.220  1.00 39.55      A    C  
ANISOU 1975  C   GLN A 903     6367   4571   4090   -513  -1220    -24  A    C  
ATOM   1976  O   GLN A 903      -6.360   0.903  -1.232  1.00 40.57      A    O  
ANISOU 1976  O   GLN A 903     6532   4643   4239   -645  -1390    -28  A    O  
ATOM   1977  CB  GLN A 903      -9.394   0.685  -0.255  1.00 45.30      A    C  
ANISOU 1977  CB  GLN A 903     7470   5220   4521   -293   -982   -148  A    C  
ATOM   1978  CG  GLN A 903      -8.884   1.913   0.475  1.00 55.55      A    C  
ANISOU 1978  CG  GLN A 903     9048   6375   5684   -352  -1171   -223  A    C  
ATOM   1979  CD  GLN A 903     -10.031   2.799   0.970  1.00 82.57      A    C  
ANISOU 1979  CD  GLN A 903    12748   9716   8909   -190  -1057   -332  A    C  
ATOM   1980  NE2 GLN A 903     -10.393   3.822   0.170  1.00 68.39      A    N  
ANISOU 1980  NE2 GLN A 903    10993   7831   7162   -162  -1029   -386  A    N  
ATOM   1981  OE1 GLN A 903     -10.606   2.549   2.043  1.00 76.79      A    O  
ANISOU 1981  OE1 GLN A 903    12191   9010   7975    -74   -984   -361  A    O  
ATOM   1982  N   ASN A 904      -6.920  -1.254  -0.869  1.00 36.19      A    N  
ANISOU 1982  N   ASN A 904     5840   4222   3688   -473  -1229     39  A    N  
ATOM   1983  CA  ASN A 904      -5.568  -1.666  -0.468  1.00 42.85      A    C  
ANISOU 1983  CA  ASN A 904     6586   5105   4589   -552  -1442    103  A    C  
ATOM   1984  C   ASN A 904      -4.648  -2.034  -1.648  1.00 39.93      A    C  
ANISOU 1984  C   ASN A 904     5891   4842   4440   -587  -1449    166  A    C  
ATOM   1985  O   ASN A 904      -3.494  -2.320  -1.420  1.00 43.92      A    O  
ANISOU 1985  O   ASN A 904     6261   5413   5014   -636  -1617    228  A    O  
ATOM   1986  CB  ASN A 904      -5.647  -2.822   0.554  1.00 41.69      A    C  
ANISOU 1986  CB  ASN A 904     6523   4974   4345   -473  -1476    147  A    C  
ATOM   1987  CG  ASN A 904      -6.085  -2.355   1.940  1.00 49.37      A    C  
ANISOU 1987  CG  ASN A 904     7825   5865   5069   -469  -1536    101  A    C  
ATOM   1988  ND2 ASN A 904      -6.993  -3.093   2.571  1.00 54.36      A    N  
ANISOU 1988  ND2 ASN A 904     8583   6507   5565   -375  -1406    118  A    N  
ATOM   1989  OD1 ASN A 904      -5.586  -1.361   2.447  1.00 53.80      A    O  
ANISOU 1989  OD1 ASN A 904     8538   6356   5549   -557  -1706     58  A    O  
ATOM   1990  N   GLY A 905      -5.159  -2.043  -2.881  1.00 37.72      A    N  
ANISOU 1990  N   GLY A 905     5483   4592   4256   -549  -1268    154  A    N  
ATOM   1991  CA  GLY A 905      -4.358  -2.316  -4.083  1.00 36.04      A    C  
ANISOU 1991  CA  GLY A 905     4985   4490   4217   -564  -1238    205  A    C  
ATOM   1992  C   GLY A 905      -4.440  -3.740  -4.592  1.00 35.90      A    C  
ANISOU 1992  C   GLY A 905     4832   4536   4273   -415  -1134    230  A    C  
ATOM   1993  O   GLY A 905      -3.585  -4.162  -5.356  1.00 41.95      A    O  
ANISOU 1993  O   GLY A 905     5372   5409   5160   -382  -1130    271  A    O  
ATOM   1994  N   PHE A 906      -5.481  -4.476  -4.204  1.00 37.87      A    N  
ANISOU 1994  N   PHE A 906     5225   4720   4443   -324  -1048    209  A    N  
ATOM   1995  CA  PHE A 906      -5.722  -5.833  -4.709  1.00 39.60      A    C  
ANISOU 1995  CA  PHE A 906     5380   4950   4718   -201   -966    229  A    C  
ATOM   1996  C   PHE A 906      -5.950  -5.768  -6.226  1.00 36.65      A    C  
ANISOU 1996  C   PHE A 906     4874   4613   4437   -176   -822    204  A    C  
ATOM   1997  O   PHE A 906      -6.722  -4.938  -6.694  1.00 40.21      A    O  
ANISOU 1997  O   PHE A 906     5374   5040   4865   -230   -731    168  A    O  
ATOM   1998  CB  PHE A 906      -6.937  -6.472  -4.009  1.00 41.01      A    C  
ANISOU 1998  CB  PHE A 906     5749   5048   4783   -168   -901    232  A    C  
ATOM   1999  CG  PHE A 906      -7.102  -7.957  -4.262  1.00 39.51      A    C  
ANISOU 1999  CG  PHE A 906     5554   4826   4631    -76   -881    270  A    C  
ATOM   2000  CD1 PHE A 906      -7.724  -8.419  -5.427  1.00 41.88      A    C  
ANISOU 2000  CD1 PHE A 906     5804   5111   4996    -40   -760    250  A    C  
ATOM   2001  CD2 PHE A 906      -6.678  -8.888  -3.331  1.00 40.11      A    C  
ANISOU 2001  CD2 PHE A 906     5714   4861   4664    -30  -1003    326  A    C  
ATOM   2002  CE1 PHE A 906      -7.905  -9.777  -5.647  1.00 46.47      A    C  
ANISOU 2002  CE1 PHE A 906     6434   5623   5598     33   -769    279  A    C  
ATOM   2003  CE2 PHE A 906      -6.852 -10.256  -3.555  1.00 40.09      A    C  
ANISOU 2003  CE2 PHE A 906     5756   4787   4688     53  -1007    363  A    C  
ATOM   2004  CZ  PHE A 906      -7.473 -10.694  -4.700  1.00 43.01      A    C  
ANISOU 2004  CZ  PHE A 906     6094   5128   5121     79   -892    336  A    C  
ATOM   2005  N   LYS A 907      -5.214  -6.606  -6.957  1.00 37.88      A    N  
ANISOU 2005  N   LYS A 907     4877   4830   4685    -79   -814    223  A    N  
ATOM   2006  CA  LYS A 907      -5.352  -6.795  -8.393  1.00 39.19      A    C  
ANISOU 2006  CA  LYS A 907     4947   5032   4911    -23   -681    197  A    C  
ATOM   2007  C   LYS A 907      -5.510  -8.287  -8.691  1.00 37.94      A    C  
ANISOU 2007  C   LYS A 907     4829   4820   4766    131   -662    190  A    C  
ATOM   2008  O   LYS A 907      -4.893  -9.132  -8.029  1.00 39.64      A    O  
ANISOU 2008  O   LYS A 907     5048   5022   4991    222   -765    220  A    O  
ATOM   2009  CB  LYS A 907      -4.108  -6.293  -9.088  1.00 42.99      A    C  
ANISOU 2009  CB  LYS A 907     5203   5658   5473    -37   -683    225  A    C  
ATOM   2010  CG  LYS A 907      -3.946  -4.782  -9.090  1.00 42.03      A    C  
ANISOU 2010  CG  LYS A 907     5058   5566   5345   -220   -706    242  A    C  
ATOM   2011  CD  LYS A 907      -2.531  -4.453  -9.545  1.00 49.46      A    C  
ANISOU 2011  CD  LYS A 907     5740   6680   6372   -263   -738    309  A    C  
ATOM   2012  CE  LYS A 907      -2.166  -2.986  -9.379  1.00 60.91      A    C  
ANISOU 2012  CE  LYS A 907     7178   8143   7821   -490   -820    352  A    C  
ATOM   2013  NZ  LYS A 907      -1.195  -2.535 -10.435  1.00 68.53      A    N1+
ANISOU 2013  NZ  LYS A 907     7889   9286   8861   -567   -757    428  A    N1+
ATOM   2014  N   MET A 908      -6.319  -8.602  -9.693  1.00 35.38      A    N  
ANISOU 2014  N   MET A 908     4556   4449   4438    158   -553    152  A    N  
ATOM   2015  CA  MET A 908      -6.435  -9.981 -10.205  1.00 34.52      A    C  
ANISOU 2015  CA  MET A 908     4519   4262   4336    298   -547    132  A    C  
ATOM   2016  C   MET A 908      -5.127 -10.553 -10.740  1.00 38.61      A    C  
ANISOU 2016  C   MET A 908     4900   4862   4908    477   -557    123  A    C  
ATOM   2017  O   MET A 908      -4.231  -9.804 -11.133  1.00 37.96      A    O  
ANISOU 2017  O   MET A 908     4620   4936   4868    473   -518    136  A    O  
ATOM   2018  CB  MET A 908      -7.479 -10.062 -11.324  1.00 31.89      A    C  
ANISOU 2018  CB  MET A 908     4262   3872   3982    274   -449     89  A    C  
ATOM   2019  CG  MET A 908      -8.891  -9.947 -10.831  1.00 31.81      A    C  
ANISOU 2019  CG  MET A 908     4378   3782   3927    145   -444    109  A    C  
ATOM   2020  SD  MET A 908     -10.100 -10.261 -12.115  1.00 35.32      A    S  
ANISOU 2020  SD  MET A 908     4901   4159   4361    114   -382     76  A    S  
ATOM   2021  CE  MET A 908     -10.194  -8.644 -12.896  1.00 33.87      A    C  
ANISOU 2021  CE  MET A 908     4601   4086   4182     50   -287     51  A    C  
ATOM   2022  N   ASP A 909      -5.064 -11.888 -10.767  1.00 36.67      A    N  
ANISOU 2022  N   ASP A 909     4769   4510   4655    636   -607    108  A    N  
ATOM   2023  CA  ASP A 909      -3.961 -12.642 -11.354  1.00 40.40      A    C  
ANISOU 2023  CA  ASP A 909     5149   5038   5162    876   -604     82  A    C  
ATOM   2024  C   ASP A 909      -4.094 -12.693 -12.868  1.00 38.40      A    C  
ANISOU 2024  C   ASP A 909     4895   4812   4883    958   -461      9  A    C  
ATOM   2025  O   ASP A 909      -5.133 -12.339 -13.438  1.00 38.75      A    O  
ANISOU 2025  O   ASP A 909     5044   4792   4886    827   -400    -17  A    O  
ATOM   2026  CB  ASP A 909      -3.956 -14.091 -10.832  1.00 45.44      A    C  
ANISOU 2026  CB  ASP A 909     5984   5497   5783   1035   -730     82  A    C  
ATOM   2027  CG  ASP A 909      -3.783 -14.173  -9.311  1.00 63.96      A    C  
ANISOU 2027  CG  ASP A 909     8365   7807   8129    971   -885    163  A    C  
ATOM   2028  OD1 ASP A 909      -2.920 -13.429  -8.764  1.00 52.74      A    O  
ANISOU 2028  OD1 ASP A 909     6742   6547   6751    943   -926    206  A    O  
ATOM   2029  OD2 ASP A 909      -4.534 -14.949  -8.655  1.00 61.85      A    O1-
ANISOU 2029  OD2 ASP A 909     8338   7354   7809    924   -973    194  A    O1-
ATOM   2030  N   GLN A 910      -3.034 -13.181 -13.498  1.00 41.05      A    N  
ANISOU 2030  N   GLN A 910     5115   5248   5234   1196   -413    -20  A    N  
ATOM   2031  CA  GLN A 910      -2.985 -13.408 -14.934  1.00 44.13      A    C  
ANISOU 2031  CA  GLN A 910     5530   5670   5566   1334   -273    -97  A    C  
ATOM   2032  C   GLN A 910      -3.979 -14.503 -15.323  1.00 42.57      A    C  
ANISOU 2032  C   GLN A 910     5672   5208   5294   1391   -328   -172  A    C  
ATOM   2033  O   GLN A 910      -3.841 -15.614 -14.851  1.00 43.80      A    O  
ANISOU 2033  O   GLN A 910     5984   5212   5447   1541   -444   -187  A    O  
ATOM   2034  CB  GLN A 910      -1.577 -13.834 -15.350  1.00 47.20      A    C  
ANISOU 2034  CB  GLN A 910     5720   6238   5975   1627   -206   -110  A    C  
ATOM   2035  CG  GLN A 910      -1.396 -14.070 -16.843  1.00 47.94      A    C  
ANISOU 2035  CG  GLN A 910     5841   6397   5977   1810    -33   -194  A    C  
ATOM   2036  CD  GLN A 910       0.035 -14.377 -17.243  1.00 50.67      A    C  
ANISOU 2036  CD  GLN A 910     5934   6981   6335   2117     73   -195  A    C  
ATOM   2037  NE2 GLN A 910       0.192 -15.020 -18.390  1.00 53.50      A    N  
ANISOU 2037  NE2 GLN A 910     6406   7338   6581   2378    202   -295  A    N  
ATOM   2038  OE1 GLN A 910       0.983 -14.028 -16.550  1.00 56.68      A    O  
ANISOU 2038  OE1 GLN A 910     6400   7938   7199   2124     40   -105  A    O  
ATOM   2039  N   PRO A 911      -4.955 -14.194 -16.196  1.00 39.24      A    N  
ANISOU 2039  N   PRO A 911     5374   4726   4810   1264   -266   -212  A    N  
ATOM   2040  CA  PRO A 911      -5.870 -15.237 -16.654  1.00 40.66      A    C  
ANISOU 2040  CA  PRO A 911     5873   4657   4917   1291   -344   -277  A    C  
ATOM   2041  C   PRO A 911      -5.205 -16.169 -17.646  1.00 42.61      A    C  
ANISOU 2041  C   PRO A 911     6245   4863   5084   1600   -302   -382  A    C  
ATOM   2042  O   PRO A 911      -4.152 -15.839 -18.195  1.00 42.31      A    O  
ANISOU 2042  O   PRO A 911     6006   5036   5034   1780   -161   -403  A    O  
ATOM   2043  CB  PRO A 911      -7.010 -14.450 -17.295  1.00 41.77      A    C  
ANISOU 2043  CB  PRO A 911     6052   4794   5025   1061   -298   -276  A    C  
ATOM   2044  CG  PRO A 911      -6.378 -13.192 -17.769  1.00 42.84      A    C  
ANISOU 2044  CG  PRO A 911     5932   5173   5171   1034   -146   -255  A    C  
ATOM   2045  CD  PRO A 911      -5.201 -12.912 -16.884  1.00 42.73      A    C  
ANISOU 2045  CD  PRO A 911     5681   5316   5239   1099   -140   -196  A    C  
ATOM   2046  N   PHE A 912      -5.829 -17.319 -17.877  1.00 45.91      A    N  
ANISOU 2046  N   PHE A 912     6998   5010   5436   1658   -425   -444  A    N  
ATOM   2047  CA  PHE A 912      -5.185 -18.432 -18.582  1.00 49.80      A    C  
ANISOU 2047  CA  PHE A 912     7690   5392   5838   2000   -431   -557  A    C  
ATOM   2048  C   PHE A 912      -4.764 -18.111 -20.023  1.00 51.61      A    C  
ANISOU 2048  C   PHE A 912     7887   5769   5953   2167   -244   -653  A    C  
ATOM   2049  O   PHE A 912      -3.687 -18.520 -20.442  1.00 52.47      A    O  
ANISOU 2049  O   PHE A 912     7946   5979   6014   2504   -146   -718  A    O  
ATOM   2050  CB  PHE A 912      -6.076 -19.685 -18.557  1.00 54.73      A    C  
ANISOU 2050  CB  PHE A 912     8743   5648   6404   1973   -637   -600  A    C  
ATOM   2051  CG  PHE A 912      -5.464 -20.861 -19.253  1.00 58.75      A    C  
ANISOU 2051  CG  PHE A 912     9530   5991   6803   2344   -670   -733  A    C  
ATOM   2052  CD1 PHE A 912      -4.488 -21.639 -18.609  1.00 61.68      A    C  
ANISOU 2052  CD1 PHE A 912     9914   6316   7207   2642   -732   -740  A    C  
ATOM   2053  CD2 PHE A 912      -5.803 -21.161 -20.586  1.00 60.55      A    C  
ANISOU 2053  CD2 PHE A 912    10013   6115   6877   2430   -640   -860  A    C  
ATOM   2054  CE1 PHE A 912      -3.897 -22.727 -19.270  1.00 65.67      A    C  
ANISOU 2054  CE1 PHE A 912    10694   6659   7599   3041   -758   -878  A    C  
ATOM   2055  CE2 PHE A 912      -5.210 -22.243 -21.254  1.00 64.45      A    C  
ANISOU 2055  CE2 PHE A 912    10803   6445   7241   2815   -664  -1005  A    C  
ATOM   2056  CZ  PHE A 912      -4.254 -23.025 -20.596  1.00 66.54      A    C  
ANISOU 2056  CZ  PHE A 912    11083   6657   7544   3134   -716  -1017  A    C  
ATOM   2057  N   TYR A 913      -5.611 -17.395 -20.765  1.00 48.51      A    N  
ANISOU 2057  N   TYR A 913     7524   5401   5508   1947   -193   -655  A    N  
ATOM   2058  CA  TYR A 913      -5.339 -17.087 -22.180  1.00 49.10      A    C  
ANISOU 2058  CA  TYR A 913     7619   5596   5440   2075    -25   -737  A    C  
ATOM   2059  C   TYR A 913      -4.473 -15.835 -22.411  1.00 47.66      A    C  
ANISOU 2059  C   TYR A 913     7046   5775   5288   2061    196   -665  A    C  
ATOM   2060  O   TYR A 913      -4.100 -15.543 -23.556  1.00 47.60      A    O  
ANISOU 2060  O   TYR A 913     7024   5911   5150   2175    365   -712  A    O  
ATOM   2061  CB  TYR A 913      -6.642 -17.040 -22.991  1.00 48.56      A    C  
ANISOU 2061  CB  TYR A 913     7817   5357   5276   1870   -107   -775  A    C  
ATOM   2062  CG  TYR A 913      -7.429 -18.327 -22.879  1.00 48.70      A    C  
ANISOU 2062  CG  TYR A 913     8231   5020   5254   1865   -338   -837  A    C  
ATOM   2063  CD1 TYR A 913      -7.164 -19.407 -23.727  1.00 51.15      A    C  
ANISOU 2063  CD1 TYR A 913     8887   5147   5402   2144   -376   -982  A    C  
ATOM   2064  CD2 TYR A 913      -8.412 -18.488 -21.894  1.00 52.03      A    C  
ANISOU 2064  CD2 TYR A 913     8695   5284   5789   1584   -522   -743  A    C  
ATOM   2065  CE1 TYR A 913      -7.867 -20.601 -23.611  1.00 56.43      A    C  
ANISOU 2065  CE1 TYR A 913     9957   5454   6031   2114   -621  -1031  A    C  
ATOM   2066  CE2 TYR A 913      -9.121 -19.680 -21.767  1.00 53.03      A    C  
ANISOU 2066  CE2 TYR A 913     9181   5085   5882   1536   -746   -771  A    C  
ATOM   2067  CZ  TYR A 913      -8.858 -20.727 -22.632  1.00 54.94      A    C  
ANISOU 2067  CZ  TYR A 913     9785   5117   5971   1786   -811   -914  A    C  
ATOM   2068  OH  TYR A 913      -9.555 -21.904 -22.487  1.00 63.41      A    O  
ANISOU 2068  OH  TYR A 913    11247   5834   7010   1709  -1065   -933  A    O  
ATOM   2069  N   ALA A 914      -4.140 -15.114 -21.342  1.00 48.51      A    N  
ANISOU 2069  N   ALA A 914     6858   6023   5549   1913    187   -548  A    N  
ATOM   2070  CA  ALA A 914      -3.228 -13.974 -21.435  1.00 52.19      A    C  
ANISOU 2070  CA  ALA A 914     6955   6814   6059   1871    357   -462  A    C  
ATOM   2071  C   ALA A 914      -1.785 -14.447 -21.479  1.00 55.61      A    C  
ANISOU 2071  C   ALA A 914     7187   7446   6497   2198    468   -473  A    C  
ATOM   2072  O   ALA A 914      -1.412 -15.399 -20.790  1.00 55.61      A    O  
ANISOU 2072  O   ALA A 914     7239   7345   6546   2396    360   -500  A    O  
ATOM   2073  CB  ALA A 914      -3.422 -13.023 -20.270  1.00 46.63      A    C  
ANISOU 2073  CB  ALA A 914     6052   6162   5505   1585    277   -341  A    C  
ATOM   2074  N   THR A 915      -0.983 -13.766 -22.289  1.00 56.08      A    N  
ANISOU 2074  N   THR A 915     7007   7799   6502   2252    682   -437  A    N  
ATOM   2075  CA  THR A 915       0.476 -13.804 -22.171  1.00 57.39      A    C  
ANISOU 2075  CA  THR A 915     6822   8266   6717   2480    810   -385  A    C  
ATOM   2076  C   THR A 915       0.916 -12.895 -21.036  1.00 54.31      A    C  
ANISOU 2076  C   THR A 915     6096   8027   6511   2231    731   -232  A    C  
ATOM   2077  O   THR A 915       0.149 -12.037 -20.592  1.00 51.71      A    O  
ANISOU 2077  O   THR A 915     5804   7608   6236   1892    639   -174  A    O  
ATOM   2078  CB  THR A 915       1.158 -13.291 -23.451  1.00 61.29      A    C  
ANISOU 2078  CB  THR A 915     7146   9062   7079   2574   1088   -368  A    C  
ATOM   2079  CG2 THR A 915       0.845 -14.207 -24.634  1.00 62.27      A    C  
ANISOU 2079  CG2 THR A 915     7625   9053   6983   2863   1177   -533  A    C  
ATOM   2080  OG1 THR A 915       0.709 -11.956 -23.729  1.00 58.23      A    O  
ANISOU 2080  OG1 THR A 915     6679   8753   6693   2201   1132   -266  A    O  
ATOM   2081  N   GLU A 916       2.177 -13.035 -20.638  1.00 56.53      A    N  
ANISOU 2081  N   GLU A 916     6046   8556   6879   2410    771   -168  A    N  
ATOM   2082  CA  GLU A 916       2.801 -12.146 -19.642  1.00 58.89      A    C  
ANISOU 2082  CA  GLU A 916     5996   9039   7343   2179    689    -14  A    C  
ATOM   2083  C   GLU A 916       2.741 -10.649 -20.037  1.00 57.37      A    C  
ANISOU 2083  C   GLU A 916     5634   9012   7151   1816    784    101  A    C  
ATOM   2084  O   GLU A 916       2.482  -9.794 -19.186  1.00 52.92      A    O  
ANISOU 2084  O   GLU A 916     5023   8399   6685   1505    642    184  A    O  
ATOM   2085  CB  GLU A 916       4.247 -12.576 -19.357  1.00 65.76      A    C  
ANISOU 2085  CB  GLU A 916     6496  10194   8296   2457    728     45  A    C  
ATOM   2086  CG  GLU A 916       4.822 -12.032 -18.059  1.00 75.12      A    C  
ANISOU 2086  CG  GLU A 916     7400  11482   9659   2261    544    182  A    C  
ATOM   2087  N   GLU A 917       2.911 -10.363 -21.329  1.00 59.62      A    N  
ANISOU 2087  N   GLU A 917     5885   9460   7307   1862   1013     98  A    N  
ATOM   2088  CA  GLU A 917       2.915  -8.990 -21.856  1.00 61.49      A    C  
ANISOU 2088  CA  GLU A 917     5989   9853   7522   1534   1114    219  A    C  
ATOM   2089  C   GLU A 917       1.535  -8.362 -21.778  1.00 54.42      A    C  
ANISOU 2089  C   GLU A 917     5415   8664   6600   1249    993    188  A    C  
ATOM   2090  O   GLU A 917       1.405  -7.202 -21.406  1.00 55.62      A    O  
ANISOU 2090  O   GLU A 917     5489   8827   6816    926    925    293  A    O  
ATOM   2091  CB  GLU A 917       3.404  -8.931 -23.312  1.00 70.38      A    C  
ANISOU 2091  CB  GLU A 917     7036  11224   8482   1675   1403    228  A    C  
ATOM   2092  CG  GLU A 917       4.828  -9.436 -23.559  1.00 82.25      A    C  
ANISOU 2092  CG  GLU A 917     8164  13096   9992   1980   1585    276  A    C  
ATOM   2093  CD  GLU A 917       4.883 -10.880 -24.053  1.00 93.65      A    C  
ANISOU 2093  CD  GLU A 917     9807  14465  11313   2470   1667     98  A    C  
ATOM   2094  OE1 GLU A 917       4.502 -11.788 -23.275  1.00 87.63      A    O  
ANISOU 2094  OE1 GLU A 917     9250  13433  10614   2624   1468     -9  A    O  
ATOM   2095  OE2 GLU A 917       5.309 -11.107 -25.209  1.00102.66      A    O1-
ANISOU 2095  OE2 GLU A 917    10922  15806  12278   2701   1927     65  A    O1-
ATOM   2096  N   ILE A 918       0.508  -9.131 -22.130  1.00 51.85      A    N  
ANISOU 2096  N   ILE A 918     5449   8073   6177   1373    954     46  A    N  
ATOM   2097  CA  ILE A 918      -0.887  -8.695 -21.953  1.00 49.88      A    C  
ANISOU 2097  CA  ILE A 918     5484   7550   5920   1138    819     13  A    C  
ATOM   2098  C   ILE A 918      -1.194  -8.442 -20.468  1.00 46.82      A    C  
ANISOU 2098  C   ILE A 918     5074   7034   5683    968    610     53  A    C  
ATOM   2099  O   ILE A 918      -1.869  -7.455 -20.139  1.00 44.63      A    O  
ANISOU 2099  O   ILE A 918     4852   6671   5436    703    534    100  A    O  
ATOM   2100  CB  ILE A 918      -1.878  -9.682 -22.614  1.00 51.28      A    C  
ANISOU 2100  CB  ILE A 918     6026   7486   5971   1298    795   -133  A    C  
ATOM   2101  CG1 ILE A 918      -1.712  -9.606 -24.137  1.00 58.31      A    C  
ANISOU 2101  CG1 ILE A 918     6981   8496   6676   1400    995   -164  A    C  
ATOM   2102  CG2 ILE A 918      -3.330  -9.362 -22.264  1.00 49.89      A    C  
ANISOU 2102  CG2 ILE A 918     6088   7051   5817   1071    635   -152  A    C  
ATOM   2103  CD1 ILE A 918      -2.209 -10.823 -24.870  1.00 64.49      A    C  
ANISOU 2103  CD1 ILE A 918     8095   9096   7312   1653    990   -322  A    C  
ATOM   2104  N   TYR A 919      -0.673  -9.296 -19.584  1.00 47.32      A    N  
ANISOU 2104  N   TYR A 919     5068   7086   5826   1134    518     36  A    N  
ATOM   2105  CA  TYR A 919      -0.891  -9.136 -18.147  1.00 48.14      A    C  
ANISOU 2105  CA  TYR A 919     5170   7078   6044    992    323     75  A    C  
ATOM   2106  C   TYR A 919      -0.248  -7.870 -17.564  1.00 44.62      A    C  
ANISOU 2106  C   TYR A 919     4472   6796   5686    743    284    203  A    C  
ATOM   2107  O   TYR A 919      -0.862  -7.211 -16.733  1.00 43.36      A    O  
ANISOU 2107  O   TYR A 919     4408   6507   5562    530    154    226  A    O  
ATOM   2108  CB  TYR A 919      -0.438 -10.380 -17.355  1.00 52.38      A    C  
ANISOU 2108  CB  TYR A 919     5715   7557   6631   1235    217     38  A    C  
ATOM   2109  CG  TYR A 919      -0.757 -10.282 -15.884  1.00 47.26      A    C  
ANISOU 2109  CG  TYR A 919     5116   6777   6062   1090     16     78  A    C  
ATOM   2110  CD1 TYR A 919      -2.066 -10.003 -15.461  1.00 45.45      A    C  
ANISOU 2110  CD1 TYR A 919     5129   6334   5807    898    -62     55  A    C  
ATOM   2111  CD2 TYR A 919       0.240 -10.408 -14.911  1.00 50.47      A    C  
ANISOU 2111  CD2 TYR A 919     5319   7296   6563   1141    -94    146  A    C  
ATOM   2112  CE1 TYR A 919      -2.386  -9.886 -14.125  1.00 45.68      A    C  
ANISOU 2112  CE1 TYR A 919     5218   6261   5877    775   -218     90  A    C  
ATOM   2113  CE2 TYR A 919      -0.075 -10.300 -13.552  1.00 51.53      A    C  
ANISOU 2113  CE2 TYR A 919     5538   7304   6738   1005   -282    180  A    C  
ATOM   2114  CZ  TYR A 919      -1.397 -10.040 -13.169  1.00 46.83      A    C  
ANISOU 2114  CZ  TYR A 919     5206   6496   6092    826   -330    149  A    C  
ATOM   2115  OH  TYR A 919      -1.761  -9.906 -11.844  1.00 46.61      A    O  
ANISOU 2115  OH  TYR A 919     5278   6358   6072    701   -485    181  A    O  
ATOM   2116  N   ILE A 920       0.957  -7.531 -18.007  1.00 46.82      A    N  
ANISOU 2116  N   ILE A 920     4442   7358   5990    767    393    290  A    N  
ATOM   2117  CA  ILE A 920       1.601  -6.259 -17.619  1.00 52.62      A    C  
ANISOU 2117  CA  ILE A 920     4942   8250   6801    482    346    431  A    C  
ATOM   2118  C   ILE A 920       0.737  -5.048 -18.042  1.00 49.76      A    C  
ANISOU 2118  C   ILE A 920     4752   7771   6381    200    358    453  A    C  
ATOM   2119  O   ILE A 920       0.629  -4.088 -17.281  1.00 51.19      A    O  
ANISOU 2119  O   ILE A 920     4948   7886   6614    -51    218    513  A    O  
ATOM   2120  CB  ILE A 920       3.053  -6.165 -18.160  1.00 57.09      A    C  
ANISOU 2120  CB  ILE A 920     5107   9182   7403    547    484    544  A    C  
ATOM   2121  CG1 ILE A 920       3.944  -7.178 -17.420  1.00 55.98      A    C  
ANISOU 2121  CG1 ILE A 920     4766   9150   7354    805    406    542  A    C  
ATOM   2122  CG2 ILE A 920       3.652  -4.754 -18.027  1.00 58.64      A    C  
ANISOU 2122  CG2 ILE A 920     5082   9539   7661    188    445    711  A    C  
ATOM   2123  CD1 ILE A 920       5.240  -7.518 -18.145  1.00 64.14      A    C  
ANISOU 2123  CD1 ILE A 920     5419  10554   8398   1020    592    613  A    C  
ATOM   2124  N   ILE A 921       0.119  -5.117 -19.222  1.00 45.92      A    N  
ANISOU 2124  N   ILE A 921     4424   7244   5779    258    504    399  A    N  
ATOM   2125  CA  ILE A 921      -0.803  -4.073 -19.683  1.00 47.71      A    C  
ANISOU 2125  CA  ILE A 921     4846   7338   5944     36    501    412  A    C  
ATOM   2126  C   ILE A 921      -2.037  -3.961 -18.760  1.00 50.04      A    C  
ANISOU 2126  C   ILE A 921     5397   7353   6265    -38    330    340  A    C  
ATOM   2127  O   ILE A 921      -2.399  -2.851 -18.360  1.00 45.67      A    O  
ANISOU 2127  O   ILE A 921     4910   6713   5728   -258    240    386  A    O  
ATOM   2128  CB  ILE A 921      -1.230  -4.287 -21.161  1.00 50.63      A    C  
ANISOU 2128  CB  ILE A 921     5349   7720   6168    138    675    366  A    C  
ATOM   2129  CG1 ILE A 921      -0.023  -4.116 -22.112  1.00 56.38      A    C  
ANISOU 2129  CG1 ILE A 921     5819   8761   6841    171    878    464  A    C  
ATOM   2130  CG2 ILE A 921      -2.337  -3.321 -21.571  1.00 48.26      A    C  
ANISOU 2130  CG2 ILE A 921     5282   7247   5808    -56    633    371  A    C  
ATOM   2131  N   MET A 922      -2.671  -5.099 -18.452  1.00 44.27      A    N  
ANISOU 2131  N   MET A 922     4813   6483   5526    147    290    235  A    N  
ATOM   2132  CA  MET A 922      -3.791  -5.154 -17.496  1.00 45.60      A    C  
ANISOU 2132  CA  MET A 922     5182   6429   5714     93    150    183  A    C  
ATOM   2133  C   MET A 922      -3.463  -4.489 -16.168  1.00 40.60      A    C  
ANISOU 2133  C   MET A 922     4484   5787   5156    -53     11    238  A    C  
ATOM   2134  O   MET A 922      -4.233  -3.668 -15.674  1.00 39.12      A    O  
ANISOU 2134  O   MET A 922     4432   5474   4958   -195    -63    237  A    O  
ATOM   2135  CB  MET A 922      -4.188  -6.594 -17.153  1.00 45.94      A    C  
ANISOU 2135  CB  MET A 922     5341   6359   5753    290    109    100  A    C  
ATOM   2136  CG  MET A 922      -5.071  -7.292 -18.125  1.00 50.61      A    C  
ANISOU 2136  CG  MET A 922     6127   6842   6263    391    163     20  A    C  
ATOM   2137  SD  MET A 922      -5.385  -8.956 -17.475  1.00 45.85      A    S  
ANISOU 2137  SD  MET A 922     5675   6077   5669    573     63    -51  A    S  
ATOM   2138  CE  MET A 922      -5.499  -9.756 -19.061  1.00 43.69      A    C  
ANISOU 2138  CE  MET A 922     5543   5779   5278    753    167   -139  A    C  
ATOM   2139  N   GLN A 923      -2.333  -4.892 -15.594  1.00 38.91      A    N  
ANISOU 2139  N   GLN A 923     4076   5702   5007      6    -33    281  A    N  
ATOM   2140  CA  GLN A 923      -1.860  -4.351 -14.309  1.00 43.66      A    C  
ANISOU 2140  CA  GLN A 923     4614   6304   5669   -130   -196    336  A    C  
ATOM   2141  C   GLN A 923      -1.673  -2.843 -14.295  1.00 44.16      A    C  
ANISOU 2141  C   GLN A 923     4657   6386   5738   -395   -243    411  A    C  
ATOM   2142  O   GLN A 923      -2.000  -2.192 -13.275  1.00 42.47      A    O  
ANISOU 2142  O   GLN A 923     4571   6045   5519   -527   -387    408  A    O  
ATOM   2143  CB  GLN A 923      -0.532  -5.002 -13.902  1.00 49.43      A    C  
ANISOU 2143  CB  GLN A 923     5091   7215   6477    -19   -241    389  A    C  
ATOM   2144  CG  GLN A 923      -0.690  -6.425 -13.407  1.00 57.18      A    C  
ANISOU 2144  CG  GLN A 923     6155   8112   7459    224   -283    322  A    C  
ATOM   2145  CD  GLN A 923       0.641  -6.990 -12.930  1.00 63.93      A    C  
ANISOU 2145  CD  GLN A 923     6754   9142   8395    354   -356    381  A    C  
ATOM   2146  NE2 GLN A 923       0.697  -7.415 -11.681  1.00 59.64      A    N  
ANISOU 2146  NE2 GLN A 923     6276   8510   7875    377   -534    386  A    N  
ATOM   2147  OE1 GLN A 923       1.611  -7.027 -13.686  1.00 65.30      A    O  
ANISOU 2147  OE1 GLN A 923     6664   9542   8604    438   -249    430  A    O  
ATOM   2148  N   SER A 924      -1.131  -2.311 -15.399  1.00 40.40      A    N  
ANISOU 2148  N   SER A 924     4040   6056   5254   -470   -125    481  A    N  
ATOM   2149  CA  SER A 924      -0.932  -0.862 -15.579  1.00 44.10      A    C  
ANISOU 2149  CA  SER A 924     4511   6527   5718   -746   -168    572  A    C  
ATOM   2150  C   SER A 924      -2.266  -0.124 -15.621  1.00 38.40      A    C  
ANISOU 2150  C   SER A 924     4100   5564   4926   -815   -198    509  A    C  
ATOM   2151  O   SER A 924      -2.380   0.962 -15.073  1.00 40.88      A    O  
ANISOU 2151  O   SER A 924     4532   5765   5236  -1002   -327    538  A    O  
ATOM   2152  CB  SER A 924      -0.103  -0.545 -16.843  1.00 46.74      A    C  
ANISOU 2152  CB  SER A 924     4632   7086   6040   -811    -10    679  A    C  
ATOM   2153  OG  SER A 924      -0.868  -0.784 -18.022  1.00 48.23      A    O  
ANISOU 2153  OG  SER A 924     4960   7233   6133   -698    153    622  A    O  
ATOM   2154  N   CYS A 925      -3.283  -0.733 -16.235  1.00 38.86      A    N  
ANISOU 2154  N   CYS A 925     4299   5540   4928   -653    -97    421  A    N  
ATOM   2155  CA  CYS A 925      -4.645  -0.188 -16.183  1.00 35.14      A    C  
ANISOU 2155  CA  CYS A 925     4087   4862   4403   -673   -132    359  A    C  
ATOM   2156  C   CYS A 925      -5.225  -0.093 -14.780  1.00 38.38      A    C  
ANISOU 2156  C   CYS A 925     4635   5128   4820   -670   -265    304  A    C  
ATOM   2157  O   CYS A 925      -6.116   0.708 -14.567  1.00 34.08      A    O  
ANISOU 2157  O   CYS A 925     4277   4437   4234   -714   -310    274  A    O  
ATOM   2158  CB  CYS A 925      -5.596  -1.009 -17.012  1.00 38.83      A    C  
ANISOU 2158  CB  CYS A 925     4645   5288   4821   -508    -28    285  A    C  
ATOM   2159  SG  CYS A 925      -5.200  -1.049 -18.753  1.00 37.94      A    S  
ANISOU 2159  SG  CYS A 925     4466   5309   4641   -488    136    326  A    S  
ATOM   2160  N   TRP A 926      -4.731  -0.927 -13.853  1.00 38.19      A    N  
ANISOU 2160  N   TRP A 926     4527   5150   4836   -598   -322    292  A    N  
ATOM   2161  CA  TRP A 926      -5.173  -0.969 -12.471  1.00 35.44      A    C  
ANISOU 2161  CA  TRP A 926     4310   4689   4468   -588   -438    249  A    C  
ATOM   2162  C   TRP A 926      -4.271  -0.215 -11.509  1.00 37.24      A    C  
ANISOU 2162  C   TRP A 926     4515   4923   4711   -742   -599    298  A    C  
ATOM   2163  O   TRP A 926      -4.376  -0.420 -10.314  1.00 35.98      A    O  
ANISOU 2163  O   TRP A 926     4447   4701   4523   -719   -703    269  A    O  
ATOM   2164  CB  TRP A 926      -5.352  -2.429 -12.027  1.00 34.66      A    C  
ANISOU 2164  CB  TRP A 926     4190   4600   4378   -415   -421    210  A    C  
ATOM   2165  CG  TRP A 926      -6.275  -3.226 -12.913  1.00 33.10      A    C  
ANISOU 2165  CG  TRP A 926     4047   4370   4161   -291   -302    161  A    C  
ATOM   2166  CD1 TRP A 926      -7.376  -2.771 -13.579  1.00 30.49      A    C  
ANISOU 2166  CD1 TRP A 926     3829   3964   3790   -305   -241    132  A    C  
ATOM   2167  CD2 TRP A 926      -6.181  -4.620 -13.205  1.00 31.61      A    C  
ANISOU 2167  CD2 TRP A 926     3820   4205   3987   -137   -261    138  A    C  
ATOM   2168  CE2 TRP A 926      -7.244  -4.937 -14.072  1.00 30.15      A    C  
ANISOU 2168  CE2 TRP A 926     3739   3952   3766    -92   -184     96  A    C  
ATOM   2169  CE3 TRP A 926      -5.295  -5.631 -12.824  1.00 34.92      A    C  
ANISOU 2169  CE3 TRP A 926     4143   4682   4442    -23   -299    150  A    C  
ATOM   2170  NE1 TRP A 926      -7.952  -3.786 -14.287  1.00 30.50      A    N  
ANISOU 2170  NE1 TRP A 926     3854   3953   3783   -196   -173     98  A    N  
ATOM   2171  CZ2 TRP A 926      -7.467  -6.230 -14.540  1.00 31.91      A    C  
ANISOU 2171  CZ2 TRP A 926     4003   4143   3980     39   -156     59  A    C  
ATOM   2172  CZ3 TRP A 926      -5.502  -6.917 -13.309  1.00 32.99      A    C  
ANISOU 2172  CZ3 TRP A 926     3946   4400   4190    139   -258    109  A    C  
ATOM   2173  CH2 TRP A 926      -6.582  -7.204 -14.149  1.00 36.54      A    C  
ANISOU 2173  CH2 TRP A 926     4528   4761   4594    157   -191     62  A    C  
ATOM   2174  N   ALA A 927      -3.426   0.697 -12.007  1.00 36.71      A    N  
ANISOU 2174  N   ALA A 927     4349   4923   4675   -919   -633    381  A    N  
ATOM   2175  CA  ALA A 927      -2.691   1.607 -11.132  1.00 38.68      A    C  
ANISOU 2175  CA  ALA A 927     4626   5140   4931  -1118   -825    433  A    C  
ATOM   2176  C   ALA A 927      -3.719   2.396 -10.312  1.00 42.72      A    C  
ANISOU 2176  C   ALA A 927     5470   5418   5344  -1131   -914    348  A    C  
ATOM   2177  O   ALA A 927      -4.725   2.870 -10.868  1.00 38.76      A    O  
ANISOU 2177  O   ALA A 927     5128   4807   4793  -1085   -830    302  A    O  
ATOM   2178  CB  ALA A 927      -1.821   2.550 -11.935  1.00 45.71      A    C  
ANISOU 2178  CB  ALA A 927     5388   6117   5862  -1344   -841    551  A    C  
ATOM   2179  N   PHE A 928      -3.509   2.450  -8.996  1.00 40.71      A    N  
ANISOU 2179  N   PHE A 928     5320   5099   5050  -1158  -1075    322  A    N  
ATOM   2180  CA  PHE A 928      -4.442   3.127  -8.092  1.00 41.84      A    C  
ANISOU 2180  CA  PHE A 928     5791   5036   5068  -1128  -1146    229  A    C  
ATOM   2181  C   PHE A 928      -4.568   4.620  -8.445  1.00 40.99      A    C  
ANISOU 2181  C   PHE A 928     5881   4772   4920  -1283  -1224    235  A    C  
ATOM   2182  O   PHE A 928      -5.680   5.157  -8.557  1.00 39.08      A    O  
ANISOU 2182  O   PHE A 928     5861   4385   4601  -1181  -1164    158  A    O  
ATOM   2183  CB  PHE A 928      -4.020   2.942  -6.625  1.00 41.51      A    C  
ANISOU 2183  CB  PHE A 928     5844   4963   4966  -1146  -1321    209  A    C  
ATOM   2184  CG  PHE A 928      -5.118   3.249  -5.662  1.00 43.78      A    C  
ANISOU 2184  CG  PHE A 928     6452   5085   5097  -1029  -1325     99  A    C  
ATOM   2185  CD1 PHE A 928      -6.053   2.257  -5.319  1.00 41.78      A    C  
ANISOU 2185  CD1 PHE A 928     6214   4865   4795   -825  -1179     49  A    C  
ATOM   2186  CD2 PHE A 928      -5.284   4.542  -5.157  1.00 44.58      A    C  
ANISOU 2186  CD2 PHE A 928     6851   4997   5090  -1115  -1461     47  A    C  
ATOM   2187  CE1 PHE A 928      -7.111   2.543  -4.453  1.00 44.94      A    C  
ANISOU 2187  CE1 PHE A 928     6879   5156   5040   -706  -1145    -39  A    C  
ATOM   2188  CE2 PHE A 928      -6.343   4.837  -4.291  1.00 47.42      A    C  
ANISOU 2188  CE2 PHE A 928     7511   5223   5284   -959  -1432    -65  A    C  
ATOM   2189  CZ  PHE A 928      -7.254   3.832  -3.932  1.00 44.54      A    C  
ANISOU 2189  CZ  PHE A 928     7115   4937   4871   -751  -1259   -103  A    C  
ATOM   2190  N   ASP A 929      -3.408   5.245  -8.640  1.00 40.44      A    N  
ANISOU 2190  N   ASP A 929     5715   4741   4910  -1528  -1363    338  A    N  
ATOM   2191  CA  ASP A 929      -3.282   6.613  -9.120  1.00 42.70      A    C  
ANISOU 2191  CA  ASP A 929     6164   4885   5176  -1734  -1461    384  A    C  
ATOM   2192  C   ASP A 929      -3.626   6.629 -10.622  1.00 46.42      A    C  
ANISOU 2192  C   ASP A 929     6522   5423   5691  -1707  -1267    433  A    C  
ATOM   2193  O   ASP A 929      -2.893   6.059 -11.433  1.00 43.58      A    O  
ANISOU 2193  O   ASP A 929     5856   5282   5420  -1754  -1163    530  A    O  
ATOM   2194  CB  ASP A 929      -1.847   7.107  -8.853  1.00 47.17      A    C  
ANISOU 2194  CB  ASP A 929     6606   5513   5804  -2044  -1675    513  A    C  
ATOM   2195  CG  ASP A 929      -1.633   8.600  -9.151  1.00 54.17      A    C  
ANISOU 2195  CG  ASP A 929     7718   6206   6657  -2318  -1839    576  A    C  
ATOM   2196  OD1 ASP A 929      -2.472   9.267  -9.778  1.00 56.89      A    O  
ANISOU 2196  OD1 ASP A 929     8283   6388   6945  -2268  -1771    538  A    O  
ATOM   2197  OD2 ASP A 929      -0.584   9.125  -8.737  1.00 62.28      A    O1-
ANISOU 2197  OD2 ASP A 929     8709   7238   7718  -2603  -2064    675  A    O1-
ATOM   2198  N   SER A 930      -4.727   7.306 -10.971  1.00 42.67      A    N  
ANISOU 2198  N   SER A 930     6307   4765   5142  -1617  -1225    366  A    N  
ATOM   2199  CA  SER A 930      -5.211   7.428 -12.357  1.00 42.22      A    C  
ANISOU 2199  CA  SER A 930     6210   4732   5099  -1581  -1071    404  A    C  
ATOM   2200  C   SER A 930      -4.194   7.966 -13.361  1.00 44.38      A    C  
ANISOU 2200  C   SER A 930     6345   5096   5423  -1845  -1084    565  A    C  
ATOM   2201  O   SER A 930      -4.256   7.608 -14.527  1.00 43.64      A    O  
ANISOU 2201  O   SER A 930     6104   5130   5348  -1808   -918    616  A    O  
ATOM   2202  CB  SER A 930      -6.456   8.318 -12.415  1.00 39.46      A    C  
ANISOU 2202  CB  SER A 930     6194   4141   4658  -1463  -1091    319  A    C  
ATOM   2203  OG  SER A 930      -6.145   9.614 -11.922  1.00 43.67      A    O  
ANISOU 2203  OG  SER A 930     7008   4449   5134  -1639  -1304    332  A    O  
ATOM   2204  N   ARG A 931      -3.292   8.823 -12.896  1.00 45.48      A    N  
ANISOU 2204  N   ARG A 931     6543   5167   5569  -2119  -1284    648  A    N  
ATOM   2205  CA  ARG A 931      -2.240   9.401 -13.733  1.00 50.87      A    C  
ANISOU 2205  CA  ARG A 931     7075   5954   6300  -2426  -1312    833  A    C  
ATOM   2206  C   ARG A 931      -1.171   8.400 -14.153  1.00 51.21      A    C  
ANISOU 2206  C   ARG A 931     6661   6353   6442  -2457  -1178    939  A    C  
ATOM   2207  O   ARG A 931      -0.486   8.657 -15.122  1.00 50.44      A    O  
ANISOU 2207  O   ARG A 931     6384   6410   6370  -2639  -1102   1092  A    O  
ATOM   2208  CB  ARG A 931      -1.548  10.552 -13.012  1.00 56.38      A    C  
ANISOU 2208  CB  ARG A 931     7960   6477   6986  -2744  -1600    904  A    C  
ATOM   2209  CG  ARG A 931      -2.457  11.724 -12.660  1.00 63.01      A    C  
ANISOU 2209  CG  ARG A 931     9297   6933   7711  -2728  -1759    810  A    C  
ATOM   2210  CD  ARG A 931      -1.769  12.701 -11.709  1.00 70.07      A    C  
ANISOU 2210  CD  ARG A 931    10422   7624   8576  -3016  -2082    844  A    C  
ATOM   2211  NE  ARG A 931      -1.372  12.078 -10.444  1.00 70.11      A    N  
ANISOU 2211  NE  ARG A 931    10347   7701   8592  -2967  -2186    772  A    N  
ATOM   2212  CZ  ARG A 931      -0.815  12.711  -9.406  1.00 80.71      A    C  
ANISOU 2212  CZ  ARG A 931    11895   8880   9893  -3174  -2484    769  A    C  
ATOM   2213  NH1 ARG A 931      -0.585  14.033  -9.424  1.00 81.27      A    N1+
ANISOU 2213  NH1 ARG A 931    12295   8675   9910  -3459  -2728    830  A    N1+
ATOM   2214  NH2 ARG A 931      -0.493  12.005  -8.317  1.00 77.26      A    N  
ANISOU 2214  NH2 ARG A 931    11363   8535   9455  -3098  -2559    706  A    N  
ATOM   2215  N   LYS A 932      -1.021   7.281 -13.435  1.00 49.75      A    N  
ANISOU 2215  N   LYS A 932     6299   6301   6302  -2270  -1146    864  A    N  
ATOM   2216  CA  LYS A 932      -0.072   6.215 -13.830  1.00 52.42      A    C  
ANISOU 2216  CA  LYS A 932     6213   6973   6730  -2219  -1009    943  A    C  
ATOM   2217  C   LYS A 932      -0.643   5.246 -14.845  1.00 47.48      A    C  
ANISOU 2217  C   LYS A 932     5492   6464   6086  -1951   -742    886  A    C  
ATOM   2218  O   LYS A 932       0.110   4.460 -15.402  1.00 53.58      A    O  
ANISOU 2218  O   LYS A 932     5950   7500   6907  -1887   -602    949  A    O  
ATOM   2219  CB  LYS A 932       0.443   5.444 -12.609  1.00 58.07      A    C  
ANISOU 2219  CB  LYS A 932     6797   7765   7501  -2140  -1127    902  A    C  
ATOM   2220  CG  LYS A 932       1.328   6.285 -11.701  1.00 67.77      A    C  
ANISOU 2220  CG  LYS A 932     8043   8948   8760  -2441  -1410    991  A    C  
ATOM   2221  CD  LYS A 932       1.682   5.522 -10.432  1.00 79.46      A    C  
ANISOU 2221  CD  LYS A 932     9453  10470  10268  -2336  -1548    936  A    C  
ATOM   2222  CE  LYS A 932       2.468   6.380  -9.450  1.00 89.45      A    C  
ANISOU 2222  CE  LYS A 932    10790  11654  11541  -2639  -1872   1008  A    C  
ATOM   2223  NZ  LYS A 932       2.425   5.785  -8.085  1.00 92.54      A    N1+
ANISOU 2223  NZ  LYS A 932    11276  11986  11897  -2506  -2028    911  A    N1+
ATOM   2224  N   ARG A 933      -1.955   5.291 -15.096  1.00 43.91      A    N  
ANISOU 2224  N   ARG A 933     5306   5821   5558  -1789   -680    770  A    N  
ATOM   2225  CA  ARG A 933      -2.588   4.386 -16.062  1.00 40.86      A    C  
ANISOU 2225  CA  ARG A 933     4869   5514   5142  -1556   -466    711  A    C  
ATOM   2226  C   ARG A 933      -2.249   4.824 -17.487  1.00 46.28      A    C  
ANISOU 2226  C   ARG A 933     5483   6311   5791  -1670   -334    827  A    C  
ATOM   2227  O   ARG A 933      -2.123   6.033 -17.746  1.00 46.71      A    O  
ANISOU 2227  O   ARG A 933     5665   6265   5816  -1906   -420    921  A    O  
ATOM   2228  CB  ARG A 933      -4.095   4.374 -15.890  1.00 38.48      A    C  
ANISOU 2228  CB  ARG A 933     4847   4995   4779  -1380   -464    576  A    C  
ATOM   2229  CG  ARG A 933      -4.524   3.855 -14.506  1.00 39.85      A    C  
ANISOU 2229  CG  ARG A 933     5095   5083   4962  -1252   -555    468  A    C  
ATOM   2230  CD  ARG A 933      -6.031   3.937 -14.301  1.00 36.50      A    C  
ANISOU 2230  CD  ARG A 933     4912   4480   4475  -1090   -539    355  A    C  
ATOM   2231  NE  ARG A 933      -6.336   3.992 -12.876  1.00 36.27      A    N  
ANISOU 2231  NE  ARG A 933     5018   4345   4421  -1046   -653    282  A    N  
ATOM   2232  CZ  ARG A 933      -7.399   4.564 -12.325  1.00 35.84      A    C  
ANISOU 2232  CZ  ARG A 933     5203   4119   4294   -961   -691    202  A    C  
ATOM   2233  NH1 ARG A 933      -8.354   5.138 -13.064  1.00 35.04      A    N1+
ANISOU 2233  NH1 ARG A 933     5231   3924   4158   -898   -642    182  A    N1+
ATOM   2234  NH2 ARG A 933      -7.485   4.606 -11.005  1.00 37.76      A    N  
ANISOU 2234  NH2 ARG A 933     5566   4292   4490   -929   -785    144  A    N  
ATOM   2235  N   PRO A 934      -2.104   3.853 -18.412  1.00 45.03      A    N  
ANISOU 2235  N   PRO A 934     5152   6343   5614  -1505   -134    821  A    N  
ATOM   2236  CA  PRO A 934      -1.867   4.213 -19.814  1.00 45.08      A    C  
ANISOU 2236  CA  PRO A 934     5121   6462   5546  -1587     15    924  A    C  
ATOM   2237  C   PRO A 934      -3.099   4.877 -20.428  1.00 44.77      A    C  
ANISOU 2237  C   PRO A 934     5402   6194   5414  -1578     -2    882  A    C  
ATOM   2238  O   PRO A 934      -4.218   4.710 -19.928  1.00 42.56      A    O  
ANISOU 2238  O   PRO A 934     5316   5723   5132  -1428    -73    752  A    O  
ATOM   2239  CB  PRO A 934      -1.584   2.852 -20.482  1.00 46.39      A    C  
ANISOU 2239  CB  PRO A 934     5088   6847   5691  -1336    221    877  A    C  
ATOM   2240  CG  PRO A 934      -2.361   1.875 -19.649  1.00 47.89      A    C  
ANISOU 2240  CG  PRO A 934     5369   6910   5918  -1100    162    714  A    C  
ATOM   2241  CD  PRO A 934      -2.232   2.385 -18.242  1.00 40.66      A    C  
ANISOU 2241  CD  PRO A 934     4486   5881   5084  -1223    -41    714  A    C  
ATOM   2242  N   SER A 935      -2.881   5.663 -21.475  1.00 46.61      A    N  
ANISOU 2242  N   SER A 935     5683   6456   5570  -1745     54   1007  A    N  
ATOM   2243  CA  SER A 935      -3.978   6.266 -22.236  1.00 45.00      A    C  
ANISOU 2243  CA  SER A 935     5773   6056   5268  -1723     38    986  A    C  
ATOM   2244  C   SER A 935      -4.525   5.250 -23.250  1.00 42.82      A    C  
ANISOU 2244  C   SER A 935     5490   5872   4908  -1486    209    909  A    C  
ATOM   2245  O   SER A 935      -3.912   4.216 -23.509  1.00 44.88      A    O  
ANISOU 2245  O   SER A 935     5535   6349   5167  -1364    357    891  A    O  
ATOM   2246  CB  SER A 935      -3.470   7.506 -22.948  1.00 44.59      A    C  
ANISOU 2246  CB  SER A 935     5802   5987   5152  -2016     13   1169  A    C  
ATOM   2247  OG  SER A 935      -2.596   7.105 -23.972  1.00 48.42      A    O  
ANISOU 2247  OG  SER A 935     6063   6760   5574  -2061    220   1283  A    O  
ATOM   2248  N   PHE A 936      -5.666   5.565 -23.838  1.00 41.56      A    N  
ANISOU 2248  N   PHE A 936     5580   5540   4672  -1416    172    865  A    N  
ATOM   2249  CA  PHE A 936      -6.225   4.723 -24.904  1.00 43.83      A    C  
ANISOU 2249  CA  PHE A 936     5907   5888   4858  -1230    295    803  A    C  
ATOM   2250  C   PHE A 936      -5.399   4.686 -26.197  1.00 42.87      A    C  
ANISOU 2250  C   PHE A 936     5710   5976   4604  -1299    478    918  A    C  
ATOM   2251  O   PHE A 936      -5.247   3.600 -26.773  1.00 44.47      A    O  
ANISOU 2251  O   PHE A 936     5829   6327   4741  -1121    624    854  A    O  
ATOM   2252  CB  PHE A 936      -7.717   5.002 -25.143  1.00 40.54      A    C  
ANISOU 2252  CB  PHE A 936     5749   5249   4405  -1127    182    728  A    C  
ATOM   2253  CG  PHE A 936      -8.604   4.363 -24.110  1.00 37.10      A    C  
ANISOU 2253  CG  PHE A 936     5313   4714   4070   -956     97    585  A    C  
ATOM   2254  CD1 PHE A 936      -8.703   2.975 -24.036  1.00 33.53      A    C  
ANISOU 2254  CD1 PHE A 936     4749   4356   3636   -786    171    486  A    C  
ATOM   2255  CD2 PHE A 936      -9.315   5.138 -23.183  1.00 37.16      A    C  
ANISOU 2255  CD2 PHE A 936     5445   4534   4142   -962    -53    553  A    C  
ATOM   2256  CE1 PHE A 936      -9.469   2.370 -23.066  1.00 31.19      A    C  
ANISOU 2256  CE1 PHE A 936     4446   3981   3424   -664    100    383  A    C  
ATOM   2257  CE2 PHE A 936     -10.118   4.530 -22.229  1.00 33.54      A    C  
ANISOU 2257  CE2 PHE A 936     4966   4021   3757   -808   -100    438  A    C  
ATOM   2258  CZ  PHE A 936     -10.203   3.144 -22.182  1.00 32.74      A    C  
ANISOU 2258  CZ  PHE A 936     4737   4026   3678   -678    -24    364  A    C  
ATOM   2259  N   PRO A 937      -4.828   5.832 -26.621  1.00 42.89      A    N  
ANISOU 2259  N   PRO A 937     5747   5993   4555  -1556    473   1090  A    N  
ATOM   2260  CA  PRO A 937      -3.809   5.759 -27.705  1.00 48.74      A    C  
ANISOU 2260  CA  PRO A 937     6345   7004   5171  -1644    685   1228  A    C  
ATOM   2261  C   PRO A 937      -2.582   4.886 -27.362  1.00 52.65      A    C  
ANISOU 2261  C   PRO A 937     6472   7801   5731  -1584    842   1239  A    C  
ATOM   2262  O   PRO A 937      -2.135   4.149 -28.228  1.00 55.19      A    O  
ANISOU 2262  O   PRO A 937     6686   8346   5938  -1448   1055   1240  A    O  
ATOM   2263  CB  PRO A 937      -3.414   7.237 -27.945  1.00 48.33      A    C  
ANISOU 2263  CB  PRO A 937     6392   6886   5085  -1986    608   1433  A    C  
ATOM   2264  CG  PRO A 937      -4.607   8.029 -27.487  1.00 47.43      A    C  
ANISOU 2264  CG  PRO A 937     6599   6413   5009  -1988    367   1367  A    C  
ATOM   2265  CD  PRO A 937      -5.210   7.233 -26.328  1.00 44.23      A    C  
ANISOU 2265  CD  PRO A 937     6140   5922   4743  -1758    282   1169  A    C  
ATOM   2266  N   ASN A 938      -2.089   4.929 -26.113  1.00 53.12      A    N  
ANISOU 2266  N   ASN A 938     6360   7861   5962  -1653    731   1236  A    N  
ATOM   2267  CA  ASN A 938      -1.049   3.962 -25.646  1.00 54.63      A    C  
ANISOU 2267  CA  ASN A 938     6201   8319   6238  -1536    841   1222  A    C  
ATOM   2268  C   ASN A 938      -1.520   2.518 -25.817  1.00 51.40      A    C  
ANISOU 2268  C   ASN A 938     5809   7927   5794  -1172    935   1035  A    C  
ATOM   2269  O   ASN A 938      -0.786   1.676 -26.336  1.00 57.37      A    O  
ANISOU 2269  O   ASN A 938     6371   8931   6494  -1006   1130   1031  A    O  
ATOM   2270  CB  ASN A 938      -0.652   4.120 -24.143  1.00 54.20      A    C  
ANISOU 2270  CB  ASN A 938     6012   8210   6369  -1631    652   1217  A    C  
ATOM   2271  CG  ASN A 938      -0.010   5.469 -23.780  1.00 59.04      A    C  
ANISOU 2271  CG  ASN A 938     6595   8802   7037  -2014    515   1402  A    C  
ATOM   2272  ND2 ASN A 938       0.634   6.158 -24.722  1.00 57.28      A    N  
ANISOU 2272  ND2 ASN A 938     6300   8736   6729  -2241    625   1594  A    N  
ATOM   2273  OD1 ASN A 938      -0.088   5.866 -22.612  1.00 60.32      A    O  
ANISOU 2273  OD1 ASN A 938     6812   8798   7307  -2110    301   1372  A    O  
ATOM   2274  N   LEU A 939      -2.749   2.249 -25.387  1.00 47.86      A    N  
ANISOU 2274  N   LEU A 939     5600   7214   5372  -1049    795    884  A    N  
ATOM   2275  CA  LEU A 939      -3.281   0.885 -25.431  1.00 47.28      A    C  
ANISOU 2275  CA  LEU A 939     5575   7110   5278   -749    835    714  A    C  
ATOM   2276  C   LEU A 939      -3.438   0.355 -26.843  1.00 47.75      A    C  
ANISOU 2276  C   LEU A 939     5743   7250   5150   -603   1002    682  A    C  
ATOM   2277  O   LEU A 939      -3.032  -0.780 -27.107  1.00 46.46      A    O  
ANISOU 2277  O   LEU A 939     5498   7212   4942   -372   1125    602  A    O  
ATOM   2278  CB  LEU A 939      -4.593   0.779 -24.671  1.00 42.27      A    C  
ANISOU 2278  CB  LEU A 939     5149   6198   4712   -693    649    591  A    C  
ATOM   2279  CG  LEU A 939      -4.433   0.888 -23.158  1.00 41.07      A    C  
ANISOU 2279  CG  LEU A 939     4903   5981   4720   -746    506    577  A    C  
ATOM   2280  CD1 LEU A 939      -5.779   1.189 -22.536  1.00 43.83      A    C  
ANISOU 2280  CD1 LEU A 939     5474   6076   5104   -738    347    496  A    C  
ATOM   2281  CD2 LEU A 939      -3.865  -0.387 -22.548  1.00 41.96      A    C  
ANISOU 2281  CD2 LEU A 939     4842   6201   4900   -557    542    506  A    C  
ATOM   2282  N   THR A 940      -3.975   1.181 -27.746  1.00 50.18      A    N  
ANISOU 2282  N   THR A 940     6252   7480   5335   -727    998    746  A    N  
ATOM   2283  CA  THR A 940      -4.098   0.792 -29.154  1.00 53.77      A    C  
ANISOU 2283  CA  THR A 940     6844   8013   5574   -612   1149    729  A    C  
ATOM   2284  C   THR A 940      -2.728   0.476 -29.769  1.00 55.27      A    C  
ANISOU 2284  C   THR A 940     6796   8538   5667   -562   1409    813  A    C  
ATOM   2285  O   THR A 940      -2.616  -0.495 -30.523  1.00 56.92      A    O  
ANISOU 2285  O   THR A 940     7052   8844   5730   -320   1556    721  A    O  
ATOM   2286  CB  THR A 940      -4.846   1.837 -30.002  1.00 58.26      A    C  
ANISOU 2286  CB  THR A 940     7673   8444   6018   -773   1083    810  A    C  
ATOM   2287  CG2 THR A 940      -6.304   1.945 -29.556  1.00 53.83      A    C  
ANISOU 2287  CG2 THR A 940     7335   7586   5533   -741    850    706  A    C  
ATOM   2288  OG1 THR A 940      -4.213   3.106 -29.857  1.00 72.05      A    O  
ANISOU 2288  OG1 THR A 940     9336  10238   7800  -1058   1074    996  A    O  
ATOM   2289  N   SER A 941      -1.698   1.250 -29.405  1.00 57.34      A    N  
ANISOU 2289  N   SER A 941     6799   8978   6010   -778   1457    984  A    N  
ATOM   2290  CA  SER A 941      -0.311   0.986 -29.859  1.00 70.52      A    C  
ANISOU 2290  CA  SER A 941     8153  11025   7617   -741   1712   1093  A    C  
ATOM   2291  C   SER A 941       0.242  -0.353 -29.347  1.00 72.29      A    C  
ANISOU 2291  C   SER A 941     8168  11384   7917   -425   1788    963  A    C  
ATOM   2292  O   SER A 941       0.761  -1.146 -30.147  1.00 72.80      A    O  
ANISOU 2292  O   SER A 941     8170  11660   7832   -179   2015    923  A    O  
ATOM   2293  CB  SER A 941       0.645   2.117 -29.458  1.00 73.15      A    C  
ANISOU 2293  CB  SER A 941     8226  11516   8052  -1087   1702   1323  A    C  
ATOM   2294  OG  SER A 941       0.162   3.369 -29.900  1.00 76.80      A    O  
ANISOU 2294  OG  SER A 941     8916  11819   8444  -1380   1611   1449  A    O  
ATOM   2295  N   PHE A 942       0.119  -0.599 -28.035  1.00 62.40      A    N  
ANISOU 2295  N   PHE A 942     6837   9998   6874   -415   1596    897  A    N  
ATOM   2296  CA  PHE A 942       0.599  -1.856 -27.419  1.00 67.26      A    C  
ANISOU 2296  CA  PHE A 942     7283  10697   7575   -120   1621    781  A    C  
ATOM   2297  C   PHE A 942      -0.102  -3.109 -27.990  1.00 67.65      A    C  
ANISOU 2297  C   PHE A 942     7597  10615   7493    218   1663    578  A    C  
ATOM   2298  O   PHE A 942       0.568  -4.096 -28.314  1.00 66.49      A    O  
ANISOU 2298  O   PHE A 942     7344  10640   7281    510   1822    513  A    O  
ATOM   2299  CB  PHE A 942       0.479  -1.819 -25.885  1.00 64.92      A    C  
ANISOU 2299  CB  PHE A 942     6913  10249   7505   -201   1382    756  A    C  
ATOM   2300  N   LEU A 943      -1.425  -3.043 -28.155  1.00 59.97      A    N  
ANISOU 2300  N   LEU A 943     6968   9343   6474    179   1516    484  A    N  
ATOM   2301  CA  LEU A 943      -2.205  -4.179 -28.688  1.00 58.09      A    C  
ANISOU 2301  CA  LEU A 943     7016   8942   6115    440   1503    301  A    C  
ATOM   2302  C   LEU A 943      -2.026  -4.405 -30.166  1.00 62.10      A    C  
ANISOU 2302  C   LEU A 943     7660   9575   6360    576   1707    283  A    C  
ATOM   2303  O   LEU A 943      -1.961  -5.554 -30.603  1.00 60.28      A    O  
ANISOU 2303  O   LEU A 943     7551   9339   6013    874   1779    143  A    O  
ATOM   2304  CB  LEU A 943      -3.684  -4.026 -28.374  1.00 59.66      A    C  
ANISOU 2304  CB  LEU A 943     7494   8813   6360    335   1268    229  A    C  
ATOM   2305  CG  LEU A 943      -3.938  -4.178 -26.870  1.00 53.44      A    C  
ANISOU 2305  CG  LEU A 943     6617   7892   5795    289   1084    202  A    C  
ATOM   2306  CD1 LEU A 943      -5.210  -3.488 -26.508  1.00 58.68      A    C  
ANISOU 2306  CD1 LEU A 943     7458   8322   6517    110    895    202  A    C  
ATOM   2307  CD2 LEU A 943      -3.998  -5.633 -26.446  1.00 58.04      A    C  
ANISOU 2307  CD2 LEU A 943     7254   8392   6407    547   1042     61  A    C  
ATOM   2308  N   GLY A 944      -1.953  -3.313 -30.926  1.00 59.25      A    N  
ANISOU 2308  N   GLY A 944     7313   9310   5889    361   1792    424  A    N  
ATOM   2309  CA  GLY A 944      -1.556  -3.350 -32.326  1.00 64.95      A    C  
ANISOU 2309  CA  GLY A 944     8119  10220   6338    456   2029    453  A    C  
ATOM   2310  C   GLY A 944      -0.203  -4.001 -32.567  1.00 71.79      A    C  
ANISOU 2310  C   GLY A 944     8706  11433   7138    698   2305    466  A    C  
ATOM   2311  O   GLY A 944      -0.054  -4.776 -33.516  1.00 76.92      A    O  
ANISOU 2311  O   GLY A 944     9507  12164   7556    975   2476    365  A    O  
ATOM   2312  N   CYS A 945       0.768  -3.704 -31.701  1.00 72.33      A    N  
ANISOU 2312  N   CYS A 945     8374  11706   7402    610   2338    587  A    N  
ATOM   2313  CA  CYS A 945       2.093  -4.348 -31.748  1.00 82.61      A    C  
ANISOU 2313  CA  CYS A 945     9333  13366   8691    861   2579    610  A    C  
ATOM   2314  C   CYS A 945       2.056  -5.838 -31.370  1.00 80.97      A    C  
ANISOU 2314  C   CYS A 945     9207  13050   8507   1275   2540    392  A    C  
ATOM   2315  O   CYS A 945       2.669  -6.665 -32.059  1.00 78.48      A    O  
ANISOU 2315  O   CYS A 945     8873  12923   8022   1623   2764    315  A    O  
ATOM   2316  CB  CYS A 945       3.111  -3.578 -30.892  1.00 91.29      A    C  
ANISOU 2316  CB  CYS A 945     9966  14709  10009    618   2579    817  A    C  
ATOM   2317  SG  CYS A 945       3.524  -1.964 -31.619  1.00 97.95      A    S  
ANISOU 2317  SG  CYS A 945    10685  15767  10763    170   2704   1107  A    S  
ATOM   2318  N   GLN A 946       1.328  -6.170 -30.301  1.00 74.05      A    N  
ANISOU 2318  N   GLN A 946     8447  11866   7823   1242   2260    295  A    N  
ATOM   2319  CA  GLN A 946       1.049  -7.574 -29.941  1.00 74.76      A    C  
ANISOU 2319  CA  GLN A 946     8715  11763   7926   1584   2165     90  A    C  
ATOM   2320  C   GLN A 946       0.350  -8.347 -31.073  1.00 71.60      A    C  
ANISOU 2320  C   GLN A 946     8748  11196   7262   1811   2208    -83  A    C  
ATOM   2321  O   GLN A 946       0.747  -9.464 -31.395  1.00 73.17      A    O  
ANISOU 2321  O   GLN A 946     9034  11421   7348   2188   2305   -220  A    O  
ATOM   2322  CB  GLN A 946       0.211  -7.665 -28.647  1.00 77.16      A    C  
ANISOU 2322  CB  GLN A 946     9110  11752   8457   1439   1852     44  A    C  
ATOM   2323  CG  GLN A 946       0.970  -7.328 -27.368  1.00 80.94      A    C  
ANISOU 2323  CG  GLN A 946     9217  12356   9182   1326   1774    158  A    C  
ATOM   2324  CD  GLN A 946       1.948  -8.423 -26.944  1.00 86.96      A    C  
ANISOU 2324  CD  GLN A 946     9779  13262   9999   1677   1834    102  A    C  
ATOM   2325  NE2 GLN A 946       3.231  -8.078 -26.819  1.00 80.65      A    N  
ANISOU 2325  NE2 GLN A 946     8547  12827   9267   1688   1980    243  A    N  
ATOM   2326  OE1 GLN A 946       1.546  -9.568 -26.717  1.00102.75      A    O  
ANISOU 2326  OE1 GLN A 946    12012  15044  11985   1931   1734    -57  A    O  
ATOM   2327  N   LEU A 947      -0.673  -7.737 -31.665  1.00 72.75      A    N  
ANISOU 2327  N   LEU A 947     9174  11162   7307   1589   2119    -76  A    N  
ATOM   2328  CA  LEU A 947      -1.450  -8.335 -32.764  1.00 77.13      A    C  
ANISOU 2328  CA  LEU A 947    10167  11536   7603   1739   2110   -225  A    C  
ATOM   2329  C   LEU A 947      -0.611  -8.513 -34.017  1.00 85.49      A    C  
ANISOU 2329  C   LEU A 947    11236  12875   8370   1975   2429   -231  A    C  
ATOM   2330  O   LEU A 947      -0.648  -9.587 -34.632  1.00 93.25      A    O  
ANISOU 2330  O   LEU A 947    12497  13779   9156   2309   2478   -409  A    O  
ATOM   2331  CB  LEU A 947      -2.714  -7.498 -33.053  1.00 80.91      A    C  
ANISOU 2331  CB  LEU A 947    10889  11789   8063   1423   1921   -185  A    C  
ATOM   2332  CG  LEU A 947      -3.731  -7.924 -34.127  1.00 80.49      A    C  
ANISOU 2332  CG  LEU A 947    11298  11516   7768   1486   1831   -312  A    C  
ATOM   2333  CD1 LEU A 947      -4.176  -9.374 -33.989  1.00 78.54      A    C  
ANISOU 2333  CD1 LEU A 947    11326  11021   7493   1746   1687   -522  A    C  
ATOM   2334  CD2 LEU A 947      -4.941  -6.994 -34.081  1.00 77.56      A    C  
ANISOU 2334  CD2 LEU A 947    11056  10946   7467   1158   1606   -240  A    C  
ATOM   2335  N   ALA A 948       0.179  -7.483 -34.352  1.00 94.61      A    N  
ANISOU 2335  N   ALA A 948    12093  14360   9493   1805   2645    -32  A    N  
ATOM   2336  CA  ALA A 948       1.150  -7.523 -35.476  1.00101.51      A    C  
ANISOU 2336  CA  ALA A 948    12882  15594  10092   2007   3007     12  A    C  
ATOM   2337  C   ALA A 948       2.175  -8.665 -35.402  1.00102.75      A    C  
ANISOU 2337  C   ALA A 948    12872  15957  10211   2468   3203    -97  A    C  
ATOM   2338  O   ALA A 948       2.758  -9.006 -36.427  1.00116.28      A    O  
ANISOU 2338  O   ALA A 948    14635  17904  11642   2742   3492   -133  A    O  
ATOM   2339  CB  ALA A 948       1.872  -6.184 -35.630  1.00100.57      A    C  
ANISOU 2339  CB  ALA A 948    12406  15805  10000   1682   3182    286  A    C  
ATOM   2340  N   ASP A 949       2.396  -9.237 -34.212  1.00102.39      A    N  
ANISOU 2340  N   ASP A 949    12641  15829  10431   2569   3052   -146  A    N  
ATOM   2341  CA  ASP A 949       2.955 -10.596 -34.071  1.00114.75      A    C  
ANISOU 2341  CA  ASP A 949    14228  17409  11962   3060   3116   -320  A    C  
ATOM   2342  C   ASP A 949       1.859 -11.652 -34.321  1.00119.11      A    C  
ANISOU 2342  C   ASP A 949    15360  17509  12388   3245   2896   -571  A    C  
ATOM   2343  O   ASP A 949       1.328 -12.274 -33.385  1.00103.84      A    O  
ANISOU 2343  O   ASP A 949    13543  15268  10644   3252   2620   -663  A    O  
ATOM   2344  CB  ASP A 949       3.613 -10.808 -32.694  1.00118.61      A    C  
ANISOU 2344  CB  ASP A 949    14319  17970  12776   3091   3011   -263  A    C  
ATOM   2345  CG  ASP A 949       4.802  -9.888 -32.449  1.00119.24      A    C  
ANISOU 2345  CG  ASP A 949    13809  18516  12982   2928   3211    -15  A    C  
ATOM   2346  OD1 ASP A 949       4.929  -8.841 -33.125  1.00119.29      A    O  
ANISOU 2346  OD1 ASP A 949    13710  18729  12885   2652   3369    150  A    O  
ATOM   2347  OD2 ASP A 949       5.611 -10.218 -31.555  1.00109.84      A    O1-
ANISOU 2347  OD2 ASP A 949    12261  17477  11997   3061   3188     25  A    O1-
ATOM   2348  N   ALA A 950       1.531 -11.812 -35.605  1.00126.73      A    N  
ANISOU 2348  N   ALA A 950    16691  18442  13019   3366   3013   -666  A    N  
ATOM   2349  CA  ALA A 950       0.727 -12.904 -36.138  1.00122.15      A    C  
ANISOU 2349  CA  ALA A 950    16681  17496  12236   3605   2859   -911  A    C  
ATOM   2350  C   ALA A 950       1.687 -13.728 -37.024  1.00122.60      A    C  
ANISOU 2350  C   ALA A 950    16817  17776  11991   4132   3174  -1040  A    C  
ATOM   2351  O   ALA A 950       1.427 -13.951 -38.205  1.00102.30      A    O  
ANISOU 2351  O   ALA A 950    14635  15163   9073   4278   3274  -1150  A    O  
ATOM   2352  CB  ALA A 950      -0.451 -12.345 -36.936  1.00115.63      A    C  
ANISOU 2352  CB  ALA A 950    16234  16455  11245   3309   2718   -912  A    C  
ATOM   2353  N   GLU A 951       2.795 -14.165 -36.407  1.00127.63      A    N  
ANISOU 2353  N   GLU A 951    17077  18653  12763   4426   3322  -1024  A    N  
ATOM   2354  CA  GLU A 951       3.893 -14.909 -37.036  1.00129.42      A    C  
ANISOU 2354  CA  GLU A 951    17249  19166  12760   4977   3652  -1122  A    C  
ATOM   2355  C   GLU A 951       4.548 -14.147 -38.186  1.00134.04      A    C  
ANISOU 2355  C   GLU A 951    17659  20204  13066   4985   4060   -996  A    C  
ATOM   2356  O   GLU A 951       4.869 -12.969 -38.036  1.00131.44      A    O  
ANISOU 2356  O   GLU A 951    16905  20169  12866   4608   4167   -743  A    O  
ATOM   2357  CB  GLU A 951       3.429 -16.302 -37.471  1.00137.07      A    C  
ANISOU 2357  CB  GLU A 951    18835  19746  13500   5401   3520  -1425  A    C  
ATOM   2358  CG  GLU A 951       2.608 -17.022 -36.400  1.00129.91      A    C  
ANISOU 2358  CG  GLU A 951    18165  18348  12847   5311   3087  -1527  A    C  
ATOM   2359  CD  GLU A 951       2.645 -18.539 -36.497  1.00140.34      A    C  
ANISOU 2359  CD  GLU A 951    19939  19362  14022   5823   2985  -1794  A    C  
ATOM   2360  OE1 GLU A 951       2.494 -19.190 -35.440  1.00138.34      A    O  
ANISOU 2360  OE1 GLU A 951    19705  18847  14012   5854   2722  -1832  A    O  
ATOM   2361  OE2 GLU A 951       2.822 -19.087 -37.610  1.00146.19      A    O1-
ANISOU 2361  OE2 GLU A 951    21046  20106  14394   6196   3157  -1965  A    O1-
TER   
HETATM 2362  C1  C6F A1001     -28.205  -1.584 -27.711  1.00 61.22      B    C  
HETATM 2363  C2  C6F A1001     -28.087  -2.901 -26.918  1.00 61.39      B    C  
HETATM 2364  C3  C6F A1001     -28.157  -4.152 -27.781  1.00 57.49      B    C  
HETATM 2365  N4  C6F A1001     -27.949  -4.030 -29.085  1.00 55.35      B    N  
HETATM 2366  C5  C6F A1001     -27.981  -5.045 -29.968  1.00 55.41      B    C  
HETATM 2367  C6  C6F A1001     -27.691  -4.664 -31.374  1.00 51.75      B    C  
HETATM 2368  O7  C6F A1001     -27.632  -5.511 -32.244  1.00 41.77      B    O  
HETATM 2369  N8  C6F A1001     -27.437  -3.380 -31.714  1.00 45.53      B    N  
HETATM 2370  C9  C6F A1001     -28.228  -6.382 -29.492  1.00 50.73      B    C  
HETATM 2371  N10 C6F A1001     -28.282  -7.483 -30.381  1.00 56.35      B    N  
HETATM 2372  C11 C6F A1001     -28.364  -8.895 -30.142  1.00 59.31      B    C  
HETATM 2373  C12 C6F A1001     -28.178  -9.746 -31.259  1.00 59.60      B    C  
HETATM 2374  C13 C6F A1001     -28.253 -11.133 -31.156  1.00 64.26      B    C  
HETATM 2375  C14 C6F A1001     -28.519 -11.742 -29.927  1.00 75.34      B    C  
HETATM 2376  N15 C6F A1001     -28.569 -13.149 -29.837  1.00 85.46      B    N  
HETATM 2377  C16 C6F A1001     -29.619 -13.936 -30.527  1.00 95.25      B    C  
HETATM 2378  C17 C6F A1001     -28.980 -15.118 -31.291  1.00110.12      B    C  
HETATM 2379  C18 C6F A1001     -28.108 -15.943 -30.323  1.00127.15      B    C  
HETATM 2380  C19 C6F A1001     -26.958 -15.032 -29.845  1.00110.42      B    C  
HETATM 2381  C20 C6F A1001     -27.548 -13.867 -29.035  1.00 83.15      B    C  
HETATM 2382  N21 C6F A1001     -27.641 -17.230 -30.922  1.00138.39      B    N  
HETATM 2383  C22 C6F A1001     -26.599 -17.151 -31.983  1.00140.85      B    C  
HETATM 2384  C23 C6F A1001     -26.393 -18.528 -32.638  1.00145.87      B    C  
HETATM 2385  N24 C6F A1001     -26.034 -19.527 -31.607  1.00140.07      B    N  
HETATM 2386  C25 C6F A1001     -25.576 -20.820 -32.163  1.00120.45      B    C  
HETATM 2387  C26 C6F A1001     -27.079 -19.647 -30.565  1.00132.35      B    C  
HETATM 2388  C27 C6F A1001     -27.350 -18.279 -29.908  1.00133.41      B    C  
HETATM 2389  C28 C6F A1001     -28.714 -10.925 -28.795  1.00 72.93      B    C  
HETATM 2390  O29 C6F A1001     -28.973 -11.464 -27.565  1.00 78.74      B    O  
HETATM 2391  C30 C6F A1001     -30.314 -11.879 -27.299  1.00 82.68      B    C  
HETATM 2392  C31 C6F A1001     -28.645  -9.529 -28.910  1.00 65.98      B    C  
HETATM 2393  N32 C6F A1001     -28.449  -6.486 -28.164  1.00 59.65      B    N  
HETATM 2394  C33 C6F A1001     -28.417  -5.457 -27.275  1.00 63.54      B    C  
HETATM 2395  N34 C6F A1001     -28.655  -5.694 -25.911  1.00 72.23      B    N  
HETATM 2396  C35 C6F A1001     -28.681  -7.046 -25.327  1.00 73.92      B    C  
HETATM 2397  C36 C6F A1001     -29.231  -6.995 -23.898  1.00 83.88      B    C  
HETATM 2398  C37 C6F A1001     -29.376  -8.440 -23.403  1.00 87.04      B    C  
HETATM 2399  O38 C6F A1001     -28.091  -9.076 -23.385  1.00 72.69      B    O  
HETATM 2400  C39 C6F A1001     -27.249  -8.989 -24.547  1.00 76.77      B    C  
HETATM 2401  C40 C6F A1001     -27.262  -7.622 -25.257  1.00 81.97      B    C  
HETATM 2402  O1  SO4 A1002     -43.412   9.566 -38.171  1.00 72.03      C    O  
HETATM 2403  O2  SO4 A1002     -41.319  10.734 -38.051  1.00 62.33      C    O  
HETATM 2404  O3  SO4 A1002     -42.390   9.887 -35.972  1.00 56.43      C    O1-
HETATM 2405  O4  SO4 A1002     -41.386   8.406 -37.582  1.00 52.59      C    O  
HETATM 2406  S   SO4 A1002     -42.134   9.664 -37.425  1.00 63.79      C    S  
HETATM 2407  O1  SO4 A1003     -22.938 -14.667 -15.251  1.00 74.49      D    O  
HETATM 2408  O2  SO4 A1003     -20.886 -13.412 -14.871  1.00 67.15      D    O  
HETATM 2409  O3  SO4 A1003     -23.002 -12.528 -14.140  1.00 74.96      D    O1-
HETATM 2410  O4  SO4 A1003     -22.022 -14.426 -13.018  1.00 99.27      D    O  
HETATM 2411  S   SO4 A1003     -22.213 -13.760 -14.328  1.00 67.82      D    S  
HETATM 2412  O1  SO4 A1004     -19.013 -12.956 -41.631  1.00 68.93      E    O  
HETATM 2413  O2  SO4 A1004     -18.893 -15.256 -40.799  1.00 78.30      E    O  
HETATM 2414  O3  SO4 A1004     -18.083 -13.418 -39.448  1.00 74.10      E    O1-
HETATM 2415  O4  SO4 A1004     -20.449 -13.676 -39.854  1.00 58.13      E    O  
HETATM 2416  S   SO4 A1004     -19.105 -13.831 -40.435  1.00 78.14      E    S  
HETATM 2417  C1  GOL A1005     -28.329   9.430 -42.038  1.00 87.72      F    C  
HETATM 2418  O1  GOL A1005     -29.706   9.641 -42.374  1.00 77.01      F    O  
HETATM 2419  C2  GOL A1005     -27.533  10.730 -42.101  1.00 84.68      F    C  
HETATM 2420  O2  GOL A1005     -28.210  11.748 -41.363  1.00 64.96      F    O  
HETATM 2421  C3  GOL A1005     -26.128  10.511 -41.531  1.00 89.99      F    C  
HETATM 2422  O3  GOL A1005     -25.404  11.740 -41.333  1.00101.71      F    O  
HETATM 2423  C1  GOL A1006       0.019   3.069  -7.424  1.00 82.00      G    C  
HETATM 2424  O1  GOL A1006      -0.798   3.866  -8.298  1.00 59.44      G    O  
HETATM 2425  C2  GOL A1006       0.107   1.615  -7.888  1.00 78.57      G    C  
HETATM 2426  O2  GOL A1006      -1.209   1.064  -7.964  1.00 57.61      G    O  
HETATM 2427  C3  GOL A1006       0.805   1.475  -9.247  1.00 81.76      G    C  
HETATM 2428  O3  GOL A1006       0.566   0.172  -9.806  1.00 85.04      G    O  
HETATM 2429  N   CXS A1007     -19.815 -19.658 -11.595  1.00 85.19      H    N  
HETATM 2430  C1  CXS A1007     -19.653 -17.918 -14.449  1.00 57.14      H    C  
HETATM 2431  O1  CXS A1007     -17.392 -19.136 -14.287  1.00 63.85      H    O  
HETATM 2432  C2  CXS A1007     -20.064 -17.649 -12.992  1.00 60.75      H    C  
HETATM 2433  O2  CXS A1007     -17.779 -17.762 -16.313  1.00 42.92      H    O  
HETATM 2434  C3  CXS A1007     -20.757 -18.817 -12.302  1.00 71.57      H    C  
HETATM 2435  O3  CXS A1007     -17.415 -16.780 -14.043  1.00 58.44      H    O  
HETATM 2436  C4  CXS A1007     -20.049 -20.068 -10.223  1.00 84.20      H    C  
HETATM 2437  C5  CXS A1007     -21.317 -20.919 -10.104  1.00 94.50      H    C  
HETATM 2438  C6  CXS A1007     -21.577 -21.322  -8.652  1.00104.33      H    C  
HETATM 2439  C7  CXS A1007     -20.364 -21.980  -7.985  1.00 93.24      H    C  
HETATM 2440  C8  CXS A1007     -19.052 -21.228  -8.221  1.00 89.68      H    C  
HETATM 2441  C9  CXS A1007     -18.853 -20.862  -9.694  1.00 76.76      H    C  
HETATM 2442  S   CXS A1007     -18.009 -17.901 -14.720  1.00 48.63      H    S  
HETATM 2443  C1  GOL A1008     -12.514 -11.397   0.705  0.50 41.67      I    C  
HETATM 2444  O1  GOL A1008     -13.812 -10.972   1.136  0.50 49.15      I    O  
HETATM 2445  C2  GOL A1008     -12.669 -12.648  -0.147  0.50 38.17      I    C  
HETATM 2446  O2  GOL A1008     -13.410 -13.646   0.555  0.50 41.82      I    O  
HETATM 2447  C3  GOL A1008     -11.322 -13.242  -0.500  0.50 34.16      I    C  
HETATM 2448  O3  GOL A1008     -11.552 -14.632  -0.732  0.50 31.21      I    O  
CONECT 2362 2363
CONECT 2363 2362 2364
CONECT 2364 2363 2365 2394
CONECT 2365 2364 2366
CONECT 2366 2365 2367 2370
CONECT 2367 2366 2368 2369
CONECT 2368 2367
CONECT 2369 2367
CONECT 2370 2366 2393 2371
CONECT 2371 2370 2372
CONECT 2372 2371 2373 2392
CONECT 2373 2372 2374
CONECT 2374 2373 2375
CONECT 2375 2374 2376 2389
CONECT 2376 2375 2381 2377
CONECT 2377 2376 2378
CONECT 2378 2377 2379
CONECT 2379 2378 2380 2382
CONECT 2380 2379 2381
CONECT 2381 2376 2380
CONECT 2382 2379 2383 2388
CONECT 2383 2382 2384
CONECT 2384 2383 2385
CONECT 2385 2384 2386 2387
CONECT 2386 2385
CONECT 2387 2385 2388
CONECT 2388 2382 2387
CONECT 2389 2375 2390 2392
CONECT 2390 2389 2391
CONECT 2391 2390
CONECT 2392 2372 2389
CONECT 2393 2370 2394
CONECT 2394 2364 2393 2395
CONECT 2395 2394 2396
CONECT 2396 2395 2397 2401
CONECT 2397 2396 2398
CONECT 2398 2397 2399
CONECT 2399 2398 2400
CONECT 2400 2399 2401
CONECT 2401 2396 2400
CONECT 2402 2406
CONECT 2403 2406
CONECT 2404 2406
CONECT 2405 2406
CONECT 2406 2402 2403 2404 2405
CONECT 2407 2411
CONECT 2408 2411
CONECT 2409 2411
CONECT 2410 2411
CONECT 2411 2407 2408 2409 2410
CONECT 2412 2416
CONECT 2413 2416
CONECT 2414 2416
CONECT 2415 2416
CONECT 2416 2412 2413 2414 2415
CONECT 2417 2418 2419
CONECT 2418 2417
CONECT 2419 2417 2420 2421
CONECT 2420 2419
CONECT 2421 2419 2422
CONECT 2422 2421
CONECT 2423 2424 2425
CONECT 2424 2423
CONECT 2425 2423 2426 2427
CONECT 2426 2425
CONECT 2427 2425 2428
CONECT 2428 2427
CONECT 2429 2436 2434
CONECT 2430 2432 2442
CONECT 2431 2442
CONECT 2432 2430 2434
CONECT 2433 2442
CONECT 2434 2432 2429
CONECT 2435 2442
CONECT 2436 2429 2437 2441
CONECT 2437 2436 2438
CONECT 2438 2437 2439
CONECT 2439 2438 2440
CONECT 2440 2439 2441
CONECT 2441 2436 2440
CONECT 2442 2430 2431 2433 2435
CONECT 2443 2444 2445
CONECT 2444 2443
CONECT 2445 2443 2446 2447
CONECT 2446 2445
CONECT 2447 2445 2448
CONECT 2448 2447
END



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